data_9DKD
# 
_entry.id   9DKD 
# 
_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   9DKD         pdb_00009dkd 10.2210/pdb9dkd/pdb 
WWPDB D_1000288253 ?            ?                   
EMDB  EMD-46953    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DKD 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  'contains the same protein in a different conformatio'                           9DIU      unspecified            
PDB  'contains the same protein in a different conformatio'                           9DI3      unspecified            
PDB  'contains the same protein bound to PAC1 and in a different conformation'        9DJU      unspecified            
PDB  'contains the same protein in a different conformatio'                           9DJY      unspecified            
PDB  'contains the same protein bound to PAC1 and in a different conformation'        9DJZ      unspecified            
PDB  'contains the same protein bound to PAC1 and in a different conformation'        9DK0      unspecified            
PDB  'contains the same protein bound to PAC1 and in a different conformation'        9DJ7      unspecified            
EMDB 'CryoEM structures of yeast cytoplasmic dynein in the presence of ATP and Lis1.' EMD-46953 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              aleschziner@ucsd.edu 
_pdbx_contact_author.name_first         Andres 
_pdbx_contact_author.name_last          Leschziner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7732-7023 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kendrick, A.A.'   1 0000-0003-3254-4582 
'Leschziner, A.E.' 2 0000-0002-7732-7023 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Multiple steps of dynein activation by Lis1 visualized by cryo-EM.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01558-w 
_citation.pdbx_database_id_PubMed   40410592 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kendrick, A.A.'      1 0000-0003-3254-4582 
primary 'Nguyen, K.H.V.'      2 0009-0000-1928-6991 
primary 'Ma, W.'              3 0000-0002-1123-5273 
primary 'Karasmanis, E.P.'    4 0000-0002-0139-0210 
primary 'Amaro, R.E.'         5 0000-0002-9275-9553 
primary 'Reck-Peterson, S.L.' 6 0000-0002-1553-465X 
primary 'Leschziner, A.E.'    7 0000-0002-7732-7023 
# 
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 'Dynein heavy chain, cytoplasmic' 331525.000 1 ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"       507.181    1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"        427.201    3 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                   24.305     1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Dynein heavy chain,cytosolic,DYHC' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GDQLTHVVEEVKTYDLVWRSIKNLWEDVQRTFETPWCRVDVLLLQSDLANFLRRADELPRAVKQFEMYKSLFSQVNMLTS
VNKILVELKDGALKPRHWNMIFRDIGKRQIQKNLLDKLEFSLKDVMVLNLTLNEILLTKIIERAQKEFVIEKSLNRIKKF
WKEAQYEVIEHSSGLKLVREWDVLEQACKEDLEELVSMKASNYYKIFEQDCLDLESKLTKLSEIQVNWVEVQFYWLDLYG
ILGENLDIQNFLPLETSKFKSLTSEYKMITTRAFQLDTTIEVIHIPNFDTTLKLTIDSLKMIKSSLSTFLERQRRQFPRF
YFLGNDDLLKIIGSGKHHDQVSKFMKKMFGSIESIIFFEDSITGVRSVEGEVLNLNEKIELKDSIQAQEWLNILDTEIKL
SVFTQFRDCLGQLKDGTDIEVVVSKYIFQAILLSAQVMWTELVEKCLQTNEFSKYWKEVDMKIKGLLDKLNKSSDNVKKK
IEALLVEYLHFNNVIGQLKNCSTKEEARLLWAKVQKFYQKNDTLDDLNSVFISQSGYLLQYKFEYIGIPERLIYTPLLLV
GFATLTDSLHQKYGGCFFGPAGTGKTETVKAFGQNLGRVVVVFNCDDSFDYQVLSRLLVGITQIGAWGCFDEFNRLDEKV
LSAVSANIQQIQNGLQVGKSHITLLEEETPLSPHTAVFITLNPGYNGRSELPENLKKSFREFSMKSPQSGTIAEMILQIM
GFEDSKSLASKIVHFLELLSSKCSSMNHYHFGLRTLKGVLRNCSPLVSEFGEGEKTVVESLKRVILPSLGDTDELVFKDE
LSKIFDSAGTPLNSKAIVQCLKDAGQRSGFSMSEEFLKKCMQFYYMQKTQQALILVGKAGCGKTATWKTVIDAMAIFDGH
ANVVYVIDTKVLTKESLYGSMLKATLEWRDGLFTSILRRVNDDITGTFKNSRIWVVFDSDLDPEYVEAMNSVLDDNKILT
LPNGERLPIPPNFRILFETDNLDHTTPATITRCGLLWFSTDVCSISSKIDHLLNKSYEALDNKLSMFELDKLKDLISDSF
DMASLTNIFTCSNDLVHILGVRTFNKLETAVQLAVHLISSYRQWFQNLDDKSLKDVITLLIKRSLLYALAGDSTGESQRA
FIQTINTYFGHDSQELSDYSTIVIANDKLSFSSFCSEIPSVSLEAHEVMRPDIVIPTIDTIKHEKIFYDLLNSKRGIILC
GPPGSGKTMIMNNALRNSSLYDVVGINFSKDTTTEHILSALHRHTNYVTTSKGLTLLPKSDIKNLVLFCDEINLPKLDKY
GSQNVVLFLRQLMEKQGFWKTPENKWVTIERIHIVGACNPPTDPGRIPMSERFTRHAAILYLGYPSGKSLSQIYEIYYKA
IFKLVPEFRSYTEPFARASVHLYNECKARYSTGLQSHYLFSPRELTRLVRGVYTAINTGPRQTLRSLIRLWAYEAWRIFA
DRLVGVKEKNSFEQLLYETVDKYLPNQDLGNISSTSLLFSGLLSLDFKEVNKTDLVNFIEERFKTFCDEELEVPMVIHES
MVDHILRIDRALKQVQGHMMLIGASRTGKTILTRFVAWLNGLKIVQPKIHRHSNLSDFDMILKKAISDCSLKESRTCLII
DESNILETAFLERMNTLLANADIPDLFQGEEYDKLLNNLRNKTRSLGLLLDTEQELYDWFVGEIAKNLHVVFTICDPTNN
KSSAMISSPALFNRCIINWMGDWDTKTMSQVANNMVDVVPMEFTDFIVPEVNKELVFTEPIQTIRDAVVNILIHFDRNFY
QKMKVGVNPRSPGYFIDGLRALVKLVTAKYQDLQENQRFVNVGLEKLNESVLKVNELNKTLSKKSTELTEKEKEARSTLD
KMLMEQNESERKQEATEEIKKILKVQEEDIRKRKEVVMKSIQDIEPTILEAQRGVKNIKKQQLTEIRSMVNPPSGVKIVM
EAVCAILGYQFSNWRDIQQFIRKDDFIHNIVHYDTTLHMKPQIRKYMEEEFLSDPNFTYETINRASKACGPLYQWVNAQI
NFSKVLENVDPLRQEMKRIEFESLKTKANLLAAEEMTQDLEASIEVSKQKYSLLIRDVEAIKTEMSNVQANLDRSISLVK
SLTFEKERWLNTTKQFSKTSQELIGNCIISSIYETYFGHLNERERGDMLVILKRLLGKFAVKYDVNYRFIDYLVTLDEKM
KWLECGLDKNDYFLENMSIVMNSQDAVPFLLDPSSHMITVISNYYGNKTVLLSFLEEGFVKRLENAVRFGSVVIIQDGEF
FDPIISRLISREFNHAGNRVTVEIGDHEVDVSGDFKLFIHSCDPSGDIPIFLRSRVRLVHFVTNKESIETRIFDITLTEE
NAEMQRKREDLIKLNTEYRLKLKNLEKRLLEELNNSQGNMLENDELMVTLNNLKKEAMNIEKKLSESEEFFPQFDNLVEE
YSIIGKHSVKIFSMLEKFGQFHWFYGISIGQFLSCFKRVFIKKSRETRAARTRVDEILWLLYQEVYCQFSTALDKKFKMI
MAMTMFCLYKFDIESEQYKEAVLTMIGVLSESSDGVPKLTVDTNDDLRYLWDYVTTKSYISALNWFKNEFFVDEWNIADV
VANSENNYFTMASERDVDGTFKLIELAKASKESLKIIPLGSIENLNYAQEEISKSKIEGGWILLQNIQMSLSWVKTYLHK
HVEETKAAEEHEKFKMFMTCHLTGDKLPAPLLQRTDRVVYEDIPGILDTVKDLWGSQFFTGKISGVWSVYCTFLLSWFHA
LITARTRLVPHGFSKKYYFNDCDFQFASVYLENVLATNSTNNIPWAQVRDHIATIVYGGKIDEEKDLEVVAKLCAHVFCG
SDNLQIVPGVRIPQPLLQQSEEEERARLTAILSNTIEPADSLSSWLQLPRESILDYERLQAKEVASSTEQLLQEM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GDQLTHVVEEVKTYDLVWRSIKNLWEDVQRTFETPWCRVDVLLLQSDLANFLRRADELPRAVKQFEMYKSLFSQVNMLTS
VNKILVELKDGALKPRHWNMIFRDIGKRQIQKNLLDKLEFSLKDVMVLNLTLNEILLTKIIERAQKEFVIEKSLNRIKKF
WKEAQYEVIEHSSGLKLVREWDVLEQACKEDLEELVSMKASNYYKIFEQDCLDLESKLTKLSEIQVNWVEVQFYWLDLYG
ILGENLDIQNFLPLETSKFKSLTSEYKMITTRAFQLDTTIEVIHIPNFDTTLKLTIDSLKMIKSSLSTFLERQRRQFPRF
YFLGNDDLLKIIGSGKHHDQVSKFMKKMFGSIESIIFFEDSITGVRSVEGEVLNLNEKIELKDSIQAQEWLNILDTEIKL
SVFTQFRDCLGQLKDGTDIEVVVSKYIFQAILLSAQVMWTELVEKCLQTNEFSKYWKEVDMKIKGLLDKLNKSSDNVKKK
IEALLVEYLHFNNVIGQLKNCSTKEEARLLWAKVQKFYQKNDTLDDLNSVFISQSGYLLQYKFEYIGIPERLIYTPLLLV
GFATLTDSLHQKYGGCFFGPAGTGKTETVKAFGQNLGRVVVVFNCDDSFDYQVLSRLLVGITQIGAWGCFDEFNRLDEKV
LSAVSANIQQIQNGLQVGKSHITLLEEETPLSPHTAVFITLNPGYNGRSELPENLKKSFREFSMKSPQSGTIAEMILQIM
GFEDSKSLASKIVHFLELLSSKCSSMNHYHFGLRTLKGVLRNCSPLVSEFGEGEKTVVESLKRVILPSLGDTDELVFKDE
LSKIFDSAGTPLNSKAIVQCLKDAGQRSGFSMSEEFLKKCMQFYYMQKTQQALILVGKAGCGKTATWKTVIDAMAIFDGH
ANVVYVIDTKVLTKESLYGSMLKATLEWRDGLFTSILRRVNDDITGTFKNSRIWVVFDSDLDPEYVEAMNSVLDDNKILT
LPNGERLPIPPNFRILFETDNLDHTTPATITRCGLLWFSTDVCSISSKIDHLLNKSYEALDNKLSMFELDKLKDLISDSF
DMASLTNIFTCSNDLVHILGVRTFNKLETAVQLAVHLISSYRQWFQNLDDKSLKDVITLLIKRSLLYALAGDSTGESQRA
FIQTINTYFGHDSQELSDYSTIVIANDKLSFSSFCSEIPSVSLEAHEVMRPDIVIPTIDTIKHEKIFYDLLNSKRGIILC
GPPGSGKTMIMNNALRNSSLYDVVGINFSKDTTTEHILSALHRHTNYVTTSKGLTLLPKSDIKNLVLFCDEINLPKLDKY
GSQNVVLFLRQLMEKQGFWKTPENKWVTIERIHIVGACNPPTDPGRIPMSERFTRHAAILYLGYPSGKSLSQIYEIYYKA
IFKLVPEFRSYTEPFARASVHLYNECKARYSTGLQSHYLFSPRELTRLVRGVYTAINTGPRQTLRSLIRLWAYEAWRIFA
DRLVGVKEKNSFEQLLYETVDKYLPNQDLGNISSTSLLFSGLLSLDFKEVNKTDLVNFIEERFKTFCDEELEVPMVIHES
MVDHILRIDRALKQVQGHMMLIGASRTGKTILTRFVAWLNGLKIVQPKIHRHSNLSDFDMILKKAISDCSLKESRTCLII
DESNILETAFLERMNTLLANADIPDLFQGEEYDKLLNNLRNKTRSLGLLLDTEQELYDWFVGEIAKNLHVVFTICDPTNN
KSSAMISSPALFNRCIINWMGDWDTKTMSQVANNMVDVVPMEFTDFIVPEVNKELVFTEPIQTIRDAVVNILIHFDRNFY
QKMKVGVNPRSPGYFIDGLRALVKLVTAKYQDLQENQRFVNVGLEKLNESVLKVNELNKTLSKKSTELTEKEKEARSTLD
KMLMEQNESERKQEATEEIKKILKVQEEDIRKRKEVVMKSIQDIEPTILEAQRGVKNIKKQQLTEIRSMVNPPSGVKIVM
EAVCAILGYQFSNWRDIQQFIRKDDFIHNIVHYDTTLHMKPQIRKYMEEEFLSDPNFTYETINRASKACGPLYQWVNAQI
NFSKVLENVDPLRQEMKRIEFESLKTKANLLAAEEMTQDLEASIEVSKQKYSLLIRDVEAIKTEMSNVQANLDRSISLVK
SLTFEKERWLNTTKQFSKTSQELIGNCIISSIYETYFGHLNERERGDMLVILKRLLGKFAVKYDVNYRFIDYLVTLDEKM
KWLECGLDKNDYFLENMSIVMNSQDAVPFLLDPSSHMITVISNYYGNKTVLLSFLEEGFVKRLENAVRFGSVVIIQDGEF
FDPIISRLISREFNHAGNRVTVEIGDHEVDVSGDFKLFIHSCDPSGDIPIFLRSRVRLVHFVTNKESIETRIFDITLTEE
NAEMQRKREDLIKLNTEYRLKLKNLEKRLLEELNNSQGNMLENDELMVTLNNLKKEAMNIEKKLSESEEFFPQFDNLVEE
YSIIGKHSVKIFSMLEKFGQFHWFYGISIGQFLSCFKRVFIKKSRETRAARTRVDEILWLLYQEVYCQFSTALDKKFKMI
MAMTMFCLYKFDIESEQYKEAVLTMIGVLSESSDGVPKLTVDTNDDLRYLWDYVTTKSYISALNWFKNEFFVDEWNIADV
VANSENNYFTMASERDVDGTFKLIELAKASKESLKIIPLGSIENLNYAQEEISKSKIEGGWILLQNIQMSLSWVKTYLHK
HVEETKAAEEHEKFKMFMTCHLTGDKLPAPLLQRTDRVVYEDIPGILDTVKDLWGSQFFTGKISGVWSVYCTFLLSWFHA
LITARTRLVPHGFSKKYYFNDCDFQFASVYLENVLATNSTNNIPWAQVRDHIATIVYGGKIDEEKDLEVVAKLCAHVFCG
SDNLQIVPGVRIPQPLLQQSEEEERARLTAILSNTIEPADSLSSWLQLPRESILDYERLQAKEVASSTEQLLQEM
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
3 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
4 'MAGNESIUM ION'             MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    GLY n 
1 2    ASP n 
1 3    GLN n 
1 4    LEU n 
1 5    THR n 
1 6    HIS n 
1 7    VAL n 
1 8    VAL n 
1 9    GLU n 
1 10   GLU n 
1 11   VAL n 
1 12   LYS n 
1 13   THR n 
1 14   TYR n 
1 15   ASP n 
1 16   LEU n 
1 17   VAL n 
1 18   TRP n 
1 19   ARG n 
1 20   SER n 
1 21   ILE n 
1 22   LYS n 
1 23   ASN n 
1 24   LEU n 
1 25   TRP n 
1 26   GLU n 
1 27   ASP n 
1 28   VAL n 
1 29   GLN n 
1 30   ARG n 
1 31   THR n 
1 32   PHE n 
1 33   GLU n 
1 34   THR n 
1 35   PRO n 
1 36   TRP n 
1 37   CYS n 
1 38   ARG n 
1 39   VAL n 
1 40   ASP n 
1 41   VAL n 
1 42   LEU n 
1 43   LEU n 
1 44   LEU n 
1 45   GLN n 
1 46   SER n 
1 47   ASP n 
1 48   LEU n 
1 49   ALA n 
1 50   ASN n 
1 51   PHE n 
1 52   LEU n 
1 53   ARG n 
1 54   ARG n 
1 55   ALA n 
1 56   ASP n 
1 57   GLU n 
1 58   LEU n 
1 59   PRO n 
1 60   ARG n 
1 61   ALA n 
1 62   VAL n 
1 63   LYS n 
1 64   GLN n 
1 65   PHE n 
1 66   GLU n 
1 67   MET n 
1 68   TYR n 
1 69   LYS n 
1 70   SER n 
1 71   LEU n 
1 72   PHE n 
1 73   SER n 
1 74   GLN n 
1 75   VAL n 
1 76   ASN n 
1 77   MET n 
1 78   LEU n 
1 79   THR n 
1 80   SER n 
1 81   VAL n 
1 82   ASN n 
1 83   LYS n 
1 84   ILE n 
1 85   LEU n 
1 86   VAL n 
1 87   GLU n 
1 88   LEU n 
1 89   LYS n 
1 90   ASP n 
1 91   GLY n 
1 92   ALA n 
1 93   LEU n 
1 94   LYS n 
1 95   PRO n 
1 96   ARG n 
1 97   HIS n 
1 98   TRP n 
1 99   ASN n 
1 100  MET n 
1 101  ILE n 
1 102  PHE n 
1 103  ARG n 
1 104  ASP n 
1 105  ILE n 
1 106  GLY n 
1 107  LYS n 
1 108  ARG n 
1 109  GLN n 
1 110  ILE n 
1 111  GLN n 
1 112  LYS n 
1 113  ASN n 
1 114  LEU n 
1 115  LEU n 
1 116  ASP n 
1 117  LYS n 
1 118  LEU n 
1 119  GLU n 
1 120  PHE n 
1 121  SER n 
1 122  LEU n 
1 123  LYS n 
1 124  ASP n 
1 125  VAL n 
1 126  MET n 
1 127  VAL n 
1 128  LEU n 
1 129  ASN n 
1 130  LEU n 
1 131  THR n 
1 132  LEU n 
1 133  ASN n 
1 134  GLU n 
1 135  ILE n 
1 136  LEU n 
1 137  LEU n 
1 138  THR n 
1 139  LYS n 
1 140  ILE n 
1 141  ILE n 
1 142  GLU n 
1 143  ARG n 
1 144  ALA n 
1 145  GLN n 
1 146  LYS n 
1 147  GLU n 
1 148  PHE n 
1 149  VAL n 
1 150  ILE n 
1 151  GLU n 
1 152  LYS n 
1 153  SER n 
1 154  LEU n 
1 155  ASN n 
1 156  ARG n 
1 157  ILE n 
1 158  LYS n 
1 159  LYS n 
1 160  PHE n 
1 161  TRP n 
1 162  LYS n 
1 163  GLU n 
1 164  ALA n 
1 165  GLN n 
1 166  TYR n 
1 167  GLU n 
1 168  VAL n 
1 169  ILE n 
1 170  GLU n 
1 171  HIS n 
1 172  SER n 
1 173  SER n 
1 174  GLY n 
1 175  LEU n 
1 176  LYS n 
1 177  LEU n 
1 178  VAL n 
1 179  ARG n 
1 180  GLU n 
1 181  TRP n 
1 182  ASP n 
1 183  VAL n 
1 184  LEU n 
1 185  GLU n 
1 186  GLN n 
1 187  ALA n 
1 188  CYS n 
1 189  LYS n 
1 190  GLU n 
1 191  ASP n 
1 192  LEU n 
1 193  GLU n 
1 194  GLU n 
1 195  LEU n 
1 196  VAL n 
1 197  SER n 
1 198  MET n 
1 199  LYS n 
1 200  ALA n 
1 201  SER n 
1 202  ASN n 
1 203  TYR n 
1 204  TYR n 
1 205  LYS n 
1 206  ILE n 
1 207  PHE n 
1 208  GLU n 
1 209  GLN n 
1 210  ASP n 
1 211  CYS n 
1 212  LEU n 
1 213  ASP n 
1 214  LEU n 
1 215  GLU n 
1 216  SER n 
1 217  LYS n 
1 218  LEU n 
1 219  THR n 
1 220  LYS n 
1 221  LEU n 
1 222  SER n 
1 223  GLU n 
1 224  ILE n 
1 225  GLN n 
1 226  VAL n 
1 227  ASN n 
1 228  TRP n 
1 229  VAL n 
1 230  GLU n 
1 231  VAL n 
1 232  GLN n 
1 233  PHE n 
1 234  TYR n 
1 235  TRP n 
1 236  LEU n 
1 237  ASP n 
1 238  LEU n 
1 239  TYR n 
1 240  GLY n 
1 241  ILE n 
1 242  LEU n 
1 243  GLY n 
1 244  GLU n 
1 245  ASN n 
1 246  LEU n 
1 247  ASP n 
1 248  ILE n 
1 249  GLN n 
1 250  ASN n 
1 251  PHE n 
1 252  LEU n 
1 253  PRO n 
1 254  LEU n 
1 255  GLU n 
1 256  THR n 
1 257  SER n 
1 258  LYS n 
1 259  PHE n 
1 260  LYS n 
1 261  SER n 
1 262  LEU n 
1 263  THR n 
1 264  SER n 
1 265  GLU n 
1 266  TYR n 
1 267  LYS n 
1 268  MET n 
1 269  ILE n 
1 270  THR n 
1 271  THR n 
1 272  ARG n 
1 273  ALA n 
1 274  PHE n 
1 275  GLN n 
1 276  LEU n 
1 277  ASP n 
1 278  THR n 
1 279  THR n 
1 280  ILE n 
1 281  GLU n 
1 282  VAL n 
1 283  ILE n 
1 284  HIS n 
1 285  ILE n 
1 286  PRO n 
1 287  ASN n 
1 288  PHE n 
1 289  ASP n 
1 290  THR n 
1 291  THR n 
1 292  LEU n 
1 293  LYS n 
1 294  LEU n 
1 295  THR n 
1 296  ILE n 
1 297  ASP n 
1 298  SER n 
1 299  LEU n 
1 300  LYS n 
1 301  MET n 
1 302  ILE n 
1 303  LYS n 
1 304  SER n 
1 305  SER n 
1 306  LEU n 
1 307  SER n 
1 308  THR n 
1 309  PHE n 
1 310  LEU n 
1 311  GLU n 
1 312  ARG n 
1 313  GLN n 
1 314  ARG n 
1 315  ARG n 
1 316  GLN n 
1 317  PHE n 
1 318  PRO n 
1 319  ARG n 
1 320  PHE n 
1 321  TYR n 
1 322  PHE n 
1 323  LEU n 
1 324  GLY n 
1 325  ASN n 
1 326  ASP n 
1 327  ASP n 
1 328  LEU n 
1 329  LEU n 
1 330  LYS n 
1 331  ILE n 
1 332  ILE n 
1 333  GLY n 
1 334  SER n 
1 335  GLY n 
1 336  LYS n 
1 337  HIS n 
1 338  HIS n 
1 339  ASP n 
1 340  GLN n 
1 341  VAL n 
1 342  SER n 
1 343  LYS n 
1 344  PHE n 
1 345  MET n 
1 346  LYS n 
1 347  LYS n 
1 348  MET n 
1 349  PHE n 
1 350  GLY n 
1 351  SER n 
1 352  ILE n 
1 353  GLU n 
1 354  SER n 
1 355  ILE n 
1 356  ILE n 
1 357  PHE n 
1 358  PHE n 
1 359  GLU n 
1 360  ASP n 
1 361  SER n 
1 362  ILE n 
1 363  THR n 
1 364  GLY n 
1 365  VAL n 
1 366  ARG n 
1 367  SER n 
1 368  VAL n 
1 369  GLU n 
1 370  GLY n 
1 371  GLU n 
1 372  VAL n 
1 373  LEU n 
1 374  ASN n 
1 375  LEU n 
1 376  ASN n 
1 377  GLU n 
1 378  LYS n 
1 379  ILE n 
1 380  GLU n 
1 381  LEU n 
1 382  LYS n 
1 383  ASP n 
1 384  SER n 
1 385  ILE n 
1 386  GLN n 
1 387  ALA n 
1 388  GLN n 
1 389  GLU n 
1 390  TRP n 
1 391  LEU n 
1 392  ASN n 
1 393  ILE n 
1 394  LEU n 
1 395  ASP n 
1 396  THR n 
1 397  GLU n 
1 398  ILE n 
1 399  LYS n 
1 400  LEU n 
1 401  SER n 
1 402  VAL n 
1 403  PHE n 
1 404  THR n 
1 405  GLN n 
1 406  PHE n 
1 407  ARG n 
1 408  ASP n 
1 409  CYS n 
1 410  LEU n 
1 411  GLY n 
1 412  GLN n 
1 413  LEU n 
1 414  LYS n 
1 415  ASP n 
1 416  GLY n 
1 417  THR n 
1 418  ASP n 
1 419  ILE n 
1 420  GLU n 
1 421  VAL n 
1 422  VAL n 
1 423  VAL n 
1 424  SER n 
1 425  LYS n 
1 426  TYR n 
1 427  ILE n 
1 428  PHE n 
1 429  GLN n 
1 430  ALA n 
1 431  ILE n 
1 432  LEU n 
1 433  LEU n 
1 434  SER n 
1 435  ALA n 
1 436  GLN n 
1 437  VAL n 
1 438  MET n 
1 439  TRP n 
1 440  THR n 
1 441  GLU n 
1 442  LEU n 
1 443  VAL n 
1 444  GLU n 
1 445  LYS n 
1 446  CYS n 
1 447  LEU n 
1 448  GLN n 
1 449  THR n 
1 450  ASN n 
1 451  GLU n 
1 452  PHE n 
1 453  SER n 
1 454  LYS n 
1 455  TYR n 
1 456  TRP n 
1 457  LYS n 
1 458  GLU n 
1 459  VAL n 
1 460  ASP n 
1 461  MET n 
1 462  LYS n 
1 463  ILE n 
1 464  LYS n 
1 465  GLY n 
1 466  LEU n 
1 467  LEU n 
1 468  ASP n 
1 469  LYS n 
1 470  LEU n 
1 471  ASN n 
1 472  LYS n 
1 473  SER n 
1 474  SER n 
1 475  ASP n 
1 476  ASN n 
1 477  VAL n 
1 478  LYS n 
1 479  LYS n 
1 480  LYS n 
1 481  ILE n 
1 482  GLU n 
1 483  ALA n 
1 484  LEU n 
1 485  LEU n 
1 486  VAL n 
1 487  GLU n 
1 488  TYR n 
1 489  LEU n 
1 490  HIS n 
1 491  PHE n 
1 492  ASN n 
1 493  ASN n 
1 494  VAL n 
1 495  ILE n 
1 496  GLY n 
1 497  GLN n 
1 498  LEU n 
1 499  LYS n 
1 500  ASN n 
1 501  CYS n 
1 502  SER n 
1 503  THR n 
1 504  LYS n 
1 505  GLU n 
1 506  GLU n 
1 507  ALA n 
1 508  ARG n 
1 509  LEU n 
1 510  LEU n 
1 511  TRP n 
1 512  ALA n 
1 513  LYS n 
1 514  VAL n 
1 515  GLN n 
1 516  LYS n 
1 517  PHE n 
1 518  TYR n 
1 519  GLN n 
1 520  LYS n 
1 521  ASN n 
1 522  ASP n 
1 523  THR n 
1 524  LEU n 
1 525  ASP n 
1 526  ASP n 
1 527  LEU n 
1 528  ASN n 
1 529  SER n 
1 530  VAL n 
1 531  PHE n 
1 532  ILE n 
1 533  SER n 
1 534  GLN n 
1 535  SER n 
1 536  GLY n 
1 537  TYR n 
1 538  LEU n 
1 539  LEU n 
1 540  GLN n 
1 541  TYR n 
1 542  LYS n 
1 543  PHE n 
1 544  GLU n 
1 545  TYR n 
1 546  ILE n 
1 547  GLY n 
1 548  ILE n 
1 549  PRO n 
1 550  GLU n 
1 551  ARG n 
1 552  LEU n 
1 553  ILE n 
1 554  TYR n 
1 555  THR n 
1 556  PRO n 
1 557  LEU n 
1 558  LEU n 
1 559  LEU n 
1 560  VAL n 
1 561  GLY n 
1 562  PHE n 
1 563  ALA n 
1 564  THR n 
1 565  LEU n 
1 566  THR n 
1 567  ASP n 
1 568  SER n 
1 569  LEU n 
1 570  HIS n 
1 571  GLN n 
1 572  LYS n 
1 573  TYR n 
1 574  GLY n 
1 575  GLY n 
1 576  CYS n 
1 577  PHE n 
1 578  PHE n 
1 579  GLY n 
1 580  PRO n 
1 581  ALA n 
1 582  GLY n 
1 583  THR n 
1 584  GLY n 
1 585  LYS n 
1 586  THR n 
1 587  GLU n 
1 588  THR n 
1 589  VAL n 
1 590  LYS n 
1 591  ALA n 
1 592  PHE n 
1 593  GLY n 
1 594  GLN n 
1 595  ASN n 
1 596  LEU n 
1 597  GLY n 
1 598  ARG n 
1 599  VAL n 
1 600  VAL n 
1 601  VAL n 
1 602  VAL n 
1 603  PHE n 
1 604  ASN n 
1 605  CYS n 
1 606  ASP n 
1 607  ASP n 
1 608  SER n 
1 609  PHE n 
1 610  ASP n 
1 611  TYR n 
1 612  GLN n 
1 613  VAL n 
1 614  LEU n 
1 615  SER n 
1 616  ARG n 
1 617  LEU n 
1 618  LEU n 
1 619  VAL n 
1 620  GLY n 
1 621  ILE n 
1 622  THR n 
1 623  GLN n 
1 624  ILE n 
1 625  GLY n 
1 626  ALA n 
1 627  TRP n 
1 628  GLY n 
1 629  CYS n 
1 630  PHE n 
1 631  ASP n 
1 632  GLU n 
1 633  PHE n 
1 634  ASN n 
1 635  ARG n 
1 636  LEU n 
1 637  ASP n 
1 638  GLU n 
1 639  LYS n 
1 640  VAL n 
1 641  LEU n 
1 642  SER n 
1 643  ALA n 
1 644  VAL n 
1 645  SER n 
1 646  ALA n 
1 647  ASN n 
1 648  ILE n 
1 649  GLN n 
1 650  GLN n 
1 651  ILE n 
1 652  GLN n 
1 653  ASN n 
1 654  GLY n 
1 655  LEU n 
1 656  GLN n 
1 657  VAL n 
1 658  GLY n 
1 659  LYS n 
1 660  SER n 
1 661  HIS n 
1 662  ILE n 
1 663  THR n 
1 664  LEU n 
1 665  LEU n 
1 666  GLU n 
1 667  GLU n 
1 668  GLU n 
1 669  THR n 
1 670  PRO n 
1 671  LEU n 
1 672  SER n 
1 673  PRO n 
1 674  HIS n 
1 675  THR n 
1 676  ALA n 
1 677  VAL n 
1 678  PHE n 
1 679  ILE n 
1 680  THR n 
1 681  LEU n 
1 682  ASN n 
1 683  PRO n 
1 684  GLY n 
1 685  TYR n 
1 686  ASN n 
1 687  GLY n 
1 688  ARG n 
1 689  SER n 
1 690  GLU n 
1 691  LEU n 
1 692  PRO n 
1 693  GLU n 
1 694  ASN n 
1 695  LEU n 
1 696  LYS n 
1 697  LYS n 
1 698  SER n 
1 699  PHE n 
1 700  ARG n 
1 701  GLU n 
1 702  PHE n 
1 703  SER n 
1 704  MET n 
1 705  LYS n 
1 706  SER n 
1 707  PRO n 
1 708  GLN n 
1 709  SER n 
1 710  GLY n 
1 711  THR n 
1 712  ILE n 
1 713  ALA n 
1 714  GLU n 
1 715  MET n 
1 716  ILE n 
1 717  LEU n 
1 718  GLN n 
1 719  ILE n 
1 720  MET n 
1 721  GLY n 
1 722  PHE n 
1 723  GLU n 
1 724  ASP n 
1 725  SER n 
1 726  LYS n 
1 727  SER n 
1 728  LEU n 
1 729  ALA n 
1 730  SER n 
1 731  LYS n 
1 732  ILE n 
1 733  VAL n 
1 734  HIS n 
1 735  PHE n 
1 736  LEU n 
1 737  GLU n 
1 738  LEU n 
1 739  LEU n 
1 740  SER n 
1 741  SER n 
1 742  LYS n 
1 743  CYS n 
1 744  SER n 
1 745  SER n 
1 746  MET n 
1 747  ASN n 
1 748  HIS n 
1 749  TYR n 
1 750  HIS n 
1 751  PHE n 
1 752  GLY n 
1 753  LEU n 
1 754  ARG n 
1 755  THR n 
1 756  LEU n 
1 757  LYS n 
1 758  GLY n 
1 759  VAL n 
1 760  LEU n 
1 761  ARG n 
1 762  ASN n 
1 763  CYS n 
1 764  SER n 
1 765  PRO n 
1 766  LEU n 
1 767  VAL n 
1 768  SER n 
1 769  GLU n 
1 770  PHE n 
1 771  GLY n 
1 772  GLU n 
1 773  GLY n 
1 774  GLU n 
1 775  LYS n 
1 776  THR n 
1 777  VAL n 
1 778  VAL n 
1 779  GLU n 
1 780  SER n 
1 781  LEU n 
1 782  LYS n 
1 783  ARG n 
1 784  VAL n 
1 785  ILE n 
1 786  LEU n 
1 787  PRO n 
1 788  SER n 
1 789  LEU n 
1 790  GLY n 
1 791  ASP n 
1 792  THR n 
1 793  ASP n 
1 794  GLU n 
1 795  LEU n 
1 796  VAL n 
1 797  PHE n 
1 798  LYS n 
1 799  ASP n 
1 800  GLU n 
1 801  LEU n 
1 802  SER n 
1 803  LYS n 
1 804  ILE n 
1 805  PHE n 
1 806  ASP n 
1 807  SER n 
1 808  ALA n 
1 809  GLY n 
1 810  THR n 
1 811  PRO n 
1 812  LEU n 
1 813  ASN n 
1 814  SER n 
1 815  LYS n 
1 816  ALA n 
1 817  ILE n 
1 818  VAL n 
1 819  GLN n 
1 820  CYS n 
1 821  LEU n 
1 822  LYS n 
1 823  ASP n 
1 824  ALA n 
1 825  GLY n 
1 826  GLN n 
1 827  ARG n 
1 828  SER n 
1 829  GLY n 
1 830  PHE n 
1 831  SER n 
1 832  MET n 
1 833  SER n 
1 834  GLU n 
1 835  GLU n 
1 836  PHE n 
1 837  LEU n 
1 838  LYS n 
1 839  LYS n 
1 840  CYS n 
1 841  MET n 
1 842  GLN n 
1 843  PHE n 
1 844  TYR n 
1 845  TYR n 
1 846  MET n 
1 847  GLN n 
1 848  LYS n 
1 849  THR n 
1 850  GLN n 
1 851  GLN n 
1 852  ALA n 
1 853  LEU n 
1 854  ILE n 
1 855  LEU n 
1 856  VAL n 
1 857  GLY n 
1 858  LYS n 
1 859  ALA n 
1 860  GLY n 
1 861  CYS n 
1 862  GLY n 
1 863  LYS n 
1 864  THR n 
1 865  ALA n 
1 866  THR n 
1 867  TRP n 
1 868  LYS n 
1 869  THR n 
1 870  VAL n 
1 871  ILE n 
1 872  ASP n 
1 873  ALA n 
1 874  MET n 
1 875  ALA n 
1 876  ILE n 
1 877  PHE n 
1 878  ASP n 
1 879  GLY n 
1 880  HIS n 
1 881  ALA n 
1 882  ASN n 
1 883  VAL n 
1 884  VAL n 
1 885  TYR n 
1 886  VAL n 
1 887  ILE n 
1 888  ASP n 
1 889  THR n 
1 890  LYS n 
1 891  VAL n 
1 892  LEU n 
1 893  THR n 
1 894  LYS n 
1 895  GLU n 
1 896  SER n 
1 897  LEU n 
1 898  TYR n 
1 899  GLY n 
1 900  SER n 
1 901  MET n 
1 902  LEU n 
1 903  LYS n 
1 904  ALA n 
1 905  THR n 
1 906  LEU n 
1 907  GLU n 
1 908  TRP n 
1 909  ARG n 
1 910  ASP n 
1 911  GLY n 
1 912  LEU n 
1 913  PHE n 
1 914  THR n 
1 915  SER n 
1 916  ILE n 
1 917  LEU n 
1 918  ARG n 
1 919  ARG n 
1 920  VAL n 
1 921  ASN n 
1 922  ASP n 
1 923  ASP n 
1 924  ILE n 
1 925  THR n 
1 926  GLY n 
1 927  THR n 
1 928  PHE n 
1 929  LYS n 
1 930  ASN n 
1 931  SER n 
1 932  ARG n 
1 933  ILE n 
1 934  TRP n 
1 935  VAL n 
1 936  VAL n 
1 937  PHE n 
1 938  ASP n 
1 939  SER n 
1 940  ASP n 
1 941  LEU n 
1 942  ASP n 
1 943  PRO n 
1 944  GLU n 
1 945  TYR n 
1 946  VAL n 
1 947  GLU n 
1 948  ALA n 
1 949  MET n 
1 950  ASN n 
1 951  SER n 
1 952  VAL n 
1 953  LEU n 
1 954  ASP n 
1 955  ASP n 
1 956  ASN n 
1 957  LYS n 
1 958  ILE n 
1 959  LEU n 
1 960  THR n 
1 961  LEU n 
1 962  PRO n 
1 963  ASN n 
1 964  GLY n 
1 965  GLU n 
1 966  ARG n 
1 967  LEU n 
1 968  PRO n 
1 969  ILE n 
1 970  PRO n 
1 971  PRO n 
1 972  ASN n 
1 973  PHE n 
1 974  ARG n 
1 975  ILE n 
1 976  LEU n 
1 977  PHE n 
1 978  GLU n 
1 979  THR n 
1 980  ASP n 
1 981  ASN n 
1 982  LEU n 
1 983  ASP n 
1 984  HIS n 
1 985  THR n 
1 986  THR n 
1 987  PRO n 
1 988  ALA n 
1 989  THR n 
1 990  ILE n 
1 991  THR n 
1 992  ARG n 
1 993  CYS n 
1 994  GLY n 
1 995  LEU n 
1 996  LEU n 
1 997  TRP n 
1 998  PHE n 
1 999  SER n 
1 1000 THR n 
1 1001 ASP n 
1 1002 VAL n 
1 1003 CYS n 
1 1004 SER n 
1 1005 ILE n 
1 1006 SER n 
1 1007 SER n 
1 1008 LYS n 
1 1009 ILE n 
1 1010 ASP n 
1 1011 HIS n 
1 1012 LEU n 
1 1013 LEU n 
1 1014 ASN n 
1 1015 LYS n 
1 1016 SER n 
1 1017 TYR n 
1 1018 GLU n 
1 1019 ALA n 
1 1020 LEU n 
1 1021 ASP n 
1 1022 ASN n 
1 1023 LYS n 
1 1024 LEU n 
1 1025 SER n 
1 1026 MET n 
1 1027 PHE n 
1 1028 GLU n 
1 1029 LEU n 
1 1030 ASP n 
1 1031 LYS n 
1 1032 LEU n 
1 1033 LYS n 
1 1034 ASP n 
1 1035 LEU n 
1 1036 ILE n 
1 1037 SER n 
1 1038 ASP n 
1 1039 SER n 
1 1040 PHE n 
1 1041 ASP n 
1 1042 MET n 
1 1043 ALA n 
1 1044 SER n 
1 1045 LEU n 
1 1046 THR n 
1 1047 ASN n 
1 1048 ILE n 
1 1049 PHE n 
1 1050 THR n 
1 1051 CYS n 
1 1052 SER n 
1 1053 ASN n 
1 1054 ASP n 
1 1055 LEU n 
1 1056 VAL n 
1 1057 HIS n 
1 1058 ILE n 
1 1059 LEU n 
1 1060 GLY n 
1 1061 VAL n 
1 1062 ARG n 
1 1063 THR n 
1 1064 PHE n 
1 1065 ASN n 
1 1066 LYS n 
1 1067 LEU n 
1 1068 GLU n 
1 1069 THR n 
1 1070 ALA n 
1 1071 VAL n 
1 1072 GLN n 
1 1073 LEU n 
1 1074 ALA n 
1 1075 VAL n 
1 1076 HIS n 
1 1077 LEU n 
1 1078 ILE n 
1 1079 SER n 
1 1080 SER n 
1 1081 TYR n 
1 1082 ARG n 
1 1083 GLN n 
1 1084 TRP n 
1 1085 PHE n 
1 1086 GLN n 
1 1087 ASN n 
1 1088 LEU n 
1 1089 ASP n 
1 1090 ASP n 
1 1091 LYS n 
1 1092 SER n 
1 1093 LEU n 
1 1094 LYS n 
1 1095 ASP n 
1 1096 VAL n 
1 1097 ILE n 
1 1098 THR n 
1 1099 LEU n 
1 1100 LEU n 
1 1101 ILE n 
1 1102 LYS n 
1 1103 ARG n 
1 1104 SER n 
1 1105 LEU n 
1 1106 LEU n 
1 1107 TYR n 
1 1108 ALA n 
1 1109 LEU n 
1 1110 ALA n 
1 1111 GLY n 
1 1112 ASP n 
1 1113 SER n 
1 1114 THR n 
1 1115 GLY n 
1 1116 GLU n 
1 1117 SER n 
1 1118 GLN n 
1 1119 ARG n 
1 1120 ALA n 
1 1121 PHE n 
1 1122 ILE n 
1 1123 GLN n 
1 1124 THR n 
1 1125 ILE n 
1 1126 ASN n 
1 1127 THR n 
1 1128 TYR n 
1 1129 PHE n 
1 1130 GLY n 
1 1131 HIS n 
1 1132 ASP n 
1 1133 SER n 
1 1134 GLN n 
1 1135 GLU n 
1 1136 LEU n 
1 1137 SER n 
1 1138 ASP n 
1 1139 TYR n 
1 1140 SER n 
1 1141 THR n 
1 1142 ILE n 
1 1143 VAL n 
1 1144 ILE n 
1 1145 ALA n 
1 1146 ASN n 
1 1147 ASP n 
1 1148 LYS n 
1 1149 LEU n 
1 1150 SER n 
1 1151 PHE n 
1 1152 SER n 
1 1153 SER n 
1 1154 PHE n 
1 1155 CYS n 
1 1156 SER n 
1 1157 GLU n 
1 1158 ILE n 
1 1159 PRO n 
1 1160 SER n 
1 1161 VAL n 
1 1162 SER n 
1 1163 LEU n 
1 1164 GLU n 
1 1165 ALA n 
1 1166 HIS n 
1 1167 GLU n 
1 1168 VAL n 
1 1169 MET n 
1 1170 ARG n 
1 1171 PRO n 
1 1172 ASP n 
1 1173 ILE n 
1 1174 VAL n 
1 1175 ILE n 
1 1176 PRO n 
1 1177 THR n 
1 1178 ILE n 
1 1179 ASP n 
1 1180 THR n 
1 1181 ILE n 
1 1182 LYS n 
1 1183 HIS n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 ILE n 
1 1187 PHE n 
1 1188 TYR n 
1 1189 ASP n 
1 1190 LEU n 
1 1191 LEU n 
1 1192 ASN n 
1 1193 SER n 
1 1194 LYS n 
1 1195 ARG n 
1 1196 GLY n 
1 1197 ILE n 
1 1198 ILE n 
1 1199 LEU n 
1 1200 CYS n 
1 1201 GLY n 
1 1202 PRO n 
1 1203 PRO n 
1 1204 GLY n 
1 1205 SER n 
1 1206 GLY n 
1 1207 LYS n 
1 1208 THR n 
1 1209 MET n 
1 1210 ILE n 
1 1211 MET n 
1 1212 ASN n 
1 1213 ASN n 
1 1214 ALA n 
1 1215 LEU n 
1 1216 ARG n 
1 1217 ASN n 
1 1218 SER n 
1 1219 SER n 
1 1220 LEU n 
1 1221 TYR n 
1 1222 ASP n 
1 1223 VAL n 
1 1224 VAL n 
1 1225 GLY n 
1 1226 ILE n 
1 1227 ASN n 
1 1228 PHE n 
1 1229 SER n 
1 1230 LYS n 
1 1231 ASP n 
1 1232 THR n 
1 1233 THR n 
1 1234 THR n 
1 1235 GLU n 
1 1236 HIS n 
1 1237 ILE n 
1 1238 LEU n 
1 1239 SER n 
1 1240 ALA n 
1 1241 LEU n 
1 1242 HIS n 
1 1243 ARG n 
1 1244 HIS n 
1 1245 THR n 
1 1246 ASN n 
1 1247 TYR n 
1 1248 VAL n 
1 1249 THR n 
1 1250 THR n 
1 1251 SER n 
1 1252 LYS n 
1 1253 GLY n 
1 1254 LEU n 
1 1255 THR n 
1 1256 LEU n 
1 1257 LEU n 
1 1258 PRO n 
1 1259 LYS n 
1 1260 SER n 
1 1261 ASP n 
1 1262 ILE n 
1 1263 LYS n 
1 1264 ASN n 
1 1265 LEU n 
1 1266 VAL n 
1 1267 LEU n 
1 1268 PHE n 
1 1269 CYS n 
1 1270 ASP n 
1 1271 GLU n 
1 1272 ILE n 
1 1273 ASN n 
1 1274 LEU n 
1 1275 PRO n 
1 1276 LYS n 
1 1277 LEU n 
1 1278 ASP n 
1 1279 LYS n 
1 1280 TYR n 
1 1281 GLY n 
1 1282 SER n 
1 1283 GLN n 
1 1284 ASN n 
1 1285 VAL n 
1 1286 VAL n 
1 1287 LEU n 
1 1288 PHE n 
1 1289 LEU n 
1 1290 ARG n 
1 1291 GLN n 
1 1292 LEU n 
1 1293 MET n 
1 1294 GLU n 
1 1295 LYS n 
1 1296 GLN n 
1 1297 GLY n 
1 1298 PHE n 
1 1299 TRP n 
1 1300 LYS n 
1 1301 THR n 
1 1302 PRO n 
1 1303 GLU n 
1 1304 ASN n 
1 1305 LYS n 
1 1306 TRP n 
1 1307 VAL n 
1 1308 THR n 
1 1309 ILE n 
1 1310 GLU n 
1 1311 ARG n 
1 1312 ILE n 
1 1313 HIS n 
1 1314 ILE n 
1 1315 VAL n 
1 1316 GLY n 
1 1317 ALA n 
1 1318 CYS n 
1 1319 ASN n 
1 1320 PRO n 
1 1321 PRO n 
1 1322 THR n 
1 1323 ASP n 
1 1324 PRO n 
1 1325 GLY n 
1 1326 ARG n 
1 1327 ILE n 
1 1328 PRO n 
1 1329 MET n 
1 1330 SER n 
1 1331 GLU n 
1 1332 ARG n 
1 1333 PHE n 
1 1334 THR n 
1 1335 ARG n 
1 1336 HIS n 
1 1337 ALA n 
1 1338 ALA n 
1 1339 ILE n 
1 1340 LEU n 
1 1341 TYR n 
1 1342 LEU n 
1 1343 GLY n 
1 1344 TYR n 
1 1345 PRO n 
1 1346 SER n 
1 1347 GLY n 
1 1348 LYS n 
1 1349 SER n 
1 1350 LEU n 
1 1351 SER n 
1 1352 GLN n 
1 1353 ILE n 
1 1354 TYR n 
1 1355 GLU n 
1 1356 ILE n 
1 1357 TYR n 
1 1358 TYR n 
1 1359 LYS n 
1 1360 ALA n 
1 1361 ILE n 
1 1362 PHE n 
1 1363 LYS n 
1 1364 LEU n 
1 1365 VAL n 
1 1366 PRO n 
1 1367 GLU n 
1 1368 PHE n 
1 1369 ARG n 
1 1370 SER n 
1 1371 TYR n 
1 1372 THR n 
1 1373 GLU n 
1 1374 PRO n 
1 1375 PHE n 
1 1376 ALA n 
1 1377 ARG n 
1 1378 ALA n 
1 1379 SER n 
1 1380 VAL n 
1 1381 HIS n 
1 1382 LEU n 
1 1383 TYR n 
1 1384 ASN n 
1 1385 GLU n 
1 1386 CYS n 
1 1387 LYS n 
1 1388 ALA n 
1 1389 ARG n 
1 1390 TYR n 
1 1391 SER n 
1 1392 THR n 
1 1393 GLY n 
1 1394 LEU n 
1 1395 GLN n 
1 1396 SER n 
1 1397 HIS n 
1 1398 TYR n 
1 1399 LEU n 
1 1400 PHE n 
1 1401 SER n 
1 1402 PRO n 
1 1403 ARG n 
1 1404 GLU n 
1 1405 LEU n 
1 1406 THR n 
1 1407 ARG n 
1 1408 LEU n 
1 1409 VAL n 
1 1410 ARG n 
1 1411 GLY n 
1 1412 VAL n 
1 1413 TYR n 
1 1414 THR n 
1 1415 ALA n 
1 1416 ILE n 
1 1417 ASN n 
1 1418 THR n 
1 1419 GLY n 
1 1420 PRO n 
1 1421 ARG n 
1 1422 GLN n 
1 1423 THR n 
1 1424 LEU n 
1 1425 ARG n 
1 1426 SER n 
1 1427 LEU n 
1 1428 ILE n 
1 1429 ARG n 
1 1430 LEU n 
1 1431 TRP n 
1 1432 ALA n 
1 1433 TYR n 
1 1434 GLU n 
1 1435 ALA n 
1 1436 TRP n 
1 1437 ARG n 
1 1438 ILE n 
1 1439 PHE n 
1 1440 ALA n 
1 1441 ASP n 
1 1442 ARG n 
1 1443 LEU n 
1 1444 VAL n 
1 1445 GLY n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 GLU n 
1 1449 LYS n 
1 1450 ASN n 
1 1451 SER n 
1 1452 PHE n 
1 1453 GLU n 
1 1454 GLN n 
1 1455 LEU n 
1 1456 LEU n 
1 1457 TYR n 
1 1458 GLU n 
1 1459 THR n 
1 1460 VAL n 
1 1461 ASP n 
1 1462 LYS n 
1 1463 TYR n 
1 1464 LEU n 
1 1465 PRO n 
1 1466 ASN n 
1 1467 GLN n 
1 1468 ASP n 
1 1469 LEU n 
1 1470 GLY n 
1 1471 ASN n 
1 1472 ILE n 
1 1473 SER n 
1 1474 SER n 
1 1475 THR n 
1 1476 SER n 
1 1477 LEU n 
1 1478 LEU n 
1 1479 PHE n 
1 1480 SER n 
1 1481 GLY n 
1 1482 LEU n 
1 1483 LEU n 
1 1484 SER n 
1 1485 LEU n 
1 1486 ASP n 
1 1487 PHE n 
1 1488 LYS n 
1 1489 GLU n 
1 1490 VAL n 
1 1491 ASN n 
1 1492 LYS n 
1 1493 THR n 
1 1494 ASP n 
1 1495 LEU n 
1 1496 VAL n 
1 1497 ASN n 
1 1498 PHE n 
1 1499 ILE n 
1 1500 GLU n 
1 1501 GLU n 
1 1502 ARG n 
1 1503 PHE n 
1 1504 LYS n 
1 1505 THR n 
1 1506 PHE n 
1 1507 CYS n 
1 1508 ASP n 
1 1509 GLU n 
1 1510 GLU n 
1 1511 LEU n 
1 1512 GLU n 
1 1513 VAL n 
1 1514 PRO n 
1 1515 MET n 
1 1516 VAL n 
1 1517 ILE n 
1 1518 HIS n 
1 1519 GLU n 
1 1520 SER n 
1 1521 MET n 
1 1522 VAL n 
1 1523 ASP n 
1 1524 HIS n 
1 1525 ILE n 
1 1526 LEU n 
1 1527 ARG n 
1 1528 ILE n 
1 1529 ASP n 
1 1530 ARG n 
1 1531 ALA n 
1 1532 LEU n 
1 1533 LYS n 
1 1534 GLN n 
1 1535 VAL n 
1 1536 GLN n 
1 1537 GLY n 
1 1538 HIS n 
1 1539 MET n 
1 1540 MET n 
1 1541 LEU n 
1 1542 ILE n 
1 1543 GLY n 
1 1544 ALA n 
1 1545 SER n 
1 1546 ARG n 
1 1547 THR n 
1 1548 GLY n 
1 1549 LYS n 
1 1550 THR n 
1 1551 ILE n 
1 1552 LEU n 
1 1553 THR n 
1 1554 ARG n 
1 1555 PHE n 
1 1556 VAL n 
1 1557 ALA n 
1 1558 TRP n 
1 1559 LEU n 
1 1560 ASN n 
1 1561 GLY n 
1 1562 LEU n 
1 1563 LYS n 
1 1564 ILE n 
1 1565 VAL n 
1 1566 GLN n 
1 1567 PRO n 
1 1568 LYS n 
1 1569 ILE n 
1 1570 HIS n 
1 1571 ARG n 
1 1572 HIS n 
1 1573 SER n 
1 1574 ASN n 
1 1575 LEU n 
1 1576 SER n 
1 1577 ASP n 
1 1578 PHE n 
1 1579 ASP n 
1 1580 MET n 
1 1581 ILE n 
1 1582 LEU n 
1 1583 LYS n 
1 1584 LYS n 
1 1585 ALA n 
1 1586 ILE n 
1 1587 SER n 
1 1588 ASP n 
1 1589 CYS n 
1 1590 SER n 
1 1591 LEU n 
1 1592 LYS n 
1 1593 GLU n 
1 1594 SER n 
1 1595 ARG n 
1 1596 THR n 
1 1597 CYS n 
1 1598 LEU n 
1 1599 ILE n 
1 1600 ILE n 
1 1601 ASP n 
1 1602 GLU n 
1 1603 SER n 
1 1604 ASN n 
1 1605 ILE n 
1 1606 LEU n 
1 1607 GLU n 
1 1608 THR n 
1 1609 ALA n 
1 1610 PHE n 
1 1611 LEU n 
1 1612 GLU n 
1 1613 ARG n 
1 1614 MET n 
1 1615 ASN n 
1 1616 THR n 
1 1617 LEU n 
1 1618 LEU n 
1 1619 ALA n 
1 1620 ASN n 
1 1621 ALA n 
1 1622 ASP n 
1 1623 ILE n 
1 1624 PRO n 
1 1625 ASP n 
1 1626 LEU n 
1 1627 PHE n 
1 1628 GLN n 
1 1629 GLY n 
1 1630 GLU n 
1 1631 GLU n 
1 1632 TYR n 
1 1633 ASP n 
1 1634 LYS n 
1 1635 LEU n 
1 1636 LEU n 
1 1637 ASN n 
1 1638 ASN n 
1 1639 LEU n 
1 1640 ARG n 
1 1641 ASN n 
1 1642 LYS n 
1 1643 THR n 
1 1644 ARG n 
1 1645 SER n 
1 1646 LEU n 
1 1647 GLY n 
1 1648 LEU n 
1 1649 LEU n 
1 1650 LEU n 
1 1651 ASP n 
1 1652 THR n 
1 1653 GLU n 
1 1654 GLN n 
1 1655 GLU n 
1 1656 LEU n 
1 1657 TYR n 
1 1658 ASP n 
1 1659 TRP n 
1 1660 PHE n 
1 1661 VAL n 
1 1662 GLY n 
1 1663 GLU n 
1 1664 ILE n 
1 1665 ALA n 
1 1666 LYS n 
1 1667 ASN n 
1 1668 LEU n 
1 1669 HIS n 
1 1670 VAL n 
1 1671 VAL n 
1 1672 PHE n 
1 1673 THR n 
1 1674 ILE n 
1 1675 CYS n 
1 1676 ASP n 
1 1677 PRO n 
1 1678 THR n 
1 1679 ASN n 
1 1680 ASN n 
1 1681 LYS n 
1 1682 SER n 
1 1683 SER n 
1 1684 ALA n 
1 1685 MET n 
1 1686 ILE n 
1 1687 SER n 
1 1688 SER n 
1 1689 PRO n 
1 1690 ALA n 
1 1691 LEU n 
1 1692 PHE n 
1 1693 ASN n 
1 1694 ARG n 
1 1695 CYS n 
1 1696 ILE n 
1 1697 ILE n 
1 1698 ASN n 
1 1699 TRP n 
1 1700 MET n 
1 1701 GLY n 
1 1702 ASP n 
1 1703 TRP n 
1 1704 ASP n 
1 1705 THR n 
1 1706 LYS n 
1 1707 THR n 
1 1708 MET n 
1 1709 SER n 
1 1710 GLN n 
1 1711 VAL n 
1 1712 ALA n 
1 1713 ASN n 
1 1714 ASN n 
1 1715 MET n 
1 1716 VAL n 
1 1717 ASP n 
1 1718 VAL n 
1 1719 VAL n 
1 1720 PRO n 
1 1721 MET n 
1 1722 GLU n 
1 1723 PHE n 
1 1724 THR n 
1 1725 ASP n 
1 1726 PHE n 
1 1727 ILE n 
1 1728 VAL n 
1 1729 PRO n 
1 1730 GLU n 
1 1731 VAL n 
1 1732 ASN n 
1 1733 LYS n 
1 1734 GLU n 
1 1735 LEU n 
1 1736 VAL n 
1 1737 PHE n 
1 1738 THR n 
1 1739 GLU n 
1 1740 PRO n 
1 1741 ILE n 
1 1742 GLN n 
1 1743 THR n 
1 1744 ILE n 
1 1745 ARG n 
1 1746 ASP n 
1 1747 ALA n 
1 1748 VAL n 
1 1749 VAL n 
1 1750 ASN n 
1 1751 ILE n 
1 1752 LEU n 
1 1753 ILE n 
1 1754 HIS n 
1 1755 PHE n 
1 1756 ASP n 
1 1757 ARG n 
1 1758 ASN n 
1 1759 PHE n 
1 1760 TYR n 
1 1761 GLN n 
1 1762 LYS n 
1 1763 MET n 
1 1764 LYS n 
1 1765 VAL n 
1 1766 GLY n 
1 1767 VAL n 
1 1768 ASN n 
1 1769 PRO n 
1 1770 ARG n 
1 1771 SER n 
1 1772 PRO n 
1 1773 GLY n 
1 1774 TYR n 
1 1775 PHE n 
1 1776 ILE n 
1 1777 ASP n 
1 1778 GLY n 
1 1779 LEU n 
1 1780 ARG n 
1 1781 ALA n 
1 1782 LEU n 
1 1783 VAL n 
1 1784 LYS n 
1 1785 LEU n 
1 1786 VAL n 
1 1787 THR n 
1 1788 ALA n 
1 1789 LYS n 
1 1790 TYR n 
1 1791 GLN n 
1 1792 ASP n 
1 1793 LEU n 
1 1794 GLN n 
1 1795 GLU n 
1 1796 ASN n 
1 1797 GLN n 
1 1798 ARG n 
1 1799 PHE n 
1 1800 VAL n 
1 1801 ASN n 
1 1802 VAL n 
1 1803 GLY n 
1 1804 LEU n 
1 1805 GLU n 
1 1806 LYS n 
1 1807 LEU n 
1 1808 ASN n 
1 1809 GLU n 
1 1810 SER n 
1 1811 VAL n 
1 1812 LEU n 
1 1813 LYS n 
1 1814 VAL n 
1 1815 ASN n 
1 1816 GLU n 
1 1817 LEU n 
1 1818 ASN n 
1 1819 LYS n 
1 1820 THR n 
1 1821 LEU n 
1 1822 SER n 
1 1823 LYS n 
1 1824 LYS n 
1 1825 SER n 
1 1826 THR n 
1 1827 GLU n 
1 1828 LEU n 
1 1829 THR n 
1 1830 GLU n 
1 1831 LYS n 
1 1832 GLU n 
1 1833 LYS n 
1 1834 GLU n 
1 1835 ALA n 
1 1836 ARG n 
1 1837 SER n 
1 1838 THR n 
1 1839 LEU n 
1 1840 ASP n 
1 1841 LYS n 
1 1842 MET n 
1 1843 LEU n 
1 1844 MET n 
1 1845 GLU n 
1 1846 GLN n 
1 1847 ASN n 
1 1848 GLU n 
1 1849 SER n 
1 1850 GLU n 
1 1851 ARG n 
1 1852 LYS n 
1 1853 GLN n 
1 1854 GLU n 
1 1855 ALA n 
1 1856 THR n 
1 1857 GLU n 
1 1858 GLU n 
1 1859 ILE n 
1 1860 LYS n 
1 1861 LYS n 
1 1862 ILE n 
1 1863 LEU n 
1 1864 LYS n 
1 1865 VAL n 
1 1866 GLN n 
1 1867 GLU n 
1 1868 GLU n 
1 1869 ASP n 
1 1870 ILE n 
1 1871 ARG n 
1 1872 LYS n 
1 1873 ARG n 
1 1874 LYS n 
1 1875 GLU n 
1 1876 VAL n 
1 1877 VAL n 
1 1878 MET n 
1 1879 LYS n 
1 1880 SER n 
1 1881 ILE n 
1 1882 GLN n 
1 1883 ASP n 
1 1884 ILE n 
1 1885 GLU n 
1 1886 PRO n 
1 1887 THR n 
1 1888 ILE n 
1 1889 LEU n 
1 1890 GLU n 
1 1891 ALA n 
1 1892 GLN n 
1 1893 ARG n 
1 1894 GLY n 
1 1895 VAL n 
1 1896 LYS n 
1 1897 ASN n 
1 1898 ILE n 
1 1899 LYS n 
1 1900 LYS n 
1 1901 GLN n 
1 1902 GLN n 
1 1903 LEU n 
1 1904 THR n 
1 1905 GLU n 
1 1906 ILE n 
1 1907 ARG n 
1 1908 SER n 
1 1909 MET n 
1 1910 VAL n 
1 1911 ASN n 
1 1912 PRO n 
1 1913 PRO n 
1 1914 SER n 
1 1915 GLY n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ILE n 
1 1919 VAL n 
1 1920 MET n 
1 1921 GLU n 
1 1922 ALA n 
1 1923 VAL n 
1 1924 CYS n 
1 1925 ALA n 
1 1926 ILE n 
1 1927 LEU n 
1 1928 GLY n 
1 1929 TYR n 
1 1930 GLN n 
1 1931 PHE n 
1 1932 SER n 
1 1933 ASN n 
1 1934 TRP n 
1 1935 ARG n 
1 1936 ASP n 
1 1937 ILE n 
1 1938 GLN n 
1 1939 GLN n 
1 1940 PHE n 
1 1941 ILE n 
1 1942 ARG n 
1 1943 LYS n 
1 1944 ASP n 
1 1945 ASP n 
1 1946 PHE n 
1 1947 ILE n 
1 1948 HIS n 
1 1949 ASN n 
1 1950 ILE n 
1 1951 VAL n 
1 1952 HIS n 
1 1953 TYR n 
1 1954 ASP n 
1 1955 THR n 
1 1956 THR n 
1 1957 LEU n 
1 1958 HIS n 
1 1959 MET n 
1 1960 LYS n 
1 1961 PRO n 
1 1962 GLN n 
1 1963 ILE n 
1 1964 ARG n 
1 1965 LYS n 
1 1966 TYR n 
1 1967 MET n 
1 1968 GLU n 
1 1969 GLU n 
1 1970 GLU n 
1 1971 PHE n 
1 1972 LEU n 
1 1973 SER n 
1 1974 ASP n 
1 1975 PRO n 
1 1976 ASN n 
1 1977 PHE n 
1 1978 THR n 
1 1979 TYR n 
1 1980 GLU n 
1 1981 THR n 
1 1982 ILE n 
1 1983 ASN n 
1 1984 ARG n 
1 1985 ALA n 
1 1986 SER n 
1 1987 LYS n 
1 1988 ALA n 
1 1989 CYS n 
1 1990 GLY n 
1 1991 PRO n 
1 1992 LEU n 
1 1993 TYR n 
1 1994 GLN n 
1 1995 TRP n 
1 1996 VAL n 
1 1997 ASN n 
1 1998 ALA n 
1 1999 GLN n 
1 2000 ILE n 
1 2001 ASN n 
1 2002 PHE n 
1 2003 SER n 
1 2004 LYS n 
1 2005 VAL n 
1 2006 LEU n 
1 2007 GLU n 
1 2008 ASN n 
1 2009 VAL n 
1 2010 ASP n 
1 2011 PRO n 
1 2012 LEU n 
1 2013 ARG n 
1 2014 GLN n 
1 2015 GLU n 
1 2016 MET n 
1 2017 LYS n 
1 2018 ARG n 
1 2019 ILE n 
1 2020 GLU n 
1 2021 PHE n 
1 2022 GLU n 
1 2023 SER n 
1 2024 LEU n 
1 2025 LYS n 
1 2026 THR n 
1 2027 LYS n 
1 2028 ALA n 
1 2029 ASN n 
1 2030 LEU n 
1 2031 LEU n 
1 2032 ALA n 
1 2033 ALA n 
1 2034 GLU n 
1 2035 GLU n 
1 2036 MET n 
1 2037 THR n 
1 2038 GLN n 
1 2039 ASP n 
1 2040 LEU n 
1 2041 GLU n 
1 2042 ALA n 
1 2043 SER n 
1 2044 ILE n 
1 2045 GLU n 
1 2046 VAL n 
1 2047 SER n 
1 2048 LYS n 
1 2049 GLN n 
1 2050 LYS n 
1 2051 TYR n 
1 2052 SER n 
1 2053 LEU n 
1 2054 LEU n 
1 2055 ILE n 
1 2056 ARG n 
1 2057 ASP n 
1 2058 VAL n 
1 2059 GLU n 
1 2060 ALA n 
1 2061 ILE n 
1 2062 LYS n 
1 2063 THR n 
1 2064 GLU n 
1 2065 MET n 
1 2066 SER n 
1 2067 ASN n 
1 2068 VAL n 
1 2069 GLN n 
1 2070 ALA n 
1 2071 ASN n 
1 2072 LEU n 
1 2073 ASP n 
1 2074 ARG n 
1 2075 SER n 
1 2076 ILE n 
1 2077 SER n 
1 2078 LEU n 
1 2079 VAL n 
1 2080 LYS n 
1 2081 SER n 
1 2082 LEU n 
1 2083 THR n 
1 2084 PHE n 
1 2085 GLU n 
1 2086 LYS n 
1 2087 GLU n 
1 2088 ARG n 
1 2089 TRP n 
1 2090 LEU n 
1 2091 ASN n 
1 2092 THR n 
1 2093 THR n 
1 2094 LYS n 
1 2095 GLN n 
1 2096 PHE n 
1 2097 SER n 
1 2098 LYS n 
1 2099 THR n 
1 2100 SER n 
1 2101 GLN n 
1 2102 GLU n 
1 2103 LEU n 
1 2104 ILE n 
1 2105 GLY n 
1 2106 ASN n 
1 2107 CYS n 
1 2108 ILE n 
1 2109 ILE n 
1 2110 SER n 
1 2111 SER n 
1 2112 ILE n 
1 2113 TYR n 
1 2114 GLU n 
1 2115 THR n 
1 2116 TYR n 
1 2117 PHE n 
1 2118 GLY n 
1 2119 HIS n 
1 2120 LEU n 
1 2121 ASN n 
1 2122 GLU n 
1 2123 ARG n 
1 2124 GLU n 
1 2125 ARG n 
1 2126 GLY n 
1 2127 ASP n 
1 2128 MET n 
1 2129 LEU n 
1 2130 VAL n 
1 2131 ILE n 
1 2132 LEU n 
1 2133 LYS n 
1 2134 ARG n 
1 2135 LEU n 
1 2136 LEU n 
1 2137 GLY n 
1 2138 LYS n 
1 2139 PHE n 
1 2140 ALA n 
1 2141 VAL n 
1 2142 LYS n 
1 2143 TYR n 
1 2144 ASP n 
1 2145 VAL n 
1 2146 ASN n 
1 2147 TYR n 
1 2148 ARG n 
1 2149 PHE n 
1 2150 ILE n 
1 2151 ASP n 
1 2152 TYR n 
1 2153 LEU n 
1 2154 VAL n 
1 2155 THR n 
1 2156 LEU n 
1 2157 ASP n 
1 2158 GLU n 
1 2159 LYS n 
1 2160 MET n 
1 2161 LYS n 
1 2162 TRP n 
1 2163 LEU n 
1 2164 GLU n 
1 2165 CYS n 
1 2166 GLY n 
1 2167 LEU n 
1 2168 ASP n 
1 2169 LYS n 
1 2170 ASN n 
1 2171 ASP n 
1 2172 TYR n 
1 2173 PHE n 
1 2174 LEU n 
1 2175 GLU n 
1 2176 ASN n 
1 2177 MET n 
1 2178 SER n 
1 2179 ILE n 
1 2180 VAL n 
1 2181 MET n 
1 2182 ASN n 
1 2183 SER n 
1 2184 GLN n 
1 2185 ASP n 
1 2186 ALA n 
1 2187 VAL n 
1 2188 PRO n 
1 2189 PHE n 
1 2190 LEU n 
1 2191 LEU n 
1 2192 ASP n 
1 2193 PRO n 
1 2194 SER n 
1 2195 SER n 
1 2196 HIS n 
1 2197 MET n 
1 2198 ILE n 
1 2199 THR n 
1 2200 VAL n 
1 2201 ILE n 
1 2202 SER n 
1 2203 ASN n 
1 2204 TYR n 
1 2205 TYR n 
1 2206 GLY n 
1 2207 ASN n 
1 2208 LYS n 
1 2209 THR n 
1 2210 VAL n 
1 2211 LEU n 
1 2212 LEU n 
1 2213 SER n 
1 2214 PHE n 
1 2215 LEU n 
1 2216 GLU n 
1 2217 GLU n 
1 2218 GLY n 
1 2219 PHE n 
1 2220 VAL n 
1 2221 LYS n 
1 2222 ARG n 
1 2223 LEU n 
1 2224 GLU n 
1 2225 ASN n 
1 2226 ALA n 
1 2227 VAL n 
1 2228 ARG n 
1 2229 PHE n 
1 2230 GLY n 
1 2231 SER n 
1 2232 VAL n 
1 2233 VAL n 
1 2234 ILE n 
1 2235 ILE n 
1 2236 GLN n 
1 2237 ASP n 
1 2238 GLY n 
1 2239 GLU n 
1 2240 PHE n 
1 2241 PHE n 
1 2242 ASP n 
1 2243 PRO n 
1 2244 ILE n 
1 2245 ILE n 
1 2246 SER n 
1 2247 ARG n 
1 2248 LEU n 
1 2249 ILE n 
1 2250 SER n 
1 2251 ARG n 
1 2252 GLU n 
1 2253 PHE n 
1 2254 ASN n 
1 2255 HIS n 
1 2256 ALA n 
1 2257 GLY n 
1 2258 ASN n 
1 2259 ARG n 
1 2260 VAL n 
1 2261 THR n 
1 2262 VAL n 
1 2263 GLU n 
1 2264 ILE n 
1 2265 GLY n 
1 2266 ASP n 
1 2267 HIS n 
1 2268 GLU n 
1 2269 VAL n 
1 2270 ASP n 
1 2271 VAL n 
1 2272 SER n 
1 2273 GLY n 
1 2274 ASP n 
1 2275 PHE n 
1 2276 LYS n 
1 2277 LEU n 
1 2278 PHE n 
1 2279 ILE n 
1 2280 HIS n 
1 2281 SER n 
1 2282 CYS n 
1 2283 ASP n 
1 2284 PRO n 
1 2285 SER n 
1 2286 GLY n 
1 2287 ASP n 
1 2288 ILE n 
1 2289 PRO n 
1 2290 ILE n 
1 2291 PHE n 
1 2292 LEU n 
1 2293 ARG n 
1 2294 SER n 
1 2295 ARG n 
1 2296 VAL n 
1 2297 ARG n 
1 2298 LEU n 
1 2299 VAL n 
1 2300 HIS n 
1 2301 PHE n 
1 2302 VAL n 
1 2303 THR n 
1 2304 ASN n 
1 2305 LYS n 
1 2306 GLU n 
1 2307 SER n 
1 2308 ILE n 
1 2309 GLU n 
1 2310 THR n 
1 2311 ARG n 
1 2312 ILE n 
1 2313 PHE n 
1 2314 ASP n 
1 2315 ILE n 
1 2316 THR n 
1 2317 LEU n 
1 2318 THR n 
1 2319 GLU n 
1 2320 GLU n 
1 2321 ASN n 
1 2322 ALA n 
1 2323 GLU n 
1 2324 MET n 
1 2325 GLN n 
1 2326 ARG n 
1 2327 LYS n 
1 2328 ARG n 
1 2329 GLU n 
1 2330 ASP n 
1 2331 LEU n 
1 2332 ILE n 
1 2333 LYS n 
1 2334 LEU n 
1 2335 ASN n 
1 2336 THR n 
1 2337 GLU n 
1 2338 TYR n 
1 2339 ARG n 
1 2340 LEU n 
1 2341 LYS n 
1 2342 LEU n 
1 2343 LYS n 
1 2344 ASN n 
1 2345 LEU n 
1 2346 GLU n 
1 2347 LYS n 
1 2348 ARG n 
1 2349 LEU n 
1 2350 LEU n 
1 2351 GLU n 
1 2352 GLU n 
1 2353 LEU n 
1 2354 ASN n 
1 2355 ASN n 
1 2356 SER n 
1 2357 GLN n 
1 2358 GLY n 
1 2359 ASN n 
1 2360 MET n 
1 2361 LEU n 
1 2362 GLU n 
1 2363 ASN n 
1 2364 ASP n 
1 2365 GLU n 
1 2366 LEU n 
1 2367 MET n 
1 2368 VAL n 
1 2369 THR n 
1 2370 LEU n 
1 2371 ASN n 
1 2372 ASN n 
1 2373 LEU n 
1 2374 LYS n 
1 2375 LYS n 
1 2376 GLU n 
1 2377 ALA n 
1 2378 MET n 
1 2379 ASN n 
1 2380 ILE n 
1 2381 GLU n 
1 2382 LYS n 
1 2383 LYS n 
1 2384 LEU n 
1 2385 SER n 
1 2386 GLU n 
1 2387 SER n 
1 2388 GLU n 
1 2389 GLU n 
1 2390 PHE n 
1 2391 PHE n 
1 2392 PRO n 
1 2393 GLN n 
1 2394 PHE n 
1 2395 ASP n 
1 2396 ASN n 
1 2397 LEU n 
1 2398 VAL n 
1 2399 GLU n 
1 2400 GLU n 
1 2401 TYR n 
1 2402 SER n 
1 2403 ILE n 
1 2404 ILE n 
1 2405 GLY n 
1 2406 LYS n 
1 2407 HIS n 
1 2408 SER n 
1 2409 VAL n 
1 2410 LYS n 
1 2411 ILE n 
1 2412 PHE n 
1 2413 SER n 
1 2414 MET n 
1 2415 LEU n 
1 2416 GLU n 
1 2417 LYS n 
1 2418 PHE n 
1 2419 GLY n 
1 2420 GLN n 
1 2421 PHE n 
1 2422 HIS n 
1 2423 TRP n 
1 2424 PHE n 
1 2425 TYR n 
1 2426 GLY n 
1 2427 ILE n 
1 2428 SER n 
1 2429 ILE n 
1 2430 GLY n 
1 2431 GLN n 
1 2432 PHE n 
1 2433 LEU n 
1 2434 SER n 
1 2435 CYS n 
1 2436 PHE n 
1 2437 LYS n 
1 2438 ARG n 
1 2439 VAL n 
1 2440 PHE n 
1 2441 ILE n 
1 2442 LYS n 
1 2443 LYS n 
1 2444 SER n 
1 2445 ARG n 
1 2446 GLU n 
1 2447 THR n 
1 2448 ARG n 
1 2449 ALA n 
1 2450 ALA n 
1 2451 ARG n 
1 2452 THR n 
1 2453 ARG n 
1 2454 VAL n 
1 2455 ASP n 
1 2456 GLU n 
1 2457 ILE n 
1 2458 LEU n 
1 2459 TRP n 
1 2460 LEU n 
1 2461 LEU n 
1 2462 TYR n 
1 2463 GLN n 
1 2464 GLU n 
1 2465 VAL n 
1 2466 TYR n 
1 2467 CYS n 
1 2468 GLN n 
1 2469 PHE n 
1 2470 SER n 
1 2471 THR n 
1 2472 ALA n 
1 2473 LEU n 
1 2474 ASP n 
1 2475 LYS n 
1 2476 LYS n 
1 2477 PHE n 
1 2478 LYS n 
1 2479 MET n 
1 2480 ILE n 
1 2481 MET n 
1 2482 ALA n 
1 2483 MET n 
1 2484 THR n 
1 2485 MET n 
1 2486 PHE n 
1 2487 CYS n 
1 2488 LEU n 
1 2489 TYR n 
1 2490 LYS n 
1 2491 PHE n 
1 2492 ASP n 
1 2493 ILE n 
1 2494 GLU n 
1 2495 SER n 
1 2496 GLU n 
1 2497 GLN n 
1 2498 TYR n 
1 2499 LYS n 
1 2500 GLU n 
1 2501 ALA n 
1 2502 VAL n 
1 2503 LEU n 
1 2504 THR n 
1 2505 MET n 
1 2506 ILE n 
1 2507 GLY n 
1 2508 VAL n 
1 2509 LEU n 
1 2510 SER n 
1 2511 GLU n 
1 2512 SER n 
1 2513 SER n 
1 2514 ASP n 
1 2515 GLY n 
1 2516 VAL n 
1 2517 PRO n 
1 2518 LYS n 
1 2519 LEU n 
1 2520 THR n 
1 2521 VAL n 
1 2522 ASP n 
1 2523 THR n 
1 2524 ASN n 
1 2525 ASP n 
1 2526 ASP n 
1 2527 LEU n 
1 2528 ARG n 
1 2529 TYR n 
1 2530 LEU n 
1 2531 TRP n 
1 2532 ASP n 
1 2533 TYR n 
1 2534 VAL n 
1 2535 THR n 
1 2536 THR n 
1 2537 LYS n 
1 2538 SER n 
1 2539 TYR n 
1 2540 ILE n 
1 2541 SER n 
1 2542 ALA n 
1 2543 LEU n 
1 2544 ASN n 
1 2545 TRP n 
1 2546 PHE n 
1 2547 LYS n 
1 2548 ASN n 
1 2549 GLU n 
1 2550 PHE n 
1 2551 PHE n 
1 2552 VAL n 
1 2553 ASP n 
1 2554 GLU n 
1 2555 TRP n 
1 2556 ASN n 
1 2557 ILE n 
1 2558 ALA n 
1 2559 ASP n 
1 2560 VAL n 
1 2561 VAL n 
1 2562 ALA n 
1 2563 ASN n 
1 2564 SER n 
1 2565 GLU n 
1 2566 ASN n 
1 2567 ASN n 
1 2568 TYR n 
1 2569 PHE n 
1 2570 THR n 
1 2571 MET n 
1 2572 ALA n 
1 2573 SER n 
1 2574 GLU n 
1 2575 ARG n 
1 2576 ASP n 
1 2577 VAL n 
1 2578 ASP n 
1 2579 GLY n 
1 2580 THR n 
1 2581 PHE n 
1 2582 LYS n 
1 2583 LEU n 
1 2584 ILE n 
1 2585 GLU n 
1 2586 LEU n 
1 2587 ALA n 
1 2588 LYS n 
1 2589 ALA n 
1 2590 SER n 
1 2591 LYS n 
1 2592 GLU n 
1 2593 SER n 
1 2594 LEU n 
1 2595 LYS n 
1 2596 ILE n 
1 2597 ILE n 
1 2598 PRO n 
1 2599 LEU n 
1 2600 GLY n 
1 2601 SER n 
1 2602 ILE n 
1 2603 GLU n 
1 2604 ASN n 
1 2605 LEU n 
1 2606 ASN n 
1 2607 TYR n 
1 2608 ALA n 
1 2609 GLN n 
1 2610 GLU n 
1 2611 GLU n 
1 2612 ILE n 
1 2613 SER n 
1 2614 LYS n 
1 2615 SER n 
1 2616 LYS n 
1 2617 ILE n 
1 2618 GLU n 
1 2619 GLY n 
1 2620 GLY n 
1 2621 TRP n 
1 2622 ILE n 
1 2623 LEU n 
1 2624 LEU n 
1 2625 GLN n 
1 2626 ASN n 
1 2627 ILE n 
1 2628 GLN n 
1 2629 MET n 
1 2630 SER n 
1 2631 LEU n 
1 2632 SER n 
1 2633 TRP n 
1 2634 VAL n 
1 2635 LYS n 
1 2636 THR n 
1 2637 TYR n 
1 2638 LEU n 
1 2639 HIS n 
1 2640 LYS n 
1 2641 HIS n 
1 2642 VAL n 
1 2643 GLU n 
1 2644 GLU n 
1 2645 THR n 
1 2646 LYS n 
1 2647 ALA n 
1 2648 ALA n 
1 2649 GLU n 
1 2650 GLU n 
1 2651 HIS n 
1 2652 GLU n 
1 2653 LYS n 
1 2654 PHE n 
1 2655 LYS n 
1 2656 MET n 
1 2657 PHE n 
1 2658 MET n 
1 2659 THR n 
1 2660 CYS n 
1 2661 HIS n 
1 2662 LEU n 
1 2663 THR n 
1 2664 GLY n 
1 2665 ASP n 
1 2666 LYS n 
1 2667 LEU n 
1 2668 PRO n 
1 2669 ALA n 
1 2670 PRO n 
1 2671 LEU n 
1 2672 LEU n 
1 2673 GLN n 
1 2674 ARG n 
1 2675 THR n 
1 2676 ASP n 
1 2677 ARG n 
1 2678 VAL n 
1 2679 VAL n 
1 2680 TYR n 
1 2681 GLU n 
1 2682 ASP n 
1 2683 ILE n 
1 2684 PRO n 
1 2685 GLY n 
1 2686 ILE n 
1 2687 LEU n 
1 2688 ASP n 
1 2689 THR n 
1 2690 VAL n 
1 2691 LYS n 
1 2692 ASP n 
1 2693 LEU n 
1 2694 TRP n 
1 2695 GLY n 
1 2696 SER n 
1 2697 GLN n 
1 2698 PHE n 
1 2699 PHE n 
1 2700 THR n 
1 2701 GLY n 
1 2702 LYS n 
1 2703 ILE n 
1 2704 SER n 
1 2705 GLY n 
1 2706 VAL n 
1 2707 TRP n 
1 2708 SER n 
1 2709 VAL n 
1 2710 TYR n 
1 2711 CYS n 
1 2712 THR n 
1 2713 PHE n 
1 2714 LEU n 
1 2715 LEU n 
1 2716 SER n 
1 2717 TRP n 
1 2718 PHE n 
1 2719 HIS n 
1 2720 ALA n 
1 2721 LEU n 
1 2722 ILE n 
1 2723 THR n 
1 2724 ALA n 
1 2725 ARG n 
1 2726 THR n 
1 2727 ARG n 
1 2728 LEU n 
1 2729 VAL n 
1 2730 PRO n 
1 2731 HIS n 
1 2732 GLY n 
1 2733 PHE n 
1 2734 SER n 
1 2735 LYS n 
1 2736 LYS n 
1 2737 TYR n 
1 2738 TYR n 
1 2739 PHE n 
1 2740 ASN n 
1 2741 ASP n 
1 2742 CYS n 
1 2743 ASP n 
1 2744 PHE n 
1 2745 GLN n 
1 2746 PHE n 
1 2747 ALA n 
1 2748 SER n 
1 2749 VAL n 
1 2750 TYR n 
1 2751 LEU n 
1 2752 GLU n 
1 2753 ASN n 
1 2754 VAL n 
1 2755 LEU n 
1 2756 ALA n 
1 2757 THR n 
1 2758 ASN n 
1 2759 SER n 
1 2760 THR n 
1 2761 ASN n 
1 2762 ASN n 
1 2763 ILE n 
1 2764 PRO n 
1 2765 TRP n 
1 2766 ALA n 
1 2767 GLN n 
1 2768 VAL n 
1 2769 ARG n 
1 2770 ASP n 
1 2771 HIS n 
1 2772 ILE n 
1 2773 ALA n 
1 2774 THR n 
1 2775 ILE n 
1 2776 VAL n 
1 2777 TYR n 
1 2778 GLY n 
1 2779 GLY n 
1 2780 LYS n 
1 2781 ILE n 
1 2782 ASP n 
1 2783 GLU n 
1 2784 GLU n 
1 2785 LYS n 
1 2786 ASP n 
1 2787 LEU n 
1 2788 GLU n 
1 2789 VAL n 
1 2790 VAL n 
1 2791 ALA n 
1 2792 LYS n 
1 2793 LEU n 
1 2794 CYS n 
1 2795 ALA n 
1 2796 HIS n 
1 2797 VAL n 
1 2798 PHE n 
1 2799 CYS n 
1 2800 GLY n 
1 2801 SER n 
1 2802 ASP n 
1 2803 ASN n 
1 2804 LEU n 
1 2805 GLN n 
1 2806 ILE n 
1 2807 VAL n 
1 2808 PRO n 
1 2809 GLY n 
1 2810 VAL n 
1 2811 ARG n 
1 2812 ILE n 
1 2813 PRO n 
1 2814 GLN n 
1 2815 PRO n 
1 2816 LEU n 
1 2817 LEU n 
1 2818 GLN n 
1 2819 GLN n 
1 2820 SER n 
1 2821 GLU n 
1 2822 GLU n 
1 2823 GLU n 
1 2824 GLU n 
1 2825 ARG n 
1 2826 ALA n 
1 2827 ARG n 
1 2828 LEU n 
1 2829 THR n 
1 2830 ALA n 
1 2831 ILE n 
1 2832 LEU n 
1 2833 SER n 
1 2834 ASN n 
1 2835 THR n 
1 2836 ILE n 
1 2837 GLU n 
1 2838 PRO n 
1 2839 ALA n 
1 2840 ASP n 
1 2841 SER n 
1 2842 LEU n 
1 2843 SER n 
1 2844 SER n 
1 2845 TRP n 
1 2846 LEU n 
1 2847 GLN n 
1 2848 LEU n 
1 2849 PRO n 
1 2850 ARG n 
1 2851 GLU n 
1 2852 SER n 
1 2853 ILE n 
1 2854 LEU n 
1 2855 ASP n 
1 2856 TYR n 
1 2857 GLU n 
1 2858 ARG n 
1 2859 LEU n 
1 2860 GLN n 
1 2861 ALA n 
1 2862 LYS n 
1 2863 GLU n 
1 2864 VAL n 
1 2865 ALA n 
1 2866 SER n 
1 2867 SER n 
1 2868 THR n 
1 2869 GLU n 
1 2870 GLN n 
1 2871 LEU n 
1 2872 LEU n 
1 2873 GLN n 
1 2874 GLU n 
1 2875 MET n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   2875 
_entity_src_gen.gene_src_common_name               
;brewer's yeast
;
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYN1, DHC1, YKR054C' 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4932 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_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               '204508 / S288c' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
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 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    GLY 1    1218 ?    ?   ?   A . n 
A 1 2    ASP 2    1219 ?    ?   ?   A . n 
A 1 3    GLN 3    1220 ?    ?   ?   A . n 
A 1 4    LEU 4    1221 ?    ?   ?   A . n 
A 1 5    THR 5    1222 ?    ?   ?   A . n 
A 1 6    HIS 6    1223 ?    ?   ?   A . n 
A 1 7    VAL 7    1224 ?    ?   ?   A . n 
A 1 8    VAL 8    1225 ?    ?   ?   A . n 
A 1 9    GLU 9    1226 ?    ?   ?   A . n 
A 1 10   GLU 10   1227 ?    ?   ?   A . n 
A 1 11   VAL 11   1228 ?    ?   ?   A . n 
A 1 12   LYS 12   1229 ?    ?   ?   A . n 
A 1 13   THR 13   1230 ?    ?   ?   A . n 
A 1 14   TYR 14   1231 ?    ?   ?   A . n 
A 1 15   ASP 15   1232 ?    ?   ?   A . n 
A 1 16   LEU 16   1233 ?    ?   ?   A . n 
A 1 17   VAL 17   1234 ?    ?   ?   A . n 
A 1 18   TRP 18   1235 ?    ?   ?   A . n 
A 1 19   ARG 19   1236 ?    ?   ?   A . n 
A 1 20   SER 20   1237 ?    ?   ?   A . n 
A 1 21   ILE 21   1238 ?    ?   ?   A . n 
A 1 22   LYS 22   1239 ?    ?   ?   A . n 
A 1 23   ASN 23   1240 ?    ?   ?   A . n 
A 1 24   LEU 24   1241 ?    ?   ?   A . n 
A 1 25   TRP 25   1242 ?    ?   ?   A . n 
A 1 26   GLU 26   1243 ?    ?   ?   A . n 
A 1 27   ASP 27   1244 ?    ?   ?   A . n 
A 1 28   VAL 28   1245 ?    ?   ?   A . n 
A 1 29   GLN 29   1246 ?    ?   ?   A . n 
A 1 30   ARG 30   1247 ?    ?   ?   A . n 
A 1 31   THR 31   1248 ?    ?   ?   A . n 
A 1 32   PHE 32   1249 ?    ?   ?   A . n 
A 1 33   GLU 33   1250 ?    ?   ?   A . n 
A 1 34   THR 34   1251 ?    ?   ?   A . n 
A 1 35   PRO 35   1252 ?    ?   ?   A . n 
A 1 36   TRP 36   1253 ?    ?   ?   A . n 
A 1 37   CYS 37   1254 ?    ?   ?   A . n 
A 1 38   ARG 38   1255 ?    ?   ?   A . n 
A 1 39   VAL 39   1256 ?    ?   ?   A . n 
A 1 40   ASP 40   1257 ?    ?   ?   A . n 
A 1 41   VAL 41   1258 ?    ?   ?   A . n 
A 1 42   LEU 42   1259 ?    ?   ?   A . n 
A 1 43   LEU 43   1260 ?    ?   ?   A . n 
A 1 44   LEU 44   1261 ?    ?   ?   A . n 
A 1 45   GLN 45   1262 ?    ?   ?   A . n 
A 1 46   SER 46   1263 ?    ?   ?   A . n 
A 1 47   ASP 47   1264 ?    ?   ?   A . n 
A 1 48   LEU 48   1265 ?    ?   ?   A . n 
A 1 49   ALA 49   1266 ?    ?   ?   A . n 
A 1 50   ASN 50   1267 ?    ?   ?   A . n 
A 1 51   PHE 51   1268 ?    ?   ?   A . n 
A 1 52   LEU 52   1269 ?    ?   ?   A . n 
A 1 53   ARG 53   1270 ?    ?   ?   A . n 
A 1 54   ARG 54   1271 ?    ?   ?   A . n 
A 1 55   ALA 55   1272 ?    ?   ?   A . n 
A 1 56   ASP 56   1273 ?    ?   ?   A . n 
A 1 57   GLU 57   1274 ?    ?   ?   A . n 
A 1 58   LEU 58   1275 ?    ?   ?   A . n 
A 1 59   PRO 59   1276 ?    ?   ?   A . n 
A 1 60   ARG 60   1277 ?    ?   ?   A . n 
A 1 61   ALA 61   1278 ?    ?   ?   A . n 
A 1 62   VAL 62   1279 ?    ?   ?   A . n 
A 1 63   LYS 63   1280 ?    ?   ?   A . n 
A 1 64   GLN 64   1281 ?    ?   ?   A . n 
A 1 65   PHE 65   1282 ?    ?   ?   A . n 
A 1 66   GLU 66   1283 ?    ?   ?   A . n 
A 1 67   MET 67   1284 ?    ?   ?   A . n 
A 1 68   TYR 68   1285 ?    ?   ?   A . n 
A 1 69   LYS 69   1286 ?    ?   ?   A . n 
A 1 70   SER 70   1287 ?    ?   ?   A . n 
A 1 71   LEU 71   1288 ?    ?   ?   A . n 
A 1 72   PHE 72   1289 ?    ?   ?   A . n 
A 1 73   SER 73   1290 ?    ?   ?   A . n 
A 1 74   GLN 74   1291 ?    ?   ?   A . n 
A 1 75   VAL 75   1292 ?    ?   ?   A . n 
A 1 76   ASN 76   1293 ?    ?   ?   A . n 
A 1 77   MET 77   1294 ?    ?   ?   A . n 
A 1 78   LEU 78   1295 ?    ?   ?   A . n 
A 1 79   THR 79   1296 ?    ?   ?   A . n 
A 1 80   SER 80   1297 ?    ?   ?   A . n 
A 1 81   VAL 81   1298 ?    ?   ?   A . n 
A 1 82   ASN 82   1299 ?    ?   ?   A . n 
A 1 83   LYS 83   1300 ?    ?   ?   A . n 
A 1 84   ILE 84   1301 ?    ?   ?   A . n 
A 1 85   LEU 85   1302 ?    ?   ?   A . n 
A 1 86   VAL 86   1303 ?    ?   ?   A . n 
A 1 87   GLU 87   1304 ?    ?   ?   A . n 
A 1 88   LEU 88   1305 ?    ?   ?   A . n 
A 1 89   LYS 89   1306 ?    ?   ?   A . n 
A 1 90   ASP 90   1307 ?    ?   ?   A . n 
A 1 91   GLY 91   1308 ?    ?   ?   A . n 
A 1 92   ALA 92   1309 ?    ?   ?   A . n 
A 1 93   LEU 93   1310 ?    ?   ?   A . n 
A 1 94   LYS 94   1311 ?    ?   ?   A . n 
A 1 95   PRO 95   1312 ?    ?   ?   A . n 
A 1 96   ARG 96   1313 ?    ?   ?   A . n 
A 1 97   HIS 97   1314 ?    ?   ?   A . n 
A 1 98   TRP 98   1315 ?    ?   ?   A . n 
A 1 99   ASN 99   1316 ?    ?   ?   A . n 
A 1 100  MET 100  1317 ?    ?   ?   A . n 
A 1 101  ILE 101  1318 ?    ?   ?   A . n 
A 1 102  PHE 102  1319 ?    ?   ?   A . n 
A 1 103  ARG 103  1320 ?    ?   ?   A . n 
A 1 104  ASP 104  1321 ?    ?   ?   A . n 
A 1 105  ILE 105  1322 ?    ?   ?   A . n 
A 1 106  GLY 106  1323 ?    ?   ?   A . n 
A 1 107  LYS 107  1324 ?    ?   ?   A . n 
A 1 108  ARG 108  1325 ?    ?   ?   A . n 
A 1 109  GLN 109  1326 ?    ?   ?   A . n 
A 1 110  ILE 110  1327 ?    ?   ?   A . n 
A 1 111  GLN 111  1328 ?    ?   ?   A . n 
A 1 112  LYS 112  1329 ?    ?   ?   A . n 
A 1 113  ASN 113  1330 ?    ?   ?   A . n 
A 1 114  LEU 114  1331 ?    ?   ?   A . n 
A 1 115  LEU 115  1332 ?    ?   ?   A . n 
A 1 116  ASP 116  1333 ?    ?   ?   A . n 
A 1 117  LYS 117  1334 ?    ?   ?   A . n 
A 1 118  LEU 118  1335 ?    ?   ?   A . n 
A 1 119  GLU 119  1336 ?    ?   ?   A . n 
A 1 120  PHE 120  1337 ?    ?   ?   A . n 
A 1 121  SER 121  1338 ?    ?   ?   A . n 
A 1 122  LEU 122  1339 ?    ?   ?   A . n 
A 1 123  LYS 123  1340 ?    ?   ?   A . n 
A 1 124  ASP 124  1341 ?    ?   ?   A . n 
A 1 125  VAL 125  1342 ?    ?   ?   A . n 
A 1 126  MET 126  1343 ?    ?   ?   A . n 
A 1 127  VAL 127  1344 ?    ?   ?   A . n 
A 1 128  LEU 128  1345 ?    ?   ?   A . n 
A 1 129  ASN 129  1346 ?    ?   ?   A . n 
A 1 130  LEU 130  1347 ?    ?   ?   A . n 
A 1 131  THR 131  1348 ?    ?   ?   A . n 
A 1 132  LEU 132  1349 ?    ?   ?   A . n 
A 1 133  ASN 133  1350 ?    ?   ?   A . n 
A 1 134  GLU 134  1351 ?    ?   ?   A . n 
A 1 135  ILE 135  1352 ?    ?   ?   A . n 
A 1 136  LEU 136  1353 ?    ?   ?   A . n 
A 1 137  LEU 137  1354 ?    ?   ?   A . n 
A 1 138  THR 138  1355 ?    ?   ?   A . n 
A 1 139  LYS 139  1356 ?    ?   ?   A . n 
A 1 140  ILE 140  1357 ?    ?   ?   A . n 
A 1 141  ILE 141  1358 ?    ?   ?   A . n 
A 1 142  GLU 142  1359 ?    ?   ?   A . n 
A 1 143  ARG 143  1360 ?    ?   ?   A . n 
A 1 144  ALA 144  1361 ?    ?   ?   A . n 
A 1 145  GLN 145  1362 ?    ?   ?   A . n 
A 1 146  LYS 146  1363 ?    ?   ?   A . n 
A 1 147  GLU 147  1364 ?    ?   ?   A . n 
A 1 148  PHE 148  1365 ?    ?   ?   A . n 
A 1 149  VAL 149  1366 ?    ?   ?   A . n 
A 1 150  ILE 150  1367 ?    ?   ?   A . n 
A 1 151  GLU 151  1368 ?    ?   ?   A . n 
A 1 152  LYS 152  1369 ?    ?   ?   A . n 
A 1 153  SER 153  1370 1370 SER SER A . n 
A 1 154  LEU 154  1371 1371 LEU LEU A . n 
A 1 155  ASN 155  1372 1372 ASN ASN A . n 
A 1 156  ARG 156  1373 1373 ARG ARG A . n 
A 1 157  ILE 157  1374 1374 ILE ILE A . n 
A 1 158  LYS 158  1375 1375 LYS LYS A . n 
A 1 159  LYS 159  1376 1376 LYS LYS A . n 
A 1 160  PHE 160  1377 1377 PHE PHE A . n 
A 1 161  TRP 161  1378 1378 TRP TRP A . n 
A 1 162  LYS 162  1379 1379 LYS LYS A . n 
A 1 163  GLU 163  1380 1380 GLU GLU A . n 
A 1 164  ALA 164  1381 1381 ALA ALA A . n 
A 1 165  GLN 165  1382 1382 GLN GLN A . n 
A 1 166  TYR 166  1383 1383 TYR TYR A . n 
A 1 167  GLU 167  1384 1384 GLU GLU A . n 
A 1 168  VAL 168  1385 1385 VAL VAL A . n 
A 1 169  ILE 169  1386 1386 ILE ILE A . n 
A 1 170  GLU 170  1387 1387 GLU GLU A . n 
A 1 171  HIS 171  1388 1388 HIS HIS A . n 
A 1 172  SER 172  1389 1389 SER SER A . n 
A 1 173  SER 173  1390 1390 SER SER A . n 
A 1 174  GLY 174  1391 1391 GLY GLY A . n 
A 1 175  LEU 175  1392 1392 LEU LEU A . n 
A 1 176  LYS 176  1393 1393 LYS LYS A . n 
A 1 177  LEU 177  1394 1394 LEU LEU A . n 
A 1 178  VAL 178  1395 1395 VAL VAL A . n 
A 1 179  ARG 179  1396 1396 ARG ARG A . n 
A 1 180  GLU 180  1397 1397 GLU GLU A . n 
A 1 181  TRP 181  1398 1398 TRP TRP A . n 
A 1 182  ASP 182  1399 1399 ASP ASP A . n 
A 1 183  VAL 183  1400 1400 VAL VAL A . n 
A 1 184  LEU 184  1401 1401 LEU LEU A . n 
A 1 185  GLU 185  1402 1402 GLU GLU A . n 
A 1 186  GLN 186  1403 1403 GLN GLN A . n 
A 1 187  ALA 187  1404 1404 ALA ALA A . n 
A 1 188  CYS 188  1405 1405 CYS CYS A . n 
A 1 189  LYS 189  1406 1406 LYS LYS A . n 
A 1 190  GLU 190  1407 ?    ?   ?   A . n 
A 1 191  ASP 191  1408 ?    ?   ?   A . n 
A 1 192  LEU 192  1409 ?    ?   ?   A . n 
A 1 193  GLU 193  1410 ?    ?   ?   A . n 
A 1 194  GLU 194  1411 ?    ?   ?   A . n 
A 1 195  LEU 195  1412 ?    ?   ?   A . n 
A 1 196  VAL 196  1413 ?    ?   ?   A . n 
A 1 197  SER 197  1414 ?    ?   ?   A . n 
A 1 198  MET 198  1415 ?    ?   ?   A . n 
A 1 199  LYS 199  1416 ?    ?   ?   A . n 
A 1 200  ALA 200  1417 ?    ?   ?   A . n 
A 1 201  SER 201  1418 ?    ?   ?   A . n 
A 1 202  ASN 202  1419 ?    ?   ?   A . n 
A 1 203  TYR 203  1420 ?    ?   ?   A . n 
A 1 204  TYR 204  1421 ?    ?   ?   A . n 
A 1 205  LYS 205  1422 ?    ?   ?   A . n 
A 1 206  ILE 206  1423 ?    ?   ?   A . n 
A 1 207  PHE 207  1424 ?    ?   ?   A . n 
A 1 208  GLU 208  1425 1425 GLU GLU A . n 
A 1 209  GLN 209  1426 1426 GLN GLN A . n 
A 1 210  ASP 210  1427 1427 ASP ASP A . n 
A 1 211  CYS 211  1428 1428 CYS CYS A . n 
A 1 212  LEU 212  1429 1429 LEU LEU A . n 
A 1 213  ASP 213  1430 1430 ASP ASP A . n 
A 1 214  LEU 214  1431 1431 LEU LEU A . n 
A 1 215  GLU 215  1432 1432 GLU GLU A . n 
A 1 216  SER 216  1433 1433 SER SER A . n 
A 1 217  LYS 217  1434 1434 LYS LYS A . n 
A 1 218  LEU 218  1435 1435 LEU LEU A . n 
A 1 219  THR 219  1436 1436 THR THR A . n 
A 1 220  LYS 220  1437 1437 LYS LYS A . n 
A 1 221  LEU 221  1438 1438 LEU LEU A . n 
A 1 222  SER 222  1439 1439 SER SER A . n 
A 1 223  GLU 223  1440 1440 GLU GLU A . n 
A 1 224  ILE 224  1441 1441 ILE ILE A . n 
A 1 225  GLN 225  1442 1442 GLN GLN A . n 
A 1 226  VAL 226  1443 1443 VAL VAL A . n 
A 1 227  ASN 227  1444 1444 ASN ASN A . n 
A 1 228  TRP 228  1445 1445 TRP TRP A . n 
A 1 229  VAL 229  1446 1446 VAL VAL A . n 
A 1 230  GLU 230  1447 1447 GLU GLU A . n 
A 1 231  VAL 231  1448 1448 VAL VAL A . n 
A 1 232  GLN 232  1449 1449 GLN GLN A . n 
A 1 233  PHE 233  1450 1450 PHE PHE A . n 
A 1 234  TYR 234  1451 1451 TYR TYR A . n 
A 1 235  TRP 235  1452 1452 TRP TRP A . n 
A 1 236  LEU 236  1453 1453 LEU LEU A . n 
A 1 237  ASP 237  1454 1454 ASP ASP A . n 
A 1 238  LEU 238  1455 1455 LEU LEU A . n 
A 1 239  TYR 239  1456 1456 TYR TYR A . n 
A 1 240  GLY 240  1457 1457 GLY GLY A . n 
A 1 241  ILE 241  1458 1458 ILE ILE A . n 
A 1 242  LEU 242  1459 1459 LEU LEU A . n 
A 1 243  GLY 243  1460 1460 GLY GLY A . n 
A 1 244  GLU 244  1461 1461 GLU GLU A . n 
A 1 245  ASN 245  1462 1462 ASN ASN A . n 
A 1 246  LEU 246  1463 1463 LEU LEU A . n 
A 1 247  ASP 247  1464 1464 ASP ASP A . n 
A 1 248  ILE 248  1465 1465 ILE ILE A . n 
A 1 249  GLN 249  1466 1466 GLN GLN A . n 
A 1 250  ASN 250  1467 1467 ASN ASN A . n 
A 1 251  PHE 251  1468 1468 PHE PHE A . n 
A 1 252  LEU 252  1469 1469 LEU LEU A . n 
A 1 253  PRO 253  1470 1470 PRO PRO A . n 
A 1 254  LEU 254  1471 1471 LEU LEU A . n 
A 1 255  GLU 255  1472 1472 GLU GLU A . n 
A 1 256  THR 256  1473 1473 THR THR A . n 
A 1 257  SER 257  1474 1474 SER SER A . n 
A 1 258  LYS 258  1475 1475 LYS LYS A . n 
A 1 259  PHE 259  1476 1476 PHE PHE A . n 
A 1 260  LYS 260  1477 1477 LYS LYS A . n 
A 1 261  SER 261  1478 1478 SER SER A . n 
A 1 262  LEU 262  1479 1479 LEU LEU A . n 
A 1 263  THR 263  1480 1480 THR THR A . n 
A 1 264  SER 264  1481 1481 SER SER A . n 
A 1 265  GLU 265  1482 1482 GLU GLU A . n 
A 1 266  TYR 266  1483 1483 TYR TYR A . n 
A 1 267  LYS 267  1484 1484 LYS LYS A . n 
A 1 268  MET 268  1485 1485 MET MET A . n 
A 1 269  ILE 269  1486 1486 ILE ILE A . n 
A 1 270  THR 270  1487 1487 THR THR A . n 
A 1 271  THR 271  1488 1488 THR THR A . n 
A 1 272  ARG 272  1489 1489 ARG ARG A . n 
A 1 273  ALA 273  1490 1490 ALA ALA A . n 
A 1 274  PHE 274  1491 1491 PHE PHE A . n 
A 1 275  GLN 275  1492 1492 GLN GLN A . n 
A 1 276  LEU 276  1493 ?    ?   ?   A . n 
A 1 277  ASP 277  1494 ?    ?   ?   A . n 
A 1 278  THR 278  1495 ?    ?   ?   A . n 
A 1 279  THR 279  1496 ?    ?   ?   A . n 
A 1 280  ILE 280  1497 ?    ?   ?   A . n 
A 1 281  GLU 281  1498 ?    ?   ?   A . n 
A 1 282  VAL 282  1499 ?    ?   ?   A . n 
A 1 283  ILE 283  1500 ?    ?   ?   A . n 
A 1 284  HIS 284  1501 ?    ?   ?   A . n 
A 1 285  ILE 285  1502 ?    ?   ?   A . n 
A 1 286  PRO 286  1503 ?    ?   ?   A . n 
A 1 287  ASN 287  1504 ?    ?   ?   A . n 
A 1 288  PHE 288  1505 1505 PHE PHE A . n 
A 1 289  ASP 289  1506 1506 ASP ASP A . n 
A 1 290  THR 290  1507 1507 THR THR A . n 
A 1 291  THR 291  1508 1508 THR THR A . n 
A 1 292  LEU 292  1509 1509 LEU LEU A . n 
A 1 293  LYS 293  1510 1510 LYS LYS A . n 
A 1 294  LEU 294  1511 1511 LEU LEU A . n 
A 1 295  THR 295  1512 1512 THR THR A . n 
A 1 296  ILE 296  1513 1513 ILE ILE A . n 
A 1 297  ASP 297  1514 1514 ASP ASP A . n 
A 1 298  SER 298  1515 1515 SER SER A . n 
A 1 299  LEU 299  1516 1516 LEU LEU A . n 
A 1 300  LYS 300  1517 1517 LYS LYS A . n 
A 1 301  MET 301  1518 1518 MET MET A . n 
A 1 302  ILE 302  1519 1519 ILE ILE A . n 
A 1 303  LYS 303  1520 1520 LYS LYS A . n 
A 1 304  SER 304  1521 1521 SER SER A . n 
A 1 305  SER 305  1522 1522 SER SER A . n 
A 1 306  LEU 306  1523 1523 LEU LEU A . n 
A 1 307  SER 307  1524 1524 SER SER A . n 
A 1 308  THR 308  1525 1525 THR THR A . n 
A 1 309  PHE 309  1526 1526 PHE PHE A . n 
A 1 310  LEU 310  1527 1527 LEU LEU A . n 
A 1 311  GLU 311  1528 1528 GLU GLU A . n 
A 1 312  ARG 312  1529 1529 ARG ARG A . n 
A 1 313  GLN 313  1530 1530 GLN GLN A . n 
A 1 314  ARG 314  1531 1531 ARG ARG A . n 
A 1 315  ARG 315  1532 1532 ARG ARG A . n 
A 1 316  GLN 316  1533 1533 GLN GLN A . n 
A 1 317  PHE 317  1534 1534 PHE PHE A . n 
A 1 318  PRO 318  1535 1535 PRO PRO A . n 
A 1 319  ARG 319  1536 1536 ARG ARG A . n 
A 1 320  PHE 320  1537 1537 PHE PHE A . n 
A 1 321  TYR 321  1538 1538 TYR TYR A . n 
A 1 322  PHE 322  1539 1539 PHE PHE A . n 
A 1 323  LEU 323  1540 1540 LEU LEU A . n 
A 1 324  GLY 324  1541 1541 GLY GLY A . n 
A 1 325  ASN 325  1542 1542 ASN ASN A . n 
A 1 326  ASP 326  1543 1543 ASP ASP A . n 
A 1 327  ASP 327  1544 1544 ASP ASP A . n 
A 1 328  LEU 328  1545 1545 LEU LEU A . n 
A 1 329  LEU 329  1546 1546 LEU LEU A . n 
A 1 330  LYS 330  1547 1547 LYS LYS A . n 
A 1 331  ILE 331  1548 1548 ILE ILE A . n 
A 1 332  ILE 332  1549 1549 ILE ILE A . n 
A 1 333  GLY 333  1550 1550 GLY GLY A . n 
A 1 334  SER 334  1551 1551 SER SER A . n 
A 1 335  GLY 335  1552 1552 GLY GLY A . n 
A 1 336  LYS 336  1553 1553 LYS LYS A . n 
A 1 337  HIS 337  1554 1554 HIS HIS A . n 
A 1 338  HIS 338  1555 1555 HIS HIS A . n 
A 1 339  ASP 339  1556 1556 ASP ASP A . n 
A 1 340  GLN 340  1557 1557 GLN GLN A . n 
A 1 341  VAL 341  1558 1558 VAL VAL A . n 
A 1 342  SER 342  1559 1559 SER SER A . n 
A 1 343  LYS 343  1560 1560 LYS LYS A . n 
A 1 344  PHE 344  1561 1561 PHE PHE A . n 
A 1 345  MET 345  1562 1562 MET MET A . n 
A 1 346  LYS 346  1563 1563 LYS LYS A . n 
A 1 347  LYS 347  1564 1564 LYS LYS A . n 
A 1 348  MET 348  1565 1565 MET MET A . n 
A 1 349  PHE 349  1566 1566 PHE PHE A . n 
A 1 350  GLY 350  1567 1567 GLY GLY A . n 
A 1 351  SER 351  1568 1568 SER SER A . n 
A 1 352  ILE 352  1569 1569 ILE ILE A . n 
A 1 353  GLU 353  1570 1570 GLU GLU A . n 
A 1 354  SER 354  1571 1571 SER SER A . n 
A 1 355  ILE 355  1572 1572 ILE ILE A . n 
A 1 356  ILE 356  1573 1573 ILE ILE A . n 
A 1 357  PHE 357  1574 1574 PHE PHE A . n 
A 1 358  PHE 358  1575 1575 PHE PHE A . n 
A 1 359  GLU 359  1576 1576 GLU GLU A . n 
A 1 360  ASP 360  1577 1577 ASP ASP A . n 
A 1 361  SER 361  1578 1578 SER SER A . n 
A 1 362  ILE 362  1579 1579 ILE ILE A . n 
A 1 363  THR 363  1580 1580 THR THR A . n 
A 1 364  GLY 364  1581 1581 GLY GLY A . n 
A 1 365  VAL 365  1582 1582 VAL VAL A . n 
A 1 366  ARG 366  1583 1583 ARG ARG A . n 
A 1 367  SER 367  1584 1584 SER SER A . n 
A 1 368  VAL 368  1585 1585 VAL VAL A . n 
A 1 369  GLU 369  1586 1586 GLU GLU A . n 
A 1 370  GLY 370  1587 1587 GLY GLY A . n 
A 1 371  GLU 371  1588 1588 GLU GLU A . n 
A 1 372  VAL 372  1589 1589 VAL VAL A . n 
A 1 373  LEU 373  1590 1590 LEU LEU A . n 
A 1 374  ASN 374  1591 1591 ASN ASN A . n 
A 1 375  LEU 375  1592 1592 LEU LEU A . n 
A 1 376  ASN 376  1593 1593 ASN ASN A . n 
A 1 377  GLU 377  1594 1594 GLU GLU A . n 
A 1 378  LYS 378  1595 1595 LYS LYS A . n 
A 1 379  ILE 379  1596 1596 ILE ILE A . n 
A 1 380  GLU 380  1597 1597 GLU GLU A . n 
A 1 381  LEU 381  1598 1598 LEU LEU A . n 
A 1 382  LYS 382  1599 1599 LYS LYS A . n 
A 1 383  ASP 383  1600 1600 ASP ASP A . n 
A 1 384  SER 384  1601 1601 SER SER A . n 
A 1 385  ILE 385  1602 1602 ILE ILE A . n 
A 1 386  GLN 386  1603 1603 GLN GLN A . n 
A 1 387  ALA 387  1604 1604 ALA ALA A . n 
A 1 388  GLN 388  1605 1605 GLN GLN A . n 
A 1 389  GLU 389  1606 1606 GLU GLU A . n 
A 1 390  TRP 390  1607 1607 TRP TRP A . n 
A 1 391  LEU 391  1608 1608 LEU LEU A . n 
A 1 392  ASN 392  1609 1609 ASN ASN A . n 
A 1 393  ILE 393  1610 1610 ILE ILE A . n 
A 1 394  LEU 394  1611 1611 LEU LEU A . n 
A 1 395  ASP 395  1612 1612 ASP ASP A . n 
A 1 396  THR 396  1613 1613 THR THR A . n 
A 1 397  GLU 397  1614 1614 GLU GLU A . n 
A 1 398  ILE 398  1615 1615 ILE ILE A . n 
A 1 399  LYS 399  1616 1616 LYS LYS A . n 
A 1 400  LEU 400  1617 1617 LEU LEU A . n 
A 1 401  SER 401  1618 1618 SER SER A . n 
A 1 402  VAL 402  1619 1619 VAL VAL A . n 
A 1 403  PHE 403  1620 1620 PHE PHE A . n 
A 1 404  THR 404  1621 1621 THR THR A . n 
A 1 405  GLN 405  1622 1622 GLN GLN A . n 
A 1 406  PHE 406  1623 1623 PHE PHE A . n 
A 1 407  ARG 407  1624 1624 ARG ARG A . n 
A 1 408  ASP 408  1625 1625 ASP ASP A . n 
A 1 409  CYS 409  1626 1626 CYS CYS A . n 
A 1 410  LEU 410  1627 1627 LEU LEU A . n 
A 1 411  GLY 411  1628 1628 GLY GLY A . n 
A 1 412  GLN 412  1629 1629 GLN GLN A . n 
A 1 413  LEU 413  1630 1630 LEU LEU A . n 
A 1 414  LYS 414  1631 1631 LYS LYS A . n 
A 1 415  ASP 415  1632 1632 ASP ASP A . n 
A 1 416  GLY 416  1633 1633 GLY GLY A . n 
A 1 417  THR 417  1634 1634 THR THR A . n 
A 1 418  ASP 418  1635 1635 ASP ASP A . n 
A 1 419  ILE 419  1636 1636 ILE ILE A . n 
A 1 420  GLU 420  1637 1637 GLU GLU A . n 
A 1 421  VAL 421  1638 1638 VAL VAL A . n 
A 1 422  VAL 422  1639 1639 VAL VAL A . n 
A 1 423  VAL 423  1640 1640 VAL VAL A . n 
A 1 424  SER 424  1641 1641 SER SER A . n 
A 1 425  LYS 425  1642 1642 LYS LYS A . n 
A 1 426  TYR 426  1643 1643 TYR TYR A . n 
A 1 427  ILE 427  1644 1644 ILE ILE A . n 
A 1 428  PHE 428  1645 1645 PHE PHE A . n 
A 1 429  GLN 429  1646 1646 GLN GLN A . n 
A 1 430  ALA 430  1647 1647 ALA ALA A . n 
A 1 431  ILE 431  1648 1648 ILE ILE A . n 
A 1 432  LEU 432  1649 1649 LEU LEU A . n 
A 1 433  LEU 433  1650 1650 LEU LEU A . n 
A 1 434  SER 434  1651 1651 SER SER A . n 
A 1 435  ALA 435  1652 1652 ALA ALA A . n 
A 1 436  GLN 436  1653 1653 GLN GLN A . n 
A 1 437  VAL 437  1654 1654 VAL VAL A . n 
A 1 438  MET 438  1655 1655 MET MET A . n 
A 1 439  TRP 439  1656 1656 TRP TRP A . n 
A 1 440  THR 440  1657 1657 THR THR A . n 
A 1 441  GLU 441  1658 1658 GLU GLU A . n 
A 1 442  LEU 442  1659 1659 LEU LEU A . n 
A 1 443  VAL 443  1660 1660 VAL VAL A . n 
A 1 444  GLU 444  1661 1661 GLU GLU A . n 
A 1 445  LYS 445  1662 1662 LYS LYS A . n 
A 1 446  CYS 446  1663 1663 CYS CYS A . n 
A 1 447  LEU 447  1664 1664 LEU LEU A . n 
A 1 448  GLN 448  1665 1665 GLN GLN A . n 
A 1 449  THR 449  1666 1666 THR THR A . n 
A 1 450  ASN 450  1667 1667 ASN ASN A . n 
A 1 451  GLU 451  1668 1668 GLU GLU A . n 
A 1 452  PHE 452  1669 1669 PHE PHE A . n 
A 1 453  SER 453  1670 1670 SER SER A . n 
A 1 454  LYS 454  1671 1671 LYS LYS A . n 
A 1 455  TYR 455  1672 1672 TYR TYR A . n 
A 1 456  TRP 456  1673 1673 TRP TRP A . n 
A 1 457  LYS 457  1674 1674 LYS LYS A . n 
A 1 458  GLU 458  1675 1675 GLU GLU A . n 
A 1 459  VAL 459  1676 1676 VAL VAL A . n 
A 1 460  ASP 460  1677 1677 ASP ASP A . n 
A 1 461  MET 461  1678 1678 MET MET A . n 
A 1 462  LYS 462  1679 1679 LYS LYS A . n 
A 1 463  ILE 463  1680 1680 ILE ILE A . n 
A 1 464  LYS 464  1681 1681 LYS LYS A . n 
A 1 465  GLY 465  1682 1682 GLY GLY A . n 
A 1 466  LEU 466  1683 1683 LEU LEU A . n 
A 1 467  LEU 467  1684 1684 LEU LEU A . n 
A 1 468  ASP 468  1685 1685 ASP ASP A . n 
A 1 469  LYS 469  1686 1686 LYS LYS A . n 
A 1 470  LEU 470  1687 1687 LEU LEU A . n 
A 1 471  ASN 471  1688 1688 ASN ASN A . n 
A 1 472  LYS 472  1689 1689 LYS LYS A . n 
A 1 473  SER 473  1690 1690 SER SER A . n 
A 1 474  SER 474  1691 1691 SER SER A . n 
A 1 475  ASP 475  1692 1692 ASP ASP A . n 
A 1 476  ASN 476  1693 1693 ASN ASN A . n 
A 1 477  VAL 477  1694 1694 VAL VAL A . n 
A 1 478  LYS 478  1695 1695 LYS LYS A . n 
A 1 479  LYS 479  1696 1696 LYS LYS A . n 
A 1 480  LYS 480  1697 1697 LYS LYS A . n 
A 1 481  ILE 481  1698 1698 ILE ILE A . n 
A 1 482  GLU 482  1699 1699 GLU GLU A . n 
A 1 483  ALA 483  1700 1700 ALA ALA A . n 
A 1 484  LEU 484  1701 1701 LEU LEU A . n 
A 1 485  LEU 485  1702 1702 LEU LEU A . n 
A 1 486  VAL 486  1703 1703 VAL VAL A . n 
A 1 487  GLU 487  1704 1704 GLU GLU A . n 
A 1 488  TYR 488  1705 1705 TYR TYR A . n 
A 1 489  LEU 489  1706 1706 LEU LEU A . n 
A 1 490  HIS 490  1707 1707 HIS HIS A . n 
A 1 491  PHE 491  1708 1708 PHE PHE A . n 
A 1 492  ASN 492  1709 1709 ASN ASN A . n 
A 1 493  ASN 493  1710 1710 ASN ASN A . n 
A 1 494  VAL 494  1711 1711 VAL VAL A . n 
A 1 495  ILE 495  1712 1712 ILE ILE A . n 
A 1 496  GLY 496  1713 1713 GLY GLY A . n 
A 1 497  GLN 497  1714 1714 GLN GLN A . n 
A 1 498  LEU 498  1715 1715 LEU LEU A . n 
A 1 499  LYS 499  1716 1716 LYS LYS A . n 
A 1 500  ASN 500  1717 1717 ASN ASN A . n 
A 1 501  CYS 501  1718 1718 CYS CYS A . n 
A 1 502  SER 502  1719 1719 SER SER A . n 
A 1 503  THR 503  1720 1720 THR THR A . n 
A 1 504  LYS 504  1721 1721 LYS LYS A . n 
A 1 505  GLU 505  1722 1722 GLU GLU A . n 
A 1 506  GLU 506  1723 1723 GLU GLU A . n 
A 1 507  ALA 507  1724 1724 ALA ALA A . n 
A 1 508  ARG 508  1725 1725 ARG ARG A . n 
A 1 509  LEU 509  1726 1726 LEU LEU A . n 
A 1 510  LEU 510  1727 1727 LEU LEU A . n 
A 1 511  TRP 511  1728 1728 TRP TRP A . n 
A 1 512  ALA 512  1729 1729 ALA ALA A . n 
A 1 513  LYS 513  1730 1730 LYS LYS A . n 
A 1 514  VAL 514  1731 1731 VAL VAL A . n 
A 1 515  GLN 515  1732 1732 GLN GLN A . n 
A 1 516  LYS 516  1733 1733 LYS LYS A . n 
A 1 517  PHE 517  1734 1734 PHE PHE A . n 
A 1 518  TYR 518  1735 1735 TYR TYR A . n 
A 1 519  GLN 519  1736 1736 GLN GLN A . n 
A 1 520  LYS 520  1737 1737 LYS LYS A . n 
A 1 521  ASN 521  1738 1738 ASN ASN A . n 
A 1 522  ASP 522  1739 1739 ASP ASP A . n 
A 1 523  THR 523  1740 1740 THR THR A . n 
A 1 524  LEU 524  1741 1741 LEU LEU A . n 
A 1 525  ASP 525  1742 1742 ASP ASP A . n 
A 1 526  ASP 526  1743 1743 ASP ASP A . n 
A 1 527  LEU 527  1744 1744 LEU LEU A . n 
A 1 528  ASN 528  1745 1745 ASN ASN A . n 
A 1 529  SER 529  1746 1746 SER SER A . n 
A 1 530  VAL 530  1747 1747 VAL VAL A . n 
A 1 531  PHE 531  1748 1748 PHE PHE A . n 
A 1 532  ILE 532  1749 1749 ILE ILE A . n 
A 1 533  SER 533  1750 1750 SER SER A . n 
A 1 534  GLN 534  1751 1751 GLN GLN A . n 
A 1 535  SER 535  1752 1752 SER SER A . n 
A 1 536  GLY 536  1753 1753 GLY GLY A . n 
A 1 537  TYR 537  1754 1754 TYR TYR A . n 
A 1 538  LEU 538  1755 1755 LEU LEU A . n 
A 1 539  LEU 539  1756 1756 LEU LEU A . n 
A 1 540  GLN 540  1757 1757 GLN GLN A . n 
A 1 541  TYR 541  1758 1758 TYR TYR A . n 
A 1 542  LYS 542  1759 1759 LYS LYS A . n 
A 1 543  PHE 543  1760 1760 PHE PHE A . n 
A 1 544  GLU 544  1761 1761 GLU GLU A . n 
A 1 545  TYR 545  1762 1762 TYR TYR A . n 
A 1 546  ILE 546  1763 1763 ILE ILE A . n 
A 1 547  GLY 547  1764 1764 GLY GLY A . n 
A 1 548  ILE 548  1765 1765 ILE ILE A . n 
A 1 549  PRO 549  1766 1766 PRO PRO A . n 
A 1 550  GLU 550  1767 1767 GLU GLU A . n 
A 1 551  ARG 551  1768 1768 ARG ARG A . n 
A 1 552  LEU 552  1769 1769 LEU LEU A . n 
A 1 553  ILE 553  1770 1770 ILE ILE A . n 
A 1 554  TYR 554  1771 1771 TYR TYR A . n 
A 1 555  THR 555  1772 1772 THR THR A . n 
A 1 556  PRO 556  1773 1773 PRO PRO A . n 
A 1 557  LEU 557  1774 1774 LEU LEU A . n 
A 1 558  LEU 558  1775 1775 LEU LEU A . n 
A 1 559  LEU 559  1776 1776 LEU LEU A . n 
A 1 560  VAL 560  1777 1777 VAL VAL A . n 
A 1 561  GLY 561  1778 1778 GLY GLY A . n 
A 1 562  PHE 562  1779 1779 PHE PHE A . n 
A 1 563  ALA 563  1780 1780 ALA ALA A . n 
A 1 564  THR 564  1781 1781 THR THR A . n 
A 1 565  LEU 565  1782 1782 LEU LEU A . n 
A 1 566  THR 566  1783 1783 THR THR A . n 
A 1 567  ASP 567  1784 1784 ASP ASP A . n 
A 1 568  SER 568  1785 1785 SER SER A . n 
A 1 569  LEU 569  1786 1786 LEU LEU A . n 
A 1 570  HIS 570  1787 1787 HIS HIS A . n 
A 1 571  GLN 571  1788 1788 GLN GLN A . n 
A 1 572  LYS 572  1789 1789 LYS LYS A . n 
A 1 573  TYR 573  1790 1790 TYR TYR A . n 
A 1 574  GLY 574  1791 1791 GLY GLY A . n 
A 1 575  GLY 575  1792 1792 GLY GLY A . n 
A 1 576  CYS 576  1793 1793 CYS CYS A . n 
A 1 577  PHE 577  1794 1794 PHE PHE A . n 
A 1 578  PHE 578  1795 1795 PHE PHE A . n 
A 1 579  GLY 579  1796 1796 GLY GLY A . n 
A 1 580  PRO 580  1797 1797 PRO PRO A . n 
A 1 581  ALA 581  1798 1798 ALA ALA A . n 
A 1 582  GLY 582  1799 1799 GLY GLY A . n 
A 1 583  THR 583  1800 1800 THR THR A . n 
A 1 584  GLY 584  1801 1801 GLY GLY A . n 
A 1 585  LYS 585  1802 1802 LYS LYS A . n 
A 1 586  THR 586  1803 1803 THR THR A . n 
A 1 587  GLU 587  1804 1804 GLU GLU A . n 
A 1 588  THR 588  1805 1805 THR THR A . n 
A 1 589  VAL 589  1806 1806 VAL VAL A . n 
A 1 590  LYS 590  1807 1807 LYS LYS A . n 
A 1 591  ALA 591  1808 1808 ALA ALA A . n 
A 1 592  PHE 592  1809 1809 PHE PHE A . n 
A 1 593  GLY 593  1810 1810 GLY GLY A . n 
A 1 594  GLN 594  1811 1811 GLN GLN A . n 
A 1 595  ASN 595  1812 1812 ASN ASN A . n 
A 1 596  LEU 596  1813 1813 LEU LEU A . n 
A 1 597  GLY 597  1814 1814 GLY GLY A . n 
A 1 598  ARG 598  1815 1815 ARG ARG A . n 
A 1 599  VAL 599  1816 1816 VAL VAL A . n 
A 1 600  VAL 600  1817 1817 VAL VAL A . n 
A 1 601  VAL 601  1818 1818 VAL VAL A . n 
A 1 602  VAL 602  1819 1819 VAL VAL A . n 
A 1 603  PHE 603  1820 1820 PHE PHE A . n 
A 1 604  ASN 604  1821 1821 ASN ASN A . n 
A 1 605  CYS 605  1822 1822 CYS CYS A . n 
A 1 606  ASP 606  1823 1823 ASP ASP A . n 
A 1 607  ASP 607  1824 1824 ASP ASP A . n 
A 1 608  SER 608  1825 1825 SER SER A . n 
A 1 609  PHE 609  1826 1826 PHE PHE A . n 
A 1 610  ASP 610  1827 1827 ASP ASP A . n 
A 1 611  TYR 611  1828 1828 TYR TYR A . n 
A 1 612  GLN 612  1829 1829 GLN GLN A . n 
A 1 613  VAL 613  1830 1830 VAL VAL A . n 
A 1 614  LEU 614  1831 1831 LEU LEU A . n 
A 1 615  SER 615  1832 1832 SER SER A . n 
A 1 616  ARG 616  1833 1833 ARG ARG A . n 
A 1 617  LEU 617  1834 1834 LEU LEU A . n 
A 1 618  LEU 618  1835 1835 LEU LEU A . n 
A 1 619  VAL 619  1836 1836 VAL VAL A . n 
A 1 620  GLY 620  1837 1837 GLY GLY A . n 
A 1 621  ILE 621  1838 1838 ILE ILE A . n 
A 1 622  THR 622  1839 1839 THR THR A . n 
A 1 623  GLN 623  1840 1840 GLN GLN A . n 
A 1 624  ILE 624  1841 1841 ILE ILE A . n 
A 1 625  GLY 625  1842 1842 GLY GLY A . n 
A 1 626  ALA 626  1843 1843 ALA ALA A . n 
A 1 627  TRP 627  1844 1844 TRP TRP A . n 
A 1 628  GLY 628  1845 1845 GLY GLY A . n 
A 1 629  CYS 629  1846 1846 CYS CYS A . n 
A 1 630  PHE 630  1847 1847 PHE PHE A . n 
A 1 631  ASP 631  1848 1848 ASP ASP A . n 
A 1 632  GLU 632  1849 1849 GLU GLU A . n 
A 1 633  PHE 633  1850 1850 PHE PHE A . n 
A 1 634  ASN 634  1851 1851 ASN ASN A . n 
A 1 635  ARG 635  1852 1852 ARG ARG A . n 
A 1 636  LEU 636  1853 1853 LEU LEU A . n 
A 1 637  ASP 637  1854 1854 ASP ASP A . n 
A 1 638  GLU 638  1855 1855 GLU GLU A . n 
A 1 639  LYS 639  1856 1856 LYS LYS A . n 
A 1 640  VAL 640  1857 1857 VAL VAL A . n 
A 1 641  LEU 641  1858 1858 LEU LEU A . n 
A 1 642  SER 642  1859 1859 SER SER A . n 
A 1 643  ALA 643  1860 1860 ALA ALA A . n 
A 1 644  VAL 644  1861 1861 VAL VAL A . n 
A 1 645  SER 645  1862 1862 SER SER A . n 
A 1 646  ALA 646  1863 1863 ALA ALA A . n 
A 1 647  ASN 647  1864 1864 ASN ASN A . n 
A 1 648  ILE 648  1865 1865 ILE ILE A . n 
A 1 649  GLN 649  1866 1866 GLN GLN A . n 
A 1 650  GLN 650  1867 1867 GLN GLN A . n 
A 1 651  ILE 651  1868 1868 ILE ILE A . n 
A 1 652  GLN 652  1869 1869 GLN GLN A . n 
A 1 653  ASN 653  1870 1870 ASN ASN A . n 
A 1 654  GLY 654  1871 1871 GLY GLY A . n 
A 1 655  LEU 655  1872 1872 LEU LEU A . n 
A 1 656  GLN 656  1873 1873 GLN GLN A . n 
A 1 657  VAL 657  1874 1874 VAL VAL A . n 
A 1 658  GLY 658  1875 1875 GLY GLY A . n 
A 1 659  LYS 659  1876 1876 LYS LYS A . n 
A 1 660  SER 660  1877 1877 SER SER A . n 
A 1 661  HIS 661  1878 1878 HIS HIS A . n 
A 1 662  ILE 662  1879 1879 ILE ILE A . n 
A 1 663  THR 663  1880 1880 THR THR A . n 
A 1 664  LEU 664  1881 1881 LEU LEU A . n 
A 1 665  LEU 665  1882 1882 LEU LEU A . n 
A 1 666  GLU 666  1883 1883 GLU GLU A . n 
A 1 667  GLU 667  1884 1884 GLU GLU A . n 
A 1 668  GLU 668  1885 1885 GLU GLU A . n 
A 1 669  THR 669  1886 1886 THR THR A . n 
A 1 670  PRO 670  1887 1887 PRO PRO A . n 
A 1 671  LEU 671  1888 1888 LEU LEU A . n 
A 1 672  SER 672  1889 1889 SER SER A . n 
A 1 673  PRO 673  1890 1890 PRO PRO A . n 
A 1 674  HIS 674  1891 1891 HIS HIS A . n 
A 1 675  THR 675  1892 1892 THR THR A . n 
A 1 676  ALA 676  1893 1893 ALA ALA A . n 
A 1 677  VAL 677  1894 1894 VAL VAL A . n 
A 1 678  PHE 678  1895 1895 PHE PHE A . n 
A 1 679  ILE 679  1896 1896 ILE ILE A . n 
A 1 680  THR 680  1897 1897 THR THR A . n 
A 1 681  LEU 681  1898 1898 LEU LEU A . n 
A 1 682  ASN 682  1899 1899 ASN ASN A . n 
A 1 683  PRO 683  1900 1900 PRO PRO A . n 
A 1 684  GLY 684  1901 1901 GLY GLY A . n 
A 1 685  TYR 685  1902 1902 TYR TYR A . n 
A 1 686  ASN 686  1903 ?    ?   ?   A . n 
A 1 687  GLY 687  1904 ?    ?   ?   A . n 
A 1 688  ARG 688  1905 1905 ARG ARG A . n 
A 1 689  SER 689  1906 1906 SER SER A . n 
A 1 690  GLU 690  1907 1907 GLU GLU A . n 
A 1 691  LEU 691  1908 1908 LEU LEU A . n 
A 1 692  PRO 692  1909 1909 PRO PRO A . n 
A 1 693  GLU 693  1910 1910 GLU GLU A . n 
A 1 694  ASN 694  1911 1911 ASN ASN A . n 
A 1 695  LEU 695  1912 1912 LEU LEU A . n 
A 1 696  LYS 696  1913 1913 LYS LYS A . n 
A 1 697  LYS 697  1914 1914 LYS LYS A . n 
A 1 698  SER 698  1915 1915 SER SER A . n 
A 1 699  PHE 699  1916 1916 PHE PHE A . n 
A 1 700  ARG 700  1917 1917 ARG ARG A . n 
A 1 701  GLU 701  1918 1918 GLU GLU A . n 
A 1 702  PHE 702  1919 1919 PHE PHE A . n 
A 1 703  SER 703  1920 1920 SER SER A . n 
A 1 704  MET 704  1921 1921 MET MET A . n 
A 1 705  LYS 705  1922 1922 LYS LYS A . n 
A 1 706  SER 706  1923 1923 SER SER A . n 
A 1 707  PRO 707  1924 1924 PRO PRO A . n 
A 1 708  GLN 708  1925 1925 GLN GLN A . n 
A 1 709  SER 709  1926 1926 SER SER A . n 
A 1 710  GLY 710  1927 1927 GLY GLY A . n 
A 1 711  THR 711  1928 1928 THR THR A . n 
A 1 712  ILE 712  1929 1929 ILE ILE A . n 
A 1 713  ALA 713  1930 1930 ALA ALA A . n 
A 1 714  GLU 714  1931 1931 GLU GLU A . n 
A 1 715  MET 715  1932 1932 MET MET A . n 
A 1 716  ILE 716  1933 1933 ILE ILE A . n 
A 1 717  LEU 717  1934 1934 LEU LEU A . n 
A 1 718  GLN 718  1935 1935 GLN GLN A . n 
A 1 719  ILE 719  1936 1936 ILE ILE A . n 
A 1 720  MET 720  1937 1937 MET MET A . n 
A 1 721  GLY 721  1938 1938 GLY GLY A . n 
A 1 722  PHE 722  1939 1939 PHE PHE A . n 
A 1 723  GLU 723  1940 1940 GLU GLU A . n 
A 1 724  ASP 724  1941 1941 ASP ASP A . n 
A 1 725  SER 725  1942 1942 SER SER A . n 
A 1 726  LYS 726  1943 1943 LYS LYS A . n 
A 1 727  SER 727  1944 1944 SER SER A . n 
A 1 728  LEU 728  1945 1945 LEU LEU A . n 
A 1 729  ALA 729  1946 1946 ALA ALA A . n 
A 1 730  SER 730  1947 1947 SER SER A . n 
A 1 731  LYS 731  1948 1948 LYS LYS A . n 
A 1 732  ILE 732  1949 1949 ILE ILE A . n 
A 1 733  VAL 733  1950 1950 VAL VAL A . n 
A 1 734  HIS 734  1951 1951 HIS HIS A . n 
A 1 735  PHE 735  1952 1952 PHE PHE A . n 
A 1 736  LEU 736  1953 1953 LEU LEU A . n 
A 1 737  GLU 737  1954 1954 GLU GLU A . n 
A 1 738  LEU 738  1955 1955 LEU LEU A . n 
A 1 739  LEU 739  1956 1956 LEU LEU A . n 
A 1 740  SER 740  1957 1957 SER SER A . n 
A 1 741  SER 741  1958 1958 SER SER A . n 
A 1 742  LYS 742  1959 1959 LYS LYS A . n 
A 1 743  CYS 743  1960 1960 CYS CYS A . n 
A 1 744  SER 744  1961 1961 SER SER A . n 
A 1 745  SER 745  1962 1962 SER SER A . n 
A 1 746  MET 746  1963 1963 MET MET A . n 
A 1 747  ASN 747  1964 1964 ASN ASN A . n 
A 1 748  HIS 748  1965 1965 HIS HIS A . n 
A 1 749  TYR 749  1966 1966 TYR TYR A . n 
A 1 750  HIS 750  1967 1967 HIS HIS A . n 
A 1 751  PHE 751  1968 1968 PHE PHE A . n 
A 1 752  GLY 752  1969 1969 GLY GLY A . n 
A 1 753  LEU 753  1970 1970 LEU LEU A . n 
A 1 754  ARG 754  1971 1971 ARG ARG A . n 
A 1 755  THR 755  1972 1972 THR THR A . n 
A 1 756  LEU 756  1973 1973 LEU LEU A . n 
A 1 757  LYS 757  1974 1974 LYS LYS A . n 
A 1 758  GLY 758  1975 1975 GLY GLY A . n 
A 1 759  VAL 759  1976 1976 VAL VAL A . n 
A 1 760  LEU 760  1977 1977 LEU LEU A . n 
A 1 761  ARG 761  1978 1978 ARG ARG A . n 
A 1 762  ASN 762  1979 1979 ASN ASN A . n 
A 1 763  CYS 763  1980 1980 CYS CYS A . n 
A 1 764  SER 764  1981 1981 SER SER A . n 
A 1 765  PRO 765  1982 1982 PRO PRO A . n 
A 1 766  LEU 766  1983 1983 LEU LEU A . n 
A 1 767  VAL 767  1984 1984 VAL VAL A . n 
A 1 768  SER 768  1985 1985 SER SER A . n 
A 1 769  GLU 769  1986 1986 GLU GLU A . n 
A 1 770  PHE 770  1987 1987 PHE PHE A . n 
A 1 771  GLY 771  1988 1988 GLY GLY A . n 
A 1 772  GLU 772  1989 1989 GLU GLU A . n 
A 1 773  GLY 773  1990 1990 GLY GLY A . n 
A 1 774  GLU 774  1991 1991 GLU GLU A . n 
A 1 775  LYS 775  1992 1992 LYS LYS A . n 
A 1 776  THR 776  1993 1993 THR THR A . n 
A 1 777  VAL 777  1994 1994 VAL VAL A . n 
A 1 778  VAL 778  1995 1995 VAL VAL A . n 
A 1 779  GLU 779  1996 1996 GLU GLU A . n 
A 1 780  SER 780  1997 1997 SER SER A . n 
A 1 781  LEU 781  1998 1998 LEU LEU A . n 
A 1 782  LYS 782  1999 1999 LYS LYS A . n 
A 1 783  ARG 783  2000 2000 ARG ARG A . n 
A 1 784  VAL 784  2001 2001 VAL VAL A . n 
A 1 785  ILE 785  2002 2002 ILE ILE A . n 
A 1 786  LEU 786  2003 2003 LEU LEU A . n 
A 1 787  PRO 787  2004 2004 PRO PRO A . n 
A 1 788  SER 788  2005 2005 SER SER A . n 
A 1 789  LEU 789  2006 2006 LEU LEU A . n 
A 1 790  GLY 790  2007 2007 GLY GLY A . n 
A 1 791  ASP 791  2008 2008 ASP ASP A . n 
A 1 792  THR 792  2009 2009 THR THR A . n 
A 1 793  ASP 793  2010 2010 ASP ASP A . n 
A 1 794  GLU 794  2011 2011 GLU GLU A . n 
A 1 795  LEU 795  2012 2012 LEU LEU A . n 
A 1 796  VAL 796  2013 2013 VAL VAL A . n 
A 1 797  PHE 797  2014 2014 PHE PHE A . n 
A 1 798  LYS 798  2015 2015 LYS LYS A . n 
A 1 799  ASP 799  2016 2016 ASP ASP A . n 
A 1 800  GLU 800  2017 2017 GLU GLU A . n 
A 1 801  LEU 801  2018 2018 LEU LEU A . n 
A 1 802  SER 802  2019 2019 SER SER A . n 
A 1 803  LYS 803  2020 2020 LYS LYS A . n 
A 1 804  ILE 804  2021 2021 ILE ILE A . n 
A 1 805  PHE 805  2022 2022 PHE PHE A . n 
A 1 806  ASP 806  2023 2023 ASP ASP A . n 
A 1 807  SER 807  2024 2024 SER SER A . n 
A 1 808  ALA 808  2025 ?    ?   ?   A . n 
A 1 809  GLY 809  2026 ?    ?   ?   A . n 
A 1 810  THR 810  2027 ?    ?   ?   A . n 
A 1 811  PRO 811  2028 ?    ?   ?   A . n 
A 1 812  LEU 812  2029 ?    ?   ?   A . n 
A 1 813  ASN 813  2030 ?    ?   ?   A . n 
A 1 814  SER 814  2031 2031 SER SER A . n 
A 1 815  LYS 815  2032 2032 LYS LYS A . n 
A 1 816  ALA 816  2033 2033 ALA ALA A . n 
A 1 817  ILE 817  2034 2034 ILE ILE A . n 
A 1 818  VAL 818  2035 2035 VAL VAL A . n 
A 1 819  GLN 819  2036 2036 GLN GLN A . n 
A 1 820  CYS 820  2037 2037 CYS CYS A . n 
A 1 821  LEU 821  2038 2038 LEU LEU A . n 
A 1 822  LYS 822  2039 2039 LYS LYS A . n 
A 1 823  ASP 823  2040 2040 ASP ASP A . n 
A 1 824  ALA 824  2041 2041 ALA ALA A . n 
A 1 825  GLY 825  2042 2042 GLY GLY A . n 
A 1 826  GLN 826  2043 2043 GLN GLN A . n 
A 1 827  ARG 827  2044 2044 ARG ARG A . n 
A 1 828  SER 828  2045 2045 SER SER A . n 
A 1 829  GLY 829  2046 2046 GLY GLY A . n 
A 1 830  PHE 830  2047 2047 PHE PHE A . n 
A 1 831  SER 831  2048 2048 SER SER A . n 
A 1 832  MET 832  2049 2049 MET MET A . n 
A 1 833  SER 833  2050 2050 SER SER A . n 
A 1 834  GLU 834  2051 2051 GLU GLU A . n 
A 1 835  GLU 835  2052 2052 GLU GLU A . n 
A 1 836  PHE 836  2053 2053 PHE PHE A . n 
A 1 837  LEU 837  2054 2054 LEU LEU A . n 
A 1 838  LYS 838  2055 2055 LYS LYS A . n 
A 1 839  LYS 839  2056 2056 LYS LYS A . n 
A 1 840  CYS 840  2057 2057 CYS CYS A . n 
A 1 841  MET 841  2058 2058 MET MET A . n 
A 1 842  GLN 842  2059 2059 GLN GLN A . n 
A 1 843  PHE 843  2060 2060 PHE PHE A . n 
A 1 844  TYR 844  2061 2061 TYR TYR A . n 
A 1 845  TYR 845  2062 2062 TYR TYR A . n 
A 1 846  MET 846  2063 2063 MET MET A . n 
A 1 847  GLN 847  2064 2064 GLN GLN A . n 
A 1 848  LYS 848  2065 2065 LYS LYS A . n 
A 1 849  THR 849  2066 2066 THR THR A . n 
A 1 850  GLN 850  2067 2067 GLN GLN A . n 
A 1 851  GLN 851  2068 2068 GLN GLN A . n 
A 1 852  ALA 852  2069 2069 ALA ALA A . n 
A 1 853  LEU 853  2070 2070 LEU LEU A . n 
A 1 854  ILE 854  2071 2071 ILE ILE A . n 
A 1 855  LEU 855  2072 2072 LEU LEU A . n 
A 1 856  VAL 856  2073 2073 VAL VAL A . n 
A 1 857  GLY 857  2074 2074 GLY GLY A . n 
A 1 858  LYS 858  2075 2075 LYS LYS A . n 
A 1 859  ALA 859  2076 2076 ALA ALA A . n 
A 1 860  GLY 860  2077 2077 GLY GLY A . n 
A 1 861  CYS 861  2078 2078 CYS CYS A . n 
A 1 862  GLY 862  2079 2079 GLY GLY A . n 
A 1 863  LYS 863  2080 2080 LYS LYS A . n 
A 1 864  THR 864  2081 2081 THR THR A . n 
A 1 865  ALA 865  2082 2082 ALA ALA A . n 
A 1 866  THR 866  2083 2083 THR THR A . n 
A 1 867  TRP 867  2084 2084 TRP TRP A . n 
A 1 868  LYS 868  2085 2085 LYS LYS A . n 
A 1 869  THR 869  2086 2086 THR THR A . n 
A 1 870  VAL 870  2087 2087 VAL VAL A . n 
A 1 871  ILE 871  2088 2088 ILE ILE A . n 
A 1 872  ASP 872  2089 2089 ASP ASP A . n 
A 1 873  ALA 873  2090 2090 ALA ALA A . n 
A 1 874  MET 874  2091 2091 MET MET A . n 
A 1 875  ALA 875  2092 2092 ALA ALA A . n 
A 1 876  ILE 876  2093 2093 ILE ILE A . n 
A 1 877  PHE 877  2094 2094 PHE PHE A . n 
A 1 878  ASP 878  2095 2095 ASP ASP A . n 
A 1 879  GLY 879  2096 2096 GLY GLY A . n 
A 1 880  HIS 880  2097 2097 HIS HIS A . n 
A 1 881  ALA 881  2098 2098 ALA ALA A . n 
A 1 882  ASN 882  2099 2099 ASN ASN A . n 
A 1 883  VAL 883  2100 2100 VAL VAL A . n 
A 1 884  VAL 884  2101 2101 VAL VAL A . n 
A 1 885  TYR 885  2102 2102 TYR TYR A . n 
A 1 886  VAL 886  2103 2103 VAL VAL A . n 
A 1 887  ILE 887  2104 2104 ILE ILE A . n 
A 1 888  ASP 888  2105 2105 ASP ASP A . n 
A 1 889  THR 889  2106 2106 THR THR A . n 
A 1 890  LYS 890  2107 2107 LYS LYS A . n 
A 1 891  VAL 891  2108 2108 VAL VAL A . n 
A 1 892  LEU 892  2109 2109 LEU LEU A . n 
A 1 893  THR 893  2110 2110 THR THR A . n 
A 1 894  LYS 894  2111 2111 LYS LYS A . n 
A 1 895  GLU 895  2112 2112 GLU GLU A . n 
A 1 896  SER 896  2113 2113 SER SER A . n 
A 1 897  LEU 897  2114 2114 LEU LEU A . n 
A 1 898  TYR 898  2115 2115 TYR TYR A . n 
A 1 899  GLY 899  2116 2116 GLY GLY A . n 
A 1 900  SER 900  2117 2117 SER SER A . n 
A 1 901  MET 901  2118 2118 MET MET A . n 
A 1 902  LEU 902  2119 2119 LEU LEU A . n 
A 1 903  LYS 903  2120 2120 LYS LYS A . n 
A 1 904  ALA 904  2121 2121 ALA ALA A . n 
A 1 905  THR 905  2122 2122 THR THR A . n 
A 1 906  LEU 906  2123 2123 LEU LEU A . n 
A 1 907  GLU 907  2124 2124 GLU GLU A . n 
A 1 908  TRP 908  2125 2125 TRP TRP A . n 
A 1 909  ARG 909  2126 2126 ARG ARG A . n 
A 1 910  ASP 910  2127 2127 ASP ASP A . n 
A 1 911  GLY 911  2128 2128 GLY GLY A . n 
A 1 912  LEU 912  2129 2129 LEU LEU A . n 
A 1 913  PHE 913  2130 2130 PHE PHE A . n 
A 1 914  THR 914  2131 2131 THR THR A . n 
A 1 915  SER 915  2132 2132 SER SER A . n 
A 1 916  ILE 916  2133 2133 ILE ILE A . n 
A 1 917  LEU 917  2134 2134 LEU LEU A . n 
A 1 918  ARG 918  2135 2135 ARG ARG A . n 
A 1 919  ARG 919  2136 2136 ARG ARG A . n 
A 1 920  VAL 920  2137 2137 VAL VAL A . n 
A 1 921  ASN 921  2138 2138 ASN ASN A . n 
A 1 922  ASP 922  2139 2139 ASP ASP A . n 
A 1 923  ASP 923  2140 2140 ASP ASP A . n 
A 1 924  ILE 924  2141 2141 ILE ILE A . n 
A 1 925  THR 925  2142 2142 THR THR A . n 
A 1 926  GLY 926  2143 2143 GLY GLY A . n 
A 1 927  THR 927  2144 2144 THR THR A . n 
A 1 928  PHE 928  2145 2145 PHE PHE A . n 
A 1 929  LYS 929  2146 2146 LYS LYS A . n 
A 1 930  ASN 930  2147 2147 ASN ASN A . n 
A 1 931  SER 931  2148 2148 SER SER A . n 
A 1 932  ARG 932  2149 2149 ARG ARG A . n 
A 1 933  ILE 933  2150 2150 ILE ILE A . n 
A 1 934  TRP 934  2151 2151 TRP TRP A . n 
A 1 935  VAL 935  2152 2152 VAL VAL A . n 
A 1 936  VAL 936  2153 2153 VAL VAL A . n 
A 1 937  PHE 937  2154 2154 PHE PHE A . n 
A 1 938  ASP 938  2155 2155 ASP ASP A . n 
A 1 939  SER 939  2156 2156 SER SER A . n 
A 1 940  ASP 940  2157 2157 ASP ASP A . n 
A 1 941  LEU 941  2158 2158 LEU LEU A . n 
A 1 942  ASP 942  2159 2159 ASP ASP A . n 
A 1 943  PRO 943  2160 2160 PRO PRO A . n 
A 1 944  GLU 944  2161 2161 GLU GLU A . n 
A 1 945  TYR 945  2162 2162 TYR TYR A . n 
A 1 946  VAL 946  2163 2163 VAL VAL A . n 
A 1 947  GLU 947  2164 2164 GLU GLU A . n 
A 1 948  ALA 948  2165 2165 ALA ALA A . n 
A 1 949  MET 949  2166 2166 MET MET A . n 
A 1 950  ASN 950  2167 2167 ASN ASN A . n 
A 1 951  SER 951  2168 2168 SER SER A . n 
A 1 952  VAL 952  2169 2169 VAL VAL A . n 
A 1 953  LEU 953  2170 2170 LEU LEU A . n 
A 1 954  ASP 954  2171 2171 ASP ASP A . n 
A 1 955  ASP 955  2172 2172 ASP ASP A . n 
A 1 956  ASN 956  2173 2173 ASN ASN A . n 
A 1 957  LYS 957  2174 2174 LYS LYS A . n 
A 1 958  ILE 958  2175 2175 ILE ILE A . n 
A 1 959  LEU 959  2176 2176 LEU LEU A . n 
A 1 960  THR 960  2177 2177 THR THR A . n 
A 1 961  LEU 961  2178 2178 LEU LEU A . n 
A 1 962  PRO 962  2179 2179 PRO PRO A . n 
A 1 963  ASN 963  2180 2180 ASN ASN A . n 
A 1 964  GLY 964  2181 2181 GLY GLY A . n 
A 1 965  GLU 965  2182 2182 GLU GLU A . n 
A 1 966  ARG 966  2183 2183 ARG ARG A . n 
A 1 967  LEU 967  2184 2184 LEU LEU A . n 
A 1 968  PRO 968  2185 2185 PRO PRO A . n 
A 1 969  ILE 969  2186 2186 ILE ILE A . n 
A 1 970  PRO 970  2187 2187 PRO PRO A . n 
A 1 971  PRO 971  2188 2188 PRO PRO A . n 
A 1 972  ASN 972  2189 2189 ASN ASN A . n 
A 1 973  PHE 973  2190 2190 PHE PHE A . n 
A 1 974  ARG 974  2191 2191 ARG ARG A . n 
A 1 975  ILE 975  2192 2192 ILE ILE A . n 
A 1 976  LEU 976  2193 2193 LEU LEU A . n 
A 1 977  PHE 977  2194 2194 PHE PHE A . n 
A 1 978  GLU 978  2195 2195 GLU GLU A . n 
A 1 979  THR 979  2196 2196 THR THR A . n 
A 1 980  ASP 980  2197 2197 ASP ASP A . n 
A 1 981  ASN 981  2198 2198 ASN ASN A . n 
A 1 982  LEU 982  2199 2199 LEU LEU A . n 
A 1 983  ASP 983  2200 2200 ASP ASP A . n 
A 1 984  HIS 984  2201 2201 HIS HIS A . n 
A 1 985  THR 985  2202 2202 THR THR A . n 
A 1 986  THR 986  2203 2203 THR THR A . n 
A 1 987  PRO 987  2204 2204 PRO PRO A . n 
A 1 988  ALA 988  2205 2205 ALA ALA A . n 
A 1 989  THR 989  2206 2206 THR THR A . n 
A 1 990  ILE 990  2207 2207 ILE ILE A . n 
A 1 991  THR 991  2208 2208 THR THR A . n 
A 1 992  ARG 992  2209 2209 ARG ARG A . n 
A 1 993  CYS 993  2210 2210 CYS CYS A . n 
A 1 994  GLY 994  2211 2211 GLY GLY A . n 
A 1 995  LEU 995  2212 2212 LEU LEU A . n 
A 1 996  LEU 996  2213 2213 LEU LEU A . n 
A 1 997  TRP 997  2214 2214 TRP TRP A . n 
A 1 998  PHE 998  2215 2215 PHE PHE A . n 
A 1 999  SER 999  2216 2216 SER SER A . n 
A 1 1000 THR 1000 2217 2217 THR THR A . n 
A 1 1001 ASP 1001 2218 2218 ASP ASP A . n 
A 1 1002 VAL 1002 2219 2219 VAL VAL A . n 
A 1 1003 CYS 1003 2220 2220 CYS CYS A . n 
A 1 1004 SER 1004 2221 2221 SER SER A . n 
A 1 1005 ILE 1005 2222 2222 ILE ILE A . n 
A 1 1006 SER 1006 2223 2223 SER SER A . n 
A 1 1007 SER 1007 2224 2224 SER SER A . n 
A 1 1008 LYS 1008 2225 2225 LYS LYS A . n 
A 1 1009 ILE 1009 2226 2226 ILE ILE A . n 
A 1 1010 ASP 1010 2227 2227 ASP ASP A . n 
A 1 1011 HIS 1011 2228 2228 HIS HIS A . n 
A 1 1012 LEU 1012 2229 2229 LEU LEU A . n 
A 1 1013 LEU 1013 2230 2230 LEU LEU A . n 
A 1 1014 ASN 1014 2231 2231 ASN ASN A . n 
A 1 1015 LYS 1015 2232 2232 LYS LYS A . n 
A 1 1016 SER 1016 2233 2233 SER SER A . n 
A 1 1017 TYR 1017 2234 2234 TYR TYR A . n 
A 1 1018 GLU 1018 2235 2235 GLU GLU A . n 
A 1 1019 ALA 1019 2236 2236 ALA ALA A . n 
A 1 1020 LEU 1020 2237 2237 LEU LEU A . n 
A 1 1021 ASP 1021 2238 ?    ?   ?   A . n 
A 1 1022 ASN 1022 2239 ?    ?   ?   A . n 
A 1 1023 LYS 1023 2240 ?    ?   ?   A . n 
A 1 1024 LEU 1024 2241 ?    ?   ?   A . n 
A 1 1025 SER 1025 2242 ?    ?   ?   A . n 
A 1 1026 MET 1026 2243 ?    ?   ?   A . n 
A 1 1027 PHE 1027 2244 2244 PHE PHE A . n 
A 1 1028 GLU 1028 2245 2245 GLU GLU A . n 
A 1 1029 LEU 1029 2246 2246 LEU LEU A . n 
A 1 1030 ASP 1030 2247 2247 ASP ASP A . n 
A 1 1031 LYS 1031 2248 2248 LYS LYS A . n 
A 1 1032 LEU 1032 2249 2249 LEU LEU A . n 
A 1 1033 LYS 1033 2250 2250 LYS LYS A . n 
A 1 1034 ASP 1034 2251 2251 ASP ASP A . n 
A 1 1035 LEU 1035 2252 2252 LEU LEU A . n 
A 1 1036 ILE 1036 2253 2253 ILE ILE A . n 
A 1 1037 SER 1037 2254 2254 SER SER A . n 
A 1 1038 ASP 1038 2255 2255 ASP ASP A . n 
A 1 1039 SER 1039 2256 2256 SER SER A . n 
A 1 1040 PHE 1040 2257 2257 PHE PHE A . n 
A 1 1041 ASP 1041 2258 2258 ASP ASP A . n 
A 1 1042 MET 1042 2259 2259 MET MET A . n 
A 1 1043 ALA 1043 2260 2260 ALA ALA A . n 
A 1 1044 SER 1044 2261 2261 SER SER A . n 
A 1 1045 LEU 1045 2262 2262 LEU LEU A . n 
A 1 1046 THR 1046 2263 2263 THR THR A . n 
A 1 1047 ASN 1047 2264 2264 ASN ASN A . n 
A 1 1048 ILE 1048 2265 2265 ILE ILE A . n 
A 1 1049 PHE 1049 2266 2266 PHE PHE A . n 
A 1 1050 THR 1050 2267 2267 THR THR A . n 
A 1 1051 CYS 1051 2268 2268 CYS CYS A . n 
A 1 1052 SER 1052 2269 2269 SER SER A . n 
A 1 1053 ASN 1053 2270 2270 ASN ASN A . n 
A 1 1054 ASP 1054 2271 2271 ASP ASP A . n 
A 1 1055 LEU 1055 2272 2272 LEU LEU A . n 
A 1 1056 VAL 1056 2273 2273 VAL VAL A . n 
A 1 1057 HIS 1057 2274 2274 HIS HIS A . n 
A 1 1058 ILE 1058 2275 2275 ILE ILE A . n 
A 1 1059 LEU 1059 2276 2276 LEU LEU A . n 
A 1 1060 GLY 1060 2277 2277 GLY GLY A . n 
A 1 1061 VAL 1061 2278 2278 VAL VAL A . n 
A 1 1062 ARG 1062 2279 2279 ARG ARG A . n 
A 1 1063 THR 1063 2280 2280 THR THR A . n 
A 1 1064 PHE 1064 2281 2281 PHE PHE A . n 
A 1 1065 ASN 1065 2282 2282 ASN ASN A . n 
A 1 1066 LYS 1066 2283 2283 LYS LYS A . n 
A 1 1067 LEU 1067 2284 2284 LEU LEU A . n 
A 1 1068 GLU 1068 2285 2285 GLU GLU A . n 
A 1 1069 THR 1069 2286 2286 THR THR A . n 
A 1 1070 ALA 1070 2287 2287 ALA ALA A . n 
A 1 1071 VAL 1071 2288 2288 VAL VAL A . n 
A 1 1072 GLN 1072 2289 2289 GLN GLN A . n 
A 1 1073 LEU 1073 2290 2290 LEU LEU A . n 
A 1 1074 ALA 1074 2291 2291 ALA ALA A . n 
A 1 1075 VAL 1075 2292 2292 VAL VAL A . n 
A 1 1076 HIS 1076 2293 2293 HIS HIS A . n 
A 1 1077 LEU 1077 2294 2294 LEU LEU A . n 
A 1 1078 ILE 1078 2295 2295 ILE ILE A . n 
A 1 1079 SER 1079 2296 2296 SER SER A . n 
A 1 1080 SER 1080 2297 2297 SER SER A . n 
A 1 1081 TYR 1081 2298 2298 TYR TYR A . n 
A 1 1082 ARG 1082 2299 2299 ARG ARG A . n 
A 1 1083 GLN 1083 2300 2300 GLN GLN A . n 
A 1 1084 TRP 1084 2301 2301 TRP TRP A . n 
A 1 1085 PHE 1085 2302 2302 PHE PHE A . n 
A 1 1086 GLN 1086 2303 2303 GLN GLN A . n 
A 1 1087 ASN 1087 2304 2304 ASN ASN A . n 
A 1 1088 LEU 1088 2305 2305 LEU LEU A . n 
A 1 1089 ASP 1089 2306 2306 ASP ASP A . n 
A 1 1090 ASP 1090 2307 2307 ASP ASP A . n 
A 1 1091 LYS 1091 2308 2308 LYS LYS A . n 
A 1 1092 SER 1092 2309 2309 SER SER A . n 
A 1 1093 LEU 1093 2310 2310 LEU LEU A . n 
A 1 1094 LYS 1094 2311 2311 LYS LYS A . n 
A 1 1095 ASP 1095 2312 2312 ASP ASP A . n 
A 1 1096 VAL 1096 2313 2313 VAL VAL A . n 
A 1 1097 ILE 1097 2314 2314 ILE ILE A . n 
A 1 1098 THR 1098 2315 2315 THR THR A . n 
A 1 1099 LEU 1099 2316 2316 LEU LEU A . n 
A 1 1100 LEU 1100 2317 2317 LEU LEU A . n 
A 1 1101 ILE 1101 2318 2318 ILE ILE A . n 
A 1 1102 LYS 1102 2319 2319 LYS LYS A . n 
A 1 1103 ARG 1103 2320 2320 ARG ARG A . n 
A 1 1104 SER 1104 2321 2321 SER SER A . n 
A 1 1105 LEU 1105 2322 2322 LEU LEU A . n 
A 1 1106 LEU 1106 2323 2323 LEU LEU A . n 
A 1 1107 TYR 1107 2324 2324 TYR TYR A . n 
A 1 1108 ALA 1108 2325 2325 ALA ALA A . n 
A 1 1109 LEU 1109 2326 2326 LEU LEU A . n 
A 1 1110 ALA 1110 2327 2327 ALA ALA A . n 
A 1 1111 GLY 1111 2328 2328 GLY GLY A . n 
A 1 1112 ASP 1112 2329 2329 ASP ASP A . n 
A 1 1113 SER 1113 2330 2330 SER SER A . n 
A 1 1114 THR 1114 2331 2331 THR THR A . n 
A 1 1115 GLY 1115 2332 2332 GLY GLY A . n 
A 1 1116 GLU 1116 2333 2333 GLU GLU A . n 
A 1 1117 SER 1117 2334 2334 SER SER A . n 
A 1 1118 GLN 1118 2335 2335 GLN GLN A . n 
A 1 1119 ARG 1119 2336 2336 ARG ARG A . n 
A 1 1120 ALA 1120 2337 2337 ALA ALA A . n 
A 1 1121 PHE 1121 2338 2338 PHE PHE A . n 
A 1 1122 ILE 1122 2339 2339 ILE ILE A . n 
A 1 1123 GLN 1123 2340 2340 GLN GLN A . n 
A 1 1124 THR 1124 2341 2341 THR THR A . n 
A 1 1125 ILE 1125 2342 2342 ILE ILE A . n 
A 1 1126 ASN 1126 2343 2343 ASN ASN A . n 
A 1 1127 THR 1127 2344 2344 THR THR A . n 
A 1 1128 TYR 1128 2345 2345 TYR TYR A . n 
A 1 1129 PHE 1129 2346 2346 PHE PHE A . n 
A 1 1130 GLY 1130 2347 2347 GLY GLY A . n 
A 1 1131 HIS 1131 2348 2348 HIS HIS A . n 
A 1 1132 ASP 1132 2349 2349 ASP ASP A . n 
A 1 1133 SER 1133 2350 2350 SER SER A . n 
A 1 1134 GLN 1134 2351 2351 GLN GLN A . n 
A 1 1135 GLU 1135 2352 2352 GLU GLU A . n 
A 1 1136 LEU 1136 2353 2353 LEU LEU A . n 
A 1 1137 SER 1137 2354 2354 SER SER A . n 
A 1 1138 ASP 1138 2355 2355 ASP ASP A . n 
A 1 1139 TYR 1139 2356 2356 TYR TYR A . n 
A 1 1140 SER 1140 2357 2357 SER SER A . n 
A 1 1141 THR 1141 2358 2358 THR THR A . n 
A 1 1142 ILE 1142 2359 2359 ILE ILE A . n 
A 1 1143 VAL 1143 2360 2360 VAL VAL A . n 
A 1 1144 ILE 1144 2361 2361 ILE ILE A . n 
A 1 1145 ALA 1145 2362 ?    ?   ?   A . n 
A 1 1146 ASN 1146 2363 ?    ?   ?   A . n 
A 1 1147 ASP 1147 2364 ?    ?   ?   A . n 
A 1 1148 LYS 1148 2365 ?    ?   ?   A . n 
A 1 1149 LEU 1149 2366 2366 LEU LEU A . n 
A 1 1150 SER 1150 2367 2367 SER SER A . n 
A 1 1151 PHE 1151 2368 2368 PHE PHE A . n 
A 1 1152 SER 1152 2369 2369 SER SER A . n 
A 1 1153 SER 1153 2370 2370 SER SER A . n 
A 1 1154 PHE 1154 2371 2371 PHE PHE A . n 
A 1 1155 CYS 1155 2372 2372 CYS CYS A . n 
A 1 1156 SER 1156 2373 2373 SER SER A . n 
A 1 1157 GLU 1157 2374 2374 GLU GLU A . n 
A 1 1158 ILE 1158 2375 2375 ILE ILE A . n 
A 1 1159 PRO 1159 2376 2376 PRO PRO A . n 
A 1 1160 SER 1160 2377 2377 SER SER A . n 
A 1 1161 VAL 1161 2378 2378 VAL VAL A . n 
A 1 1162 SER 1162 2379 2379 SER SER A . n 
A 1 1163 LEU 1163 2380 2380 LEU LEU A . n 
A 1 1164 GLU 1164 2381 2381 GLU GLU A . n 
A 1 1165 ALA 1165 2382 2382 ALA ALA A . n 
A 1 1166 HIS 1166 2383 2383 HIS HIS A . n 
A 1 1167 GLU 1167 2384 2384 GLU GLU A . n 
A 1 1168 VAL 1168 2385 2385 VAL VAL A . n 
A 1 1169 MET 1169 2386 2386 MET MET A . n 
A 1 1170 ARG 1170 2387 2387 ARG ARG A . n 
A 1 1171 PRO 1171 2388 2388 PRO PRO A . n 
A 1 1172 ASP 1172 2389 2389 ASP ASP A . n 
A 1 1173 ILE 1173 2390 2390 ILE ILE A . n 
A 1 1174 VAL 1174 2391 2391 VAL VAL A . n 
A 1 1175 ILE 1175 2392 2392 ILE ILE A . n 
A 1 1176 PRO 1176 2393 2393 PRO PRO A . n 
A 1 1177 THR 1177 2394 2394 THR THR A . n 
A 1 1178 ILE 1178 2395 2395 ILE ILE A . n 
A 1 1179 ASP 1179 2396 2396 ASP ASP A . n 
A 1 1180 THR 1180 2397 2397 THR THR A . n 
A 1 1181 ILE 1181 2398 2398 ILE ILE A . n 
A 1 1182 LYS 1182 2399 2399 LYS LYS A . n 
A 1 1183 HIS 1183 2400 2400 HIS HIS A . n 
A 1 1184 GLU 1184 2401 2401 GLU GLU A . n 
A 1 1185 LYS 1185 2402 2402 LYS LYS A . n 
A 1 1186 ILE 1186 2403 2403 ILE ILE A . n 
A 1 1187 PHE 1187 2404 2404 PHE PHE A . n 
A 1 1188 TYR 1188 2405 2405 TYR TYR A . n 
A 1 1189 ASP 1189 2406 2406 ASP ASP A . n 
A 1 1190 LEU 1190 2407 2407 LEU LEU A . n 
A 1 1191 LEU 1191 2408 2408 LEU LEU A . n 
A 1 1192 ASN 1192 2409 2409 ASN ASN A . n 
A 1 1193 SER 1193 2410 2410 SER SER A . n 
A 1 1194 LYS 1194 2411 2411 LYS LYS A . n 
A 1 1195 ARG 1195 2412 2412 ARG ARG A . n 
A 1 1196 GLY 1196 2413 2413 GLY GLY A . n 
A 1 1197 ILE 1197 2414 2414 ILE ILE A . n 
A 1 1198 ILE 1198 2415 2415 ILE ILE A . n 
A 1 1199 LEU 1199 2416 2416 LEU LEU A . n 
A 1 1200 CYS 1200 2417 2417 CYS CYS A . n 
A 1 1201 GLY 1201 2418 2418 GLY GLY A . n 
A 1 1202 PRO 1202 2419 2419 PRO PRO A . n 
A 1 1203 PRO 1203 2420 2420 PRO PRO A . n 
A 1 1204 GLY 1204 2421 2421 GLY GLY A . n 
A 1 1205 SER 1205 2422 2422 SER SER A . n 
A 1 1206 GLY 1206 2423 2423 GLY GLY A . n 
A 1 1207 LYS 1207 2424 2424 LYS LYS A . n 
A 1 1208 THR 1208 2425 2425 THR THR A . n 
A 1 1209 MET 1209 2426 2426 MET MET A . n 
A 1 1210 ILE 1210 2427 2427 ILE ILE A . n 
A 1 1211 MET 1211 2428 2428 MET MET A . n 
A 1 1212 ASN 1212 2429 2429 ASN ASN A . n 
A 1 1213 ASN 1213 2430 2430 ASN ASN A . n 
A 1 1214 ALA 1214 2431 2431 ALA ALA A . n 
A 1 1215 LEU 1215 2432 2432 LEU LEU A . n 
A 1 1216 ARG 1216 2433 2433 ARG ARG A . n 
A 1 1217 ASN 1217 2434 2434 ASN ASN A . n 
A 1 1218 SER 1218 2435 2435 SER SER A . n 
A 1 1219 SER 1219 2436 2436 SER SER A . n 
A 1 1220 LEU 1220 2437 2437 LEU LEU A . n 
A 1 1221 TYR 1221 2438 2438 TYR TYR A . n 
A 1 1222 ASP 1222 2439 2439 ASP ASP A . n 
A 1 1223 VAL 1223 2440 2440 VAL VAL A . n 
A 1 1224 VAL 1224 2441 2441 VAL VAL A . n 
A 1 1225 GLY 1225 2442 2442 GLY GLY A . n 
A 1 1226 ILE 1226 2443 2443 ILE ILE A . n 
A 1 1227 ASN 1227 2444 2444 ASN ASN A . n 
A 1 1228 PHE 1228 2445 2445 PHE PHE A . n 
A 1 1229 SER 1229 2446 2446 SER SER A . n 
A 1 1230 LYS 1230 2447 2447 LYS LYS A . n 
A 1 1231 ASP 1231 2448 2448 ASP ASP A . n 
A 1 1232 THR 1232 2449 2449 THR THR A . n 
A 1 1233 THR 1233 2450 2450 THR THR A . n 
A 1 1234 THR 1234 2451 2451 THR THR A . n 
A 1 1235 GLU 1235 2452 2452 GLU GLU A . n 
A 1 1236 HIS 1236 2453 2453 HIS HIS A . n 
A 1 1237 ILE 1237 2454 2454 ILE ILE A . n 
A 1 1238 LEU 1238 2455 2455 LEU LEU A . n 
A 1 1239 SER 1239 2456 2456 SER SER A . n 
A 1 1240 ALA 1240 2457 2457 ALA ALA A . n 
A 1 1241 LEU 1241 2458 2458 LEU LEU A . n 
A 1 1242 HIS 1242 2459 2459 HIS HIS A . n 
A 1 1243 ARG 1243 2460 2460 ARG ARG A . n 
A 1 1244 HIS 1244 2461 2461 HIS HIS A . n 
A 1 1245 THR 1245 2462 2462 THR THR A . n 
A 1 1246 ASN 1246 2463 2463 ASN ASN A . n 
A 1 1247 TYR 1247 2464 2464 TYR TYR A . n 
A 1 1248 VAL 1248 2465 2465 VAL VAL A . n 
A 1 1249 THR 1249 2466 2466 THR THR A . n 
A 1 1250 THR 1250 2467 ?    ?   ?   A . n 
A 1 1251 SER 1251 2468 ?    ?   ?   A . n 
A 1 1252 LYS 1252 2469 ?    ?   ?   A . n 
A 1 1253 GLY 1253 2470 2470 GLY GLY A . n 
A 1 1254 LEU 1254 2471 2471 LEU LEU A . n 
A 1 1255 THR 1255 2472 2472 THR THR A . n 
A 1 1256 LEU 1256 2473 2473 LEU LEU A . n 
A 1 1257 LEU 1257 2474 2474 LEU LEU A . n 
A 1 1258 PRO 1258 2475 2475 PRO PRO A . n 
A 1 1259 LYS 1259 2476 2476 LYS LYS A . n 
A 1 1260 SER 1260 2477 2477 SER SER A . n 
A 1 1261 ASP 1261 2478 2478 ASP ASP A . n 
A 1 1262 ILE 1262 2479 2479 ILE ILE A . n 
A 1 1263 LYS 1263 2480 2480 LYS LYS A . n 
A 1 1264 ASN 1264 2481 2481 ASN ASN A . n 
A 1 1265 LEU 1265 2482 2482 LEU LEU A . n 
A 1 1266 VAL 1266 2483 2483 VAL VAL A . n 
A 1 1267 LEU 1267 2484 2484 LEU LEU A . n 
A 1 1268 PHE 1268 2485 2485 PHE PHE A . n 
A 1 1269 CYS 1269 2486 2486 CYS CYS A . n 
A 1 1270 ASP 1270 2487 2487 ASP ASP A . n 
A 1 1271 GLU 1271 2488 2488 GLU GLU A . n 
A 1 1272 ILE 1272 2489 2489 ILE ILE A . n 
A 1 1273 ASN 1273 2490 2490 ASN ASN A . n 
A 1 1274 LEU 1274 2491 2491 LEU LEU A . n 
A 1 1275 PRO 1275 2492 2492 PRO PRO A . n 
A 1 1276 LYS 1276 2493 2493 LYS LYS A . n 
A 1 1277 LEU 1277 2494 2494 LEU LEU A . n 
A 1 1278 ASP 1278 2495 2495 ASP ASP A . n 
A 1 1279 LYS 1279 2496 2496 LYS LYS A . n 
A 1 1280 TYR 1280 2497 2497 TYR TYR A . n 
A 1 1281 GLY 1281 2498 2498 GLY GLY A . n 
A 1 1282 SER 1282 2499 2499 SER SER A . n 
A 1 1283 GLN 1283 2500 2500 GLN GLN A . n 
A 1 1284 ASN 1284 2501 2501 ASN ASN A . n 
A 1 1285 VAL 1285 2502 2502 VAL VAL A . n 
A 1 1286 VAL 1286 2503 2503 VAL VAL A . n 
A 1 1287 LEU 1287 2504 2504 LEU LEU A . n 
A 1 1288 PHE 1288 2505 2505 PHE PHE A . n 
A 1 1289 LEU 1289 2506 2506 LEU LEU A . n 
A 1 1290 ARG 1290 2507 2507 ARG ARG A . n 
A 1 1291 GLN 1291 2508 2508 GLN GLN A . n 
A 1 1292 LEU 1292 2509 2509 LEU LEU A . n 
A 1 1293 MET 1293 2510 2510 MET MET A . n 
A 1 1294 GLU 1294 2511 2511 GLU GLU A . n 
A 1 1295 LYS 1295 2512 2512 LYS LYS A . n 
A 1 1296 GLN 1296 2513 2513 GLN GLN A . n 
A 1 1297 GLY 1297 2514 2514 GLY GLY A . n 
A 1 1298 PHE 1298 2515 2515 PHE PHE A . n 
A 1 1299 TRP 1299 2516 2516 TRP TRP A . n 
A 1 1300 LYS 1300 2517 2517 LYS LYS A . n 
A 1 1301 THR 1301 2518 2518 THR THR A . n 
A 1 1302 PRO 1302 2519 2519 PRO PRO A . n 
A 1 1303 GLU 1303 2520 2520 GLU GLU A . n 
A 1 1304 ASN 1304 2521 2521 ASN ASN A . n 
A 1 1305 LYS 1305 2522 2522 LYS LYS A . n 
A 1 1306 TRP 1306 2523 2523 TRP TRP A . n 
A 1 1307 VAL 1307 2524 2524 VAL VAL A . n 
A 1 1308 THR 1308 2525 2525 THR THR A . n 
A 1 1309 ILE 1309 2526 2526 ILE ILE A . n 
A 1 1310 GLU 1310 2527 2527 GLU GLU A . n 
A 1 1311 ARG 1311 2528 2528 ARG ARG A . n 
A 1 1312 ILE 1312 2529 2529 ILE ILE A . n 
A 1 1313 HIS 1313 2530 2530 HIS HIS A . n 
A 1 1314 ILE 1314 2531 2531 ILE ILE A . n 
A 1 1315 VAL 1315 2532 2532 VAL VAL A . n 
A 1 1316 GLY 1316 2533 2533 GLY GLY A . n 
A 1 1317 ALA 1317 2534 2534 ALA ALA A . n 
A 1 1318 CYS 1318 2535 2535 CYS CYS A . n 
A 1 1319 ASN 1319 2536 2536 ASN ASN A . n 
A 1 1320 PRO 1320 2537 2537 PRO PRO A . n 
A 1 1321 PRO 1321 2538 2538 PRO PRO A . n 
A 1 1322 THR 1322 2539 2539 THR THR A . n 
A 1 1323 ASP 1323 2540 2540 ASP ASP A . n 
A 1 1324 PRO 1324 2541 2541 PRO PRO A . n 
A 1 1325 GLY 1325 2542 2542 GLY GLY A . n 
A 1 1326 ARG 1326 2543 2543 ARG ARG A . n 
A 1 1327 ILE 1327 2544 2544 ILE ILE A . n 
A 1 1328 PRO 1328 2545 2545 PRO PRO A . n 
A 1 1329 MET 1329 2546 2546 MET MET A . n 
A 1 1330 SER 1330 2547 2547 SER SER A . n 
A 1 1331 GLU 1331 2548 2548 GLU GLU A . n 
A 1 1332 ARG 1332 2549 2549 ARG ARG A . n 
A 1 1333 PHE 1333 2550 2550 PHE PHE A . n 
A 1 1334 THR 1334 2551 2551 THR THR A . n 
A 1 1335 ARG 1335 2552 2552 ARG ARG A . n 
A 1 1336 HIS 1336 2553 2553 HIS HIS A . n 
A 1 1337 ALA 1337 2554 2554 ALA ALA A . n 
A 1 1338 ALA 1338 2555 2555 ALA ALA A . n 
A 1 1339 ILE 1339 2556 2556 ILE ILE A . n 
A 1 1340 LEU 1340 2557 2557 LEU LEU A . n 
A 1 1341 TYR 1341 2558 2558 TYR TYR A . n 
A 1 1342 LEU 1342 2559 2559 LEU LEU A . n 
A 1 1343 GLY 1343 2560 2560 GLY GLY A . n 
A 1 1344 TYR 1344 2561 2561 TYR TYR A . n 
A 1 1345 PRO 1345 2562 2562 PRO PRO A . n 
A 1 1346 SER 1346 2563 2563 SER SER A . n 
A 1 1347 GLY 1347 2564 2564 GLY GLY A . n 
A 1 1348 LYS 1348 2565 2565 LYS LYS A . n 
A 1 1349 SER 1349 2566 2566 SER SER A . n 
A 1 1350 LEU 1350 2567 2567 LEU LEU A . n 
A 1 1351 SER 1351 2568 2568 SER SER A . n 
A 1 1352 GLN 1352 2569 2569 GLN GLN A . n 
A 1 1353 ILE 1353 2570 2570 ILE ILE A . n 
A 1 1354 TYR 1354 2571 2571 TYR TYR A . n 
A 1 1355 GLU 1355 2572 2572 GLU GLU A . n 
A 1 1356 ILE 1356 2573 2573 ILE ILE A . n 
A 1 1357 TYR 1357 2574 2574 TYR TYR A . n 
A 1 1358 TYR 1358 2575 2575 TYR TYR A . n 
A 1 1359 LYS 1359 2576 2576 LYS LYS A . n 
A 1 1360 ALA 1360 2577 2577 ALA ALA A . n 
A 1 1361 ILE 1361 2578 2578 ILE ILE A . n 
A 1 1362 PHE 1362 2579 2579 PHE PHE A . n 
A 1 1363 LYS 1363 2580 2580 LYS LYS A . n 
A 1 1364 LEU 1364 2581 2581 LEU LEU A . n 
A 1 1365 VAL 1365 2582 2582 VAL VAL A . n 
A 1 1366 PRO 1366 2583 2583 PRO PRO A . n 
A 1 1367 GLU 1367 2584 2584 GLU GLU A . n 
A 1 1368 PHE 1368 2585 2585 PHE PHE A . n 
A 1 1369 ARG 1369 2586 2586 ARG ARG A . n 
A 1 1370 SER 1370 2587 2587 SER SER A . n 
A 1 1371 TYR 1371 2588 2588 TYR TYR A . n 
A 1 1372 THR 1372 2589 2589 THR THR A . n 
A 1 1373 GLU 1373 2590 2590 GLU GLU A . n 
A 1 1374 PRO 1374 2591 2591 PRO PRO A . n 
A 1 1375 PHE 1375 2592 2592 PHE PHE A . n 
A 1 1376 ALA 1376 2593 2593 ALA ALA A . n 
A 1 1377 ARG 1377 2594 2594 ARG ARG A . n 
A 1 1378 ALA 1378 2595 2595 ALA ALA A . n 
A 1 1379 SER 1379 2596 2596 SER SER A . n 
A 1 1380 VAL 1380 2597 2597 VAL VAL A . n 
A 1 1381 HIS 1381 2598 2598 HIS HIS A . n 
A 1 1382 LEU 1382 2599 2599 LEU LEU A . n 
A 1 1383 TYR 1383 2600 2600 TYR TYR A . n 
A 1 1384 ASN 1384 2601 2601 ASN ASN A . n 
A 1 1385 GLU 1385 2602 2602 GLU GLU A . n 
A 1 1386 CYS 1386 2603 2603 CYS CYS A . n 
A 1 1387 LYS 1387 2604 2604 LYS LYS A . n 
A 1 1388 ALA 1388 2605 2605 ALA ALA A . n 
A 1 1389 ARG 1389 2606 2606 ARG ARG A . n 
A 1 1390 TYR 1390 2607 2607 TYR TYR A . n 
A 1 1391 SER 1391 2608 2608 SER SER A . n 
A 1 1392 THR 1392 2609 2609 THR THR A . n 
A 1 1393 GLY 1393 2610 2610 GLY GLY A . n 
A 1 1394 LEU 1394 2611 2611 LEU LEU A . n 
A 1 1395 GLN 1395 2612 2612 GLN GLN A . n 
A 1 1396 SER 1396 2613 2613 SER SER A . n 
A 1 1397 HIS 1397 2614 2614 HIS HIS A . n 
A 1 1398 TYR 1398 2615 2615 TYR TYR A . n 
A 1 1399 LEU 1399 2616 2616 LEU LEU A . n 
A 1 1400 PHE 1400 2617 2617 PHE PHE A . n 
A 1 1401 SER 1401 2618 2618 SER SER A . n 
A 1 1402 PRO 1402 2619 2619 PRO PRO A . n 
A 1 1403 ARG 1403 2620 2620 ARG ARG A . n 
A 1 1404 GLU 1404 2621 2621 GLU GLU A . n 
A 1 1405 LEU 1405 2622 2622 LEU LEU A . n 
A 1 1406 THR 1406 2623 2623 THR THR A . n 
A 1 1407 ARG 1407 2624 2624 ARG ARG A . n 
A 1 1408 LEU 1408 2625 2625 LEU LEU A . n 
A 1 1409 VAL 1409 2626 2626 VAL VAL A . n 
A 1 1410 ARG 1410 2627 2627 ARG ARG A . n 
A 1 1411 GLY 1411 2628 2628 GLY GLY A . n 
A 1 1412 VAL 1412 2629 2629 VAL VAL A . n 
A 1 1413 TYR 1413 2630 2630 TYR TYR A . n 
A 1 1414 THR 1414 2631 2631 THR THR A . n 
A 1 1415 ALA 1415 2632 2632 ALA ALA A . n 
A 1 1416 ILE 1416 2633 2633 ILE ILE A . n 
A 1 1417 ASN 1417 2634 2634 ASN ASN A . n 
A 1 1418 THR 1418 2635 2635 THR THR A . n 
A 1 1419 GLY 1419 2636 2636 GLY GLY A . n 
A 1 1420 PRO 1420 2637 2637 PRO PRO A . n 
A 1 1421 ARG 1421 2638 2638 ARG ARG A . n 
A 1 1422 GLN 1422 2639 2639 GLN GLN A . n 
A 1 1423 THR 1423 2640 2640 THR THR A . n 
A 1 1424 LEU 1424 2641 2641 LEU LEU A . n 
A 1 1425 ARG 1425 2642 2642 ARG ARG A . n 
A 1 1426 SER 1426 2643 2643 SER SER A . n 
A 1 1427 LEU 1427 2644 2644 LEU LEU A . n 
A 1 1428 ILE 1428 2645 2645 ILE ILE A . n 
A 1 1429 ARG 1429 2646 2646 ARG ARG A . n 
A 1 1430 LEU 1430 2647 2647 LEU LEU A . n 
A 1 1431 TRP 1431 2648 2648 TRP TRP A . n 
A 1 1432 ALA 1432 2649 2649 ALA ALA A . n 
A 1 1433 TYR 1433 2650 2650 TYR TYR A . n 
A 1 1434 GLU 1434 2651 2651 GLU GLU A . n 
A 1 1435 ALA 1435 2652 2652 ALA ALA A . n 
A 1 1436 TRP 1436 2653 2653 TRP TRP A . n 
A 1 1437 ARG 1437 2654 2654 ARG ARG A . n 
A 1 1438 ILE 1438 2655 2655 ILE ILE A . n 
A 1 1439 PHE 1439 2656 2656 PHE PHE A . n 
A 1 1440 ALA 1440 2657 2657 ALA ALA A . n 
A 1 1441 ASP 1441 2658 2658 ASP ASP A . n 
A 1 1442 ARG 1442 2659 2659 ARG ARG A . n 
A 1 1443 LEU 1443 2660 2660 LEU LEU A . n 
A 1 1444 VAL 1444 2661 2661 VAL VAL A . n 
A 1 1445 GLY 1445 2662 2662 GLY GLY A . n 
A 1 1446 VAL 1446 2663 2663 VAL VAL A . n 
A 1 1447 LYS 1447 2664 2664 LYS LYS A . n 
A 1 1448 GLU 1448 2665 2665 GLU GLU A . n 
A 1 1449 LYS 1449 2666 2666 LYS LYS A . n 
A 1 1450 ASN 1450 2667 2667 ASN ASN A . n 
A 1 1451 SER 1451 2668 2668 SER SER A . n 
A 1 1452 PHE 1452 2669 2669 PHE PHE A . n 
A 1 1453 GLU 1453 2670 2670 GLU GLU A . n 
A 1 1454 GLN 1454 2671 2671 GLN GLN A . n 
A 1 1455 LEU 1455 2672 2672 LEU LEU A . n 
A 1 1456 LEU 1456 2673 2673 LEU LEU A . n 
A 1 1457 TYR 1457 2674 2674 TYR TYR A . n 
A 1 1458 GLU 1458 2675 2675 GLU GLU A . n 
A 1 1459 THR 1459 2676 2676 THR THR A . n 
A 1 1460 VAL 1460 2677 2677 VAL VAL A . n 
A 1 1461 ASP 1461 2678 2678 ASP ASP A . n 
A 1 1462 LYS 1462 2679 2679 LYS LYS A . n 
A 1 1463 TYR 1463 2680 2680 TYR TYR A . n 
A 1 1464 LEU 1464 2681 2681 LEU LEU A . n 
A 1 1465 PRO 1465 2682 2682 PRO PRO A . n 
A 1 1466 ASN 1466 2683 ?    ?   ?   A . n 
A 1 1467 GLN 1467 2684 ?    ?   ?   A . n 
A 1 1468 ASP 1468 2685 ?    ?   ?   A . n 
A 1 1469 LEU 1469 2686 2686 LEU LEU A . n 
A 1 1470 GLY 1470 2687 2687 GLY GLY A . n 
A 1 1471 ASN 1471 2688 2688 ASN ASN A . n 
A 1 1472 ILE 1472 2689 2689 ILE ILE A . n 
A 1 1473 SER 1473 2690 2690 SER SER A . n 
A 1 1474 SER 1474 2691 2691 SER SER A . n 
A 1 1475 THR 1475 2692 2692 THR THR A . n 
A 1 1476 SER 1476 2693 2693 SER SER A . n 
A 1 1477 LEU 1477 2694 2694 LEU LEU A . n 
A 1 1478 LEU 1478 2695 2695 LEU LEU A . n 
A 1 1479 PHE 1479 2696 2696 PHE PHE A . n 
A 1 1480 SER 1480 2697 2697 SER SER A . n 
A 1 1481 GLY 1481 2698 2698 GLY GLY A . n 
A 1 1482 LEU 1482 2699 2699 LEU LEU A . n 
A 1 1483 LEU 1483 2700 2700 LEU LEU A . n 
A 1 1484 SER 1484 2701 2701 SER SER A . n 
A 1 1485 LEU 1485 2702 2702 LEU LEU A . n 
A 1 1486 ASP 1486 2703 2703 ASP ASP A . n 
A 1 1487 PHE 1487 2704 2704 PHE PHE A . n 
A 1 1488 LYS 1488 2705 2705 LYS LYS A . n 
A 1 1489 GLU 1489 2706 2706 GLU GLU A . n 
A 1 1490 VAL 1490 2707 2707 VAL VAL A . n 
A 1 1491 ASN 1491 2708 2708 ASN ASN A . n 
A 1 1492 LYS 1492 2709 2709 LYS LYS A . n 
A 1 1493 THR 1493 2710 2710 THR THR A . n 
A 1 1494 ASP 1494 2711 2711 ASP ASP A . n 
A 1 1495 LEU 1495 2712 2712 LEU LEU A . n 
A 1 1496 VAL 1496 2713 2713 VAL VAL A . n 
A 1 1497 ASN 1497 2714 2714 ASN ASN A . n 
A 1 1498 PHE 1498 2715 2715 PHE PHE A . n 
A 1 1499 ILE 1499 2716 2716 ILE ILE A . n 
A 1 1500 GLU 1500 2717 2717 GLU GLU A . n 
A 1 1501 GLU 1501 2718 2718 GLU GLU A . n 
A 1 1502 ARG 1502 2719 2719 ARG ARG A . n 
A 1 1503 PHE 1503 2720 2720 PHE PHE A . n 
A 1 1504 LYS 1504 2721 2721 LYS LYS A . n 
A 1 1505 THR 1505 2722 2722 THR THR A . n 
A 1 1506 PHE 1506 2723 2723 PHE PHE A . n 
A 1 1507 CYS 1507 2724 2724 CYS CYS A . n 
A 1 1508 ASP 1508 2725 2725 ASP ASP A . n 
A 1 1509 GLU 1509 2726 2726 GLU GLU A . n 
A 1 1510 GLU 1510 2727 2727 GLU GLU A . n 
A 1 1511 LEU 1511 2728 2728 LEU LEU A . n 
A 1 1512 GLU 1512 2729 2729 GLU GLU A . n 
A 1 1513 VAL 1513 2730 2730 VAL VAL A . n 
A 1 1514 PRO 1514 2731 2731 PRO PRO A . n 
A 1 1515 MET 1515 2732 2732 MET MET A . n 
A 1 1516 VAL 1516 2733 2733 VAL VAL A . n 
A 1 1517 ILE 1517 2734 2734 ILE ILE A . n 
A 1 1518 HIS 1518 2735 2735 HIS HIS A . n 
A 1 1519 GLU 1519 2736 2736 GLU GLU A . n 
A 1 1520 SER 1520 2737 2737 SER SER A . n 
A 1 1521 MET 1521 2738 2738 MET MET A . n 
A 1 1522 VAL 1522 2739 2739 VAL VAL A . n 
A 1 1523 ASP 1523 2740 2740 ASP ASP A . n 
A 1 1524 HIS 1524 2741 2741 HIS HIS A . n 
A 1 1525 ILE 1525 2742 2742 ILE ILE A . n 
A 1 1526 LEU 1526 2743 2743 LEU LEU A . n 
A 1 1527 ARG 1527 2744 2744 ARG ARG A . n 
A 1 1528 ILE 1528 2745 2745 ILE ILE A . n 
A 1 1529 ASP 1529 2746 2746 ASP ASP A . n 
A 1 1530 ARG 1530 2747 2747 ARG ARG A . n 
A 1 1531 ALA 1531 2748 2748 ALA ALA A . n 
A 1 1532 LEU 1532 2749 2749 LEU LEU A . n 
A 1 1533 LYS 1533 2750 2750 LYS LYS A . n 
A 1 1534 GLN 1534 2751 2751 GLN GLN A . n 
A 1 1535 VAL 1535 2752 2752 VAL VAL A . n 
A 1 1536 GLN 1536 2753 2753 GLN GLN A . n 
A 1 1537 GLY 1537 2754 2754 GLY GLY A . n 
A 1 1538 HIS 1538 2755 2755 HIS HIS A . n 
A 1 1539 MET 1539 2756 2756 MET MET A . n 
A 1 1540 MET 1540 2757 2757 MET MET A . n 
A 1 1541 LEU 1541 2758 2758 LEU LEU A . n 
A 1 1542 ILE 1542 2759 2759 ILE ILE A . n 
A 1 1543 GLY 1543 2760 2760 GLY GLY A . n 
A 1 1544 ALA 1544 2761 2761 ALA ALA A . n 
A 1 1545 SER 1545 2762 2762 SER SER A . n 
A 1 1546 ARG 1546 2763 2763 ARG ARG A . n 
A 1 1547 THR 1547 2764 2764 THR THR A . n 
A 1 1548 GLY 1548 2765 2765 GLY GLY A . n 
A 1 1549 LYS 1549 2766 2766 LYS LYS A . n 
A 1 1550 THR 1550 2767 2767 THR THR A . n 
A 1 1551 ILE 1551 2768 2768 ILE ILE A . n 
A 1 1552 LEU 1552 2769 2769 LEU LEU A . n 
A 1 1553 THR 1553 2770 2770 THR THR A . n 
A 1 1554 ARG 1554 2771 2771 ARG ARG A . n 
A 1 1555 PHE 1555 2772 2772 PHE PHE A . n 
A 1 1556 VAL 1556 2773 2773 VAL VAL A . n 
A 1 1557 ALA 1557 2774 2774 ALA ALA A . n 
A 1 1558 TRP 1558 2775 2775 TRP TRP A . n 
A 1 1559 LEU 1559 2776 2776 LEU LEU A . n 
A 1 1560 ASN 1560 2777 2777 ASN ASN A . n 
A 1 1561 GLY 1561 2778 2778 GLY GLY A . n 
A 1 1562 LEU 1562 2779 2779 LEU LEU A . n 
A 1 1563 LYS 1563 2780 2780 LYS LYS A . n 
A 1 1564 ILE 1564 2781 2781 ILE ILE A . n 
A 1 1565 VAL 1565 2782 2782 VAL VAL A . n 
A 1 1566 GLN 1566 2783 2783 GLN GLN A . n 
A 1 1567 PRO 1567 2784 2784 PRO PRO A . n 
A 1 1568 LYS 1568 2785 2785 LYS LYS A . n 
A 1 1569 ILE 1569 2786 2786 ILE ILE A . n 
A 1 1570 HIS 1570 2787 ?    ?   ?   A . n 
A 1 1571 ARG 1571 2788 2788 ARG ARG A . n 
A 1 1572 HIS 1572 2789 2789 HIS HIS A . n 
A 1 1573 SER 1573 2790 2790 SER SER A . n 
A 1 1574 ASN 1574 2791 2791 ASN ASN A . n 
A 1 1575 LEU 1575 2792 2792 LEU LEU A . n 
A 1 1576 SER 1576 2793 2793 SER SER A . n 
A 1 1577 ASP 1577 2794 2794 ASP ASP A . n 
A 1 1578 PHE 1578 2795 2795 PHE PHE A . n 
A 1 1579 ASP 1579 2796 2796 ASP ASP A . n 
A 1 1580 MET 1580 2797 2797 MET MET A . n 
A 1 1581 ILE 1581 2798 2798 ILE ILE A . n 
A 1 1582 LEU 1582 2799 2799 LEU LEU A . n 
A 1 1583 LYS 1583 2800 2800 LYS LYS A . n 
A 1 1584 LYS 1584 2801 2801 LYS LYS A . n 
A 1 1585 ALA 1585 2802 2802 ALA ALA A . n 
A 1 1586 ILE 1586 2803 2803 ILE ILE A . n 
A 1 1587 SER 1587 2804 2804 SER SER A . n 
A 1 1588 ASP 1588 2805 2805 ASP ASP A . n 
A 1 1589 CYS 1589 2806 2806 CYS CYS A . n 
A 1 1590 SER 1590 2807 2807 SER SER A . n 
A 1 1591 LEU 1591 2808 2808 LEU LEU A . n 
A 1 1592 LYS 1592 2809 2809 LYS LYS A . n 
A 1 1593 GLU 1593 2810 2810 GLU GLU A . n 
A 1 1594 SER 1594 2811 2811 SER SER A . n 
A 1 1595 ARG 1595 2812 2812 ARG ARG A . n 
A 1 1596 THR 1596 2813 2813 THR THR A . n 
A 1 1597 CYS 1597 2814 2814 CYS CYS A . n 
A 1 1598 LEU 1598 2815 2815 LEU LEU A . n 
A 1 1599 ILE 1599 2816 2816 ILE ILE A . n 
A 1 1600 ILE 1600 2817 2817 ILE ILE A . n 
A 1 1601 ASP 1601 2818 2818 ASP ASP A . n 
A 1 1602 GLU 1602 2819 2819 GLU GLU A . n 
A 1 1603 SER 1603 2820 2820 SER SER A . n 
A 1 1604 ASN 1604 2821 2821 ASN ASN A . n 
A 1 1605 ILE 1605 2822 2822 ILE ILE A . n 
A 1 1606 LEU 1606 2823 2823 LEU LEU A . n 
A 1 1607 GLU 1607 2824 2824 GLU GLU A . n 
A 1 1608 THR 1608 2825 2825 THR THR A . n 
A 1 1609 ALA 1609 2826 2826 ALA ALA A . n 
A 1 1610 PHE 1610 2827 2827 PHE PHE A . n 
A 1 1611 LEU 1611 2828 2828 LEU LEU A . n 
A 1 1612 GLU 1612 2829 2829 GLU GLU A . n 
A 1 1613 ARG 1613 2830 2830 ARG ARG A . n 
A 1 1614 MET 1614 2831 2831 MET MET A . n 
A 1 1615 ASN 1615 2832 2832 ASN ASN A . n 
A 1 1616 THR 1616 2833 2833 THR THR A . n 
A 1 1617 LEU 1617 2834 2834 LEU LEU A . n 
A 1 1618 LEU 1618 2835 2835 LEU LEU A . n 
A 1 1619 ALA 1619 2836 2836 ALA ALA A . n 
A 1 1620 ASN 1620 2837 2837 ASN ASN A . n 
A 1 1621 ALA 1621 2838 2838 ALA ALA A . n 
A 1 1622 ASP 1622 2839 2839 ASP ASP A . n 
A 1 1623 ILE 1623 2840 2840 ILE ILE A . n 
A 1 1624 PRO 1624 2841 2841 PRO PRO A . n 
A 1 1625 ASP 1625 2842 2842 ASP ASP A . n 
A 1 1626 LEU 1626 2843 2843 LEU LEU A . n 
A 1 1627 PHE 1627 2844 2844 PHE PHE A . n 
A 1 1628 GLN 1628 2845 2845 GLN GLN A . n 
A 1 1629 GLY 1629 2846 2846 GLY GLY A . n 
A 1 1630 GLU 1630 2847 2847 GLU GLU A . n 
A 1 1631 GLU 1631 2848 2848 GLU GLU A . n 
A 1 1632 TYR 1632 2849 2849 TYR TYR A . n 
A 1 1633 ASP 1633 2850 2850 ASP ASP A . n 
A 1 1634 LYS 1634 2851 2851 LYS LYS A . n 
A 1 1635 LEU 1635 2852 2852 LEU LEU A . n 
A 1 1636 LEU 1636 2853 2853 LEU LEU A . n 
A 1 1637 ASN 1637 2854 2854 ASN ASN A . n 
A 1 1638 ASN 1638 2855 2855 ASN ASN A . n 
A 1 1639 LEU 1639 2856 2856 LEU LEU A . n 
A 1 1640 ARG 1640 2857 2857 ARG ARG A . n 
A 1 1641 ASN 1641 2858 2858 ASN ASN A . n 
A 1 1642 LYS 1642 2859 2859 LYS LYS A . n 
A 1 1643 THR 1643 2860 2860 THR THR A . n 
A 1 1644 ARG 1644 2861 ?    ?   ?   A . n 
A 1 1645 SER 1645 2862 ?    ?   ?   A . n 
A 1 1646 LEU 1646 2863 ?    ?   ?   A . n 
A 1 1647 GLY 1647 2864 ?    ?   ?   A . n 
A 1 1648 LEU 1648 2865 ?    ?   ?   A . n 
A 1 1649 LEU 1649 2866 ?    ?   ?   A . n 
A 1 1650 LEU 1650 2867 ?    ?   ?   A . n 
A 1 1651 ASP 1651 2868 ?    ?   ?   A . n 
A 1 1652 THR 1652 2869 2869 THR THR A . n 
A 1 1653 GLU 1653 2870 2870 GLU GLU A . n 
A 1 1654 GLN 1654 2871 2871 GLN GLN A . n 
A 1 1655 GLU 1655 2872 2872 GLU GLU A . n 
A 1 1656 LEU 1656 2873 2873 LEU LEU A . n 
A 1 1657 TYR 1657 2874 2874 TYR TYR A . n 
A 1 1658 ASP 1658 2875 2875 ASP ASP A . n 
A 1 1659 TRP 1659 2876 2876 TRP TRP A . n 
A 1 1660 PHE 1660 2877 2877 PHE PHE A . n 
A 1 1661 VAL 1661 2878 2878 VAL VAL A . n 
A 1 1662 GLY 1662 2879 2879 GLY GLY A . n 
A 1 1663 GLU 1663 2880 2880 GLU GLU A . n 
A 1 1664 ILE 1664 2881 2881 ILE ILE A . n 
A 1 1665 ALA 1665 2882 2882 ALA ALA A . n 
A 1 1666 LYS 1666 2883 2883 LYS LYS A . n 
A 1 1667 ASN 1667 2884 2884 ASN ASN A . n 
A 1 1668 LEU 1668 2885 2885 LEU LEU A . n 
A 1 1669 HIS 1669 2886 2886 HIS HIS A . n 
A 1 1670 VAL 1670 2887 2887 VAL VAL A . n 
A 1 1671 VAL 1671 2888 2888 VAL VAL A . n 
A 1 1672 PHE 1672 2889 2889 PHE PHE A . n 
A 1 1673 THR 1673 2890 2890 THR THR A . n 
A 1 1674 ILE 1674 2891 2891 ILE ILE A . n 
A 1 1675 CYS 1675 2892 2892 CYS CYS A . n 
A 1 1676 ASP 1676 2893 2893 ASP ASP A . n 
A 1 1677 PRO 1677 2894 2894 PRO PRO A . n 
A 1 1678 THR 1678 2895 ?    ?   ?   A . n 
A 1 1679 ASN 1679 2896 ?    ?   ?   A . n 
A 1 1680 ASN 1680 2897 ?    ?   ?   A . n 
A 1 1681 LYS 1681 2898 2898 LYS LYS A . n 
A 1 1682 SER 1682 2899 2899 SER SER A . n 
A 1 1683 SER 1683 2900 2900 SER SER A . n 
A 1 1684 ALA 1684 2901 2901 ALA ALA A . n 
A 1 1685 MET 1685 2902 2902 MET MET A . n 
A 1 1686 ILE 1686 2903 2903 ILE ILE A . n 
A 1 1687 SER 1687 2904 2904 SER SER A . n 
A 1 1688 SER 1688 2905 2905 SER SER A . n 
A 1 1689 PRO 1689 2906 2906 PRO PRO A . n 
A 1 1690 ALA 1690 2907 2907 ALA ALA A . n 
A 1 1691 LEU 1691 2908 2908 LEU LEU A . n 
A 1 1692 PHE 1692 2909 2909 PHE PHE A . n 
A 1 1693 ASN 1693 2910 2910 ASN ASN A . n 
A 1 1694 ARG 1694 2911 2911 ARG ARG A . n 
A 1 1695 CYS 1695 2912 2912 CYS CYS A . n 
A 1 1696 ILE 1696 2913 2913 ILE ILE A . n 
A 1 1697 ILE 1697 2914 2914 ILE ILE A . n 
A 1 1698 ASN 1698 2915 2915 ASN ASN A . n 
A 1 1699 TRP 1699 2916 2916 TRP TRP A . n 
A 1 1700 MET 1700 2917 2917 MET MET A . n 
A 1 1701 GLY 1701 2918 2918 GLY GLY A . n 
A 1 1702 ASP 1702 2919 2919 ASP ASP A . n 
A 1 1703 TRP 1703 2920 2920 TRP TRP A . n 
A 1 1704 ASP 1704 2921 2921 ASP ASP A . n 
A 1 1705 THR 1705 2922 2922 THR THR A . n 
A 1 1706 LYS 1706 2923 2923 LYS LYS A . n 
A 1 1707 THR 1707 2924 2924 THR THR A . n 
A 1 1708 MET 1708 2925 2925 MET MET A . n 
A 1 1709 SER 1709 2926 2926 SER SER A . n 
A 1 1710 GLN 1710 2927 2927 GLN GLN A . n 
A 1 1711 VAL 1711 2928 2928 VAL VAL A . n 
A 1 1712 ALA 1712 2929 2929 ALA ALA A . n 
A 1 1713 ASN 1713 2930 2930 ASN ASN A . n 
A 1 1714 ASN 1714 2931 2931 ASN ASN A . n 
A 1 1715 MET 1715 2932 2932 MET MET A . n 
A 1 1716 VAL 1716 2933 2933 VAL VAL A . n 
A 1 1717 ASP 1717 2934 2934 ASP ASP A . n 
A 1 1718 VAL 1718 2935 2935 VAL VAL A . n 
A 1 1719 VAL 1719 2936 2936 VAL VAL A . n 
A 1 1720 PRO 1720 2937 2937 PRO PRO A . n 
A 1 1721 MET 1721 2938 2938 MET MET A . n 
A 1 1722 GLU 1722 2939 2939 GLU GLU A . n 
A 1 1723 PHE 1723 2940 2940 PHE PHE A . n 
A 1 1724 THR 1724 2941 2941 THR THR A . n 
A 1 1725 ASP 1725 2942 ?    ?   ?   A . n 
A 1 1726 PHE 1726 2943 ?    ?   ?   A . n 
A 1 1727 ILE 1727 2944 ?    ?   ?   A . n 
A 1 1728 VAL 1728 2945 ?    ?   ?   A . n 
A 1 1729 PRO 1729 2946 ?    ?   ?   A . n 
A 1 1730 GLU 1730 2947 ?    ?   ?   A . n 
A 1 1731 VAL 1731 2948 ?    ?   ?   A . n 
A 1 1732 ASN 1732 2949 ?    ?   ?   A . n 
A 1 1733 LYS 1733 2950 ?    ?   ?   A . n 
A 1 1734 GLU 1734 2951 ?    ?   ?   A . n 
A 1 1735 LEU 1735 2952 ?    ?   ?   A . n 
A 1 1736 VAL 1736 2953 ?    ?   ?   A . n 
A 1 1737 PHE 1737 2954 ?    ?   ?   A . n 
A 1 1738 THR 1738 2955 ?    ?   ?   A . n 
A 1 1739 GLU 1739 2956 ?    ?   ?   A . n 
A 1 1740 PRO 1740 2957 ?    ?   ?   A . n 
A 1 1741 ILE 1741 2958 ?    ?   ?   A . n 
A 1 1742 GLN 1742 2959 ?    ?   ?   A . n 
A 1 1743 THR 1743 2960 2960 THR THR A . n 
A 1 1744 ILE 1744 2961 2961 ILE ILE A . n 
A 1 1745 ARG 1745 2962 2962 ARG ARG A . n 
A 1 1746 ASP 1746 2963 2963 ASP ASP A . n 
A 1 1747 ALA 1747 2964 2964 ALA ALA A . n 
A 1 1748 VAL 1748 2965 2965 VAL VAL A . n 
A 1 1749 VAL 1749 2966 2966 VAL VAL A . n 
A 1 1750 ASN 1750 2967 2967 ASN ASN A . n 
A 1 1751 ILE 1751 2968 2968 ILE ILE A . n 
A 1 1752 LEU 1752 2969 2969 LEU LEU A . n 
A 1 1753 ILE 1753 2970 2970 ILE ILE A . n 
A 1 1754 HIS 1754 2971 2971 HIS HIS A . n 
A 1 1755 PHE 1755 2972 2972 PHE PHE A . n 
A 1 1756 ASP 1756 2973 2973 ASP ASP A . n 
A 1 1757 ARG 1757 2974 2974 ARG ARG A . n 
A 1 1758 ASN 1758 2975 2975 ASN ASN A . n 
A 1 1759 PHE 1759 2976 2976 PHE PHE A . n 
A 1 1760 TYR 1760 2977 2977 TYR TYR A . n 
A 1 1761 GLN 1761 2978 2978 GLN GLN A . n 
A 1 1762 LYS 1762 2979 2979 LYS LYS A . n 
A 1 1763 MET 1763 2980 2980 MET MET A . n 
A 1 1764 LYS 1764 2981 ?    ?   ?   A . n 
A 1 1765 VAL 1765 2982 ?    ?   ?   A . n 
A 1 1766 GLY 1766 2983 ?    ?   ?   A . n 
A 1 1767 VAL 1767 2984 ?    ?   ?   A . n 
A 1 1768 ASN 1768 2985 2985 ASN ASN A . n 
A 1 1769 PRO 1769 2986 2986 PRO PRO A . n 
A 1 1770 ARG 1770 2987 2987 ARG ARG A . n 
A 1 1771 SER 1771 2988 2988 SER SER A . n 
A 1 1772 PRO 1772 2989 2989 PRO PRO A . n 
A 1 1773 GLY 1773 2990 2990 GLY GLY A . n 
A 1 1774 TYR 1774 2991 2991 TYR TYR A . n 
A 1 1775 PHE 1775 2992 2992 PHE PHE A . n 
A 1 1776 ILE 1776 2993 2993 ILE ILE A . n 
A 1 1777 ASP 1777 2994 2994 ASP ASP A . n 
A 1 1778 GLY 1778 2995 2995 GLY GLY A . n 
A 1 1779 LEU 1779 2996 2996 LEU LEU A . n 
A 1 1780 ARG 1780 2997 2997 ARG ARG A . n 
A 1 1781 ALA 1781 2998 2998 ALA ALA A . n 
A 1 1782 LEU 1782 2999 2999 LEU LEU A . n 
A 1 1783 VAL 1783 3000 3000 VAL VAL A . n 
A 1 1784 LYS 1784 3001 3001 LYS LYS A . n 
A 1 1785 LEU 1785 3002 3002 LEU LEU A . n 
A 1 1786 VAL 1786 3003 3003 VAL VAL A . n 
A 1 1787 THR 1787 3004 3004 THR THR A . n 
A 1 1788 ALA 1788 3005 3005 ALA ALA A . n 
A 1 1789 LYS 1789 3006 3006 LYS LYS A . n 
A 1 1790 TYR 1790 3007 3007 TYR TYR A . n 
A 1 1791 GLN 1791 3008 3008 GLN GLN A . n 
A 1 1792 ASP 1792 3009 3009 ASP ASP A . n 
A 1 1793 LEU 1793 3010 3010 LEU LEU A . n 
A 1 1794 GLN 1794 3011 3011 GLN GLN A . n 
A 1 1795 GLU 1795 3012 3012 GLU GLU A . n 
A 1 1796 ASN 1796 3013 3013 ASN ASN A . n 
A 1 1797 GLN 1797 3014 3014 GLN GLN A . n 
A 1 1798 ARG 1798 3015 3015 ARG ARG A . n 
A 1 1799 PHE 1799 3016 3016 PHE PHE A . n 
A 1 1800 VAL 1800 3017 3017 VAL VAL A . n 
A 1 1801 ASN 1801 3018 3018 ASN ASN A . n 
A 1 1802 VAL 1802 3019 3019 VAL VAL A . n 
A 1 1803 GLY 1803 3020 3020 GLY GLY A . n 
A 1 1804 LEU 1804 3021 3021 LEU LEU A . n 
A 1 1805 GLU 1805 3022 3022 GLU GLU A . n 
A 1 1806 LYS 1806 3023 3023 LYS LYS A . n 
A 1 1807 LEU 1807 3024 3024 LEU LEU A . n 
A 1 1808 ASN 1808 3025 3025 ASN ASN A . n 
A 1 1809 GLU 1809 3026 ?    ?   ?   A . n 
A 1 1810 SER 1810 3027 ?    ?   ?   A . n 
A 1 1811 VAL 1811 3028 ?    ?   ?   A . n 
A 1 1812 LEU 1812 3029 ?    ?   ?   A . n 
A 1 1813 LYS 1813 3030 ?    ?   ?   A . n 
A 1 1814 VAL 1814 3031 ?    ?   ?   A . n 
A 1 1815 ASN 1815 3032 ?    ?   ?   A . n 
A 1 1816 GLU 1816 3033 ?    ?   ?   A . n 
A 1 1817 LEU 1817 3034 ?    ?   ?   A . n 
A 1 1818 ASN 1818 3035 ?    ?   ?   A . n 
A 1 1819 LYS 1819 3036 ?    ?   ?   A . n 
A 1 1820 THR 1820 3037 ?    ?   ?   A . n 
A 1 1821 LEU 1821 3038 ?    ?   ?   A . n 
A 1 1822 SER 1822 3039 ?    ?   ?   A . n 
A 1 1823 LYS 1823 3040 ?    ?   ?   A . n 
A 1 1824 LYS 1824 3041 ?    ?   ?   A . n 
A 1 1825 SER 1825 3042 ?    ?   ?   A . n 
A 1 1826 THR 1826 3043 ?    ?   ?   A . n 
A 1 1827 GLU 1827 3044 ?    ?   ?   A . n 
A 1 1828 LEU 1828 3045 ?    ?   ?   A . n 
A 1 1829 THR 1829 3046 ?    ?   ?   A . n 
A 1 1830 GLU 1830 3047 ?    ?   ?   A . n 
A 1 1831 LYS 1831 3048 ?    ?   ?   A . n 
A 1 1832 GLU 1832 3049 ?    ?   ?   A . n 
A 1 1833 LYS 1833 3050 ?    ?   ?   A . n 
A 1 1834 GLU 1834 3051 ?    ?   ?   A . n 
A 1 1835 ALA 1835 3052 ?    ?   ?   A . n 
A 1 1836 ARG 1836 3053 ?    ?   ?   A . n 
A 1 1837 SER 1837 3054 ?    ?   ?   A . n 
A 1 1838 THR 1838 3055 ?    ?   ?   A . n 
A 1 1839 LEU 1839 3056 ?    ?   ?   A . n 
A 1 1840 ASP 1840 3057 ?    ?   ?   A . n 
A 1 1841 LYS 1841 3058 ?    ?   ?   A . n 
A 1 1842 MET 1842 3059 ?    ?   ?   A . n 
A 1 1843 LEU 1843 3060 ?    ?   ?   A . n 
A 1 1844 MET 1844 3061 ?    ?   ?   A . n 
A 1 1845 GLU 1845 3062 ?    ?   ?   A . n 
A 1 1846 GLN 1846 3063 ?    ?   ?   A . n 
A 1 1847 ASN 1847 3064 ?    ?   ?   A . n 
A 1 1848 GLU 1848 3065 ?    ?   ?   A . n 
A 1 1849 SER 1849 3066 ?    ?   ?   A . n 
A 1 1850 GLU 1850 3067 ?    ?   ?   A . n 
A 1 1851 ARG 1851 3068 ?    ?   ?   A . n 
A 1 1852 LYS 1852 3069 ?    ?   ?   A . n 
A 1 1853 GLN 1853 3070 ?    ?   ?   A . n 
A 1 1854 GLU 1854 3071 ?    ?   ?   A . n 
A 1 1855 ALA 1855 3072 ?    ?   ?   A . n 
A 1 1856 THR 1856 3073 ?    ?   ?   A . n 
A 1 1857 GLU 1857 3074 ?    ?   ?   A . n 
A 1 1858 GLU 1858 3075 ?    ?   ?   A . n 
A 1 1859 ILE 1859 3076 ?    ?   ?   A . n 
A 1 1860 LYS 1860 3077 ?    ?   ?   A . n 
A 1 1861 LYS 1861 3078 ?    ?   ?   A . n 
A 1 1862 ILE 1862 3079 ?    ?   ?   A . n 
A 1 1863 LEU 1863 3080 ?    ?   ?   A . n 
A 1 1864 LYS 1864 3081 ?    ?   ?   A . n 
A 1 1865 VAL 1865 3082 ?    ?   ?   A . n 
A 1 1866 GLN 1866 3083 ?    ?   ?   A . n 
A 1 1867 GLU 1867 3084 ?    ?   ?   A . n 
A 1 1868 GLU 1868 3085 ?    ?   ?   A . n 
A 1 1869 ASP 1869 3086 ?    ?   ?   A . n 
A 1 1870 ILE 1870 3087 ?    ?   ?   A . n 
A 1 1871 ARG 1871 3088 ?    ?   ?   A . n 
A 1 1872 LYS 1872 3089 ?    ?   ?   A . n 
A 1 1873 ARG 1873 3090 ?    ?   ?   A . n 
A 1 1874 LYS 1874 3091 ?    ?   ?   A . n 
A 1 1875 GLU 1875 3092 ?    ?   ?   A . n 
A 1 1876 VAL 1876 3093 ?    ?   ?   A . n 
A 1 1877 VAL 1877 3094 ?    ?   ?   A . n 
A 1 1878 MET 1878 3095 ?    ?   ?   A . n 
A 1 1879 LYS 1879 3096 ?    ?   ?   A . n 
A 1 1880 SER 1880 3097 ?    ?   ?   A . n 
A 1 1881 ILE 1881 3098 ?    ?   ?   A . n 
A 1 1882 GLN 1882 3099 ?    ?   ?   A . n 
A 1 1883 ASP 1883 3100 ?    ?   ?   A . n 
A 1 1884 ILE 1884 3101 ?    ?   ?   A . n 
A 1 1885 GLU 1885 3102 ?    ?   ?   A . n 
A 1 1886 PRO 1886 3103 ?    ?   ?   A . n 
A 1 1887 THR 1887 3104 ?    ?   ?   A . n 
A 1 1888 ILE 1888 3105 ?    ?   ?   A . n 
A 1 1889 LEU 1889 3106 ?    ?   ?   A . n 
A 1 1890 GLU 1890 3107 ?    ?   ?   A . n 
A 1 1891 ALA 1891 3108 ?    ?   ?   A . n 
A 1 1892 GLN 1892 3109 ?    ?   ?   A . n 
A 1 1893 ARG 1893 3110 ?    ?   ?   A . n 
A 1 1894 GLY 1894 3111 ?    ?   ?   A . n 
A 1 1895 VAL 1895 3112 ?    ?   ?   A . n 
A 1 1896 LYS 1896 3113 ?    ?   ?   A . n 
A 1 1897 ASN 1897 3114 ?    ?   ?   A . n 
A 1 1898 ILE 1898 3115 ?    ?   ?   A . n 
A 1 1899 LYS 1899 3116 ?    ?   ?   A . n 
A 1 1900 LYS 1900 3117 ?    ?   ?   A . n 
A 1 1901 GLN 1901 3118 ?    ?   ?   A . n 
A 1 1902 GLN 1902 3119 ?    ?   ?   A . n 
A 1 1903 LEU 1903 3120 ?    ?   ?   A . n 
A 1 1904 THR 1904 3121 ?    ?   ?   A . n 
A 1 1905 GLU 1905 3122 ?    ?   ?   A . n 
A 1 1906 ILE 1906 3123 ?    ?   ?   A . n 
A 1 1907 ARG 1907 3124 ?    ?   ?   A . n 
A 1 1908 SER 1908 3125 ?    ?   ?   A . n 
A 1 1909 MET 1909 3126 ?    ?   ?   A . n 
A 1 1910 VAL 1910 3127 ?    ?   ?   A . n 
A 1 1911 ASN 1911 3128 ?    ?   ?   A . n 
A 1 1912 PRO 1912 3129 ?    ?   ?   A . n 
A 1 1913 PRO 1913 3130 ?    ?   ?   A . n 
A 1 1914 SER 1914 3131 ?    ?   ?   A . n 
A 1 1915 GLY 1915 3132 ?    ?   ?   A . n 
A 1 1916 VAL 1916 3133 ?    ?   ?   A . n 
A 1 1917 LYS 1917 3134 ?    ?   ?   A . n 
A 1 1918 ILE 1918 3135 ?    ?   ?   A . n 
A 1 1919 VAL 1919 3136 ?    ?   ?   A . n 
A 1 1920 MET 1920 3137 ?    ?   ?   A . n 
A 1 1921 GLU 1921 3138 ?    ?   ?   A . n 
A 1 1922 ALA 1922 3139 ?    ?   ?   A . n 
A 1 1923 VAL 1923 3140 ?    ?   ?   A . n 
A 1 1924 CYS 1924 3141 ?    ?   ?   A . n 
A 1 1925 ALA 1925 3142 ?    ?   ?   A . n 
A 1 1926 ILE 1926 3143 ?    ?   ?   A . n 
A 1 1927 LEU 1927 3144 ?    ?   ?   A . n 
A 1 1928 GLY 1928 3145 ?    ?   ?   A . n 
A 1 1929 TYR 1929 3146 ?    ?   ?   A . n 
A 1 1930 GLN 1930 3147 ?    ?   ?   A . n 
A 1 1931 PHE 1931 3148 ?    ?   ?   A . n 
A 1 1932 SER 1932 3149 ?    ?   ?   A . n 
A 1 1933 ASN 1933 3150 ?    ?   ?   A . n 
A 1 1934 TRP 1934 3151 ?    ?   ?   A . n 
A 1 1935 ARG 1935 3152 ?    ?   ?   A . n 
A 1 1936 ASP 1936 3153 ?    ?   ?   A . n 
A 1 1937 ILE 1937 3154 ?    ?   ?   A . n 
A 1 1938 GLN 1938 3155 ?    ?   ?   A . n 
A 1 1939 GLN 1939 3156 ?    ?   ?   A . n 
A 1 1940 PHE 1940 3157 ?    ?   ?   A . n 
A 1 1941 ILE 1941 3158 ?    ?   ?   A . n 
A 1 1942 ARG 1942 3159 ?    ?   ?   A . n 
A 1 1943 LYS 1943 3160 ?    ?   ?   A . n 
A 1 1944 ASP 1944 3161 ?    ?   ?   A . n 
A 1 1945 ASP 1945 3162 ?    ?   ?   A . n 
A 1 1946 PHE 1946 3163 ?    ?   ?   A . n 
A 1 1947 ILE 1947 3164 ?    ?   ?   A . n 
A 1 1948 HIS 1948 3165 ?    ?   ?   A . n 
A 1 1949 ASN 1949 3166 ?    ?   ?   A . n 
A 1 1950 ILE 1950 3167 ?    ?   ?   A . n 
A 1 1951 VAL 1951 3168 ?    ?   ?   A . n 
A 1 1952 HIS 1952 3169 ?    ?   ?   A . n 
A 1 1953 TYR 1953 3170 ?    ?   ?   A . n 
A 1 1954 ASP 1954 3171 ?    ?   ?   A . n 
A 1 1955 THR 1955 3172 ?    ?   ?   A . n 
A 1 1956 THR 1956 3173 ?    ?   ?   A . n 
A 1 1957 LEU 1957 3174 ?    ?   ?   A . n 
A 1 1958 HIS 1958 3175 ?    ?   ?   A . n 
A 1 1959 MET 1959 3176 ?    ?   ?   A . n 
A 1 1960 LYS 1960 3177 ?    ?   ?   A . n 
A 1 1961 PRO 1961 3178 ?    ?   ?   A . n 
A 1 1962 GLN 1962 3179 ?    ?   ?   A . n 
A 1 1963 ILE 1963 3180 ?    ?   ?   A . n 
A 1 1964 ARG 1964 3181 ?    ?   ?   A . n 
A 1 1965 LYS 1965 3182 ?    ?   ?   A . n 
A 1 1966 TYR 1966 3183 ?    ?   ?   A . n 
A 1 1967 MET 1967 3184 ?    ?   ?   A . n 
A 1 1968 GLU 1968 3185 ?    ?   ?   A . n 
A 1 1969 GLU 1969 3186 ?    ?   ?   A . n 
A 1 1970 GLU 1970 3187 ?    ?   ?   A . n 
A 1 1971 PHE 1971 3188 ?    ?   ?   A . n 
A 1 1972 LEU 1972 3189 ?    ?   ?   A . n 
A 1 1973 SER 1973 3190 ?    ?   ?   A . n 
A 1 1974 ASP 1974 3191 ?    ?   ?   A . n 
A 1 1975 PRO 1975 3192 ?    ?   ?   A . n 
A 1 1976 ASN 1976 3193 ?    ?   ?   A . n 
A 1 1977 PHE 1977 3194 ?    ?   ?   A . n 
A 1 1978 THR 1978 3195 ?    ?   ?   A . n 
A 1 1979 TYR 1979 3196 ?    ?   ?   A . n 
A 1 1980 GLU 1980 3197 ?    ?   ?   A . n 
A 1 1981 THR 1981 3198 ?    ?   ?   A . n 
A 1 1982 ILE 1982 3199 ?    ?   ?   A . n 
A 1 1983 ASN 1983 3200 ?    ?   ?   A . n 
A 1 1984 ARG 1984 3201 ?    ?   ?   A . n 
A 1 1985 ALA 1985 3202 ?    ?   ?   A . n 
A 1 1986 SER 1986 3203 ?    ?   ?   A . n 
A 1 1987 LYS 1987 3204 ?    ?   ?   A . n 
A 1 1988 ALA 1988 3205 ?    ?   ?   A . n 
A 1 1989 CYS 1989 3206 ?    ?   ?   A . n 
A 1 1990 GLY 1990 3207 ?    ?   ?   A . n 
A 1 1991 PRO 1991 3208 ?    ?   ?   A . n 
A 1 1992 LEU 1992 3209 ?    ?   ?   A . n 
A 1 1993 TYR 1993 3210 ?    ?   ?   A . n 
A 1 1994 GLN 1994 3211 ?    ?   ?   A . n 
A 1 1995 TRP 1995 3212 ?    ?   ?   A . n 
A 1 1996 VAL 1996 3213 ?    ?   ?   A . n 
A 1 1997 ASN 1997 3214 ?    ?   ?   A . n 
A 1 1998 ALA 1998 3215 ?    ?   ?   A . n 
A 1 1999 GLN 1999 3216 ?    ?   ?   A . n 
A 1 2000 ILE 2000 3217 ?    ?   ?   A . n 
A 1 2001 ASN 2001 3218 ?    ?   ?   A . n 
A 1 2002 PHE 2002 3219 ?    ?   ?   A . n 
A 1 2003 SER 2003 3220 ?    ?   ?   A . n 
A 1 2004 LYS 2004 3221 ?    ?   ?   A . n 
A 1 2005 VAL 2005 3222 ?    ?   ?   A . n 
A 1 2006 LEU 2006 3223 ?    ?   ?   A . n 
A 1 2007 GLU 2007 3224 ?    ?   ?   A . n 
A 1 2008 ASN 2008 3225 ?    ?   ?   A . n 
A 1 2009 VAL 2009 3226 ?    ?   ?   A . n 
A 1 2010 ASP 2010 3227 ?    ?   ?   A . n 
A 1 2011 PRO 2011 3228 ?    ?   ?   A . n 
A 1 2012 LEU 2012 3229 ?    ?   ?   A . n 
A 1 2013 ARG 2013 3230 ?    ?   ?   A . n 
A 1 2014 GLN 2014 3231 ?    ?   ?   A . n 
A 1 2015 GLU 2015 3232 ?    ?   ?   A . n 
A 1 2016 MET 2016 3233 ?    ?   ?   A . n 
A 1 2017 LYS 2017 3234 ?    ?   ?   A . n 
A 1 2018 ARG 2018 3235 ?    ?   ?   A . n 
A 1 2019 ILE 2019 3236 ?    ?   ?   A . n 
A 1 2020 GLU 2020 3237 ?    ?   ?   A . n 
A 1 2021 PHE 2021 3238 ?    ?   ?   A . n 
A 1 2022 GLU 2022 3239 ?    ?   ?   A . n 
A 1 2023 SER 2023 3240 ?    ?   ?   A . n 
A 1 2024 LEU 2024 3241 ?    ?   ?   A . n 
A 1 2025 LYS 2025 3242 ?    ?   ?   A . n 
A 1 2026 THR 2026 3243 ?    ?   ?   A . n 
A 1 2027 LYS 2027 3244 ?    ?   ?   A . n 
A 1 2028 ALA 2028 3245 ?    ?   ?   A . n 
A 1 2029 ASN 2029 3246 ?    ?   ?   A . n 
A 1 2030 LEU 2030 3247 ?    ?   ?   A . n 
A 1 2031 LEU 2031 3248 ?    ?   ?   A . n 
A 1 2032 ALA 2032 3249 ?    ?   ?   A . n 
A 1 2033 ALA 2033 3250 ?    ?   ?   A . n 
A 1 2034 GLU 2034 3251 ?    ?   ?   A . n 
A 1 2035 GLU 2035 3252 ?    ?   ?   A . n 
A 1 2036 MET 2036 3253 ?    ?   ?   A . n 
A 1 2037 THR 2037 3254 ?    ?   ?   A . n 
A 1 2038 GLN 2038 3255 ?    ?   ?   A . n 
A 1 2039 ASP 2039 3256 ?    ?   ?   A . n 
A 1 2040 LEU 2040 3257 ?    ?   ?   A . n 
A 1 2041 GLU 2041 3258 ?    ?   ?   A . n 
A 1 2042 ALA 2042 3259 ?    ?   ?   A . n 
A 1 2043 SER 2043 3260 ?    ?   ?   A . n 
A 1 2044 ILE 2044 3261 ?    ?   ?   A . n 
A 1 2045 GLU 2045 3262 ?    ?   ?   A . n 
A 1 2046 VAL 2046 3263 ?    ?   ?   A . n 
A 1 2047 SER 2047 3264 ?    ?   ?   A . n 
A 1 2048 LYS 2048 3265 ?    ?   ?   A . n 
A 1 2049 GLN 2049 3266 ?    ?   ?   A . n 
A 1 2050 LYS 2050 3267 ?    ?   ?   A . n 
A 1 2051 TYR 2051 3268 ?    ?   ?   A . n 
A 1 2052 SER 2052 3269 ?    ?   ?   A . n 
A 1 2053 LEU 2053 3270 ?    ?   ?   A . n 
A 1 2054 LEU 2054 3271 ?    ?   ?   A . n 
A 1 2055 ILE 2055 3272 ?    ?   ?   A . n 
A 1 2056 ARG 2056 3273 ?    ?   ?   A . n 
A 1 2057 ASP 2057 3274 ?    ?   ?   A . n 
A 1 2058 VAL 2058 3275 ?    ?   ?   A . n 
A 1 2059 GLU 2059 3276 ?    ?   ?   A . n 
A 1 2060 ALA 2060 3277 ?    ?   ?   A . n 
A 1 2061 ILE 2061 3278 ?    ?   ?   A . n 
A 1 2062 LYS 2062 3279 ?    ?   ?   A . n 
A 1 2063 THR 2063 3280 ?    ?   ?   A . n 
A 1 2064 GLU 2064 3281 ?    ?   ?   A . n 
A 1 2065 MET 2065 3282 ?    ?   ?   A . n 
A 1 2066 SER 2066 3283 ?    ?   ?   A . n 
A 1 2067 ASN 2067 3284 ?    ?   ?   A . n 
A 1 2068 VAL 2068 3285 ?    ?   ?   A . n 
A 1 2069 GLN 2069 3286 ?    ?   ?   A . n 
A 1 2070 ALA 2070 3287 ?    ?   ?   A . n 
A 1 2071 ASN 2071 3288 ?    ?   ?   A . n 
A 1 2072 LEU 2072 3289 ?    ?   ?   A . n 
A 1 2073 ASP 2073 3290 ?    ?   ?   A . n 
A 1 2074 ARG 2074 3291 ?    ?   ?   A . n 
A 1 2075 SER 2075 3292 ?    ?   ?   A . n 
A 1 2076 ILE 2076 3293 ?    ?   ?   A . n 
A 1 2077 SER 2077 3294 ?    ?   ?   A . n 
A 1 2078 LEU 2078 3295 ?    ?   ?   A . n 
A 1 2079 VAL 2079 3296 ?    ?   ?   A . n 
A 1 2080 LYS 2080 3297 ?    ?   ?   A . n 
A 1 2081 SER 2081 3298 3298 SER SER A . n 
A 1 2082 LEU 2082 3299 3299 LEU LEU A . n 
A 1 2083 THR 2083 3300 3300 THR THR A . n 
A 1 2084 PHE 2084 3301 3301 PHE PHE A . n 
A 1 2085 GLU 2085 3302 3302 GLU GLU A . n 
A 1 2086 LYS 2086 3303 3303 LYS LYS A . n 
A 1 2087 GLU 2087 3304 3304 GLU GLU A . n 
A 1 2088 ARG 2088 3305 3305 ARG ARG A . n 
A 1 2089 TRP 2089 3306 3306 TRP TRP A . n 
A 1 2090 LEU 2090 3307 3307 LEU LEU A . n 
A 1 2091 ASN 2091 3308 3308 ASN ASN A . n 
A 1 2092 THR 2092 3309 3309 THR THR A . n 
A 1 2093 THR 2093 3310 3310 THR THR A . n 
A 1 2094 LYS 2094 3311 3311 LYS LYS A . n 
A 1 2095 GLN 2095 3312 3312 GLN GLN A . n 
A 1 2096 PHE 2096 3313 3313 PHE PHE A . n 
A 1 2097 SER 2097 3314 3314 SER SER A . n 
A 1 2098 LYS 2098 3315 3315 LYS LYS A . n 
A 1 2099 THR 2099 3316 3316 THR THR A . n 
A 1 2100 SER 2100 3317 3317 SER SER A . n 
A 1 2101 GLN 2101 3318 3318 GLN GLN A . n 
A 1 2102 GLU 2102 3319 3319 GLU GLU A . n 
A 1 2103 LEU 2103 3320 3320 LEU LEU A . n 
A 1 2104 ILE 2104 3321 3321 ILE ILE A . n 
A 1 2105 GLY 2105 3322 3322 GLY GLY A . n 
A 1 2106 ASN 2106 3323 3323 ASN ASN A . n 
A 1 2107 CYS 2107 3324 3324 CYS CYS A . n 
A 1 2108 ILE 2108 3325 3325 ILE ILE A . n 
A 1 2109 ILE 2109 3326 3326 ILE ILE A . n 
A 1 2110 SER 2110 3327 3327 SER SER A . n 
A 1 2111 SER 2111 3328 3328 SER SER A . n 
A 1 2112 ILE 2112 3329 3329 ILE ILE A . n 
A 1 2113 TYR 2113 3330 3330 TYR TYR A . n 
A 1 2114 GLU 2114 3331 3331 GLU GLU A . n 
A 1 2115 THR 2115 3332 3332 THR THR A . n 
A 1 2116 TYR 2116 3333 3333 TYR TYR A . n 
A 1 2117 PHE 2117 3334 3334 PHE PHE A . n 
A 1 2118 GLY 2118 3335 3335 GLY GLY A . n 
A 1 2119 HIS 2119 3336 3336 HIS HIS A . n 
A 1 2120 LEU 2120 3337 3337 LEU LEU A . n 
A 1 2121 ASN 2121 3338 3338 ASN ASN A . n 
A 1 2122 GLU 2122 3339 3339 GLU GLU A . n 
A 1 2123 ARG 2123 3340 3340 ARG ARG A . n 
A 1 2124 GLU 2124 3341 3341 GLU GLU A . n 
A 1 2125 ARG 2125 3342 3342 ARG ARG A . n 
A 1 2126 GLY 2126 3343 3343 GLY GLY A . n 
A 1 2127 ASP 2127 3344 3344 ASP ASP A . n 
A 1 2128 MET 2128 3345 3345 MET MET A . n 
A 1 2129 LEU 2129 3346 3346 LEU LEU A . n 
A 1 2130 VAL 2130 3347 3347 VAL VAL A . n 
A 1 2131 ILE 2131 3348 3348 ILE ILE A . n 
A 1 2132 LEU 2132 3349 3349 LEU LEU A . n 
A 1 2133 LYS 2133 3350 3350 LYS LYS A . n 
A 1 2134 ARG 2134 3351 3351 ARG ARG A . n 
A 1 2135 LEU 2135 3352 3352 LEU LEU A . n 
A 1 2136 LEU 2136 3353 3353 LEU LEU A . n 
A 1 2137 GLY 2137 3354 3354 GLY GLY A . n 
A 1 2138 LYS 2138 3355 3355 LYS LYS A . n 
A 1 2139 PHE 2139 3356 3356 PHE PHE A . n 
A 1 2140 ALA 2140 3357 3357 ALA ALA A . n 
A 1 2141 VAL 2141 3358 3358 VAL VAL A . n 
A 1 2142 LYS 2142 3359 3359 LYS LYS A . n 
A 1 2143 TYR 2143 3360 3360 TYR TYR A . n 
A 1 2144 ASP 2144 3361 3361 ASP ASP A . n 
A 1 2145 VAL 2145 3362 3362 VAL VAL A . n 
A 1 2146 ASN 2146 3363 3363 ASN ASN A . n 
A 1 2147 TYR 2147 3364 3364 TYR TYR A . n 
A 1 2148 ARG 2148 3365 3365 ARG ARG A . n 
A 1 2149 PHE 2149 3366 3366 PHE PHE A . n 
A 1 2150 ILE 2150 3367 3367 ILE ILE A . n 
A 1 2151 ASP 2151 3368 3368 ASP ASP A . n 
A 1 2152 TYR 2152 3369 3369 TYR TYR A . n 
A 1 2153 LEU 2153 3370 3370 LEU LEU A . n 
A 1 2154 VAL 2154 3371 3371 VAL VAL A . n 
A 1 2155 THR 2155 3372 3372 THR THR A . n 
A 1 2156 LEU 2156 3373 3373 LEU LEU A . n 
A 1 2157 ASP 2157 3374 3374 ASP ASP A . n 
A 1 2158 GLU 2158 3375 3375 GLU GLU A . n 
A 1 2159 LYS 2159 3376 3376 LYS LYS A . n 
A 1 2160 MET 2160 3377 3377 MET MET A . n 
A 1 2161 LYS 2161 3378 3378 LYS LYS A . n 
A 1 2162 TRP 2162 3379 3379 TRP TRP A . n 
A 1 2163 LEU 2163 3380 3380 LEU LEU A . n 
A 1 2164 GLU 2164 3381 3381 GLU GLU A . n 
A 1 2165 CYS 2165 3382 3382 CYS CYS A . n 
A 1 2166 GLY 2166 3383 3383 GLY GLY A . n 
A 1 2167 LEU 2167 3384 3384 LEU LEU A . n 
A 1 2168 ASP 2168 3385 3385 ASP ASP A . n 
A 1 2169 LYS 2169 3386 3386 LYS LYS A . n 
A 1 2170 ASN 2170 3387 3387 ASN ASN A . n 
A 1 2171 ASP 2171 3388 3388 ASP ASP A . n 
A 1 2172 TYR 2172 3389 3389 TYR TYR A . n 
A 1 2173 PHE 2173 3390 3390 PHE PHE A . n 
A 1 2174 LEU 2174 3391 3391 LEU LEU A . n 
A 1 2175 GLU 2175 3392 3392 GLU GLU A . n 
A 1 2176 ASN 2176 3393 3393 ASN ASN A . n 
A 1 2177 MET 2177 3394 3394 MET MET A . n 
A 1 2178 SER 2178 3395 3395 SER SER A . n 
A 1 2179 ILE 2179 3396 3396 ILE ILE A . n 
A 1 2180 VAL 2180 3397 3397 VAL VAL A . n 
A 1 2181 MET 2181 3398 3398 MET MET A . n 
A 1 2182 ASN 2182 3399 3399 ASN ASN A . n 
A 1 2183 SER 2183 3400 3400 SER SER A . n 
A 1 2184 GLN 2184 3401 3401 GLN GLN A . n 
A 1 2185 ASP 2185 3402 3402 ASP ASP A . n 
A 1 2186 ALA 2186 3403 3403 ALA ALA A . n 
A 1 2187 VAL 2187 3404 3404 VAL VAL A . n 
A 1 2188 PRO 2188 3405 3405 PRO PRO A . n 
A 1 2189 PHE 2189 3406 3406 PHE PHE A . n 
A 1 2190 LEU 2190 3407 3407 LEU LEU A . n 
A 1 2191 LEU 2191 3408 3408 LEU LEU A . n 
A 1 2192 ASP 2192 3409 3409 ASP ASP A . n 
A 1 2193 PRO 2193 3410 3410 PRO PRO A . n 
A 1 2194 SER 2194 3411 3411 SER SER A . n 
A 1 2195 SER 2195 3412 3412 SER SER A . n 
A 1 2196 HIS 2196 3413 3413 HIS HIS A . n 
A 1 2197 MET 2197 3414 3414 MET MET A . n 
A 1 2198 ILE 2198 3415 3415 ILE ILE A . n 
A 1 2199 THR 2199 3416 3416 THR THR A . n 
A 1 2200 VAL 2200 3417 3417 VAL VAL A . n 
A 1 2201 ILE 2201 3418 3418 ILE ILE A . n 
A 1 2202 SER 2202 3419 3419 SER SER A . n 
A 1 2203 ASN 2203 3420 3420 ASN ASN A . n 
A 1 2204 TYR 2204 3421 3421 TYR TYR A . n 
A 1 2205 TYR 2205 3422 3422 TYR TYR A . n 
A 1 2206 GLY 2206 3423 3423 GLY GLY A . n 
A 1 2207 ASN 2207 3424 3424 ASN ASN A . n 
A 1 2208 LYS 2208 3425 3425 LYS LYS A . n 
A 1 2209 THR 2209 3426 3426 THR THR A . n 
A 1 2210 VAL 2210 3427 3427 VAL VAL A . n 
A 1 2211 LEU 2211 3428 3428 LEU LEU A . n 
A 1 2212 LEU 2212 3429 3429 LEU LEU A . n 
A 1 2213 SER 2213 3430 3430 SER SER A . n 
A 1 2214 PHE 2214 3431 3431 PHE PHE A . n 
A 1 2215 LEU 2215 3432 ?    ?   ?   A . n 
A 1 2216 GLU 2216 3433 ?    ?   ?   A . n 
A 1 2217 GLU 2217 3434 ?    ?   ?   A . n 
A 1 2218 GLY 2218 3435 3435 GLY GLY A . n 
A 1 2219 PHE 2219 3436 3436 PHE PHE A . n 
A 1 2220 VAL 2220 3437 3437 VAL VAL A . n 
A 1 2221 LYS 2221 3438 3438 LYS LYS A . n 
A 1 2222 ARG 2222 3439 3439 ARG ARG A . n 
A 1 2223 LEU 2223 3440 3440 LEU LEU A . n 
A 1 2224 GLU 2224 3441 3441 GLU GLU A . n 
A 1 2225 ASN 2225 3442 3442 ASN ASN A . n 
A 1 2226 ALA 2226 3443 3443 ALA ALA A . n 
A 1 2227 VAL 2227 3444 3444 VAL VAL A . n 
A 1 2228 ARG 2228 3445 3445 ARG ARG A . n 
A 1 2229 PHE 2229 3446 3446 PHE PHE A . n 
A 1 2230 GLY 2230 3447 3447 GLY GLY A . n 
A 1 2231 SER 2231 3448 3448 SER SER A . n 
A 1 2232 VAL 2232 3449 3449 VAL VAL A . n 
A 1 2233 VAL 2233 3450 3450 VAL VAL A . n 
A 1 2234 ILE 2234 3451 3451 ILE ILE A . n 
A 1 2235 ILE 2235 3452 3452 ILE ILE A . n 
A 1 2236 GLN 2236 3453 3453 GLN GLN A . n 
A 1 2237 ASP 2237 3454 3454 ASP ASP A . n 
A 1 2238 GLY 2238 3455 3455 GLY GLY A . n 
A 1 2239 GLU 2239 3456 3456 GLU GLU A . n 
A 1 2240 PHE 2240 3457 3457 PHE PHE A . n 
A 1 2241 PHE 2241 3458 3458 PHE PHE A . n 
A 1 2242 ASP 2242 3459 ?    ?   ?   A . n 
A 1 2243 PRO 2243 3460 3460 PRO PRO A . n 
A 1 2244 ILE 2244 3461 3461 ILE ILE A . n 
A 1 2245 ILE 2245 3462 3462 ILE ILE A . n 
A 1 2246 SER 2246 3463 3463 SER SER A . n 
A 1 2247 ARG 2247 3464 3464 ARG ARG A . n 
A 1 2248 LEU 2248 3465 3465 LEU LEU A . n 
A 1 2249 ILE 2249 3466 3466 ILE ILE A . n 
A 1 2250 SER 2250 3467 3467 SER SER A . n 
A 1 2251 ARG 2251 3468 3468 ARG ARG A . n 
A 1 2252 GLU 2252 3469 3469 GLU GLU A . n 
A 1 2253 PHE 2253 3470 3470 PHE PHE A . n 
A 1 2254 ASN 2254 3471 3471 ASN ASN A . n 
A 1 2255 HIS 2255 3472 3472 HIS HIS A . n 
A 1 2256 ALA 2256 3473 3473 ALA ALA A . n 
A 1 2257 GLY 2257 3474 ?    ?   ?   A . n 
A 1 2258 ASN 2258 3475 ?    ?   ?   A . n 
A 1 2259 ARG 2259 3476 ?    ?   ?   A . n 
A 1 2260 VAL 2260 3477 3477 VAL VAL A . n 
A 1 2261 THR 2261 3478 3478 THR THR A . n 
A 1 2262 VAL 2262 3479 3479 VAL VAL A . n 
A 1 2263 GLU 2263 3480 3480 GLU GLU A . n 
A 1 2264 ILE 2264 3481 3481 ILE ILE A . n 
A 1 2265 GLY 2265 3482 3482 GLY GLY A . n 
A 1 2266 ASP 2266 3483 3483 ASP ASP A . n 
A 1 2267 HIS 2267 3484 3484 HIS HIS A . n 
A 1 2268 GLU 2268 3485 3485 GLU GLU A . n 
A 1 2269 VAL 2269 3486 3486 VAL VAL A . n 
A 1 2270 ASP 2270 3487 3487 ASP ASP A . n 
A 1 2271 VAL 2271 3488 3488 VAL VAL A . n 
A 1 2272 SER 2272 3489 3489 SER SER A . n 
A 1 2273 GLY 2273 3490 3490 GLY GLY A . n 
A 1 2274 ASP 2274 3491 3491 ASP ASP A . n 
A 1 2275 PHE 2275 3492 3492 PHE PHE A . n 
A 1 2276 LYS 2276 3493 3493 LYS LYS A . n 
A 1 2277 LEU 2277 3494 3494 LEU LEU A . n 
A 1 2278 PHE 2278 3495 3495 PHE PHE A . n 
A 1 2279 ILE 2279 3496 3496 ILE ILE A . n 
A 1 2280 HIS 2280 3497 3497 HIS HIS A . n 
A 1 2281 SER 2281 3498 3498 SER SER A . n 
A 1 2282 CYS 2282 3499 3499 CYS CYS A . n 
A 1 2283 ASP 2283 3500 3500 ASP ASP A . n 
A 1 2284 PRO 2284 3501 3501 PRO PRO A . n 
A 1 2285 SER 2285 3502 ?    ?   ?   A . n 
A 1 2286 GLY 2286 3503 ?    ?   ?   A . n 
A 1 2287 ASP 2287 3504 ?    ?   ?   A . n 
A 1 2288 ILE 2288 3505 3505 ILE ILE A . n 
A 1 2289 PRO 2289 3506 3506 PRO PRO A . n 
A 1 2290 ILE 2290 3507 3507 ILE ILE A . n 
A 1 2291 PHE 2291 3508 3508 PHE PHE A . n 
A 1 2292 LEU 2292 3509 3509 LEU LEU A . n 
A 1 2293 ARG 2293 3510 3510 ARG ARG A . n 
A 1 2294 SER 2294 3511 3511 SER SER A . n 
A 1 2295 ARG 2295 3512 3512 ARG ARG A . n 
A 1 2296 VAL 2296 3513 3513 VAL VAL A . n 
A 1 2297 ARG 2297 3514 3514 ARG ARG A . n 
A 1 2298 LEU 2298 3515 3515 LEU LEU A . n 
A 1 2299 VAL 2299 3516 3516 VAL VAL A . n 
A 1 2300 HIS 2300 3517 3517 HIS HIS A . n 
A 1 2301 PHE 2301 3518 3518 PHE PHE A . n 
A 1 2302 VAL 2302 3519 3519 VAL VAL A . n 
A 1 2303 THR 2303 3520 3520 THR THR A . n 
A 1 2304 ASN 2304 3521 3521 ASN ASN A . n 
A 1 2305 LYS 2305 3522 3522 LYS LYS A . n 
A 1 2306 GLU 2306 3523 3523 GLU GLU A . n 
A 1 2307 SER 2307 3524 3524 SER SER A . n 
A 1 2308 ILE 2308 3525 3525 ILE ILE A . n 
A 1 2309 GLU 2309 3526 3526 GLU GLU A . n 
A 1 2310 THR 2310 3527 3527 THR THR A . n 
A 1 2311 ARG 2311 3528 3528 ARG ARG A . n 
A 1 2312 ILE 2312 3529 3529 ILE ILE A . n 
A 1 2313 PHE 2313 3530 3530 PHE PHE A . n 
A 1 2314 ASP 2314 3531 3531 ASP ASP A . n 
A 1 2315 ILE 2315 3532 3532 ILE ILE A . n 
A 1 2316 THR 2316 3533 3533 THR THR A . n 
A 1 2317 LEU 2317 3534 3534 LEU LEU A . n 
A 1 2318 THR 2318 3535 3535 THR THR A . n 
A 1 2319 GLU 2319 3536 3536 GLU GLU A . n 
A 1 2320 GLU 2320 3537 3537 GLU GLU A . n 
A 1 2321 ASN 2321 3538 3538 ASN ASN A . n 
A 1 2322 ALA 2322 3539 3539 ALA ALA A . n 
A 1 2323 GLU 2323 3540 3540 GLU ALA A . n 
A 1 2324 MET 2324 3541 3541 MET ALA A . n 
A 1 2325 GLN 2325 3542 3542 GLN GLN A . n 
A 1 2326 ARG 2326 3543 3543 ARG ARG A . n 
A 1 2327 LYS 2327 3544 3544 LYS LYS A . n 
A 1 2328 ARG 2328 3545 3545 ARG ARG A . n 
A 1 2329 GLU 2329 3546 3546 GLU GLU A . n 
A 1 2330 ASP 2330 3547 3547 ASP ASP A . n 
A 1 2331 LEU 2331 3548 3548 LEU LEU A . n 
A 1 2332 ILE 2332 3549 3549 ILE ILE A . n 
A 1 2333 LYS 2333 3550 3550 LYS LYS A . n 
A 1 2334 LEU 2334 3551 3551 LEU LEU A . n 
A 1 2335 ASN 2335 3552 3552 ASN ASN A . n 
A 1 2336 THR 2336 3553 3553 THR THR A . n 
A 1 2337 GLU 2337 3554 3554 GLU GLU A . n 
A 1 2338 TYR 2338 3555 3555 TYR TYR A . n 
A 1 2339 ARG 2339 3556 3556 ARG ARG A . n 
A 1 2340 LEU 2340 3557 3557 LEU LEU A . n 
A 1 2341 LYS 2341 3558 3558 LYS LYS A . n 
A 1 2342 LEU 2342 3559 3559 LEU LEU A . n 
A 1 2343 LYS 2343 3560 3560 LYS LYS A . n 
A 1 2344 ASN 2344 3561 3561 ASN ASN A . n 
A 1 2345 LEU 2345 3562 3562 LEU LEU A . n 
A 1 2346 GLU 2346 3563 3563 GLU GLU A . n 
A 1 2347 LYS 2347 3564 3564 LYS LYS A . n 
A 1 2348 ARG 2348 3565 3565 ARG ARG A . n 
A 1 2349 LEU 2349 3566 3566 LEU LEU A . n 
A 1 2350 LEU 2350 3567 3567 LEU LEU A . n 
A 1 2351 GLU 2351 3568 3568 GLU GLU A . n 
A 1 2352 GLU 2352 3569 3569 GLU GLU A . n 
A 1 2353 LEU 2353 3570 3570 LEU LEU A . n 
A 1 2354 ASN 2354 3571 3571 ASN ASN A . n 
A 1 2355 ASN 2355 3572 3572 ASN ASN A . n 
A 1 2356 SER 2356 3573 3573 SER ALA A . n 
A 1 2357 GLN 2357 3574 ?    ?   ?   A . n 
A 1 2358 GLY 2358 3575 ?    ?   ?   A . n 
A 1 2359 ASN 2359 3576 ?    ?   ?   A . n 
A 1 2360 MET 2360 3577 ?    ?   ?   A . n 
A 1 2361 LEU 2361 3578 ?    ?   ?   A . n 
A 1 2362 GLU 2362 3579 ?    ?   ?   A . n 
A 1 2363 ASN 2363 3580 ?    ?   ?   A . n 
A 1 2364 ASP 2364 3581 ?    ?   ?   A . n 
A 1 2365 GLU 2365 3582 ?    ?   ?   A . n 
A 1 2366 LEU 2366 3583 ?    ?   ?   A . n 
A 1 2367 MET 2367 3584 ?    ?   ?   A . n 
A 1 2368 VAL 2368 3585 ?    ?   ?   A . n 
A 1 2369 THR 2369 3586 ?    ?   ?   A . n 
A 1 2370 LEU 2370 3587 ?    ?   ?   A . n 
A 1 2371 ASN 2371 3588 ?    ?   ?   A . n 
A 1 2372 ASN 2372 3589 ?    ?   ?   A . n 
A 1 2373 LEU 2373 3590 ?    ?   ?   A . n 
A 1 2374 LYS 2374 3591 ?    ?   ?   A . n 
A 1 2375 LYS 2375 3592 3592 LYS LYS A . n 
A 1 2376 GLU 2376 3593 3593 GLU GLU A . n 
A 1 2377 ALA 2377 3594 3594 ALA ALA A . n 
A 1 2378 MET 2378 3595 3595 MET MET A . n 
A 1 2379 ASN 2379 3596 3596 ASN ASN A . n 
A 1 2380 ILE 2380 3597 3597 ILE ILE A . n 
A 1 2381 GLU 2381 3598 3598 GLU GLU A . n 
A 1 2382 LYS 2382 3599 3599 LYS LYS A . n 
A 1 2383 LYS 2383 3600 3600 LYS LYS A . n 
A 1 2384 LEU 2384 3601 3601 LEU LEU A . n 
A 1 2385 SER 2385 3602 3602 SER SER A . n 
A 1 2386 GLU 2386 3603 3603 GLU GLU A . n 
A 1 2387 SER 2387 3604 3604 SER SER A . n 
A 1 2388 GLU 2388 3605 3605 GLU GLU A . n 
A 1 2389 GLU 2389 3606 3606 GLU GLU A . n 
A 1 2390 PHE 2390 3607 3607 PHE PHE A . n 
A 1 2391 PHE 2391 3608 3608 PHE PHE A . n 
A 1 2392 PRO 2392 3609 3609 PRO PRO A . n 
A 1 2393 GLN 2393 3610 3610 GLN GLN A . n 
A 1 2394 PHE 2394 3611 3611 PHE PHE A . n 
A 1 2395 ASP 2395 3612 3612 ASP ASP A . n 
A 1 2396 ASN 2396 3613 3613 ASN ASN A . n 
A 1 2397 LEU 2397 3614 3614 LEU LEU A . n 
A 1 2398 VAL 2398 3615 3615 VAL VAL A . n 
A 1 2399 GLU 2399 3616 3616 GLU GLU A . n 
A 1 2400 GLU 2400 3617 3617 GLU GLU A . n 
A 1 2401 TYR 2401 3618 3618 TYR TYR A . n 
A 1 2402 SER 2402 3619 3619 SER SER A . n 
A 1 2403 ILE 2403 3620 3620 ILE ILE A . n 
A 1 2404 ILE 2404 3621 3621 ILE ILE A . n 
A 1 2405 GLY 2405 3622 3622 GLY GLY A . n 
A 1 2406 LYS 2406 3623 3623 LYS LYS A . n 
A 1 2407 HIS 2407 3624 3624 HIS HIS A . n 
A 1 2408 SER 2408 3625 3625 SER SER A . n 
A 1 2409 VAL 2409 3626 3626 VAL VAL A . n 
A 1 2410 LYS 2410 3627 3627 LYS LYS A . n 
A 1 2411 ILE 2411 3628 3628 ILE ILE A . n 
A 1 2412 PHE 2412 3629 3629 PHE PHE A . n 
A 1 2413 SER 2413 3630 3630 SER SER A . n 
A 1 2414 MET 2414 3631 3631 MET MET A . n 
A 1 2415 LEU 2415 3632 3632 LEU LEU A . n 
A 1 2416 GLU 2416 3633 3633 GLU GLU A . n 
A 1 2417 LYS 2417 3634 3634 LYS LYS A . n 
A 1 2418 PHE 2418 3635 3635 PHE PHE A . n 
A 1 2419 GLY 2419 3636 3636 GLY GLY A . n 
A 1 2420 GLN 2420 3637 3637 GLN GLN A . n 
A 1 2421 PHE 2421 3638 3638 PHE PHE A . n 
A 1 2422 HIS 2422 3639 3639 HIS HIS A . n 
A 1 2423 TRP 2423 3640 3640 TRP TRP A . n 
A 1 2424 PHE 2424 3641 3641 PHE PHE A . n 
A 1 2425 TYR 2425 3642 3642 TYR TYR A . n 
A 1 2426 GLY 2426 3643 3643 GLY GLY A . n 
A 1 2427 ILE 2427 3644 3644 ILE ILE A . n 
A 1 2428 SER 2428 3645 3645 SER SER A . n 
A 1 2429 ILE 2429 3646 3646 ILE ILE A . n 
A 1 2430 GLY 2430 3647 3647 GLY GLY A . n 
A 1 2431 GLN 2431 3648 3648 GLN GLN A . n 
A 1 2432 PHE 2432 3649 3649 PHE PHE A . n 
A 1 2433 LEU 2433 3650 3650 LEU LEU A . n 
A 1 2434 SER 2434 3651 3651 SER SER A . n 
A 1 2435 CYS 2435 3652 3652 CYS CYS A . n 
A 1 2436 PHE 2436 3653 3653 PHE PHE A . n 
A 1 2437 LYS 2437 3654 3654 LYS LYS A . n 
A 1 2438 ARG 2438 3655 3655 ARG ARG A . n 
A 1 2439 VAL 2439 3656 3656 VAL VAL A . n 
A 1 2440 PHE 2440 3657 3657 PHE PHE A . n 
A 1 2441 ILE 2441 3658 3658 ILE ILE A . n 
A 1 2442 LYS 2442 3659 3659 LYS LYS A . n 
A 1 2443 LYS 2443 3660 ?    ?   ?   A . n 
A 1 2444 SER 2444 3661 ?    ?   ?   A . n 
A 1 2445 ARG 2445 3662 ?    ?   ?   A . n 
A 1 2446 GLU 2446 3663 ?    ?   ?   A . n 
A 1 2447 THR 2447 3664 ?    ?   ?   A . n 
A 1 2448 ARG 2448 3665 ?    ?   ?   A . n 
A 1 2449 ALA 2449 3666 ?    ?   ?   A . n 
A 1 2450 ALA 2450 3667 ?    ?   ?   A . n 
A 1 2451 ARG 2451 3668 ?    ?   ?   A . n 
A 1 2452 THR 2452 3669 3669 THR THR A . n 
A 1 2453 ARG 2453 3670 3670 ARG ARG A . n 
A 1 2454 VAL 2454 3671 3671 VAL VAL A . n 
A 1 2455 ASP 2455 3672 3672 ASP ASP A . n 
A 1 2456 GLU 2456 3673 3673 GLU GLU A . n 
A 1 2457 ILE 2457 3674 3674 ILE ILE A . n 
A 1 2458 LEU 2458 3675 3675 LEU LEU A . n 
A 1 2459 TRP 2459 3676 3676 TRP TRP A . n 
A 1 2460 LEU 2460 3677 3677 LEU LEU A . n 
A 1 2461 LEU 2461 3678 3678 LEU LEU A . n 
A 1 2462 TYR 2462 3679 3679 TYR TYR A . n 
A 1 2463 GLN 2463 3680 3680 GLN GLN A . n 
A 1 2464 GLU 2464 3681 3681 GLU GLU A . n 
A 1 2465 VAL 2465 3682 3682 VAL VAL A . n 
A 1 2466 TYR 2466 3683 3683 TYR TYR A . n 
A 1 2467 CYS 2467 3684 3684 CYS CYS A . n 
A 1 2468 GLN 2468 3685 3685 GLN GLN A . n 
A 1 2469 PHE 2469 3686 3686 PHE PHE A . n 
A 1 2470 SER 2470 3687 3687 SER SER A . n 
A 1 2471 THR 2471 3688 3688 THR THR A . n 
A 1 2472 ALA 2472 3689 3689 ALA ALA A . n 
A 1 2473 LEU 2473 3690 3690 LEU LEU A . n 
A 1 2474 ASP 2474 3691 3691 ASP ASP A . n 
A 1 2475 LYS 2475 3692 3692 LYS LYS A . n 
A 1 2476 LYS 2476 3693 3693 LYS LYS A . n 
A 1 2477 PHE 2477 3694 3694 PHE PHE A . n 
A 1 2478 LYS 2478 3695 3695 LYS LYS A . n 
A 1 2479 MET 2479 3696 3696 MET MET A . n 
A 1 2480 ILE 2480 3697 3697 ILE ILE A . n 
A 1 2481 MET 2481 3698 3698 MET MET A . n 
A 1 2482 ALA 2482 3699 3699 ALA ALA A . n 
A 1 2483 MET 2483 3700 3700 MET MET A . n 
A 1 2484 THR 2484 3701 3701 THR THR A . n 
A 1 2485 MET 2485 3702 3702 MET MET A . n 
A 1 2486 PHE 2486 3703 3703 PHE PHE A . n 
A 1 2487 CYS 2487 3704 3704 CYS CYS A . n 
A 1 2488 LEU 2488 3705 3705 LEU LEU A . n 
A 1 2489 TYR 2489 3706 3706 TYR TYR A . n 
A 1 2490 LYS 2490 3707 3707 LYS LYS A . n 
A 1 2491 PHE 2491 3708 3708 PHE PHE A . n 
A 1 2492 ASP 2492 3709 3709 ASP ASP A . n 
A 1 2493 ILE 2493 3710 3710 ILE ILE A . n 
A 1 2494 GLU 2494 3711 3711 GLU GLU A . n 
A 1 2495 SER 2495 3712 3712 SER SER A . n 
A 1 2496 GLU 2496 3713 3713 GLU GLU A . n 
A 1 2497 GLN 2497 3714 3714 GLN GLN A . n 
A 1 2498 TYR 2498 3715 3715 TYR TYR A . n 
A 1 2499 LYS 2499 3716 3716 LYS LYS A . n 
A 1 2500 GLU 2500 3717 3717 GLU GLU A . n 
A 1 2501 ALA 2501 3718 3718 ALA ALA A . n 
A 1 2502 VAL 2502 3719 3719 VAL VAL A . n 
A 1 2503 LEU 2503 3720 3720 LEU LEU A . n 
A 1 2504 THR 2504 3721 3721 THR THR A . n 
A 1 2505 MET 2505 3722 3722 MET MET A . n 
A 1 2506 ILE 2506 3723 3723 ILE ILE A . n 
A 1 2507 GLY 2507 3724 3724 GLY GLY A . n 
A 1 2508 VAL 2508 3725 3725 VAL VAL A . n 
A 1 2509 LEU 2509 3726 3726 LEU LEU A . n 
A 1 2510 SER 2510 3727 3727 SER SER A . n 
A 1 2511 GLU 2511 3728 3728 GLU GLU A . n 
A 1 2512 SER 2512 3729 3729 SER SER A . n 
A 1 2513 SER 2513 3730 3730 SER SER A . n 
A 1 2514 ASP 2514 3731 3731 ASP ASP A . n 
A 1 2515 GLY 2515 3732 3732 GLY GLY A . n 
A 1 2516 VAL 2516 3733 3733 VAL VAL A . n 
A 1 2517 PRO 2517 3734 3734 PRO PRO A . n 
A 1 2518 LYS 2518 3735 3735 LYS LYS A . n 
A 1 2519 LEU 2519 3736 3736 LEU LEU A . n 
A 1 2520 THR 2520 3737 3737 THR THR A . n 
A 1 2521 VAL 2521 3738 ?    ?   ?   A . n 
A 1 2522 ASP 2522 3739 ?    ?   ?   A . n 
A 1 2523 THR 2523 3740 ?    ?   ?   A . n 
A 1 2524 ASN 2524 3741 3741 ASN ASN A . n 
A 1 2525 ASP 2525 3742 3742 ASP ASP A . n 
A 1 2526 ASP 2526 3743 3743 ASP ASP A . n 
A 1 2527 LEU 2527 3744 3744 LEU LEU A . n 
A 1 2528 ARG 2528 3745 3745 ARG ARG A . n 
A 1 2529 TYR 2529 3746 3746 TYR TYR A . n 
A 1 2530 LEU 2530 3747 3747 LEU LEU A . n 
A 1 2531 TRP 2531 3748 3748 TRP TRP A . n 
A 1 2532 ASP 2532 3749 3749 ASP ASP A . n 
A 1 2533 TYR 2533 3750 3750 TYR TYR A . n 
A 1 2534 VAL 2534 3751 3751 VAL VAL A . n 
A 1 2535 THR 2535 3752 3752 THR THR A . n 
A 1 2536 THR 2536 3753 3753 THR THR A . n 
A 1 2537 LYS 2537 3754 3754 LYS LYS A . n 
A 1 2538 SER 2538 3755 3755 SER SER A . n 
A 1 2539 TYR 2539 3756 3756 TYR TYR A . n 
A 1 2540 ILE 2540 3757 3757 ILE ILE A . n 
A 1 2541 SER 2541 3758 3758 SER SER A . n 
A 1 2542 ALA 2542 3759 3759 ALA ALA A . n 
A 1 2543 LEU 2543 3760 3760 LEU LEU A . n 
A 1 2544 ASN 2544 3761 3761 ASN ASN A . n 
A 1 2545 TRP 2545 3762 3762 TRP TRP A . n 
A 1 2546 PHE 2546 3763 3763 PHE PHE A . n 
A 1 2547 LYS 2547 3764 3764 LYS LYS A . n 
A 1 2548 ASN 2548 3765 3765 ASN ASN A . n 
A 1 2549 GLU 2549 3766 3766 GLU GLU A . n 
A 1 2550 PHE 2550 3767 3767 PHE PHE A . n 
A 1 2551 PHE 2551 3768 3768 PHE PHE A . n 
A 1 2552 VAL 2552 3769 3769 VAL VAL A . n 
A 1 2553 ASP 2553 3770 3770 ASP ASP A . n 
A 1 2554 GLU 2554 3771 3771 GLU GLU A . n 
A 1 2555 TRP 2555 3772 3772 TRP TRP A . n 
A 1 2556 ASN 2556 3773 3773 ASN ASN A . n 
A 1 2557 ILE 2557 3774 3774 ILE ILE A . n 
A 1 2558 ALA 2558 3775 3775 ALA ALA A . n 
A 1 2559 ASP 2559 3776 3776 ASP ASP A . n 
A 1 2560 VAL 2560 3777 3777 VAL VAL A . n 
A 1 2561 VAL 2561 3778 3778 VAL VAL A . n 
A 1 2562 ALA 2562 3779 3779 ALA ALA A . n 
A 1 2563 ASN 2563 3780 3780 ASN ASN A . n 
A 1 2564 SER 2564 3781 3781 SER SER A . n 
A 1 2565 GLU 2565 3782 3782 GLU GLU A . n 
A 1 2566 ASN 2566 3783 3783 ASN ASN A . n 
A 1 2567 ASN 2567 3784 3784 ASN ASN A . n 
A 1 2568 TYR 2568 3785 3785 TYR TYR A . n 
A 1 2569 PHE 2569 3786 3786 PHE PHE A . n 
A 1 2570 THR 2570 3787 3787 THR THR A . n 
A 1 2571 MET 2571 3788 3788 MET MET A . n 
A 1 2572 ALA 2572 3789 3789 ALA ALA A . n 
A 1 2573 SER 2573 3790 3790 SER SER A . n 
A 1 2574 GLU 2574 3791 3791 GLU GLU A . n 
A 1 2575 ARG 2575 3792 3792 ARG ARG A . n 
A 1 2576 ASP 2576 3793 3793 ASP ASP A . n 
A 1 2577 VAL 2577 3794 3794 VAL VAL A . n 
A 1 2578 ASP 2578 3795 3795 ASP ASP A . n 
A 1 2579 GLY 2579 3796 3796 GLY GLY A . n 
A 1 2580 THR 2580 3797 3797 THR THR A . n 
A 1 2581 PHE 2581 3798 3798 PHE PHE A . n 
A 1 2582 LYS 2582 3799 3799 LYS LYS A . n 
A 1 2583 LEU 2583 3800 3800 LEU LEU A . n 
A 1 2584 ILE 2584 3801 3801 ILE ILE A . n 
A 1 2585 GLU 2585 3802 3802 GLU GLU A . n 
A 1 2586 LEU 2586 3803 3803 LEU LEU A . n 
A 1 2587 ALA 2587 3804 3804 ALA ALA A . n 
A 1 2588 LYS 2588 3805 3805 LYS LYS A . n 
A 1 2589 ALA 2589 3806 3806 ALA ALA A . n 
A 1 2590 SER 2590 3807 3807 SER SER A . n 
A 1 2591 LYS 2591 3808 3808 LYS LYS A . n 
A 1 2592 GLU 2592 3809 3809 GLU GLU A . n 
A 1 2593 SER 2593 3810 3810 SER SER A . n 
A 1 2594 LEU 2594 3811 3811 LEU LEU A . n 
A 1 2595 LYS 2595 3812 3812 LYS LYS A . n 
A 1 2596 ILE 2596 3813 3813 ILE ILE A . n 
A 1 2597 ILE 2597 3814 3814 ILE ILE A . n 
A 1 2598 PRO 2598 3815 3815 PRO PRO A . n 
A 1 2599 LEU 2599 3816 3816 LEU LEU A . n 
A 1 2600 GLY 2600 3817 3817 GLY GLY A . n 
A 1 2601 SER 2601 3818 3818 SER SER A . n 
A 1 2602 ILE 2602 3819 3819 ILE ILE A . n 
A 1 2603 GLU 2603 3820 3820 GLU GLU A . n 
A 1 2604 ASN 2604 3821 3821 ASN ASN A . n 
A 1 2605 LEU 2605 3822 3822 LEU LEU A . n 
A 1 2606 ASN 2606 3823 3823 ASN ASN A . n 
A 1 2607 TYR 2607 3824 3824 TYR TYR A . n 
A 1 2608 ALA 2608 3825 3825 ALA ALA A . n 
A 1 2609 GLN 2609 3826 3826 GLN GLN A . n 
A 1 2610 GLU 2610 3827 3827 GLU GLU A . n 
A 1 2611 GLU 2611 3828 3828 GLU GLU A . n 
A 1 2612 ILE 2612 3829 3829 ILE ILE A . n 
A 1 2613 SER 2613 3830 3830 SER SER A . n 
A 1 2614 LYS 2614 3831 3831 LYS LYS A . n 
A 1 2615 SER 2615 3832 3832 SER SER A . n 
A 1 2616 LYS 2616 3833 3833 LYS LYS A . n 
A 1 2617 ILE 2617 3834 3834 ILE ILE A . n 
A 1 2618 GLU 2618 3835 3835 GLU GLU A . n 
A 1 2619 GLY 2619 3836 3836 GLY GLY A . n 
A 1 2620 GLY 2620 3837 3837 GLY GLY A . n 
A 1 2621 TRP 2621 3838 3838 TRP TRP A . n 
A 1 2622 ILE 2622 3839 3839 ILE ILE A . n 
A 1 2623 LEU 2623 3840 3840 LEU LEU A . n 
A 1 2624 LEU 2624 3841 3841 LEU LEU A . n 
A 1 2625 GLN 2625 3842 3842 GLN GLN A . n 
A 1 2626 ASN 2626 3843 3843 ASN ASN A . n 
A 1 2627 ILE 2627 3844 3844 ILE ILE A . n 
A 1 2628 GLN 2628 3845 3845 GLN GLN A . n 
A 1 2629 MET 2629 3846 3846 MET MET A . n 
A 1 2630 SER 2630 3847 3847 SER SER A . n 
A 1 2631 LEU 2631 3848 3848 LEU LEU A . n 
A 1 2632 SER 2632 3849 3849 SER SER A . n 
A 1 2633 TRP 2633 3850 3850 TRP TRP A . n 
A 1 2634 VAL 2634 3851 3851 VAL VAL A . n 
A 1 2635 LYS 2635 3852 3852 LYS LYS A . n 
A 1 2636 THR 2636 3853 3853 THR THR A . n 
A 1 2637 TYR 2637 3854 3854 TYR TYR A . n 
A 1 2638 LEU 2638 3855 3855 LEU LEU A . n 
A 1 2639 HIS 2639 3856 3856 HIS HIS A . n 
A 1 2640 LYS 2640 3857 3857 LYS LYS A . n 
A 1 2641 HIS 2641 3858 3858 HIS HIS A . n 
A 1 2642 VAL 2642 3859 3859 VAL VAL A . n 
A 1 2643 GLU 2643 3860 3860 GLU GLU A . n 
A 1 2644 GLU 2644 3861 ?    ?   ?   A . n 
A 1 2645 THR 2645 3862 ?    ?   ?   A . n 
A 1 2646 LYS 2646 3863 ?    ?   ?   A . n 
A 1 2647 ALA 2647 3864 ?    ?   ?   A . n 
A 1 2648 ALA 2648 3865 ?    ?   ?   A . n 
A 1 2649 GLU 2649 3866 ?    ?   ?   A . n 
A 1 2650 GLU 2650 3867 3867 GLU GLU A . n 
A 1 2651 HIS 2651 3868 3868 HIS HIS A . n 
A 1 2652 GLU 2652 3869 3869 GLU GLU A . n 
A 1 2653 LYS 2653 3870 3870 LYS LYS A . n 
A 1 2654 PHE 2654 3871 3871 PHE PHE A . n 
A 1 2655 LYS 2655 3872 3872 LYS LYS A . n 
A 1 2656 MET 2656 3873 3873 MET MET A . n 
A 1 2657 PHE 2657 3874 3874 PHE PHE A . n 
A 1 2658 MET 2658 3875 3875 MET MET A . n 
A 1 2659 THR 2659 3876 3876 THR THR A . n 
A 1 2660 CYS 2660 3877 3877 CYS CYS A . n 
A 1 2661 HIS 2661 3878 3878 HIS HIS A . n 
A 1 2662 LEU 2662 3879 3879 LEU LEU A . n 
A 1 2663 THR 2663 3880 3880 THR THR A . n 
A 1 2664 GLY 2664 3881 3881 GLY GLY A . n 
A 1 2665 ASP 2665 3882 3882 ASP ASP A . n 
A 1 2666 LYS 2666 3883 3883 LYS LYS A . n 
A 1 2667 LEU 2667 3884 3884 LEU LEU A . n 
A 1 2668 PRO 2668 3885 3885 PRO PRO A . n 
A 1 2669 ALA 2669 3886 3886 ALA ALA A . n 
A 1 2670 PRO 2670 3887 3887 PRO PRO A . n 
A 1 2671 LEU 2671 3888 3888 LEU LEU A . n 
A 1 2672 LEU 2672 3889 3889 LEU LEU A . n 
A 1 2673 GLN 2673 3890 3890 GLN GLN A . n 
A 1 2674 ARG 2674 3891 3891 ARG ARG A . n 
A 1 2675 THR 2675 3892 3892 THR THR A . n 
A 1 2676 ASP 2676 3893 3893 ASP ASP A . n 
A 1 2677 ARG 2677 3894 3894 ARG ARG A . n 
A 1 2678 VAL 2678 3895 3895 VAL VAL A . n 
A 1 2679 VAL 2679 3896 3896 VAL VAL A . n 
A 1 2680 TYR 2680 3897 3897 TYR TYR A . n 
A 1 2681 GLU 2681 3898 3898 GLU GLU A . n 
A 1 2682 ASP 2682 3899 3899 ASP ASP A . n 
A 1 2683 ILE 2683 3900 3900 ILE ILE A . n 
A 1 2684 PRO 2684 3901 3901 PRO PRO A . n 
A 1 2685 GLY 2685 3902 3902 GLY GLY A . n 
A 1 2686 ILE 2686 3903 3903 ILE ILE A . n 
A 1 2687 LEU 2687 3904 3904 LEU LEU A . n 
A 1 2688 ASP 2688 3905 3905 ASP ASP A . n 
A 1 2689 THR 2689 3906 3906 THR THR A . n 
A 1 2690 VAL 2690 3907 3907 VAL VAL A . n 
A 1 2691 LYS 2691 3908 3908 LYS LYS A . n 
A 1 2692 ASP 2692 3909 3909 ASP ASP A . n 
A 1 2693 LEU 2693 3910 3910 LEU LEU A . n 
A 1 2694 TRP 2694 3911 3911 TRP TRP A . n 
A 1 2695 GLY 2695 3912 3912 GLY GLY A . n 
A 1 2696 SER 2696 3913 3913 SER SER A . n 
A 1 2697 GLN 2697 3914 3914 GLN GLN A . n 
A 1 2698 PHE 2698 3915 3915 PHE PHE A . n 
A 1 2699 PHE 2699 3916 3916 PHE PHE A . n 
A 1 2700 THR 2700 3917 ?    ?   ?   A . n 
A 1 2701 GLY 2701 3918 ?    ?   ?   A . n 
A 1 2702 LYS 2702 3919 ?    ?   ?   A . n 
A 1 2703 ILE 2703 3920 3920 ILE ILE A . n 
A 1 2704 SER 2704 3921 3921 SER SER A . n 
A 1 2705 GLY 2705 3922 3922 GLY GLY A . n 
A 1 2706 VAL 2706 3923 3923 VAL VAL A . n 
A 1 2707 TRP 2707 3924 3924 TRP TRP A . n 
A 1 2708 SER 2708 3925 3925 SER SER A . n 
A 1 2709 VAL 2709 3926 3926 VAL VAL A . n 
A 1 2710 TYR 2710 3927 3927 TYR TYR A . n 
A 1 2711 CYS 2711 3928 3928 CYS CYS A . n 
A 1 2712 THR 2712 3929 3929 THR THR A . n 
A 1 2713 PHE 2713 3930 3930 PHE PHE A . n 
A 1 2714 LEU 2714 3931 3931 LEU LEU A . n 
A 1 2715 LEU 2715 3932 3932 LEU LEU A . n 
A 1 2716 SER 2716 3933 3933 SER SER A . n 
A 1 2717 TRP 2717 3934 3934 TRP TRP A . n 
A 1 2718 PHE 2718 3935 3935 PHE PHE A . n 
A 1 2719 HIS 2719 3936 3936 HIS HIS A . n 
A 1 2720 ALA 2720 3937 3937 ALA ALA A . n 
A 1 2721 LEU 2721 3938 3938 LEU LEU A . n 
A 1 2722 ILE 2722 3939 3939 ILE ILE A . n 
A 1 2723 THR 2723 3940 3940 THR THR A . n 
A 1 2724 ALA 2724 3941 3941 ALA ALA A . n 
A 1 2725 ARG 2725 3942 3942 ARG ARG A . n 
A 1 2726 THR 2726 3943 3943 THR THR A . n 
A 1 2727 ARG 2727 3944 3944 ARG ARG A . n 
A 1 2728 LEU 2728 3945 3945 LEU LEU A . n 
A 1 2729 VAL 2729 3946 3946 VAL VAL A . n 
A 1 2730 PRO 2730 3947 3947 PRO PRO A . n 
A 1 2731 HIS 2731 3948 3948 HIS HIS A . n 
A 1 2732 GLY 2732 3949 3949 GLY GLY A . n 
A 1 2733 PHE 2733 3950 3950 PHE PHE A . n 
A 1 2734 SER 2734 3951 3951 SER SER A . n 
A 1 2735 LYS 2735 3952 3952 LYS LYS A . n 
A 1 2736 LYS 2736 3953 3953 LYS LYS A . n 
A 1 2737 TYR 2737 3954 3954 TYR TYR A . n 
A 1 2738 TYR 2738 3955 3955 TYR TYR A . n 
A 1 2739 PHE 2739 3956 3956 PHE PHE A . n 
A 1 2740 ASN 2740 3957 3957 ASN ASN A . n 
A 1 2741 ASP 2741 3958 3958 ASP ASP A . n 
A 1 2742 CYS 2742 3959 3959 CYS CYS A . n 
A 1 2743 ASP 2743 3960 3960 ASP ASP A . n 
A 1 2744 PHE 2744 3961 3961 PHE PHE A . n 
A 1 2745 GLN 2745 3962 3962 GLN GLN A . n 
A 1 2746 PHE 2746 3963 3963 PHE PHE A . n 
A 1 2747 ALA 2747 3964 3964 ALA ALA A . n 
A 1 2748 SER 2748 3965 3965 SER SER A . n 
A 1 2749 VAL 2749 3966 3966 VAL VAL A . n 
A 1 2750 TYR 2750 3967 3967 TYR TYR A . n 
A 1 2751 LEU 2751 3968 3968 LEU LEU A . n 
A 1 2752 GLU 2752 3969 3969 GLU GLU A . n 
A 1 2753 ASN 2753 3970 3970 ASN ASN A . n 
A 1 2754 VAL 2754 3971 3971 VAL VAL A . n 
A 1 2755 LEU 2755 3972 3972 LEU LEU A . n 
A 1 2756 ALA 2756 3973 3973 ALA ALA A . n 
A 1 2757 THR 2757 3974 3974 THR THR A . n 
A 1 2758 ASN 2758 3975 3975 ASN ASN A . n 
A 1 2759 SER 2759 3976 3976 SER SER A . n 
A 1 2760 THR 2760 3977 3977 THR THR A . n 
A 1 2761 ASN 2761 3978 3978 ASN ASN A . n 
A 1 2762 ASN 2762 3979 3979 ASN ASN A . n 
A 1 2763 ILE 2763 3980 3980 ILE ILE A . n 
A 1 2764 PRO 2764 3981 3981 PRO PRO A . n 
A 1 2765 TRP 2765 3982 3982 TRP TRP A . n 
A 1 2766 ALA 2766 3983 3983 ALA ALA A . n 
A 1 2767 GLN 2767 3984 3984 GLN GLN A . n 
A 1 2768 VAL 2768 3985 3985 VAL VAL A . n 
A 1 2769 ARG 2769 3986 3986 ARG ARG A . n 
A 1 2770 ASP 2770 3987 3987 ASP ASP A . n 
A 1 2771 HIS 2771 3988 3988 HIS HIS A . n 
A 1 2772 ILE 2772 3989 3989 ILE ILE A . n 
A 1 2773 ALA 2773 3990 3990 ALA ALA A . n 
A 1 2774 THR 2774 3991 3991 THR THR A . n 
A 1 2775 ILE 2775 3992 3992 ILE ILE A . n 
A 1 2776 VAL 2776 3993 3993 VAL VAL A . n 
A 1 2777 TYR 2777 3994 3994 TYR TYR A . n 
A 1 2778 GLY 2778 3995 3995 GLY GLY A . n 
A 1 2779 GLY 2779 3996 3996 GLY GLY A . n 
A 1 2780 LYS 2780 3997 3997 LYS LYS A . n 
A 1 2781 ILE 2781 3998 3998 ILE ILE A . n 
A 1 2782 ASP 2782 3999 3999 ASP ASP A . n 
A 1 2783 GLU 2783 4000 4000 GLU GLU A . n 
A 1 2784 GLU 2784 4001 4001 GLU GLU A . n 
A 1 2785 LYS 2785 4002 4002 LYS LYS A . n 
A 1 2786 ASP 2786 4003 4003 ASP ASP A . n 
A 1 2787 LEU 2787 4004 4004 LEU LEU A . n 
A 1 2788 GLU 2788 4005 4005 GLU GLU A . n 
A 1 2789 VAL 2789 4006 4006 VAL VAL A . n 
A 1 2790 VAL 2790 4007 4007 VAL VAL A . n 
A 1 2791 ALA 2791 4008 4008 ALA ALA A . n 
A 1 2792 LYS 2792 4009 4009 LYS LYS A . n 
A 1 2793 LEU 2793 4010 4010 LEU LEU A . n 
A 1 2794 CYS 2794 4011 4011 CYS CYS A . n 
A 1 2795 ALA 2795 4012 4012 ALA ALA A . n 
A 1 2796 HIS 2796 4013 4013 HIS HIS A . n 
A 1 2797 VAL 2797 4014 4014 VAL VAL A . n 
A 1 2798 PHE 2798 4015 4015 PHE PHE A . n 
A 1 2799 CYS 2799 4016 4016 CYS CYS A . n 
A 1 2800 GLY 2800 4017 4017 GLY GLY A . n 
A 1 2801 SER 2801 4018 4018 SER SER A . n 
A 1 2802 ASP 2802 4019 4019 ASP ASP A . n 
A 1 2803 ASN 2803 4020 4020 ASN ASN A . n 
A 1 2804 LEU 2804 4021 4021 LEU LEU A . n 
A 1 2805 GLN 2805 4022 4022 GLN GLN A . n 
A 1 2806 ILE 2806 4023 4023 ILE ILE A . n 
A 1 2807 VAL 2807 4024 4024 VAL VAL A . n 
A 1 2808 PRO 2808 4025 4025 PRO PRO A . n 
A 1 2809 GLY 2809 4026 4026 GLY GLY A . n 
A 1 2810 VAL 2810 4027 4027 VAL VAL A . n 
A 1 2811 ARG 2811 4028 4028 ARG ARG A . n 
A 1 2812 ILE 2812 4029 4029 ILE ILE A . n 
A 1 2813 PRO 2813 4030 4030 PRO PRO A . n 
A 1 2814 GLN 2814 4031 4031 GLN GLN A . n 
A 1 2815 PRO 2815 4032 4032 PRO PRO A . n 
A 1 2816 LEU 2816 4033 4033 LEU LEU A . n 
A 1 2817 LEU 2817 4034 4034 LEU LEU A . n 
A 1 2818 GLN 2818 4035 4035 GLN GLN A . n 
A 1 2819 GLN 2819 4036 4036 GLN GLN A . n 
A 1 2820 SER 2820 4037 4037 SER SER A . n 
A 1 2821 GLU 2821 4038 4038 GLU GLU A . n 
A 1 2822 GLU 2822 4039 4039 GLU GLU A . n 
A 1 2823 GLU 2823 4040 4040 GLU GLU A . n 
A 1 2824 GLU 2824 4041 4041 GLU GLU A . n 
A 1 2825 ARG 2825 4042 4042 ARG ARG A . n 
A 1 2826 ALA 2826 4043 4043 ALA ALA A . n 
A 1 2827 ARG 2827 4044 4044 ARG ARG A . n 
A 1 2828 LEU 2828 4045 4045 LEU LEU A . n 
A 1 2829 THR 2829 4046 4046 THR THR A . n 
A 1 2830 ALA 2830 4047 4047 ALA ALA A . n 
A 1 2831 ILE 2831 4048 4048 ILE ILE A . n 
A 1 2832 LEU 2832 4049 4049 LEU LEU A . n 
A 1 2833 SER 2833 4050 4050 SER SER A . n 
A 1 2834 ASN 2834 4051 4051 ASN ASN A . n 
A 1 2835 THR 2835 4052 4052 THR THR A . n 
A 1 2836 ILE 2836 4053 4053 ILE ILE A . n 
A 1 2837 GLU 2837 4054 4054 GLU GLU A . n 
A 1 2838 PRO 2838 4055 4055 PRO PRO A . n 
A 1 2839 ALA 2839 4056 4056 ALA ALA A . n 
A 1 2840 ASP 2840 4057 4057 ASP ASP A . n 
A 1 2841 SER 2841 4058 4058 SER SER A . n 
A 1 2842 LEU 2842 4059 4059 LEU LEU A . n 
A 1 2843 SER 2843 4060 4060 SER SER A . n 
A 1 2844 SER 2844 4061 4061 SER SER A . n 
A 1 2845 TRP 2845 4062 4062 TRP TRP A . n 
A 1 2846 LEU 2846 4063 4063 LEU LEU A . n 
A 1 2847 GLN 2847 4064 4064 GLN GLN A . n 
A 1 2848 LEU 2848 4065 4065 LEU LEU A . n 
A 1 2849 PRO 2849 4066 4066 PRO PRO A . n 
A 1 2850 ARG 2850 4067 4067 ARG ARG A . n 
A 1 2851 GLU 2851 4068 4068 GLU GLU A . n 
A 1 2852 SER 2852 4069 4069 SER SER A . n 
A 1 2853 ILE 2853 4070 4070 ILE ILE A . n 
A 1 2854 LEU 2854 4071 4071 LEU LEU A . n 
A 1 2855 ASP 2855 4072 4072 ASP ASP A . n 
A 1 2856 TYR 2856 4073 4073 TYR TYR A . n 
A 1 2857 GLU 2857 4074 4074 GLU GLU A . n 
A 1 2858 ARG 2858 4075 4075 ARG ARG A . n 
A 1 2859 LEU 2859 4076 4076 LEU LEU A . n 
A 1 2860 GLN 2860 4077 4077 GLN GLN A . n 
A 1 2861 ALA 2861 4078 4078 ALA ALA A . n 
A 1 2862 LYS 2862 4079 4079 LYS LYS A . n 
A 1 2863 GLU 2863 4080 4080 GLU GLU A . n 
A 1 2864 VAL 2864 4081 4081 VAL VAL A . n 
A 1 2865 ALA 2865 4082 4082 ALA ALA A . n 
A 1 2866 SER 2866 4083 4083 SER SER A . n 
A 1 2867 SER 2867 4084 4084 SER SER A . n 
A 1 2868 THR 2868 4085 4085 THR THR A . n 
A 1 2869 GLU 2869 4086 4086 GLU GLU A . n 
A 1 2870 GLN 2870 4087 4087 GLN GLN A . n 
A 1 2871 LEU 2871 4088 4088 LEU LEU A . n 
A 1 2872 LEU 2872 4089 4089 LEU LEU A . n 
A 1 2873 GLN 2873 4090 4090 GLN GLN A . n 
A 1 2874 GLU 2874 4091 4091 GLU GLU A . n 
A 1 2875 MET 2875 4092 ?    ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ATP 1 4101 4101 ATP ATP A . 
C 3 ADP 1 4102 4102 ADP ADP A . 
D 3 ADP 1 4103 4104 ADP ADP A . 
E 3 ADP 1 4104 4107 ADP ADP A . 
F 4 MG  1 4105 1    MG  MG  A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A SER 1370 ? OG  ? A SER 153  OG  
2   1 Y 1 A LEU 1371 ? CG  ? A LEU 154  CG  
3   1 Y 1 A LEU 1371 ? CD1 ? A LEU 154  CD1 
4   1 Y 1 A LEU 1371 ? CD2 ? A LEU 154  CD2 
5   1 Y 1 A ASN 1372 ? CG  ? A ASN 155  CG  
6   1 Y 1 A ASN 1372 ? OD1 ? A ASN 155  OD1 
7   1 Y 1 A ASN 1372 ? ND2 ? A ASN 155  ND2 
8   1 Y 1 A ARG 1373 ? CG  ? A ARG 156  CG  
9   1 Y 1 A ARG 1373 ? CD  ? A ARG 156  CD  
10  1 Y 1 A ARG 1373 ? NE  ? A ARG 156  NE  
11  1 Y 1 A ARG 1373 ? CZ  ? A ARG 156  CZ  
12  1 Y 1 A ARG 1373 ? NH1 ? A ARG 156  NH1 
13  1 Y 1 A ARG 1373 ? NH2 ? A ARG 156  NH2 
14  1 Y 1 A ILE 1374 ? CG1 ? A ILE 157  CG1 
15  1 Y 1 A ILE 1374 ? CG2 ? A ILE 157  CG2 
16  1 Y 1 A ILE 1374 ? CD1 ? A ILE 157  CD1 
17  1 Y 1 A LYS 1375 ? CG  ? A LYS 158  CG  
18  1 Y 1 A LYS 1375 ? CD  ? A LYS 158  CD  
19  1 Y 1 A LYS 1375 ? CE  ? A LYS 158  CE  
20  1 Y 1 A LYS 1375 ? NZ  ? A LYS 158  NZ  
21  1 Y 1 A LYS 1376 ? CG  ? A LYS 159  CG  
22  1 Y 1 A LYS 1376 ? CD  ? A LYS 159  CD  
23  1 Y 1 A LYS 1376 ? CE  ? A LYS 159  CE  
24  1 Y 1 A LYS 1376 ? NZ  ? A LYS 159  NZ  
25  1 Y 1 A PHE 1377 ? CG  ? A PHE 160  CG  
26  1 Y 1 A PHE 1377 ? CD1 ? A PHE 160  CD1 
27  1 Y 1 A PHE 1377 ? CD2 ? A PHE 160  CD2 
28  1 Y 1 A PHE 1377 ? CE1 ? A PHE 160  CE1 
29  1 Y 1 A PHE 1377 ? CE2 ? A PHE 160  CE2 
30  1 Y 1 A PHE 1377 ? CZ  ? A PHE 160  CZ  
31  1 Y 1 A GLU 1380 ? CG  ? A GLU 163  CG  
32  1 Y 1 A GLU 1380 ? CD  ? A GLU 163  CD  
33  1 Y 1 A GLU 1380 ? OE1 ? A GLU 163  OE1 
34  1 Y 1 A GLU 1380 ? OE2 ? A GLU 163  OE2 
35  1 Y 1 A GLN 1382 ? CG  ? A GLN 165  CG  
36  1 Y 1 A GLN 1382 ? CD  ? A GLN 165  CD  
37  1 Y 1 A GLN 1382 ? OE1 ? A GLN 165  OE1 
38  1 Y 1 A GLN 1382 ? NE2 ? A GLN 165  NE2 
39  1 Y 1 A GLU 1384 ? CG  ? A GLU 167  CG  
40  1 Y 1 A GLU 1384 ? CD  ? A GLU 167  CD  
41  1 Y 1 A GLU 1384 ? OE1 ? A GLU 167  OE1 
42  1 Y 1 A GLU 1384 ? OE2 ? A GLU 167  OE2 
43  1 Y 1 A VAL 1385 ? CG1 ? A VAL 168  CG1 
44  1 Y 1 A VAL 1385 ? CG2 ? A VAL 168  CG2 
45  1 Y 1 A ILE 1386 ? CG1 ? A ILE 169  CG1 
46  1 Y 1 A ILE 1386 ? CG2 ? A ILE 169  CG2 
47  1 Y 1 A ILE 1386 ? CD1 ? A ILE 169  CD1 
48  1 Y 1 A HIS 1388 ? CG  ? A HIS 171  CG  
49  1 Y 1 A HIS 1388 ? ND1 ? A HIS 171  ND1 
50  1 Y 1 A HIS 1388 ? CD2 ? A HIS 171  CD2 
51  1 Y 1 A HIS 1388 ? CE1 ? A HIS 171  CE1 
52  1 Y 1 A HIS 1388 ? NE2 ? A HIS 171  NE2 
53  1 Y 1 A SER 1389 ? OG  ? A SER 172  OG  
54  1 Y 1 A ARG 1396 ? CG  ? A ARG 179  CG  
55  1 Y 1 A ARG 1396 ? CD  ? A ARG 179  CD  
56  1 Y 1 A ARG 1396 ? NE  ? A ARG 179  NE  
57  1 Y 1 A ARG 1396 ? CZ  ? A ARG 179  CZ  
58  1 Y 1 A ARG 1396 ? NH1 ? A ARG 179  NH1 
59  1 Y 1 A ARG 1396 ? NH2 ? A ARG 179  NH2 
60  1 Y 1 A GLU 1397 ? CG  ? A GLU 180  CG  
61  1 Y 1 A GLU 1397 ? CD  ? A GLU 180  CD  
62  1 Y 1 A GLU 1397 ? OE1 ? A GLU 180  OE1 
63  1 Y 1 A GLU 1397 ? OE2 ? A GLU 180  OE2 
64  1 Y 1 A ASP 1399 ? CG  ? A ASP 182  CG  
65  1 Y 1 A ASP 1399 ? OD1 ? A ASP 182  OD1 
66  1 Y 1 A ASP 1399 ? OD2 ? A ASP 182  OD2 
67  1 Y 1 A VAL 1400 ? CG1 ? A VAL 183  CG1 
68  1 Y 1 A VAL 1400 ? CG2 ? A VAL 183  CG2 
69  1 Y 1 A LEU 1401 ? CG  ? A LEU 184  CG  
70  1 Y 1 A LEU 1401 ? CD1 ? A LEU 184  CD1 
71  1 Y 1 A LEU 1401 ? CD2 ? A LEU 184  CD2 
72  1 Y 1 A GLN 1403 ? CG  ? A GLN 186  CG  
73  1 Y 1 A GLN 1403 ? CD  ? A GLN 186  CD  
74  1 Y 1 A GLN 1403 ? OE1 ? A GLN 186  OE1 
75  1 Y 1 A GLN 1403 ? NE2 ? A GLN 186  NE2 
76  1 Y 1 A CYS 1405 ? SG  ? A CYS 188  SG  
77  1 Y 1 A LYS 1406 ? CG  ? A LYS 189  CG  
78  1 Y 1 A LYS 1406 ? CD  ? A LYS 189  CD  
79  1 Y 1 A LYS 1406 ? CE  ? A LYS 189  CE  
80  1 Y 1 A LYS 1406 ? NZ  ? A LYS 189  NZ  
81  1 Y 1 A GLU 1425 ? CG  ? A GLU 208  CG  
82  1 Y 1 A GLU 1425 ? CD  ? A GLU 208  CD  
83  1 Y 1 A GLU 1425 ? OE1 ? A GLU 208  OE1 
84  1 Y 1 A GLU 1425 ? OE2 ? A GLU 208  OE2 
85  1 Y 1 A GLN 1426 ? CG  ? A GLN 209  CG  
86  1 Y 1 A GLN 1426 ? CD  ? A GLN 209  CD  
87  1 Y 1 A GLN 1426 ? OE1 ? A GLN 209  OE1 
88  1 Y 1 A GLN 1426 ? NE2 ? A GLN 209  NE2 
89  1 Y 1 A ASP 1427 ? CG  ? A ASP 210  CG  
90  1 Y 1 A ASP 1427 ? OD1 ? A ASP 210  OD1 
91  1 Y 1 A ASP 1427 ? OD2 ? A ASP 210  OD2 
92  1 Y 1 A CYS 1428 ? SG  ? A CYS 211  SG  
93  1 Y 1 A LEU 1429 ? CG  ? A LEU 212  CG  
94  1 Y 1 A LEU 1429 ? CD1 ? A LEU 212  CD1 
95  1 Y 1 A LEU 1429 ? CD2 ? A LEU 212  CD2 
96  1 Y 1 A ASP 1430 ? CG  ? A ASP 213  CG  
97  1 Y 1 A ASP 1430 ? OD1 ? A ASP 213  OD1 
98  1 Y 1 A ASP 1430 ? OD2 ? A ASP 213  OD2 
99  1 Y 1 A LEU 1431 ? CG  ? A LEU 214  CG  
100 1 Y 1 A LEU 1431 ? CD1 ? A LEU 214  CD1 
101 1 Y 1 A LEU 1431 ? CD2 ? A LEU 214  CD2 
102 1 Y 1 A GLU 1432 ? CG  ? A GLU 215  CG  
103 1 Y 1 A GLU 1432 ? CD  ? A GLU 215  CD  
104 1 Y 1 A GLU 1432 ? OE1 ? A GLU 215  OE1 
105 1 Y 1 A GLU 1432 ? OE2 ? A GLU 215  OE2 
106 1 Y 1 A SER 1433 ? OG  ? A SER 216  OG  
107 1 Y 1 A LYS 1437 ? CG  ? A LYS 220  CG  
108 1 Y 1 A LYS 1437 ? CD  ? A LYS 220  CD  
109 1 Y 1 A LYS 1437 ? CE  ? A LYS 220  CE  
110 1 Y 1 A LYS 1437 ? NZ  ? A LYS 220  NZ  
111 1 Y 1 A GLU 1440 ? CG  ? A GLU 223  CG  
112 1 Y 1 A GLU 1440 ? CD  ? A GLU 223  CD  
113 1 Y 1 A GLU 1440 ? OE1 ? A GLU 223  OE1 
114 1 Y 1 A GLU 1440 ? OE2 ? A GLU 223  OE2 
115 1 Y 1 A PHE 1450 ? CG  ? A PHE 233  CG  
116 1 Y 1 A PHE 1450 ? CD1 ? A PHE 233  CD1 
117 1 Y 1 A PHE 1450 ? CD2 ? A PHE 233  CD2 
118 1 Y 1 A PHE 1450 ? CE1 ? A PHE 233  CE1 
119 1 Y 1 A PHE 1450 ? CE2 ? A PHE 233  CE2 
120 1 Y 1 A PHE 1450 ? CZ  ? A PHE 233  CZ  
121 1 Y 1 A LEU 1453 ? CG  ? A LEU 236  CG  
122 1 Y 1 A LEU 1453 ? CD1 ? A LEU 236  CD1 
123 1 Y 1 A LEU 1453 ? CD2 ? A LEU 236  CD2 
124 1 Y 1 A GLU 1461 ? CG  ? A GLU 244  CG  
125 1 Y 1 A GLU 1461 ? CD  ? A GLU 244  CD  
126 1 Y 1 A GLU 1461 ? OE1 ? A GLU 244  OE1 
127 1 Y 1 A GLU 1461 ? OE2 ? A GLU 244  OE2 
128 1 Y 1 A LEU 1469 ? CG  ? A LEU 252  CG  
129 1 Y 1 A LEU 1469 ? CD1 ? A LEU 252  CD1 
130 1 Y 1 A LEU 1469 ? CD2 ? A LEU 252  CD2 
131 1 Y 1 A PRO 1470 ? CG  ? A PRO 253  CG  
132 1 Y 1 A PRO 1470 ? CD  ? A PRO 253  CD  
133 1 Y 1 A LEU 1471 ? CG  ? A LEU 254  CG  
134 1 Y 1 A LEU 1471 ? CD1 ? A LEU 254  CD1 
135 1 Y 1 A LEU 1471 ? CD2 ? A LEU 254  CD2 
136 1 Y 1 A LYS 1477 ? CG  ? A LYS 260  CG  
137 1 Y 1 A LYS 1477 ? CD  ? A LYS 260  CD  
138 1 Y 1 A LYS 1477 ? CE  ? A LYS 260  CE  
139 1 Y 1 A LYS 1477 ? NZ  ? A LYS 260  NZ  
140 1 Y 1 A GLU 1482 ? CG  ? A GLU 265  CG  
141 1 Y 1 A GLU 1482 ? CD  ? A GLU 265  CD  
142 1 Y 1 A GLU 1482 ? OE1 ? A GLU 265  OE1 
143 1 Y 1 A GLU 1482 ? OE2 ? A GLU 265  OE2 
144 1 Y 1 A LYS 1484 ? CG  ? A LYS 267  CG  
145 1 Y 1 A LYS 1484 ? CD  ? A LYS 267  CD  
146 1 Y 1 A LYS 1484 ? CE  ? A LYS 267  CE  
147 1 Y 1 A LYS 1484 ? NZ  ? A LYS 267  NZ  
148 1 Y 1 A THR 1507 ? OG1 ? A THR 290  OG1 
149 1 Y 1 A THR 1507 ? CG2 ? A THR 290  CG2 
150 1 Y 1 A LYS 1510 ? CG  ? A LYS 293  CG  
151 1 Y 1 A LYS 1510 ? CD  ? A LYS 293  CD  
152 1 Y 1 A LYS 1510 ? CE  ? A LYS 293  CE  
153 1 Y 1 A LYS 1510 ? NZ  ? A LYS 293  NZ  
154 1 Y 1 A LEU 1511 ? CG  ? A LEU 294  CG  
155 1 Y 1 A LEU 1511 ? CD1 ? A LEU 294  CD1 
156 1 Y 1 A LEU 1511 ? CD2 ? A LEU 294  CD2 
157 1 Y 1 A ASP 1514 ? CG  ? A ASP 297  CG  
158 1 Y 1 A ASP 1514 ? OD1 ? A ASP 297  OD1 
159 1 Y 1 A ASP 1514 ? OD2 ? A ASP 297  OD2 
160 1 Y 1 A SER 1515 ? OG  ? A SER 298  OG  
161 1 Y 1 A LYS 1517 ? CG  ? A LYS 300  CG  
162 1 Y 1 A LYS 1517 ? CD  ? A LYS 300  CD  
163 1 Y 1 A LYS 1517 ? CE  ? A LYS 300  CE  
164 1 Y 1 A LYS 1517 ? NZ  ? A LYS 300  NZ  
165 1 Y 1 A MET 1518 ? CG  ? A MET 301  CG  
166 1 Y 1 A MET 1518 ? SD  ? A MET 301  SD  
167 1 Y 1 A MET 1518 ? CE  ? A MET 301  CE  
168 1 Y 1 A ARG 1529 ? CG  ? A ARG 312  CG  
169 1 Y 1 A ARG 1529 ? CD  ? A ARG 312  CD  
170 1 Y 1 A ARG 1529 ? NE  ? A ARG 312  NE  
171 1 Y 1 A ARG 1529 ? CZ  ? A ARG 312  CZ  
172 1 Y 1 A ARG 1529 ? NH1 ? A ARG 312  NH1 
173 1 Y 1 A ARG 1529 ? NH2 ? A ARG 312  NH2 
174 1 Y 1 A LYS 1553 ? CG  ? A LYS 336  CG  
175 1 Y 1 A LYS 1553 ? CD  ? A LYS 336  CD  
176 1 Y 1 A LYS 1553 ? CE  ? A LYS 336  CE  
177 1 Y 1 A LYS 1553 ? NZ  ? A LYS 336  NZ  
178 1 Y 1 A ASP 1824 ? CG  ? A ASP 607  CG  
179 1 Y 1 A ASP 1824 ? OD1 ? A ASP 607  OD1 
180 1 Y 1 A ASP 1824 ? OD2 ? A ASP 607  OD2 
181 1 Y 1 A ILE 1838 ? CG1 ? A ILE 621  CG1 
182 1 Y 1 A ILE 1838 ? CG2 ? A ILE 621  CG2 
183 1 Y 1 A ILE 1838 ? CD1 ? A ILE 621  CD1 
184 1 Y 1 A ASP 1854 ? CG  ? A ASP 637  CG  
185 1 Y 1 A ASP 1854 ? OD1 ? A ASP 637  OD1 
186 1 Y 1 A ASP 1854 ? OD2 ? A ASP 637  OD2 
187 1 Y 1 A GLU 1855 ? CG  ? A GLU 638  CG  
188 1 Y 1 A GLU 1855 ? CD  ? A GLU 638  CD  
189 1 Y 1 A GLU 1855 ? OE1 ? A GLU 638  OE1 
190 1 Y 1 A GLU 1855 ? OE2 ? A GLU 638  OE2 
191 1 Y 1 A SER 1859 ? OG  ? A SER 642  OG  
192 1 Y 1 A GLU 1883 ? CG  ? A GLU 666  CG  
193 1 Y 1 A GLU 1883 ? CD  ? A GLU 666  CD  
194 1 Y 1 A GLU 1883 ? OE1 ? A GLU 666  OE1 
195 1 Y 1 A GLU 1883 ? OE2 ? A GLU 666  OE2 
196 1 Y 1 A LYS 1922 ? CG  ? A LYS 705  CG  
197 1 Y 1 A LYS 1922 ? CD  ? A LYS 705  CD  
198 1 Y 1 A LYS 1922 ? CE  ? A LYS 705  CE  
199 1 Y 1 A LYS 1922 ? NZ  ? A LYS 705  NZ  
200 1 Y 1 A SER 1962 ? OG  ? A SER 745  OG  
201 1 Y 1 A GLU 2112 ? CG  ? A GLU 895  CG  
202 1 Y 1 A GLU 2112 ? CD  ? A GLU 895  CD  
203 1 Y 1 A GLU 2112 ? OE1 ? A GLU 895  OE1 
204 1 Y 1 A GLU 2112 ? OE2 ? A GLU 895  OE2 
205 1 Y 1 A LYS 2120 ? CG  ? A LYS 903  CG  
206 1 Y 1 A LYS 2120 ? CD  ? A LYS 903  CD  
207 1 Y 1 A LYS 2120 ? CE  ? A LYS 903  CE  
208 1 Y 1 A LYS 2120 ? NZ  ? A LYS 903  NZ  
209 1 Y 1 A ASP 2448 ? CG  ? A ASP 1231 CG  
210 1 Y 1 A ASP 2448 ? OD1 ? A ASP 1231 OD1 
211 1 Y 1 A ASP 2448 ? OD2 ? A ASP 1231 OD2 
212 1 Y 1 A LYS 2496 ? CG  ? A LYS 1279 CG  
213 1 Y 1 A LYS 2496 ? CD  ? A LYS 1279 CD  
214 1 Y 1 A LYS 2496 ? CE  ? A LYS 1279 CE  
215 1 Y 1 A LYS 2496 ? NZ  ? A LYS 1279 NZ  
216 1 Y 1 A PRO 2541 ? CG  ? A PRO 1324 CG  
217 1 Y 1 A PRO 2541 ? CD  ? A PRO 1324 CD  
218 1 Y 1 A LEU 2700 ? CG  ? A LEU 1483 CG  
219 1 Y 1 A LEU 2700 ? CD1 ? A LEU 1483 CD1 
220 1 Y 1 A LEU 2700 ? CD2 ? A LEU 1483 CD2 
221 1 Y 1 A LEU 2702 ? CG  ? A LEU 1485 CG  
222 1 Y 1 A LEU 2702 ? CD1 ? A LEU 1485 CD1 
223 1 Y 1 A LEU 2702 ? CD2 ? A LEU 1485 CD2 
224 1 Y 1 A GLU 2718 ? CG  ? A GLU 1501 CG  
225 1 Y 1 A GLU 2718 ? CD  ? A GLU 1501 CD  
226 1 Y 1 A GLU 2718 ? OE1 ? A GLU 1501 OE1 
227 1 Y 1 A GLU 2718 ? OE2 ? A GLU 1501 OE2 
228 1 Y 1 A ASP 2725 ? CG  ? A ASP 1508 CG  
229 1 Y 1 A ASP 2725 ? OD1 ? A ASP 1508 OD1 
230 1 Y 1 A ASP 2725 ? OD2 ? A ASP 1508 OD2 
231 1 Y 1 A LEU 2769 ? CG  ? A LEU 1552 CG  
232 1 Y 1 A LEU 2769 ? CD1 ? A LEU 1552 CD1 
233 1 Y 1 A LEU 2769 ? CD2 ? A LEU 1552 CD2 
234 1 Y 1 A ARG 2788 ? CG  ? A ARG 1571 CG  
235 1 Y 1 A ARG 2788 ? CD  ? A ARG 1571 CD  
236 1 Y 1 A ARG 2788 ? NE  ? A ARG 1571 NE  
237 1 Y 1 A ARG 2788 ? CZ  ? A ARG 1571 CZ  
238 1 Y 1 A ARG 2788 ? NH1 ? A ARG 1571 NH1 
239 1 Y 1 A ARG 2788 ? NH2 ? A ARG 1571 NH2 
240 1 Y 1 A HIS 2789 ? CG  ? A HIS 1572 CG  
241 1 Y 1 A HIS 2789 ? ND1 ? A HIS 1572 ND1 
242 1 Y 1 A HIS 2789 ? CD2 ? A HIS 1572 CD2 
243 1 Y 1 A HIS 2789 ? CE1 ? A HIS 1572 CE1 
244 1 Y 1 A HIS 2789 ? NE2 ? A HIS 1572 NE2 
245 1 Y 1 A ASP 2794 ? CG  ? A ASP 1577 CG  
246 1 Y 1 A ASP 2794 ? OD1 ? A ASP 1577 OD1 
247 1 Y 1 A ASP 2794 ? OD2 ? A ASP 1577 OD2 
248 1 Y 1 A MET 2797 ? CG  ? A MET 1580 CG  
249 1 Y 1 A MET 2797 ? SD  ? A MET 1580 SD  
250 1 Y 1 A MET 2797 ? CE  ? A MET 1580 CE  
251 1 Y 1 A LYS 2801 ? CG  ? A LYS 1584 CG  
252 1 Y 1 A LYS 2801 ? CD  ? A LYS 1584 CD  
253 1 Y 1 A LYS 2801 ? CE  ? A LYS 1584 CE  
254 1 Y 1 A LYS 2801 ? NZ  ? A LYS 1584 NZ  
255 1 Y 1 A ASP 2805 ? CG  ? A ASP 1588 CG  
256 1 Y 1 A ASP 2805 ? OD1 ? A ASP 1588 OD1 
257 1 Y 1 A ASP 2805 ? OD2 ? A ASP 1588 OD2 
258 1 Y 1 A LEU 2808 ? CG  ? A LEU 1591 CG  
259 1 Y 1 A LEU 2808 ? CD1 ? A LEU 1591 CD1 
260 1 Y 1 A LEU 2808 ? CD2 ? A LEU 1591 CD2 
261 1 Y 1 A LYS 2809 ? CG  ? A LYS 1592 CG  
262 1 Y 1 A LYS 2809 ? CD  ? A LYS 1592 CD  
263 1 Y 1 A LYS 2809 ? CE  ? A LYS 1592 CE  
264 1 Y 1 A LYS 2809 ? NZ  ? A LYS 1592 NZ  
265 1 Y 1 A GLU 2810 ? CG  ? A GLU 1593 CG  
266 1 Y 1 A GLU 2810 ? CD  ? A GLU 1593 CD  
267 1 Y 1 A GLU 2810 ? OE1 ? A GLU 1593 OE1 
268 1 Y 1 A GLU 2810 ? OE2 ? A GLU 1593 OE2 
269 1 Y 1 A GLU 2824 ? CG  ? A GLU 1607 CG  
270 1 Y 1 A GLU 2824 ? CD  ? A GLU 1607 CD  
271 1 Y 1 A GLU 2824 ? OE1 ? A GLU 1607 OE1 
272 1 Y 1 A GLU 2824 ? OE2 ? A GLU 1607 OE2 
273 1 Y 1 A GLU 2829 ? CG  ? A GLU 1612 CG  
274 1 Y 1 A GLU 2829 ? CD  ? A GLU 1612 CD  
275 1 Y 1 A GLU 2829 ? OE1 ? A GLU 1612 OE1 
276 1 Y 1 A GLU 2829 ? OE2 ? A GLU 1612 OE2 
277 1 Y 1 A GLU 2848 ? CG  ? A GLU 1631 CG  
278 1 Y 1 A GLU 2848 ? CD  ? A GLU 1631 CD  
279 1 Y 1 A GLU 2848 ? OE1 ? A GLU 1631 OE1 
280 1 Y 1 A GLU 2848 ? OE2 ? A GLU 1631 OE2 
281 1 Y 1 A ASP 2850 ? CG  ? A ASP 1633 CG  
282 1 Y 1 A ASP 2850 ? OD1 ? A ASP 1633 OD1 
283 1 Y 1 A ASP 2850 ? OD2 ? A ASP 1633 OD2 
284 1 Y 1 A LEU 2852 ? CG  ? A LEU 1635 CG  
285 1 Y 1 A LEU 2852 ? CD1 ? A LEU 1635 CD1 
286 1 Y 1 A LEU 2852 ? CD2 ? A LEU 1635 CD2 
287 1 Y 1 A ASN 2854 ? CG  ? A ASN 1637 CG  
288 1 Y 1 A ASN 2854 ? OD1 ? A ASN 1637 OD1 
289 1 Y 1 A ASN 2854 ? ND2 ? A ASN 1637 ND2 
290 1 Y 1 A LYS 2859 ? CG  ? A LYS 1642 CG  
291 1 Y 1 A LYS 2859 ? CD  ? A LYS 1642 CD  
292 1 Y 1 A LYS 2859 ? CE  ? A LYS 1642 CE  
293 1 Y 1 A LYS 2859 ? NZ  ? A LYS 1642 NZ  
294 1 Y 1 A THR 2869 ? OG1 ? A THR 1652 OG1 
295 1 Y 1 A THR 2869 ? CG2 ? A THR 1652 CG2 
296 1 Y 1 A GLU 2872 ? CG  ? A GLU 1655 CG  
297 1 Y 1 A GLU 2872 ? CD  ? A GLU 1655 CD  
298 1 Y 1 A GLU 2872 ? OE1 ? A GLU 1655 OE1 
299 1 Y 1 A GLU 2872 ? OE2 ? A GLU 1655 OE2 
300 1 Y 1 A SER 2900 ? OG  ? A SER 1683 OG  
301 1 Y 1 A MET 2902 ? CG  ? A MET 1685 CG  
302 1 Y 1 A MET 2902 ? SD  ? A MET 1685 SD  
303 1 Y 1 A MET 2902 ? CE  ? A MET 1685 CE  
304 1 Y 1 A VAL 2935 ? CG1 ? A VAL 1718 CG1 
305 1 Y 1 A VAL 2935 ? CG2 ? A VAL 1718 CG2 
306 1 Y 1 A GLU 2939 ? CG  ? A GLU 1722 CG  
307 1 Y 1 A GLU 2939 ? CD  ? A GLU 1722 CD  
308 1 Y 1 A GLU 2939 ? OE1 ? A GLU 1722 OE1 
309 1 Y 1 A GLU 2939 ? OE2 ? A GLU 1722 OE2 
310 1 Y 1 A PHE 2940 ? CG  ? A PHE 1723 CG  
311 1 Y 1 A PHE 2940 ? CD1 ? A PHE 1723 CD1 
312 1 Y 1 A PHE 2940 ? CD2 ? A PHE 1723 CD2 
313 1 Y 1 A PHE 2940 ? CE1 ? A PHE 1723 CE1 
314 1 Y 1 A PHE 2940 ? CE2 ? A PHE 1723 CE2 
315 1 Y 1 A PHE 2940 ? CZ  ? A PHE 1723 CZ  
316 1 Y 1 A LYS 2979 ? CG  ? A LYS 1762 CG  
317 1 Y 1 A LYS 2979 ? CD  ? A LYS 1762 CD  
318 1 Y 1 A LYS 2979 ? CE  ? A LYS 1762 CE  
319 1 Y 1 A LYS 2979 ? NZ  ? A LYS 1762 NZ  
320 1 Y 1 A PRO 2986 ? CG  ? A PRO 1769 CG  
321 1 Y 1 A PRO 2986 ? CD  ? A PRO 1769 CD  
322 1 Y 1 A VAL 3000 ? CG1 ? A VAL 1783 CG1 
323 1 Y 1 A VAL 3000 ? CG2 ? A VAL 1783 CG2 
324 1 Y 1 A LEU 3002 ? CG  ? A LEU 1785 CG  
325 1 Y 1 A LEU 3002 ? CD1 ? A LEU 1785 CD1 
326 1 Y 1 A LEU 3002 ? CD2 ? A LEU 1785 CD2 
327 1 Y 1 A GLN 3008 ? CG  ? A GLN 1791 CG  
328 1 Y 1 A GLN 3008 ? CD  ? A GLN 1791 CD  
329 1 Y 1 A GLN 3008 ? OE1 ? A GLN 1791 OE1 
330 1 Y 1 A GLN 3008 ? NE2 ? A GLN 1791 NE2 
331 1 Y 1 A ASP 3009 ? CG  ? A ASP 1792 CG  
332 1 Y 1 A ASP 3009 ? OD1 ? A ASP 1792 OD1 
333 1 Y 1 A ASP 3009 ? OD2 ? A ASP 1792 OD2 
334 1 Y 1 A GLN 3011 ? CG  ? A GLN 1794 CG  
335 1 Y 1 A GLN 3011 ? CD  ? A GLN 1794 CD  
336 1 Y 1 A GLN 3011 ? OE1 ? A GLN 1794 OE1 
337 1 Y 1 A GLN 3011 ? NE2 ? A GLN 1794 NE2 
338 1 Y 1 A GLU 3012 ? CG  ? A GLU 1795 CG  
339 1 Y 1 A GLU 3012 ? CD  ? A GLU 1795 CD  
340 1 Y 1 A GLU 3012 ? OE1 ? A GLU 1795 OE1 
341 1 Y 1 A GLU 3012 ? OE2 ? A GLU 1795 OE2 
342 1 Y 1 A ASN 3013 ? CG  ? A ASN 1796 CG  
343 1 Y 1 A ASN 3013 ? OD1 ? A ASN 1796 OD1 
344 1 Y 1 A ASN 3013 ? ND2 ? A ASN 1796 ND2 
345 1 Y 1 A ARG 3015 ? CG  ? A ARG 1798 CG  
346 1 Y 1 A ARG 3015 ? CD  ? A ARG 1798 CD  
347 1 Y 1 A ARG 3015 ? NE  ? A ARG 1798 NE  
348 1 Y 1 A ARG 3015 ? CZ  ? A ARG 1798 CZ  
349 1 Y 1 A ARG 3015 ? NH1 ? A ARG 1798 NH1 
350 1 Y 1 A ARG 3015 ? NH2 ? A ARG 1798 NH2 
351 1 Y 1 A PHE 3016 ? CG  ? A PHE 1799 CG  
352 1 Y 1 A PHE 3016 ? CD1 ? A PHE 1799 CD1 
353 1 Y 1 A PHE 3016 ? CD2 ? A PHE 1799 CD2 
354 1 Y 1 A PHE 3016 ? CE1 ? A PHE 1799 CE1 
355 1 Y 1 A PHE 3016 ? CE2 ? A PHE 1799 CE2 
356 1 Y 1 A PHE 3016 ? CZ  ? A PHE 1799 CZ  
357 1 Y 1 A VAL 3017 ? CG1 ? A VAL 1800 CG1 
358 1 Y 1 A VAL 3017 ? CG2 ? A VAL 1800 CG2 
359 1 Y 1 A ASN 3018 ? CG  ? A ASN 1801 CG  
360 1 Y 1 A ASN 3018 ? OD1 ? A ASN 1801 OD1 
361 1 Y 1 A ASN 3018 ? ND2 ? A ASN 1801 ND2 
362 1 Y 1 A VAL 3019 ? CG1 ? A VAL 1802 CG1 
363 1 Y 1 A VAL 3019 ? CG2 ? A VAL 1802 CG2 
364 1 Y 1 A LEU 3021 ? CG  ? A LEU 1804 CG  
365 1 Y 1 A LEU 3021 ? CD1 ? A LEU 1804 CD1 
366 1 Y 1 A LEU 3021 ? CD2 ? A LEU 1804 CD2 
367 1 Y 1 A GLU 3022 ? CG  ? A GLU 1805 CG  
368 1 Y 1 A GLU 3022 ? CD  ? A GLU 1805 CD  
369 1 Y 1 A GLU 3022 ? OE1 ? A GLU 1805 OE1 
370 1 Y 1 A GLU 3022 ? OE2 ? A GLU 1805 OE2 
371 1 Y 1 A LYS 3023 ? CG  ? A LYS 1806 CG  
372 1 Y 1 A LYS 3023 ? CD  ? A LYS 1806 CD  
373 1 Y 1 A LYS 3023 ? CE  ? A LYS 1806 CE  
374 1 Y 1 A LYS 3023 ? NZ  ? A LYS 1806 NZ  
375 1 Y 1 A LEU 3024 ? CG  ? A LEU 1807 CG  
376 1 Y 1 A LEU 3024 ? CD1 ? A LEU 1807 CD1 
377 1 Y 1 A LEU 3024 ? CD2 ? A LEU 1807 CD2 
378 1 Y 1 A ASN 3025 ? CG  ? A ASN 1808 CG  
379 1 Y 1 A ASN 3025 ? OD1 ? A ASN 1808 OD1 
380 1 Y 1 A ASN 3025 ? ND2 ? A ASN 1808 ND2 
381 1 Y 1 A SER 3298 ? OG  ? A SER 2081 OG  
382 1 Y 1 A LEU 3299 ? CG  ? A LEU 2082 CG  
383 1 Y 1 A LEU 3299 ? CD1 ? A LEU 2082 CD1 
384 1 Y 1 A LEU 3299 ? CD2 ? A LEU 2082 CD2 
385 1 Y 1 A THR 3300 ? OG1 ? A THR 2083 OG1 
386 1 Y 1 A THR 3300 ? CG2 ? A THR 2083 CG2 
387 1 Y 1 A PHE 3301 ? CG  ? A PHE 2084 CG  
388 1 Y 1 A PHE 3301 ? CD1 ? A PHE 2084 CD1 
389 1 Y 1 A PHE 3301 ? CD2 ? A PHE 2084 CD2 
390 1 Y 1 A PHE 3301 ? CE1 ? A PHE 2084 CE1 
391 1 Y 1 A PHE 3301 ? CE2 ? A PHE 2084 CE2 
392 1 Y 1 A PHE 3301 ? CZ  ? A PHE 2084 CZ  
393 1 Y 1 A GLU 3302 ? CG  ? A GLU 2085 CG  
394 1 Y 1 A GLU 3302 ? CD  ? A GLU 2085 CD  
395 1 Y 1 A GLU 3302 ? OE1 ? A GLU 2085 OE1 
396 1 Y 1 A GLU 3302 ? OE2 ? A GLU 2085 OE2 
397 1 Y 1 A LYS 3303 ? CG  ? A LYS 2086 CG  
398 1 Y 1 A LYS 3303 ? CD  ? A LYS 2086 CD  
399 1 Y 1 A LYS 3303 ? CE  ? A LYS 2086 CE  
400 1 Y 1 A LYS 3303 ? NZ  ? A LYS 2086 NZ  
401 1 Y 1 A GLU 3304 ? CG  ? A GLU 2087 CG  
402 1 Y 1 A GLU 3304 ? CD  ? A GLU 2087 CD  
403 1 Y 1 A GLU 3304 ? OE1 ? A GLU 2087 OE1 
404 1 Y 1 A GLU 3304 ? OE2 ? A GLU 2087 OE2 
405 1 Y 1 A ARG 3305 ? CG  ? A ARG 2088 CG  
406 1 Y 1 A ARG 3305 ? CD  ? A ARG 2088 CD  
407 1 Y 1 A ARG 3305 ? NE  ? A ARG 2088 NE  
408 1 Y 1 A ARG 3305 ? CZ  ? A ARG 2088 CZ  
409 1 Y 1 A ARG 3305 ? NH1 ? A ARG 2088 NH1 
410 1 Y 1 A ARG 3305 ? NH2 ? A ARG 2088 NH2 
411 1 Y 1 A TRP 3306 ? CG  ? A TRP 2089 CG  
412 1 Y 1 A TRP 3306 ? CD1 ? A TRP 2089 CD1 
413 1 Y 1 A TRP 3306 ? CD2 ? A TRP 2089 CD2 
414 1 Y 1 A TRP 3306 ? NE1 ? A TRP 2089 NE1 
415 1 Y 1 A TRP 3306 ? CE2 ? A TRP 2089 CE2 
416 1 Y 1 A TRP 3306 ? CE3 ? A TRP 2089 CE3 
417 1 Y 1 A TRP 3306 ? CZ2 ? A TRP 2089 CZ2 
418 1 Y 1 A TRP 3306 ? CZ3 ? A TRP 2089 CZ3 
419 1 Y 1 A TRP 3306 ? CH2 ? A TRP 2089 CH2 
420 1 Y 1 A LEU 3307 ? CG  ? A LEU 2090 CG  
421 1 Y 1 A LEU 3307 ? CD1 ? A LEU 2090 CD1 
422 1 Y 1 A LEU 3307 ? CD2 ? A LEU 2090 CD2 
423 1 Y 1 A ASN 3308 ? CG  ? A ASN 2091 CG  
424 1 Y 1 A ASN 3308 ? OD1 ? A ASN 2091 OD1 
425 1 Y 1 A ASN 3308 ? ND2 ? A ASN 2091 ND2 
426 1 Y 1 A THR 3309 ? OG1 ? A THR 2092 OG1 
427 1 Y 1 A THR 3309 ? CG2 ? A THR 2092 CG2 
428 1 Y 1 A THR 3310 ? OG1 ? A THR 2093 OG1 
429 1 Y 1 A THR 3310 ? CG2 ? A THR 2093 CG2 
430 1 Y 1 A LYS 3311 ? CG  ? A LYS 2094 CG  
431 1 Y 1 A LYS 3311 ? CD  ? A LYS 2094 CD  
432 1 Y 1 A LYS 3311 ? CE  ? A LYS 2094 CE  
433 1 Y 1 A LYS 3311 ? NZ  ? A LYS 2094 NZ  
434 1 Y 1 A GLN 3312 ? CG  ? A GLN 2095 CG  
435 1 Y 1 A GLN 3312 ? CD  ? A GLN 2095 CD  
436 1 Y 1 A GLN 3312 ? OE1 ? A GLN 2095 OE1 
437 1 Y 1 A GLN 3312 ? NE2 ? A GLN 2095 NE2 
438 1 Y 1 A LYS 3315 ? CG  ? A LYS 2098 CG  
439 1 Y 1 A LYS 3315 ? CD  ? A LYS 2098 CD  
440 1 Y 1 A LYS 3315 ? CE  ? A LYS 2098 CE  
441 1 Y 1 A LYS 3315 ? NZ  ? A LYS 2098 NZ  
442 1 Y 1 A ARG 3340 ? CG  ? A ARG 2123 CG  
443 1 Y 1 A ARG 3340 ? CD  ? A ARG 2123 CD  
444 1 Y 1 A ARG 3340 ? NE  ? A ARG 2123 NE  
445 1 Y 1 A ARG 3340 ? CZ  ? A ARG 2123 CZ  
446 1 Y 1 A ARG 3340 ? NH1 ? A ARG 2123 NH1 
447 1 Y 1 A ARG 3340 ? NH2 ? A ARG 2123 NH2 
448 1 Y 1 A ASP 3344 ? CG  ? A ASP 2127 CG  
449 1 Y 1 A ASP 3344 ? OD1 ? A ASP 2127 OD1 
450 1 Y 1 A ASP 3344 ? OD2 ? A ASP 2127 OD2 
451 1 Y 1 A MET 3345 ? CG  ? A MET 2128 CG  
452 1 Y 1 A MET 3345 ? SD  ? A MET 2128 SD  
453 1 Y 1 A MET 3345 ? CE  ? A MET 2128 CE  
454 1 Y 1 A ILE 3348 ? CG1 ? A ILE 2131 CG1 
455 1 Y 1 A ILE 3348 ? CG2 ? A ILE 2131 CG2 
456 1 Y 1 A ILE 3348 ? CD1 ? A ILE 2131 CD1 
457 1 Y 1 A PHE 3356 ? CG  ? A PHE 2139 CG  
458 1 Y 1 A PHE 3356 ? CD1 ? A PHE 2139 CD1 
459 1 Y 1 A PHE 3356 ? CD2 ? A PHE 2139 CD2 
460 1 Y 1 A PHE 3356 ? CE1 ? A PHE 2139 CE1 
461 1 Y 1 A PHE 3356 ? CE2 ? A PHE 2139 CE2 
462 1 Y 1 A PHE 3356 ? CZ  ? A PHE 2139 CZ  
463 1 Y 1 A LYS 3359 ? CG  ? A LYS 2142 CG  
464 1 Y 1 A LYS 3359 ? CD  ? A LYS 2142 CD  
465 1 Y 1 A LYS 3359 ? CE  ? A LYS 2142 CE  
466 1 Y 1 A LYS 3359 ? NZ  ? A LYS 2142 NZ  
467 1 Y 1 A TYR 3360 ? CG  ? A TYR 2143 CG  
468 1 Y 1 A TYR 3360 ? CD1 ? A TYR 2143 CD1 
469 1 Y 1 A TYR 3360 ? CD2 ? A TYR 2143 CD2 
470 1 Y 1 A TYR 3360 ? CE1 ? A TYR 2143 CE1 
471 1 Y 1 A TYR 3360 ? CE2 ? A TYR 2143 CE2 
472 1 Y 1 A TYR 3360 ? CZ  ? A TYR 2143 CZ  
473 1 Y 1 A TYR 3360 ? OH  ? A TYR 2143 OH  
474 1 Y 1 A ASP 3361 ? CG  ? A ASP 2144 CG  
475 1 Y 1 A ASP 3361 ? OD1 ? A ASP 2144 OD1 
476 1 Y 1 A ASP 3361 ? OD2 ? A ASP 2144 OD2 
477 1 Y 1 A ASN 3363 ? CG  ? A ASN 2146 CG  
478 1 Y 1 A ASN 3363 ? OD1 ? A ASN 2146 OD1 
479 1 Y 1 A ASN 3363 ? ND2 ? A ASN 2146 ND2 
480 1 Y 1 A ASP 3368 ? CG  ? A ASP 2151 CG  
481 1 Y 1 A ASP 3368 ? OD1 ? A ASP 2151 OD1 
482 1 Y 1 A ASP 3368 ? OD2 ? A ASP 2151 OD2 
483 1 Y 1 A TYR 3369 ? CG  ? A TYR 2152 CG  
484 1 Y 1 A TYR 3369 ? CD1 ? A TYR 2152 CD1 
485 1 Y 1 A TYR 3369 ? CD2 ? A TYR 2152 CD2 
486 1 Y 1 A TYR 3369 ? CE1 ? A TYR 2152 CE1 
487 1 Y 1 A TYR 3369 ? CE2 ? A TYR 2152 CE2 
488 1 Y 1 A TYR 3369 ? CZ  ? A TYR 2152 CZ  
489 1 Y 1 A TYR 3369 ? OH  ? A TYR 2152 OH  
490 1 Y 1 A LEU 3370 ? CG  ? A LEU 2153 CG  
491 1 Y 1 A LEU 3370 ? CD1 ? A LEU 2153 CD1 
492 1 Y 1 A LEU 3370 ? CD2 ? A LEU 2153 CD2 
493 1 Y 1 A THR 3372 ? OG1 ? A THR 2155 OG1 
494 1 Y 1 A THR 3372 ? CG2 ? A THR 2155 CG2 
495 1 Y 1 A LEU 3373 ? CG  ? A LEU 2156 CG  
496 1 Y 1 A LEU 3373 ? CD1 ? A LEU 2156 CD1 
497 1 Y 1 A LEU 3373 ? CD2 ? A LEU 2156 CD2 
498 1 Y 1 A ASP 3374 ? CG  ? A ASP 2157 CG  
499 1 Y 1 A ASP 3374 ? OD1 ? A ASP 2157 OD1 
500 1 Y 1 A ASP 3374 ? OD2 ? A ASP 2157 OD2 
501 1 Y 1 A LYS 3376 ? CG  ? A LYS 2159 CG  
502 1 Y 1 A LYS 3376 ? CD  ? A LYS 2159 CD  
503 1 Y 1 A LYS 3376 ? CE  ? A LYS 2159 CE  
504 1 Y 1 A LYS 3376 ? NZ  ? A LYS 2159 NZ  
505 1 Y 1 A MET 3377 ? CG  ? A MET 2160 CG  
506 1 Y 1 A MET 3377 ? SD  ? A MET 2160 SD  
507 1 Y 1 A MET 3377 ? CE  ? A MET 2160 CE  
508 1 Y 1 A LYS 3378 ? CG  ? A LYS 2161 CG  
509 1 Y 1 A LYS 3378 ? CD  ? A LYS 2161 CD  
510 1 Y 1 A LYS 3378 ? CE  ? A LYS 2161 CE  
511 1 Y 1 A LYS 3378 ? NZ  ? A LYS 2161 NZ  
512 1 Y 1 A LEU 3380 ? CG  ? A LEU 2163 CG  
513 1 Y 1 A LEU 3380 ? CD1 ? A LEU 2163 CD1 
514 1 Y 1 A LEU 3380 ? CD2 ? A LEU 2163 CD2 
515 1 Y 1 A LYS 3386 ? CG  ? A LYS 2169 CG  
516 1 Y 1 A LYS 3386 ? CD  ? A LYS 2169 CD  
517 1 Y 1 A LYS 3386 ? CE  ? A LYS 2169 CE  
518 1 Y 1 A LYS 3386 ? NZ  ? A LYS 2169 NZ  
519 1 Y 1 A ILE 3396 ? CG1 ? A ILE 2179 CG1 
520 1 Y 1 A ILE 3396 ? CG2 ? A ILE 2179 CG2 
521 1 Y 1 A ILE 3396 ? CD1 ? A ILE 2179 CD1 
522 1 Y 1 A PHE 3446 ? CG  ? A PHE 2229 CG  
523 1 Y 1 A PHE 3446 ? CD1 ? A PHE 2229 CD1 
524 1 Y 1 A PHE 3446 ? CD2 ? A PHE 2229 CD2 
525 1 Y 1 A PHE 3446 ? CE1 ? A PHE 2229 CE1 
526 1 Y 1 A PHE 3446 ? CE2 ? A PHE 2229 CE2 
527 1 Y 1 A PHE 3446 ? CZ  ? A PHE 2229 CZ  
528 1 Y 1 A ILE 3461 ? CG1 ? A ILE 2244 CG1 
529 1 Y 1 A ILE 3461 ? CG2 ? A ILE 2244 CG2 
530 1 Y 1 A ILE 3461 ? CD1 ? A ILE 2244 CD1 
531 1 Y 1 A VAL 3479 ? CG1 ? A VAL 2262 CG1 
532 1 Y 1 A VAL 3479 ? CG2 ? A VAL 2262 CG2 
533 1 Y 1 A GLU 3480 ? CG  ? A GLU 2263 CG  
534 1 Y 1 A GLU 3480 ? CD  ? A GLU 2263 CD  
535 1 Y 1 A GLU 3480 ? OE1 ? A GLU 2263 OE1 
536 1 Y 1 A GLU 3480 ? OE2 ? A GLU 2263 OE2 
537 1 Y 1 A ASP 3483 ? CG  ? A ASP 2266 CG  
538 1 Y 1 A ASP 3483 ? OD1 ? A ASP 2266 OD1 
539 1 Y 1 A ASP 3483 ? OD2 ? A ASP 2266 OD2 
540 1 Y 1 A HIS 3484 ? CG  ? A HIS 2267 CG  
541 1 Y 1 A HIS 3484 ? ND1 ? A HIS 2267 ND1 
542 1 Y 1 A HIS 3484 ? CD2 ? A HIS 2267 CD2 
543 1 Y 1 A HIS 3484 ? CE1 ? A HIS 2267 CE1 
544 1 Y 1 A HIS 3484 ? NE2 ? A HIS 2267 NE2 
545 1 Y 1 A GLU 3485 ? CG  ? A GLU 2268 CG  
546 1 Y 1 A GLU 3485 ? CD  ? A GLU 2268 CD  
547 1 Y 1 A GLU 3485 ? OE1 ? A GLU 2268 OE1 
548 1 Y 1 A GLU 3485 ? OE2 ? A GLU 2268 OE2 
549 1 Y 1 A VAL 3486 ? CG1 ? A VAL 2269 CG1 
550 1 Y 1 A VAL 3486 ? CG2 ? A VAL 2269 CG2 
551 1 Y 1 A ASP 3491 ? CG  ? A ASP 2274 CG  
552 1 Y 1 A ASP 3491 ? OD1 ? A ASP 2274 OD1 
553 1 Y 1 A ASP 3491 ? OD2 ? A ASP 2274 OD2 
554 1 Y 1 A PHE 3518 ? CG  ? A PHE 2301 CG  
555 1 Y 1 A PHE 3518 ? CD1 ? A PHE 2301 CD1 
556 1 Y 1 A PHE 3518 ? CD2 ? A PHE 2301 CD2 
557 1 Y 1 A PHE 3518 ? CE1 ? A PHE 2301 CE1 
558 1 Y 1 A PHE 3518 ? CE2 ? A PHE 2301 CE2 
559 1 Y 1 A PHE 3518 ? CZ  ? A PHE 2301 CZ  
560 1 Y 1 A ASN 3521 ? CG  ? A ASN 2304 CG  
561 1 Y 1 A ASN 3521 ? OD1 ? A ASN 2304 OD1 
562 1 Y 1 A ASN 3521 ? ND2 ? A ASN 2304 ND2 
563 1 Y 1 A LYS 3522 ? CG  ? A LYS 2305 CG  
564 1 Y 1 A LYS 3522 ? CD  ? A LYS 2305 CD  
565 1 Y 1 A LYS 3522 ? CE  ? A LYS 2305 CE  
566 1 Y 1 A LYS 3522 ? NZ  ? A LYS 2305 NZ  
567 1 Y 1 A GLU 3523 ? CG  ? A GLU 2306 CG  
568 1 Y 1 A GLU 3523 ? CD  ? A GLU 2306 CD  
569 1 Y 1 A GLU 3523 ? OE1 ? A GLU 2306 OE1 
570 1 Y 1 A GLU 3523 ? OE2 ? A GLU 2306 OE2 
571 1 Y 1 A THR 3527 ? OG1 ? A THR 2310 OG1 
572 1 Y 1 A THR 3527 ? CG2 ? A THR 2310 CG2 
573 1 Y 1 A ARG 3528 ? CG  ? A ARG 2311 CG  
574 1 Y 1 A ARG 3528 ? CD  ? A ARG 2311 CD  
575 1 Y 1 A ARG 3528 ? NE  ? A ARG 2311 NE  
576 1 Y 1 A ARG 3528 ? CZ  ? A ARG 2311 CZ  
577 1 Y 1 A ARG 3528 ? NH1 ? A ARG 2311 NH1 
578 1 Y 1 A ARG 3528 ? NH2 ? A ARG 2311 NH2 
579 1 Y 1 A PHE 3530 ? CG  ? A PHE 2313 CG  
580 1 Y 1 A PHE 3530 ? CD1 ? A PHE 2313 CD1 
581 1 Y 1 A PHE 3530 ? CD2 ? A PHE 2313 CD2 
582 1 Y 1 A PHE 3530 ? CE1 ? A PHE 2313 CE1 
583 1 Y 1 A PHE 3530 ? CE2 ? A PHE 2313 CE2 
584 1 Y 1 A PHE 3530 ? CZ  ? A PHE 2313 CZ  
585 1 Y 1 A LEU 3534 ? CG  ? A LEU 2317 CG  
586 1 Y 1 A LEU 3534 ? CD1 ? A LEU 2317 CD1 
587 1 Y 1 A LEU 3534 ? CD2 ? A LEU 2317 CD2 
588 1 Y 1 A GLU 3540 ? CG  ? A GLU 2323 CG  
589 1 Y 1 A GLU 3540 ? CD  ? A GLU 2323 CD  
590 1 Y 1 A GLU 3540 ? OE1 ? A GLU 2323 OE1 
591 1 Y 1 A GLU 3540 ? OE2 ? A GLU 2323 OE2 
592 1 Y 1 A MET 3541 ? CG  ? A MET 2324 CG  
593 1 Y 1 A MET 3541 ? SD  ? A MET 2324 SD  
594 1 Y 1 A MET 3541 ? CE  ? A MET 2324 CE  
595 1 Y 1 A GLN 3542 ? CG  ? A GLN 2325 CG  
596 1 Y 1 A GLN 3542 ? CD  ? A GLN 2325 CD  
597 1 Y 1 A GLN 3542 ? OE1 ? A GLN 2325 OE1 
598 1 Y 1 A GLN 3542 ? NE2 ? A GLN 2325 NE2 
599 1 Y 1 A ARG 3543 ? CG  ? A ARG 2326 CG  
600 1 Y 1 A ARG 3543 ? CD  ? A ARG 2326 CD  
601 1 Y 1 A ARG 3543 ? NE  ? A ARG 2326 NE  
602 1 Y 1 A ARG 3543 ? CZ  ? A ARG 2326 CZ  
603 1 Y 1 A ARG 3543 ? NH1 ? A ARG 2326 NH1 
604 1 Y 1 A ARG 3543 ? NH2 ? A ARG 2326 NH2 
605 1 Y 1 A ARG 3545 ? CG  ? A ARG 2328 CG  
606 1 Y 1 A ARG 3545 ? CD  ? A ARG 2328 CD  
607 1 Y 1 A ARG 3545 ? NE  ? A ARG 2328 NE  
608 1 Y 1 A ARG 3545 ? CZ  ? A ARG 2328 CZ  
609 1 Y 1 A ARG 3545 ? NH1 ? A ARG 2328 NH1 
610 1 Y 1 A ARG 3545 ? NH2 ? A ARG 2328 NH2 
611 1 Y 1 A GLU 3546 ? CG  ? A GLU 2329 CG  
612 1 Y 1 A GLU 3546 ? CD  ? A GLU 2329 CD  
613 1 Y 1 A GLU 3546 ? OE1 ? A GLU 2329 OE1 
614 1 Y 1 A GLU 3546 ? OE2 ? A GLU 2329 OE2 
615 1 Y 1 A ASP 3547 ? CG  ? A ASP 2330 CG  
616 1 Y 1 A ASP 3547 ? OD1 ? A ASP 2330 OD1 
617 1 Y 1 A ASP 3547 ? OD2 ? A ASP 2330 OD2 
618 1 Y 1 A LEU 3548 ? CG  ? A LEU 2331 CG  
619 1 Y 1 A LEU 3548 ? CD1 ? A LEU 2331 CD1 
620 1 Y 1 A LEU 3548 ? CD2 ? A LEU 2331 CD2 
621 1 Y 1 A ILE 3549 ? CG1 ? A ILE 2332 CG1 
622 1 Y 1 A ILE 3549 ? CG2 ? A ILE 2332 CG2 
623 1 Y 1 A ILE 3549 ? CD1 ? A ILE 2332 CD1 
624 1 Y 1 A LYS 3550 ? CG  ? A LYS 2333 CG  
625 1 Y 1 A LYS 3550 ? CD  ? A LYS 2333 CD  
626 1 Y 1 A LYS 3550 ? CE  ? A LYS 2333 CE  
627 1 Y 1 A LYS 3550 ? NZ  ? A LYS 2333 NZ  
628 1 Y 1 A LEU 3551 ? CG  ? A LEU 2334 CG  
629 1 Y 1 A LEU 3551 ? CD1 ? A LEU 2334 CD1 
630 1 Y 1 A LEU 3551 ? CD2 ? A LEU 2334 CD2 
631 1 Y 1 A ASN 3552 ? CG  ? A ASN 2335 CG  
632 1 Y 1 A ASN 3552 ? OD1 ? A ASN 2335 OD1 
633 1 Y 1 A ASN 3552 ? ND2 ? A ASN 2335 ND2 
634 1 Y 1 A THR 3553 ? OG1 ? A THR 2336 OG1 
635 1 Y 1 A THR 3553 ? CG2 ? A THR 2336 CG2 
636 1 Y 1 A GLU 3554 ? CG  ? A GLU 2337 CG  
637 1 Y 1 A GLU 3554 ? CD  ? A GLU 2337 CD  
638 1 Y 1 A GLU 3554 ? OE1 ? A GLU 2337 OE1 
639 1 Y 1 A GLU 3554 ? OE2 ? A GLU 2337 OE2 
640 1 Y 1 A TYR 3555 ? CG  ? A TYR 2338 CG  
641 1 Y 1 A TYR 3555 ? CD1 ? A TYR 2338 CD1 
642 1 Y 1 A TYR 3555 ? CD2 ? A TYR 2338 CD2 
643 1 Y 1 A TYR 3555 ? CE1 ? A TYR 2338 CE1 
644 1 Y 1 A TYR 3555 ? CE2 ? A TYR 2338 CE2 
645 1 Y 1 A TYR 3555 ? CZ  ? A TYR 2338 CZ  
646 1 Y 1 A TYR 3555 ? OH  ? A TYR 2338 OH  
647 1 Y 1 A ARG 3556 ? CG  ? A ARG 2339 CG  
648 1 Y 1 A ARG 3556 ? CD  ? A ARG 2339 CD  
649 1 Y 1 A ARG 3556 ? NE  ? A ARG 2339 NE  
650 1 Y 1 A ARG 3556 ? CZ  ? A ARG 2339 CZ  
651 1 Y 1 A ARG 3556 ? NH1 ? A ARG 2339 NH1 
652 1 Y 1 A ARG 3556 ? NH2 ? A ARG 2339 NH2 
653 1 Y 1 A LEU 3557 ? CG  ? A LEU 2340 CG  
654 1 Y 1 A LEU 3557 ? CD1 ? A LEU 2340 CD1 
655 1 Y 1 A LEU 3557 ? CD2 ? A LEU 2340 CD2 
656 1 Y 1 A LYS 3558 ? CG  ? A LYS 2341 CG  
657 1 Y 1 A LYS 3558 ? CD  ? A LYS 2341 CD  
658 1 Y 1 A LYS 3558 ? CE  ? A LYS 2341 CE  
659 1 Y 1 A LYS 3558 ? NZ  ? A LYS 2341 NZ  
660 1 Y 1 A LEU 3559 ? CG  ? A LEU 2342 CG  
661 1 Y 1 A LEU 3559 ? CD1 ? A LEU 2342 CD1 
662 1 Y 1 A LEU 3559 ? CD2 ? A LEU 2342 CD2 
663 1 Y 1 A LYS 3560 ? CG  ? A LYS 2343 CG  
664 1 Y 1 A LYS 3560 ? CD  ? A LYS 2343 CD  
665 1 Y 1 A LYS 3560 ? CE  ? A LYS 2343 CE  
666 1 Y 1 A LYS 3560 ? NZ  ? A LYS 2343 NZ  
667 1 Y 1 A ASN 3561 ? CG  ? A ASN 2344 CG  
668 1 Y 1 A ASN 3561 ? OD1 ? A ASN 2344 OD1 
669 1 Y 1 A ASN 3561 ? ND2 ? A ASN 2344 ND2 
670 1 Y 1 A LEU 3562 ? CG  ? A LEU 2345 CG  
671 1 Y 1 A LEU 3562 ? CD1 ? A LEU 2345 CD1 
672 1 Y 1 A LEU 3562 ? CD2 ? A LEU 2345 CD2 
673 1 Y 1 A GLU 3563 ? CG  ? A GLU 2346 CG  
674 1 Y 1 A GLU 3563 ? CD  ? A GLU 2346 CD  
675 1 Y 1 A GLU 3563 ? OE1 ? A GLU 2346 OE1 
676 1 Y 1 A GLU 3563 ? OE2 ? A GLU 2346 OE2 
677 1 Y 1 A LYS 3564 ? CG  ? A LYS 2347 CG  
678 1 Y 1 A LYS 3564 ? CD  ? A LYS 2347 CD  
679 1 Y 1 A LYS 3564 ? CE  ? A LYS 2347 CE  
680 1 Y 1 A LYS 3564 ? NZ  ? A LYS 2347 NZ  
681 1 Y 1 A ARG 3565 ? CG  ? A ARG 2348 CG  
682 1 Y 1 A ARG 3565 ? CD  ? A ARG 2348 CD  
683 1 Y 1 A ARG 3565 ? NE  ? A ARG 2348 NE  
684 1 Y 1 A ARG 3565 ? CZ  ? A ARG 2348 CZ  
685 1 Y 1 A ARG 3565 ? NH1 ? A ARG 2348 NH1 
686 1 Y 1 A ARG 3565 ? NH2 ? A ARG 2348 NH2 
687 1 Y 1 A LEU 3566 ? CG  ? A LEU 2349 CG  
688 1 Y 1 A LEU 3566 ? CD1 ? A LEU 2349 CD1 
689 1 Y 1 A LEU 3566 ? CD2 ? A LEU 2349 CD2 
690 1 Y 1 A LEU 3567 ? CG  ? A LEU 2350 CG  
691 1 Y 1 A LEU 3567 ? CD1 ? A LEU 2350 CD1 
692 1 Y 1 A LEU 3567 ? CD2 ? A LEU 2350 CD2 
693 1 Y 1 A GLU 3568 ? CG  ? A GLU 2351 CG  
694 1 Y 1 A GLU 3568 ? CD  ? A GLU 2351 CD  
695 1 Y 1 A GLU 3568 ? OE1 ? A GLU 2351 OE1 
696 1 Y 1 A GLU 3568 ? OE2 ? A GLU 2351 OE2 
697 1 Y 1 A GLU 3569 ? CG  ? A GLU 2352 CG  
698 1 Y 1 A GLU 3569 ? CD  ? A GLU 2352 CD  
699 1 Y 1 A GLU 3569 ? OE1 ? A GLU 2352 OE1 
700 1 Y 1 A GLU 3569 ? OE2 ? A GLU 2352 OE2 
701 1 Y 1 A LEU 3570 ? CG  ? A LEU 2353 CG  
702 1 Y 1 A LEU 3570 ? CD1 ? A LEU 2353 CD1 
703 1 Y 1 A LEU 3570 ? CD2 ? A LEU 2353 CD2 
704 1 Y 1 A ASN 3571 ? CG  ? A ASN 2354 CG  
705 1 Y 1 A ASN 3571 ? OD1 ? A ASN 2354 OD1 
706 1 Y 1 A ASN 3571 ? ND2 ? A ASN 2354 ND2 
707 1 Y 1 A ASN 3572 ? CG  ? A ASN 2355 CG  
708 1 Y 1 A ASN 3572 ? OD1 ? A ASN 2355 OD1 
709 1 Y 1 A ASN 3572 ? ND2 ? A ASN 2355 ND2 
710 1 Y 1 A SER 3573 ? OG  ? A SER 2356 OG  
711 1 Y 1 A LYS 3592 ? CG  ? A LYS 2375 CG  
712 1 Y 1 A LYS 3592 ? CD  ? A LYS 2375 CD  
713 1 Y 1 A LYS 3592 ? CE  ? A LYS 2375 CE  
714 1 Y 1 A LYS 3592 ? NZ  ? A LYS 2375 NZ  
715 1 Y 1 A GLU 3593 ? CG  ? A GLU 2376 CG  
716 1 Y 1 A GLU 3593 ? CD  ? A GLU 2376 CD  
717 1 Y 1 A GLU 3593 ? OE1 ? A GLU 2376 OE1 
718 1 Y 1 A GLU 3593 ? OE2 ? A GLU 2376 OE2 
719 1 Y 1 A MET 3595 ? CG  ? A MET 2378 CG  
720 1 Y 1 A MET 3595 ? SD  ? A MET 2378 SD  
721 1 Y 1 A MET 3595 ? CE  ? A MET 2378 CE  
722 1 Y 1 A ASN 3596 ? CG  ? A ASN 2379 CG  
723 1 Y 1 A ASN 3596 ? OD1 ? A ASN 2379 OD1 
724 1 Y 1 A ASN 3596 ? ND2 ? A ASN 2379 ND2 
725 1 Y 1 A ILE 3597 ? CG1 ? A ILE 2380 CG1 
726 1 Y 1 A ILE 3597 ? CG2 ? A ILE 2380 CG2 
727 1 Y 1 A ILE 3597 ? CD1 ? A ILE 2380 CD1 
728 1 Y 1 A GLU 3598 ? CG  ? A GLU 2381 CG  
729 1 Y 1 A GLU 3598 ? CD  ? A GLU 2381 CD  
730 1 Y 1 A GLU 3598 ? OE1 ? A GLU 2381 OE1 
731 1 Y 1 A GLU 3598 ? OE2 ? A GLU 2381 OE2 
732 1 Y 1 A LYS 3599 ? CG  ? A LYS 2382 CG  
733 1 Y 1 A LYS 3599 ? CD  ? A LYS 2382 CD  
734 1 Y 1 A LYS 3599 ? CE  ? A LYS 2382 CE  
735 1 Y 1 A LYS 3599 ? NZ  ? A LYS 2382 NZ  
736 1 Y 1 A LYS 3600 ? CG  ? A LYS 2383 CG  
737 1 Y 1 A LYS 3600 ? CD  ? A LYS 2383 CD  
738 1 Y 1 A LYS 3600 ? CE  ? A LYS 2383 CE  
739 1 Y 1 A LYS 3600 ? NZ  ? A LYS 2383 NZ  
740 1 Y 1 A LEU 3601 ? CG  ? A LEU 2384 CG  
741 1 Y 1 A LEU 3601 ? CD1 ? A LEU 2384 CD1 
742 1 Y 1 A LEU 3601 ? CD2 ? A LEU 2384 CD2 
743 1 Y 1 A SER 3602 ? OG  ? A SER 2385 OG  
744 1 Y 1 A GLU 3603 ? CG  ? A GLU 2386 CG  
745 1 Y 1 A GLU 3603 ? CD  ? A GLU 2386 CD  
746 1 Y 1 A GLU 3603 ? OE1 ? A GLU 2386 OE1 
747 1 Y 1 A GLU 3603 ? OE2 ? A GLU 2386 OE2 
748 1 Y 1 A SER 3604 ? OG  ? A SER 2387 OG  
749 1 Y 1 A GLU 3605 ? CG  ? A GLU 2388 CG  
750 1 Y 1 A GLU 3605 ? CD  ? A GLU 2388 CD  
751 1 Y 1 A GLU 3605 ? OE1 ? A GLU 2388 OE1 
752 1 Y 1 A GLU 3605 ? OE2 ? A GLU 2388 OE2 
753 1 Y 1 A GLU 3606 ? CG  ? A GLU 2389 CG  
754 1 Y 1 A GLU 3606 ? CD  ? A GLU 2389 CD  
755 1 Y 1 A GLU 3606 ? OE1 ? A GLU 2389 OE1 
756 1 Y 1 A GLU 3606 ? OE2 ? A GLU 2389 OE2 
757 1 Y 1 A PHE 3607 ? CG  ? A PHE 2390 CG  
758 1 Y 1 A PHE 3607 ? CD1 ? A PHE 2390 CD1 
759 1 Y 1 A PHE 3607 ? CD2 ? A PHE 2390 CD2 
760 1 Y 1 A PHE 3607 ? CE1 ? A PHE 2390 CE1 
761 1 Y 1 A PHE 3607 ? CE2 ? A PHE 2390 CE2 
762 1 Y 1 A PHE 3607 ? CZ  ? A PHE 2390 CZ  
763 1 Y 1 A PHE 3608 ? CG  ? A PHE 2391 CG  
764 1 Y 1 A PHE 3608 ? CD1 ? A PHE 2391 CD1 
765 1 Y 1 A PHE 3608 ? CD2 ? A PHE 2391 CD2 
766 1 Y 1 A PHE 3608 ? CE1 ? A PHE 2391 CE1 
767 1 Y 1 A PHE 3608 ? CE2 ? A PHE 2391 CE2 
768 1 Y 1 A PHE 3608 ? CZ  ? A PHE 2391 CZ  
769 1 Y 1 A GLN 3610 ? CG  ? A GLN 2393 CG  
770 1 Y 1 A GLN 3610 ? CD  ? A GLN 2393 CD  
771 1 Y 1 A GLN 3610 ? OE1 ? A GLN 2393 OE1 
772 1 Y 1 A GLN 3610 ? NE2 ? A GLN 2393 NE2 
773 1 Y 1 A PHE 3611 ? CG  ? A PHE 2394 CG  
774 1 Y 1 A PHE 3611 ? CD1 ? A PHE 2394 CD1 
775 1 Y 1 A PHE 3611 ? CD2 ? A PHE 2394 CD2 
776 1 Y 1 A PHE 3611 ? CE1 ? A PHE 2394 CE1 
777 1 Y 1 A PHE 3611 ? CE2 ? A PHE 2394 CE2 
778 1 Y 1 A PHE 3611 ? CZ  ? A PHE 2394 CZ  
779 1 Y 1 A ASP 3612 ? CG  ? A ASP 2395 CG  
780 1 Y 1 A ASP 3612 ? OD1 ? A ASP 2395 OD1 
781 1 Y 1 A ASP 3612 ? OD2 ? A ASP 2395 OD2 
782 1 Y 1 A ASN 3613 ? CG  ? A ASN 2396 CG  
783 1 Y 1 A ASN 3613 ? OD1 ? A ASN 2396 OD1 
784 1 Y 1 A ASN 3613 ? ND2 ? A ASN 2396 ND2 
785 1 Y 1 A LEU 3614 ? CG  ? A LEU 2397 CG  
786 1 Y 1 A LEU 3614 ? CD1 ? A LEU 2397 CD1 
787 1 Y 1 A LEU 3614 ? CD2 ? A LEU 2397 CD2 
788 1 Y 1 A GLU 3616 ? CG  ? A GLU 2399 CG  
789 1 Y 1 A GLU 3616 ? CD  ? A GLU 2399 CD  
790 1 Y 1 A GLU 3616 ? OE1 ? A GLU 2399 OE1 
791 1 Y 1 A GLU 3616 ? OE2 ? A GLU 2399 OE2 
792 1 Y 1 A LYS 3623 ? CG  ? A LYS 2406 CG  
793 1 Y 1 A LYS 3623 ? CD  ? A LYS 2406 CD  
794 1 Y 1 A LYS 3623 ? CE  ? A LYS 2406 CE  
795 1 Y 1 A LYS 3623 ? NZ  ? A LYS 2406 NZ  
796 1 Y 1 A GLU 3633 ? CG  ? A GLU 2416 CG  
797 1 Y 1 A GLU 3633 ? CD  ? A GLU 2416 CD  
798 1 Y 1 A GLU 3633 ? OE1 ? A GLU 2416 OE1 
799 1 Y 1 A GLU 3633 ? OE2 ? A GLU 2416 OE2 
800 1 Y 1 A SER 3645 ? OG  ? A SER 2428 OG  
801 1 Y 1 A GLN 3648 ? CG  ? A GLN 2431 CG  
802 1 Y 1 A GLN 3648 ? CD  ? A GLN 2431 CD  
803 1 Y 1 A GLN 3648 ? OE1 ? A GLN 2431 OE1 
804 1 Y 1 A GLN 3648 ? NE2 ? A GLN 2431 NE2 
805 1 Y 1 A ARG 3655 ? CG  ? A ARG 2438 CG  
806 1 Y 1 A ARG 3655 ? CD  ? A ARG 2438 CD  
807 1 Y 1 A ARG 3655 ? NE  ? A ARG 2438 NE  
808 1 Y 1 A ARG 3655 ? CZ  ? A ARG 2438 CZ  
809 1 Y 1 A ARG 3655 ? NH1 ? A ARG 2438 NH1 
810 1 Y 1 A ARG 3655 ? NH2 ? A ARG 2438 NH2 
811 1 Y 1 A ILE 3658 ? CG1 ? A ILE 2441 CG1 
812 1 Y 1 A ILE 3658 ? CG2 ? A ILE 2441 CG2 
813 1 Y 1 A ILE 3658 ? CD1 ? A ILE 2441 CD1 
814 1 Y 1 A LYS 3659 ? CG  ? A LYS 2442 CG  
815 1 Y 1 A LYS 3659 ? CD  ? A LYS 2442 CD  
816 1 Y 1 A LYS 3659 ? CE  ? A LYS 2442 CE  
817 1 Y 1 A LYS 3659 ? NZ  ? A LYS 2442 NZ  
818 1 Y 1 A ARG 3670 ? CG  ? A ARG 2453 CG  
819 1 Y 1 A ARG 3670 ? CD  ? A ARG 2453 CD  
820 1 Y 1 A ARG 3670 ? NE  ? A ARG 2453 NE  
821 1 Y 1 A ARG 3670 ? CZ  ? A ARG 2453 CZ  
822 1 Y 1 A ARG 3670 ? NH1 ? A ARG 2453 NH1 
823 1 Y 1 A ARG 3670 ? NH2 ? A ARG 2453 NH2 
824 1 Y 1 A VAL 3671 ? CG1 ? A VAL 2454 CG1 
825 1 Y 1 A VAL 3671 ? CG2 ? A VAL 2454 CG2 
826 1 Y 1 A ASP 3672 ? CG  ? A ASP 2455 CG  
827 1 Y 1 A ASP 3672 ? OD1 ? A ASP 2455 OD1 
828 1 Y 1 A ASP 3672 ? OD2 ? A ASP 2455 OD2 
829 1 Y 1 A GLU 3728 ? CG  ? A GLU 2511 CG  
830 1 Y 1 A GLU 3728 ? CD  ? A GLU 2511 CD  
831 1 Y 1 A GLU 3728 ? OE1 ? A GLU 2511 OE1 
832 1 Y 1 A GLU 3728 ? OE2 ? A GLU 2511 OE2 
833 1 Y 1 A ASP 3742 ? CG  ? A ASP 2525 CG  
834 1 Y 1 A ASP 3742 ? OD1 ? A ASP 2525 OD1 
835 1 Y 1 A ASP 3742 ? OD2 ? A ASP 2525 OD2 
836 1 Y 1 A ASP 3743 ? CG  ? A ASP 2526 CG  
837 1 Y 1 A ASP 3743 ? OD1 ? A ASP 2526 OD1 
838 1 Y 1 A ASP 3743 ? OD2 ? A ASP 2526 OD2 
839 1 Y 1 A ARG 3745 ? CG  ? A ARG 2528 CG  
840 1 Y 1 A ARG 3745 ? CD  ? A ARG 2528 CD  
841 1 Y 1 A ARG 3745 ? NE  ? A ARG 2528 NE  
842 1 Y 1 A ARG 3745 ? CZ  ? A ARG 2528 CZ  
843 1 Y 1 A ARG 3745 ? NH1 ? A ARG 2528 NH1 
844 1 Y 1 A ARG 3745 ? NH2 ? A ARG 2528 NH2 
845 1 Y 1 A TYR 3746 ? CG  ? A TYR 2529 CG  
846 1 Y 1 A TYR 3746 ? CD1 ? A TYR 2529 CD1 
847 1 Y 1 A TYR 3746 ? CD2 ? A TYR 2529 CD2 
848 1 Y 1 A TYR 3746 ? CE1 ? A TYR 2529 CE1 
849 1 Y 1 A TYR 3746 ? CE2 ? A TYR 2529 CE2 
850 1 Y 1 A TYR 3746 ? CZ  ? A TYR 2529 CZ  
851 1 Y 1 A TYR 3746 ? OH  ? A TYR 2529 OH  
852 1 Y 1 A ASP 3749 ? CG  ? A ASP 2532 CG  
853 1 Y 1 A ASP 3749 ? OD1 ? A ASP 2532 OD1 
854 1 Y 1 A ASP 3749 ? OD2 ? A ASP 2532 OD2 
855 1 Y 1 A THR 3753 ? OG1 ? A THR 2536 OG1 
856 1 Y 1 A THR 3753 ? CG2 ? A THR 2536 CG2 
857 1 Y 1 A LYS 3764 ? CG  ? A LYS 2547 CG  
858 1 Y 1 A LYS 3764 ? CD  ? A LYS 2547 CD  
859 1 Y 1 A LYS 3764 ? CE  ? A LYS 2547 CE  
860 1 Y 1 A LYS 3764 ? NZ  ? A LYS 2547 NZ  
861 1 Y 1 A ASN 3765 ? CG  ? A ASN 2548 CG  
862 1 Y 1 A ASN 3765 ? OD1 ? A ASN 2548 OD1 
863 1 Y 1 A ASN 3765 ? ND2 ? A ASN 2548 ND2 
864 1 Y 1 A GLU 3766 ? CG  ? A GLU 2549 CG  
865 1 Y 1 A GLU 3766 ? CD  ? A GLU 2549 CD  
866 1 Y 1 A GLU 3766 ? OE1 ? A GLU 2549 OE1 
867 1 Y 1 A GLU 3766 ? OE2 ? A GLU 2549 OE2 
868 1 Y 1 A GLU 3771 ? CG  ? A GLU 2554 CG  
869 1 Y 1 A GLU 3771 ? CD  ? A GLU 2554 CD  
870 1 Y 1 A GLU 3771 ? OE1 ? A GLU 2554 OE1 
871 1 Y 1 A GLU 3771 ? OE2 ? A GLU 2554 OE2 
872 1 Y 1 A ASN 3780 ? CG  ? A ASN 2563 CG  
873 1 Y 1 A ASN 3780 ? OD1 ? A ASN 2563 OD1 
874 1 Y 1 A ASN 3780 ? ND2 ? A ASN 2563 ND2 
875 1 Y 1 A GLU 3782 ? CG  ? A GLU 2565 CG  
876 1 Y 1 A GLU 3782 ? CD  ? A GLU 2565 CD  
877 1 Y 1 A GLU 3782 ? OE1 ? A GLU 2565 OE1 
878 1 Y 1 A GLU 3782 ? OE2 ? A GLU 2565 OE2 
879 1 Y 1 A ASN 3784 ? CG  ? A ASN 2567 CG  
880 1 Y 1 A ASN 3784 ? OD1 ? A ASN 2567 OD1 
881 1 Y 1 A ASN 3784 ? ND2 ? A ASN 2567 ND2 
882 1 Y 1 A GLU 3802 ? CG  ? A GLU 2585 CG  
883 1 Y 1 A GLU 3802 ? CD  ? A GLU 2585 CD  
884 1 Y 1 A GLU 3802 ? OE1 ? A GLU 2585 OE1 
885 1 Y 1 A GLU 3802 ? OE2 ? A GLU 2585 OE2 
886 1 Y 1 A LYS 3805 ? CG  ? A LYS 2588 CG  
887 1 Y 1 A LYS 3805 ? CD  ? A LYS 2588 CD  
888 1 Y 1 A LYS 3805 ? CE  ? A LYS 2588 CE  
889 1 Y 1 A LYS 3805 ? NZ  ? A LYS 2588 NZ  
890 1 Y 1 A LYS 3808 ? CG  ? A LYS 2591 CG  
891 1 Y 1 A LYS 3808 ? CD  ? A LYS 2591 CD  
892 1 Y 1 A LYS 3808 ? CE  ? A LYS 2591 CE  
893 1 Y 1 A LYS 3808 ? NZ  ? A LYS 2591 NZ  
894 1 Y 1 A ILE 3819 ? CG1 ? A ILE 2602 CG1 
895 1 Y 1 A ILE 3819 ? CG2 ? A ILE 2602 CG2 
896 1 Y 1 A ILE 3819 ? CD1 ? A ILE 2602 CD1 
897 1 Y 1 A GLU 3820 ? CG  ? A GLU 2603 CG  
898 1 Y 1 A GLU 3820 ? CD  ? A GLU 2603 CD  
899 1 Y 1 A GLU 3820 ? OE1 ? A GLU 2603 OE1 
900 1 Y 1 A GLU 3820 ? OE2 ? A GLU 2603 OE2 
901 1 Y 1 A ASN 3823 ? CG  ? A ASN 2606 CG  
902 1 Y 1 A ASN 3823 ? OD1 ? A ASN 2606 OD1 
903 1 Y 1 A ASN 3823 ? ND2 ? A ASN 2606 ND2 
904 1 Y 1 A GLN 3826 ? CG  ? A GLN 2609 CG  
905 1 Y 1 A GLN 3826 ? CD  ? A GLN 2609 CD  
906 1 Y 1 A GLN 3826 ? OE1 ? A GLN 2609 OE1 
907 1 Y 1 A GLN 3826 ? NE2 ? A GLN 2609 NE2 
908 1 Y 1 A GLU 3827 ? CG  ? A GLU 2610 CG  
909 1 Y 1 A GLU 3827 ? CD  ? A GLU 2610 CD  
910 1 Y 1 A GLU 3827 ? OE1 ? A GLU 2610 OE1 
911 1 Y 1 A GLU 3827 ? OE2 ? A GLU 2610 OE2 
912 1 Y 1 A SER 3830 ? OG  ? A SER 2613 OG  
913 1 Y 1 A LYS 3831 ? CG  ? A LYS 2614 CG  
914 1 Y 1 A LYS 3831 ? CD  ? A LYS 2614 CD  
915 1 Y 1 A LYS 3831 ? CE  ? A LYS 2614 CE  
916 1 Y 1 A LYS 3831 ? NZ  ? A LYS 2614 NZ  
917 1 Y 1 A ILE 3834 ? CG1 ? A ILE 2617 CG1 
918 1 Y 1 A ILE 3834 ? CG2 ? A ILE 2617 CG2 
919 1 Y 1 A ILE 3834 ? CD1 ? A ILE 2617 CD1 
920 1 Y 1 A TRP 3850 ? CG  ? A TRP 2633 CG  
921 1 Y 1 A TRP 3850 ? CD1 ? A TRP 2633 CD1 
922 1 Y 1 A TRP 3850 ? CD2 ? A TRP 2633 CD2 
923 1 Y 1 A TRP 3850 ? NE1 ? A TRP 2633 NE1 
924 1 Y 1 A TRP 3850 ? CE2 ? A TRP 2633 CE2 
925 1 Y 1 A TRP 3850 ? CE3 ? A TRP 2633 CE3 
926 1 Y 1 A TRP 3850 ? CZ2 ? A TRP 2633 CZ2 
927 1 Y 1 A TRP 3850 ? CZ3 ? A TRP 2633 CZ3 
928 1 Y 1 A TRP 3850 ? CH2 ? A TRP 2633 CH2 
929 1 Y 1 A LYS 3857 ? CG  ? A LYS 2640 CG  
930 1 Y 1 A LYS 3857 ? CD  ? A LYS 2640 CD  
931 1 Y 1 A LYS 3857 ? CE  ? A LYS 2640 CE  
932 1 Y 1 A LYS 3857 ? NZ  ? A LYS 2640 NZ  
933 1 Y 1 A GLU 3867 ? CG  ? A GLU 2650 CG  
934 1 Y 1 A GLU 3867 ? CD  ? A GLU 2650 CD  
935 1 Y 1 A GLU 3867 ? OE1 ? A GLU 2650 OE1 
936 1 Y 1 A GLU 3867 ? OE2 ? A GLU 2650 OE2 
937 1 Y 1 A GLU 3869 ? CG  ? A GLU 2652 CG  
938 1 Y 1 A GLU 3869 ? CD  ? A GLU 2652 CD  
939 1 Y 1 A GLU 3869 ? OE1 ? A GLU 2652 OE1 
940 1 Y 1 A GLU 3869 ? OE2 ? A GLU 2652 OE2 
941 1 Y 1 A LYS 3870 ? CG  ? A LYS 2653 CG  
942 1 Y 1 A LYS 3870 ? CD  ? A LYS 2653 CD  
943 1 Y 1 A LYS 3870 ? CE  ? A LYS 2653 CE  
944 1 Y 1 A LYS 3870 ? NZ  ? A LYS 2653 NZ  
945 1 Y 1 A ASP 3882 ? CG  ? A ASP 2665 CG  
946 1 Y 1 A ASP 3882 ? OD1 ? A ASP 2665 OD1 
947 1 Y 1 A ASP 3882 ? OD2 ? A ASP 2665 OD2 
# 
_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                     9DKD 
_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                         9DKD 
_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                   9DKD 
_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                                 9DKD 
_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                            . 
_refine.ls_d_res_low                             ? 
_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                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_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       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_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' ? 0.003 ? 18251 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.645 ? 24766 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 7.029 ? 2511  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.044 ? 2880  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 3104  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9DKD 
_struct.title                        'CryoEM structures of yeast cytoplasmic dynein in the presence of ATP and Lis1.' 
_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        9DKD 
_struct_keywords.text            'Enzyme, AAA protein, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYHC_YEAST 
_struct_ref.pdbx_db_accession          P36022 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQLTHVVEEVKTYDLVWRSIKNLWEDVQRTFETPWCRVDVLLLQSDLANFLRRADELPRAVKQFEMYKSLFSQVNMLTSV
NKILVELKDGALKPRHWNMIFRDIGKRQIQKNLLDKLEFSLKDVMVLNLTLNEILLTKIIERAQKEFVIEKSLNRIKKFW
KEAQYEVIEHSSGLKLVREWDVLEQACKEDLEELVSMKASNYYKIFEQDCLDLESKLTKLSEIQVNWVEVQFYWLDLYGI
LGENLDIQNFLPLETSKFKSLTSEYKMITTRAFQLDTTIEVIHIPNFDTTLKLTIDSLKMIKSSLSTFLERQRRQFPRFY
FLGNDDLLKIIGSGKHHDQVSKFMKKMFGSIESIIFLEDFITGVRSVEGEVLNLNEKIELKDSIQAQEWLNILDTEIKLS
VFTQFRDCLGQLKDGTDIEVVVSKYIFQAILLSAQVMWTELVEKCLQTNQFSKYWKEVDMKIKGLLDKLNKSSDNVKKKI
EALLVEYLHFNNVIGQLKNCSTKEEARLLWAKVQKFYQKNDTLDDLNSVFISQSGYLLQYKFEYIGIPERLIYTPLLLIG
FATLTDSLHQKYGGCFFGPAGTGKTETVKAFGQNLGRVVVVFNCDDSFDYQVLSRLLVGITQIGAWGCFDEFNRLDEKVL
SAVSANIQQIQNGLQVGKSHITLLEEETPLSPHTAVFITLNPGYNGRSELPENLKKSFREFSMKSPQSGTIAEMILQIMG
FEDSKSLASKIVHFLELLSSKCSSMNHYHFGLRTLKGVLRNCSPLISEFGEGEKTVVESLKRVILPSLGDTDELVFKDEL
SKIFDSAGTPLNSKAIVQCLKDAGQRSGFSMSEEFLKKCMQFYYMQKTQQALILVGKAGCGKTATWKTVIDAMAIFDGHA
NVVYVIDTKVLTKESLYGSMLKATLEWRDGLFTSILRRVNDDITGTFKNSRIWVVFDSDLDPEYVEAMNSVLDDNKILTL
PNGERLPIPPNFRILFETDNLDHTTPATITRCGLLWFSTDVCSISSKIDHLLNKSYEALDNKLSMFELDKLKDLISDSFD
MASLTNIFTCSNDLVHILGVRTFNKLETAVQLAVHLISSYRQWFQNLDDKSLKDVITLLIKRSLLYALAGDSTGESQRAF
IQTINTYFGHDSQELSDYSTIVIANDKLSFSSFCSEIPSVSLEAHEVMRPDIVIPTIDTIKHEKIFYDLLNSKRGIILCG
PPGSGKTMIMNNALRNSSLYDVVGINFSKDTTTEHILSALHRHTNYVTTSKGLTLLPKSDIKNLVLFCDEINLPKLDKYG
SQNVVLFLRQLMEKQGFWKTPENKWVTIERIHIVGACNPPTDPGRIPMSERFTRHAAILYLGYPSGKSLSQIYEIYYKAI
FKLVPEFRSYTEPFARASVHLYNECKARYSTGLQSHYLFSPRELTRLVRGVYTAINTGPRQTLRSLIRLWAYEAWRIFAD
RLVGVKEKNSFEQLLYETVDKYLPNQDLGNISSTSLLFSGLLSLDFKEVNKTDLVNFIEERFKTFCDEELEVPMVIHESM
VDHILRIDRALKQVQGHMMLIGASRTGKTILTRFVAWLNGLKIVQPKIHRHSNLSDFDMILKKAISDCSLKESRTCLIID
ESNILETAFLERMNTLLANADIPDLFQGEEYDKLLNNLRNKTRSLGLLLDTEQELYDWFVGEIAKNLHVVFTICDPTNNK
SSAMISSPALFNRCIINWMGDWDTKTMSQVANNMVDVIPMEFTDFIVPEVNKELVFTEPIQTIRDAVVNILIHFDRNFYQ
KMKVGVNPRSPGYFIDGLRALVKLVTAKYQDLQENQRFVNVGLEKLNESVLKVNELNKTLSKKSTELTEKEKEARSTLDK
MLMEQNESERKQEATEEIKKILKVQEEDIRKRKEVVMKSIQDIEPTILEAQRGVKNIKKQQLTEIRSMVNPPSGVKIVME
AVCAILGYQFSNWRDIQQFIRKDDFIHNIVHYDTTLHMKPQIRKYMEEEFLSDPNFTYETINRASKACGPLYQWVNAQIN
FSKVLENVDPLRQEMKRIEFESLKTKANLLAAEEMTQDLEASIEVSKRKYSLLIRDVEAIKTEMSNVQANLDRSISLVKS
LTFEKERWLNTTKQFSKTSQELIGNCIISSIYETYFGHLNERERADMLVILKRLLGKFAVKYDVNYRFIDYLVTLDEKMK
WLECGLDKNDYFLENMSIVMNSQDAVPFLLDPSSHMITVISNYYGNKTVLLSFLEEGFVKRLENAIRFGSVVIIQDGEFF
DPIISRLISREFNHAGNRVTVEIGDHEVDVSGDFKLFIHSCDPSGDIPIFLRSRVRLVHFVTNKESIETRIFDITLTEEN
AEMQRKREDLIKLNTEYKLKLKNLEKRLLEELNNSQGNMLENDELMVTLNNLKKEAMNIEKKLSESEEFFPQFDNLVEEY
SIIGKHSVKIFSMLEKFGQFHWFYGISIGQFLSCFKRVFIKKSRETRAARTRVDEILWLLYQEVYCQFSTALDKKFKMIM
AMTMFCLYKFDIESEQYKEAVLTMIGVLSESSDGVPKLTVDTNNDLRYLWDYVTTKSYISALNWFKNEFFVDEWNIADVV
ANSENNYFTMASERDVDGTFKLIELAKASKESLKIIPLGSIENLNYAQEEISKSKIEGGWILLQNIQMSLSWVKTYLHKH
VEETKAAEEHEKFKMFMTCHLTGDKLPAPLLQRTDRFVYEDIPGILDTVKDLWGSQFFTGKISGVWSVYCTFLLSWFHAL
ITARTRLVPHGFSKKYYFNDCDFQFASVYLENVLATNSTNNIPWAQVRDHIATIVYGGKIDEEKDLEVVAKLCAHVFCGS
DNLQIVPGVRIPQPLLQQSEEEERARLTAILSNTIEPADSLSSWLQLPRESILNYERLQAKEVASSTEQLLQEM
;
_struct_ref.pdbx_align_begin           1219 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DKD 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 2875 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P36022 
_struct_ref_seq.db_align_beg                  1219 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4092 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1219 
_struct_ref_seq.pdbx_auth_seq_align_end       4092 
# 
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 9DKD GLY A 1    ? UNP P36022 ?   ?    'expression tag' 1218 1  
1 9DKD PHE A 358  ? UNP P36022 LEU 1575 conflict         1575 2  
1 9DKD SER A 361  ? UNP P36022 PHE 1578 conflict         1578 3  
1 9DKD GLU A 451  ? UNP P36022 GLN 1668 conflict         1668 4  
1 9DKD VAL A 560  ? UNP P36022 ILE 1777 conflict         1777 5  
1 9DKD VAL A 767  ? UNP P36022 ILE 1984 conflict         1984 6  
1 9DKD VAL A 1719 ? UNP P36022 ILE 2936 conflict         2936 7  
1 9DKD GLN A 2049 ? UNP P36022 ARG 3266 conflict         3266 8  
1 9DKD GLY A 2126 ? UNP P36022 ALA 3343 conflict         3343 9  
1 9DKD VAL A 2227 ? UNP P36022 ILE 3444 conflict         3444 10 
1 9DKD ARG A 2339 ? UNP P36022 LYS 3556 conflict         3556 11 
1 9DKD ASP A 2525 ? UNP P36022 ASN 3742 conflict         3742 12 
1 9DKD VAL A 2678 ? UNP P36022 PHE 3895 conflict         3895 13 
1 9DKD ASP A 2855 ? UNP P36022 ASN 4072 conflict         4072 14 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 SER A 153  ? GLU A 163  ? SER A 1370 GLU A 1380 1 ? 11 
HELX_P HELX_P2   AA2 GLU A 180  ? LYS A 189  ? GLU A 1397 LYS A 1406 1 ? 10 
HELX_P HELX_P3   AA3 GLN A 209  ? LEU A 242  ? GLN A 1426 LEU A 1459 1 ? 34 
HELX_P HELX_P4   AA4 ASN A 245  ? ASN A 250  ? ASN A 1462 ASN A 1467 1 ? 6  
HELX_P HELX_P5   AA5 LEU A 252  ? GLN A 275  ? LEU A 1469 GLN A 1492 1 ? 24 
HELX_P HELX_P6   AA6 ASP A 289  ? PHE A 317  ? ASP A 1506 PHE A 1534 1 ? 29 
HELX_P HELX_P7   AA7 ARG A 319  ? LEU A 323  ? ARG A 1536 LEU A 1540 5 ? 5  
HELX_P HELX_P8   AA8 GLY A 324  ? SER A 334  ? GLY A 1541 SER A 1551 1 ? 11 
HELX_P HELX_P9   AA9 PHE A 344  ? GLY A 350  ? PHE A 1561 GLY A 1567 1 ? 7  
HELX_P HELX_P10  AB1 GLN A 386  ? ASP A 415  ? GLN A 1603 ASP A 1632 1 ? 30 
HELX_P HELX_P11  AB2 ASP A 418  ? VAL A 423  ? ASP A 1635 VAL A 1640 1 ? 6  
HELX_P HELX_P12  AB3 ILE A 427  ? GLN A 448  ? ILE A 1644 GLN A 1665 1 ? 22 
HELX_P HELX_P13  AB4 PHE A 452  ? LYS A 472  ? PHE A 1669 LYS A 1689 1 ? 21 
HELX_P HELX_P14  AB5 SER A 474  ? ASN A 500  ? SER A 1691 ASN A 1717 1 ? 27 
HELX_P HELX_P15  AB6 THR A 503  ? LYS A 513  ? THR A 1720 LYS A 1730 1 ? 11 
HELX_P HELX_P16  AB7 THR A 555  ? GLN A 571  ? THR A 1772 GLN A 1788 1 ? 17 
HELX_P HELX_P17  AB8 LYS A 585  ? LEU A 596  ? LYS A 1802 LEU A 1813 1 ? 12 
HELX_P HELX_P18  AB9 ASP A 610  ? GLY A 625  ? ASP A 1827 GLY A 1842 1 ? 16 
HELX_P HELX_P19  AC1 GLU A 632  ? LEU A 636  ? GLU A 1849 LEU A 1853 5 ? 5  
HELX_P HELX_P20  AC2 ASP A 637  ? VAL A 657  ? ASP A 1854 VAL A 1874 1 ? 21 
HELX_P HELX_P21  AC3 PRO A 692  ? LYS A 697  ? PRO A 1909 LYS A 1914 1 ? 6  
HELX_P HELX_P22  AC4 GLN A 708  ? GLY A 721  ? GLN A 1925 GLY A 1938 1 ? 14 
HELX_P HELX_P23  AC5 SER A 725  ? CYS A 743  ? SER A 1942 CYS A 1960 1 ? 19 
HELX_P HELX_P24  AC6 GLY A 752  ? SER A 768  ? GLY A 1969 SER A 1985 1 ? 17 
HELX_P HELX_P25  AC7 GLY A 773  ? ILE A 785  ? GLY A 1990 ILE A 2002 1 ? 13 
HELX_P HELX_P26  AC8 LEU A 786  ? LEU A 789  ? LEU A 2003 LEU A 2006 5 ? 4  
HELX_P HELX_P27  AC9 ASP A 791  ? PHE A 805  ? ASP A 2008 PHE A 2022 1 ? 15 
HELX_P HELX_P28  AD1 LYS A 815  ? GLY A 829  ? LYS A 2032 GLY A 2046 1 ? 15 
HELX_P HELX_P29  AD2 SER A 833  ? LYS A 848  ? SER A 2050 LYS A 2065 1 ? 16 
HELX_P HELX_P30  AD3 GLY A 862  ? GLY A 879  ? GLY A 2079 GLY A 2096 1 ? 18 
HELX_P HELX_P31  AD4 THR A 893  ? TYR A 898  ? THR A 2110 TYR A 2115 1 ? 6  
HELX_P HELX_P32  AD5 GLY A 911  ? ASP A 923  ? GLY A 2128 ASP A 2140 1 ? 13 
HELX_P HELX_P33  AD6 GLY A 926  ? LYS A 929  ? GLY A 2143 LYS A 2146 5 ? 4  
HELX_P HELX_P34  AD7 ASP A 942  ? GLU A 947  ? ASP A 2159 GLU A 2164 1 ? 6  
HELX_P HELX_P35  AD8 MET A 949  ? ASP A 954  ? MET A 2166 ASP A 2171 1 ? 6  
HELX_P HELX_P36  AD9 ALA A 988  ? CYS A 993  ? ALA A 2205 CYS A 2210 1 ? 6  
HELX_P HELX_P37  AE1 SER A 1004 ? LEU A 1020 ? SER A 2221 LEU A 2237 1 ? 17 
HELX_P HELX_P38  AE2 GLU A 1028 ? SER A 1039 ? GLU A 2245 SER A 2256 1 ? 12 
HELX_P HELX_P39  AE3 ASP A 1041 ? ASN A 1053 ? ASP A 2258 ASN A 2270 1 ? 13 
HELX_P HELX_P40  AE4 ARG A 1062 ? ASN A 1065 ? ARG A 2279 ASN A 2282 5 ? 4  
HELX_P HELX_P41  AE5 LYS A 1066 ? TYR A 1081 ? LYS A 2283 TYR A 2298 1 ? 16 
HELX_P HELX_P42  AE6 ARG A 1082 ? PHE A 1085 ? ARG A 2299 PHE A 2302 5 ? 4  
HELX_P HELX_P43  AE7 ASP A 1089 ? ALA A 1110 ? ASP A 2306 ALA A 2327 1 ? 22 
HELX_P HELX_P44  AE8 THR A 1114 ? GLY A 1130 ? THR A 2331 GLY A 2347 1 ? 17 
HELX_P HELX_P45  AE9 CYS A 1155 ? GLU A 1157 ? CYS A 2372 GLU A 2374 5 ? 3  
HELX_P HELX_P46  AF1 GLU A 1164 ? VAL A 1168 ? GLU A 2381 VAL A 2385 5 ? 5  
HELX_P HELX_P47  AF2 THR A 1177 ? SER A 1193 ? THR A 2394 SER A 2410 1 ? 17 
HELX_P HELX_P48  AF3 GLY A 1206 ? LEU A 1215 ? GLY A 2423 LEU A 2432 1 ? 10 
HELX_P HELX_P49  AF4 THR A 1233 ? ARG A 1243 ? THR A 2450 ARG A 2460 1 ? 11 
HELX_P HELX_P50  AF5 GLN A 1283 ? GLN A 1296 ? GLN A 2500 GLN A 2513 1 ? 14 
HELX_P HELX_P51  AF6 SER A 1330 ? ARG A 1335 ? SER A 2547 ARG A 2552 1 ? 6  
HELX_P HELX_P52  AF7 SER A 1346 ? LYS A 1363 ? SER A 2563 LYS A 2580 1 ? 18 
HELX_P HELX_P53  AF8 VAL A 1365 ? SER A 1370 ? VAL A 2582 SER A 2587 5 ? 6  
HELX_P HELX_P54  AF9 TYR A 1371 ? ARG A 1389 ? TYR A 2588 ARG A 2606 1 ? 19 
HELX_P HELX_P55  AG1 SER A 1401 ? THR A 1418 ? SER A 2618 THR A 2635 1 ? 18 
HELX_P HELX_P56  AG2 THR A 1423 ? PHE A 1439 ? THR A 2640 PHE A 2656 1 ? 17 
HELX_P HELX_P57  AG3 ALA A 1440 ? ARG A 1442 ? ALA A 2657 ARG A 2659 5 ? 3  
HELX_P HELX_P58  AG4 GLY A 1445 ? LEU A 1464 ? GLY A 2662 LEU A 2681 1 ? 20 
HELX_P HELX_P59  AG5 ASN A 1491 ? GLU A 1510 ? ASN A 2708 GLU A 2727 1 ? 20 
HELX_P HELX_P60  AG6 HIS A 1518 ? LYS A 1533 ? HIS A 2735 LYS A 2750 1 ? 16 
HELX_P HELX_P61  AG7 GLY A 1548 ? ASN A 1560 ? GLY A 2765 ASN A 2777 1 ? 13 
HELX_P HELX_P62  AG8 ASN A 1574 ? GLU A 1593 ? ASN A 2791 GLU A 2810 1 ? 20 
HELX_P HELX_P63  AG9 GLU A 1607 ? ASN A 1620 ? GLU A 2824 ASN A 2837 1 ? 14 
HELX_P HELX_P64  AH1 ILE A 1623 ? PHE A 1627 ? ILE A 2840 PHE A 2844 5 ? 5  
HELX_P HELX_P65  AH2 GLY A 1629 ? THR A 1643 ? GLY A 2846 THR A 2860 1 ? 15 
HELX_P HELX_P66  AH3 GLU A 1653 ? ASN A 1667 ? GLU A 2870 ASN A 2884 1 ? 15 
HELX_P HELX_P67  AH4 SER A 1682 ? SER A 1688 ? SER A 2899 SER A 2905 1 ? 7  
HELX_P HELX_P68  AH5 ASP A 1704 ? ASP A 1717 ? ASP A 2921 ASP A 2934 1 ? 14 
HELX_P HELX_P69  AH6 ILE A 1744 ? MET A 1763 ? ILE A 2961 MET A 2980 1 ? 20 
HELX_P HELX_P70  AH7 PRO A 1772 ? ASN A 1808 ? PRO A 2989 ASN A 3025 1 ? 37 
HELX_P HELX_P71  AH8 LEU A 2082 ? PHE A 2117 ? LEU A 3299 PHE A 3334 1 ? 36 
HELX_P HELX_P72  AH9 ASN A 2121 ? ALA A 2140 ? ASN A 3338 ALA A 3357 1 ? 20 
HELX_P HELX_P73  AI1 ARG A 2148 ? VAL A 2154 ? ARG A 3365 VAL A 3371 1 ? 7  
HELX_P HELX_P74  AI2 THR A 2155 ? GLY A 2166 ? THR A 3372 GLY A 3383 1 ? 12 
HELX_P HELX_P75  AI3 ASN A 2170 ? ASN A 2182 ? ASN A 3387 ASN A 3399 1 ? 13 
HELX_P HELX_P76  AI4 SER A 2195 ? GLY A 2206 ? SER A 3412 GLY A 3423 1 ? 12 
HELX_P HELX_P77  AI5 PHE A 2219 ? GLY A 2230 ? PHE A 3436 GLY A 3447 1 ? 12 
HELX_P HELX_P78  AI6 ASP A 2237 ? PHE A 2241 ? ASP A 3454 PHE A 3458 5 ? 5  
HELX_P HELX_P79  AI7 ILE A 2245 ? ARG A 2251 ? ILE A 3462 ARG A 3468 1 ? 7  
HELX_P HELX_P80  AI8 PRO A 2289 ? SER A 2294 ? PRO A 3506 SER A 3511 1 ? 6  
HELX_P HELX_P81  AI9 ASN A 2304 ? GLU A 2320 ? ASN A 3521 GLU A 3537 1 ? 17 
HELX_P HELX_P82  AJ1 ASN A 2321 ? ASN A 2355 ? ASN A 3538 ASN A 3572 1 ? 35 
HELX_P HELX_P83  AJ2 GLU A 2376 ? GLU A 2388 ? GLU A 3593 GLU A 3605 1 ? 13 
HELX_P HELX_P84  AJ3 PHE A 2390 ? TYR A 2401 ? PHE A 3607 TYR A 3618 1 ? 12 
HELX_P HELX_P85  AJ4 SER A 2402 ? HIS A 2422 ? SER A 3619 HIS A 3639 1 ? 21 
HELX_P HELX_P86  AJ5 SER A 2428 ? LYS A 2442 ? SER A 3645 LYS A 3659 1 ? 15 
HELX_P HELX_P87  AJ6 ARG A 2453 ? SER A 2470 ? ARG A 3670 SER A 3687 1 ? 18 
HELX_P HELX_P88  AJ7 ASP A 2474 ? PHE A 2491 ? ASP A 3691 PHE A 3708 1 ? 18 
HELX_P HELX_P89  AJ8 SER A 2495 ? SER A 2510 ? SER A 3712 SER A 3727 1 ? 16 
HELX_P HELX_P90  AJ9 ASP A 2525 ? THR A 2535 ? ASP A 3742 THR A 3752 1 ? 11 
HELX_P HELX_P91  AK1 SER A 2538 ? PHE A 2551 ? SER A 3755 PHE A 3768 1 ? 14 
HELX_P HELX_P92  AK2 ASN A 2556 ? ASN A 2563 ? ASN A 3773 ASN A 3780 1 ? 8  
HELX_P HELX_P93  AK3 GLY A 2579 ? LYS A 2591 ? GLY A 3796 LYS A 3808 1 ? 13 
HELX_P HELX_P94  AK4 SER A 2601 ? GLY A 2619 ? SER A 3818 GLY A 3836 1 ? 19 
HELX_P HELX_P95  AK5 SER A 2630 ? GLU A 2643 ? SER A 3847 GLU A 3860 1 ? 14 
HELX_P HELX_P96  AK6 PRO A 2668 ? ARG A 2674 ? PRO A 3885 ARG A 3891 1 ? 7  
HELX_P HELX_P97  AK7 GLY A 2685 ? GLN A 2697 ? GLY A 3902 GLN A 3914 1 ? 13 
HELX_P HELX_P98  AK8 VAL A 2706 ? ARG A 2727 ? VAL A 3923 ARG A 3944 1 ? 22 
HELX_P HELX_P99  AK9 ASN A 2740 ? ASN A 2758 ? ASN A 3957 ASN A 3975 1 ? 19 
HELX_P HELX_P100 AL1 PRO A 2764 ? ILE A 2775 ? PRO A 3981 ILE A 3992 1 ? 12 
HELX_P HELX_P101 AL2 GLU A 2783 ? PHE A 2798 ? GLU A 4000 PHE A 4015 1 ? 16 
HELX_P HELX_P102 AL3 SER A 2820 ? THR A 2835 ? SER A 4037 THR A 4052 1 ? 16 
HELX_P HELX_P103 AL4 PRO A 2849 ? GLN A 2873 ? PRO A 4066 GLN A 4090 1 ? 25 
# 
_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 
metalc1 metalc ? ? A THR 1208 OG1 ? ? ? 1_555 F MG . MG ? ? A THR 2425 A MG 4105 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc2 metalc ? ? A ASP 1270 OD2 ? ? ? 1_555 F MG . MG ? ? A ASP 2487 A MG 4105 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc3 metalc ? ? E ADP .    O2B ? ? ? 1_555 F MG . MG ? ? A ADP 4104 A MG 4105 1_555 ? ? ? ? ? ? ? 2.414 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG1 ? A THR 1208 ? A THR 2425 ? 1_555 MG ? F MG . ? A MG 4105 ? 1_555 OD2 ? A ASP 1270 ? A ASP 2487 ? 1_555 95.3  ? 
2 OG1 ? A THR 1208 ? A THR 2425 ? 1_555 MG ? F MG . ? A MG 4105 ? 1_555 O2B ? E ADP .    ? A ADP 4104 ? 1_555 84.0  ? 
3 OD2 ? A ASP 1270 ? A ASP 2487 ? 1_555 MG ? F MG . ? A MG 4105 ? 1_555 O2B ? E ADP .    ? A ADP 4104 ? 1_555 156.2 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 5 ? 
AA9 ? 4 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 5 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA9 1 2 ? anti-parallel 
AA9 2 3 ? parallel      
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 354  ? PHE A 357  ? SER A 1571 PHE A 1574 
AA1 2 SER A 361  ? ARG A 366  ? SER A 1578 ARG A 1583 
AA1 3 VAL A 372  ? GLU A 380  ? VAL A 1589 GLU A 1597 
AA2 1 LYS A 516  ? PHE A 517  ? LYS A 1733 PHE A 1734 
AA2 2 PHE A 531  ? GLN A 534  ? PHE A 1748 GLN A 1751 
AA2 3 TYR A 537  ? GLN A 540  ? TYR A 1754 GLN A 1757 
AA3 1 VAL A 600  ? ASN A 604  ? VAL A 1817 ASN A 1821 
AA3 2 TRP A 627  ? ASP A 631  ? TRP A 1844 ASP A 1848 
AA3 3 ALA A 676  ? LEU A 681  ? ALA A 1893 LEU A 1898 
AA3 4 GLY A 574  ? PHE A 578  ? GLY A 1791 PHE A 1795 
AA3 5 PHE A 699  ? ARG A 700  ? PHE A 1916 ARG A 1917 
AA4 1 HIS A 661  ? LEU A 664  ? HIS A 1878 LEU A 1881 
AA4 2 GLU A 667  ? PRO A 670  ? GLU A 1884 PRO A 1887 
AA5 1 ALA A 881  ? VAL A 886  ? ALA A 2098 VAL A 2103 
AA5 2 SER A 931  ? PHE A 937  ? SER A 2148 PHE A 2154 
AA5 3 PHE A 973  ? THR A 979  ? PHE A 2190 THR A 2196 
AA5 4 ALA A 852  ? GLY A 857  ? ALA A 2069 GLY A 2074 
AA5 5 GLY A 994  ? PHE A 998  ? GLY A 2211 PHE A 2215 
AA6 1 SER A 1140 ? VAL A 1143 ? SER A 2357 VAL A 2360 
AA6 2 SER A 1150 ? SER A 1153 ? SER A 2367 SER A 2370 
AA7 1 TYR A 1221 ? VAL A 1223 ? TYR A 2438 VAL A 2440 
AA7 2 ASN A 1264 ? ASP A 1270 ? ASN A 2481 ASP A 2487 
AA7 3 ILE A 1226 ? ASN A 1227 ? ILE A 2443 ASN A 2444 
AA8 1 TYR A 1221 ? VAL A 1223 ? TYR A 2438 VAL A 2440 
AA8 2 ASN A 1264 ? ASP A 1270 ? ASN A 2481 ASP A 2487 
AA8 3 ILE A 1312 ? CYS A 1318 ? ILE A 2529 CYS A 2535 
AA8 4 GLY A 1196 ? CYS A 1200 ? GLY A 2413 CYS A 2417 
AA8 5 ALA A 1337 ? TYR A 1341 ? ALA A 2554 TYR A 2558 
AA9 1 THR A 1245 ? VAL A 1248 ? THR A 2462 VAL A 2465 
AA9 2 THR A 1255 ? PRO A 1258 ? THR A 2472 PRO A 2475 
AA9 3 TRP A 1306 ? ILE A 1309 ? TRP A 2523 ILE A 2526 
AA9 4 GLY A 1297 ? TRP A 1299 ? GLY A 2514 TRP A 2516 
AB1 1 PHE A 1479 ? SER A 1480 ? PHE A 2696 SER A 2697 
AB1 2 LYS A 1488 ? GLU A 1489 ? LYS A 2705 GLU A 2706 
AB2 1 LYS A 1563 ? VAL A 1565 ? LYS A 2780 VAL A 2782 
AB2 2 THR A 1596 ? ASP A 1601 ? THR A 2813 ASP A 2818 
AB2 3 HIS A 1669 ? ILE A 1674 ? HIS A 2886 ILE A 2891 
AB2 4 HIS A 1538 ? ILE A 1542 ? HIS A 2755 ILE A 2759 
AB2 5 CYS A 1695 ? TRP A 1699 ? CYS A 2912 TRP A 2916 
AB3 1 THR A 2209 ? LEU A 2212 ? THR A 3426 LEU A 3429 
AB3 2 VAL A 2232 ? ILE A 2235 ? VAL A 3449 ILE A 3452 
AB3 3 LEU A 2277 ? SER A 2281 ? LEU A 3494 SER A 3498 
AB3 4 PRO A 2188 ? LEU A 2191 ? PRO A 3405 LEU A 3408 
AB3 5 ARG A 2297 ? HIS A 2300 ? ARG A 3514 HIS A 3517 
AB4 1 THR A 2261 ? ILE A 2264 ? THR A 3478 ILE A 3481 
AB4 2 HIS A 2267 ? ASP A 2270 ? HIS A 3484 ASP A 3487 
AB5 1 LEU A 2594 ? PRO A 2598 ? LEU A 3811 PRO A 3815 
AB5 2 GLY A 2620 ? GLN A 2625 ? GLY A 3837 GLN A 3842 
AB5 3 PHE A 2654 ? HIS A 2661 ? PHE A 3871 HIS A 3878 
AB5 4 PHE A 2569 ? SER A 2573 ? PHE A 3786 SER A 3790 
AB5 5 ASP A 2676 ? TYR A 2680 ? ASP A 3893 TYR A 3897 
# 
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 SER A 354  ? N SER A 1571 O ARG A 366  ? O ARG A 1583 
AA1 2 3 N VAL A 365  ? N VAL A 1582 O LEU A 373  ? O LEU A 1590 
AA2 1 2 N LYS A 516  ? N LYS A 1733 O SER A 533  ? O SER A 1750 
AA2 2 3 N ILE A 532  ? N ILE A 1749 O LEU A 539  ? O LEU A 1756 
AA3 1 2 N PHE A 603  ? N PHE A 1820 O CYS A 629  ? O CYS A 1846 
AA3 2 3 N PHE A 630  ? N PHE A 1847 O PHE A 678  ? O PHE A 1895 
AA3 3 4 O LEU A 681  ? O LEU A 1898 N PHE A 577  ? N PHE A 1794 
AA3 4 5 N GLY A 574  ? N GLY A 1791 O ARG A 700  ? O ARG A 1917 
AA4 1 2 N ILE A 662  ? N ILE A 1879 O THR A 669  ? O THR A 1886 
AA5 1 2 N TYR A 885  ? N TYR A 2102 O VAL A 936  ? O VAL A 2153 
AA5 2 3 N PHE A 937  ? N PHE A 2154 O LEU A 976  ? O LEU A 2193 
AA5 3 4 O THR A 979  ? O THR A 2196 N LEU A 855  ? N LEU A 2072 
AA5 4 5 N ILE A 854  ? N ILE A 2071 O LEU A 996  ? O LEU A 2213 
AA6 1 2 N VAL A 1143 ? N VAL A 2360 O SER A 1150 ? O SER A 2367 
AA7 1 2 N ASP A 1222 ? N ASP A 2439 O VAL A 1266 ? O VAL A 2483 
AA7 2 3 O ASP A 1270 ? O ASP A 2487 N ILE A 1226 ? N ILE A 2443 
AA8 1 2 N ASP A 1222 ? N ASP A 2439 O VAL A 1266 ? O VAL A 2483 
AA8 2 3 N LEU A 1265 ? N LEU A 2482 O HIS A 1313 ? O HIS A 2530 
AA8 3 4 O GLY A 1316 ? O GLY A 2533 N ILE A 1197 ? N ILE A 2414 
AA8 4 5 N ILE A 1198 ? N ILE A 2415 O LEU A 1340 ? O LEU A 2557 
AA9 1 2 N ASN A 1246 ? N ASN A 2463 O LEU A 1257 ? O LEU A 2474 
AA9 2 3 N LEU A 1256 ? N LEU A 2473 O THR A 1308 ? O THR A 2525 
AA9 3 4 O VAL A 1307 ? O VAL A 2524 N PHE A 1298 ? N PHE A 2515 
AB1 1 2 N SER A 1480 ? N SER A 2697 O LYS A 1488 ? O LYS A 2705 
AB2 1 2 N LYS A 1563 ? N LYS A 2780 O CYS A 1597 ? O CYS A 2814 
AB2 2 3 N LEU A 1598 ? N LEU A 2815 O VAL A 1671 ? O VAL A 2888 
AB2 3 4 O PHE A 1672 ? O PHE A 2889 N MET A 1539 ? N MET A 2756 
AB2 4 5 N ILE A 1542 ? N ILE A 2759 O ASN A 1698 ? O ASN A 2915 
AB3 1 2 N LEU A 2212 ? N LEU A 3429 O ILE A 2234 ? O ILE A 3451 
AB3 2 3 N ILE A 2235 ? N ILE A 3452 O HIS A 2280 ? O HIS A 3497 
AB3 3 4 O ILE A 2279 ? O ILE A 3496 N LEU A 2190 ? N LEU A 3407 
AB3 4 5 N PHE A 2189 ? N PHE A 3406 O ARG A 2297 ? O ARG A 3514 
AB4 1 2 N VAL A 2262 ? N VAL A 3479 O VAL A 2269 ? O VAL A 3486 
AB5 1 2 N ILE A 2597 ? N ILE A 3814 O LEU A 2623 ? O LEU A 3840 
AB5 2 3 N ILE A 2622 ? N ILE A 3839 O PHE A 2657 ? O PHE A 3874 
AB5 3 4 O MET A 2658 ? O MET A 3875 N MET A 2571 ? N MET A 3788 
AB5 4 5 N THR A 2570 ? N THR A 3787 O ASP A 2676 ? O ASP A 3893 
# 
_pdbx_entry_details.entry_id                   9DKD 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 1389 ? ? 57.60   -124.39 
2  1 GLN A 1557 ? ? 71.33   -7.08   
3  1 SER A 1962 ? ? -92.20  53.32   
4  1 SER A 2156 ? ? -161.58 -169.28 
5  1 TYR A 2615 ? ? -93.49  53.19   
6  1 ALA A 2657 ? ? -91.55  50.55   
7  1 GLU A 2729 ? ? -92.88  48.88   
8  1 PHE A 2909 ? ? -67.30  0.59    
9  1 PHE A 3607 ? ? -131.05 -35.12  
10 1 GLU A 3711 ? ? -126.75 -169.91 
11 1 LYS A 3735 ? ? -94.55  59.40   
12 1 SER A 3847 ? ? -101.59 79.49   
13 1 THR A 3853 ? ? -90.43  -62.39  
14 1 THR A 3880 ? ? -90.50  58.32   
15 1 PHE A 4015 ? ? -98.66  37.28   
16 1 PRO A 4025 ? ? -58.97  -4.22   
17 1 LEU A 4034 ? ? -96.70  33.97   
18 1 ASP A 4057 ? ? -97.42  33.52   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DKD 
_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                    9DKD 
_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                  3.3 
_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               119768 
_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       '50 mM TrisHCl [pH 8.0], 150 mM KOAc, 2 mM MgOAc, 1mM EGTA,  1 mM DTT' 
_em_buffer.pH            8 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'yeast dynein in the presence of ATP and PAC1' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9DKD 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             750 
_em_imaging.nominal_defocus_max             2800 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9DKD 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277.15 
_em_vitrification.instrument            'FEI VITROBOT MARK II' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9DKD 
_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 GLY 1218 ? A GLY 1    
2   1 Y 1 A ASP 1219 ? A ASP 2    
3   1 Y 1 A GLN 1220 ? A GLN 3    
4   1 Y 1 A LEU 1221 ? A LEU 4    
5   1 Y 1 A THR 1222 ? A THR 5    
6   1 Y 1 A HIS 1223 ? A HIS 6    
7   1 Y 1 A VAL 1224 ? A VAL 7    
8   1 Y 1 A VAL 1225 ? A VAL 8    
9   1 Y 1 A GLU 1226 ? A GLU 9    
10  1 Y 1 A GLU 1227 ? A GLU 10   
11  1 Y 1 A VAL 1228 ? A VAL 11   
12  1 Y 1 A LYS 1229 ? A LYS 12   
13  1 Y 1 A THR 1230 ? A THR 13   
14  1 Y 1 A TYR 1231 ? A TYR 14   
15  1 Y 1 A ASP 1232 ? A ASP 15   
16  1 Y 1 A LEU 1233 ? A LEU 16   
17  1 Y 1 A VAL 1234 ? A VAL 17   
18  1 Y 1 A TRP 1235 ? A TRP 18   
19  1 Y 1 A ARG 1236 ? A ARG 19   
20  1 Y 1 A SER 1237 ? A SER 20   
21  1 Y 1 A ILE 1238 ? A ILE 21   
22  1 Y 1 A LYS 1239 ? A LYS 22   
23  1 Y 1 A ASN 1240 ? A ASN 23   
24  1 Y 1 A LEU 1241 ? A LEU 24   
25  1 Y 1 A TRP 1242 ? A TRP 25   
26  1 Y 1 A GLU 1243 ? A GLU 26   
27  1 Y 1 A ASP 1244 ? A ASP 27   
28  1 Y 1 A VAL 1245 ? A VAL 28   
29  1 Y 1 A GLN 1246 ? A GLN 29   
30  1 Y 1 A ARG 1247 ? A ARG 30   
31  1 Y 1 A THR 1248 ? A THR 31   
32  1 Y 1 A PHE 1249 ? A PHE 32   
33  1 Y 1 A GLU 1250 ? A GLU 33   
34  1 Y 1 A THR 1251 ? A THR 34   
35  1 Y 1 A PRO 1252 ? A PRO 35   
36  1 Y 1 A TRP 1253 ? A TRP 36   
37  1 Y 1 A CYS 1254 ? A CYS 37   
38  1 Y 1 A ARG 1255 ? A ARG 38   
39  1 Y 1 A VAL 1256 ? A VAL 39   
40  1 Y 1 A ASP 1257 ? A ASP 40   
41  1 Y 1 A VAL 1258 ? A VAL 41   
42  1 Y 1 A LEU 1259 ? A LEU 42   
43  1 Y 1 A LEU 1260 ? A LEU 43   
44  1 Y 1 A LEU 1261 ? A LEU 44   
45  1 Y 1 A GLN 1262 ? A GLN 45   
46  1 Y 1 A SER 1263 ? A SER 46   
47  1 Y 1 A ASP 1264 ? A ASP 47   
48  1 Y 1 A LEU 1265 ? A LEU 48   
49  1 Y 1 A ALA 1266 ? A ALA 49   
50  1 Y 1 A ASN 1267 ? A ASN 50   
51  1 Y 1 A PHE 1268 ? A PHE 51   
52  1 Y 1 A LEU 1269 ? A LEU 52   
53  1 Y 1 A ARG 1270 ? A ARG 53   
54  1 Y 1 A ARG 1271 ? A ARG 54   
55  1 Y 1 A ALA 1272 ? A ALA 55   
56  1 Y 1 A ASP 1273 ? A ASP 56   
57  1 Y 1 A GLU 1274 ? A GLU 57   
58  1 Y 1 A LEU 1275 ? A LEU 58   
59  1 Y 1 A PRO 1276 ? A PRO 59   
60  1 Y 1 A ARG 1277 ? A ARG 60   
61  1 Y 1 A ALA 1278 ? A ALA 61   
62  1 Y 1 A VAL 1279 ? A VAL 62   
63  1 Y 1 A LYS 1280 ? A LYS 63   
64  1 Y 1 A GLN 1281 ? A GLN 64   
65  1 Y 1 A PHE 1282 ? A PHE 65   
66  1 Y 1 A GLU 1283 ? A GLU 66   
67  1 Y 1 A MET 1284 ? A MET 67   
68  1 Y 1 A TYR 1285 ? A TYR 68   
69  1 Y 1 A LYS 1286 ? A LYS 69   
70  1 Y 1 A SER 1287 ? A SER 70   
71  1 Y 1 A LEU 1288 ? A LEU 71   
72  1 Y 1 A PHE 1289 ? A PHE 72   
73  1 Y 1 A SER 1290 ? A SER 73   
74  1 Y 1 A GLN 1291 ? A GLN 74   
75  1 Y 1 A VAL 1292 ? A VAL 75   
76  1 Y 1 A ASN 1293 ? A ASN 76   
77  1 Y 1 A MET 1294 ? A MET 77   
78  1 Y 1 A LEU 1295 ? A LEU 78   
79  1 Y 1 A THR 1296 ? A THR 79   
80  1 Y 1 A SER 1297 ? A SER 80   
81  1 Y 1 A VAL 1298 ? A VAL 81   
82  1 Y 1 A ASN 1299 ? A ASN 82   
83  1 Y 1 A LYS 1300 ? A LYS 83   
84  1 Y 1 A ILE 1301 ? A ILE 84   
85  1 Y 1 A LEU 1302 ? A LEU 85   
86  1 Y 1 A VAL 1303 ? A VAL 86   
87  1 Y 1 A GLU 1304 ? A GLU 87   
88  1 Y 1 A LEU 1305 ? A LEU 88   
89  1 Y 1 A LYS 1306 ? A LYS 89   
90  1 Y 1 A ASP 1307 ? A ASP 90   
91  1 Y 1 A GLY 1308 ? A GLY 91   
92  1 Y 1 A ALA 1309 ? A ALA 92   
93  1 Y 1 A LEU 1310 ? A LEU 93   
94  1 Y 1 A LYS 1311 ? A LYS 94   
95  1 Y 1 A PRO 1312 ? A PRO 95   
96  1 Y 1 A ARG 1313 ? A ARG 96   
97  1 Y 1 A HIS 1314 ? A HIS 97   
98  1 Y 1 A TRP 1315 ? A TRP 98   
99  1 Y 1 A ASN 1316 ? A ASN 99   
100 1 Y 1 A MET 1317 ? A MET 100  
101 1 Y 1 A ILE 1318 ? A ILE 101  
102 1 Y 1 A PHE 1319 ? A PHE 102  
103 1 Y 1 A ARG 1320 ? A ARG 103  
104 1 Y 1 A ASP 1321 ? A ASP 104  
105 1 Y 1 A ILE 1322 ? A ILE 105  
106 1 Y 1 A GLY 1323 ? A GLY 106  
107 1 Y 1 A LYS 1324 ? A LYS 107  
108 1 Y 1 A ARG 1325 ? A ARG 108  
109 1 Y 1 A GLN 1326 ? A GLN 109  
110 1 Y 1 A ILE 1327 ? A ILE 110  
111 1 Y 1 A GLN 1328 ? A GLN 111  
112 1 Y 1 A LYS 1329 ? A LYS 112  
113 1 Y 1 A ASN 1330 ? A ASN 113  
114 1 Y 1 A LEU 1331 ? A LEU 114  
115 1 Y 1 A LEU 1332 ? A LEU 115  
116 1 Y 1 A ASP 1333 ? A ASP 116  
117 1 Y 1 A LYS 1334 ? A LYS 117  
118 1 Y 1 A LEU 1335 ? A LEU 118  
119 1 Y 1 A GLU 1336 ? A GLU 119  
120 1 Y 1 A PHE 1337 ? A PHE 120  
121 1 Y 1 A SER 1338 ? A SER 121  
122 1 Y 1 A LEU 1339 ? A LEU 122  
123 1 Y 1 A LYS 1340 ? A LYS 123  
124 1 Y 1 A ASP 1341 ? A ASP 124  
125 1 Y 1 A VAL 1342 ? A VAL 125  
126 1 Y 1 A MET 1343 ? A MET 126  
127 1 Y 1 A VAL 1344 ? A VAL 127  
128 1 Y 1 A LEU 1345 ? A LEU 128  
129 1 Y 1 A ASN 1346 ? A ASN 129  
130 1 Y 1 A LEU 1347 ? A LEU 130  
131 1 Y 1 A THR 1348 ? A THR 131  
132 1 Y 1 A LEU 1349 ? A LEU 132  
133 1 Y 1 A ASN 1350 ? A ASN 133  
134 1 Y 1 A GLU 1351 ? A GLU 134  
135 1 Y 1 A ILE 1352 ? A ILE 135  
136 1 Y 1 A LEU 1353 ? A LEU 136  
137 1 Y 1 A LEU 1354 ? A LEU 137  
138 1 Y 1 A THR 1355 ? A THR 138  
139 1 Y 1 A LYS 1356 ? A LYS 139  
140 1 Y 1 A ILE 1357 ? A ILE 140  
141 1 Y 1 A ILE 1358 ? A ILE 141  
142 1 Y 1 A GLU 1359 ? A GLU 142  
143 1 Y 1 A ARG 1360 ? A ARG 143  
144 1 Y 1 A ALA 1361 ? A ALA 144  
145 1 Y 1 A GLN 1362 ? A GLN 145  
146 1 Y 1 A LYS 1363 ? A LYS 146  
147 1 Y 1 A GLU 1364 ? A GLU 147  
148 1 Y 1 A PHE 1365 ? A PHE 148  
149 1 Y 1 A VAL 1366 ? A VAL 149  
150 1 Y 1 A ILE 1367 ? A ILE 150  
151 1 Y 1 A GLU 1368 ? A GLU 151  
152 1 Y 1 A LYS 1369 ? A LYS 152  
153 1 Y 1 A GLU 1407 ? A GLU 190  
154 1 Y 1 A ASP 1408 ? A ASP 191  
155 1 Y 1 A LEU 1409 ? A LEU 192  
156 1 Y 1 A GLU 1410 ? A GLU 193  
157 1 Y 1 A GLU 1411 ? A GLU 194  
158 1 Y 1 A LEU 1412 ? A LEU 195  
159 1 Y 1 A VAL 1413 ? A VAL 196  
160 1 Y 1 A SER 1414 ? A SER 197  
161 1 Y 1 A MET 1415 ? A MET 198  
162 1 Y 1 A LYS 1416 ? A LYS 199  
163 1 Y 1 A ALA 1417 ? A ALA 200  
164 1 Y 1 A SER 1418 ? A SER 201  
165 1 Y 1 A ASN 1419 ? A ASN 202  
166 1 Y 1 A TYR 1420 ? A TYR 203  
167 1 Y 1 A TYR 1421 ? A TYR 204  
168 1 Y 1 A LYS 1422 ? A LYS 205  
169 1 Y 1 A ILE 1423 ? A ILE 206  
170 1 Y 1 A PHE 1424 ? A PHE 207  
171 1 Y 1 A LEU 1493 ? A LEU 276  
172 1 Y 1 A ASP 1494 ? A ASP 277  
173 1 Y 1 A THR 1495 ? A THR 278  
174 1 Y 1 A THR 1496 ? A THR 279  
175 1 Y 1 A ILE 1497 ? A ILE 280  
176 1 Y 1 A GLU 1498 ? A GLU 281  
177 1 Y 1 A VAL 1499 ? A VAL 282  
178 1 Y 1 A ILE 1500 ? A ILE 283  
179 1 Y 1 A HIS 1501 ? A HIS 284  
180 1 Y 1 A ILE 1502 ? A ILE 285  
181 1 Y 1 A PRO 1503 ? A PRO 286  
182 1 Y 1 A ASN 1504 ? A ASN 287  
183 1 Y 1 A ASN 1903 ? A ASN 686  
184 1 Y 1 A GLY 1904 ? A GLY 687  
185 1 Y 1 A ALA 2025 ? A ALA 808  
186 1 Y 1 A GLY 2026 ? A GLY 809  
187 1 Y 1 A THR 2027 ? A THR 810  
188 1 Y 1 A PRO 2028 ? A PRO 811  
189 1 Y 1 A LEU 2029 ? A LEU 812  
190 1 Y 1 A ASN 2030 ? A ASN 813  
191 1 Y 1 A ASP 2238 ? A ASP 1021 
192 1 Y 1 A ASN 2239 ? A ASN 1022 
193 1 Y 1 A LYS 2240 ? A LYS 1023 
194 1 Y 1 A LEU 2241 ? A LEU 1024 
195 1 Y 1 A SER 2242 ? A SER 1025 
196 1 Y 1 A MET 2243 ? A MET 1026 
197 1 Y 1 A ALA 2362 ? A ALA 1145 
198 1 Y 1 A ASN 2363 ? A ASN 1146 
199 1 Y 1 A ASP 2364 ? A ASP 1147 
200 1 Y 1 A LYS 2365 ? A LYS 1148 
201 1 Y 1 A THR 2467 ? A THR 1250 
202 1 Y 1 A SER 2468 ? A SER 1251 
203 1 Y 1 A LYS 2469 ? A LYS 1252 
204 1 Y 1 A ASN 2683 ? A ASN 1466 
205 1 Y 1 A GLN 2684 ? A GLN 1467 
206 1 Y 1 A ASP 2685 ? A ASP 1468 
207 1 Y 1 A HIS 2787 ? A HIS 1570 
208 1 Y 1 A ARG 2861 ? A ARG 1644 
209 1 Y 1 A SER 2862 ? A SER 1645 
210 1 Y 1 A LEU 2863 ? A LEU 1646 
211 1 Y 1 A GLY 2864 ? A GLY 1647 
212 1 Y 1 A LEU 2865 ? A LEU 1648 
213 1 Y 1 A LEU 2866 ? A LEU 1649 
214 1 Y 1 A LEU 2867 ? A LEU 1650 
215 1 Y 1 A ASP 2868 ? A ASP 1651 
216 1 Y 1 A THR 2895 ? A THR 1678 
217 1 Y 1 A ASN 2896 ? A ASN 1679 
218 1 Y 1 A ASN 2897 ? A ASN 1680 
219 1 Y 1 A ASP 2942 ? A ASP 1725 
220 1 Y 1 A PHE 2943 ? A PHE 1726 
221 1 Y 1 A ILE 2944 ? A ILE 1727 
222 1 Y 1 A VAL 2945 ? A VAL 1728 
223 1 Y 1 A PRO 2946 ? A PRO 1729 
224 1 Y 1 A GLU 2947 ? A GLU 1730 
225 1 Y 1 A VAL 2948 ? A VAL 1731 
226 1 Y 1 A ASN 2949 ? A ASN 1732 
227 1 Y 1 A LYS 2950 ? A LYS 1733 
228 1 Y 1 A GLU 2951 ? A GLU 1734 
229 1 Y 1 A LEU 2952 ? A LEU 1735 
230 1 Y 1 A VAL 2953 ? A VAL 1736 
231 1 Y 1 A PHE 2954 ? A PHE 1737 
232 1 Y 1 A THR 2955 ? A THR 1738 
233 1 Y 1 A GLU 2956 ? A GLU 1739 
234 1 Y 1 A PRO 2957 ? A PRO 1740 
235 1 Y 1 A ILE 2958 ? A ILE 1741 
236 1 Y 1 A GLN 2959 ? A GLN 1742 
237 1 Y 1 A LYS 2981 ? A LYS 1764 
238 1 Y 1 A VAL 2982 ? A VAL 1765 
239 1 Y 1 A GLY 2983 ? A GLY 1766 
240 1 Y 1 A VAL 2984 ? A VAL 1767 
241 1 Y 1 A GLU 3026 ? A GLU 1809 
242 1 Y 1 A SER 3027 ? A SER 1810 
243 1 Y 1 A VAL 3028 ? A VAL 1811 
244 1 Y 1 A LEU 3029 ? A LEU 1812 
245 1 Y 1 A LYS 3030 ? A LYS 1813 
246 1 Y 1 A VAL 3031 ? A VAL 1814 
247 1 Y 1 A ASN 3032 ? A ASN 1815 
248 1 Y 1 A GLU 3033 ? A GLU 1816 
249 1 Y 1 A LEU 3034 ? A LEU 1817 
250 1 Y 1 A ASN 3035 ? A ASN 1818 
251 1 Y 1 A LYS 3036 ? A LYS 1819 
252 1 Y 1 A THR 3037 ? A THR 1820 
253 1 Y 1 A LEU 3038 ? A LEU 1821 
254 1 Y 1 A SER 3039 ? A SER 1822 
255 1 Y 1 A LYS 3040 ? A LYS 1823 
256 1 Y 1 A LYS 3041 ? A LYS 1824 
257 1 Y 1 A SER 3042 ? A SER 1825 
258 1 Y 1 A THR 3043 ? A THR 1826 
259 1 Y 1 A GLU 3044 ? A GLU 1827 
260 1 Y 1 A LEU 3045 ? A LEU 1828 
261 1 Y 1 A THR 3046 ? A THR 1829 
262 1 Y 1 A GLU 3047 ? A GLU 1830 
263 1 Y 1 A LYS 3048 ? A LYS 1831 
264 1 Y 1 A GLU 3049 ? A GLU 1832 
265 1 Y 1 A LYS 3050 ? A LYS 1833 
266 1 Y 1 A GLU 3051 ? A GLU 1834 
267 1 Y 1 A ALA 3052 ? A ALA 1835 
268 1 Y 1 A ARG 3053 ? A ARG 1836 
269 1 Y 1 A SER 3054 ? A SER 1837 
270 1 Y 1 A THR 3055 ? A THR 1838 
271 1 Y 1 A LEU 3056 ? A LEU 1839 
272 1 Y 1 A ASP 3057 ? A ASP 1840 
273 1 Y 1 A LYS 3058 ? A LYS 1841 
274 1 Y 1 A MET 3059 ? A MET 1842 
275 1 Y 1 A LEU 3060 ? A LEU 1843 
276 1 Y 1 A MET 3061 ? A MET 1844 
277 1 Y 1 A GLU 3062 ? A GLU 1845 
278 1 Y 1 A GLN 3063 ? A GLN 1846 
279 1 Y 1 A ASN 3064 ? A ASN 1847 
280 1 Y 1 A GLU 3065 ? A GLU 1848 
281 1 Y 1 A SER 3066 ? A SER 1849 
282 1 Y 1 A GLU 3067 ? A GLU 1850 
283 1 Y 1 A ARG 3068 ? A ARG 1851 
284 1 Y 1 A LYS 3069 ? A LYS 1852 
285 1 Y 1 A GLN 3070 ? A GLN 1853 
286 1 Y 1 A GLU 3071 ? A GLU 1854 
287 1 Y 1 A ALA 3072 ? A ALA 1855 
288 1 Y 1 A THR 3073 ? A THR 1856 
289 1 Y 1 A GLU 3074 ? A GLU 1857 
290 1 Y 1 A GLU 3075 ? A GLU 1858 
291 1 Y 1 A ILE 3076 ? A ILE 1859 
292 1 Y 1 A LYS 3077 ? A LYS 1860 
293 1 Y 1 A LYS 3078 ? A LYS 1861 
294 1 Y 1 A ILE 3079 ? A ILE 1862 
295 1 Y 1 A LEU 3080 ? A LEU 1863 
296 1 Y 1 A LYS 3081 ? A LYS 1864 
297 1 Y 1 A VAL 3082 ? A VAL 1865 
298 1 Y 1 A GLN 3083 ? A GLN 1866 
299 1 Y 1 A GLU 3084 ? A GLU 1867 
300 1 Y 1 A GLU 3085 ? A GLU 1868 
301 1 Y 1 A ASP 3086 ? A ASP 1869 
302 1 Y 1 A ILE 3087 ? A ILE 1870 
303 1 Y 1 A ARG 3088 ? A ARG 1871 
304 1 Y 1 A LYS 3089 ? A LYS 1872 
305 1 Y 1 A ARG 3090 ? A ARG 1873 
306 1 Y 1 A LYS 3091 ? A LYS 1874 
307 1 Y 1 A GLU 3092 ? A GLU 1875 
308 1 Y 1 A VAL 3093 ? A VAL 1876 
309 1 Y 1 A VAL 3094 ? A VAL 1877 
310 1 Y 1 A MET 3095 ? A MET 1878 
311 1 Y 1 A LYS 3096 ? A LYS 1879 
312 1 Y 1 A SER 3097 ? A SER 1880 
313 1 Y 1 A ILE 3098 ? A ILE 1881 
314 1 Y 1 A GLN 3099 ? A GLN 1882 
315 1 Y 1 A ASP 3100 ? A ASP 1883 
316 1 Y 1 A ILE 3101 ? A ILE 1884 
317 1 Y 1 A GLU 3102 ? A GLU 1885 
318 1 Y 1 A PRO 3103 ? A PRO 1886 
319 1 Y 1 A THR 3104 ? A THR 1887 
320 1 Y 1 A ILE 3105 ? A ILE 1888 
321 1 Y 1 A LEU 3106 ? A LEU 1889 
322 1 Y 1 A GLU 3107 ? A GLU 1890 
323 1 Y 1 A ALA 3108 ? A ALA 1891 
324 1 Y 1 A GLN 3109 ? A GLN 1892 
325 1 Y 1 A ARG 3110 ? A ARG 1893 
326 1 Y 1 A GLY 3111 ? A GLY 1894 
327 1 Y 1 A VAL 3112 ? A VAL 1895 
328 1 Y 1 A LYS 3113 ? A LYS 1896 
329 1 Y 1 A ASN 3114 ? A ASN 1897 
330 1 Y 1 A ILE 3115 ? A ILE 1898 
331 1 Y 1 A LYS 3116 ? A LYS 1899 
332 1 Y 1 A LYS 3117 ? A LYS 1900 
333 1 Y 1 A GLN 3118 ? A GLN 1901 
334 1 Y 1 A GLN 3119 ? A GLN 1902 
335 1 Y 1 A LEU 3120 ? A LEU 1903 
336 1 Y 1 A THR 3121 ? A THR 1904 
337 1 Y 1 A GLU 3122 ? A GLU 1905 
338 1 Y 1 A ILE 3123 ? A ILE 1906 
339 1 Y 1 A ARG 3124 ? A ARG 1907 
340 1 Y 1 A SER 3125 ? A SER 1908 
341 1 Y 1 A MET 3126 ? A MET 1909 
342 1 Y 1 A VAL 3127 ? A VAL 1910 
343 1 Y 1 A ASN 3128 ? A ASN 1911 
344 1 Y 1 A PRO 3129 ? A PRO 1912 
345 1 Y 1 A PRO 3130 ? A PRO 1913 
346 1 Y 1 A SER 3131 ? A SER 1914 
347 1 Y 1 A GLY 3132 ? A GLY 1915 
348 1 Y 1 A VAL 3133 ? A VAL 1916 
349 1 Y 1 A LYS 3134 ? A LYS 1917 
350 1 Y 1 A ILE 3135 ? A ILE 1918 
351 1 Y 1 A VAL 3136 ? A VAL 1919 
352 1 Y 1 A MET 3137 ? A MET 1920 
353 1 Y 1 A GLU 3138 ? A GLU 1921 
354 1 Y 1 A ALA 3139 ? A ALA 1922 
355 1 Y 1 A VAL 3140 ? A VAL 1923 
356 1 Y 1 A CYS 3141 ? A CYS 1924 
357 1 Y 1 A ALA 3142 ? A ALA 1925 
358 1 Y 1 A ILE 3143 ? A ILE 1926 
359 1 Y 1 A LEU 3144 ? A LEU 1927 
360 1 Y 1 A GLY 3145 ? A GLY 1928 
361 1 Y 1 A TYR 3146 ? A TYR 1929 
362 1 Y 1 A GLN 3147 ? A GLN 1930 
363 1 Y 1 A PHE 3148 ? A PHE 1931 
364 1 Y 1 A SER 3149 ? A SER 1932 
365 1 Y 1 A ASN 3150 ? A ASN 1933 
366 1 Y 1 A TRP 3151 ? A TRP 1934 
367 1 Y 1 A ARG 3152 ? A ARG 1935 
368 1 Y 1 A ASP 3153 ? A ASP 1936 
369 1 Y 1 A ILE 3154 ? A ILE 1937 
370 1 Y 1 A GLN 3155 ? A GLN 1938 
371 1 Y 1 A GLN 3156 ? A GLN 1939 
372 1 Y 1 A PHE 3157 ? A PHE 1940 
373 1 Y 1 A ILE 3158 ? A ILE 1941 
374 1 Y 1 A ARG 3159 ? A ARG 1942 
375 1 Y 1 A LYS 3160 ? A LYS 1943 
376 1 Y 1 A ASP 3161 ? A ASP 1944 
377 1 Y 1 A ASP 3162 ? A ASP 1945 
378 1 Y 1 A PHE 3163 ? A PHE 1946 
379 1 Y 1 A ILE 3164 ? A ILE 1947 
380 1 Y 1 A HIS 3165 ? A HIS 1948 
381 1 Y 1 A ASN 3166 ? A ASN 1949 
382 1 Y 1 A ILE 3167 ? A ILE 1950 
383 1 Y 1 A VAL 3168 ? A VAL 1951 
384 1 Y 1 A HIS 3169 ? A HIS 1952 
385 1 Y 1 A TYR 3170 ? A TYR 1953 
386 1 Y 1 A ASP 3171 ? A ASP 1954 
387 1 Y 1 A THR 3172 ? A THR 1955 
388 1 Y 1 A THR 3173 ? A THR 1956 
389 1 Y 1 A LEU 3174 ? A LEU 1957 
390 1 Y 1 A HIS 3175 ? A HIS 1958 
391 1 Y 1 A MET 3176 ? A MET 1959 
392 1 Y 1 A LYS 3177 ? A LYS 1960 
393 1 Y 1 A PRO 3178 ? A PRO 1961 
394 1 Y 1 A GLN 3179 ? A GLN 1962 
395 1 Y 1 A ILE 3180 ? A ILE 1963 
396 1 Y 1 A ARG 3181 ? A ARG 1964 
397 1 Y 1 A LYS 3182 ? A LYS 1965 
398 1 Y 1 A TYR 3183 ? A TYR 1966 
399 1 Y 1 A MET 3184 ? A MET 1967 
400 1 Y 1 A GLU 3185 ? A GLU 1968 
401 1 Y 1 A GLU 3186 ? A GLU 1969 
402 1 Y 1 A GLU 3187 ? A GLU 1970 
403 1 Y 1 A PHE 3188 ? A PHE 1971 
404 1 Y 1 A LEU 3189 ? A LEU 1972 
405 1 Y 1 A SER 3190 ? A SER 1973 
406 1 Y 1 A ASP 3191 ? A ASP 1974 
407 1 Y 1 A PRO 3192 ? A PRO 1975 
408 1 Y 1 A ASN 3193 ? A ASN 1976 
409 1 Y 1 A PHE 3194 ? A PHE 1977 
410 1 Y 1 A THR 3195 ? A THR 1978 
411 1 Y 1 A TYR 3196 ? A TYR 1979 
412 1 Y 1 A GLU 3197 ? A GLU 1980 
413 1 Y 1 A THR 3198 ? A THR 1981 
414 1 Y 1 A ILE 3199 ? A ILE 1982 
415 1 Y 1 A ASN 3200 ? A ASN 1983 
416 1 Y 1 A ARG 3201 ? A ARG 1984 
417 1 Y 1 A ALA 3202 ? A ALA 1985 
418 1 Y 1 A SER 3203 ? A SER 1986 
419 1 Y 1 A LYS 3204 ? A LYS 1987 
420 1 Y 1 A ALA 3205 ? A ALA 1988 
421 1 Y 1 A CYS 3206 ? A CYS 1989 
422 1 Y 1 A GLY 3207 ? A GLY 1990 
423 1 Y 1 A PRO 3208 ? A PRO 1991 
424 1 Y 1 A LEU 3209 ? A LEU 1992 
425 1 Y 1 A TYR 3210 ? A TYR 1993 
426 1 Y 1 A GLN 3211 ? A GLN 1994 
427 1 Y 1 A TRP 3212 ? A TRP 1995 
428 1 Y 1 A VAL 3213 ? A VAL 1996 
429 1 Y 1 A ASN 3214 ? A ASN 1997 
430 1 Y 1 A ALA 3215 ? A ALA 1998 
431 1 Y 1 A GLN 3216 ? A GLN 1999 
432 1 Y 1 A ILE 3217 ? A ILE 2000 
433 1 Y 1 A ASN 3218 ? A ASN 2001 
434 1 Y 1 A PHE 3219 ? A PHE 2002 
435 1 Y 1 A SER 3220 ? A SER 2003 
436 1 Y 1 A LYS 3221 ? A LYS 2004 
437 1 Y 1 A VAL 3222 ? A VAL 2005 
438 1 Y 1 A LEU 3223 ? A LEU 2006 
439 1 Y 1 A GLU 3224 ? A GLU 2007 
440 1 Y 1 A ASN 3225 ? A ASN 2008 
441 1 Y 1 A VAL 3226 ? A VAL 2009 
442 1 Y 1 A ASP 3227 ? A ASP 2010 
443 1 Y 1 A PRO 3228 ? A PRO 2011 
444 1 Y 1 A LEU 3229 ? A LEU 2012 
445 1 Y 1 A ARG 3230 ? A ARG 2013 
446 1 Y 1 A GLN 3231 ? A GLN 2014 
447 1 Y 1 A GLU 3232 ? A GLU 2015 
448 1 Y 1 A MET 3233 ? A MET 2016 
449 1 Y 1 A LYS 3234 ? A LYS 2017 
450 1 Y 1 A ARG 3235 ? A ARG 2018 
451 1 Y 1 A ILE 3236 ? A ILE 2019 
452 1 Y 1 A GLU 3237 ? A GLU 2020 
453 1 Y 1 A PHE 3238 ? A PHE 2021 
454 1 Y 1 A GLU 3239 ? A GLU 2022 
455 1 Y 1 A SER 3240 ? A SER 2023 
456 1 Y 1 A LEU 3241 ? A LEU 2024 
457 1 Y 1 A LYS 3242 ? A LYS 2025 
458 1 Y 1 A THR 3243 ? A THR 2026 
459 1 Y 1 A LYS 3244 ? A LYS 2027 
460 1 Y 1 A ALA 3245 ? A ALA 2028 
461 1 Y 1 A ASN 3246 ? A ASN 2029 
462 1 Y 1 A LEU 3247 ? A LEU 2030 
463 1 Y 1 A LEU 3248 ? A LEU 2031 
464 1 Y 1 A ALA 3249 ? A ALA 2032 
465 1 Y 1 A ALA 3250 ? A ALA 2033 
466 1 Y 1 A GLU 3251 ? A GLU 2034 
467 1 Y 1 A GLU 3252 ? A GLU 2035 
468 1 Y 1 A MET 3253 ? A MET 2036 
469 1 Y 1 A THR 3254 ? A THR 2037 
470 1 Y 1 A GLN 3255 ? A GLN 2038 
471 1 Y 1 A ASP 3256 ? A ASP 2039 
472 1 Y 1 A LEU 3257 ? A LEU 2040 
473 1 Y 1 A GLU 3258 ? A GLU 2041 
474 1 Y 1 A ALA 3259 ? A ALA 2042 
475 1 Y 1 A SER 3260 ? A SER 2043 
476 1 Y 1 A ILE 3261 ? A ILE 2044 
477 1 Y 1 A GLU 3262 ? A GLU 2045 
478 1 Y 1 A VAL 3263 ? A VAL 2046 
479 1 Y 1 A SER 3264 ? A SER 2047 
480 1 Y 1 A LYS 3265 ? A LYS 2048 
481 1 Y 1 A GLN 3266 ? A GLN 2049 
482 1 Y 1 A LYS 3267 ? A LYS 2050 
483 1 Y 1 A TYR 3268 ? A TYR 2051 
484 1 Y 1 A SER 3269 ? A SER 2052 
485 1 Y 1 A LEU 3270 ? A LEU 2053 
486 1 Y 1 A LEU 3271 ? A LEU 2054 
487 1 Y 1 A ILE 3272 ? A ILE 2055 
488 1 Y 1 A ARG 3273 ? A ARG 2056 
489 1 Y 1 A ASP 3274 ? A ASP 2057 
490 1 Y 1 A VAL 3275 ? A VAL 2058 
491 1 Y 1 A GLU 3276 ? A GLU 2059 
492 1 Y 1 A ALA 3277 ? A ALA 2060 
493 1 Y 1 A ILE 3278 ? A ILE 2061 
494 1 Y 1 A LYS 3279 ? A LYS 2062 
495 1 Y 1 A THR 3280 ? A THR 2063 
496 1 Y 1 A GLU 3281 ? A GLU 2064 
497 1 Y 1 A MET 3282 ? A MET 2065 
498 1 Y 1 A SER 3283 ? A SER 2066 
499 1 Y 1 A ASN 3284 ? A ASN 2067 
500 1 Y 1 A VAL 3285 ? A VAL 2068 
501 1 Y 1 A GLN 3286 ? A GLN 2069 
502 1 Y 1 A ALA 3287 ? A ALA 2070 
503 1 Y 1 A ASN 3288 ? A ASN 2071 
504 1 Y 1 A LEU 3289 ? A LEU 2072 
505 1 Y 1 A ASP 3290 ? A ASP 2073 
506 1 Y 1 A ARG 3291 ? A ARG 2074 
507 1 Y 1 A SER 3292 ? A SER 2075 
508 1 Y 1 A ILE 3293 ? A ILE 2076 
509 1 Y 1 A SER 3294 ? A SER 2077 
510 1 Y 1 A LEU 3295 ? A LEU 2078 
511 1 Y 1 A VAL 3296 ? A VAL 2079 
512 1 Y 1 A LYS 3297 ? A LYS 2080 
513 1 Y 1 A LEU 3432 ? A LEU 2215 
514 1 Y 1 A GLU 3433 ? A GLU 2216 
515 1 Y 1 A GLU 3434 ? A GLU 2217 
516 1 Y 1 A ASP 3459 ? A ASP 2242 
517 1 Y 1 A GLY 3474 ? A GLY 2257 
518 1 Y 1 A ASN 3475 ? A ASN 2258 
519 1 Y 1 A ARG 3476 ? A ARG 2259 
520 1 Y 1 A SER 3502 ? A SER 2285 
521 1 Y 1 A GLY 3503 ? A GLY 2286 
522 1 Y 1 A ASP 3504 ? A ASP 2287 
523 1 Y 1 A GLN 3574 ? A GLN 2357 
524 1 Y 1 A GLY 3575 ? A GLY 2358 
525 1 Y 1 A ASN 3576 ? A ASN 2359 
526 1 Y 1 A MET 3577 ? A MET 2360 
527 1 Y 1 A LEU 3578 ? A LEU 2361 
528 1 Y 1 A GLU 3579 ? A GLU 2362 
529 1 Y 1 A ASN 3580 ? A ASN 2363 
530 1 Y 1 A ASP 3581 ? A ASP 2364 
531 1 Y 1 A GLU 3582 ? A GLU 2365 
532 1 Y 1 A LEU 3583 ? A LEU 2366 
533 1 Y 1 A MET 3584 ? A MET 2367 
534 1 Y 1 A VAL 3585 ? A VAL 2368 
535 1 Y 1 A THR 3586 ? A THR 2369 
536 1 Y 1 A LEU 3587 ? A LEU 2370 
537 1 Y 1 A ASN 3588 ? A ASN 2371 
538 1 Y 1 A ASN 3589 ? A ASN 2372 
539 1 Y 1 A LEU 3590 ? A LEU 2373 
540 1 Y 1 A LYS 3591 ? A LYS 2374 
541 1 Y 1 A LYS 3660 ? A LYS 2443 
542 1 Y 1 A SER 3661 ? A SER 2444 
543 1 Y 1 A ARG 3662 ? A ARG 2445 
544 1 Y 1 A GLU 3663 ? A GLU 2446 
545 1 Y 1 A THR 3664 ? A THR 2447 
546 1 Y 1 A ARG 3665 ? A ARG 2448 
547 1 Y 1 A ALA 3666 ? A ALA 2449 
548 1 Y 1 A ALA 3667 ? A ALA 2450 
549 1 Y 1 A ARG 3668 ? A ARG 2451 
550 1 Y 1 A VAL 3738 ? A VAL 2521 
551 1 Y 1 A ASP 3739 ? A ASP 2522 
552 1 Y 1 A THR 3740 ? A THR 2523 
553 1 Y 1 A GLU 3861 ? A GLU 2644 
554 1 Y 1 A THR 3862 ? A THR 2645 
555 1 Y 1 A LYS 3863 ? A LYS 2646 
556 1 Y 1 A ALA 3864 ? A ALA 2647 
557 1 Y 1 A ALA 3865 ? A ALA 2648 
558 1 Y 1 A GLU 3866 ? A GLU 2649 
559 1 Y 1 A THR 3917 ? A THR 2700 
560 1 Y 1 A GLY 3918 ? A GLY 2701 
561 1 Y 1 A LYS 3919 ? A LYS 2702 
562 1 Y 1 A MET 4092 ? A MET 2875 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
ATP PG     P  N N 116 
ATP O1G    O  N N 117 
ATP O2G    O  N N 118 
ATP O3G    O  N N 119 
ATP PB     P  N R 120 
ATP O1B    O  N N 121 
ATP O2B    O  N N 122 
ATP O3B    O  N N 123 
ATP PA     P  N R 124 
ATP O1A    O  N N 125 
ATP O2A    O  N N 126 
ATP O3A    O  N N 127 
ATP "O5'"  O  N N 128 
ATP "C5'"  C  N N 129 
ATP "C4'"  C  N R 130 
ATP "O4'"  O  N N 131 
ATP "C3'"  C  N S 132 
ATP "O3'"  O  N N 133 
ATP "C2'"  C  N R 134 
ATP "O2'"  O  N N 135 
ATP "C1'"  C  N R 136 
ATP N9     N  Y N 137 
ATP C8     C  Y N 138 
ATP N7     N  Y N 139 
ATP C5     C  Y N 140 
ATP C6     C  Y N 141 
ATP N6     N  N N 142 
ATP N1     N  Y N 143 
ATP C2     C  Y N 144 
ATP N3     N  Y N 145 
ATP C4     C  Y N 146 
ATP HOG2   H  N N 147 
ATP HOG3   H  N N 148 
ATP HOB2   H  N N 149 
ATP HOA2   H  N N 150 
ATP "H5'1" H  N N 151 
ATP "H5'2" H  N N 152 
ATP "H4'"  H  N N 153 
ATP "H3'"  H  N N 154 
ATP "HO3'" H  N N 155 
ATP "H2'"  H  N N 156 
ATP "HO2'" H  N N 157 
ATP "H1'"  H  N N 158 
ATP H8     H  N N 159 
ATP HN61   H  N N 160 
ATP HN62   H  N N 161 
ATP H2     H  N N 162 
CYS N      N  N N 163 
CYS CA     C  N R 164 
CYS C      C  N N 165 
CYS O      O  N N 166 
CYS CB     C  N N 167 
CYS SG     S  N N 168 
CYS OXT    O  N N 169 
CYS H      H  N N 170 
CYS H2     H  N N 171 
CYS HA     H  N N 172 
CYS HB2    H  N N 173 
CYS HB3    H  N N 174 
CYS HG     H  N N 175 
CYS HXT    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-08 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DKD 
_em_admin.last_update        2025-06-04 
_em_admin.map_release_date   2025-06-04 
_em_admin.title              'CryoEM structures of yeast cytoplasmic dynein in the presence of ATP and Lis1.' 
# 
_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_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          4932 
_em_entity_assembly_naturalsource.organism             'Saccharomyces cerevisiae' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               'ATCC 204508 / S288c' 
_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          4932 
_em_entity_assembly_recombinant.organism             'Saccharomyces cerevisiae' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               'ATCC 204508 / S288c' 
# 
_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         54 
_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  ? ? ? PHENIX ? 
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           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9DKD 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . SER A 1 153  ? 120.255 140.835 178.772 1.00 155.48 ? 1370 SER A N     1 
ATOM   2     C  CA    . SER A 1 153  ? 120.711 141.544 177.582 1.00 158.84 ? 1370 SER A CA    1 
ATOM   3     C  C     . SER A 1 153  ? 119.548 141.840 176.642 1.00 163.23 ? 1370 SER A C     1 
ATOM   4     O  O     . SER A 1 153  ? 119.511 142.891 175.997 1.00 163.15 ? 1370 SER A O     1 
ATOM   5     C  CB    . SER A 1 153  ? 121.783 140.732 176.852 1.00 156.75 ? 1370 SER A CB    1 
ATOM   6     N  N     . LEU A 1 154  ? 118.604 140.898 176.568 1.00 164.03 ? 1371 LEU A N     1 
ATOM   7     C  CA    . LEU A 1 154  ? 117.437 141.078 175.710 1.00 162.36 ? 1371 LEU A CA    1 
ATOM   8     C  C     . LEU A 1 154  ? 116.572 142.237 176.187 1.00 161.50 ? 1371 LEU A C     1 
ATOM   9     O  O     . LEU A 1 154  ? 116.077 143.026 175.373 1.00 161.59 ? 1371 LEU A O     1 
ATOM   10    C  CB    . LEU A 1 154  ? 116.621 139.786 175.656 1.00 160.66 ? 1371 LEU A CB    1 
ATOM   11    N  N     . ASN A 1 155  ? 116.382 142.357 177.504 1.00 160.59 ? 1372 ASN A N     1 
ATOM   12    C  CA    . ASN A 1 155  ? 115.608 143.469 178.047 1.00 159.76 ? 1372 ASN A CA    1 
ATOM   13    C  C     . ASN A 1 155  ? 116.294 144.803 177.779 1.00 160.82 ? 1372 ASN A C     1 
ATOM   14    O  O     . ASN A 1 155  ? 115.632 145.792 177.441 1.00 158.84 ? 1372 ASN A O     1 
ATOM   15    C  CB    . ASN A 1 155  ? 115.387 143.270 179.547 1.00 156.95 ? 1372 ASN A CB    1 
ATOM   16    N  N     . ARG A 1 156  ? 117.622 144.846 177.923 1.00 161.69 ? 1373 ARG A N     1 
ATOM   17    C  CA    . ARG A 1 156  ? 118.363 146.071 177.642 1.00 160.38 ? 1373 ARG A CA    1 
ATOM   18    C  C     . ARG A 1 156  ? 118.265 146.455 176.171 1.00 160.29 ? 1373 ARG A C     1 
ATOM   19    O  O     . ARG A 1 156  ? 118.085 147.633 175.841 1.00 160.29 ? 1373 ARG A O     1 
ATOM   20    C  CB    . ARG A 1 156  ? 119.825 145.906 178.058 1.00 156.63 ? 1373 ARG A CB    1 
ATOM   21    N  N     . ILE A 1 157  ? 118.373 145.472 175.273 1.00 160.68 ? 1374 ILE A N     1 
ATOM   22    C  CA    . ILE A 1 157  ? 118.266 145.749 173.842 1.00 160.68 ? 1374 ILE A CA    1 
ATOM   23    C  C     . ILE A 1 157  ? 116.863 146.233 173.490 1.00 160.37 ? 1374 ILE A C     1 
ATOM   24    O  O     . ILE A 1 157  ? 116.695 147.164 172.690 1.00 159.68 ? 1374 ILE A O     1 
ATOM   25    C  CB    . ILE A 1 157  ? 118.657 144.504 173.027 1.00 158.28 ? 1374 ILE A CB    1 
ATOM   26    N  N     . LYS A 1 158  ? 115.836 145.608 174.076 1.00 160.07 ? 1375 LYS A N     1 
ATOM   27    C  CA    . LYS A 1 158  ? 114.463 146.029 173.818 1.00 158.65 ? 1375 LYS A CA    1 
ATOM   28    C  C     . LYS A 1 158  ? 114.212 147.443 174.325 1.00 158.37 ? 1375 LYS A C     1 
ATOM   29    O  O     . LYS A 1 158  ? 113.567 148.247 173.643 1.00 156.34 ? 1375 LYS A O     1 
ATOM   30    C  CB    . LYS A 1 158  ? 113.485 145.046 174.461 1.00 159.10 ? 1375 LYS A CB    1 
ATOM   31    N  N     . LYS A 1 159  ? 114.720 147.768 175.519 1.00 160.07 ? 1376 LYS A N     1 
ATOM   32    C  CA    . LYS A 1 159  ? 114.568 149.119 176.051 1.00 159.23 ? 1376 LYS A CA    1 
ATOM   33    C  C     . LYS A 1 159  ? 115.314 150.138 175.198 1.00 159.24 ? 1376 LYS A C     1 
ATOM   34    O  O     . LYS A 1 159  ? 114.823 151.254 174.985 1.00 156.88 ? 1376 LYS A O     1 
ATOM   35    C  CB    . LYS A 1 159  ? 115.053 149.170 177.499 1.00 155.75 ? 1376 LYS A CB    1 
ATOM   36    N  N     . PHE A 1 160  ? 116.501 149.774 174.705 1.00 160.63 ? 1377 PHE A N     1 
ATOM   37    C  CA    . PHE A 1 160  ? 117.257 150.676 173.842 1.00 157.58 ? 1377 PHE A CA    1 
ATOM   38    C  C     . PHE A 1 160  ? 116.526 150.932 172.529 1.00 156.23 ? 1377 PHE A C     1 
ATOM   39    O  O     . PHE A 1 160  ? 116.509 152.064 172.032 1.00 155.02 ? 1377 PHE A O     1 
ATOM   40    C  CB    . PHE A 1 160  ? 118.649 150.103 173.578 1.00 156.16 ? 1377 PHE A CB    1 
ATOM   41    N  N     . TRP A 1 161  ? 115.920 149.892 171.948 1.00 155.68 ? 1378 TRP A N     1 
ATOM   42    C  CA    . TRP A 1 161  ? 115.170 150.093 170.711 1.00 154.85 ? 1378 TRP A CA    1 
ATOM   43    C  C     . TRP A 1 161  ? 113.891 150.887 170.950 1.00 156.28 ? 1378 TRP A C     1 
ATOM   44    O  O     . TRP A 1 161  ? 113.496 151.700 170.106 1.00 156.52 ? 1378 TRP A O     1 
ATOM   45    C  CB    . TRP A 1 161  ? 114.855 148.757 170.041 1.00 154.28 ? 1378 TRP A CB    1 
ATOM   46    C  CG    . TRP A 1 161  ? 114.124 148.949 168.748 1.00 154.67 ? 1378 TRP A CG    1 
ATOM   47    C  CD1   . TRP A 1 161  ? 112.794 148.749 168.522 1.00 151.60 ? 1378 TRP A CD1   1 
ATOM   48    C  CD2   . TRP A 1 161  ? 114.666 149.462 167.525 1.00 154.62 ? 1378 TRP A CD2   1 
ATOM   49    N  NE1   . TRP A 1 161  ? 112.482 149.063 167.221 1.00 150.54 ? 1378 TRP A NE1   1 
ATOM   50    C  CE2   . TRP A 1 161  ? 113.614 149.508 166.589 1.00 152.52 ? 1378 TRP A CE2   1 
ATOM   51    C  CE3   . TRP A 1 161  ? 115.943 149.869 167.125 1.00 153.76 ? 1378 TRP A CE3   1 
ATOM   52    C  CZ2   . TRP A 1 161  ? 113.798 149.944 165.279 1.00 149.67 ? 1378 TRP A CZ2   1 
ATOM   53    C  CZ3   . TRP A 1 161  ? 116.124 150.302 165.823 1.00 152.12 ? 1378 TRP A CZ3   1 
ATOM   54    C  CH2   . TRP A 1 161  ? 115.057 150.339 164.917 1.00 149.02 ? 1378 TRP A CH2   1 
ATOM   55    N  N     . LYS A 1 162  ? 113.223 150.666 172.086 1.00 156.57 ? 1379 LYS A N     1 
ATOM   56    C  CA    . LYS A 1 162  ? 112.044 151.463 172.406 1.00 155.95 ? 1379 LYS A CA    1 
ATOM   57    C  C     . LYS A 1 162  ? 112.399 152.911 172.713 1.00 156.95 ? 1379 LYS A C     1 
ATOM   58    O  O     . LYS A 1 162  ? 111.553 153.794 172.538 1.00 154.90 ? 1379 LYS A O     1 
ATOM   59    C  CB    . LYS A 1 162  ? 111.286 150.849 173.584 1.00 153.08 ? 1379 LYS A CB    1 
ATOM   60    C  CG    . LYS A 1 162  ? 110.624 149.515 173.272 1.00 149.81 ? 1379 LYS A CG    1 
ATOM   61    C  CD    . LYS A 1 162  ? 109.704 149.614 172.068 1.00 145.40 ? 1379 LYS A CD    1 
ATOM   62    C  CE    . LYS A 1 162  ? 109.545 148.264 171.391 1.00 141.79 ? 1379 LYS A CE    1 
ATOM   63    N  NZ    . LYS A 1 162  ? 108.820 148.371 170.096 1.00 136.18 ? 1379 LYS A NZ    1 
ATOM   64    N  N     . GLU A 1 163  ? 113.623 153.172 173.165 1.00 157.84 ? 1380 GLU A N     1 
ATOM   65    C  CA    . GLU A 1 163  ? 114.100 154.528 173.396 1.00 156.62 ? 1380 GLU A CA    1 
ATOM   66    C  C     . GLU A 1 163  ? 114.800 155.125 172.183 1.00 158.06 ? 1380 GLU A C     1 
ATOM   67    O  O     . GLU A 1 163  ? 115.251 156.273 172.252 1.00 158.10 ? 1380 GLU A O     1 
ATOM   68    C  CB    . GLU A 1 163  ? 115.049 154.555 174.599 1.00 153.30 ? 1380 GLU A CB    1 
ATOM   69    N  N     . ALA A 1 164  ? 114.906 154.379 171.084 1.00 158.76 ? 1381 ALA A N     1 
ATOM   70    C  CA    . ALA A 1 164  ? 115.560 154.891 169.887 1.00 156.54 ? 1381 ALA A CA    1 
ATOM   71    C  C     . ALA A 1 164  ? 114.720 155.995 169.258 1.00 158.95 ? 1381 ALA A C     1 
ATOM   72    O  O     . ALA A 1 164  ? 113.510 155.841 169.069 1.00 159.52 ? 1381 ALA A O     1 
ATOM   73    C  CB    . ALA A 1 164  ? 115.791 153.763 168.883 1.00 152.67 ? 1381 ALA A CB    1 
ATOM   74    N  N     . GLN A 1 165  ? 115.367 157.109 168.929 1.00 158.32 ? 1382 GLN A N     1 
ATOM   75    C  CA    . GLN A 1 165  ? 114.677 158.273 168.393 1.00 157.04 ? 1382 GLN A CA    1 
ATOM   76    C  C     . GLN A 1 165  ? 115.606 158.976 167.410 1.00 156.53 ? 1382 GLN A C     1 
ATOM   77    O  O     . GLN A 1 165  ? 116.622 158.420 166.982 1.00 154.22 ? 1382 GLN A O     1 
ATOM   78    C  CB    . GLN A 1 165  ? 114.220 159.201 169.527 1.00 155.36 ? 1382 GLN A CB    1 
ATOM   79    N  N     . TYR A 1 166  ? 115.252 160.207 167.052 1.00 159.06 ? 1383 TYR A N     1 
ATOM   80    C  CA    . TYR A 1 166  ? 115.968 160.968 166.041 1.00 159.76 ? 1383 TYR A CA    1 
ATOM   81    C  C     . TYR A 1 166  ? 116.185 162.393 166.531 1.00 161.69 ? 1383 TYR A C     1 
ATOM   82    O  O     . TYR A 1 166  ? 115.447 162.899 167.381 1.00 160.38 ? 1383 TYR A O     1 
ATOM   83    C  CB    . TYR A 1 166  ? 115.207 160.966 164.707 1.00 156.87 ? 1383 TYR A CB    1 
ATOM   84    C  CG    . TYR A 1 166  ? 114.933 159.579 164.162 1.00 154.50 ? 1383 TYR A CG    1 
ATOM   85    C  CD1   . TYR A 1 166  ? 113.789 158.877 164.527 1.00 153.00 ? 1383 TYR A CD1   1 
ATOM   86    C  CD2   . TYR A 1 166  ? 115.813 158.977 163.271 1.00 154.77 ? 1383 TYR A CD2   1 
ATOM   87    C  CE1   . TYR A 1 166  ? 113.534 157.614 164.027 1.00 153.64 ? 1383 TYR A CE1   1 
ATOM   88    C  CE2   . TYR A 1 166  ? 115.566 157.715 162.765 1.00 154.26 ? 1383 TYR A CE2   1 
ATOM   89    C  CZ    . TYR A 1 166  ? 114.426 157.038 163.146 1.00 155.09 ? 1383 TYR A CZ    1 
ATOM   90    O  OH    . TYR A 1 166  ? 114.178 155.781 162.645 1.00 155.70 ? 1383 TYR A OH    1 
ATOM   91    N  N     . GLU A 1 167  ? 117.211 163.036 165.982 1.00 162.03 ? 1384 GLU A N     1 
ATOM   92    C  CA    . GLU A 1 167  ? 117.627 164.368 166.399 1.00 162.49 ? 1384 GLU A CA    1 
ATOM   93    C  C     . GLU A 1 167  ? 117.253 165.396 165.340 1.00 165.20 ? 1384 GLU A C     1 
ATOM   94    O  O     . GLU A 1 167  ? 117.408 165.152 164.140 1.00 164.98 ? 1384 GLU A O     1 
ATOM   95    C  CB    . GLU A 1 167  ? 119.136 164.412 166.658 1.00 157.47 ? 1384 GLU A CB    1 
ATOM   96    N  N     . VAL A 1 168  ? 116.757 166.547 165.791 1.00 166.15 ? 1385 VAL A N     1 
ATOM   97    C  CA    . VAL A 1 168  ? 116.388 167.643 164.893 1.00 165.20 ? 1385 VAL A CA    1 
ATOM   98    C  C     . VAL A 1 168  ? 117.624 168.528 164.760 1.00 165.72 ? 1385 VAL A C     1 
ATOM   99    O  O     . VAL A 1 168  ? 117.811 169.494 165.501 1.00 163.99 ? 1385 VAL A O     1 
ATOM   100   C  CB    . VAL A 1 168  ? 115.171 168.412 165.397 1.00 161.98 ? 1385 VAL A CB    1 
ATOM   101   N  N     . ILE A 1 169  ? 118.483 168.189 163.797 1.00 167.43 ? 1386 ILE A N     1 
ATOM   102   C  CA    . ILE A 1 169  ? 119.707 168.937 163.542 1.00 168.38 ? 1386 ILE A CA    1 
ATOM   103   C  C     . ILE A 1 169  ? 119.892 169.279 162.072 1.00 168.81 ? 1386 ILE A C     1 
ATOM   104   O  O     . ILE A 1 169  ? 120.913 169.866 161.710 1.00 170.20 ? 1386 ILE A O     1 
ATOM   105   C  CB    . ILE A 1 169  ? 120.945 168.182 164.069 1.00 163.21 ? 1386 ILE A CB    1 
ATOM   106   N  N     . GLU A 1 170  ? 118.939 168.932 161.213 1.00 167.49 ? 1387 GLU A N     1 
ATOM   107   C  CA    . GLU A 1 170  ? 119.066 169.145 159.780 1.00 166.72 ? 1387 GLU A CA    1 
ATOM   108   C  C     . GLU A 1 170  ? 118.633 170.562 159.406 1.00 167.13 ? 1387 GLU A C     1 
ATOM   109   O  O     . GLU A 1 170  ? 118.256 171.376 160.254 1.00 166.49 ? 1387 GLU A O     1 
ATOM   110   C  CB    . GLU A 1 170  ? 118.248 168.103 159.024 1.00 164.41 ? 1387 GLU A CB    1 
ATOM   111   C  CG    . GLU A 1 170  ? 116.747 168.292 159.162 1.00 164.00 ? 1387 GLU A CG    1 
ATOM   112   C  CD    . GLU A 1 170  ? 116.167 167.553 160.355 1.00 163.42 ? 1387 GLU A CD    1 
ATOM   113   O  OE1   . GLU A 1 170  ? 116.951 167.015 161.166 1.00 163.57 ? 1387 GLU A OE1   1 
ATOM   114   O  OE2   . GLU A 1 170  ? 114.926 167.510 160.481 1.00 161.74 ? 1387 GLU A OE2   1 
ATOM   115   N  N     . HIS A 1 171  ? 118.687 170.858 158.110 1.00 167.00 ? 1388 HIS A N     1 
ATOM   116   C  CA    . HIS A 1 171  ? 118.271 172.146 157.575 1.00 164.86 ? 1388 HIS A CA    1 
ATOM   117   C  C     . HIS A 1 171  ? 116.942 171.995 156.848 1.00 164.38 ? 1388 HIS A C     1 
ATOM   118   O  O     . HIS A 1 171  ? 116.679 170.960 156.228 1.00 162.23 ? 1388 HIS A O     1 
ATOM   119   C  CB    . HIS A 1 171  ? 119.328 172.712 156.624 1.00 161.13 ? 1388 HIS A CB    1 
ATOM   120   N  N     . SER A 1 172  ? 116.112 173.041 156.931 1.00 165.58 ? 1389 SER A N     1 
ATOM   121   C  CA    . SER A 1 172  ? 114.740 173.059 156.406 1.00 164.63 ? 1389 SER A CA    1 
ATOM   122   C  C     . SER A 1 172  ? 113.984 171.914 157.071 1.00 164.80 ? 1389 SER A C     1 
ATOM   123   O  O     . SER A 1 172  ? 113.947 171.869 158.313 1.00 164.33 ? 1389 SER A O     1 
ATOM   124   C  CB    . SER A 1 172  ? 114.768 173.047 154.875 1.00 160.55 ? 1389 SER A CB    1 
ATOM   125   N  N     . SER A 1 173  ? 113.378 170.990 156.326 1.00 164.23 ? 1390 SER A N     1 
ATOM   126   C  CA    . SER A 1 173  ? 112.730 169.827 156.918 1.00 162.29 ? 1390 SER A CA    1 
ATOM   127   C  C     . SER A 1 173  ? 113.468 168.536 156.587 1.00 159.59 ? 1390 SER A C     1 
ATOM   128   O  O     . SER A 1 173  ? 113.981 167.876 157.495 1.00 157.85 ? 1390 SER A O     1 
ATOM   129   C  CB    . SER A 1 173  ? 111.273 169.741 156.445 1.00 162.68 ? 1390 SER A CB    1 
ATOM   130   O  OG    . SER A 1 173  ? 111.192 169.868 155.036 1.00 159.56 ? 1390 SER A OG    1 
ATOM   131   N  N     . GLY A 1 174  ? 113.562 168.188 155.302 1.00 158.15 ? 1391 GLY A N     1 
ATOM   132   C  CA    . GLY A 1 174  ? 114.289 166.999 154.875 1.00 157.43 ? 1391 GLY A CA    1 
ATOM   133   C  C     . GLY A 1 174  ? 113.799 165.737 155.556 1.00 156.08 ? 1391 GLY A C     1 
ATOM   134   O  O     . GLY A 1 174  ? 112.594 165.462 155.622 1.00 155.09 ? 1391 GLY A O     1 
ATOM   135   N  N     . LEU A 1 175  ? 114.747 164.960 156.069 1.00 154.53 ? 1392 LEU A N     1 
ATOM   136   C  CA    . LEU A 1 175  ? 114.484 163.889 157.017 1.00 155.39 ? 1392 LEU A CA    1 
ATOM   137   C  C     . LEU A 1 175  ? 114.979 164.278 158.400 1.00 157.77 ? 1392 LEU A C     1 
ATOM   138   O  O     . LEU A 1 175  ? 115.906 165.078 158.548 1.00 159.36 ? 1392 LEU A O     1 
ATOM   139   C  CB    . LEU A 1 175  ? 115.167 162.574 156.621 1.00 156.30 ? 1392 LEU A CB    1 
ATOM   140   C  CG    . LEU A 1 175  ? 114.772 161.741 155.408 1.00 149.98 ? 1392 LEU A CG    1 
ATOM   141   C  CD1   . LEU A 1 175  ? 115.762 160.607 155.228 1.00 144.83 ? 1392 LEU A CD1   1 
ATOM   142   C  CD2   . LEU A 1 175  ? 113.378 161.189 155.613 1.00 148.40 ? 1392 LEU A CD2   1 
ATOM   143   N  N     . LYS A 1 176  ? 114.333 163.706 159.409 1.00 156.89 ? 1393 LYS A N     1 
ATOM   144   C  CA    . LYS A 1 176  ? 114.905 163.671 160.744 1.00 158.16 ? 1393 LYS A CA    1 
ATOM   145   C  C     . LYS A 1 176  ? 116.218 162.897 160.713 1.00 161.21 ? 1393 LYS A C     1 
ATOM   146   O  O     . LYS A 1 176  ? 116.389 161.961 159.925 1.00 159.84 ? 1393 LYS A O     1 
ATOM   147   C  CB    . LYS A 1 176  ? 113.901 163.036 161.699 1.00 155.64 ? 1393 LYS A CB    1 
ATOM   148   C  CG    . LYS A 1 176  ? 113.562 161.608 161.333 1.00 154.96 ? 1393 LYS A CG    1 
ATOM   149   C  CD    . LYS A 1 176  ? 112.463 161.085 162.205 1.00 151.86 ? 1393 LYS A CD    1 
ATOM   150   C  CE    . LYS A 1 176  ? 111.173 161.759 161.814 1.00 149.43 ? 1393 LYS A CE    1 
ATOM   151   N  NZ    . LYS A 1 176  ? 110.757 161.390 160.432 1.00 148.91 ? 1393 LYS A NZ    1 
ATOM   152   N  N     . LEU A 1 177  ? 117.161 163.305 161.555 1.00 161.49 ? 1394 LEU A N     1 
ATOM   153   C  CA    . LEU A 1 177  ? 118.543 162.880 161.412 1.00 160.80 ? 1394 LEU A CA    1 
ATOM   154   C  C     . LEU A 1 177  ? 119.034 162.260 162.713 1.00 158.92 ? 1394 LEU A C     1 
ATOM   155   O  O     . LEU A 1 177  ? 118.561 162.591 163.802 1.00 158.98 ? 1394 LEU A O     1 
ATOM   156   C  CB    . LEU A 1 177  ? 119.420 164.068 160.993 1.00 160.72 ? 1394 LEU A CB    1 
ATOM   157   C  CG    . LEU A 1 177  ? 120.825 163.823 160.457 1.00 158.36 ? 1394 LEU A CG    1 
ATOM   158   C  CD1   . LEU A 1 177  ? 120.784 162.830 159.309 1.00 156.42 ? 1394 LEU A CD1   1 
ATOM   159   C  CD2   . LEU A 1 177  ? 121.380 165.148 159.980 1.00 156.33 ? 1394 LEU A CD2   1 
ATOM   160   N  N     . VAL A 1 178  ? 119.984 161.338 162.585 1.00 158.33 ? 1395 VAL A N     1 
ATOM   161   C  CA    . VAL A 1 178  ? 120.487 160.567 163.715 1.00 158.67 ? 1395 VAL A CA    1 
ATOM   162   C  C     . VAL A 1 178  ? 121.982 160.825 163.862 1.00 158.81 ? 1395 VAL A C     1 
ATOM   163   O  O     . VAL A 1 178  ? 122.686 161.105 162.886 1.00 158.43 ? 1395 VAL A O     1 
ATOM   164   C  CB    . VAL A 1 178  ? 120.176 159.058 163.542 1.00 154.36 ? 1395 VAL A CB    1 
ATOM   165   C  CG1   . VAL A 1 178  ? 120.983 158.455 162.402 1.00 150.35 ? 1395 VAL A CG1   1 
ATOM   166   C  CG2   . VAL A 1 178  ? 120.389 158.287 164.844 1.00 153.22 ? 1395 VAL A CG2   1 
ATOM   167   N  N     . ARG A 1 179  ? 122.459 160.763 165.105 1.00 157.16 ? 1396 ARG A N     1 
ATOM   168   C  CA    . ARG A 1 179  ? 123.862 160.972 165.428 1.00 153.90 ? 1396 ARG A CA    1 
ATOM   169   C  C     . ARG A 1 179  ? 124.375 159.790 166.242 1.00 155.80 ? 1396 ARG A C     1 
ATOM   170   O  O     . ARG A 1 179  ? 123.602 158.944 166.702 1.00 156.48 ? 1396 ARG A O     1 
ATOM   171   C  CB    . ARG A 1 179  ? 124.070 162.284 166.198 1.00 151.67 ? 1396 ARG A CB    1 
ATOM   172   N  N     . GLU A 1 180  ? 125.701 159.746 166.406 1.00 156.57 ? 1397 GLU A N     1 
ATOM   173   C  CA    . GLU A 1 180  ? 126.401 158.714 167.177 1.00 154.49 ? 1397 GLU A CA    1 
ATOM   174   C  C     . GLU A 1 180  ? 126.103 157.314 166.632 1.00 153.82 ? 1397 GLU A C     1 
ATOM   175   O  O     . GLU A 1 180  ? 125.494 156.471 167.294 1.00 154.81 ? 1397 GLU A O     1 
ATOM   176   C  CB    . GLU A 1 180  ? 126.063 158.815 168.670 1.00 152.65 ? 1397 GLU A CB    1 
ATOM   177   N  N     . TRP A 1 181  ? 126.541 157.088 165.391 1.00 151.70 ? 1398 TRP A N     1 
ATOM   178   C  CA    . TRP A 1 181  ? 126.284 155.812 164.730 1.00 151.55 ? 1398 TRP A CA    1 
ATOM   179   C  C     . TRP A 1 181  ? 127.076 154.674 165.364 1.00 152.00 ? 1398 TRP A C     1 
ATOM   180   O  O     . TRP A 1 181  ? 126.585 153.542 165.445 1.00 150.91 ? 1398 TRP A O     1 
ATOM   181   C  CB    . TRP A 1 181  ? 126.612 155.918 163.241 1.00 150.27 ? 1398 TRP A CB    1 
ATOM   182   C  CG    . TRP A 1 181  ? 125.433 156.264 162.390 1.00 147.61 ? 1398 TRP A CG    1 
ATOM   183   C  CD1   . TRP A 1 181  ? 125.170 157.466 161.802 1.00 146.43 ? 1398 TRP A CD1   1 
ATOM   184   C  CD2   . TRP A 1 181  ? 124.348 155.400 162.040 1.00 145.44 ? 1398 TRP A CD2   1 
ATOM   185   N  NE1   . TRP A 1 181  ? 123.991 157.401 161.100 1.00 144.76 ? 1398 TRP A NE1   1 
ATOM   186   C  CE2   . TRP A 1 181  ? 123.466 156.142 161.232 1.00 144.25 ? 1398 TRP A CE2   1 
ATOM   187   C  CE3   . TRP A 1 181  ? 124.038 154.068 162.330 1.00 143.35 ? 1398 TRP A CE3   1 
ATOM   188   C  CZ2   . TRP A 1 181  ? 122.294 155.598 160.713 1.00 142.45 ? 1398 TRP A CZ2   1 
ATOM   189   C  CZ3   . TRP A 1 181  ? 122.876 153.531 161.813 1.00 141.65 ? 1398 TRP A CZ3   1 
ATOM   190   C  CH2   . TRP A 1 181  ? 122.018 154.293 161.013 1.00 141.81 ? 1398 TRP A CH2   1 
ATOM   191   N  N     . ASP A 1 182  ? 128.307 154.956 165.806 1.00 152.68 ? 1399 ASP A N     1 
ATOM   192   C  CA    . ASP A 1 182  ? 129.204 153.897 166.265 1.00 151.71 ? 1399 ASP A CA    1 
ATOM   193   C  C     . ASP A 1 182  ? 128.671 153.204 167.514 1.00 151.33 ? 1399 ASP A C     1 
ATOM   194   O  O     . ASP A 1 182  ? 128.755 151.976 167.631 1.00 150.00 ? 1399 ASP A O     1 
ATOM   195   C  CB    . ASP A 1 182  ? 130.597 154.469 166.524 1.00 149.78 ? 1399 ASP A CB    1 
ATOM   196   N  N     . VAL A 1 183  ? 128.120 153.975 168.456 1.00 151.08 ? 1400 VAL A N     1 
ATOM   197   C  CA    . VAL A 1 183  ? 127.586 153.391 169.685 1.00 150.29 ? 1400 VAL A CA    1 
ATOM   198   C  C     . VAL A 1 183  ? 126.392 152.495 169.380 1.00 153.72 ? 1400 VAL A C     1 
ATOM   199   O  O     . VAL A 1 183  ? 126.263 151.396 169.936 1.00 153.22 ? 1400 VAL A O     1 
ATOM   200   C  CB    . VAL A 1 183  ? 127.220 154.500 170.688 1.00 145.14 ? 1400 VAL A CB    1 
ATOM   201   N  N     . LEU A 1 184  ? 125.503 152.948 168.491 1.00 154.90 ? 1401 LEU A N     1 
ATOM   202   C  CA    . LEU A 1 184  ? 124.339 152.146 168.124 1.00 152.44 ? 1401 LEU A CA    1 
ATOM   203   C  C     . LEU A 1 184  ? 124.749 150.867 167.404 1.00 151.19 ? 1401 LEU A C     1 
ATOM   204   O  O     . LEU A 1 184  ? 124.182 149.797 167.654 1.00 150.16 ? 1401 LEU A O     1 
ATOM   205   C  CB    . LEU A 1 184  ? 123.388 152.970 167.257 1.00 150.49 ? 1401 LEU A CB    1 
ATOM   206   N  N     . GLU A 1 185  ? 125.736 150.955 166.506 1.00 152.08 ? 1402 GLU A N     1 
ATOM   207   C  CA    . GLU A 1 185  ? 126.200 149.761 165.803 1.00 152.14 ? 1402 GLU A CA    1 
ATOM   208   C  C     . GLU A 1 185  ? 126.887 148.784 166.751 1.00 150.53 ? 1402 GLU A C     1 
ATOM   209   O  O     . GLU A 1 185  ? 126.726 147.565 166.613 1.00 149.86 ? 1402 GLU A O     1 
ATOM   210   C  CB    . GLU A 1 185  ? 127.132 150.151 164.656 1.00 151.72 ? 1402 GLU A CB    1 
ATOM   211   C  CG    . GLU A 1 185  ? 126.442 150.935 163.553 1.00 152.30 ? 1402 GLU A CG    1 
ATOM   212   C  CD    . GLU A 1 185  ? 125.053 150.405 163.252 1.00 153.47 ? 1402 GLU A CD    1 
ATOM   213   O  OE1   . GLU A 1 185  ? 124.946 149.275 162.730 1.00 153.92 ? 1402 GLU A OE1   1 
ATOM   214   O  OE2   . GLU A 1 185  ? 124.067 151.113 163.548 1.00 149.79 ? 1402 GLU A OE2   1 
ATOM   215   N  N     . GLN A 1 186  ? 127.657 149.295 167.716 1.00 150.21 ? 1403 GLN A N     1 
ATOM   216   C  CA    . GLN A 1 186  ? 128.281 148.420 168.704 1.00 149.49 ? 1403 GLN A CA    1 
ATOM   217   C  C     . GLN A 1 186  ? 127.245 147.764 169.608 1.00 151.00 ? 1403 GLN A C     1 
ATOM   218   O  O     . GLN A 1 186  ? 127.415 146.604 170.000 1.00 150.50 ? 1403 GLN A O     1 
ATOM   219   C  CB    . GLN A 1 186  ? 129.292 149.205 169.538 1.00 148.80 ? 1403 GLN A CB    1 
ATOM   220   N  N     . ALA A 1 187  ? 126.178 148.489 169.957 1.00 151.44 ? 1404 ALA A N     1 
ATOM   221   C  CA    . ALA A 1 187  ? 125.102 147.892 170.742 1.00 150.75 ? 1404 ALA A CA    1 
ATOM   222   C  C     . ALA A 1 187  ? 124.361 146.825 169.945 1.00 150.00 ? 1404 ALA A C     1 
ATOM   223   O  O     . ALA A 1 187  ? 124.000 145.775 170.490 1.00 147.85 ? 1404 ALA A O     1 
ATOM   224   C  CB    . ALA A 1 187  ? 124.136 148.977 171.217 1.00 149.35 ? 1404 ALA A CB    1 
ATOM   225   N  N     . CYS A 1 188  ? 124.117 147.081 168.657 1.00 149.46 ? 1405 CYS A N     1 
ATOM   226   C  CA    . CYS A 1 188  ? 123.422 146.108 167.820 1.00 145.39 ? 1405 CYS A CA    1 
ATOM   227   C  C     . CYS A 1 188  ? 124.267 144.859 167.597 1.00 146.24 ? 1405 CYS A C     1 
ATOM   228   O  O     . CYS A 1 188  ? 123.739 143.741 167.581 1.00 146.06 ? 1405 CYS A O     1 
ATOM   229   C  CB    . CYS A 1 188  ? 123.042 146.743 166.483 1.00 142.30 ? 1405 CYS A CB    1 
ATOM   230   N  N     . LYS A 1 189  ? 125.574 145.027 167.418 1.00 147.72 ? 1406 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 189  ? 126.468 143.898 167.186 1.00 146.36 ? 1406 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 189  ? 126.643 143.063 168.450 1.00 144.34 ? 1406 LYS A C     1 
ATOM   233   O  O     . LYS A 1 189  ? 126.183 141.923 168.520 1.00 142.41 ? 1406 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 189  ? 127.829 144.388 166.687 1.00 147.79 ? 1406 LYS A CB    1 
ATOM   235   N  N     . GLU A 1 208  ? 114.912 128.176 172.118 1.00 157.31 ? 1425 GLU A N     1 
ATOM   236   C  CA    . GLU A 1 208  ? 115.686 128.541 170.937 1.00 158.03 ? 1425 GLU A CA    1 
ATOM   237   C  C     . GLU A 1 208  ? 114.904 129.500 170.047 1.00 156.52 ? 1425 GLU A C     1 
ATOM   238   O  O     . GLU A 1 208  ? 115.488 130.233 169.247 1.00 155.91 ? 1425 GLU A O     1 
ATOM   239   C  CB    . GLU A 1 208  ? 116.080 127.291 170.147 1.00 155.85 ? 1425 GLU A CB    1 
ATOM   240   N  N     . GLN A 1 209  ? 113.576 129.480 170.191 1.00 154.67 ? 1426 GLN A N     1 
ATOM   241   C  CA    . GLN A 1 209  ? 112.724 130.350 169.386 1.00 152.78 ? 1426 GLN A CA    1 
ATOM   242   C  C     . GLN A 1 209  ? 112.965 131.820 169.708 1.00 154.53 ? 1426 GLN A C     1 
ATOM   243   O  O     . GLN A 1 209  ? 113.014 132.657 168.800 1.00 154.97 ? 1426 GLN A O     1 
ATOM   244   C  CB    . GLN A 1 209  ? 111.255 129.987 169.600 1.00 152.94 ? 1426 GLN A CB    1 
ATOM   245   N  N     . ASP A 1 210  ? 113.119 132.150 170.994 1.00 155.66 ? 1427 ASP A N     1 
ATOM   246   C  CA    . ASP A 1 210  ? 113.384 133.533 171.382 1.00 154.69 ? 1427 ASP A CA    1 
ATOM   247   C  C     . ASP A 1 210  ? 114.734 134.008 170.857 1.00 154.62 ? 1427 ASP A C     1 
ATOM   248   O  O     . ASP A 1 210  ? 114.852 135.139 170.368 1.00 152.85 ? 1427 ASP A O     1 
ATOM   249   C  CB    . ASP A 1 210  ? 113.321 133.671 172.902 1.00 151.97 ? 1427 ASP A CB    1 
ATOM   250   N  N     . CYS A 1 211  ? 115.760 133.158 170.947 1.00 155.91 ? 1428 CYS A N     1 
ATOM   251   C  CA    . CYS A 1 211  ? 117.077 133.522 170.431 1.00 155.12 ? 1428 CYS A CA    1 
ATOM   252   C  C     . CYS A 1 211  ? 117.052 133.692 168.917 1.00 154.53 ? 1428 CYS A C     1 
ATOM   253   O  O     . CYS A 1 211  ? 117.678 134.612 168.379 1.00 154.37 ? 1428 CYS A O     1 
ATOM   254   C  CB    . CYS A 1 211  ? 118.109 132.470 170.837 1.00 154.29 ? 1428 CYS A CB    1 
ATOM   255   N  N     . LEU A 1 212  ? 116.335 132.810 168.213 1.00 155.17 ? 1429 LEU A N     1 
ATOM   256   C  CA    . LEU A 1 212  ? 116.221 132.932 166.763 1.00 155.55 ? 1429 LEU A CA    1 
ATOM   257   C  C     . LEU A 1 212  ? 115.483 134.206 166.371 1.00 154.35 ? 1429 LEU A C     1 
ATOM   258   O  O     . LEU A 1 212  ? 115.876 134.893 165.420 1.00 154.20 ? 1429 LEU A O     1 
ATOM   259   C  CB    . LEU A 1 212  ? 115.516 131.704 166.187 1.00 154.36 ? 1429 LEU A CB    1 
ATOM   260   N  N     . ASP A 1 213  ? 114.411 134.539 167.097 1.00 153.20 ? 1430 ASP A N     1 
ATOM   261   C  CA    . ASP A 1 213  ? 113.681 135.774 166.828 1.00 151.57 ? 1430 ASP A CA    1 
ATOM   262   C  C     . ASP A 1 213  ? 114.551 136.997 167.083 1.00 153.31 ? 1430 ASP A C     1 
ATOM   263   O  O     . ASP A 1 213  ? 114.531 137.953 166.300 1.00 153.31 ? 1430 ASP A O     1 
ATOM   264   C  CB    . ASP A 1 213  ? 112.413 135.829 167.681 1.00 151.38 ? 1430 ASP A CB    1 
ATOM   265   N  N     . LEU A 1 214  ? 115.327 136.982 168.171 1.00 154.67 ? 1431 LEU A N     1 
ATOM   266   C  CA    . LEU A 1 214  ? 116.217 138.101 168.469 1.00 154.20 ? 1431 LEU A CA    1 
ATOM   267   C  C     . LEU A 1 214  ? 117.305 138.247 167.411 1.00 152.56 ? 1431 LEU A C     1 
ATOM   268   O  O     . LEU A 1 214  ? 117.633 139.368 167.005 1.00 151.97 ? 1431 LEU A O     1 
ATOM   269   C  CB    . LEU A 1 214  ? 116.837 137.923 169.855 1.00 151.97 ? 1431 LEU A CB    1 
ATOM   270   N  N     . GLU A 1 215  ? 117.874 137.128 166.953 1.00 152.84 ? 1432 GLU A N     1 
ATOM   271   C  CA    . GLU A 1 215  ? 118.906 137.186 165.921 1.00 150.93 ? 1432 GLU A CA    1 
ATOM   272   C  C     . GLU A 1 215  ? 118.344 137.691 164.597 1.00 150.80 ? 1432 GLU A C     1 
ATOM   273   O  O     . GLU A 1 215  ? 118.983 138.505 163.916 1.00 151.26 ? 1432 GLU A O     1 
ATOM   274   C  CB    . GLU A 1 215  ? 119.547 135.810 165.744 1.00 151.95 ? 1432 GLU A CB    1 
ATOM   275   N  N     . SER A 1 216  ? 117.154 137.216 164.213 1.00 150.45 ? 1433 SER A N     1 
ATOM   276   C  CA    . SER A 1 216  ? 116.517 137.707 162.995 1.00 148.94 ? 1433 SER A CA    1 
ATOM   277   C  C     . SER A 1 216  ? 116.181 139.188 163.099 1.00 148.65 ? 1433 SER A C     1 
ATOM   278   O  O     . SER A 1 216  ? 116.366 139.932 162.128 1.00 146.31 ? 1433 SER A O     1 
ATOM   279   C  CB    . SER A 1 216  ? 115.256 136.896 162.697 1.00 147.77 ? 1433 SER A CB    1 
ATOM   280   N  N     . LYS A 1 217  ? 115.701 139.630 164.265 1.00 149.92 ? 1434 LYS A N     1 
ATOM   281   C  CA    . LYS A 1 217  ? 115.422 141.045 164.475 1.00 147.68 ? 1434 LYS A CA    1 
ATOM   282   C  C     . LYS A 1 217  ? 116.692 141.879 164.376 1.00 147.45 ? 1434 LYS A C     1 
ATOM   283   O  O     . LYS A 1 217  ? 116.681 142.956 163.776 1.00 145.48 ? 1434 LYS A O     1 
ATOM   284   C  CB    . LYS A 1 217  ? 114.737 141.241 165.832 1.00 146.10 ? 1434 LYS A CB    1 
ATOM   285   C  CG    . LYS A 1 217  ? 114.339 142.677 166.166 1.00 146.29 ? 1434 LYS A CG    1 
ATOM   286   C  CD    . LYS A 1 217  ? 115.343 143.358 167.091 1.00 147.33 ? 1434 LYS A CD    1 
ATOM   287   C  CE    . LYS A 1 217  ? 115.293 142.770 168.492 1.00 148.10 ? 1434 LYS A CE    1 
ATOM   288   N  NZ    . LYS A 1 217  ? 116.258 143.436 169.412 1.00 146.70 ? 1434 LYS A NZ    1 
ATOM   289   N  N     . LEU A 1 218  ? 117.797 141.397 164.952 1.00 149.79 ? 1435 LEU A N     1 
ATOM   290   C  CA    . LEU A 1 218  ? 119.051 142.144 164.891 1.00 147.87 ? 1435 LEU A CA    1 
ATOM   291   C  C     . LEU A 1 218  ? 119.592 142.220 163.467 1.00 146.86 ? 1435 LEU A C     1 
ATOM   292   O  O     . LEU A 1 218  ? 120.093 143.270 163.046 1.00 146.49 ? 1435 LEU A O     1 
ATOM   293   C  CB    . LEU A 1 218  ? 120.084 141.515 165.826 1.00 146.71 ? 1435 LEU A CB    1 
ATOM   294   C  CG    . LEU A 1 218  ? 120.002 141.951 167.291 1.00 145.11 ? 1435 LEU A CG    1 
ATOM   295   C  CD1   . LEU A 1 218  ? 121.013 141.194 168.138 1.00 139.18 ? 1435 LEU A CD1   1 
ATOM   296   C  CD2   . LEU A 1 218  ? 120.207 143.454 167.419 1.00 145.33 ? 1435 LEU A CD2   1 
ATOM   297   N  N     . THR A 1 219  ? 119.504 141.121 162.712 1.00 147.93 ? 1436 THR A N     1 
ATOM   298   C  CA    . THR A 1 219  ? 119.948 141.146 161.319 1.00 147.06 ? 1436 THR A CA    1 
ATOM   299   C  C     . THR A 1 219  ? 119.082 142.080 160.479 1.00 145.31 ? 1436 THR A C     1 
ATOM   300   O  O     . THR A 1 219  ? 119.596 142.838 159.642 1.00 145.11 ? 1436 THR A O     1 
ATOM   301   C  CB    . THR A 1 219  ? 119.934 139.733 160.736 1.00 146.63 ? 1436 THR A CB    1 
ATOM   302   O  OG1   . THR A 1 219  ? 120.484 138.815 161.689 1.00 149.68 ? 1436 THR A OG1   1 
ATOM   303   C  CG2   . THR A 1 219  ? 120.754 139.678 159.455 1.00 144.09 ? 1436 THR A CG2   1 
ATOM   304   N  N     . LYS A 1 220  ? 117.764 142.049 160.699 1.00 144.29 ? 1437 LYS A N     1 
ATOM   305   C  CA    . LYS A 1 220  ? 116.874 142.970 160.002 1.00 144.71 ? 1437 LYS A CA    1 
ATOM   306   C  C     . LYS A 1 220  ? 117.186 144.414 160.369 1.00 144.56 ? 1437 LYS A C     1 
ATOM   307   O  O     . LYS A 1 220  ? 117.184 145.292 159.501 1.00 143.54 ? 1437 LYS A O     1 
ATOM   308   C  CB    . LYS A 1 220  ? 115.417 142.635 160.321 1.00 144.94 ? 1437 LYS A CB    1 
ATOM   309   N  N     . LEU A 1 221  ? 117.470 144.675 161.648 1.00 144.92 ? 1438 LEU A N     1 
ATOM   310   C  CA    . LEU A 1 221  ? 117.820 146.024 162.079 1.00 144.69 ? 1438 LEU A CA    1 
ATOM   311   C  C     . LEU A 1 221  ? 119.117 146.490 161.436 1.00 143.23 ? 1438 LEU A C     1 
ATOM   312   O  O     . LEU A 1 221  ? 119.242 147.659 161.062 1.00 143.15 ? 1438 LEU A O     1 
ATOM   313   C  CB    . LEU A 1 221  ? 117.932 146.083 163.602 1.00 146.14 ? 1438 LEU A CB    1 
ATOM   314   C  CG    . LEU A 1 221  ? 116.622 146.123 164.393 1.00 149.77 ? 1438 LEU A CG    1 
ATOM   315   C  CD1   . LEU A 1 221  ? 116.880 146.505 165.844 1.00 149.46 ? 1438 LEU A CD1   1 
ATOM   316   C  CD2   . LEU A 1 221  ? 115.614 147.056 163.743 1.00 151.16 ? 1438 LEU A CD2   1 
ATOM   317   N  N     . SER A 1 222  ? 120.101 145.595 161.316 1.00 142.69 ? 1439 SER A N     1 
ATOM   318   C  CA    . SER A 1 222  ? 121.343 145.949 160.635 1.00 141.15 ? 1439 SER A CA    1 
ATOM   319   C  C     . SER A 1 222  ? 121.089 146.283 159.171 1.00 140.93 ? 1439 SER A C     1 
ATOM   320   O  O     . SER A 1 222  ? 121.671 147.234 158.632 1.00 141.12 ? 1439 SER A O     1 
ATOM   321   C  CB    . SER A 1 222  ? 122.356 144.811 160.759 1.00 141.04 ? 1439 SER A CB    1 
ATOM   322   O  OG    . SER A 1 222  ? 123.496 145.057 159.954 1.00 137.39 ? 1439 SER A OG    1 
ATOM   323   N  N     . GLU A 1 223  ? 120.208 145.521 158.515 1.00 140.91 ? 1440 GLU A N     1 
ATOM   324   C  CA    . GLU A 1 223  ? 119.835 145.840 157.138 1.00 141.44 ? 1440 GLU A CA    1 
ATOM   325   C  C     . GLU A 1 223  ? 119.145 147.199 157.050 1.00 141.77 ? 1440 GLU A C     1 
ATOM   326   O  O     . GLU A 1 223  ? 119.381 147.967 156.107 1.00 140.50 ? 1440 GLU A O     1 
ATOM   327   C  CB    . GLU A 1 223  ? 118.935 144.743 156.571 1.00 139.92 ? 1440 GLU A CB    1 
ATOM   328   N  N     . ILE A 1 224  ? 118.293 147.515 158.028 1.00 141.83 ? 1441 ILE A N     1 
ATOM   329   C  CA    . ILE A 1 224  ? 117.592 148.798 158.025 1.00 140.85 ? 1441 ILE A CA    1 
ATOM   330   C  C     . ILE A 1 224  ? 118.567 149.951 158.246 1.00 140.20 ? 1441 ILE A C     1 
ATOM   331   O  O     . ILE A 1 224  ? 118.450 151.005 157.614 1.00 140.71 ? 1441 ILE A O     1 
ATOM   332   C  CB    . ILE A 1 224  ? 116.457 148.797 159.068 1.00 140.82 ? 1441 ILE A CB    1 
ATOM   333   C  CG1   . ILE A 1 224  ? 115.425 147.719 158.731 1.00 139.40 ? 1441 ILE A CG1   1 
ATOM   334   C  CG2   . ILE A 1 224  ? 115.797 150.163 159.168 1.00 141.41 ? 1441 ILE A CG2   1 
ATOM   335   C  CD1   . ILE A 1 224  ? 114.871 147.805 157.330 1.00 135.71 ? 1441 ILE A CD1   1 
ATOM   336   N  N     . GLN A 1 225  ? 119.544 149.776 159.139 1.00 140.00 ? 1442 GLN A N     1 
ATOM   337   C  CA    . GLN A 1 225  ? 120.547 150.823 159.327 1.00 139.60 ? 1442 GLN A CA    1 
ATOM   338   C  C     . GLN A 1 225  ? 121.447 150.975 158.107 1.00 139.65 ? 1442 GLN A C     1 
ATOM   339   O  O     . GLN A 1 225  ? 121.904 152.086 157.818 1.00 139.23 ? 1442 GLN A O     1 
ATOM   340   C  CB    . GLN A 1 225  ? 121.389 150.562 160.581 1.00 140.05 ? 1442 GLN A CB    1 
ATOM   341   C  CG    . GLN A 1 225  ? 120.631 150.318 161.904 1.00 141.37 ? 1442 GLN A CG    1 
ATOM   342   C  CD    . GLN A 1 225  ? 119.798 151.498 162.428 1.00 139.30 ? 1442 GLN A CD    1 
ATOM   343   O  OE1   . GLN A 1 225  ? 119.444 152.428 161.703 1.00 138.45 ? 1442 GLN A OE1   1 
ATOM   344   N  NE2   . GLN A 1 225  ? 119.483 151.447 163.717 1.00 137.76 ? 1442 GLN A NE2   1 
ATOM   345   N  N     . VAL A 1 226  ? 121.717 149.881 157.386 1.00 140.62 ? 1443 VAL A N     1 
ATOM   346   C  CA    . VAL A 1 226  ? 122.434 149.990 156.116 1.00 140.95 ? 1443 VAL A CA    1 
ATOM   347   C  C     . VAL A 1 226  ? 121.620 150.809 155.119 1.00 138.65 ? 1443 VAL A C     1 
ATOM   348   O  O     . VAL A 1 226  ? 122.147 151.712 154.451 1.00 137.45 ? 1443 VAL A O     1 
ATOM   349   C  CB    . VAL A 1 226  ? 122.768 148.588 155.571 1.00 141.49 ? 1443 VAL A CB    1 
ATOM   350   C  CG1   . VAL A 1 226  ? 123.076 148.642 154.080 1.00 139.67 ? 1443 VAL A CG1   1 
ATOM   351   C  CG2   . VAL A 1 226  ? 123.938 147.989 156.334 1.00 140.57 ? 1443 VAL A CG2   1 
ATOM   352   N  N     . ASN A 1 227  ? 120.318 150.514 155.020 1.00 138.10 ? 1444 ASN A N     1 
ATOM   353   C  CA    . ASN A 1 227  ? 119.414 151.321 154.203 1.00 137.96 ? 1444 ASN A CA    1 
ATOM   354   C  C     . ASN A 1 227  ? 119.448 152.784 154.627 1.00 138.47 ? 1444 ASN A C     1 
ATOM   355   O  O     . ASN A 1 227  ? 119.443 153.681 153.781 1.00 136.85 ? 1444 ASN A O     1 
ATOM   356   C  CB    . ASN A 1 227  ? 117.990 150.763 154.304 1.00 138.47 ? 1444 ASN A CB    1 
ATOM   357   C  CG    . ASN A 1 227  ? 116.952 151.635 153.602 1.00 135.17 ? 1444 ASN A CG    1 
ATOM   358   O  OD1   . ASN A 1 227  ? 117.248 152.336 152.634 1.00 133.19 ? 1444 ASN A OD1   1 
ATOM   359   N  ND2   . ASN A 1 227  ? 115.721 151.589 154.097 1.00 132.74 ? 1444 ASN A ND2   1 
ATOM   360   N  N     . TRP A 1 228  ? 119.508 153.039 155.933 1.00 140.58 ? 1445 TRP A N     1 
ATOM   361   C  CA    . TRP A 1 228  ? 119.490 154.408 156.436 1.00 140.03 ? 1445 TRP A CA    1 
ATOM   362   C  C     . TRP A 1 228  ? 120.757 155.163 156.039 1.00 138.76 ? 1445 TRP A C     1 
ATOM   363   O  O     . TRP A 1 228  ? 120.683 156.258 155.464 1.00 137.41 ? 1445 TRP A O     1 
ATOM   364   C  CB    . TRP A 1 228  ? 119.310 154.386 157.956 1.00 141.35 ? 1445 TRP A CB    1 
ATOM   365   C  CG    . TRP A 1 228  ? 118.731 155.639 158.542 1.00 141.98 ? 1445 TRP A CG    1 
ATOM   366   C  CD1   . TRP A 1 228  ? 119.377 156.558 159.316 1.00 143.21 ? 1445 TRP A CD1   1 
ATOM   367   C  CD2   . TRP A 1 228  ? 117.384 156.107 158.403 1.00 143.97 ? 1445 TRP A CD2   1 
ATOM   368   N  NE1   . TRP A 1 228  ? 118.516 157.570 159.667 1.00 145.54 ? 1445 TRP A NE1   1 
ATOM   369   C  CE2   . TRP A 1 228  ? 117.286 157.317 159.119 1.00 147.05 ? 1445 TRP A CE2   1 
ATOM   370   C  CE3   . TRP A 1 228  ? 116.251 155.621 157.742 1.00 143.13 ? 1445 TRP A CE3   1 
ATOM   371   C  CZ2   . TRP A 1 228  ? 116.102 158.048 159.192 1.00 147.74 ? 1445 TRP A CZ2   1 
ATOM   372   C  CZ3   . TRP A 1 228  ? 115.076 156.348 157.816 1.00 143.46 ? 1445 TRP A CZ3   1 
ATOM   373   C  CH2   . TRP A 1 228  ? 115.011 157.548 158.536 1.00 145.54 ? 1445 TRP A CH2   1 
ATOM   374   N  N     . VAL A 1 229  ? 121.931 154.584 156.314 1.00 138.54 ? 1446 VAL A N     1 
ATOM   375   C  CA    . VAL A 1 229  ? 123.173 155.288 155.999 1.00 137.92 ? 1446 VAL A CA    1 
ATOM   376   C  C     . VAL A 1 229  ? 123.287 155.496 154.495 1.00 137.06 ? 1446 VAL A C     1 
ATOM   377   O  O     . VAL A 1 229  ? 123.686 156.575 154.033 1.00 135.81 ? 1446 VAL A O     1 
ATOM   378   C  CB    . VAL A 1 229  ? 124.407 154.559 156.573 1.00 137.89 ? 1446 VAL A CB    1 
ATOM   379   C  CG1   . VAL A 1 229  ? 124.473 154.721 158.083 1.00 138.17 ? 1446 VAL A CG1   1 
ATOM   380   C  CG2   . VAL A 1 229  ? 124.450 153.093 156.178 1.00 138.27 ? 1446 VAL A CG2   1 
ATOM   381   N  N     . GLU A 1 230  ? 122.869 154.501 153.706 1.00 135.76 ? 1447 GLU A N     1 
ATOM   382   C  CA    . GLU A 1 230  ? 122.897 154.672 152.260 1.00 132.98 ? 1447 GLU A CA    1 
ATOM   383   C  C     . GLU A 1 230  ? 121.866 155.695 151.794 1.00 133.09 ? 1447 GLU A C     1 
ATOM   384   O  O     . GLU A 1 230  ? 122.093 156.388 150.798 1.00 132.51 ? 1447 GLU A O     1 
ATOM   385   C  CB    . GLU A 1 230  ? 122.695 153.325 151.567 1.00 133.97 ? 1447 GLU A CB    1 
ATOM   386   C  CG    . GLU A 1 230  ? 123.856 152.360 151.783 1.00 135.63 ? 1447 GLU A CG    1 
ATOM   387   C  CD    . GLU A 1 230  ? 123.885 151.230 150.775 1.00 137.65 ? 1447 GLU A CD    1 
ATOM   388   O  OE1   . GLU A 1 230  ? 123.444 151.444 149.626 1.00 135.91 ? 1447 GLU A OE1   1 
ATOM   389   O  OE2   . GLU A 1 230  ? 124.357 150.130 151.129 1.00 138.76 ? 1447 GLU A OE2   1 
ATOM   390   N  N     . VAL A 1 231  ? 120.747 155.850 152.513 1.00 134.88 ? 1448 VAL A N     1 
ATOM   391   C  CA    . VAL A 1 231  ? 119.738 156.770 152.000 1.00 134.49 ? 1448 VAL A CA    1 
ATOM   392   C  C     . VAL A 1 231  ? 120.132 158.218 152.270 1.00 131.92 ? 1448 VAL A C     1 
ATOM   393   O  O     . VAL A 1 231  ? 119.892 159.079 151.419 1.00 128.51 ? 1448 VAL A O     1 
ATOM   394   C  CB    . VAL A 1 231  ? 118.315 156.443 152.513 1.00 135.66 ? 1448 VAL A CB    1 
ATOM   395   C  CG1   . VAL A 1 231  ? 118.084 156.861 153.950 1.00 137.19 ? 1448 VAL A CG1   1 
ATOM   396   C  CG2   . VAL A 1 231  ? 117.276 157.098 151.614 1.00 131.25 ? 1448 VAL A CG2   1 
ATOM   397   N  N     . GLN A 1 232  ? 120.786 158.532 153.400 1.00 132.00 ? 1449 GLN A N     1 
ATOM   398   C  CA    . GLN A 1 232  ? 121.315 159.904 153.460 1.00 130.20 ? 1449 GLN A CA    1 
ATOM   399   C  C     . GLN A 1 232  ? 122.562 160.070 152.594 1.00 132.76 ? 1449 GLN A C     1 
ATOM   400   O  O     . GLN A 1 232  ? 122.799 161.164 152.060 1.00 132.16 ? 1449 GLN A O     1 
ATOM   401   C  CB    . GLN A 1 232  ? 121.590 160.443 154.877 1.00 130.66 ? 1449 GLN A CB    1 
ATOM   402   C  CG    . GLN A 1 232  ? 120.559 160.233 155.977 1.00 136.00 ? 1449 GLN A CG    1 
ATOM   403   C  CD    . GLN A 1 232  ? 120.579 158.878 156.589 1.00 138.31 ? 1449 GLN A CD    1 
ATOM   404   O  OE1   . GLN A 1 232  ? 121.647 158.335 156.875 1.00 136.25 ? 1449 GLN A OE1   1 
ATOM   405   N  NE2   . GLN A 1 232  ? 119.404 158.291 156.772 1.00 139.23 ? 1449 GLN A NE2   1 
ATOM   406   N  N     . PHE A 1 233  ? 123.349 159.002 152.404 1.00 134.20 ? 1450 PHE A N     1 
ATOM   407   C  CA    . PHE A 1 233  ? 124.496 159.094 151.504 1.00 132.86 ? 1450 PHE A CA    1 
ATOM   408   C  C     . PHE A 1 233  ? 124.068 159.397 150.073 1.00 132.89 ? 1450 PHE A C     1 
ATOM   409   O  O     . PHE A 1 233  ? 124.796 160.072 149.336 1.00 132.55 ? 1450 PHE A O     1 
ATOM   410   C  CB    . PHE A 1 233  ? 125.306 157.798 151.552 1.00 130.73 ? 1450 PHE A CB    1 
ATOM   411   N  N     . TYR A 1 234  ? 122.895 158.912 149.666 1.00 132.92 ? 1451 TYR A N     1 
ATOM   412   C  CA    . TYR A 1 234  ? 122.371 159.246 148.346 1.00 131.37 ? 1451 TYR A CA    1 
ATOM   413   C  C     . TYR A 1 234  ? 121.630 160.579 148.367 1.00 132.28 ? 1451 TYR A C     1 
ATOM   414   O  O     . TYR A 1 234  ? 121.711 161.359 147.409 1.00 132.27 ? 1451 TYR A O     1 
ATOM   415   C  CB    . TYR A 1 234  ? 121.445 158.135 147.835 1.00 129.70 ? 1451 TYR A CB    1 
ATOM   416   C  CG    . TYR A 1 234  ? 122.026 156.728 147.826 1.00 129.73 ? 1451 TYR A CG    1 
ATOM   417   C  CD1   . TYR A 1 234  ? 123.399 156.507 147.769 1.00 129.50 ? 1451 TYR A CD1   1 
ATOM   418   C  CD2   . TYR A 1 234  ? 121.189 155.617 147.862 1.00 127.01 ? 1451 TYR A CD2   1 
ATOM   419   C  CE1   . TYR A 1 234  ? 123.919 155.223 147.757 1.00 128.37 ? 1451 TYR A CE1   1 
ATOM   420   C  CE2   . TYR A 1 234  ? 121.702 154.332 147.851 1.00 126.55 ? 1451 TYR A CE2   1 
ATOM   421   C  CZ    . TYR A 1 234  ? 123.065 154.141 147.797 1.00 129.23 ? 1451 TYR A CZ    1 
ATOM   422   O  OH    . TYR A 1 234  ? 123.576 152.863 147.784 1.00 132.14 ? 1451 TYR A OH    1 
ATOM   423   N  N     . TRP A 1 235  ? 120.912 160.870 149.456 1.00 132.85 ? 1452 TRP A N     1 
ATOM   424   C  CA    . TRP A 1 235  ? 120.108 162.080 149.497 1.00 131.64 ? 1452 TRP A CA    1 
ATOM   425   C  C     . TRP A 1 235  ? 120.936 163.338 149.679 1.00 130.97 ? 1452 TRP A C     1 
ATOM   426   O  O     . TRP A 1 235  ? 120.392 164.425 149.496 1.00 132.27 ? 1452 TRP A O     1 
ATOM   427   C  CB    . TRP A 1 235  ? 119.041 161.993 150.587 1.00 132.21 ? 1452 TRP A CB    1 
ATOM   428   C  CG    . TRP A 1 235  ? 117.834 162.803 150.226 1.00 132.25 ? 1452 TRP A CG    1 
ATOM   429   C  CD1   . TRP A 1 235  ? 117.580 164.097 150.577 1.00 129.86 ? 1452 TRP A CD1   1 
ATOM   430   C  CD2   . TRP A 1 235  ? 116.755 162.401 149.376 1.00 133.41 ? 1452 TRP A CD2   1 
ATOM   431   N  NE1   . TRP A 1 235  ? 116.393 164.513 150.029 1.00 130.39 ? 1452 TRP A NE1   1 
ATOM   432   C  CE2   . TRP A 1 235  ? 115.869 163.491 149.283 1.00 133.34 ? 1452 TRP A CE2   1 
ATOM   433   C  CE3   . TRP A 1 235  ? 116.443 161.218 148.699 1.00 132.89 ? 1452 TRP A CE3   1 
ATOM   434   C  CZ2   . TRP A 1 235  ? 114.693 163.434 148.544 1.00 134.31 ? 1452 TRP A CZ2   1 
ATOM   435   C  CZ3   . TRP A 1 235  ? 115.277 161.166 147.963 1.00 130.84 ? 1452 TRP A CZ3   1 
ATOM   436   C  CH2   . TRP A 1 235  ? 114.416 162.267 147.895 1.00 131.44 ? 1452 TRP A CH2   1 
ATOM   437   N  N     . LEU A 1 236  ? 122.226 163.224 150.001 1.00 129.31 ? 1453 LEU A N     1 
ATOM   438   C  CA    . LEU A 1 236  ? 123.108 164.381 149.863 1.00 131.11 ? 1453 LEU A CA    1 
ATOM   439   C  C     . LEU A 1 236  ? 123.005 164.971 148.456 1.00 132.11 ? 1453 LEU A C     1 
ATOM   440   O  O     . LEU A 1 236  ? 122.524 166.097 148.265 1.00 132.25 ? 1453 LEU A O     1 
ATOM   441   C  CB    . LEU A 1 236  ? 124.550 163.982 150.186 1.00 129.73 ? 1453 LEU A CB    1 
ATOM   442   N  N     . ASP A 1 237  ? 123.380 164.181 147.446 1.00 130.47 ? 1454 ASP A N     1 
ATOM   443   C  CA    . ASP A 1 237  ? 123.265 164.636 146.063 1.00 129.12 ? 1454 ASP A CA    1 
ATOM   444   C  C     . ASP A 1 237  ? 121.812 164.763 145.620 1.00 129.06 ? 1454 ASP A C     1 
ATOM   445   O  O     . ASP A 1 237  ? 121.491 165.644 144.811 1.00 126.59 ? 1454 ASP A O     1 
ATOM   446   C  CB    . ASP A 1 237  ? 124.017 163.687 145.131 1.00 126.10 ? 1454 ASP A CB    1 
ATOM   447   C  CG    . ASP A 1 237  ? 124.550 164.385 143.892 1.00 120.00 ? 1454 ASP A CG    1 
ATOM   448   O  OD1   . ASP A 1 237  ? 124.354 165.612 143.766 1.00 120.39 ? 1454 ASP A OD1   1 
ATOM   449   O  OD2   . ASP A 1 237  ? 125.165 163.706 143.044 1.00 103.26 ? 1454 ASP A OD2   1 
ATOM   450   N  N     . LEU A 1 238  ? 120.923 163.900 146.124 1.00 132.27 ? 1455 LEU A N     1 
ATOM   451   C  CA    . LEU A 1 238  ? 119.530 163.957 145.690 1.00 132.90 ? 1455 LEU A CA    1 
ATOM   452   C  C     . LEU A 1 238  ? 118.835 165.238 146.146 1.00 131.15 ? 1455 LEU A C     1 
ATOM   453   O  O     . LEU A 1 238  ? 118.031 165.795 145.396 1.00 129.14 ? 1455 LEU A O     1 
ATOM   454   C  CB    . LEU A 1 238  ? 118.772 162.720 146.170 1.00 133.63 ? 1455 LEU A CB    1 
ATOM   455   C  CG    . LEU A 1 238  ? 119.137 161.453 145.386 1.00 131.13 ? 1455 LEU A CG    1 
ATOM   456   C  CD1   . LEU A 1 238  ? 118.389 160.227 145.894 1.00 127.17 ? 1455 LEU A CD1   1 
ATOM   457   C  CD2   . LEU A 1 238  ? 118.897 161.654 143.894 1.00 126.99 ? 1455 LEU A CD2   1 
ATOM   458   N  N     . TYR A 1 239  ? 119.124 165.728 147.352 1.00 132.02 ? 1456 TYR A N     1 
ATOM   459   C  CA    . TYR A 1 239  ? 118.626 167.033 147.758 1.00 134.09 ? 1456 TYR A CA    1 
ATOM   460   C  C     . TYR A 1 239  ? 119.417 168.162 147.115 1.00 135.86 ? 1456 TYR A C     1 
ATOM   461   O  O     . TYR A 1 239  ? 118.869 169.251 146.906 1.00 138.05 ? 1456 TYR A O     1 
ATOM   462   C  CB    . TYR A 1 239  ? 118.664 167.169 149.281 1.00 134.02 ? 1456 TYR A CB    1 
ATOM   463   C  CG    . TYR A 1 239  ? 118.075 168.465 149.789 1.00 132.44 ? 1456 TYR A CG    1 
ATOM   464   C  CD1   . TYR A 1 239  ? 116.704 168.680 149.775 1.00 131.14 ? 1456 TYR A CD1   1 
ATOM   465   C  CD2   . TYR A 1 239  ? 118.893 169.478 150.272 1.00 130.87 ? 1456 TYR A CD2   1 
ATOM   466   C  CE1   . TYR A 1 239  ? 116.162 169.867 150.234 1.00 130.76 ? 1456 TYR A CE1   1 
ATOM   467   C  CE2   . TYR A 1 239  ? 118.362 170.667 150.732 1.00 133.66 ? 1456 TYR A CE2   1 
ATOM   468   C  CZ    . TYR A 1 239  ? 116.996 170.856 150.712 1.00 134.01 ? 1456 TYR A CZ    1 
ATOM   469   O  OH    . TYR A 1 239  ? 116.465 172.039 151.171 1.00 136.51 ? 1456 TYR A OH    1 
ATOM   470   N  N     . GLY A 1 240  ? 120.697 167.931 146.798 1.00 133.36 ? 1457 GLY A N     1 
ATOM   471   C  CA    . GLY A 1 240  ? 121.458 168.946 146.090 1.00 132.08 ? 1457 GLY A CA    1 
ATOM   472   C  C     . GLY A 1 240  ? 120.920 169.247 144.705 1.00 131.88 ? 1457 GLY A C     1 
ATOM   473   O  O     . GLY A 1 240  ? 120.991 170.389 144.243 1.00 131.62 ? 1457 GLY A O     1 
ATOM   474   N  N     . ILE A 1 241  ? 120.377 168.238 144.024 1.00 131.49 ? 1458 ILE A N     1 
ATOM   475   C  CA    . ILE A 1 241  ? 119.917 168.395 142.647 1.00 129.79 ? 1458 ILE A CA    1 
ATOM   476   C  C     . ILE A 1 241  ? 118.407 168.299 142.508 1.00 130.88 ? 1458 ILE A C     1 
ATOM   477   O  O     . ILE A 1 241  ? 117.885 168.540 141.409 1.00 128.66 ? 1458 ILE A O     1 
ATOM   478   C  CB    . ILE A 1 241  ? 120.595 167.378 141.713 1.00 119.61 ? 1458 ILE A CB    1 
ATOM   479   C  CG1   . ILE A 1 241  ? 120.018 165.982 141.956 1.00 117.69 ? 1458 ILE A CG1   1 
ATOM   480   C  CG2   . ILE A 1 241  ? 122.096 167.401 141.927 1.00 115.97 ? 1458 ILE A CG2   1 
ATOM   481   C  CD1   . ILE A 1 241  ? 120.050 165.087 140.749 1.00 111.55 ? 1458 ILE A CD1   1 
ATOM   482   N  N     . LEU A 1 242  ? 117.690 167.958 143.564 1.00 133.12 ? 1459 LEU A N     1 
ATOM   483   C  CA    . LEU A 1 242  ? 116.240 167.818 143.479 1.00 132.91 ? 1459 LEU A CA    1 
ATOM   484   C  C     . LEU A 1 242  ? 115.504 168.718 144.458 1.00 131.53 ? 1459 LEU A C     1 
ATOM   485   O  O     . LEU A 1 242  ? 114.441 169.244 144.119 1.00 130.22 ? 1459 LEU A O     1 
ATOM   486   C  CB    . LEU A 1 242  ? 115.832 166.350 143.716 1.00 131.62 ? 1459 LEU A CB    1 
ATOM   487   C  CG    . LEU A 1 242  ? 116.311 165.305 142.702 1.00 127.71 ? 1459 LEU A CG    1 
ATOM   488   C  CD1   . LEU A 1 242  ? 115.822 163.914 143.086 1.00 121.10 ? 1459 LEU A CD1   1 
ATOM   489   C  CD2   . LEU A 1 242  ? 115.870 165.666 141.296 1.00 128.92 ? 1459 LEU A CD2   1 
ATOM   490   N  N     . GLY A 1 243  ? 116.039 168.910 145.662 1.00 131.54 ? 1460 GLY A N     1 
ATOM   491   C  CA    . GLY A 1 243  ? 115.418 169.801 146.622 1.00 132.58 ? 1460 GLY A CA    1 
ATOM   492   C  C     . GLY A 1 243  ? 115.669 171.272 146.383 1.00 134.40 ? 1460 GLY A C     1 
ATOM   493   O  O     . GLY A 1 243  ? 115.051 172.108 147.048 1.00 137.11 ? 1460 GLY A O     1 
ATOM   494   N  N     . GLU A 1 244  ? 116.564 171.608 145.449 1.00 131.79 ? 1461 GLU A N     1 
ATOM   495   C  CA    . GLU A 1 244  ? 116.842 173.003 145.132 1.00 132.03 ? 1461 GLU A CA    1 
ATOM   496   C  C     . GLU A 1 244  ? 116.967 173.234 143.629 1.00 132.01 ? 1461 GLU A C     1 
ATOM   497   O  O     . GLU A 1 244  ? 117.459 174.290 143.213 1.00 131.35 ? 1461 GLU A O     1 
ATOM   498   C  CB    . GLU A 1 244  ? 118.120 173.477 145.834 1.00 130.36 ? 1461 GLU A CB    1 
ATOM   499   N  N     . ASN A 1 245  ? 116.536 172.279 142.807 1.00 131.92 ? 1462 ASN A N     1 
ATOM   500   C  CA    . ASN A 1 245  ? 116.639 172.408 141.356 1.00 131.09 ? 1462 ASN A CA    1 
ATOM   501   C  C     . ASN A 1 245  ? 115.551 171.548 140.729 1.00 127.94 ? 1462 ASN A C     1 
ATOM   502   O  O     . ASN A 1 245  ? 115.668 170.319 140.706 1.00 124.57 ? 1462 ASN A O     1 
ATOM   503   C  CB    . ASN A 1 245  ? 118.022 171.990 140.866 1.00 128.85 ? 1462 ASN A CB    1 
ATOM   504   C  CG    . ASN A 1 245  ? 118.531 172.866 139.738 1.00 123.01 ? 1462 ASN A CG    1 
ATOM   505   O  OD1   . ASN A 1 245  ? 117.806 173.159 138.787 1.00 119.58 ? 1462 ASN A OD1   1 
ATOM   506   N  ND2   . ASN A 1 245  ? 119.788 173.284 139.835 1.00 119.09 ? 1462 ASN A ND2   1 
ATOM   507   N  N     . LEU A 1 246  ? 114.501 172.192 140.222 1.00 128.30 ? 1463 LEU A N     1 
ATOM   508   C  CA    . LEU A 1 246  ? 113.378 171.476 139.629 1.00 128.36 ? 1463 LEU A CA    1 
ATOM   509   C  C     . LEU A 1 246  ? 113.617 171.082 138.178 1.00 126.61 ? 1463 LEU A C     1 
ATOM   510   O  O     . LEU A 1 246  ? 112.830 170.302 137.630 1.00 127.72 ? 1463 LEU A O     1 
ATOM   511   C  CB    . LEU A 1 246  ? 112.103 172.321 139.722 1.00 128.42 ? 1463 LEU A CB    1 
ATOM   512   C  CG    . LEU A 1 246  ? 111.289 172.252 141.018 1.00 129.38 ? 1463 LEU A CG    1 
ATOM   513   C  CD1   . LEU A 1 246  ? 111.927 173.073 142.132 1.00 127.70 ? 1463 LEU A CD1   1 
ATOM   514   C  CD2   . LEU A 1 246  ? 109.857 172.703 140.770 1.00 127.95 ? 1463 LEU A CD2   1 
ATOM   515   N  N     . ASP A 1 247  ? 114.672 171.595 137.542 1.00 122.05 ? 1464 ASP A N     1 
ATOM   516   C  CA    . ASP A 1 247  ? 114.900 171.283 136.135 1.00 118.31 ? 1464 ASP A CA    1 
ATOM   517   C  C     . ASP A 1 247  ? 115.341 169.835 135.949 1.00 117.14 ? 1464 ASP A C     1 
ATOM   518   O  O     . ASP A 1 247  ? 114.947 169.184 134.974 1.00 116.10 ? 1464 ASP A O     1 
ATOM   519   C  CB    . ASP A 1 247  ? 115.929 172.243 135.541 1.00 111.98 ? 1464 ASP A CB    1 
ATOM   520   C  CG    . ASP A 1 247  ? 115.725 172.471 134.054 1.00 107.23 ? 1464 ASP A CG    1 
ATOM   521   O  OD1   . ASP A 1 247  ? 115.073 171.627 133.404 1.00 110.61 ? 1464 ASP A OD1   1 
ATOM   522   O  OD2   . ASP A 1 247  ? 116.211 173.497 133.535 1.00 97.71  ? 1464 ASP A OD2   1 
ATOM   523   N  N     . ILE A 1 248  ? 116.159 169.314 136.869 1.00 117.81 ? 1465 ILE A N     1 
ATOM   524   C  CA    . ILE A 1 248  ? 116.556 167.909 136.790 1.00 120.17 ? 1465 ILE A CA    1 
ATOM   525   C  C     . ILE A 1 248  ? 115.338 167.009 136.953 1.00 125.06 ? 1465 ILE A C     1 
ATOM   526   O  O     . ILE A 1 248  ? 115.118 166.086 136.161 1.00 126.54 ? 1465 ILE A O     1 
ATOM   527   C  CB    . ILE A 1 248  ? 117.639 167.577 137.834 1.00 120.75 ? 1465 ILE A CB    1 
ATOM   528   C  CG1   . ILE A 1 248  ? 118.942 168.332 137.557 1.00 107.38 ? 1465 ILE A CG1   1 
ATOM   529   C  CG2   . ILE A 1 248  ? 117.906 166.079 137.867 1.00 114.17 ? 1465 ILE A CG2   1 
ATOM   530   C  CD1   . ILE A 1 248  ? 119.086 169.624 138.322 1.00 112.37 ? 1465 ILE A CD1   1 
ATOM   531   N  N     . GLN A 1 249  ? 114.510 167.286 137.963 1.00 125.66 ? 1466 GLN A N     1 
ATOM   532   C  CA    . GLN A 1 249  ? 113.335 166.457 138.202 1.00 126.58 ? 1466 GLN A CA    1 
ATOM   533   C  C     . GLN A 1 249  ? 112.246 166.658 137.158 1.00 129.24 ? 1466 GLN A C     1 
ATOM   534   O  O     . GLN A 1 249  ? 111.339 165.826 137.075 1.00 130.78 ? 1466 GLN A O     1 
ATOM   535   C  CB    . GLN A 1 249  ? 112.771 166.720 139.600 1.00 126.92 ? 1466 GLN A CB    1 
ATOM   536   C  CG    . GLN A 1 249  ? 111.999 168.015 139.740 1.00 130.34 ? 1466 GLN A CG    1 
ATOM   537   C  CD    . GLN A 1 249  ? 111.836 168.439 141.185 1.00 131.84 ? 1466 GLN A CD    1 
ATOM   538   O  OE1   . GLN A 1 249  ? 112.772 168.940 141.805 1.00 129.70 ? 1466 GLN A OE1   1 
ATOM   539   N  NE2   . GLN A 1 249  ? 110.641 168.241 141.729 1.00 133.61 ? 1466 GLN A NE2   1 
ATOM   540   N  N     . ASN A 1 250  ? 112.305 167.733 136.371 1.00 128.72 ? 1467 ASN A N     1 
ATOM   541   C  CA    . ASN A 1 250  ? 111.365 167.956 135.280 1.00 128.92 ? 1467 ASN A CA    1 
ATOM   542   C  C     . ASN A 1 250  ? 112.039 167.876 133.914 1.00 129.01 ? 1467 ASN A C     1 
ATOM   543   O  O     . ASN A 1 250  ? 111.537 168.450 132.942 1.00 129.26 ? 1467 ASN A O     1 
ATOM   544   C  CB    . ASN A 1 250  ? 110.667 169.305 135.453 1.00 130.63 ? 1467 ASN A CB    1 
ATOM   545   C  CG    . ASN A 1 250  ? 109.440 169.214 136.340 1.00 134.43 ? 1467 ASN A CG    1 
ATOM   546   O  OD1   . ASN A 1 250  ? 109.421 168.464 137.316 1.00 132.83 ? 1467 ASN A OD1   1 
ATOM   547   N  ND2   . ASN A 1 250  ? 108.409 169.980 136.004 1.00 139.53 ? 1467 ASN A ND2   1 
ATOM   548   N  N     . PHE A 1 251  ? 113.175 167.180 133.827 1.00 127.90 ? 1468 PHE A N     1 
ATOM   549   C  CA    . PHE A 1 251  ? 113.932 167.113 132.580 1.00 126.04 ? 1468 PHE A CA    1 
ATOM   550   C  C     . PHE A 1 251  ? 113.184 166.326 131.507 1.00 129.59 ? 1468 PHE A C     1 
ATOM   551   O  O     . PHE A 1 251  ? 112.828 166.870 130.455 1.00 131.11 ? 1468 PHE A O     1 
ATOM   552   C  CB    . PHE A 1 251  ? 115.306 166.497 132.851 1.00 118.61 ? 1468 PHE A CB    1 
ATOM   553   C  CG    . PHE A 1 251  ? 116.305 166.738 131.762 1.00 108.81 ? 1468 PHE A CG    1 
ATOM   554   C  CD1   . PHE A 1 251  ? 117.025 167.921 131.716 1.00 100.82 ? 1468 PHE A CD1   1 
ATOM   555   C  CD2   . PHE A 1 251  ? 116.534 165.780 130.791 1.00 101.63 ? 1468 PHE A CD2   1 
ATOM   556   C  CE1   . PHE A 1 251  ? 117.949 168.146 130.716 1.00 91.99  ? 1468 PHE A CE1   1 
ATOM   557   C  CE2   . PHE A 1 251  ? 117.457 165.999 129.790 1.00 91.58  ? 1468 PHE A CE2   1 
ATOM   558   C  CZ    . PHE A 1 251  ? 118.166 167.184 129.752 1.00 88.03  ? 1468 PHE A CZ    1 
ATOM   559   N  N     . LEU A 1 252  ? 112.932 165.040 131.755 1.00 130.70 ? 1469 LEU A N     1 
ATOM   560   C  CA    . LEU A 1 252  ? 112.235 164.198 130.794 1.00 133.30 ? 1469 LEU A CA    1 
ATOM   561   C  C     . LEU A 1 252  ? 110.923 163.700 131.387 1.00 135.72 ? 1469 LEU A C     1 
ATOM   562   O  O     . LEU A 1 252  ? 110.837 163.478 132.596 1.00 136.34 ? 1469 LEU A O     1 
ATOM   563   C  CB    . LEU A 1 252  ? 113.094 162.997 130.377 1.00 131.55 ? 1469 LEU A CB    1 
ATOM   564   N  N     . PRO A 1 253  ? 109.889 163.486 130.551 1.00 136.84 ? 1470 PRO A N     1 
ATOM   565   C  CA    . PRO A 1 253  ? 108.534 163.237 131.077 1.00 136.80 ? 1470 PRO A CA    1 
ATOM   566   C  C     . PRO A 1 253  ? 108.394 161.960 131.895 1.00 137.91 ? 1470 PRO A C     1 
ATOM   567   O  O     . PRO A 1 253  ? 107.872 161.994 133.016 1.00 138.69 ? 1470 PRO A O     1 
ATOM   568   C  CB    . PRO A 1 253  ? 107.679 163.173 129.805 1.00 136.17 ? 1470 PRO A CB    1 
ATOM   569   N  N     . LEU A 1 254  ? 108.840 160.828 131.342 1.00 137.01 ? 1471 LEU A N     1 
ATOM   570   C  CA    . LEU A 1 254  ? 108.857 159.590 132.116 1.00 137.79 ? 1471 LEU A CA    1 
ATOM   571   C  C     . LEU A 1 254  ? 109.792 159.713 133.311 1.00 137.21 ? 1471 LEU A C     1 
ATOM   572   O  O     . LEU A 1 254  ? 109.481 159.237 134.409 1.00 134.14 ? 1471 LEU A O     1 
ATOM   573   C  CB    . LEU A 1 254  ? 109.270 158.419 131.226 1.00 136.28 ? 1471 LEU A CB    1 
ATOM   574   N  N     . GLU A 1 255  ? 110.938 160.364 133.114 1.00 137.16 ? 1472 GLU A N     1 
ATOM   575   C  CA    . GLU A 1 255  ? 111.850 160.642 134.215 1.00 133.69 ? 1472 GLU A CA    1 
ATOM   576   C  C     . GLU A 1 255  ? 111.232 161.607 135.225 1.00 132.79 ? 1472 GLU A C     1 
ATOM   577   O  O     . GLU A 1 255  ? 111.481 161.485 136.431 1.00 129.65 ? 1472 GLU A O     1 
ATOM   578   C  CB    . GLU A 1 255  ? 113.163 161.179 133.645 1.00 131.22 ? 1472 GLU A CB    1 
ATOM   579   C  CG    . GLU A 1 255  ? 114.238 161.488 134.655 1.00 129.26 ? 1472 GLU A CG    1 
ATOM   580   C  CD    . GLU A 1 255  ? 114.351 162.965 134.927 1.00 129.18 ? 1472 GLU A CD    1 
ATOM   581   O  OE1   . GLU A 1 255  ? 113.906 163.766 134.079 1.00 126.50 ? 1472 GLU A OE1   1 
ATOM   582   O  OE2   . GLU A 1 255  ? 114.901 163.326 135.981 1.00 129.24 ? 1472 GLU A OE2   1 
ATOM   583   N  N     . THR A 1 256  ? 110.414 162.558 134.757 1.00 136.16 ? 1473 THR A N     1 
ATOM   584   C  CA    . THR A 1 256  ? 109.691 163.436 135.674 1.00 137.32 ? 1473 THR A CA    1 
ATOM   585   C  C     . THR A 1 256  ? 108.708 162.650 136.530 1.00 138.63 ? 1473 THR A C     1 
ATOM   586   O  O     . THR A 1 256  ? 108.599 162.887 137.738 1.00 138.64 ? 1473 THR A O     1 
ATOM   587   C  CB    . THR A 1 256  ? 108.955 164.532 134.900 1.00 136.71 ? 1473 THR A CB    1 
ATOM   588   O  OG1   . THR A 1 256  ? 109.888 165.248 134.080 1.00 136.03 ? 1473 THR A OG1   1 
ATOM   589   C  CG2   . THR A 1 256  ? 108.278 165.508 135.852 1.00 134.03 ? 1473 THR A CG2   1 
ATOM   590   N  N     . SER A 1 257  ? 107.982 161.709 135.921 1.00 139.35 ? 1474 SER A N     1 
ATOM   591   C  CA    . SER A 1 257  ? 107.069 160.866 136.690 1.00 139.96 ? 1474 SER A CA    1 
ATOM   592   C  C     . SER A 1 257  ? 107.830 159.985 137.673 1.00 138.53 ? 1474 SER A C     1 
ATOM   593   O  O     . SER A 1 257  ? 107.371 159.752 138.799 1.00 139.00 ? 1474 SER A O     1 
ATOM   594   C  CB    . SER A 1 257  ? 106.224 160.012 135.745 1.00 141.11 ? 1474 SER A CB    1 
ATOM   595   O  OG    . SER A 1 257  ? 107.029 159.068 135.059 1.00 138.97 ? 1474 SER A OG    1 
ATOM   596   N  N     . LYS A 1 258  ? 108.997 159.486 137.259 1.00 136.50 ? 1475 LYS A N     1 
ATOM   597   C  CA    . LYS A 1 258  ? 109.823 158.672 138.143 1.00 136.00 ? 1475 LYS A CA    1 
ATOM   598   C  C     . LYS A 1 258  ? 110.297 159.470 139.354 1.00 135.33 ? 1475 LYS A C     1 
ATOM   599   O  O     . LYS A 1 258  ? 110.240 158.980 140.487 1.00 134.12 ? 1475 LYS A O     1 
ATOM   600   C  CB    . LYS A 1 258  ? 111.004 158.101 137.357 1.00 133.83 ? 1475 LYS A CB    1 
ATOM   601   C  CG    . LYS A 1 258  ? 111.973 157.255 138.162 1.00 126.51 ? 1475 LYS A CG    1 
ATOM   602   C  CD    . LYS A 1 258  ? 113.287 157.985 138.371 1.00 123.03 ? 1475 LYS A CD    1 
ATOM   603   C  CE    . LYS A 1 258  ? 114.046 158.113 137.059 1.00 123.66 ? 1475 LYS A CE    1 
ATOM   604   N  NZ    . LYS A 1 258  ? 115.380 158.753 137.232 1.00 113.76 ? 1475 LYS A NZ    1 
ATOM   605   N  N     . PHE A 1 259  ? 110.735 160.714 139.147 1.00 134.57 ? 1476 PHE A N     1 
ATOM   606   C  CA    . PHE A 1 259  ? 111.145 161.524 140.290 1.00 133.75 ? 1476 PHE A CA    1 
ATOM   607   C  C     . PHE A 1 259  ? 109.960 162.032 141.105 1.00 135.61 ? 1476 PHE A C     1 
ATOM   608   O  O     . PHE A 1 259  ? 110.117 162.298 142.301 1.00 135.74 ? 1476 PHE A O     1 
ATOM   609   C  CB    . PHE A 1 259  ? 112.026 162.694 139.844 1.00 133.23 ? 1476 PHE A CB    1 
ATOM   610   C  CG    . PHE A 1 259  ? 113.465 162.313 139.619 1.00 132.45 ? 1476 PHE A CG    1 
ATOM   611   C  CD1   . PHE A 1 259  ? 113.927 161.065 139.993 1.00 130.04 ? 1476 PHE A CD1   1 
ATOM   612   C  CD2   . PHE A 1 259  ? 114.368 163.217 139.090 1.00 131.49 ? 1476 PHE A CD2   1 
ATOM   613   C  CE1   . PHE A 1 259  ? 115.249 160.709 139.808 1.00 125.05 ? 1476 PHE A CE1   1 
ATOM   614   C  CE2   . PHE A 1 259  ? 115.696 162.870 138.908 1.00 128.86 ? 1476 PHE A CE2   1 
ATOM   615   C  CZ    . PHE A 1 259  ? 116.134 161.613 139.264 1.00 123.71 ? 1476 PHE A CZ    1 
ATOM   616   N  N     . LYS A 1 260  ? 108.776 162.159 140.502 1.00 136.99 ? 1477 LYS A N     1 
ATOM   617   C  CA    . LYS A 1 260  ? 107.581 162.460 141.286 1.00 137.34 ? 1477 LYS A CA    1 
ATOM   618   C  C     . LYS A 1 260  ? 107.227 161.301 142.211 1.00 136.97 ? 1477 LYS A C     1 
ATOM   619   O  O     . LYS A 1 260  ? 106.871 161.513 143.378 1.00 135.92 ? 1477 LYS A O     1 
ATOM   620   C  CB    . LYS A 1 260  ? 106.412 162.787 140.358 1.00 135.22 ? 1477 LYS A CB    1 
ATOM   621   N  N     . SER A 1 261  ? 107.320 160.069 141.704 1.00 138.12 ? 1478 SER A N     1 
ATOM   622   C  CA    . SER A 1 261  ? 107.140 158.897 142.555 1.00 138.60 ? 1478 SER A CA    1 
ATOM   623   C  C     . SER A 1 261  ? 108.225 158.827 143.622 1.00 137.73 ? 1478 SER A C     1 
ATOM   624   O  O     . SER A 1 261  ? 107.965 158.413 144.758 1.00 138.49 ? 1478 SER A O     1 
ATOM   625   C  CB    . SER A 1 261  ? 107.134 157.627 141.706 1.00 139.50 ? 1478 SER A CB    1 
ATOM   626   O  OG    . SER A 1 261  ? 108.348 157.490 140.986 1.00 137.95 ? 1478 SER A OG    1 
ATOM   627   N  N     . LEU A 1 262  ? 109.451 159.222 143.265 1.00 136.17 ? 1479 LEU A N     1 
ATOM   628   C  CA    . LEU A 1 262  ? 110.532 159.350 144.239 1.00 135.45 ? 1479 LEU A CA    1 
ATOM   629   C  C     . LEU A 1 262  ? 110.148 160.291 145.376 1.00 136.18 ? 1479 LEU A C     1 
ATOM   630   O  O     . LEU A 1 262  ? 110.310 159.956 146.555 1.00 135.38 ? 1479 LEU A O     1 
ATOM   631   C  CB    . LEU A 1 262  ? 111.798 159.837 143.523 1.00 134.01 ? 1479 LEU A CB    1 
ATOM   632   C  CG    . LEU A 1 262  ? 113.163 159.962 144.202 1.00 133.93 ? 1479 LEU A CG    1 
ATOM   633   C  CD1   . LEU A 1 262  ? 114.262 159.793 143.187 1.00 129.76 ? 1479 LEU A CD1   1 
ATOM   634   C  CD2   . LEU A 1 262  ? 113.296 161.336 144.803 1.00 135.28 ? 1479 LEU A CD2   1 
ATOM   635   N  N     . THR A 1 263  ? 109.639 161.478 145.036 1.00 137.82 ? 1480 THR A N     1 
ATOM   636   C  CA    . THR A 1 263  ? 109.265 162.451 146.059 1.00 137.94 ? 1480 THR A CA    1 
ATOM   637   C  C     . THR A 1 263  ? 108.105 161.948 146.911 1.00 138.70 ? 1480 THR A C     1 
ATOM   638   O  O     . THR A 1 263  ? 108.090 162.154 148.131 1.00 139.18 ? 1480 THR A O     1 
ATOM   639   C  CB    . THR A 1 263  ? 108.910 163.791 145.414 1.00 138.37 ? 1480 THR A CB    1 
ATOM   640   O  OG1   . THR A 1 263  ? 107.957 163.584 144.365 1.00 139.72 ? 1480 THR A OG1   1 
ATOM   641   C  CG2   . THR A 1 263  ? 110.156 164.453 144.841 1.00 138.72 ? 1480 THR A CG2   1 
ATOM   642   N  N     . SER A 1 264  ? 107.123 161.290 146.287 1.00 139.30 ? 1481 SER A N     1 
ATOM   643   C  CA    . SER A 1 264  ? 105.988 160.758 147.038 1.00 138.45 ? 1481 SER A CA    1 
ATOM   644   C  C     . SER A 1 264  ? 106.431 159.671 148.012 1.00 139.25 ? 1481 SER A C     1 
ATOM   645   O  O     . SER A 1 264  ? 105.995 159.641 149.171 1.00 139.83 ? 1481 SER A O     1 
ATOM   646   C  CB    . SER A 1 264  ? 104.926 160.223 146.076 1.00 138.51 ? 1481 SER A CB    1 
ATOM   647   O  OG    . SER A 1 264  ? 105.353 159.019 145.464 1.00 140.30 ? 1481 SER A OG    1 
ATOM   648   N  N     . GLU A 1 265  ? 107.311 158.772 147.559 1.00 139.73 ? 1482 GLU A N     1 
ATOM   649   C  CA    . GLU A 1 265  ? 107.835 157.734 148.440 1.00 139.81 ? 1482 GLU A CA    1 
ATOM   650   C  C     . GLU A 1 265  ? 108.669 158.334 149.564 1.00 140.15 ? 1482 GLU A C     1 
ATOM   651   O  O     . GLU A 1 265  ? 108.604 157.871 150.709 1.00 140.81 ? 1482 GLU A O     1 
ATOM   652   C  CB    . GLU A 1 265  ? 108.660 156.731 147.636 1.00 137.26 ? 1482 GLU A CB    1 
ATOM   653   N  N     . TYR A 1 266  ? 109.456 159.367 149.255 1.00 139.91 ? 1483 TYR A N     1 
ATOM   654   C  CA    . TYR A 1 266  ? 110.242 160.053 150.275 1.00 140.62 ? 1483 TYR A CA    1 
ATOM   655   C  C     . TYR A 1 266  ? 109.342 160.663 151.340 1.00 140.35 ? 1483 TYR A C     1 
ATOM   656   O  O     . TYR A 1 266  ? 109.595 160.520 152.542 1.00 140.40 ? 1483 TYR A O     1 
ATOM   657   C  CB    . TYR A 1 266  ? 111.094 161.130 149.609 1.00 140.96 ? 1483 TYR A CB    1 
ATOM   658   C  CG    . TYR A 1 266  ? 112.184 161.722 150.466 1.00 140.63 ? 1483 TYR A CG    1 
ATOM   659   C  CD1   . TYR A 1 266  ? 113.299 160.975 150.826 1.00 140.69 ? 1483 TYR A CD1   1 
ATOM   660   C  CD2   . TYR A 1 266  ? 112.120 163.047 150.878 1.00 139.59 ? 1483 TYR A CD2   1 
ATOM   661   C  CE1   . TYR A 1 266  ? 114.308 161.527 151.589 1.00 140.54 ? 1483 TYR A CE1   1 
ATOM   662   C  CE2   . TYR A 1 266  ? 113.119 163.605 151.639 1.00 141.14 ? 1483 TYR A CE2   1 
ATOM   663   C  CZ    . TYR A 1 266  ? 114.209 162.843 151.994 1.00 141.91 ? 1483 TYR A CZ    1 
ATOM   664   O  OH    . TYR A 1 266  ? 115.206 163.413 152.747 1.00 141.17 ? 1483 TYR A OH    1 
ATOM   665   N  N     . LYS A 1 267  ? 108.264 161.321 150.911 1.00 140.78 ? 1484 LYS A N     1 
ATOM   666   C  CA    . LYS A 1 267  ? 107.331 161.925 151.855 1.00 141.28 ? 1484 LYS A CA    1 
ATOM   667   C  C     . LYS A 1 267  ? 106.636 160.867 152.704 1.00 142.73 ? 1484 LYS A C     1 
ATOM   668   O  O     . LYS A 1 267  ? 106.466 161.052 153.915 1.00 143.31 ? 1484 LYS A O     1 
ATOM   669   C  CB    . LYS A 1 267  ? 106.305 162.770 151.103 1.00 140.50 ? 1484 LYS A CB    1 
ATOM   670   N  N     . MET A 1 268  ? 106.235 159.750 152.091 1.00 143.87 ? 1485 MET A N     1 
ATOM   671   C  CA    . MET A 1 268  ? 105.497 158.732 152.834 1.00 145.64 ? 1485 MET A CA    1 
ATOM   672   C  C     . MET A 1 268  ? 106.400 158.009 153.836 1.00 146.39 ? 1485 MET A C     1 
ATOM   673   O  O     . MET A 1 268  ? 105.979 157.733 154.971 1.00 147.23 ? 1485 MET A O     1 
ATOM   674   C  CB    . MET A 1 268  ? 104.807 157.774 151.848 1.00 146.20 ? 1485 MET A CB    1 
ATOM   675   C  CG    . MET A 1 268  ? 105.666 156.690 151.203 1.00 145.15 ? 1485 MET A CG    1 
ATOM   676   S  SD    . MET A 1 268  ? 104.757 155.549 150.130 1.00 146.57 ? 1485 MET A SD    1 
ATOM   677   C  CE    . MET A 1 268  ? 104.043 154.390 151.289 1.00 142.72 ? 1485 MET A CE    1 
ATOM   678   N  N     . ILE A 1 269  ? 107.661 157.752 153.470 1.00 145.96 ? 1486 ILE A N     1 
ATOM   679   C  CA    . ILE A 1 269  ? 108.568 157.136 154.435 1.00 146.30 ? 1486 ILE A CA    1 
ATOM   680   C  C     . ILE A 1 269  ? 108.970 158.140 155.509 1.00 145.38 ? 1486 ILE A C     1 
ATOM   681   O  O     . ILE A 1 269  ? 109.215 157.754 156.656 1.00 145.46 ? 1486 ILE A O     1 
ATOM   682   C  CB    . ILE A 1 269  ? 109.796 156.504 153.745 1.00 145.70 ? 1486 ILE A CB    1 
ATOM   683   C  CG1   . ILE A 1 269  ? 110.693 157.558 153.092 1.00 143.97 ? 1486 ILE A CG1   1 
ATOM   684   C  CG2   . ILE A 1 269  ? 109.353 155.459 152.733 1.00 145.39 ? 1486 ILE A CG2   1 
ATOM   685   C  CD1   . ILE A 1 269  ? 111.997 157.000 152.552 1.00 139.22 ? 1486 ILE A CD1   1 
ATOM   686   N  N     . THR A 1 270  ? 109.014 159.437 155.179 1.00 144.90 ? 1487 THR A N     1 
ATOM   687   C  CA    . THR A 1 270  ? 109.256 160.449 156.203 1.00 145.63 ? 1487 THR A CA    1 
ATOM   688   C  C     . THR A 1 270  ? 108.122 160.477 157.218 1.00 146.24 ? 1487 THR A C     1 
ATOM   689   O  O     . THR A 1 270  ? 108.361 160.527 158.433 1.00 145.75 ? 1487 THR A O     1 
ATOM   690   C  CB    . THR A 1 270  ? 109.409 161.825 155.555 1.00 145.44 ? 1487 THR A CB    1 
ATOM   691   O  OG1   . THR A 1 270  ? 110.401 161.768 154.525 1.00 145.46 ? 1487 THR A OG1   1 
ATOM   692   C  CG2   . THR A 1 270  ? 109.831 162.853 156.592 1.00 141.83 ? 1487 THR A CG2   1 
ATOM   693   N  N     . THR A 1 271  ? 106.880 160.432 156.731 1.00 147.14 ? 1488 THR A N     1 
ATOM   694   C  CA    . THR A 1 271  ? 105.723 160.452 157.619 1.00 148.90 ? 1488 THR A CA    1 
ATOM   695   C  C     . THR A 1 271  ? 105.681 159.215 158.506 1.00 149.96 ? 1488 THR A C     1 
ATOM   696   O  O     . THR A 1 271  ? 105.405 159.315 159.707 1.00 151.34 ? 1488 THR A O     1 
ATOM   697   C  CB    . THR A 1 271  ? 104.435 160.568 156.805 1.00 149.54 ? 1488 THR A CB    1 
ATOM   698   O  OG1   . THR A 1 271  ? 104.570 161.621 155.843 1.00 146.68 ? 1488 THR A OG1   1 
ATOM   699   C  CG2   . THR A 1 271  ? 103.254 160.868 157.715 1.00 150.43 ? 1488 THR A CG2   1 
ATOM   700   N  N     . ARG A 1 272  ? 105.965 158.037 157.942 1.00 148.89 ? 1489 ARG A N     1 
ATOM   701   C  CA    . ARG A 1 272  ? 105.938 156.837 158.771 1.00 149.25 ? 1489 ARG A CA    1 
ATOM   702   C  C     . ARG A 1 272  ? 107.184 156.677 159.635 1.00 148.43 ? 1489 ARG A C     1 
ATOM   703   O  O     . ARG A 1 272  ? 107.165 155.875 160.574 1.00 147.95 ? 1489 ARG A O     1 
ATOM   704   C  CB    . ARG A 1 272  ? 105.734 155.591 157.912 1.00 148.69 ? 1489 ARG A CB    1 
ATOM   705   C  CG    . ARG A 1 272  ? 106.911 155.190 157.054 1.00 148.84 ? 1489 ARG A CG    1 
ATOM   706   C  CD    . ARG A 1 272  ? 106.382 154.397 155.881 1.00 150.44 ? 1489 ARG A CD    1 
ATOM   707   N  NE    . ARG A 1 272  ? 105.116 154.968 155.440 1.00 150.32 ? 1489 ARG A NE    1 
ATOM   708   C  CZ    . ARG A 1 272  ? 104.181 154.310 154.771 1.00 150.53 ? 1489 ARG A CZ    1 
ATOM   709   N  NH1   . ARG A 1 272  ? 104.340 153.043 154.426 1.00 150.91 ? 1489 ARG A NH1   1 
ATOM   710   N  NH2   . ARG A 1 272  ? 103.053 154.936 154.448 1.00 149.88 ? 1489 ARG A NH2   1 
ATOM   711   N  N     . ALA A 1 273  ? 108.261 157.408 159.345 1.00 147.82 ? 1490 ALA A N     1 
ATOM   712   C  CA    . ALA A 1 273  ? 109.373 157.472 160.285 1.00 146.04 ? 1490 ALA A CA    1 
ATOM   713   C  C     . ALA A 1 273  ? 109.049 158.395 161.451 1.00 146.03 ? 1490 ALA A C     1 
ATOM   714   O  O     . ALA A 1 273  ? 109.445 158.125 162.591 1.00 143.96 ? 1490 ALA A O     1 
ATOM   715   C  CB    . ALA A 1 273  ? 110.645 157.930 159.572 1.00 146.33 ? 1490 ALA A CB    1 
ATOM   716   N  N     . PHE A 1 274  ? 108.339 159.494 161.181 1.00 148.76 ? 1491 PHE A N     1 
ATOM   717   C  CA    . PHE A 1 274  ? 107.906 160.374 162.263 1.00 150.93 ? 1491 PHE A CA    1 
ATOM   718   C  C     . PHE A 1 274  ? 106.845 159.708 163.129 1.00 152.28 ? 1491 PHE A C     1 
ATOM   719   O  O     . PHE A 1 274  ? 106.837 159.879 164.354 1.00 151.58 ? 1491 PHE A O     1 
ATOM   720   C  CB    . PHE A 1 274  ? 107.389 161.697 161.696 1.00 150.67 ? 1491 PHE A CB    1 
ATOM   721   C  CG    . PHE A 1 274  ? 107.288 162.795 162.719 1.00 150.33 ? 1491 PHE A CG    1 
ATOM   722   C  CD1   . PHE A 1 274  ? 108.406 163.209 163.425 1.00 147.28 ? 1491 PHE A CD1   1 
ATOM   723   C  CD2   . PHE A 1 274  ? 106.076 163.416 162.972 1.00 150.29 ? 1491 PHE A CD2   1 
ATOM   724   C  CE1   . PHE A 1 274  ? 108.318 164.217 164.366 1.00 144.76 ? 1491 PHE A CE1   1 
ATOM   725   C  CE2   . PHE A 1 274  ? 105.981 164.426 163.912 1.00 149.46 ? 1491 PHE A CE2   1 
ATOM   726   C  CZ    . PHE A 1 274  ? 107.105 164.827 164.610 1.00 146.10 ? 1491 PHE A CZ    1 
ATOM   727   N  N     . GLN A 1 275  ? 105.947 158.946 162.516 1.00 152.71 ? 1492 GLN A N     1 
ATOM   728   C  CA    . GLN A 1 275  ? 104.881 158.274 163.246 1.00 151.98 ? 1492 GLN A CA    1 
ATOM   729   C  C     . GLN A 1 275  ? 105.316 156.882 163.692 1.00 147.98 ? 1492 GLN A C     1 
ATOM   730   O  O     . GLN A 1 275  ? 106.363 156.719 164.319 1.00 145.29 ? 1492 GLN A O     1 
ATOM   731   C  CB    . GLN A 1 275  ? 103.620 158.181 162.383 1.00 152.41 ? 1492 GLN A CB    1 
ATOM   732   C  CG    . GLN A 1 275  ? 102.856 159.490 162.246 1.00 153.43 ? 1492 GLN A CG    1 
ATOM   733   C  CD    . GLN A 1 275  ? 102.913 160.342 163.500 1.00 153.27 ? 1492 GLN A CD    1 
ATOM   734   O  OE1   . GLN A 1 275  ? 103.560 161.390 163.523 1.00 152.14 ? 1492 GLN A OE1   1 
ATOM   735   N  NE2   . GLN A 1 275  ? 102.225 159.903 164.548 1.00 152.49 ? 1492 GLN A NE2   1 
ATOM   736   N  N     . PHE A 1 288  ? 105.406 146.961 158.414 1.00 151.01 ? 1505 PHE A N     1 
ATOM   737   C  CA    . PHE A 1 288  ? 106.356 148.020 158.097 1.00 151.60 ? 1505 PHE A CA    1 
ATOM   738   C  C     . PHE A 1 288  ? 107.677 147.439 157.601 1.00 150.74 ? 1505 PHE A C     1 
ATOM   739   O  O     . PHE A 1 288  ? 108.418 148.098 156.873 1.00 149.74 ? 1505 PHE A O     1 
ATOM   740   C  CB    . PHE A 1 288  ? 106.595 148.910 159.321 1.00 153.01 ? 1505 PHE A CB    1 
ATOM   741   C  CG    . PHE A 1 288  ? 107.571 150.027 159.078 1.00 154.73 ? 1505 PHE A CG    1 
ATOM   742   C  CD1   . PHE A 1 288  ? 107.388 150.909 158.024 1.00 154.09 ? 1505 PHE A CD1   1 
ATOM   743   C  CD2   . PHE A 1 288  ? 108.676 150.191 159.898 1.00 152.55 ? 1505 PHE A CD2   1 
ATOM   744   C  CE1   . PHE A 1 288  ? 108.287 151.935 157.795 1.00 153.10 ? 1505 PHE A CE1   1 
ATOM   745   C  CE2   . PHE A 1 288  ? 109.578 151.216 159.675 1.00 151.45 ? 1505 PHE A CE2   1 
ATOM   746   C  CZ    . PHE A 1 288  ? 109.382 152.089 158.622 1.00 152.68 ? 1505 PHE A CZ    1 
ATOM   747   N  N     . ASP A 1 289  ? 107.962 146.196 157.997 1.00 151.43 ? 1506 ASP A N     1 
ATOM   748   C  CA    . ASP A 1 289  ? 109.211 145.554 157.600 1.00 151.34 ? 1506 ASP A CA    1 
ATOM   749   C  C     . ASP A 1 289  ? 109.250 145.304 156.096 1.00 151.15 ? 1506 ASP A C     1 
ATOM   750   O  O     . ASP A 1 289  ? 110.226 145.655 155.422 1.00 149.33 ? 1506 ASP A O     1 
ATOM   751   C  CB    . ASP A 1 289  ? 109.390 144.246 158.369 1.00 149.52 ? 1506 ASP A CB    1 
ATOM   752   C  CG    . ASP A 1 289  ? 109.318 144.441 159.870 1.00 149.48 ? 1506 ASP A CG    1 
ATOM   753   O  OD1   . ASP A 1 289  ? 109.622 145.558 160.340 1.00 148.30 ? 1506 ASP A OD1   1 
ATOM   754   O  OD2   . ASP A 1 289  ? 108.955 143.479 160.579 1.00 151.36 ? 1506 ASP A OD2   1 
ATOM   755   N  N     . THR A 1 290  ? 108.188 144.700 155.553 1.00 152.57 ? 1507 THR A N     1 
ATOM   756   C  CA    . THR A 1 290  ? 108.106 144.496 154.111 1.00 150.73 ? 1507 THR A CA    1 
ATOM   757   C  C     . THR A 1 290  ? 108.014 145.820 153.364 1.00 151.96 ? 1507 THR A C     1 
ATOM   758   O  O     . THR A 1 290  ? 108.558 145.945 152.261 1.00 150.08 ? 1507 THR A O     1 
ATOM   759   C  CB    . THR A 1 290  ? 106.906 143.613 153.768 1.00 147.32 ? 1507 THR A CB    1 
ATOM   760   N  N     . THR A 1 291  ? 107.341 146.814 153.951 1.00 154.58 ? 1508 THR A N     1 
ATOM   761   C  CA    . THR A 1 291  ? 107.254 148.129 153.325 1.00 152.89 ? 1508 THR A CA    1 
ATOM   762   C  C     . THR A 1 291  ? 108.629 148.775 153.199 1.00 150.06 ? 1508 THR A C     1 
ATOM   763   O  O     . THR A 1 291  ? 108.969 149.331 152.151 1.00 147.44 ? 1508 THR A O     1 
ATOM   764   C  CB    . THR A 1 291  ? 106.311 149.028 154.125 1.00 151.85 ? 1508 THR A CB    1 
ATOM   765   O  OG1   . THR A 1 291  ? 105.012 148.426 154.186 1.00 154.52 ? 1508 THR A OG1   1 
ATOM   766   C  CG2   . THR A 1 291  ? 106.194 150.397 153.473 1.00 148.54 ? 1508 THR A CG2   1 
ATOM   767   N  N     . LEU A 1 292  ? 109.450 148.688 154.245 1.00 150.21 ? 1509 LEU A N     1 
ATOM   768   C  CA    . LEU A 1 292  ? 110.779 149.283 154.188 1.00 147.41 ? 1509 LEU A CA    1 
ATOM   769   C  C     . LEU A 1 292  ? 111.753 148.449 153.362 1.00 145.92 ? 1509 LEU A C     1 
ATOM   770   O  O     . LEU A 1 292  ? 112.696 149.007 152.786 1.00 142.10 ? 1509 LEU A O     1 
ATOM   771   C  CB    . LEU A 1 292  ? 111.304 149.506 155.608 1.00 145.52 ? 1509 LEU A CB    1 
ATOM   772   C  CG    . LEU A 1 292  ? 112.518 150.416 155.784 1.00 141.57 ? 1509 LEU A CG    1 
ATOM   773   C  CD1   . LEU A 1 292  ? 112.297 151.722 155.055 1.00 140.33 ? 1509 LEU A CD1   1 
ATOM   774   C  CD2   . LEU A 1 292  ? 112.711 150.698 157.256 1.00 140.73 ? 1509 LEU A CD2   1 
ATOM   775   N  N     . LYS A 1 293  ? 111.538 147.132 153.272 1.00 147.28 ? 1510 LYS A N     1 
ATOM   776   C  CA    . LYS A 1 293  ? 112.280 146.330 152.302 1.00 144.42 ? 1510 LYS A CA    1 
ATOM   777   C  C     . LYS A 1 293  ? 111.953 146.758 150.875 1.00 141.83 ? 1510 LYS A C     1 
ATOM   778   O  O     . LYS A 1 293  ? 112.848 146.879 150.029 1.00 139.97 ? 1510 LYS A O     1 
ATOM   779   C  CB    . LYS A 1 293  ? 111.975 144.846 152.504 1.00 145.21 ? 1510 LYS A CB    1 
ATOM   780   N  N     . LEU A 1 294  ? 110.672 147.006 150.594 1.00 142.42 ? 1511 LEU A N     1 
ATOM   781   C  CA    . LEU A 1 294  ? 110.298 147.564 149.300 1.00 140.82 ? 1511 LEU A CA    1 
ATOM   782   C  C     . LEU A 1 294  ? 110.869 148.963 149.115 1.00 138.72 ? 1511 LEU A C     1 
ATOM   783   O  O     . LEU A 1 294  ? 111.184 149.358 147.990 1.00 135.72 ? 1511 LEU A O     1 
ATOM   784   C  CB    . LEU A 1 294  ? 108.776 147.584 149.155 1.00 142.70 ? 1511 LEU A CB    1 
ATOM   785   N  N     . THR A 1 295  ? 111.024 149.715 150.206 1.00 139.83 ? 1512 THR A N     1 
ATOM   786   C  CA    . THR A 1 295  ? 111.601 151.054 150.124 1.00 139.40 ? 1512 THR A CA    1 
ATOM   787   C  C     . THR A 1 295  ? 113.071 151.007 149.719 1.00 133.31 ? 1512 THR A C     1 
ATOM   788   O  O     . THR A 1 295  ? 113.506 151.771 148.852 1.00 128.67 ? 1512 THR A O     1 
ATOM   789   C  CB    . THR A 1 295  ? 111.441 151.781 151.459 1.00 141.57 ? 1512 THR A CB    1 
ATOM   790   O  OG1   . THR A 1 295  ? 110.061 151.776 151.848 1.00 144.92 ? 1512 THR A OG1   1 
ATOM   791   C  CG2   . THR A 1 295  ? 111.936 153.216 151.350 1.00 136.46 ? 1512 THR A CG2   1 
ATOM   792   N  N     . ILE A 1 296  ? 113.858 150.128 150.346 1.00 133.29 ? 1513 ILE A N     1 
ATOM   793   C  CA    . ILE A 1 296  ? 115.267 150.028 149.960 1.00 129.10 ? 1513 ILE A CA    1 
ATOM   794   C  C     . ILE A 1 296  ? 115.398 149.419 148.563 1.00 126.38 ? 1513 ILE A C     1 
ATOM   795   O  O     . ILE A 1 296  ? 116.289 149.805 147.793 1.00 122.89 ? 1513 ILE A O     1 
ATOM   796   C  CB    . ILE A 1 296  ? 116.090 149.262 151.023 1.00 131.32 ? 1513 ILE A CB    1 
ATOM   797   C  CG1   . ILE A 1 296  ? 117.551 149.083 150.588 1.00 130.34 ? 1513 ILE A CG1   1 
ATOM   798   C  CG2   . ILE A 1 296  ? 115.486 147.918 151.345 1.00 131.01 ? 1513 ILE A CG2   1 
ATOM   799   C  CD1   . ILE A 1 296  ? 118.290 150.373 150.294 1.00 130.30 ? 1513 ILE A CD1   1 
ATOM   800   N  N     . ASP A 1 297  ? 114.503 148.494 148.193 1.00 129.83 ? 1514 ASP A N     1 
ATOM   801   C  CA    . ASP A 1 297  ? 114.499 147.984 146.823 1.00 127.57 ? 1514 ASP A CA    1 
ATOM   802   C  C     . ASP A 1 297  ? 114.210 149.095 145.817 1.00 122.94 ? 1514 ASP A C     1 
ATOM   803   O  O     . ASP A 1 297  ? 114.871 149.190 144.775 1.00 120.46 ? 1514 ASP A O     1 
ATOM   804   C  CB    . ASP A 1 297  ? 113.476 146.857 146.686 1.00 127.07 ? 1514 ASP A CB    1 
ATOM   805   N  N     . SER A 1 298  ? 113.240 149.959 146.124 1.00 124.10 ? 1515 SER A N     1 
ATOM   806   C  CA    . SER A 1 298  ? 112.931 151.085 145.253 1.00 122.18 ? 1515 SER A CA    1 
ATOM   807   C  C     . SER A 1 298  ? 114.066 152.098 145.221 1.00 118.42 ? 1515 SER A C     1 
ATOM   808   O  O     . SER A 1 298  ? 114.298 152.723 144.185 1.00 115.51 ? 1515 SER A O     1 
ATOM   809   C  CB    . SER A 1 298  ? 111.635 151.759 145.702 1.00 125.85 ? 1515 SER A CB    1 
ATOM   810   N  N     . LEU A 1 299  ? 114.768 152.285 146.341 1.00 119.04 ? 1516 LEU A N     1 
ATOM   811   C  CA    . LEU A 1 299  ? 115.920 153.181 146.360 1.00 116.19 ? 1516 LEU A CA    1 
ATOM   812   C  C     . LEU A 1 299  ? 117.038 152.658 145.468 1.00 112.87 ? 1516 LEU A C     1 
ATOM   813   O  O     . LEU A 1 299  ? 117.661 153.426 144.722 1.00 109.69 ? 1516 LEU A O     1 
ATOM   814   C  CB    . LEU A 1 299  ? 116.413 153.364 147.794 1.00 118.62 ? 1516 LEU A CB    1 
ATOM   815   C  CG    . LEU A 1 299  ? 115.662 154.418 148.606 1.00 118.95 ? 1516 LEU A CG    1 
ATOM   816   C  CD1   . LEU A 1 299  ? 115.754 154.110 150.090 1.00 125.07 ? 1516 LEU A CD1   1 
ATOM   817   C  CD2   . LEU A 1 299  ? 116.205 155.804 148.305 1.00 111.72 ? 1516 LEU A CD2   1 
ATOM   818   N  N     . LYS A 1 300  ? 117.295 151.350 145.520 1.00 114.96 ? 1517 LYS A N     1 
ATOM   819   C  CA    . LYS A 1 300  ? 118.262 150.751 144.605 1.00 112.57 ? 1517 LYS A CA    1 
ATOM   820   C  C     . LYS A 1 300  ? 117.808 150.897 143.157 1.00 110.14 ? 1517 LYS A C     1 
ATOM   821   O  O     . LYS A 1 300  ? 118.619 151.194 142.271 1.00 104.79 ? 1517 LYS A O     1 
ATOM   822   C  CB    . LYS A 1 300  ? 118.476 149.280 144.959 1.00 113.71 ? 1517 LYS A CB    1 
ATOM   823   N  N     . MET A 1 301  ? 116.509 150.708 142.903 1.00 112.87 ? 1518 MET A N     1 
ATOM   824   C  CA    . MET A 1 301  ? 115.985 150.824 141.544 1.00 109.46 ? 1518 MET A CA    1 
ATOM   825   C  C     . MET A 1 301  ? 116.113 152.246 141.007 1.00 104.63 ? 1518 MET A C     1 
ATOM   826   O  O     . MET A 1 301  ? 116.490 152.444 139.847 1.00 103.29 ? 1518 MET A O     1 
ATOM   827   C  CB    . MET A 1 301  ? 114.527 150.367 141.506 1.00 109.68 ? 1518 MET A CB    1 
ATOM   828   N  N     . ILE A 1 302  ? 115.802 153.251 141.829 1.00 105.78 ? 1519 ILE A N     1 
ATOM   829   C  CA    . ILE A 1 302  ? 115.884 154.631 141.360 1.00 103.97 ? 1519 ILE A CA    1 
ATOM   830   C  C     . ILE A 1 302  ? 117.336 155.073 141.219 1.00 100.25 ? 1519 ILE A C     1 
ATOM   831   O  O     . ILE A 1 302  ? 117.657 155.867 140.329 1.00 97.72  ? 1519 ILE A O     1 
ATOM   832   C  CB    . ILE A 1 302  ? 115.078 155.582 142.269 1.00 107.96 ? 1519 ILE A CB    1 
ATOM   833   C  CG1   . ILE A 1 302  ? 115.631 155.583 143.692 1.00 109.15 ? 1519 ILE A CG1   1 
ATOM   834   C  CG2   . ILE A 1 302  ? 113.597 155.225 142.244 1.00 110.97 ? 1519 ILE A CG2   1 
ATOM   835   C  CD1   . ILE A 1 302  ? 115.054 156.624 144.596 1.00 112.67 ? 1519 ILE A CD1   1 
ATOM   836   N  N     . LYS A 1 303  ? 118.241 154.569 142.067 1.00 100.38 ? 1520 LYS A N     1 
ATOM   837   C  CA    . LYS A 1 303  ? 119.654 154.868 141.860 1.00 97.75  ? 1520 LYS A CA    1 
ATOM   838   C  C     . LYS A 1 303  ? 120.166 154.227 140.574 1.00 95.51  ? 1520 LYS A C     1 
ATOM   839   O  O     . LYS A 1 303  ? 120.941 154.844 139.836 1.00 91.98  ? 1520 LYS A O     1 
ATOM   840   C  CB    . LYS A 1 303  ? 120.482 154.416 143.064 1.00 102.51 ? 1520 LYS A CB    1 
ATOM   841   C  CG    . LYS A 1 303  ? 121.985 154.610 142.891 1.00 101.16 ? 1520 LYS A CG    1 
ATOM   842   C  CD    . LYS A 1 303  ? 122.326 156.041 142.487 1.00 94.24  ? 1520 LYS A CD    1 
ATOM   843   C  CE    . LYS A 1 303  ? 122.148 157.013 143.630 1.00 100.75 ? 1520 LYS A CE    1 
ATOM   844   N  NZ    . LYS A 1 303  ? 123.215 156.823 144.638 1.00 106.94 ? 1520 LYS A NZ    1 
ATOM   845   N  N     . SER A 1 304  ? 119.729 153.000 140.280 1.00 96.97  ? 1521 SER A N     1 
ATOM   846   C  CA    . SER A 1 304  ? 120.094 152.371 139.015 1.00 93.95  ? 1521 SER A CA    1 
ATOM   847   C  C     . SER A 1 304  ? 119.532 153.147 137.830 1.00 90.33  ? 1521 SER A C     1 
ATOM   848   O  O     . SER A 1 304  ? 120.211 153.320 136.813 1.00 89.08  ? 1521 SER A O     1 
ATOM   849   C  CB    . SER A 1 304  ? 119.607 150.923 138.988 1.00 96.42  ? 1521 SER A CB    1 
ATOM   850   O  OG    . SER A 1 304  ? 119.893 150.314 137.742 1.00 96.08  ? 1521 SER A OG    1 
ATOM   851   N  N     . SER A 1 305  ? 118.290 153.624 137.948 1.00 90.42  ? 1522 SER A N     1 
ATOM   852   C  CA    . SER A 1 305  ? 117.684 154.410 136.878 1.00 89.29  ? 1522 SER A CA    1 
ATOM   853   C  C     . SER A 1 305  ? 118.430 155.720 136.662 1.00 88.23  ? 1522 SER A C     1 
ATOM   854   O  O     . SER A 1 305  ? 118.651 156.133 135.519 1.00 86.85  ? 1522 SER A O     1 
ATOM   855   C  CB    . SER A 1 305  ? 116.213 154.676 137.195 1.00 96.18  ? 1522 SER A CB    1 
ATOM   856   O  OG    . SER A 1 305  ? 116.079 155.773 138.081 1.00 100.93 ? 1522 SER A OG    1 
ATOM   857   N  N     . LEU A 1 306  ? 118.836 156.383 137.748 1.00 88.62  ? 1523 LEU A N     1 
ATOM   858   C  CA    . LEU A 1 306  ? 119.624 157.605 137.623 1.00 84.48  ? 1523 LEU A CA    1 
ATOM   859   C  C     . LEU A 1 306  ? 120.992 157.318 137.014 1.00 79.30  ? 1523 LEU A C     1 
ATOM   860   O  O     . LEU A 1 306  ? 121.509 158.122 136.227 1.00 75.36  ? 1523 LEU A O     1 
ATOM   861   C  CB    . LEU A 1 306  ? 119.768 158.273 138.991 1.00 84.18  ? 1523 LEU A CB    1 
ATOM   862   C  CG    . LEU A 1 306  ? 120.270 159.717 139.049 1.00 74.64  ? 1523 LEU A CG    1 
ATOM   863   C  CD1   . LEU A 1 306  ? 119.507 160.490 140.108 1.00 79.37  ? 1523 LEU A CD1   1 
ATOM   864   C  CD2   . LEU A 1 306  ? 121.761 159.764 139.338 1.00 73.84  ? 1523 LEU A CD2   1 
ATOM   865   N  N     . SER A 1 307  ? 121.591 156.179 137.369 1.00 82.41  ? 1524 SER A N     1 
ATOM   866   C  CA    . SER A 1 307  ? 122.881 155.800 136.801 1.00 81.54  ? 1524 SER A CA    1 
ATOM   867   C  C     . SER A 1 307  ? 122.776 155.579 135.298 1.00 76.51  ? 1524 SER A C     1 
ATOM   868   O  O     . SER A 1 307  ? 123.607 156.073 134.530 1.00 73.25  ? 1524 SER A O     1 
ATOM   869   C  CB    . SER A 1 307  ? 123.411 154.545 137.494 1.00 88.26  ? 1524 SER A CB    1 
ATOM   870   O  OG    . SER A 1 307  ? 122.720 153.390 137.051 1.00 89.17  ? 1524 SER A OG    1 
ATOM   871   N  N     . THR A 1 308  ? 121.746 154.852 134.854 1.00 75.99  ? 1525 THR A N     1 
ATOM   872   C  CA    . THR A 1 308  ? 121.571 154.652 133.416 1.00 73.03  ? 1525 THR A CA    1 
ATOM   873   C  C     . THR A 1 308  ? 121.134 155.929 132.708 1.00 73.30  ? 1525 THR A C     1 
ATOM   874   O  O     . THR A 1 308  ? 121.425 156.098 131.521 1.00 71.84  ? 1525 THR A O     1 
ATOM   875   C  CB    . THR A 1 308  ? 120.577 153.525 133.128 1.00 77.71  ? 1525 THR A CB    1 
ATOM   876   O  OG1   . THR A 1 308  ? 119.240 153.973 133.385 1.00 81.28  ? 1525 THR A OG1   1 
ATOM   877   C  CG2   . THR A 1 308  ? 120.901 152.276 133.934 1.00 82.29  ? 1525 THR A CG2   1 
ATOM   878   N  N     . PHE A 1 309  ? 120.458 156.843 133.407 1.00 74.75  ? 1526 PHE A N     1 
ATOM   879   C  CA    . PHE A 1 309  ? 120.121 158.127 132.802 1.00 73.17  ? 1526 PHE A CA    1 
ATOM   880   C  C     . PHE A 1 309  ? 121.373 158.962 132.559 1.00 71.63  ? 1526 PHE A C     1 
ATOM   881   O  O     . PHE A 1 309  ? 121.553 159.532 131.474 1.00 71.75  ? 1526 PHE A O     1 
ATOM   882   C  CB    . PHE A 1 309  ? 119.131 158.879 133.690 1.00 73.82  ? 1526 PHE A CB    1 
ATOM   883   C  CG    . PHE A 1 309  ? 119.051 160.348 133.397 1.00 73.21  ? 1526 PHE A CG    1 
ATOM   884   C  CD1   . PHE A 1 309  ? 118.520 160.802 132.201 1.00 75.25  ? 1526 PHE A CD1   1 
ATOM   885   C  CD2   . PHE A 1 309  ? 119.502 161.274 134.320 1.00 70.52  ? 1526 PHE A CD2   1 
ATOM   886   C  CE1   . PHE A 1 309  ? 118.446 162.154 131.931 1.00 76.71  ? 1526 PHE A CE1   1 
ATOM   887   C  CE2   . PHE A 1 309  ? 119.429 162.624 134.057 1.00 75.63  ? 1526 PHE A CE2   1 
ATOM   888   C  CZ    . PHE A 1 309  ? 118.901 163.066 132.861 1.00 80.44  ? 1526 PHE A CZ    1 
ATOM   889   N  N     . LEU A 1 310  ? 122.255 159.040 133.560 1.00 70.12  ? 1527 LEU A N     1 
ATOM   890   C  CA    . LEU A 1 310  ? 123.542 159.698 133.361 1.00 63.74  ? 1527 LEU A CA    1 
ATOM   891   C  C     . LEU A 1 310  ? 124.372 158.980 132.308 1.00 58.59  ? 1527 LEU A C     1 
ATOM   892   O  O     . LEU A 1 310  ? 125.100 159.625 131.545 1.00 57.42  ? 1527 LEU A O     1 
ATOM   893   C  CB    . LEU A 1 310  ? 124.311 159.776 134.679 1.00 61.87  ? 1527 LEU A CB    1 
ATOM   894   C  CG    . LEU A 1 310  ? 123.841 160.811 135.702 1.00 62.19  ? 1527 LEU A CG    1 
ATOM   895   C  CD1   . LEU A 1 310  ? 124.895 161.014 136.779 1.00 56.33  ? 1527 LEU A CD1   1 
ATOM   896   C  CD2   . LEU A 1 310  ? 123.505 162.127 135.025 1.00 62.86  ? 1527 LEU A CD2   1 
ATOM   897   N  N     . GLU A 1 311  ? 124.263 157.651 132.239 1.00 56.16  ? 1528 GLU A N     1 
ATOM   898   C  CA    . GLU A 1 311  ? 124.974 156.897 131.215 1.00 54.91  ? 1528 GLU A CA    1 
ATOM   899   C  C     . GLU A 1 311  ? 124.482 157.253 129.820 1.00 54.63  ? 1528 GLU A C     1 
ATOM   900   O  O     . GLU A 1 311  ? 125.288 157.435 128.907 1.00 55.23  ? 1528 GLU A O     1 
ATOM   901   C  CB    . GLU A 1 311  ? 124.825 155.398 131.470 1.00 63.91  ? 1528 GLU A CB    1 
ATOM   902   C  CG    . GLU A 1 311  ? 125.930 154.810 132.324 1.00 66.08  ? 1528 GLU A CG    1 
ATOM   903   C  CD    . GLU A 1 311  ? 127.298 155.318 131.925 1.00 60.61  ? 1528 GLU A CD    1 
ATOM   904   O  OE1   . GLU A 1 311  ? 127.741 155.009 130.800 1.00 61.54  ? 1528 GLU A OE1   1 
ATOM   905   O  OE2   . GLU A 1 311  ? 127.930 156.026 132.736 1.00 56.33  ? 1528 GLU A OE2   1 
ATOM   906   N  N     . ARG A 1 312  ? 123.165 157.360 129.635 1.00 54.13  ? 1529 ARG A N     1 
ATOM   907   C  CA    . ARG A 1 312  ? 122.623 157.752 128.337 1.00 52.13  ? 1529 ARG A CA    1 
ATOM   908   C  C     . ARG A 1 312  ? 123.011 159.183 127.986 1.00 51.70  ? 1529 ARG A C     1 
ATOM   909   O  O     . ARG A 1 312  ? 123.314 159.485 126.822 1.00 49.63  ? 1529 ARG A O     1 
ATOM   910   C  CB    . ARG A 1 312  ? 121.103 157.589 128.330 1.00 52.37  ? 1529 ARG A CB    1 
ATOM   911   N  N     . GLN A 1 313  ? 123.010 160.074 128.983 1.00 53.40  ? 1530 GLN A N     1 
ATOM   912   C  CA    . GLN A 1 313  ? 123.463 161.445 128.760 1.00 49.65  ? 1530 GLN A CA    1 
ATOM   913   C  C     . GLN A 1 313  ? 124.920 161.474 128.324 1.00 46.70  ? 1530 GLN A C     1 
ATOM   914   O  O     . GLN A 1 313  ? 125.310 162.285 127.477 1.00 45.63  ? 1530 GLN A O     1 
ATOM   915   C  CB    . GLN A 1 313  ? 123.276 162.271 130.032 1.00 50.44  ? 1530 GLN A CB    1 
ATOM   916   C  CG    . GLN A 1 313  ? 121.850 162.713 130.297 1.00 58.55  ? 1530 GLN A CG    1 
ATOM   917   C  CD    . GLN A 1 313  ? 121.252 163.481 129.139 1.00 61.80  ? 1530 GLN A CD    1 
ATOM   918   O  OE1   . GLN A 1 313  ? 120.145 163.188 128.691 1.00 63.51  ? 1530 GLN A OE1   1 
ATOM   919   N  NE2   . GLN A 1 313  ? 121.981 164.477 128.651 1.00 59.39  ? 1530 GLN A NE2   1 
ATOM   920   N  N     . ARG A 1 314  ? 125.738 160.590 128.893 1.00 45.89  ? 1531 ARG A N     1 
ATOM   921   C  CA    . ARG A 1 314  ? 127.140 160.505 128.513 1.00 40.64  ? 1531 ARG A CA    1 
ATOM   922   C  C     . ARG A 1 314  ? 127.333 159.833 127.158 1.00 44.46  ? 1531 ARG A C     1 
ATOM   923   O  O     . ARG A 1 314  ? 128.297 160.143 126.455 1.00 43.11  ? 1531 ARG A O     1 
ATOM   924   C  CB    . ARG A 1 314  ? 127.915 159.763 129.599 1.00 38.95  ? 1531 ARG A CB    1 
ATOM   925   C  CG    . ARG A 1 314  ? 128.439 160.662 130.704 1.00 33.62  ? 1531 ARG A CG    1 
ATOM   926   C  CD    . ARG A 1 314  ? 128.498 159.929 132.033 1.00 35.15  ? 1531 ARG A CD    1 
ATOM   927   N  NE    . ARG A 1 314  ? 129.387 160.607 132.969 1.00 29.36  ? 1531 ARG A NE    1 
ATOM   928   C  CZ    . ARG A 1 314  ? 129.777 160.106 134.133 1.00 29.95  ? 1531 ARG A CZ    1 
ATOM   929   N  NH1   . ARG A 1 314  ? 129.402 158.901 134.527 1.00 27.47  ? 1531 ARG A NH1   1 
ATOM   930   N  NH2   . ARG A 1 314  ? 130.576 160.827 134.914 1.00 35.28  ? 1531 ARG A NH2   1 
ATOM   931   N  N     . ARG A 1 315  ? 126.448 158.910 126.778 1.00 44.16  ? 1532 ARG A N     1 
ATOM   932   C  CA    . ARG A 1 315  ? 126.535 158.313 125.447 1.00 41.80  ? 1532 ARG A CA    1 
ATOM   933   C  C     . ARG A 1 315  ? 126.167 159.323 124.370 1.00 44.04  ? 1532 ARG A C     1 
ATOM   934   O  O     . ARG A 1 315  ? 126.749 159.311 123.279 1.00 47.30  ? 1532 ARG A O     1 
ATOM   935   C  CB    . ARG A 1 315  ? 125.632 157.083 125.337 1.00 41.61  ? 1532 ARG A CB    1 
ATOM   936   C  CG    . ARG A 1 315  ? 125.964 155.948 126.284 1.00 47.33  ? 1532 ARG A CG    1 
ATOM   937   C  CD    . ARG A 1 315  ? 126.935 154.946 125.703 1.00 51.20  ? 1532 ARG A CD    1 
ATOM   938   N  NE    . ARG A 1 315  ? 127.725 154.326 126.759 1.00 55.28  ? 1532 ARG A NE    1 
ATOM   939   C  CZ    . ARG A 1 315  ? 128.420 153.207 126.620 1.00 51.87  ? 1532 ARG A CZ    1 
ATOM   940   N  NH1   . ARG A 1 315  ? 128.442 152.545 125.475 1.00 53.20  ? 1532 ARG A NH1   1 
ATOM   941   N  NH2   . ARG A 1 315  ? 129.106 152.737 127.657 1.00 46.17  ? 1532 ARG A NH2   1 
ATOM   942   N  N     . GLN A 1 316  ? 125.187 160.189 124.645 1.00 40.82  ? 1533 GLN A N     1 
ATOM   943   C  CA    . GLN A 1 316  ? 124.805 161.196 123.658 1.00 39.34  ? 1533 GLN A CA    1 
ATOM   944   C  C     . GLN A 1 316  ? 125.933 162.192 123.412 1.00 39.31  ? 1533 GLN A C     1 
ATOM   945   O  O     . GLN A 1 316  ? 126.231 162.525 122.259 1.00 38.06  ? 1533 GLN A O     1 
ATOM   946   C  CB    . GLN A 1 316  ? 123.535 161.919 124.101 1.00 43.89  ? 1533 GLN A CB    1 
ATOM   947   C  CG    . GLN A 1 316  ? 122.258 161.293 123.569 1.00 48.16  ? 1533 GLN A CG    1 
ATOM   948   C  CD    . GLN A 1 316  ? 121.050 161.614 124.421 1.00 57.11  ? 1533 GLN A CD    1 
ATOM   949   O  OE1   . GLN A 1 316  ? 121.178 162.134 125.529 1.00 60.05  ? 1533 GLN A OE1   1 
ATOM   950   N  NE2   . GLN A 1 316  ? 119.866 161.305 123.908 1.00 56.58  ? 1533 GLN A NE2   1 
ATOM   951   N  N     . PHE A 1 317  ? 126.570 162.677 124.474 1.00 37.26  ? 1534 PHE A N     1 
ATOM   952   C  CA    . PHE A 1 317  ? 127.749 163.534 124.361 1.00 32.95  ? 1534 PHE A CA    1 
ATOM   953   C  C     . PHE A 1 317  ? 128.880 162.901 125.158 1.00 34.03  ? 1534 PHE A C     1 
ATOM   954   O  O     . PHE A 1 317  ? 128.924 163.035 126.393 1.00 36.13  ? 1534 PHE A O     1 
ATOM   955   C  CB    . PHE A 1 317  ? 127.470 164.952 124.843 1.00 30.09  ? 1534 PHE A CB    1 
ATOM   956   C  CG    . PHE A 1 317  ? 128.513 165.948 124.427 1.00 28.07  ? 1534 PHE A CG    1 
ATOM   957   C  CD1   . PHE A 1 317  ? 129.002 165.958 123.132 1.00 30.69  ? 1534 PHE A CD1   1 
ATOM   958   C  CD2   . PHE A 1 317  ? 129.000 166.877 125.326 1.00 26.57  ? 1534 PHE A CD2   1 
ATOM   959   C  CE1   . PHE A 1 317  ? 129.963 166.875 122.746 1.00 28.18  ? 1534 PHE A CE1   1 
ATOM   960   C  CE2   . PHE A 1 317  ? 129.956 167.795 124.947 1.00 26.61  ? 1534 PHE A CE2   1 
ATOM   961   C  CZ    . PHE A 1 317  ? 130.440 167.795 123.656 1.00 24.13  ? 1534 PHE A CZ    1 
ATOM   962   N  N     . PRO A 1 318  ? 129.809 162.204 124.496 1.00 31.61  ? 1535 PRO A N     1 
ATOM   963   C  CA    . PRO A 1 318  ? 130.883 161.513 125.225 1.00 26.38  ? 1535 PRO A CA    1 
ATOM   964   C  C     . PRO A 1 318  ? 131.930 162.435 125.828 1.00 25.78  ? 1535 PRO A C     1 
ATOM   965   O  O     . PRO A 1 318  ? 132.839 161.941 126.503 1.00 31.03  ? 1535 PRO A O     1 
ATOM   966   C  CB    . PRO A 1 318  ? 131.497 160.599 124.155 1.00 29.32  ? 1535 PRO A CB    1 
ATOM   967   C  CG    . PRO A 1 318  ? 131.124 161.220 122.857 1.00 30.68  ? 1535 PRO A CG    1 
ATOM   968   C  CD    . PRO A 1 318  ? 129.820 161.907 123.055 1.00 30.62  ? 1535 PRO A CD    1 
ATOM   969   N  N     . ARG A 1 319  ? 131.846 163.747 125.613 1.00 26.08  ? 1536 ARG A N     1 
ATOM   970   C  CA    . ARG A 1 319  ? 132.685 164.685 126.345 1.00 22.34  ? 1536 ARG A CA    1 
ATOM   971   C  C     . ARG A 1 319  ? 132.102 165.064 127.701 1.00 23.70  ? 1536 ARG A C     1 
ATOM   972   O  O     . ARG A 1 319  ? 132.806 165.684 128.504 1.00 23.26  ? 1536 ARG A O     1 
ATOM   973   C  CB    . ARG A 1 319  ? 132.933 165.946 125.515 1.00 21.35  ? 1536 ARG A CB    1 
ATOM   974   C  CG    . ARG A 1 319  ? 134.312 165.992 124.897 1.00 16.60  ? 1536 ARG A CG    1 
ATOM   975   C  CD    . ARG A 1 319  ? 134.709 167.399 124.514 1.00 17.63  ? 1536 ARG A CD    1 
ATOM   976   N  NE    . ARG A 1 319  ? 136.056 167.441 123.958 1.00 16.04  ? 1536 ARG A NE    1 
ATOM   977   C  CZ    . ARG A 1 319  ? 136.339 167.249 122.679 1.00 13.81  ? 1536 ARG A CZ    1 
ATOM   978   N  NH1   . ARG A 1 319  ? 135.391 166.997 121.792 1.00 11.98  ? 1536 ARG A NH1   1 
ATOM   979   N  NH2   . ARG A 1 319  ? 137.605 167.312 122.278 1.00 11.76  ? 1536 ARG A NH2   1 
ATOM   980   N  N     . PHE A 1 320  ? 130.837 164.718 127.973 1.00 27.59  ? 1537 PHE A N     1 
ATOM   981   C  CA    . PHE A 1 320  ? 130.341 164.728 129.348 1.00 29.00  ? 1537 PHE A CA    1 
ATOM   982   C  C     . PHE A 1 320  ? 131.105 163.791 130.259 1.00 27.53  ? 1537 PHE A C     1 
ATOM   983   O  O     . PHE A 1 320  ? 131.096 163.987 131.479 1.00 29.68  ? 1537 PHE A O     1 
ATOM   984   C  CB    . PHE A 1 320  ? 128.870 164.317 129.431 1.00 34.09  ? 1537 PHE A CB    1 
ATOM   985   C  CG    . PHE A 1 320  ? 127.910 165.340 128.937 1.00 32.10  ? 1537 PHE A CG    1 
ATOM   986   C  CD1   . PHE A 1 320  ? 128.310 166.642 128.736 1.00 30.16  ? 1537 PHE A CD1   1 
ATOM   987   C  CD2   . PHE A 1 320  ? 126.580 165.012 128.755 1.00 34.81  ? 1537 PHE A CD2   1 
ATOM   988   C  CE1   . PHE A 1 320  ? 127.416 167.585 128.313 1.00 36.01  ? 1537 PHE A CE1   1 
ATOM   989   C  CE2   . PHE A 1 320  ? 125.677 165.952 128.332 1.00 35.11  ? 1537 PHE A CE2   1 
ATOM   990   C  CZ    . PHE A 1 320  ? 126.096 167.244 128.109 1.00 38.19  ? 1537 PHE A CZ    1 
ATOM   991   N  N     . TYR A 1 321  ? 131.758 162.781 129.701 1.00 27.05  ? 1538 TYR A N     1 
ATOM   992   C  CA    . TYR A 1 321  ? 132.173 161.634 130.487 1.00 29.35  ? 1538 TYR A CA    1 
ATOM   993   C  C     . TYR A 1 321  ? 133.525 161.894 131.148 1.00 28.31  ? 1538 TYR A C     1 
ATOM   994   O  O     . TYR A 1 321  ? 134.046 161.015 131.843 1.00 27.89  ? 1538 TYR A O     1 
ATOM   995   C  CB    . TYR A 1 321  ? 132.178 160.398 129.569 1.00 30.11  ? 1538 TYR A CB    1 
ATOM   996   C  CG    . TYR A 1 321  ? 132.343 159.037 130.222 1.00 32.88  ? 1538 TYR A CG    1 
ATOM   997   C  CD1   . TYR A 1 321  ? 131.270 158.464 130.887 1.00 39.69  ? 1538 TYR A CD1   1 
ATOM   998   C  CD2   . TYR A 1 321  ? 133.503 158.296 130.123 1.00 34.82  ? 1538 TYR A CD2   1 
ATOM   999   C  CE1   . TYR A 1 321  ? 131.343 157.227 131.479 1.00 40.31  ? 1538 TYR A CE1   1 
ATOM   1000  C  CE2   . TYR A 1 321  ? 133.584 157.034 130.714 1.00 37.10  ? 1538 TYR A CE2   1 
ATOM   1001  C  CZ    . TYR A 1 321  ? 132.503 156.510 131.391 1.00 40.17  ? 1538 TYR A CZ    1 
ATOM   1002  O  OH    . TYR A 1 321  ? 132.595 155.266 131.981 1.00 46.49  ? 1538 TYR A OH    1 
ATOM   1003  N  N     . PHE A 1 322  ? 134.097 163.089 130.925 1.00 28.36  ? 1539 PHE A N     1 
ATOM   1004  C  CA    . PHE A 1 322  ? 135.235 163.626 131.666 1.00 25.58  ? 1539 PHE A CA    1 
ATOM   1005  C  C     . PHE A 1 322  ? 134.833 164.280 132.979 1.00 27.24  ? 1539 PHE A C     1 
ATOM   1006  O  O     . PHE A 1 322  ? 135.710 164.553 133.805 1.00 28.18  ? 1539 PHE A O     1 
ATOM   1007  C  CB    . PHE A 1 322  ? 135.981 164.684 130.841 1.00 22.68  ? 1539 PHE A CB    1 
ATOM   1008  C  CG    . PHE A 1 322  ? 136.722 164.139 129.657 1.00 20.63  ? 1539 PHE A CG    1 
ATOM   1009  C  CD1   . PHE A 1 322  ? 137.144 162.824 129.628 1.00 20.42  ? 1539 PHE A CD1   1 
ATOM   1010  C  CD2   . PHE A 1 322  ? 137.008 164.954 128.573 1.00 20.93  ? 1539 PHE A CD2   1 
ATOM   1011  C  CE1   . PHE A 1 322  ? 137.826 162.330 128.537 1.00 21.10  ? 1539 PHE A CE1   1 
ATOM   1012  C  CE2   . PHE A 1 322  ? 137.690 164.463 127.481 1.00 20.44  ? 1539 PHE A CE2   1 
ATOM   1013  C  CZ    . PHE A 1 322  ? 138.098 163.151 127.464 1.00 19.96  ? 1539 PHE A CZ    1 
ATOM   1014  N  N     . LEU A 1 323  ? 133.549 164.556 133.181 1.00 29.70  ? 1540 LEU A N     1 
ATOM   1015  C  CA    . LEU A 1 323  ? 133.071 165.240 134.372 1.00 30.74  ? 1540 LEU A CA    1 
ATOM   1016  C  C     . LEU A 1 323  ? 132.620 164.246 135.433 1.00 34.44  ? 1540 LEU A C     1 
ATOM   1017  O  O     . LEU A 1 323  ? 132.359 163.073 135.156 1.00 35.08  ? 1540 LEU A O     1 
ATOM   1018  C  CB    . LEU A 1 323  ? 131.907 166.172 134.039 1.00 28.04  ? 1540 LEU A CB    1 
ATOM   1019  C  CG    . LEU A 1 323  ? 132.099 167.228 132.959 1.00 28.37  ? 1540 LEU A CG    1 
ATOM   1020  C  CD1   . LEU A 1 323  ? 130.768 167.852 132.632 1.00 31.46  ? 1540 LEU A CD1   1 
ATOM   1021  C  CD2   . LEU A 1 323  ? 133.064 168.280 133.443 1.00 35.87  ? 1540 LEU A CD2   1 
ATOM   1022  N  N     . GLY A 1 324  ? 132.521 164.739 136.664 1.00 33.12  ? 1541 GLY A N     1 
ATOM   1023  C  CA    . GLY A 1 324  ? 131.886 163.996 137.726 1.00 37.36  ? 1541 GLY A CA    1 
ATOM   1024  C  C     . GLY A 1 324  ? 130.380 164.001 137.569 1.00 47.16  ? 1541 GLY A C     1 
ATOM   1025  O  O     . GLY A 1 324  ? 129.819 164.608 136.657 1.00 54.64  ? 1541 GLY A O     1 
ATOM   1026  N  N     . ASN A 1 325  ? 129.713 163.290 138.478 1.00 48.64  ? 1542 ASN A N     1 
ATOM   1027  C  CA    . ASN A 1 325  ? 128.256 163.229 138.430 1.00 51.70  ? 1542 ASN A CA    1 
ATOM   1028  C  C     . ASN A 1 325  ? 127.633 164.595 138.695 1.00 53.02  ? 1542 ASN A C     1 
ATOM   1029  O  O     . ASN A 1 325  ? 126.680 164.990 138.012 1.00 54.59  ? 1542 ASN A O     1 
ATOM   1030  C  CB    . ASN A 1 325  ? 127.742 162.194 139.429 1.00 61.47  ? 1542 ASN A CB    1 
ATOM   1031  C  CG    . ASN A 1 325  ? 128.367 162.346 140.803 1.00 68.15  ? 1542 ASN A CG    1 
ATOM   1032  O  OD1   . ASN A 1 325  ? 129.149 163.265 141.045 1.00 67.61  ? 1542 ASN A OD1   1 
ATOM   1033  N  ND2   . ASN A 1 325  ? 128.024 161.440 141.711 1.00 69.41  ? 1542 ASN A ND2   1 
ATOM   1034  N  N     . ASP A 1 326  ? 128.174 165.338 139.666 1.00 52.89  ? 1543 ASP A N     1 
ATOM   1035  C  CA    . ASP A 1 326  ? 127.567 166.605 140.071 1.00 59.61  ? 1543 ASP A CA    1 
ATOM   1036  C  C     . ASP A 1 326  ? 127.640 167.651 138.963 1.00 57.84  ? 1543 ASP A C     1 
ATOM   1037  O  O     . ASP A 1 326  ? 126.698 168.431 138.779 1.00 63.29  ? 1543 ASP A O     1 
ATOM   1038  C  CB    . ASP A 1 326  ? 128.234 167.118 141.347 1.00 59.73  ? 1543 ASP A CB    1 
ATOM   1039  C  CG    . ASP A 1 326  ? 129.742 167.213 141.224 1.00 60.36  ? 1543 ASP A CG    1 
ATOM   1040  O  OD1   . ASP A 1 326  ? 130.288 166.778 140.188 1.00 58.72  ? 1543 ASP A OD1   1 
ATOM   1041  O  OD2   . ASP A 1 326  ? 130.384 167.724 142.165 1.00 63.67  ? 1543 ASP A OD2   1 
ATOM   1042  N  N     . ASP A 1 327  ? 128.748 167.686 138.220 1.00 51.64  ? 1544 ASP A N     1 
ATOM   1043  C  CA    . ASP A 1 327  ? 128.858 168.628 137.110 1.00 50.23  ? 1544 ASP A CA    1 
ATOM   1044  C  C     . ASP A 1 327  ? 127.854 168.299 136.013 1.00 51.33  ? 1544 ASP A C     1 
ATOM   1045  O  O     . ASP A 1 327  ? 127.264 169.204 135.408 1.00 55.60  ? 1544 ASP A O     1 
ATOM   1046  C  CB    . ASP A 1 327  ? 130.284 168.625 136.565 1.00 48.84  ? 1544 ASP A CB    1 
ATOM   1047  C  CG    . ASP A 1 327  ? 131.295 169.115 137.582 1.00 50.94  ? 1544 ASP A CG    1 
ATOM   1048  O  OD1   . ASP A 1 327  ? 131.444 170.344 137.729 1.00 50.10  ? 1544 ASP A OD1   1 
ATOM   1049  O  OD2   . ASP A 1 327  ? 131.939 168.271 138.239 1.00 53.23  ? 1544 ASP A OD2   1 
ATOM   1050  N  N     . LEU A 1 328  ? 127.636 167.007 135.755 1.00 49.21  ? 1545 LEU A N     1 
ATOM   1051  C  CA    . LEU A 1 328  ? 126.596 166.603 134.814 1.00 48.55  ? 1545 LEU A CA    1 
ATOM   1052  C  C     . LEU A 1 328  ? 125.223 167.043 135.285 1.00 56.37  ? 1545 LEU A C     1 
ATOM   1053  O  O     . LEU A 1 328  ? 124.405 167.507 134.484 1.00 57.92  ? 1545 LEU A O     1 
ATOM   1054  C  CB    . LEU A 1 328  ? 126.600 165.091 134.625 1.00 44.53  ? 1545 LEU A CB    1 
ATOM   1055  C  CG    . LEU A 1 328  ? 127.758 164.503 133.846 1.00 39.14  ? 1545 LEU A CG    1 
ATOM   1056  C  CD1   . LEU A 1 328  ? 127.360 163.129 133.383 1.00 40.44  ? 1545 LEU A CD1   1 
ATOM   1057  C  CD2   . LEU A 1 328  ? 128.069 165.403 132.686 1.00 35.79  ? 1545 LEU A CD2   1 
ATOM   1058  N  N     . LEU A 1 329  ? 124.944 166.874 136.578 1.00 58.15  ? 1546 LEU A N     1 
ATOM   1059  C  CA    . LEU A 1 329  ? 123.641 167.254 137.106 1.00 60.65  ? 1546 LEU A CA    1 
ATOM   1060  C  C     . LEU A 1 329  ? 123.426 168.758 136.997 1.00 63.36  ? 1546 LEU A C     1 
ATOM   1061  O  O     . LEU A 1 329  ? 122.332 169.211 136.641 1.00 70.77  ? 1546 LEU A O     1 
ATOM   1062  C  CB    . LEU A 1 329  ? 123.516 166.769 138.548 1.00 64.35  ? 1546 LEU A CB    1 
ATOM   1063  C  CG    . LEU A 1 329  ? 123.570 165.238 138.626 1.00 66.07  ? 1546 LEU A CG    1 
ATOM   1064  C  CD1   . LEU A 1 329  ? 123.674 164.733 140.055 1.00 74.50  ? 1546 LEU A CD1   1 
ATOM   1065  C  CD2   . LEU A 1 329  ? 122.381 164.612 137.912 1.00 66.37  ? 1546 LEU A CD2   1 
ATOM   1066  N  N     . LYS A 1 330  ? 124.473 169.545 137.256 1.00 56.84  ? 1547 LYS A N     1 
ATOM   1067  C  CA    . LYS A 1 330  ? 124.372 170.993 137.094 1.00 57.12  ? 1547 LYS A CA    1 
ATOM   1068  C  C     . LYS A 1 330  ? 124.147 171.385 135.635 1.00 60.84  ? 1547 LYS A C     1 
ATOM   1069  O  O     . LYS A 1 330  ? 123.321 172.259 135.343 1.00 64.74  ? 1547 LYS A O     1 
ATOM   1070  C  CB    . LYS A 1 330  ? 125.625 171.670 137.646 1.00 56.43  ? 1547 LYS A CB    1 
ATOM   1071  C  CG    . LYS A 1 330  ? 125.796 171.520 139.148 1.00 56.03  ? 1547 LYS A CG    1 
ATOM   1072  C  CD    . LYS A 1 330  ? 127.114 172.109 139.617 1.00 54.10  ? 1547 LYS A CD    1 
ATOM   1073  C  CE    . LYS A 1 330  ? 127.282 171.947 141.118 1.00 51.17  ? 1547 LYS A CE    1 
ATOM   1074  N  NZ    . LYS A 1 330  ? 127.375 170.513 141.512 1.00 47.12  ? 1547 LYS A NZ    1 
ATOM   1075  N  N     . ILE A 1 331  ? 124.863 170.747 134.703 1.00 59.22  ? 1548 ILE A N     1 
ATOM   1076  C  CA    . ILE A 1 331  ? 124.701 171.087 133.290 1.00 60.14  ? 1548 ILE A CA    1 
ATOM   1077  C  C     . ILE A 1 331  ? 123.305 170.721 132.794 1.00 65.94  ? 1548 ILE A C     1 
ATOM   1078  O  O     . ILE A 1 331  ? 122.652 171.516 132.107 1.00 68.95  ? 1548 ILE A O     1 
ATOM   1079  C  CB    . ILE A 1 331  ? 125.805 170.427 132.444 1.00 54.27  ? 1548 ILE A CB    1 
ATOM   1080  C  CG1   . ILE A 1 331  ? 127.138 171.133 132.685 1.00 48.80  ? 1548 ILE A CG1   1 
ATOM   1081  C  CG2   . ILE A 1 331  ? 125.454 170.448 130.965 1.00 50.74  ? 1548 ILE A CG2   1 
ATOM   1082  C  CD1   . ILE A 1 331  ? 128.301 170.468 132.015 1.00 43.89  ? 1548 ILE A CD1   1 
ATOM   1083  N  N     . ILE A 1 332  ? 122.814 169.528 133.142 1.00 68.39  ? 1549 ILE A N     1 
ATOM   1084  C  CA    . ILE A 1 332  ? 121.478 169.140 132.698 1.00 74.09  ? 1549 ILE A CA    1 
ATOM   1085  C  C     . ILE A 1 332  ? 120.390 169.932 133.415 1.00 76.29  ? 1549 ILE A C     1 
ATOM   1086  O  O     . ILE A 1 332  ? 119.285 170.074 132.881 1.00 81.89  ? 1549 ILE A O     1 
ATOM   1087  C  CB    . ILE A 1 332  ? 121.253 167.623 132.861 1.00 72.81  ? 1549 ILE A CB    1 
ATOM   1088  C  CG1   . ILE A 1 332  ? 121.217 167.225 134.335 1.00 70.45  ? 1549 ILE A CG1   1 
ATOM   1089  C  CG2   . ILE A 1 332  ? 122.315 166.837 132.103 1.00 66.77  ? 1549 ILE A CG2   1 
ATOM   1090  C  CD1   . ILE A 1 332  ? 121.092 165.745 134.559 1.00 67.64  ? 1549 ILE A CD1   1 
ATOM   1091  N  N     . GLY A 1 333  ? 120.665 170.460 134.613 1.00 71.94  ? 1550 GLY A N     1 
ATOM   1092  C  CA    . GLY A 1 333  ? 119.732 171.385 135.229 1.00 80.15  ? 1550 GLY A CA    1 
ATOM   1093  C  C     . GLY A 1 333  ? 119.770 172.777 134.646 1.00 81.39  ? 1550 GLY A C     1 
ATOM   1094  O  O     . GLY A 1 333  ? 118.803 173.528 134.795 1.00 89.55  ? 1550 GLY A O     1 
ATOM   1095  N  N     . SER A 1 334  ? 120.875 173.142 133.995 1.00 76.46  ? 1551 SER A N     1 
ATOM   1096  C  CA    . SER A 1 334  ? 120.956 174.402 133.257 1.00 81.69  ? 1551 SER A CA    1 
ATOM   1097  C  C     . SER A 1 334  ? 120.327 174.216 131.873 1.00 86.09  ? 1551 SER A C     1 
ATOM   1098  O  O     . SER A 1 334  ? 120.988 174.253 130.833 1.00 83.08  ? 1551 SER A O     1 
ATOM   1099  C  CB    . SER A 1 334  ? 122.400 174.869 133.157 1.00 77.10  ? 1551 SER A CB    1 
ATOM   1100  O  OG    . SER A 1 334  ? 122.507 176.020 132.338 1.00 77.19  ? 1551 SER A OG    1 
ATOM   1101  N  N     . GLY A 1 335  ? 119.011 174.015 131.879 1.00 88.98  ? 1552 GLY A N     1 
ATOM   1102  C  CA    . GLY A 1 335  ? 118.281 173.756 130.653 1.00 89.85  ? 1552 GLY A CA    1 
ATOM   1103  C  C     . GLY A 1 335  ? 118.027 174.996 129.822 1.00 93.34  ? 1552 GLY A C     1 
ATOM   1104  O  O     . GLY A 1 335  ? 118.517 175.105 128.694 1.00 91.64  ? 1552 GLY A O     1 
ATOM   1105  N  N     . LYS A 1 336  ? 117.261 175.940 130.370 1.00 93.21  ? 1553 LYS A N     1 
ATOM   1106  C  CA    . LYS A 1 336  ? 116.960 177.198 129.698 1.00 92.07  ? 1553 LYS A CA    1 
ATOM   1107  C  C     . LYS A 1 336  ? 117.689 178.374 130.336 1.00 85.94  ? 1553 LYS A C     1 
ATOM   1108  O  O     . LYS A 1 336  ? 117.227 179.516 130.239 1.00 81.75  ? 1553 LYS A O     1 
ATOM   1109  C  CB    . LYS A 1 336  ? 115.452 177.449 129.688 1.00 89.62  ? 1553 LYS A CB    1 
ATOM   1110  N  N     . HIS A 1 337  ? 118.823 178.115 130.983 1.00 84.67  ? 1554 HIS A N     1 
ATOM   1111  C  CA    . HIS A 1 337  ? 119.559 179.139 131.711 1.00 82.50  ? 1554 HIS A CA    1 
ATOM   1112  C  C     . HIS A 1 337  ? 120.828 179.568 130.988 1.00 79.53  ? 1554 HIS A C     1 
ATOM   1113  O  O     . HIS A 1 337  ? 121.261 180.714 131.150 1.00 77.11  ? 1554 HIS A O     1 
ATOM   1114  C  CB    . HIS A 1 337  ? 119.909 178.614 133.111 1.00 82.47  ? 1554 HIS A CB    1 
ATOM   1115  C  CG    . HIS A 1 337  ? 120.482 179.644 134.035 1.00 84.45  ? 1554 HIS A CG    1 
ATOM   1116  N  ND1   . HIS A 1 337  ? 120.419 180.994 133.765 1.00 88.08  ? 1554 HIS A ND1   1 
ATOM   1117  C  CD2   . HIS A 1 337  ? 121.182 179.525 135.188 1.00 83.74  ? 1554 HIS A CD2   1 
ATOM   1118  C  CE1   . HIS A 1 337  ? 121.019 181.664 134.733 1.00 86.90  ? 1554 HIS A CE1   1 
ATOM   1119  N  NE2   . HIS A 1 337  ? 121.491 180.796 135.609 1.00 85.80  ? 1554 HIS A NE2   1 
ATOM   1120  N  N     . HIS A 1 338  ? 121.423 178.674 130.191 1.00 80.20  ? 1555 HIS A N     1 
ATOM   1121  C  CA    . HIS A 1 338  ? 122.628 178.927 129.394 1.00 77.65  ? 1555 HIS A CA    1 
ATOM   1122  C  C     . HIS A 1 338  ? 123.827 179.319 130.259 1.00 75.73  ? 1555 HIS A C     1 
ATOM   1123  O  O     . HIS A 1 338  ? 124.801 179.894 129.760 1.00 70.27  ? 1555 HIS A O     1 
ATOM   1124  C  CB    . HIS A 1 338  ? 122.367 179.993 128.316 1.00 76.14  ? 1555 HIS A CB    1 
ATOM   1125  C  CG    . HIS A 1 338  ? 123.328 179.957 127.166 1.00 70.28  ? 1555 HIS A CG    1 
ATOM   1126  N  ND1   . HIS A 1 338  ? 124.692 179.843 127.331 1.00 65.03  ? 1555 HIS A ND1   1 
ATOM   1127  C  CD2   . HIS A 1 338  ? 123.119 180.048 125.831 1.00 66.65  ? 1555 HIS A CD2   1 
ATOM   1128  C  CE1   . HIS A 1 338  ? 125.279 179.850 126.149 1.00 63.28  ? 1555 HIS A CE1   1 
ATOM   1129  N  NE2   . HIS A 1 338  ? 124.348 179.973 125.221 1.00 62.39  ? 1555 HIS A NE2   1 
ATOM   1130  N  N     . ASP A 1 339  ? 123.789 179.008 131.551 1.00 76.87  ? 1556 ASP A N     1 
ATOM   1131  C  CA    . ASP A 1 339  ? 124.839 179.401 132.474 1.00 74.19  ? 1556 ASP A CA    1 
ATOM   1132  C  C     . ASP A 1 339  ? 125.353 178.175 133.213 1.00 69.12  ? 1556 ASP A C     1 
ATOM   1133  O  O     . ASP A 1 339  ? 124.680 177.145 133.291 1.00 70.88  ? 1556 ASP A O     1 
ATOM   1134  C  CB    . ASP A 1 339  ? 124.343 180.459 133.466 1.00 79.47  ? 1556 ASP A CB    1 
ATOM   1135  C  CG    . ASP A 1 339  ? 124.067 181.793 132.799 1.00 84.61  ? 1556 ASP A CG    1 
ATOM   1136  O  OD1   . ASP A 1 339  ? 124.729 182.094 131.784 1.00 87.30  ? 1556 ASP A OD1   1 
ATOM   1137  O  OD2   . ASP A 1 339  ? 123.192 182.538 133.286 1.00 85.90  ? 1556 ASP A OD2   1 
ATOM   1138  N  N     . GLN A 1 340  ? 126.595 178.296 133.694 1.00 66.80  ? 1557 GLN A N     1 
ATOM   1139  C  CA    . GLN A 1 340  ? 127.340 177.292 134.454 1.00 63.92  ? 1557 GLN A CA    1 
ATOM   1140  C  C     . GLN A 1 340  ? 127.771 176.115 133.583 1.00 61.67  ? 1557 GLN A C     1 
ATOM   1141  O  O     . GLN A 1 340  ? 128.532 175.257 134.037 1.00 60.20  ? 1557 GLN A O     1 
ATOM   1142  C  CB    . GLN A 1 340  ? 126.545 176.796 135.669 1.00 68.33  ? 1557 GLN A CB    1 
ATOM   1143  C  CG    . GLN A 1 340  ? 126.446 177.802 136.805 1.00 79.85  ? 1557 GLN A CG    1 
ATOM   1144  C  CD    . GLN A 1 340  ? 125.342 178.820 136.594 1.00 82.15  ? 1557 GLN A CD    1 
ATOM   1145  O  OE1   . GLN A 1 340  ? 124.170 178.465 136.470 1.00 78.68  ? 1557 GLN A OE1   1 
ATOM   1146  N  NE2   . GLN A 1 340  ? 125.712 180.095 136.556 1.00 81.38  ? 1557 GLN A NE2   1 
ATOM   1147  N  N     . VAL A 1 341  ? 127.312 176.067 132.328 1.00 62.33  ? 1558 VAL A N     1 
ATOM   1148  C  CA    . VAL A 1 341  ? 127.905 175.167 131.342 1.00 54.87  ? 1558 VAL A CA    1 
ATOM   1149  C  C     . VAL A 1 341  ? 129.061 175.837 130.627 1.00 48.92  ? 1558 VAL A C     1 
ATOM   1150  O  O     . VAL A 1 341  ? 129.806 175.165 129.898 1.00 49.86  ? 1558 VAL A O     1 
ATOM   1151  C  CB    . VAL A 1 341  ? 126.871 174.689 130.303 1.00 53.39  ? 1558 VAL A CB    1 
ATOM   1152  C  CG1   . VAL A 1 341  ? 125.640 174.141 130.998 1.00 61.53  ? 1558 VAL A CG1   1 
ATOM   1153  C  CG2   . VAL A 1 341  ? 126.501 175.818 129.360 1.00 58.90  ? 1558 VAL A CG2   1 
ATOM   1154  N  N     . SER A 1 342  ? 129.227 177.142 130.808 1.00 48.97  ? 1559 SER A N     1 
ATOM   1155  C  CA    . SER A 1 342  ? 130.358 177.890 130.292 1.00 47.28  ? 1559 SER A CA    1 
ATOM   1156  C  C     . SER A 1 342  ? 131.548 177.873 131.241 1.00 46.74  ? 1559 SER A C     1 
ATOM   1157  O  O     . SER A 1 342  ? 132.611 178.395 130.888 1.00 43.25  ? 1559 SER A O     1 
ATOM   1158  C  CB    . SER A 1 342  ? 129.928 179.333 130.015 1.00 49.32  ? 1559 SER A CB    1 
ATOM   1159  O  OG    . SER A 1 342  ? 131.038 180.164 129.759 1.00 51.79  ? 1559 SER A OG    1 
ATOM   1160  N  N     . LYS A 1 343  ? 131.391 177.290 132.429 1.00 48.93  ? 1560 LYS A N     1 
ATOM   1161  C  CA    . LYS A 1 343  ? 132.465 177.195 133.409 1.00 49.87  ? 1560 LYS A CA    1 
ATOM   1162  C  C     . LYS A 1 343  ? 133.136 175.830 133.435 1.00 50.96  ? 1560 LYS A C     1 
ATOM   1163  O  O     . LYS A 1 343  ? 134.337 175.751 133.714 1.00 51.14  ? 1560 LYS A O     1 
ATOM   1164  C  CB    . LYS A 1 343  ? 131.934 177.511 134.812 1.00 46.20  ? 1560 LYS A CB    1 
ATOM   1165  C  CG    . LYS A 1 343  ? 131.489 178.954 135.025 1.00 54.34  ? 1560 LYS A CG    1 
ATOM   1166  C  CD    . LYS A 1 343  ? 132.383 179.949 134.301 1.00 58.86  ? 1560 LYS A CD    1 
ATOM   1167  C  CE    . LYS A 1 343  ? 131.757 181.335 134.276 1.00 55.59  ? 1560 LYS A CE    1 
ATOM   1168  N  NZ    . LYS A 1 343  ? 130.642 181.433 133.294 1.00 53.24  ? 1560 LYS A NZ    1 
ATOM   1169  N  N     . PHE A 1 344  ? 132.399 174.758 133.152 1.00 46.42  ? 1561 PHE A N     1 
ATOM   1170  C  CA    . PHE A 1 344  ? 132.956 173.412 133.162 1.00 40.65  ? 1561 PHE A CA    1 
ATOM   1171  C  C     . PHE A 1 344  ? 133.561 173.017 131.824 1.00 36.75  ? 1561 PHE A C     1 
ATOM   1172  O  O     . PHE A 1 344  ? 134.014 171.877 131.672 1.00 38.43  ? 1561 PHE A O     1 
ATOM   1173  C  CB    . PHE A 1 344  ? 131.882 172.389 133.546 1.00 40.22  ? 1561 PHE A CB    1 
ATOM   1174  C  CG    . PHE A 1 344  ? 131.167 172.710 134.822 1.00 48.06  ? 1561 PHE A CG    1 
ATOM   1175  C  CD1   . PHE A 1 344  ? 131.865 173.129 135.941 1.00 52.59  ? 1561 PHE A CD1   1 
ATOM   1176  C  CD2   . PHE A 1 344  ? 129.793 172.567 134.910 1.00 52.06  ? 1561 PHE A CD2   1 
ATOM   1177  C  CE1   . PHE A 1 344  ? 131.200 173.424 137.119 1.00 56.67  ? 1561 PHE A CE1   1 
ATOM   1178  C  CE2   . PHE A 1 344  ? 129.124 172.857 136.082 1.00 53.31  ? 1561 PHE A CE2   1 
ATOM   1179  C  CZ    . PHE A 1 344  ? 129.828 173.284 137.189 1.00 53.24  ? 1561 PHE A CZ    1 
ATOM   1180  N  N     . MET A 1 345  ? 133.578 173.920 130.852 1.00 32.73  ? 1562 MET A N     1 
ATOM   1181  C  CA    . MET A 1 345  ? 134.047 173.566 129.524 1.00 29.42  ? 1562 MET A CA    1 
ATOM   1182  C  C     . MET A 1 345  ? 135.566 173.656 129.412 1.00 26.98  ? 1562 MET A C     1 
ATOM   1183  O  O     . MET A 1 345  ? 136.134 173.243 128.396 1.00 26.57  ? 1562 MET A O     1 
ATOM   1184  C  CB    . MET A 1 345  ? 133.307 174.437 128.497 1.00 28.73  ? 1562 MET A CB    1 
ATOM   1185  C  CG    . MET A 1 345  ? 133.534 174.111 127.034 1.00 27.94  ? 1562 MET A CG    1 
ATOM   1186  S  SD    . MET A 1 345  ? 132.518 175.151 125.984 1.00 29.99  ? 1562 MET A SD    1 
ATOM   1187  C  CE    . MET A 1 345  ? 130.925 174.408 126.329 1.00 36.86  ? 1562 MET A CE    1 
ATOM   1188  N  N     . LYS A 1 346  ? 136.244 174.135 130.456 1.00 29.20  ? 1563 LYS A N     1 
ATOM   1189  C  CA    . LYS A 1 346  ? 137.664 173.834 130.602 1.00 30.91  ? 1563 LYS A CA    1 
ATOM   1190  C  C     . LYS A 1 346  ? 137.872 172.357 130.907 1.00 29.27  ? 1563 LYS A C     1 
ATOM   1191  O  O     . LYS A 1 346  ? 138.822 171.740 130.412 1.00 26.53  ? 1563 LYS A O     1 
ATOM   1192  C  CB    . LYS A 1 346  ? 138.278 174.701 131.700 1.00 36.74  ? 1563 LYS A CB    1 
ATOM   1193  C  CG    . LYS A 1 346  ? 139.757 174.445 131.949 1.00 39.86  ? 1563 LYS A CG    1 
ATOM   1194  C  CD    . LYS A 1 346  ? 140.630 175.371 131.129 1.00 39.46  ? 1563 LYS A CD    1 
ATOM   1195  C  CE    . LYS A 1 346  ? 142.102 175.163 131.444 1.00 42.96  ? 1563 LYS A CE    1 
ATOM   1196  N  NZ    . LYS A 1 346  ? 142.334 174.967 132.901 1.00 45.78  ? 1563 LYS A NZ    1 
ATOM   1197  N  N     . LYS A 1 347  ? 136.990 171.775 131.722 1.00 27.73  ? 1564 LYS A N     1 
ATOM   1198  C  CA    . LYS A 1 347  ? 137.087 170.355 132.037 1.00 24.76  ? 1564 LYS A CA    1 
ATOM   1199  C  C     . LYS A 1 347  ? 136.666 169.496 130.852 1.00 24.89  ? 1564 LYS A C     1 
ATOM   1200  O  O     . LYS A 1 347  ? 137.325 168.502 130.529 1.00 27.98  ? 1564 LYS A O     1 
ATOM   1201  C  CB    . LYS A 1 347  ? 136.231 170.029 133.259 1.00 26.47  ? 1564 LYS A CB    1 
ATOM   1202  C  CG    . LYS A 1 347  ? 136.654 170.725 134.535 1.00 30.21  ? 1564 LYS A CG    1 
ATOM   1203  C  CD    . LYS A 1 347  ? 136.068 170.027 135.750 1.00 32.66  ? 1564 LYS A CD    1 
ATOM   1204  C  CE    . LYS A 1 347  ? 134.743 170.650 136.150 1.00 39.20  ? 1564 LYS A CE    1 
ATOM   1205  N  NZ    . LYS A 1 347  ? 134.938 171.922 136.896 1.00 41.01  ? 1564 LYS A NZ    1 
ATOM   1206  N  N     . MET A 1 348  ? 135.556 169.853 130.201 1.00 22.72  ? 1565 MET A N     1 
ATOM   1207  C  CA    . MET A 1 348  ? 135.054 169.027 129.105 1.00 22.49  ? 1565 MET A CA    1 
ATOM   1208  C  C     . MET A 1 348  ? 135.946 169.123 127.873 1.00 20.57  ? 1565 MET A C     1 
ATOM   1209  O  O     . MET A 1 348  ? 136.324 168.102 127.289 1.00 21.76  ? 1565 MET A O     1 
ATOM   1210  C  CB    . MET A 1 348  ? 133.623 169.425 128.743 1.00 23.47  ? 1565 MET A CB    1 
ATOM   1211  C  CG    . MET A 1 348  ? 132.618 169.243 129.850 1.00 22.60  ? 1565 MET A CG    1 
ATOM   1212  S  SD    . MET A 1 348  ? 130.962 169.754 129.357 1.00 23.55  ? 1565 MET A SD    1 
ATOM   1213  C  CE    . MET A 1 348  ? 131.310 171.278 128.489 1.00 25.81  ? 1565 MET A CE    1 
ATOM   1214  N  N     . PHE A 1 349  ? 136.293 170.340 127.462 1.00 18.66  ? 1566 PHE A N     1 
ATOM   1215  C  CA    . PHE A 1 349  ? 136.912 170.549 126.161 1.00 18.46  ? 1566 PHE A CA    1 
ATOM   1216  C  C     . PHE A 1 349  ? 138.424 170.714 126.218 1.00 20.56  ? 1566 PHE A C     1 
ATOM   1217  O  O     . PHE A 1 349  ? 139.079 170.612 125.175 1.00 19.93  ? 1566 PHE A O     1 
ATOM   1218  C  CB    . PHE A 1 349  ? 136.303 171.778 125.482 1.00 18.73  ? 1566 PHE A CB    1 
ATOM   1219  C  CG    . PHE A 1 349  ? 135.043 171.492 124.718 1.00 16.91  ? 1566 PHE A CG    1 
ATOM   1220  C  CD1   . PHE A 1 349  ? 133.965 170.878 125.332 1.00 16.01  ? 1566 PHE A CD1   1 
ATOM   1221  C  CD2   . PHE A 1 349  ? 134.935 171.845 123.385 1.00 18.95  ? 1566 PHE A CD2   1 
ATOM   1222  C  CE1   . PHE A 1 349  ? 132.806 170.619 124.630 1.00 17.60  ? 1566 PHE A CE1   1 
ATOM   1223  C  CE2   . PHE A 1 349  ? 133.778 171.589 122.679 1.00 21.89  ? 1566 PHE A CE2   1 
ATOM   1224  C  CZ    . PHE A 1 349  ? 132.713 170.975 123.303 1.00 21.39  ? 1566 PHE A CZ    1 
ATOM   1225  N  N     . GLY A 1 350  ? 138.989 170.977 127.388 1.00 21.47  ? 1567 GLY A N     1 
ATOM   1226  C  CA    . GLY A 1 350  ? 140.428 171.061 127.565 1.00 21.39  ? 1567 GLY A CA    1 
ATOM   1227  C  C     . GLY A 1 350  ? 141.083 172.379 127.208 1.00 21.07  ? 1567 GLY A C     1 
ATOM   1228  O  O     . GLY A 1 350  ? 142.057 172.776 127.851 1.00 21.69  ? 1567 GLY A O     1 
ATOM   1229  N  N     . SER A 1 351  ? 140.571 173.071 126.188 1.00 22.09  ? 1568 SER A N     1 
ATOM   1230  C  CA    . SER A 1 351  ? 141.168 174.334 125.776 1.00 21.98  ? 1568 SER A CA    1 
ATOM   1231  C  C     . SER A 1 351  ? 140.115 175.403 125.508 1.00 24.60  ? 1568 SER A C     1 
ATOM   1232  O  O     . SER A 1 351  ? 140.296 176.248 124.625 1.00 24.57  ? 1568 SER A O     1 
ATOM   1233  C  CB    . SER A 1 351  ? 142.044 174.152 124.539 1.00 17.01  ? 1568 SER A CB    1 
ATOM   1234  O  OG    . SER A 1 351  ? 142.955 175.228 124.420 1.00 17.77  ? 1568 SER A OG    1 
ATOM   1235  N  N     . ILE A 1 352  ? 139.015 175.385 126.255 1.00 25.51  ? 1569 ILE A N     1 
ATOM   1236  C  CA    . ILE A 1 352  ? 137.970 176.397 126.162 1.00 23.48  ? 1569 ILE A CA    1 
ATOM   1237  C  C     . ILE A 1 352  ? 137.788 177.012 127.538 1.00 30.19  ? 1569 ILE A C     1 
ATOM   1238  O  O     . ILE A 1 352  ? 137.686 176.288 128.534 1.00 32.81  ? 1569 ILE A O     1 
ATOM   1239  C  CB    . ILE A 1 352  ? 136.640 175.809 125.657 1.00 22.57  ? 1569 ILE A CB    1 
ATOM   1240  C  CG1   . ILE A 1 352  ? 136.840 175.109 124.319 1.00 24.09  ? 1569 ILE A CG1   1 
ATOM   1241  C  CG2   . ILE A 1 352  ? 135.602 176.900 125.514 1.00 26.87  ? 1569 ILE A CG2   1 
ATOM   1242  C  CD1   . ILE A 1 352  ? 137.296 176.020 123.244 1.00 21.03  ? 1569 ILE A CD1   1 
ATOM   1243  N  N     . GLU A 1 353  ? 137.748 178.341 127.598 1.00 31.19  ? 1570 GLU A N     1 
ATOM   1244  C  CA    . GLU A 1 353  ? 137.519 179.011 128.870 1.00 33.98  ? 1570 GLU A CA    1 
ATOM   1245  C  C     . GLU A 1 353  ? 136.038 179.266 129.125 1.00 33.48  ? 1570 GLU A C     1 
ATOM   1246  O  O     . GLU A 1 353  ? 135.533 178.951 130.207 1.00 33.45  ? 1570 GLU A O     1 
ATOM   1247  C  CB    . GLU A 1 353  ? 138.295 180.328 128.923 1.00 37.60  ? 1570 GLU A CB    1 
ATOM   1248  C  CG    . GLU A 1 353  ? 138.545 180.843 130.330 1.00 43.17  ? 1570 GLU A CG    1 
ATOM   1249  C  CD    . GLU A 1 353  ? 139.686 181.838 130.388 1.00 47.60  ? 1570 GLU A CD    1 
ATOM   1250  O  OE1   . GLU A 1 353  ? 139.702 182.775 129.562 1.00 47.46  ? 1570 GLU A OE1   1 
ATOM   1251  O  OE2   . GLU A 1 353  ? 140.568 181.681 131.257 1.00 47.52  ? 1570 GLU A OE2   1 
ATOM   1252  N  N     . SER A 1 354  ? 135.327 179.825 128.148 1.00 33.22  ? 1571 SER A N     1 
ATOM   1253  C  CA    . SER A 1 354  ? 133.945 180.215 128.386 1.00 36.96  ? 1571 SER A CA    1 
ATOM   1254  C  C     . SER A 1 354  ? 133.184 180.312 127.072 1.00 40.08  ? 1571 SER A C     1 
ATOM   1255  O  O     . SER A 1 354  ? 133.770 180.479 125.999 1.00 41.38  ? 1571 SER A O     1 
ATOM   1256  C  CB    . SER A 1 354  ? 133.871 181.547 129.141 1.00 43.87  ? 1571 SER A CB    1 
ATOM   1257  O  OG    . SER A 1 354  ? 134.258 182.625 128.309 1.00 44.47  ? 1571 SER A OG    1 
ATOM   1258  N  N     . ILE A 1 355  ? 131.861 180.200 127.182 1.00 42.66  ? 1572 ILE A N     1 
ATOM   1259  C  CA    . ILE A 1 355  ? 130.943 180.454 126.077 1.00 44.53  ? 1572 ILE A CA    1 
ATOM   1260  C  C     . ILE A 1 355  ? 130.633 181.943 126.019 1.00 50.72  ? 1572 ILE A C     1 
ATOM   1261  O  O     . ILE A 1 355  ? 130.427 182.588 127.055 1.00 56.13  ? 1572 ILE A O     1 
ATOM   1262  C  CB    . ILE A 1 355  ? 129.651 179.632 126.255 1.00 47.17  ? 1572 ILE A CB    1 
ATOM   1263  C  CG1   . ILE A 1 355  ? 129.932 178.130 126.215 1.00 44.71  ? 1572 ILE A CG1   1 
ATOM   1264  C  CG2   . ILE A 1 355  ? 128.606 180.009 125.209 1.00 50.26  ? 1572 ILE A CG2   1 
ATOM   1265  C  CD1   . ILE A 1 355  ? 129.979 177.565 124.820 1.00 43.46  ? 1572 ILE A CD1   1 
ATOM   1266  N  N     . ILE A 1 356  ? 130.599 182.502 124.811 1.00 51.32  ? 1573 ILE A N     1 
ATOM   1267  C  CA    . ILE A 1 356  ? 130.044 183.830 124.574 1.00 60.30  ? 1573 ILE A CA    1 
ATOM   1268  C  C     . ILE A 1 356  ? 128.694 183.666 123.892 1.00 61.08  ? 1573 ILE A C     1 
ATOM   1269  O  O     . ILE A 1 356  ? 128.544 182.841 122.983 1.00 59.87  ? 1573 ILE A O     1 
ATOM   1270  C  CB    . ILE A 1 356  ? 130.984 184.714 123.737 1.00 58.64  ? 1573 ILE A CB    1 
ATOM   1271  C  CG1   . ILE A 1 356  ? 131.468 183.978 122.491 1.00 53.16  ? 1573 ILE A CG1   1 
ATOM   1272  C  CG2   . ILE A 1 356  ? 132.148 185.194 124.573 1.00 57.45  ? 1573 ILE A CG2   1 
ATOM   1273  C  CD1   . ILE A 1 356  ? 132.193 184.867 121.530 1.00 55.37  ? 1573 ILE A CD1   1 
ATOM   1274  N  N     . PHE A 1 357  ? 127.708 184.430 124.349 1.00 66.42  ? 1574 PHE A N     1 
ATOM   1275  C  CA    . PHE A 1 357  ? 126.360 184.371 123.806 1.00 69.31  ? 1574 PHE A CA    1 
ATOM   1276  C  C     . PHE A 1 357  ? 125.768 185.772 123.751 1.00 77.57  ? 1574 PHE A C     1 
ATOM   1277  O  O     . PHE A 1 357  ? 125.918 186.558 124.691 1.00 77.93  ? 1574 PHE A O     1 
ATOM   1278  C  CB    . PHE A 1 357  ? 125.474 183.422 124.638 1.00 69.38  ? 1574 PHE A CB    1 
ATOM   1279  C  CG    . PHE A 1 357  ? 125.275 183.855 126.067 1.00 77.84  ? 1574 PHE A CG    1 
ATOM   1280  C  CD1   . PHE A 1 357  ? 126.165 183.456 127.052 1.00 73.66  ? 1574 PHE A CD1   1 
ATOM   1281  C  CD2   . PHE A 1 357  ? 124.178 184.622 126.435 1.00 82.70  ? 1574 PHE A CD2   1 
ATOM   1282  C  CE1   . PHE A 1 357  ? 125.986 183.843 128.369 1.00 77.41  ? 1574 PHE A CE1   1 
ATOM   1283  C  CE2   . PHE A 1 357  ? 123.993 185.010 127.750 1.00 83.97  ? 1574 PHE A CE2   1 
ATOM   1284  C  CZ    . PHE A 1 357  ? 124.898 184.618 128.718 1.00 79.38  ? 1574 PHE A CZ    1 
ATOM   1285  N  N     . PHE A 1 358  ? 125.116 186.087 122.633 1.00 79.30  ? 1575 PHE A N     1 
ATOM   1286  C  CA    . PHE A 1 358  ? 124.428 187.362 122.449 1.00 81.79  ? 1575 PHE A CA    1 
ATOM   1287  C  C     . PHE A 1 358  ? 122.991 187.087 122.034 1.00 80.63  ? 1575 PHE A C     1 
ATOM   1288  O  O     . PHE A 1 358  ? 122.753 186.452 121.001 1.00 79.91  ? 1575 PHE A O     1 
ATOM   1289  C  CB    . PHE A 1 358  ? 125.134 188.238 121.412 1.00 84.66  ? 1575 PHE A CB    1 
ATOM   1290  C  CG    . PHE A 1 358  ? 126.586 188.483 121.709 1.00 88.22  ? 1575 PHE A CG    1 
ATOM   1291  C  CD1   . PHE A 1 358  ? 126.960 189.424 122.655 1.00 88.89  ? 1575 PHE A CD1   1 
ATOM   1292  C  CD2   . PHE A 1 358  ? 127.576 187.784 121.040 1.00 80.85  ? 1575 PHE A CD2   1 
ATOM   1293  C  CE1   . PHE A 1 358  ? 128.292 189.659 122.933 1.00 86.84  ? 1575 PHE A CE1   1 
ATOM   1294  C  CE2   . PHE A 1 358  ? 128.912 188.016 121.315 1.00 75.50  ? 1575 PHE A CE2   1 
ATOM   1295  C  CZ    . PHE A 1 358  ? 129.269 188.954 122.262 1.00 81.22  ? 1575 PHE A CZ    1 
ATOM   1296  N  N     . GLU A 1 359  ? 122.045 187.572 122.843 1.00 83.84  ? 1576 GLU A N     1 
ATOM   1297  C  CA    . GLU A 1 359  ? 120.607 187.487 122.574 1.00 85.35  ? 1576 GLU A CA    1 
ATOM   1298  C  C     . GLU A 1 359  ? 120.155 186.035 122.398 1.00 81.69  ? 1576 GLU A C     1 
ATOM   1299  O  O     . GLU A 1 359  ? 119.502 185.671 121.416 1.00 76.86  ? 1576 GLU A O     1 
ATOM   1300  C  CB    . GLU A 1 359  ? 120.227 188.343 121.360 1.00 87.86  ? 1576 GLU A CB    1 
ATOM   1301  C  CG    . GLU A 1 359  ? 120.787 189.758 121.408 1.00 91.06  ? 1576 GLU A CG    1 
ATOM   1302  C  CD    . GLU A 1 359  ? 120.520 190.537 120.137 1.00 95.13  ? 1576 GLU A CD    1 
ATOM   1303  O  OE1   . GLU A 1 359  ? 121.001 190.113 119.065 1.00 97.36  ? 1576 GLU A OE1   1 
ATOM   1304  O  OE2   . GLU A 1 359  ? 119.829 191.575 120.209 1.00 91.08  ? 1576 GLU A OE2   1 
ATOM   1305  N  N     . ASP A 1 360  ? 120.518 185.213 123.389 1.00 82.50  ? 1577 ASP A N     1 
ATOM   1306  C  CA    . ASP A 1 360  ? 120.159 183.791 123.445 1.00 80.35  ? 1577 ASP A CA    1 
ATOM   1307  C  C     . ASP A 1 360  ? 120.609 183.047 122.188 1.00 78.51  ? 1577 ASP A C     1 
ATOM   1308  O  O     . ASP A 1 360  ? 119.868 182.246 121.616 1.00 79.92  ? 1577 ASP A O     1 
ATOM   1309  C  CB    . ASP A 1 360  ? 118.657 183.609 123.683 1.00 81.18  ? 1577 ASP A CB    1 
ATOM   1310  C  CG    . ASP A 1 360  ? 118.316 182.242 124.246 1.00 82.50  ? 1577 ASP A CG    1 
ATOM   1311  O  OD1   . ASP A 1 360  ? 118.619 181.993 125.432 1.00 82.08  ? 1577 ASP A OD1   1 
ATOM   1312  O  OD2   . ASP A 1 360  ? 117.744 181.417 123.504 1.00 82.23  ? 1577 ASP A OD2   1 
ATOM   1313  N  N     . SER A 1 361  ? 121.835 183.322 121.750 1.00 75.13  ? 1578 SER A N     1 
ATOM   1314  C  CA    . SER A 1 361  ? 122.398 182.651 120.588 1.00 69.75  ? 1578 SER A CA    1 
ATOM   1315  C  C     . SER A 1 361  ? 123.912 182.652 120.717 1.00 69.31  ? 1578 SER A C     1 
ATOM   1316  O  O     . SER A 1 361  ? 124.493 183.601 121.249 1.00 74.12  ? 1578 SER A O     1 
ATOM   1317  C  CB    . SER A 1 361  ? 121.968 183.331 119.285 1.00 71.24  ? 1578 SER A CB    1 
ATOM   1318  O  OG    . SER A 1 361  ? 122.185 182.476 118.180 1.00 71.49  ? 1578 SER A OG    1 
ATOM   1319  N  N     . ILE A 1 362  ? 124.541 181.594 120.219 1.00 64.31  ? 1579 ILE A N     1 
ATOM   1320  C  CA    . ILE A 1 362  ? 125.971 181.377 120.400 1.00 59.13  ? 1579 ILE A CA    1 
ATOM   1321  C  C     . ILE A 1 362  ? 126.706 181.823 119.147 1.00 54.98  ? 1579 ILE A C     1 
ATOM   1322  O  O     . ILE A 1 362  ? 126.333 181.448 118.031 1.00 54.74  ? 1579 ILE A O     1 
ATOM   1323  C  CB    . ILE A 1 362  ? 126.263 179.900 120.703 1.00 55.16  ? 1579 ILE A CB    1 
ATOM   1324  C  CG1   . ILE A 1 362  ? 125.347 179.399 121.813 1.00 58.59  ? 1579 ILE A CG1   1 
ATOM   1325  C  CG2   . ILE A 1 362  ? 127.717 179.712 121.092 1.00 46.32  ? 1579 ILE A CG2   1 
ATOM   1326  C  CD1   . ILE A 1 362  ? 125.340 177.911 121.934 1.00 56.86  ? 1579 ILE A CD1   1 
ATOM   1327  N  N     . THR A 1 363  ? 127.755 182.620 119.328 1.00 51.66  ? 1580 THR A N     1 
ATOM   1328  C  CA    . THR A 1 363  ? 128.614 183.005 118.221 1.00 52.03  ? 1580 THR A CA    1 
ATOM   1329  C  C     . THR A 1 363  ? 130.042 182.501 118.372 1.00 50.04  ? 1580 THR A C     1 
ATOM   1330  O  O     . THR A 1 363  ? 130.877 182.798 117.511 1.00 44.06  ? 1580 THR A O     1 
ATOM   1331  C  CB    . THR A 1 363  ? 128.634 184.527 118.057 1.00 57.04  ? 1580 THR A CB    1 
ATOM   1332  O  OG1   . THR A 1 363  ? 129.348 184.868 116.862 1.00 55.47  ? 1580 THR A OG1   1 
ATOM   1333  C  CG2   . THR A 1 363  ? 129.311 185.174 119.243 1.00 59.79  ? 1580 THR A CG2   1 
ATOM   1334  N  N     . GLY A 1 364  ? 130.346 181.761 119.428 1.00 50.28  ? 1581 GLY A N     1 
ATOM   1335  C  CA    . GLY A 1 364  ? 131.650 181.149 119.545 1.00 45.88  ? 1581 GLY A CA    1 
ATOM   1336  C  C     . GLY A 1 364  ? 131.977 180.796 120.982 1.00 45.26  ? 1581 GLY A C     1 
ATOM   1337  O  O     . GLY A 1 364  ? 131.111 180.793 121.851 1.00 48.34  ? 1581 GLY A O     1 
ATOM   1338  N  N     . VAL A 1 365  ? 133.259 180.487 121.189 1.00 39.97  ? 1582 VAL A N     1 
ATOM   1339  C  CA    . VAL A 1 365  ? 133.807 180.092 122.477 1.00 35.23  ? 1582 VAL A CA    1 
ATOM   1340  C  C     . VAL A 1 365  ? 135.094 180.871 122.714 1.00 32.87  ? 1582 VAL A C     1 
ATOM   1341  O  O     . VAL A 1 365  ? 135.729 181.368 121.781 1.00 32.82  ? 1582 VAL A O     1 
ATOM   1342  C  CB    . VAL A 1 365  ? 134.084 178.576 122.550 1.00 30.71  ? 1582 VAL A CB    1 
ATOM   1343  C  CG1   . VAL A 1 365  ? 132.792 177.791 122.515 1.00 34.88  ? 1582 VAL A CG1   1 
ATOM   1344  C  CG2   . VAL A 1 365  ? 134.972 178.161 121.400 1.00 29.21  ? 1582 VAL A CG2   1 
ATOM   1345  N  N     . ARG A 1 366  ? 135.477 180.974 123.983 1.00 30.78  ? 1583 ARG A N     1 
ATOM   1346  C  CA    . ARG A 1 366  ? 136.716 181.630 124.378 1.00 31.14  ? 1583 ARG A CA    1 
ATOM   1347  C  C     . ARG A 1 366  ? 137.734 180.587 124.812 1.00 31.71  ? 1583 ARG A C     1 
ATOM   1348  O  O     . ARG A 1 366  ? 137.432 179.730 125.648 1.00 33.08  ? 1583 ARG A O     1 
ATOM   1349  C  CB    . ARG A 1 366  ? 136.488 182.629 125.513 1.00 37.20  ? 1583 ARG A CB    1 
ATOM   1350  C  CG    . ARG A 1 366  ? 135.314 183.561 125.310 1.00 44.05  ? 1583 ARG A CG    1 
ATOM   1351  C  CD    . ARG A 1 366  ? 135.415 184.841 126.148 1.00 43.11  ? 1583 ARG A CD    1 
ATOM   1352  N  NE    . ARG A 1 366  ? 136.440 185.766 125.676 1.00 42.24  ? 1583 ARG A NE    1 
ATOM   1353  C  CZ    . ARG A 1 366  ? 137.695 185.796 126.106 1.00 43.12  ? 1583 ARG A CZ    1 
ATOM   1354  N  NH1   . ARG A 1 366  ? 138.116 184.994 127.070 1.00 38.27  ? 1583 ARG A NH1   1 
ATOM   1355  N  NH2   . ARG A 1 366  ? 138.545 186.664 125.565 1.00 42.50  ? 1583 ARG A NH2   1 
ATOM   1356  N  N     . SER A 1 367  ? 138.935 180.667 124.249 1.00 29.96  ? 1584 SER A N     1 
ATOM   1357  C  CA    . SER A 1 367  ? 140.012 179.785 124.663 1.00 28.60  ? 1584 SER A CA    1 
ATOM   1358  C  C     . SER A 1 367  ? 140.542 180.209 126.031 1.00 31.79  ? 1584 SER A C     1 
ATOM   1359  O  O     . SER A 1 367  ? 140.219 181.280 126.551 1.00 35.39  ? 1584 SER A O     1 
ATOM   1360  C  CB    . SER A 1 367  ? 141.139 179.792 123.634 1.00 25.70  ? 1584 SER A CB    1 
ATOM   1361  O  OG    . SER A 1 367  ? 141.987 180.905 123.836 1.00 28.06  ? 1584 SER A OG    1 
ATOM   1362  N  N     . VAL A 1 368  ? 141.381 179.345 126.609 1.00 30.93  ? 1585 VAL A N     1 
ATOM   1363  C  CA    . VAL A 1 368  ? 141.936 179.604 127.936 1.00 31.16  ? 1585 VAL A CA    1 
ATOM   1364  C  C     . VAL A 1 368  ? 142.820 180.843 127.914 1.00 34.07  ? 1585 VAL A C     1 
ATOM   1365  O  O     . VAL A 1 368  ? 142.879 181.603 128.888 1.00 35.26  ? 1585 VAL A O     1 
ATOM   1366  C  CB    . VAL A 1 368  ? 142.706 178.369 128.438 1.00 27.64  ? 1585 VAL A CB    1 
ATOM   1367  C  CG1   . VAL A 1 368  ? 143.050 178.513 129.911 1.00 26.14  ? 1585 VAL A CG1   1 
ATOM   1368  C  CG2   . VAL A 1 368  ? 141.897 177.115 128.195 1.00 29.07  ? 1585 VAL A CG2   1 
ATOM   1369  N  N     . GLU A 1 369  ? 143.511 181.072 126.803 1.00 34.98  ? 1586 GLU A N     1 
ATOM   1370  C  CA    . GLU A 1 369  ? 144.375 182.233 126.642 1.00 34.28  ? 1586 GLU A CA    1 
ATOM   1371  C  C     . GLU A 1 369  ? 143.620 183.481 126.199 1.00 33.73  ? 1586 GLU A C     1 
ATOM   1372  O  O     . GLU A 1 369  ? 144.253 184.445 125.758 1.00 36.04  ? 1586 GLU A O     1 
ATOM   1373  C  CB    . GLU A 1 369  ? 145.491 181.913 125.645 1.00 30.37  ? 1586 GLU A CB    1 
ATOM   1374  C  CG    . GLU A 1 369  ? 146.343 180.717 126.043 1.00 27.54  ? 1586 GLU A CG    1 
ATOM   1375  C  CD    . GLU A 1 369  ? 145.800 179.401 125.512 1.00 28.72  ? 1586 GLU A CD    1 
ATOM   1376  O  OE1   . GLU A 1 369  ? 145.279 179.385 124.377 1.00 25.50  ? 1586 GLU A OE1   1 
ATOM   1377  O  OE2   . GLU A 1 369  ? 145.897 178.384 126.229 1.00 27.79  ? 1586 GLU A OE2   1 
ATOM   1378  N  N     . GLY A 1 370  ? 142.291 183.486 126.302 1.00 32.47  ? 1587 GLY A N     1 
ATOM   1379  C  CA    . GLY A 1 370  ? 141.492 184.645 125.974 1.00 34.03  ? 1587 GLY A CA    1 
ATOM   1380  C  C     . GLY A 1 370  ? 141.111 184.782 124.516 1.00 34.39  ? 1587 GLY A C     1 
ATOM   1381  O  O     . GLY A 1 370  ? 140.370 185.712 124.174 1.00 34.93  ? 1587 GLY A O     1 
ATOM   1382  N  N     . GLU A 1 371  ? 141.591 183.896 123.647 1.00 32.40  ? 1588 GLU A N     1 
ATOM   1383  C  CA    . GLU A 1 371  ? 141.274 183.991 122.229 1.00 30.84  ? 1588 GLU A CA    1 
ATOM   1384  C  C     . GLU A 1 371  ? 139.821 183.618 121.977 1.00 32.97  ? 1588 GLU A C     1 
ATOM   1385  O  O     . GLU A 1 371  ? 139.275 182.709 122.607 1.00 33.82  ? 1588 GLU A O     1 
ATOM   1386  C  CB    . GLU A 1 371  ? 142.188 183.081 121.415 1.00 27.19  ? 1588 GLU A CB    1 
ATOM   1387  C  CG    . GLU A 1 371  ? 142.145 183.316 119.915 1.00 27.38  ? 1588 GLU A CG    1 
ATOM   1388  C  CD    . GLU A 1 371  ? 142.954 182.295 119.141 1.00 26.93  ? 1588 GLU A CD    1 
ATOM   1389  O  OE1   . GLU A 1 371  ? 142.714 181.083 119.319 1.00 28.09  ? 1588 GLU A OE1   1 
ATOM   1390  O  OE2   . GLU A 1 371  ? 143.831 182.703 118.355 1.00 24.41  ? 1588 GLU A OE2   1 
ATOM   1391  N  N     . VAL A 1 372  ? 139.201 184.320 121.040 1.00 30.23  ? 1589 VAL A N     1 
ATOM   1392  C  CA    . VAL A 1 372  ? 137.809 184.099 120.675 1.00 31.56  ? 1589 VAL A CA    1 
ATOM   1393  C  C     . VAL A 1 372  ? 137.756 183.357 119.346 1.00 29.75  ? 1589 VAL A C     1 
ATOM   1394  O  O     . VAL A 1 372  ? 138.525 183.648 118.420 1.00 28.58  ? 1589 VAL A O     1 
ATOM   1395  C  CB    . VAL A 1 372  ? 137.036 185.436 120.628 1.00 36.73  ? 1589 VAL A CB    1 
ATOM   1396  C  CG1   . VAL A 1 372  ? 137.657 186.409 119.631 1.00 33.42  ? 1589 VAL A CG1   1 
ATOM   1397  C  CG2   . VAL A 1 372  ? 135.577 185.202 120.301 1.00 37.30  ? 1589 VAL A CG2   1 
ATOM   1398  N  N     . LEU A 1 373  ? 136.883 182.356 119.271 1.00 30.12  ? 1590 LEU A N     1 
ATOM   1399  C  CA    . LEU A 1 373  ? 136.644 181.602 118.048 1.00 31.27  ? 1590 LEU A CA    1 
ATOM   1400  C  C     . LEU A 1 373  ? 135.322 182.067 117.456 1.00 34.41  ? 1590 LEU A C     1 
ATOM   1401  O  O     . LEU A 1 373  ? 134.308 182.110 118.157 1.00 35.98  ? 1590 LEU A O     1 
ATOM   1402  C  CB    . LEU A 1 373  ? 136.616 180.098 118.322 1.00 25.14  ? 1590 LEU A CB    1 
ATOM   1403  C  CG    . LEU A 1 373  ? 135.984 179.229 117.234 1.00 26.17  ? 1590 LEU A CG    1 
ATOM   1404  C  CD1   . LEU A 1 373  ? 136.926 179.093 116.054 1.00 27.07  ? 1590 LEU A CD1   1 
ATOM   1405  C  CD2   . LEU A 1 373  ? 135.619 177.862 117.778 1.00 23.74  ? 1590 LEU A CD2   1 
ATOM   1406  N  N     . ASN A 1 374  ? 135.337 182.430 116.177 1.00 34.03  ? 1591 ASN A N     1 
ATOM   1407  C  CA    . ASN A 1 374  ? 134.143 182.919 115.497 1.00 35.32  ? 1591 ASN A CA    1 
ATOM   1408  C  C     . ASN A 1 374  ? 133.508 181.769 114.726 1.00 39.60  ? 1591 ASN A C     1 
ATOM   1409  O  O     . ASN A 1 374  ? 134.051 181.316 113.713 1.00 42.08  ? 1591 ASN A O     1 
ATOM   1410  C  CB    . ASN A 1 374  ? 134.488 184.082 114.570 1.00 34.68  ? 1591 ASN A CB    1 
ATOM   1411  C  CG    . ASN A 1 374  ? 135.164 185.227 115.298 1.00 37.70  ? 1591 ASN A CG    1 
ATOM   1412  O  OD1   . ASN A 1 374  ? 134.571 185.858 116.173 1.00 35.46  ? 1591 ASN A OD1   1 
ATOM   1413  N  ND2   . ASN A 1 374  ? 136.412 185.502 114.938 1.00 43.61  ? 1591 ASN A ND2   1 
ATOM   1414  N  N     . LEU A 1 375  ? 132.360 181.298 115.207 1.00 39.77  ? 1592 LEU A N     1 
ATOM   1415  C  CA    . LEU A 1 375  ? 131.629 180.239 114.530 1.00 38.90  ? 1592 LEU A CA    1 
ATOM   1416  C  C     . LEU A 1 375  ? 131.087 180.734 113.191 1.00 42.77  ? 1592 LEU A C     1 
ATOM   1417  O  O     . LEU A 1 375  ? 130.849 181.928 112.989 1.00 43.19  ? 1592 LEU A O     1 
ATOM   1418  C  CB    . LEU A 1 375  ? 130.488 179.726 115.408 1.00 35.71  ? 1592 LEU A CB    1 
ATOM   1419  C  CG    . LEU A 1 375  ? 130.725 178.402 116.134 1.00 29.22  ? 1592 LEU A CG    1 
ATOM   1420  C  CD1   . LEU A 1 375  ? 131.934 178.488 117.037 1.00 30.76  ? 1592 LEU A CD1   1 
ATOM   1421  C  CD2   . LEU A 1 375  ? 129.497 178.010 116.932 1.00 35.69  ? 1592 LEU A CD2   1 
ATOM   1422  N  N     . ASN A 1 376  ? 130.914 179.788 112.261 1.00 41.52  ? 1593 ASN A N     1 
ATOM   1423  C  CA    . ASN A 1 376  ? 130.470 180.134 110.913 1.00 45.04  ? 1593 ASN A CA    1 
ATOM   1424  C  C     . ASN A 1 376  ? 129.078 180.749 110.925 1.00 45.53  ? 1593 ASN A C     1 
ATOM   1425  O  O     . ASN A 1 376  ? 128.827 181.751 110.246 1.00 44.04  ? 1593 ASN A O     1 
ATOM   1426  C  CB    . ASN A 1 376  ? 130.489 178.895 110.022 1.00 46.01  ? 1593 ASN A CB    1 
ATOM   1427  C  CG    . ASN A 1 376  ? 131.827 178.677 109.358 1.00 40.30  ? 1593 ASN A CG    1 
ATOM   1428  O  OD1   . ASN A 1 376  ? 132.709 179.534 109.411 1.00 39.21  ? 1593 ASN A OD1   1 
ATOM   1429  N  ND2   . ASN A 1 376  ? 131.984 177.526 108.718 1.00 35.03  ? 1593 ASN A ND2   1 
ATOM   1430  N  N     . GLU A 1 377  ? 128.161 180.164 111.690 1.00 48.16  ? 1594 GLU A N     1 
ATOM   1431  C  CA    . GLU A 1 377  ? 126.824 180.709 111.843 1.00 51.08  ? 1594 GLU A CA    1 
ATOM   1432  C  C     . GLU A 1 377  ? 126.431 180.626 113.309 1.00 52.56  ? 1594 GLU A C     1 
ATOM   1433  O  O     . GLU A 1 377  ? 126.963 179.816 114.071 1.00 51.01  ? 1594 GLU A O     1 
ATOM   1434  C  CB    . GLU A 1 377  ? 125.798 179.972 110.966 1.00 50.64  ? 1594 GLU A CB    1 
ATOM   1435  C  CG    . GLU A 1 377  ? 125.213 178.702 111.579 1.00 52.91  ? 1594 GLU A CG    1 
ATOM   1436  C  CD    . GLU A 1 377  ? 126.093 177.477 111.391 1.00 51.60  ? 1594 GLU A CD    1 
ATOM   1437  O  OE1   . GLU A 1 377  ? 127.325 177.581 111.557 1.00 49.97  ? 1594 GLU A OE1   1 
ATOM   1438  O  OE2   . GLU A 1 377  ? 125.544 176.401 111.075 1.00 51.46  ? 1594 GLU A OE2   1 
ATOM   1439  N  N     . LYS A 1 378  ? 125.505 181.494 113.699 1.00 55.16  ? 1595 LYS A N     1 
ATOM   1440  C  CA    . LYS A 1 378  ? 125.017 181.494 115.068 1.00 57.81  ? 1595 LYS A CA    1 
ATOM   1441  C  C     . LYS A 1 378  ? 124.251 180.210 115.364 1.00 61.38  ? 1595 LYS A C     1 
ATOM   1442  O  O     . LYS A 1 378  ? 123.624 179.619 114.480 1.00 62.68  ? 1595 LYS A O     1 
ATOM   1443  C  CB    . LYS A 1 378  ? 124.147 182.729 115.319 1.00 61.88  ? 1595 LYS A CB    1 
ATOM   1444  C  CG    . LYS A 1 378  ? 122.670 182.576 114.989 1.00 64.21  ? 1595 LYS A CG    1 
ATOM   1445  C  CD    . LYS A 1 378  ? 121.969 183.923 115.005 1.00 66.29  ? 1595 LYS A CD    1 
ATOM   1446  C  CE    . LYS A 1 378  ? 120.559 183.821 114.450 1.00 71.94  ? 1595 LYS A CE    1 
ATOM   1447  N  NZ    . LYS A 1 378  ? 120.548 183.291 113.060 1.00 72.00  ? 1595 LYS A NZ    1 
ATOM   1448  N  N     . ILE A 1 379  ? 124.349 179.750 116.609 1.00 62.42  ? 1596 ILE A N     1 
ATOM   1449  C  CA    . ILE A 1 379  ? 123.626 178.563 117.059 1.00 62.67  ? 1596 ILE A CA    1 
ATOM   1450  C  C     . ILE A 1 379  ? 122.314 179.046 117.668 1.00 70.82  ? 1596 ILE A C     1 
ATOM   1451  O  O     . ILE A 1 379  ? 122.287 179.551 118.791 1.00 72.36  ? 1596 ILE A O     1 
ATOM   1452  C  CB    . ILE A 1 379  ? 124.442 177.737 118.055 1.00 58.53  ? 1596 ILE A CB    1 
ATOM   1453  C  CG1   . ILE A 1 379  ? 125.758 177.285 117.419 1.00 57.89  ? 1596 ILE A CG1   1 
ATOM   1454  C  CG2   . ILE A 1 379  ? 123.641 176.537 118.534 1.00 59.27  ? 1596 ILE A CG2   1 
ATOM   1455  C  CD1   . ILE A 1 379  ? 125.577 176.459 116.170 1.00 57.83  ? 1596 ILE A CD1   1 
ATOM   1456  N  N     . GLU A 1 380  ? 121.223 178.909 116.918 1.00 74.13  ? 1597 GLU A N     1 
ATOM   1457  C  CA    . GLU A 1 380  ? 119.924 179.355 117.398 1.00 74.73  ? 1597 GLU A CA    1 
ATOM   1458  C  C     . GLU A 1 380  ? 119.477 178.510 118.582 1.00 76.30  ? 1597 GLU A C     1 
ATOM   1459  O  O     . GLU A 1 380  ? 119.582 177.281 118.566 1.00 77.09  ? 1597 GLU A O     1 
ATOM   1460  C  CB    . GLU A 1 380  ? 118.888 179.284 116.277 1.00 77.44  ? 1597 GLU A CB    1 
ATOM   1461  C  CG    . GLU A 1 380  ? 117.547 179.987 116.545 1.00 80.75  ? 1597 GLU A CG    1 
ATOM   1462  C  CD    . GLU A 1 380  ? 117.678 181.415 117.064 1.00 80.84  ? 1597 GLU A CD    1 
ATOM   1463  O  OE1   . GLU A 1 380  ? 117.457 182.350 116.267 1.00 79.51  ? 1597 GLU A OE1   1 
ATOM   1464  O  OE2   . GLU A 1 380  ? 117.939 181.613 118.271 1.00 80.33  ? 1597 GLU A OE2   1 
ATOM   1465  N  N     . LEU A 1 381  ? 118.981 179.178 119.619 1.00 79.14  ? 1598 LEU A N     1 
ATOM   1466  C  CA    . LEU A 1 381  ? 118.579 178.514 120.847 1.00 79.15  ? 1598 LEU A CA    1 
ATOM   1467  C  C     . LEU A 1 381  ? 117.169 178.935 121.227 1.00 82.31  ? 1598 LEU A C     1 
ATOM   1468  O  O     . LEU A 1 381  ? 116.794 180.105 121.104 1.00 82.97  ? 1598 LEU A O     1 
ATOM   1469  C  CB    . LEU A 1 381  ? 119.544 178.832 121.992 1.00 74.32  ? 1598 LEU A CB    1 
ATOM   1470  C  CG    . LEU A 1 381  ? 120.690 177.838 122.168 1.00 69.10  ? 1598 LEU A CG    1 
ATOM   1471  C  CD1   . LEU A 1 381  ? 121.545 178.218 123.358 1.00 65.16  ? 1598 LEU A CD1   1 
ATOM   1472  C  CD2   . LEU A 1 381  ? 120.145 176.434 122.329 1.00 68.98  ? 1598 LEU A CD2   1 
ATOM   1473  N  N     . LYS A 1 382  ? 116.388 177.963 121.687 1.00 83.20  ? 1599 LYS A N     1 
ATOM   1474  C  CA    . LYS A 1 382  ? 115.034 178.187 122.168 1.00 90.38  ? 1599 LYS A CA    1 
ATOM   1475  C  C     . LYS A 1 382  ? 114.920 177.612 123.574 1.00 91.93  ? 1599 LYS A C     1 
ATOM   1476  O  O     . LYS A 1 382  ? 115.868 177.034 124.113 1.00 88.28  ? 1599 LYS A O     1 
ATOM   1477  C  CB    . LYS A 1 382  ? 113.985 177.553 121.242 1.00 92.13  ? 1599 LYS A CB    1 
ATOM   1478  C  CG    . LYS A 1 382  ? 113.590 178.383 120.022 1.00 92.88  ? 1599 LYS A CG    1 
ATOM   1479  C  CD    . LYS A 1 382  ? 114.648 178.347 118.931 1.00 90.14  ? 1599 LYS A CD    1 
ATOM   1480  C  CE    . LYS A 1 382  ? 114.724 176.969 118.293 1.00 89.04  ? 1599 LYS A CE    1 
ATOM   1481  N  NZ    . LYS A 1 382  ? 115.706 176.922 117.175 1.00 89.97  ? 1599 LYS A NZ    1 
ATOM   1482  N  N     . ASP A 1 383  ? 113.742 177.782 124.178 1.00 96.84  ? 1600 ASP A N     1 
ATOM   1483  C  CA    . ASP A 1 383  ? 113.483 177.146 125.465 1.00 97.28  ? 1600 ASP A CA    1 
ATOM   1484  C  C     . ASP A 1 383  ? 113.369 175.634 125.324 1.00 93.33  ? 1600 ASP A C     1 
ATOM   1485  O  O     . ASP A 1 383  ? 113.706 174.898 126.259 1.00 89.73  ? 1600 ASP A O     1 
ATOM   1486  C  CB    . ASP A 1 383  ? 112.214 177.723 126.091 1.00 97.50  ? 1600 ASP A CB    1 
ATOM   1487  C  CG    . ASP A 1 383  ? 110.979 177.459 125.254 1.00 96.69  ? 1600 ASP A CG    1 
ATOM   1488  O  OD1   . ASP A 1 383  ? 111.096 177.439 124.010 1.00 96.97  ? 1600 ASP A OD1   1 
ATOM   1489  O  OD2   . ASP A 1 383  ? 109.892 177.268 125.838 1.00 95.31  ? 1600 ASP A OD2   1 
ATOM   1490  N  N     . SER A 1 384  ? 112.902 175.156 124.171 1.00 91.94  ? 1601 SER A N     1 
ATOM   1491  C  CA    . SER A 1 384  ? 112.765 173.722 123.916 1.00 89.53  ? 1601 SER A CA    1 
ATOM   1492  C  C     . SER A 1 384  ? 114.063 173.185 123.313 1.00 86.21  ? 1601 SER A C     1 
ATOM   1493  O  O     . SER A 1 384  ? 114.167 172.880 122.124 1.00 83.68  ? 1601 SER A O     1 
ATOM   1494  C  CB    . SER A 1 384  ? 111.574 173.457 123.005 1.00 92.44  ? 1601 SER A CB    1 
ATOM   1495  O  OG    . SER A 1 384  ? 111.861 173.845 121.672 1.00 94.59  ? 1601 SER A OG    1 
ATOM   1496  N  N     . ILE A 1 385  ? 115.074 173.079 124.173 1.00 87.52  ? 1602 ILE A N     1 
ATOM   1497  C  CA    . ILE A 1 385  ? 116.374 172.552 123.780 1.00 81.40  ? 1602 ILE A CA    1 
ATOM   1498  C  C     . ILE A 1 385  ? 116.901 171.661 124.897 1.00 77.26  ? 1602 ILE A C     1 
ATOM   1499  O  O     . ILE A 1 385  ? 116.589 171.854 126.077 1.00 75.21  ? 1602 ILE A O     1 
ATOM   1500  C  CB    . ILE A 1 385  ? 117.373 173.687 123.435 1.00 76.12  ? 1602 ILE A CB    1 
ATOM   1501  C  CG1   . ILE A 1 385  ? 118.556 173.147 122.626 1.00 62.78  ? 1602 ILE A CG1   1 
ATOM   1502  C  CG2   . ILE A 1 385  ? 117.854 174.406 124.689 1.00 74.47  ? 1602 ILE A CG2   1 
ATOM   1503  C  CD1   . ILE A 1 385  ? 118.155 172.429 121.363 1.00 60.00  ? 1602 ILE A CD1   1 
ATOM   1504  N  N     . GLN A 1 386  ? 117.670 170.650 124.509 1.00 71.47  ? 1603 GLN A N     1 
ATOM   1505  C  CA    . GLN A 1 386  ? 118.369 169.782 125.441 1.00 63.15  ? 1603 GLN A CA    1 
ATOM   1506  C  C     . GLN A 1 386  ? 119.843 170.165 125.470 1.00 57.43  ? 1603 GLN A C     1 
ATOM   1507  O  O     . GLN A 1 386  ? 120.388 170.662 124.482 1.00 56.48  ? 1603 GLN A O     1 
ATOM   1508  C  CB    . GLN A 1 386  ? 118.205 168.314 125.043 1.00 60.62  ? 1603 GLN A CB    1 
ATOM   1509  C  CG    . GLN A 1 386  ? 118.451 167.323 126.165 1.00 63.35  ? 1603 GLN A CG    1 
ATOM   1510  C  CD    . GLN A 1 386  ? 117.738 166.008 125.935 1.00 69.24  ? 1603 GLN A CD    1 
ATOM   1511  O  OE1   . GLN A 1 386  ? 116.948 165.874 125.001 1.00 70.68  ? 1603 GLN A OE1   1 
ATOM   1512  N  NE2   . GLN A 1 386  ? 118.023 165.023 126.777 1.00 70.68  ? 1603 GLN A NE2   1 
ATOM   1513  N  N     . ALA A 1 387  ? 120.480 169.943 126.622 1.00 53.22  ? 1604 ALA A N     1 
ATOM   1514  C  CA    . ALA A 1 387  ? 121.864 170.372 126.801 1.00 48.40  ? 1604 ALA A CA    1 
ATOM   1515  C  C     . ALA A 1 387  ? 122.806 169.622 125.866 1.00 51.49  ? 1604 ALA A C     1 
ATOM   1516  O  O     . ALA A 1 387  ? 123.632 170.233 125.173 1.00 46.53  ? 1604 ALA A O     1 
ATOM   1517  C  CB    . ALA A 1 387  ? 122.285 170.183 128.258 1.00 52.38  ? 1604 ALA A CB    1 
ATOM   1518  N  N     . GLN A 1 388  ? 122.680 168.292 125.817 1.00 54.36  ? 1605 GLN A N     1 
ATOM   1519  C  CA    . GLN A 1 388  ? 123.604 167.494 125.019 1.00 46.10  ? 1605 GLN A CA    1 
ATOM   1520  C  C     . GLN A 1 388  ? 123.407 167.722 123.527 1.00 46.56  ? 1605 GLN A C     1 
ATOM   1521  O  O     . GLN A 1 388  ? 124.369 167.623 122.761 1.00 45.82  ? 1605 GLN A O     1 
ATOM   1522  C  CB    . GLN A 1 388  ? 123.483 166.011 125.408 1.00 42.01  ? 1605 GLN A CB    1 
ATOM   1523  C  CG    . GLN A 1 388  ? 122.083 165.360 125.409 1.00 49.60  ? 1605 GLN A CG    1 
ATOM   1524  C  CD    . GLN A 1 388  ? 121.419 165.203 124.046 1.00 54.18  ? 1605 GLN A CD    1 
ATOM   1525  O  OE1   . GLN A 1 388  ? 122.076 165.205 123.008 1.00 53.63  ? 1605 GLN A OE1   1 
ATOM   1526  N  NE2   . GLN A 1 388  ? 120.101 165.054 124.052 1.00 57.42  ? 1605 GLN A NE2   1 
ATOM   1527  N  N     . GLU A 1 389  ? 122.186 168.054 123.099 1.00 49.49  ? 1606 GLU A N     1 
ATOM   1528  C  CA    . GLU A 1 389  ? 121.943 168.311 121.683 1.00 49.13  ? 1606 GLU A CA    1 
ATOM   1529  C  C     . GLU A 1 389  ? 122.688 169.553 121.210 1.00 47.38  ? 1606 GLU A C     1 
ATOM   1530  O  O     . GLU A 1 389  ? 123.432 169.505 120.220 1.00 49.54  ? 1606 GLU A O     1 
ATOM   1531  C  CB    . GLU A 1 389  ? 120.444 168.453 121.425 1.00 51.74  ? 1606 GLU A CB    1 
ATOM   1532  C  CG    . GLU A 1 389  ? 120.098 168.806 119.990 1.00 53.05  ? 1606 GLU A CG    1 
ATOM   1533  C  CD    . GLU A 1 389  ? 118.607 168.781 119.729 1.00 62.10  ? 1606 GLU A CD    1 
ATOM   1534  O  OE1   . GLU A 1 389  ? 117.834 168.691 120.705 1.00 69.70  ? 1606 GLU A OE1   1 
ATOM   1535  O  OE2   . GLU A 1 389  ? 118.207 168.852 118.548 1.00 59.89  ? 1606 GLU A OE2   1 
ATOM   1536  N  N     . TRP A 1 390  ? 122.525 170.673 121.919 1.00 45.62  ? 1607 TRP A N     1 
ATOM   1537  C  CA    . TRP A 1 390  ? 123.222 171.880 121.500 1.00 44.13  ? 1607 TRP A CA    1 
ATOM   1538  C  C     . TRP A 1 390  ? 124.713 171.801 121.780 1.00 44.56  ? 1607 TRP A C     1 
ATOM   1539  O  O     . TRP A 1 390  ? 125.486 172.465 121.089 1.00 45.18  ? 1607 TRP A O     1 
ATOM   1540  C  CB    . TRP A 1 390  ? 122.611 173.130 122.145 1.00 47.10  ? 1607 TRP A CB    1 
ATOM   1541  C  CG    . TRP A 1 390  ? 122.981 173.398 123.575 1.00 44.96  ? 1607 TRP A CG    1 
ATOM   1542  C  CD1   . TRP A 1 390  ? 122.272 173.039 124.676 1.00 47.32  ? 1607 TRP A CD1   1 
ATOM   1543  C  CD2   . TRP A 1 390  ? 124.128 174.113 124.055 1.00 41.01  ? 1607 TRP A CD2   1 
ATOM   1544  N  NE1   . TRP A 1 390  ? 122.908 173.466 125.815 1.00 46.85  ? 1607 TRP A NE1   1 
ATOM   1545  C  CE2   . TRP A 1 390  ? 124.051 174.129 125.460 1.00 42.26  ? 1607 TRP A CE2   1 
ATOM   1546  C  CE3   . TRP A 1 390  ? 125.218 174.728 123.435 1.00 38.80  ? 1607 TRP A CE3   1 
ATOM   1547  C  CZ2   . TRP A 1 390  ? 125.017 174.737 126.254 1.00 41.56  ? 1607 TRP A CZ2   1 
ATOM   1548  C  CZ3   . TRP A 1 390  ? 126.177 175.332 124.227 1.00 39.37  ? 1607 TRP A CZ3   1 
ATOM   1549  C  CH2   . TRP A 1 390  ? 126.070 175.333 125.620 1.00 40.46  ? 1607 TRP A CH2   1 
ATOM   1550  N  N     . LEU A 1 391  ? 125.145 170.975 122.736 1.00 43.65  ? 1608 LEU A N     1 
ATOM   1551  C  CA    . LEU A 1 391  ? 126.581 170.763 122.901 1.00 39.31  ? 1608 LEU A CA    1 
ATOM   1552  C  C     . LEU A 1 391  ? 127.166 169.937 121.758 1.00 39.05  ? 1608 LEU A C     1 
ATOM   1553  O  O     . LEU A 1 391  ? 128.295 170.191 121.326 1.00 38.62  ? 1608 LEU A O     1 
ATOM   1554  C  CB    . LEU A 1 391  ? 126.864 170.132 124.260 1.00 34.37  ? 1608 LEU A CB    1 
ATOM   1555  C  CG    . LEU A 1 391  ? 126.752 171.201 125.347 1.00 35.83  ? 1608 LEU A CG    1 
ATOM   1556  C  CD1   . LEU A 1 391  ? 126.817 170.621 126.737 1.00 36.01  ? 1608 LEU A CD1   1 
ATOM   1557  C  CD2   . LEU A 1 391  ? 127.868 172.213 125.148 1.00 35.79  ? 1608 LEU A CD2   1 
ATOM   1558  N  N     . ASN A 1 392  ? 126.419 168.951 121.248 1.00 39.91  ? 1609 ASN A N     1 
ATOM   1559  C  CA    . ASN A 1 392  ? 126.857 168.228 120.056 1.00 36.54  ? 1609 ASN A CA    1 
ATOM   1560  C  C     . ASN A 1 392  ? 126.949 169.158 118.853 1.00 37.18  ? 1609 ASN A C     1 
ATOM   1561  O  O     . ASN A 1 392  ? 127.930 169.114 118.094 1.00 40.65  ? 1609 ASN A O     1 
ATOM   1562  C  CB    . ASN A 1 392  ? 125.900 167.075 119.754 1.00 36.34  ? 1609 ASN A CB    1 
ATOM   1563  C  CG    . ASN A 1 392  ? 126.241 165.814 120.517 1.00 39.40  ? 1609 ASN A CG    1 
ATOM   1564  O  OD1   . ASN A 1 392  ? 127.262 165.177 120.260 1.00 43.75  ? 1609 ASN A OD1   1 
ATOM   1565  N  ND2   . ASN A 1 392  ? 125.378 165.435 121.449 1.00 41.59  ? 1609 ASN A ND2   1 
ATOM   1566  N  N     . ILE A 1 393  ? 125.932 170.006 118.666 1.00 38.88  ? 1610 ILE A N     1 
ATOM   1567  C  CA    . ILE A 1 393  ? 125.972 170.986 117.581 1.00 39.10  ? 1610 ILE A CA    1 
ATOM   1568  C  C     . ILE A 1 393  ? 127.150 171.934 117.760 1.00 38.21  ? 1610 ILE A C     1 
ATOM   1569  O  O     . ILE A 1 393  ? 127.854 172.253 116.798 1.00 37.42  ? 1610 ILE A O     1 
ATOM   1570  C  CB    . ILE A 1 393  ? 124.640 171.755 117.479 1.00 43.26  ? 1610 ILE A CB    1 
ATOM   1571  C  CG1   . ILE A 1 393  ? 123.461 170.793 117.326 1.00 43.34  ? 1610 ILE A CG1   1 
ATOM   1572  C  CG2   . ILE A 1 393  ? 124.673 172.729 116.313 1.00 44.30  ? 1610 ILE A CG2   1 
ATOM   1573  C  CD1   . ILE A 1 393  ? 122.113 171.484 117.310 1.00 40.97  ? 1610 ILE A CD1   1 
ATOM   1574  N  N     . LEU A 1 394  ? 127.396 172.382 118.996 1.00 36.86  ? 1611 LEU A N     1 
ATOM   1575  C  CA    . LEU A 1 394  ? 128.504 173.292 119.264 1.00 35.95  ? 1611 LEU A CA    1 
ATOM   1576  C  C     . LEU A 1 394  ? 129.850 172.641 118.978 1.00 37.43  ? 1611 LEU A C     1 
ATOM   1577  O  O     . LEU A 1 394  ? 130.736 173.276 118.404 1.00 34.64  ? 1611 LEU A O     1 
ATOM   1578  C  CB    . LEU A 1 394  ? 128.444 173.775 120.713 1.00 34.02  ? 1611 LEU A CB    1 
ATOM   1579  C  CG    . LEU A 1 394  ? 129.735 174.355 121.295 1.00 31.74  ? 1611 LEU A CG    1 
ATOM   1580  C  CD1   . LEU A 1 394  ? 130.030 175.728 120.712 1.00 29.26  ? 1611 LEU A CD1   1 
ATOM   1581  C  CD2   . LEU A 1 394  ? 129.658 174.420 122.805 1.00 34.24  ? 1611 LEU A CD2   1 
ATOM   1582  N  N     . ASP A 1 395  ? 130.023 171.376 119.366 1.00 35.92  ? 1612 ASP A N     1 
ATOM   1583  C  CA    . ASP A 1 395  ? 131.302 170.702 119.157 1.00 28.09  ? 1612 ASP A CA    1 
ATOM   1584  C  C     . ASP A 1 395  ? 131.569 170.472 117.674 1.00 29.79  ? 1612 ASP A C     1 
ATOM   1585  O  O     . ASP A 1 395  ? 132.669 170.759 117.173 1.00 34.13  ? 1612 ASP A O     1 
ATOM   1586  C  CB    . ASP A 1 395  ? 131.319 169.381 119.923 1.00 25.66  ? 1612 ASP A CB    1 
ATOM   1587  C  CG    . ASP A 1 395  ? 132.671 168.705 119.892 1.00 31.93  ? 1612 ASP A CG    1 
ATOM   1588  O  OD1   . ASP A 1 395  ? 133.677 169.386 119.601 1.00 29.29  ? 1612 ASP A OD1   1 
ATOM   1589  O  OD2   . ASP A 1 395  ? 132.729 167.488 120.163 1.00 39.64  ? 1612 ASP A OD2   1 
ATOM   1590  N  N     . THR A 1 396  ? 130.567 169.965 116.948 1.00 33.03  ? 1613 THR A N     1 
ATOM   1591  C  CA    . THR A 1 396  ? 130.749 169.758 115.516 1.00 32.82  ? 1613 THR A CA    1 
ATOM   1592  C  C     . THR A 1 396  ? 130.929 171.086 114.791 1.00 33.95  ? 1613 THR A C     1 
ATOM   1593  O  O     . THR A 1 396  ? 131.713 171.180 113.841 1.00 33.74  ? 1613 THR A O     1 
ATOM   1594  C  CB    . THR A 1 396  ? 129.572 168.978 114.938 1.00 34.98  ? 1613 THR A CB    1 
ATOM   1595  O  OG1   . THR A 1 396  ? 129.284 167.858 115.783 1.00 37.31  ? 1613 THR A OG1   1 
ATOM   1596  C  CG2   . THR A 1 396  ? 129.909 168.469 113.546 1.00 32.27  ? 1613 THR A CG2   1 
ATOM   1597  N  N     . GLU A 1 397  ? 130.249 172.139 115.253 1.00 32.02  ? 1614 GLU A N     1 
ATOM   1598  C  CA    . GLU A 1 397  ? 130.423 173.449 114.643 1.00 32.34  ? 1614 GLU A CA    1 
ATOM   1599  C  C     . GLU A 1 397  ? 131.777 174.053 114.980 1.00 29.62  ? 1614 GLU A C     1 
ATOM   1600  O  O     . GLU A 1 397  ? 132.322 174.808 114.177 1.00 30.43  ? 1614 GLU A O     1 
ATOM   1601  C  CB    . GLU A 1 397  ? 129.298 174.387 115.074 1.00 36.10  ? 1614 GLU A CB    1 
ATOM   1602  C  CG    . GLU A 1 397  ? 129.104 175.566 114.140 1.00 39.86  ? 1614 GLU A CG    1 
ATOM   1603  C  CD    . GLU A 1 397  ? 128.890 175.142 112.701 1.00 41.75  ? 1614 GLU A CD    1 
ATOM   1604  O  OE1   . GLU A 1 397  ? 128.092 174.211 112.464 1.00 43.02  ? 1614 GLU A OE1   1 
ATOM   1605  O  OE2   . GLU A 1 397  ? 129.527 175.734 111.805 1.00 41.15  ? 1614 GLU A OE2   1 
ATOM   1606  N  N     . ILE A 1 398  ? 132.337 173.732 116.147 1.00 25.65  ? 1615 ILE A N     1 
ATOM   1607  C  CA    . ILE A 1 398  ? 133.692 174.169 116.471 1.00 26.52  ? 1615 ILE A CA    1 
ATOM   1608  C  C     . ILE A 1 398  ? 134.687 173.523 115.518 1.00 26.68  ? 1615 ILE A C     1 
ATOM   1609  O  O     . ILE A 1 398  ? 135.582 174.187 114.979 1.00 27.98  ? 1615 ILE A O     1 
ATOM   1610  C  CB    . ILE A 1 398  ? 134.024 173.850 117.941 1.00 24.86  ? 1615 ILE A CB    1 
ATOM   1611  C  CG1   . ILE A 1 398  ? 133.467 174.929 118.865 1.00 27.71  ? 1615 ILE A CG1   1 
ATOM   1612  C  CG2   . ILE A 1 398  ? 135.521 173.730 118.154 1.00 20.93  ? 1615 ILE A CG2   1 
ATOM   1613  C  CD1   . ILE A 1 398  ? 133.665 174.622 120.326 1.00 29.30  ? 1615 ILE A CD1   1 
ATOM   1614  N  N     . LYS A 1 399  ? 134.529 172.217 115.281 1.00 24.50  ? 1616 LYS A N     1 
ATOM   1615  C  CA    . LYS A 1 399  ? 135.416 171.534 114.341 1.00 21.48  ? 1616 LYS A CA    1 
ATOM   1616  C  C     . LYS A 1 399  ? 135.271 172.093 112.927 1.00 24.34  ? 1616 LYS A C     1 
ATOM   1617  O  O     . LYS A 1 399  ? 136.273 172.378 112.256 1.00 24.45  ? 1616 LYS A O     1 
ATOM   1618  C  CB    . LYS A 1 399  ? 135.146 170.031 114.359 1.00 22.53  ? 1616 LYS A CB    1 
ATOM   1619  C  CG    . LYS A 1 399  ? 135.622 169.338 115.622 1.00 18.58  ? 1616 LYS A CG    1 
ATOM   1620  C  CD    . LYS A 1 399  ? 135.353 167.845 115.575 1.00 14.52  ? 1616 LYS A CD    1 
ATOM   1621  C  CE    . LYS A 1 399  ? 135.802 167.172 116.858 1.00 14.53  ? 1616 LYS A CE    1 
ATOM   1622  N  NZ    . LYS A 1 399  ? 135.910 168.146 117.979 1.00 14.24  ? 1616 LYS A NZ    1 
ATOM   1623  N  N     . LEU A 1 400  ? 134.029 172.290 112.471 1.00 27.26  ? 1617 LEU A N     1 
ATOM   1624  C  CA    . LEU A 1 400  ? 133.807 172.848 111.139 1.00 27.35  ? 1617 LEU A CA    1 
ATOM   1625  C  C     . LEU A 1 400  ? 134.273 174.295 111.033 1.00 27.58  ? 1617 LEU A C     1 
ATOM   1626  O  O     . LEU A 1 400  ? 134.729 174.711 109.967 1.00 29.18  ? 1617 LEU A O     1 
ATOM   1627  C  CB    . LEU A 1 400  ? 132.333 172.739 110.744 1.00 26.74  ? 1617 LEU A CB    1 
ATOM   1628  C  CG    . LEU A 1 400  ? 131.828 171.473 110.039 1.00 26.09  ? 1617 LEU A CG    1 
ATOM   1629  C  CD1   . LEU A 1 400  ? 132.500 171.347 108.682 1.00 28.58  ? 1617 LEU A CD1   1 
ATOM   1630  C  CD2   . LEU A 1 400  ? 132.031 170.202 110.842 1.00 26.22  ? 1617 LEU A CD2   1 
ATOM   1631  N  N     . SER A 1 401  ? 134.193 175.071 112.116 1.00 24.56  ? 1618 SER A N     1 
ATOM   1632  C  CA    . SER A 1 401  ? 134.634 176.459 112.065 1.00 24.06  ? 1618 SER A CA    1 
ATOM   1633  C  C     . SER A 1 401  ? 136.151 176.553 112.039 1.00 25.27  ? 1618 SER A C     1 
ATOM   1634  O  O     . SER A 1 401  ? 136.710 177.406 111.342 1.00 27.12  ? 1618 SER A O     1 
ATOM   1635  C  CB    . SER A 1 401  ? 134.076 177.230 113.256 1.00 24.60  ? 1618 SER A CB    1 
ATOM   1636  O  OG    . SER A 1 401  ? 134.910 177.066 114.386 1.00 24.90  ? 1618 SER A OG    1 
ATOM   1637  N  N     . VAL A 1 402  ? 136.833 175.688 112.794 1.00 26.95  ? 1619 VAL A N     1 
ATOM   1638  C  CA    . VAL A 1 402  ? 138.290 175.625 112.706 1.00 22.09  ? 1619 VAL A CA    1 
ATOM   1639  C  C     . VAL A 1 402  ? 138.711 175.211 111.303 1.00 22.11  ? 1619 VAL A C     1 
ATOM   1640  O  O     . VAL A 1 402  ? 139.641 175.789 110.722 1.00 22.39  ? 1619 VAL A O     1 
ATOM   1641  C  CB    . VAL A 1 402  ? 138.854 174.675 113.780 1.00 18.00  ? 1619 VAL A CB    1 
ATOM   1642  C  CG1   . VAL A 1 402  ? 140.324 174.401 113.529 1.00 16.20  ? 1619 VAL A CG1   1 
ATOM   1643  C  CG2   . VAL A 1 402  ? 138.666 175.269 115.162 1.00 15.93  ? 1619 VAL A CG2   1 
ATOM   1644  N  N     . PHE A 1 403  ? 138.010 174.231 110.719 1.00 24.37  ? 1620 PHE A N     1 
ATOM   1645  C  CA    . PHE A 1 403  ? 138.311 173.838 109.346 1.00 24.38  ? 1620 PHE A CA    1 
ATOM   1646  C  C     . PHE A 1 403  ? 138.056 174.977 108.366 1.00 28.79  ? 1620 PHE A C     1 
ATOM   1647  O  O     . PHE A 1 403  ? 138.821 175.165 107.416 1.00 32.01  ? 1620 PHE A O     1 
ATOM   1648  C  CB    . PHE A 1 403  ? 137.491 172.618 108.933 1.00 21.23  ? 1620 PHE A CB    1 
ATOM   1649  C  CG    . PHE A 1 403  ? 137.535 172.352 107.457 1.00 22.15  ? 1620 PHE A CG    1 
ATOM   1650  C  CD1   . PHE A 1 403  ? 138.658 171.791 106.881 1.00 20.75  ? 1620 PHE A CD1   1 
ATOM   1651  C  CD2   . PHE A 1 403  ? 136.471 172.696 106.641 1.00 27.69  ? 1620 PHE A CD2   1 
ATOM   1652  C  CE1   . PHE A 1 403  ? 138.714 171.558 105.525 1.00 22.50  ? 1620 PHE A CE1   1 
ATOM   1653  C  CE2   . PHE A 1 403  ? 136.526 172.475 105.284 1.00 29.13  ? 1620 PHE A CE2   1 
ATOM   1654  C  CZ    . PHE A 1 403  ? 137.646 171.899 104.726 1.00 27.65  ? 1620 PHE A CZ    1 
ATOM   1655  N  N     . THR A 1 404  ? 136.964 175.720 108.555 1.00 28.23  ? 1621 THR A N     1 
ATOM   1656  C  CA    . THR A 1 404  ? 136.623 176.801 107.637 1.00 28.86  ? 1621 THR A CA    1 
ATOM   1657  C  C     . THR A 1 404  ? 137.637 177.933 107.718 1.00 29.63  ? 1621 THR A C     1 
ATOM   1658  O  O     . THR A 1 404  ? 138.037 178.491 106.689 1.00 32.99  ? 1621 THR A O     1 
ATOM   1659  C  CB    . THR A 1 404  ? 135.215 177.309 107.942 1.00 28.54  ? 1621 THR A CB    1 
ATOM   1660  O  OG1   . THR A 1 404  ? 134.267 176.269 107.671 1.00 31.09  ? 1621 THR A OG1   1 
ATOM   1661  C  CG2   . THR A 1 404  ? 134.873 178.520 107.090 1.00 29.02  ? 1621 THR A CG2   1 
ATOM   1662  N  N     . GLN A 1 405  ? 138.070 178.280 108.932 1.00 27.23  ? 1622 GLN A N     1 
ATOM   1663  C  CA    . GLN A 1 405  ? 139.120 179.280 109.080 1.00 28.79  ? 1622 GLN A CA    1 
ATOM   1664  C  C     . GLN A 1 405  ? 140.422 178.802 108.453 1.00 32.27  ? 1622 GLN A C     1 
ATOM   1665  O  O     . GLN A 1 405  ? 141.128 179.585 107.807 1.00 37.39  ? 1622 GLN A O     1 
ATOM   1666  C  CB    . GLN A 1 405  ? 139.321 179.625 110.554 1.00 25.58  ? 1622 GLN A CB    1 
ATOM   1667  C  CG    . GLN A 1 405  ? 138.132 180.319 111.186 1.00 29.23  ? 1622 GLN A CG    1 
ATOM   1668  C  CD    . GLN A 1 405  ? 138.539 181.450 112.102 1.00 34.10  ? 1622 GLN A CD    1 
ATOM   1669  O  OE1   . GLN A 1 405  ? 139.619 181.430 112.687 1.00 35.41  ? 1622 GLN A OE1   1 
ATOM   1670  N  NE2   . GLN A 1 405  ? 137.672 182.445 112.235 1.00 33.95  ? 1622 GLN A NE2   1 
ATOM   1671  N  N     . PHE A 1 406  ? 140.746 177.513 108.612 1.00 31.32  ? 1623 PHE A N     1 
ATOM   1672  C  CA    . PHE A 1 406  ? 141.934 176.972 107.958 1.00 28.72  ? 1623 PHE A CA    1 
ATOM   1673  C  C     . PHE A 1 406  ? 141.818 177.056 106.442 1.00 29.33  ? 1623 PHE A C     1 
ATOM   1674  O  O     . PHE A 1 406  ? 142.779 177.428 105.766 1.00 33.41  ? 1623 PHE A O     1 
ATOM   1675  C  CB    . PHE A 1 406  ? 142.171 175.525 108.392 1.00 24.86  ? 1623 PHE A CB    1 
ATOM   1676  C  CG    . PHE A 1 406  ? 142.887 174.691 107.362 1.00 24.05  ? 1623 PHE A CG    1 
ATOM   1677  C  CD1   . PHE A 1 406  ? 144.216 174.931 107.047 1.00 22.79  ? 1623 PHE A CD1   1 
ATOM   1678  C  CD2   . PHE A 1 406  ? 142.228 173.665 106.710 1.00 27.78  ? 1623 PHE A CD2   1 
ATOM   1679  C  CE1   . PHE A 1 406  ? 144.863 174.171 106.096 1.00 22.16  ? 1623 PHE A CE1   1 
ATOM   1680  C  CE2   . PHE A 1 406  ? 142.876 172.899 105.764 1.00 27.87  ? 1623 PHE A CE2   1 
ATOM   1681  C  CZ    . PHE A 1 406  ? 144.194 173.151 105.459 1.00 26.34  ? 1623 PHE A CZ    1 
ATOM   1682  N  N     . ARG A 1 407  ? 140.654 176.709 105.893 1.00 29.77  ? 1624 ARG A N     1 
ATOM   1683  C  CA    . ARG A 1 407  ? 140.475 176.735 104.444 1.00 36.57  ? 1624 ARG A CA    1 
ATOM   1684  C  C     . ARG A 1 407  ? 140.564 178.154 103.900 1.00 39.22  ? 1624 ARG A C     1 
ATOM   1685  O  O     . ARG A 1 407  ? 141.210 178.390 102.871 1.00 39.87  ? 1624 ARG A O     1 
ATOM   1686  C  CB    . ARG A 1 407  ? 139.136 176.101 104.070 1.00 35.41  ? 1624 ARG A CB    1 
ATOM   1687  C  CG    . ARG A 1 407  ? 138.873 176.056 102.575 1.00 35.69  ? 1624 ARG A CG    1 
ATOM   1688  C  CD    . ARG A 1 407  ? 137.410 175.777 102.276 1.00 37.39  ? 1624 ARG A CD    1 
ATOM   1689  N  NE    . ARG A 1 407  ? 136.567 176.936 102.541 1.00 37.97  ? 1624 ARG A NE    1 
ATOM   1690  C  CZ    . ARG A 1 407  ? 135.383 176.880 103.135 1.00 37.38  ? 1624 ARG A CZ    1 
ATOM   1691  N  NH1   . ARG A 1 407  ? 134.869 175.732 103.544 1.00 35.06  ? 1624 ARG A NH1   1 
ATOM   1692  N  NH2   . ARG A 1 407  ? 134.697 178.003 103.322 1.00 38.60  ? 1624 ARG A NH2   1 
ATOM   1693  N  N     . ASP A 1 408  ? 139.931 179.111 104.585 1.00 37.09  ? 1625 ASP A N     1 
ATOM   1694  C  CA    . ASP A 1 408  ? 139.995 180.505 104.158 1.00 36.73  ? 1625 ASP A CA    1 
ATOM   1695  C  C     . ASP A 1 408  ? 141.418 181.041 104.233 1.00 39.40  ? 1625 ASP A C     1 
ATOM   1696  O  O     . ASP A 1 408  ? 141.887 181.705 103.300 1.00 41.37  ? 1625 ASP A O     1 
ATOM   1697  C  CB    . ASP A 1 408  ? 139.056 181.356 105.010 1.00 34.11  ? 1625 ASP A CB    1 
ATOM   1698  C  CG    . ASP A 1 408  ? 137.600 181.137 104.663 1.00 39.05  ? 1625 ASP A CG    1 
ATOM   1699  O  OD1   . ASP A 1 408  ? 137.298 180.142 103.973 1.00 41.95  ? 1625 ASP A OD1   1 
ATOM   1700  O  OD2   . ASP A 1 408  ? 136.756 181.957 105.081 1.00 35.93  ? 1625 ASP A OD2   1 
ATOM   1701  N  N     . CYS A 1 409  ? 142.130 180.745 105.326 1.00 39.02  ? 1626 CYS A N     1 
ATOM   1702  C  CA    . CYS A 1 409  ? 143.507 181.204 105.460 1.00 38.49  ? 1626 CYS A CA    1 
ATOM   1703  C  C     . CYS A 1 409  ? 144.412 180.550 104.424 1.00 35.49  ? 1626 CYS A C     1 
ATOM   1704  O  O     . CYS A 1 409  ? 145.305 181.203 103.876 1.00 35.86  ? 1626 CYS A O     1 
ATOM   1705  C  CB    . CYS A 1 409  ? 144.016 180.923 106.873 1.00 36.11  ? 1626 CYS A CB    1 
ATOM   1706  S  SG    . CYS A 1 409  ? 145.602 181.689 107.259 1.00 45.84  ? 1626 CYS A SG    1 
ATOM   1707  N  N     . LEU A 1 410  ? 144.193 179.266 104.136 1.00 34.62  ? 1627 LEU A N     1 
ATOM   1708  C  CA    . LEU A 1 410  ? 145.011 178.570 103.152 1.00 37.59  ? 1627 LEU A CA    1 
ATOM   1709  C  C     . LEU A 1 410  ? 144.781 179.122 101.754 1.00 37.92  ? 1627 LEU A C     1 
ATOM   1710  O  O     . LEU A 1 410  ? 145.737 179.328 101.001 1.00 42.99  ? 1627 LEU A O     1 
ATOM   1711  C  CB    . LEU A 1 410  ? 144.717 177.072 103.198 1.00 36.84  ? 1627 LEU A CB    1 
ATOM   1712  C  CG    . LEU A 1 410  ? 145.377 176.199 102.133 1.00 35.70  ? 1627 LEU A CG    1 
ATOM   1713  C  CD1   . LEU A 1 410  ? 146.890 176.302 102.215 1.00 30.44  ? 1627 LEU A CD1   1 
ATOM   1714  C  CD2   . LEU A 1 410  ? 144.928 174.760 102.293 1.00 35.53  ? 1627 LEU A CD2   1 
ATOM   1715  N  N     . GLY A 1 411  ? 143.522 179.384 101.393 1.00 36.43  ? 1628 GLY A N     1 
ATOM   1716  C  CA    . GLY A 1 411  ? 143.250 179.998 100.104 1.00 42.23  ? 1628 GLY A CA    1 
ATOM   1717  C  C     . GLY A 1 411  ? 143.821 181.399 99.997  1.00 47.37  ? 1628 GLY A C     1 
ATOM   1718  O  O     . GLY A 1 411  ? 144.374 181.779 98.959  1.00 49.00  ? 1628 GLY A O     1 
ATOM   1719  N  N     . GLN A 1 412  ? 143.709 182.180 101.075 1.00 46.42  ? 1629 GLN A N     1 
ATOM   1720  C  CA    . GLN A 1 412  ? 144.250 183.534 101.076 1.00 43.40  ? 1629 GLN A CA    1 
ATOM   1721  C  C     . GLN A 1 412  ? 145.768 183.524 100.939 1.00 42.83  ? 1629 GLN A C     1 
ATOM   1722  O  O     . GLN A 1 412  ? 146.335 184.320 100.183 1.00 44.07  ? 1629 GLN A O     1 
ATOM   1723  C  CB    . GLN A 1 412  ? 143.816 184.253 102.353 1.00 39.41  ? 1629 GLN A CB    1 
ATOM   1724  C  CG    . GLN A 1 412  ? 144.126 185.730 102.386 1.00 43.64  ? 1629 GLN A CG    1 
ATOM   1725  C  CD    . GLN A 1 412  ? 143.401 186.444 103.507 1.00 49.96  ? 1629 GLN A CD    1 
ATOM   1726  O  OE1   . GLN A 1 412  ? 142.604 185.843 104.226 1.00 51.32  ? 1629 GLN A OE1   1 
ATOM   1727  N  NE2   . GLN A 1 412  ? 143.675 187.733 103.663 1.00 49.14  ? 1629 GLN A NE2   1 
ATOM   1728  N  N     . LEU A 1 413  ? 146.443 182.612 101.644 1.00 39.69  ? 1630 LEU A N     1 
ATOM   1729  C  CA    . LEU A 1 413  ? 147.892 182.495 101.519 1.00 38.95  ? 1630 LEU A CA    1 
ATOM   1730  C  C     . LEU A 1 413  ? 148.296 181.949 100.155 1.00 40.28  ? 1630 LEU A C     1 
ATOM   1731  O  O     . LEU A 1 413  ? 149.383 182.266 99.661  1.00 41.32  ? 1630 LEU A O     1 
ATOM   1732  C  CB    . LEU A 1 413  ? 148.446 181.607 102.634 1.00 35.23  ? 1630 LEU A CB    1 
ATOM   1733  C  CG    . LEU A 1 413  ? 149.007 182.319 103.867 1.00 29.95  ? 1630 LEU A CG    1 
ATOM   1734  C  CD1   . LEU A 1 413  ? 147.901 182.972 104.670 1.00 28.16  ? 1630 LEU A CD1   1 
ATOM   1735  C  CD2   . LEU A 1 413  ? 149.790 181.352 104.733 1.00 30.78  ? 1630 LEU A CD2   1 
ATOM   1736  N  N     . LYS A 1 414  ? 147.444 181.125 99.539  1.00 42.21  ? 1631 LYS A N     1 
ATOM   1737  C  CA    . LYS A 1 414  ? 147.708 180.667 98.181  1.00 45.70  ? 1631 LYS A CA    1 
ATOM   1738  C  C     . LYS A 1 414  ? 147.558 181.799 97.176  1.00 51.57  ? 1631 LYS A C     1 
ATOM   1739  O  O     . LYS A 1 414  ? 148.219 181.791 96.132  1.00 55.85  ? 1631 LYS A O     1 
ATOM   1740  C  CB    . LYS A 1 414  ? 146.767 179.517 97.820  1.00 42.53  ? 1631 LYS A CB    1 
ATOM   1741  C  CG    . LYS A 1 414  ? 147.229 178.151 98.299  1.00 40.34  ? 1631 LYS A CG    1 
ATOM   1742  C  CD    . LYS A 1 414  ? 148.265 177.553 97.363  1.00 42.65  ? 1631 LYS A CD    1 
ATOM   1743  C  CE    . LYS A 1 414  ? 148.604 176.125 97.759  1.00 39.45  ? 1631 LYS A CE    1 
ATOM   1744  N  NZ    . LYS A 1 414  ? 150.028 175.789 97.483  1.00 33.92  ? 1631 LYS A NZ    1 
ATOM   1745  N  N     . ASP A 1 415  ? 146.705 182.779 97.474  1.00 48.66  ? 1632 ASP A N     1 
ATOM   1746  C  CA    . ASP A 1 415  ? 146.491 183.921 96.593  1.00 48.75  ? 1632 ASP A CA    1 
ATOM   1747  C  C     . ASP A 1 415  ? 147.621 184.948 96.647  1.00 50.42  ? 1632 ASP A C     1 
ATOM   1748  O  O     . ASP A 1 415  ? 147.474 186.032 96.075  1.00 53.46  ? 1632 ASP A O     1 
ATOM   1749  C  CB    . ASP A 1 415  ? 145.164 184.605 96.934  1.00 50.73  ? 1632 ASP A CB    1 
ATOM   1750  C  CG    . ASP A 1 415  ? 143.963 183.748 96.595  1.00 51.47  ? 1632 ASP A CG    1 
ATOM   1751  O  OD1   . ASP A 1 415  ? 144.065 182.917 95.669  1.00 49.08  ? 1632 ASP A OD1   1 
ATOM   1752  O  OD2   . ASP A 1 415  ? 142.917 183.903 97.258  1.00 52.44  ? 1632 ASP A OD2   1 
ATOM   1753  N  N     . GLY A 1 416  ? 148.733 184.642 97.312  1.00 49.66  ? 1633 GLY A N     1 
ATOM   1754  C  CA    . GLY A 1 416  ? 149.841 185.565 97.419  1.00 51.53  ? 1633 GLY A CA    1 
ATOM   1755  C  C     . GLY A 1 416  ? 149.747 186.551 98.562  1.00 51.64  ? 1633 GLY A C     1 
ATOM   1756  O  O     . GLY A 1 416  ? 150.669 187.358 98.737  1.00 49.83  ? 1633 GLY A O     1 
ATOM   1757  N  N     . THR A 1 417  ? 148.667 186.517 99.337  1.00 51.16  ? 1634 THR A N     1 
ATOM   1758  C  CA    . THR A 1 417  ? 148.495 187.447 100.443 1.00 48.76  ? 1634 THR A CA    1 
ATOM   1759  C  C     . THR A 1 417  ? 149.508 187.159 101.545 1.00 46.40  ? 1634 THR A C     1 
ATOM   1760  O  O     . THR A 1 417  ? 149.771 186.002 101.884 1.00 46.28  ? 1634 THR A O     1 
ATOM   1761  C  CB    . THR A 1 417  ? 147.068 187.350 100.986 1.00 48.84  ? 1634 THR A CB    1 
ATOM   1762  O  OG1   . THR A 1 417  ? 146.138 187.621 99.930  1.00 52.73  ? 1634 THR A OG1   1 
ATOM   1763  C  CG2   . THR A 1 417  ? 146.834 188.345 102.104 1.00 48.49  ? 1634 THR A CG2   1 
ATOM   1764  N  N     . ASP A 1 418  ? 150.084 188.224 102.097 1.00 48.18  ? 1635 ASP A N     1 
ATOM   1765  C  CA    . ASP A 1 418  ? 151.109 188.098 103.120 1.00 49.79  ? 1635 ASP A CA    1 
ATOM   1766  C  C     . ASP A 1 418  ? 150.512 187.585 104.430 1.00 44.33  ? 1635 ASP A C     1 
ATOM   1767  O  O     . ASP A 1 418  ? 149.309 187.686 104.681 1.00 42.21  ? 1635 ASP A O     1 
ATOM   1768  C  CB    . ASP A 1 418  ? 151.794 189.445 103.345 1.00 51.51  ? 1635 ASP A CB    1 
ATOM   1769  C  CG    . ASP A 1 418  ? 153.282 189.310 103.560 1.00 49.84  ? 1635 ASP A CG    1 
ATOM   1770  O  OD1   . ASP A 1 418  ? 153.730 188.196 103.895 1.00 48.98  ? 1635 ASP A OD1   1 
ATOM   1771  O  OD2   . ASP A 1 418  ? 154.004 190.315 103.397 1.00 49.30  ? 1635 ASP A OD2   1 
ATOM   1772  N  N     . ILE A 1 419  ? 151.380 187.018 105.270 1.00 43.21  ? 1636 ILE A N     1 
ATOM   1773  C  CA    . ILE A 1 419  ? 150.922 186.497 106.555 1.00 42.52  ? 1636 ILE A CA    1 
ATOM   1774  C  C     . ILE A 1 419  ? 150.722 187.626 107.565 1.00 42.28  ? 1636 ILE A C     1 
ATOM   1775  O  O     . ILE A 1 419  ? 149.888 187.511 108.476 1.00 40.58  ? 1636 ILE A O     1 
ATOM   1776  C  CB    . ILE A 1 419  ? 151.898 185.422 107.075 1.00 43.17  ? 1636 ILE A CB    1 
ATOM   1777  C  CG1   . ILE A 1 419  ? 151.317 184.705 108.297 1.00 35.11  ? 1636 ILE A CG1   1 
ATOM   1778  C  CG2   . ILE A 1 419  ? 153.262 186.018 107.391 1.00 41.79  ? 1636 ILE A CG2   1 
ATOM   1779  C  CD1   . ILE A 1 419  ? 152.014 183.418 108.640 1.00 22.53  ? 1636 ILE A CD1   1 
ATOM   1780  N  N     . GLU A 1 420  ? 151.444 188.740 107.400 1.00 44.15  ? 1637 GLU A N     1 
ATOM   1781  C  CA    . GLU A 1 420  ? 151.411 189.832 108.365 1.00 43.16  ? 1637 GLU A CA    1 
ATOM   1782  C  C     . GLU A 1 420  ? 150.045 190.500 108.458 1.00 44.81  ? 1637 GLU A C     1 
ATOM   1783  O  O     . GLU A 1 420  ? 149.762 191.166 109.458 1.00 48.84  ? 1637 GLU A O     1 
ATOM   1784  C  CB    . GLU A 1 420  ? 152.470 190.875 108.006 1.00 44.18  ? 1637 GLU A CB    1 
ATOM   1785  C  CG    . GLU A 1 420  ? 153.859 190.577 108.551 1.00 46.48  ? 1637 GLU A CG    1 
ATOM   1786  C  CD    . GLU A 1 420  ? 154.765 189.917 107.531 1.00 46.64  ? 1637 GLU A CD    1 
ATOM   1787  O  OE1   . GLU A 1 420  ? 154.285 189.592 106.427 1.00 46.41  ? 1637 GLU A OE1   1 
ATOM   1788  O  OE2   . GLU A 1 420  ? 155.963 189.733 107.829 1.00 40.24  ? 1637 GLU A OE2   1 
ATOM   1789  N  N     . VAL A 1 421  ? 149.192 190.339 107.448 1.00 43.93  ? 1638 VAL A N     1 
ATOM   1790  C  CA    . VAL A 1 421  ? 147.845 190.890 107.504 1.00 43.56  ? 1638 VAL A CA    1 
ATOM   1791  C  C     . VAL A 1 421  ? 146.825 189.861 107.993 1.00 43.16  ? 1638 VAL A C     1 
ATOM   1792  O  O     . VAL A 1 421  ? 145.788 190.251 108.551 1.00 43.21  ? 1638 VAL A O     1 
ATOM   1793  C  CB    . VAL A 1 421  ? 147.443 191.462 106.124 1.00 41.82  ? 1638 VAL A CB    1 
ATOM   1794  C  CG1   . VAL A 1 421  ? 147.343 190.361 105.089 1.00 42.03  ? 1638 VAL A CG1   1 
ATOM   1795  C  CG2   . VAL A 1 421  ? 146.159 192.288 106.201 1.00 45.61  ? 1638 VAL A CG2   1 
ATOM   1796  N  N     . VAL A 1 422  ? 147.109 188.563 107.850 1.00 44.89  ? 1639 VAL A N     1 
ATOM   1797  C  CA    . VAL A 1 422  ? 146.169 187.519 108.239 1.00 43.18  ? 1639 VAL A CA    1 
ATOM   1798  C  C     . VAL A 1 422  ? 146.465 186.976 109.637 1.00 39.04  ? 1639 VAL A C     1 
ATOM   1799  O  O     . VAL A 1 422  ? 145.711 186.134 110.145 1.00 37.68  ? 1639 VAL A O     1 
ATOM   1800  C  CB    . VAL A 1 422  ? 146.166 186.390 107.180 1.00 42.77  ? 1639 VAL A CB    1 
ATOM   1801  C  CG1   . VAL A 1 422  ? 147.482 185.644 107.178 1.00 37.72  ? 1639 VAL A CG1   1 
ATOM   1802  C  CG2   . VAL A 1 422  ? 144.947 185.464 107.280 1.00 39.74  ? 1639 VAL A CG2   1 
ATOM   1803  N  N     . VAL A 1 423  ? 147.536 187.452 110.284 1.00 38.50  ? 1640 VAL A N     1 
ATOM   1804  C  CA    . VAL A 1 423  ? 147.783 187.089 111.683 1.00 33.66  ? 1640 VAL A CA    1 
ATOM   1805  C  C     . VAL A 1 423  ? 146.609 187.503 112.565 1.00 36.92  ? 1640 VAL A C     1 
ATOM   1806  O  O     . VAL A 1 423  ? 146.160 186.737 113.428 1.00 34.87  ? 1640 VAL A O     1 
ATOM   1807  C  CB    . VAL A 1 423  ? 149.104 187.708 112.177 1.00 31.73  ? 1640 VAL A CB    1 
ATOM   1808  C  CG1   . VAL A 1 423  ? 149.213 187.609 113.686 1.00 27.98  ? 1640 VAL A CG1   1 
ATOM   1809  C  CG2   . VAL A 1 423  ? 150.280 186.996 111.561 1.00 34.97  ? 1640 VAL A CG2   1 
ATOM   1810  N  N     . SER A 1 424  ? 146.074 188.700 112.347 1.00 37.62  ? 1641 SER A N     1 
ATOM   1811  C  CA    . SER A 1 424  ? 145.014 189.241 113.185 1.00 33.90  ? 1641 SER A CA    1 
ATOM   1812  C  C     . SER A 1 424  ? 143.616 188.924 112.668 1.00 34.88  ? 1641 SER A C     1 
ATOM   1813  O  O     . SER A 1 424  ? 142.641 189.468 113.193 1.00 42.05  ? 1641 SER A O     1 
ATOM   1814  C  CB    . SER A 1 424  ? 145.175 190.755 113.325 1.00 36.90  ? 1641 SER A CB    1 
ATOM   1815  O  OG    . SER A 1 424  ? 143.977 191.348 113.792 1.00 44.29  ? 1641 SER A OG    1 
ATOM   1816  N  N     . LYS A 1 425  ? 143.491 188.067 111.655 1.00 32.65  ? 1642 LYS A N     1 
ATOM   1817  C  CA    . LYS A 1 425  ? 142.192 187.751 111.069 1.00 34.67  ? 1642 LYS A CA    1 
ATOM   1818  C  C     . LYS A 1 425  ? 141.588 186.475 111.647 1.00 35.97  ? 1642 LYS A C     1 
ATOM   1819  O  O     . LYS A 1 425  ? 140.464 186.493 112.157 1.00 36.99  ? 1642 LYS A O     1 
ATOM   1820  C  CB    . LYS A 1 425  ? 142.317 187.640 109.544 1.00 38.22  ? 1642 LYS A CB    1 
ATOM   1821  C  CG    . LYS A 1 425  ? 142.632 188.952 108.849 1.00 42.79  ? 1642 LYS A CG    1 
ATOM   1822  C  CD    . LYS A 1 425  ? 142.458 188.831 107.346 1.00 45.61  ? 1642 LYS A CD    1 
ATOM   1823  C  CE    . LYS A 1 425  ? 140.994 188.672 106.974 1.00 47.59  ? 1642 LYS A CE    1 
ATOM   1824  N  NZ    . LYS A 1 425  ? 140.805 188.548 105.503 1.00 50.74  ? 1642 LYS A NZ    1 
ATOM   1825  N  N     . TYR A 1 426  ? 142.314 185.364 111.576 1.00 35.98  ? 1643 TYR A N     1 
ATOM   1826  C  CA    . TYR A 1 426  ? 141.826 184.070 112.028 1.00 30.35  ? 1643 TYR A CA    1 
ATOM   1827  C  C     . TYR A 1 426  ? 142.544 183.646 113.303 1.00 29.37  ? 1643 TYR A C     1 
ATOM   1828  O  O     . TYR A 1 426  ? 143.507 184.275 113.747 1.00 32.14  ? 1643 TYR A O     1 
ATOM   1829  C  CB    . TYR A 1 426  ? 142.007 183.007 110.938 1.00 30.38  ? 1643 TYR A CB    1 
ATOM   1830  C  CG    . TYR A 1 426  ? 141.389 183.382 109.613 1.00 35.59  ? 1643 TYR A CG    1 
ATOM   1831  C  CD1   . TYR A 1 426  ? 140.012 183.485 109.472 1.00 37.08  ? 1643 TYR A CD1   1 
ATOM   1832  C  CD2   . TYR A 1 426  ? 142.181 183.627 108.502 1.00 38.39  ? 1643 TYR A CD2   1 
ATOM   1833  C  CE1   . TYR A 1 426  ? 139.443 183.830 108.262 1.00 40.14  ? 1643 TYR A CE1   1 
ATOM   1834  C  CE2   . TYR A 1 426  ? 141.621 183.971 107.288 1.00 40.41  ? 1643 TYR A CE2   1 
ATOM   1835  C  CZ    . TYR A 1 426  ? 140.253 184.070 107.174 1.00 41.95  ? 1643 TYR A CZ    1 
ATOM   1836  O  OH    . TYR A 1 426  ? 139.691 184.413 105.967 1.00 44.13  ? 1643 TYR A OH    1 
ATOM   1837  N  N     . ILE A 1 427  ? 142.058 182.550 113.886 1.00 28.96  ? 1644 ILE A N     1 
ATOM   1838  C  CA    . ILE A 1 427  ? 142.600 182.008 115.127 1.00 22.08  ? 1644 ILE A CA    1 
ATOM   1839  C  C     . ILE A 1 427  ? 143.982 181.425 114.870 1.00 18.42  ? 1644 ILE A C     1 
ATOM   1840  O  O     . ILE A 1 427  ? 144.397 181.275 113.716 1.00 19.20  ? 1644 ILE A O     1 
ATOM   1841  C  CB    . ILE A 1 427  ? 141.658 180.951 115.729 1.00 20.45  ? 1644 ILE A CB    1 
ATOM   1842  C  CG1   . ILE A 1 427  ? 141.493 179.775 114.769 1.00 18.46  ? 1644 ILE A CG1   1 
ATOM   1843  C  CG2   . ILE A 1 427  ? 140.309 181.567 116.042 1.00 24.98  ? 1644 ILE A CG2   1 
ATOM   1844  C  CD1   . ILE A 1 427  ? 140.544 178.717 115.268 1.00 17.31  ? 1644 ILE A CD1   1 
ATOM   1845  N  N     . PHE A 1 428  ? 144.707 181.102 115.945 1.00 16.54  ? 1645 PHE A N     1 
ATOM   1846  C  CA    . PHE A 1 428  ? 146.083 180.635 115.803 1.00 17.29  ? 1645 PHE A CA    1 
ATOM   1847  C  C     . PHE A 1 428  ? 146.161 179.306 115.063 1.00 20.15  ? 1645 PHE A C     1 
ATOM   1848  O  O     . PHE A 1 428  ? 147.078 179.091 114.266 1.00 23.17  ? 1645 PHE A O     1 
ATOM   1849  C  CB    . PHE A 1 428  ? 146.749 180.512 117.173 1.00 16.78  ? 1645 PHE A CB    1 
ATOM   1850  C  CG    . PHE A 1 428  ? 147.955 179.613 117.176 1.00 18.61  ? 1645 PHE A CG    1 
ATOM   1851  C  CD1   . PHE A 1 428  ? 149.089 179.949 116.460 1.00 17.06  ? 1645 PHE A CD1   1 
ATOM   1852  C  CD2   . PHE A 1 428  ? 147.950 178.430 117.891 1.00 21.82  ? 1645 PHE A CD2   1 
ATOM   1853  C  CE1   . PHE A 1 428  ? 150.184 179.117 116.443 1.00 17.12  ? 1645 PHE A CE1   1 
ATOM   1854  C  CE2   . PHE A 1 428  ? 149.050 177.599 117.891 1.00 20.18  ? 1645 PHE A CE2   1 
ATOM   1855  C  CZ    . PHE A 1 428  ? 150.171 177.946 117.170 1.00 20.02  ? 1645 PHE A CZ    1 
ATOM   1856  N  N     . GLN A 1 429  ? 145.220 178.396 115.325 1.00 18.51  ? 1646 GLN A N     1 
ATOM   1857  C  CA    . GLN A 1 429  ? 145.292 177.060 114.737 1.00 13.55  ? 1646 GLN A CA    1 
ATOM   1858  C  C     . GLN A 1 429  ? 145.177 177.107 113.216 1.00 12.58  ? 1646 GLN A C     1 
ATOM   1859  O  O     . GLN A 1 429  ? 145.874 176.368 112.510 1.00 13.90  ? 1646 GLN A O     1 
ATOM   1860  C  CB    . GLN A 1 429  ? 144.201 176.177 115.336 1.00 9.46   ? 1646 GLN A CB    1 
ATOM   1861  C  CG    . GLN A 1 429  ? 144.182 174.762 114.812 1.00 8.73   ? 1646 GLN A CG    1 
ATOM   1862  C  CD    . GLN A 1 429  ? 143.402 173.842 115.713 1.00 9.66   ? 1646 GLN A CD    1 
ATOM   1863  O  OE1   . GLN A 1 429  ? 143.100 174.190 116.851 1.00 10.27  ? 1646 GLN A OE1   1 
ATOM   1864  N  NE2   . GLN A 1 429  ? 143.068 172.661 115.212 1.00 9.91   ? 1646 GLN A NE2   1 
ATOM   1865  N  N     . ALA A 1 430  ? 144.313 177.980 112.695 1.00 11.58  ? 1647 ALA A N     1 
ATOM   1866  C  CA    . ALA A 1 430  ? 144.136 178.085 111.250 1.00 14.69  ? 1647 ALA A CA    1 
ATOM   1867  C  C     . ALA A 1 430  ? 145.395 178.611 110.571 1.00 16.96  ? 1647 ALA A C     1 
ATOM   1868  O  O     . ALA A 1 430  ? 145.835 178.062 109.553 1.00 20.25  ? 1647 ALA A O     1 
ATOM   1869  C  CB    . ALA A 1 430  ? 142.944 178.985 110.938 1.00 20.02  ? 1647 ALA A CB    1 
ATOM   1870  N  N     . ILE A 1 431  ? 145.988 179.675 111.119 1.00 17.82  ? 1648 ILE A N     1 
ATOM   1871  C  CA    . ILE A 1 431  ? 147.218 180.219 110.549 1.00 16.71  ? 1648 ILE A CA    1 
ATOM   1872  C  C     . ILE A 1 431  ? 148.347 179.210 110.675 1.00 16.16  ? 1648 ILE A C     1 
ATOM   1873  O  O     . ILE A 1 431  ? 149.169 179.061 109.765 1.00 19.56  ? 1648 ILE A O     1 
ATOM   1874  C  CB    . ILE A 1 431  ? 147.585 181.556 111.219 1.00 18.02  ? 1648 ILE A CB    1 
ATOM   1875  C  CG1   . ILE A 1 431  ? 146.348 182.436 111.384 1.00 26.35  ? 1648 ILE A CG1   1 
ATOM   1876  C  CG2   . ILE A 1 431  ? 148.640 182.278 110.404 1.00 17.20  ? 1648 ILE A CG2   1 
ATOM   1877  C  CD1   . ILE A 1 431  ? 146.508 183.513 112.428 1.00 24.73  ? 1648 ILE A CD1   1 
ATOM   1878  N  N     . LEU A 1 432  ? 148.392 178.497 111.803 1.00 14.55  ? 1649 LEU A N     1 
ATOM   1879  C  CA    . LEU A 1 432  ? 149.350 177.415 112.008 1.00 14.25  ? 1649 LEU A CA    1 
ATOM   1880  C  C     . LEU A 1 432  ? 149.280 176.383 110.892 1.00 17.62  ? 1649 LEU A C     1 
ATOM   1881  O  O     . LEU A 1 432  ? 150.279 176.114 110.213 1.00 17.08  ? 1649 LEU A O     1 
ATOM   1882  C  CB    . LEU A 1 432  ? 149.075 176.748 113.355 1.00 13.94  ? 1649 LEU A CB    1 
ATOM   1883  C  CG    . LEU A 1 432  ? 149.938 175.547 113.728 1.00 14.94  ? 1649 LEU A CG    1 
ATOM   1884  C  CD1   . LEU A 1 432  ? 151.370 175.962 113.844 1.00 13.24  ? 1649 LEU A CD1   1 
ATOM   1885  C  CD2   . LEU A 1 432  ? 149.450 174.906 115.020 1.00 14.18  ? 1649 LEU A CD2   1 
ATOM   1886  N  N     . LEU A 1 433  ? 148.100 175.797 110.690 1.00 17.89  ? 1650 LEU A N     1 
ATOM   1887  C  CA    . LEU A 1 433  ? 147.971 174.715 109.722 1.00 13.76  ? 1650 LEU A CA    1 
ATOM   1888  C  C     . LEU A 1 433  ? 148.173 175.214 108.296 1.00 15.30  ? 1650 LEU A C     1 
ATOM   1889  O  O     . LEU A 1 433  ? 148.814 174.534 107.485 1.00 19.08  ? 1650 LEU A O     1 
ATOM   1890  C  CB    . LEU A 1 433  ? 146.615 174.035 109.878 1.00 13.45  ? 1650 LEU A CB    1 
ATOM   1891  C  CG    . LEU A 1 433  ? 146.400 172.808 108.999 1.00 16.09  ? 1650 LEU A CG    1 
ATOM   1892  C  CD1   . LEU A 1 433  ? 147.569 171.854 109.111 1.00 12.54  ? 1650 LEU A CD1   1 
ATOM   1893  C  CD2   . LEU A 1 433  ? 145.112 172.119 109.381 1.00 20.20  ? 1650 LEU A CD2   1 
ATOM   1894  N  N     . SER A 1 434  ? 147.650 176.401 107.971 1.00 14.61  ? 1651 SER A N     1 
ATOM   1895  C  CA    . SER A 1 434  ? 147.828 176.941 106.626 1.00 16.47  ? 1651 SER A CA    1 
ATOM   1896  C  C     . SER A 1 434  ? 149.293 177.239 106.332 1.00 17.11  ? 1651 SER A C     1 
ATOM   1897  O  O     . SER A 1 434  ? 149.791 176.918 105.245 1.00 20.44  ? 1651 SER A O     1 
ATOM   1898  C  CB    . SER A 1 434  ? 146.980 178.198 106.454 1.00 20.11  ? 1651 SER A CB    1 
ATOM   1899  O  OG    . SER A 1 434  ? 147.440 179.237 107.298 1.00 24.71  ? 1651 SER A OG    1 
ATOM   1900  N  N     . ALA A 1 435  ? 150.005 177.839 107.292 1.00 15.58  ? 1652 ALA A N     1 
ATOM   1901  C  CA    . ALA A 1 435  ? 151.421 178.122 107.100 1.00 13.77  ? 1652 ALA A CA    1 
ATOM   1902  C  C     . ALA A 1 435  ? 152.230 176.840 106.992 1.00 14.41  ? 1652 ALA A C     1 
ATOM   1903  O  O     . ALA A 1 435  ? 153.170 176.766 106.197 1.00 18.88  ? 1652 ALA A O     1 
ATOM   1904  C  CB    . ALA A 1 435  ? 151.945 178.988 108.244 1.00 15.00  ? 1652 ALA A CB    1 
ATOM   1905  N  N     . GLN A 1 436  ? 151.879 175.820 107.779 1.00 12.01  ? 1653 GLN A N     1 
ATOM   1906  C  CA    . GLN A 1 436  ? 152.592 174.549 107.695 1.00 12.21  ? 1653 GLN A CA    1 
ATOM   1907  C  C     . GLN A 1 436  ? 152.382 173.884 106.339 1.00 12.93  ? 1653 GLN A C     1 
ATOM   1908  O  O     . GLN A 1 436  ? 153.331 173.352 105.747 1.00 13.31  ? 1653 GLN A O     1 
ATOM   1909  C  CB    . GLN A 1 436  ? 152.149 173.631 108.831 1.00 11.47  ? 1653 GLN A CB    1 
ATOM   1910  C  CG    . GLN A 1 436  ? 152.959 173.814 110.102 1.00 10.60  ? 1653 GLN A CG    1 
ATOM   1911  C  CD    . GLN A 1 436  ? 152.271 173.252 111.324 1.00 11.27  ? 1653 GLN A CD    1 
ATOM   1912  O  OE1   . GLN A 1 436  ? 151.068 173.002 111.312 1.00 12.08  ? 1653 GLN A OE1   1 
ATOM   1913  N  NE2   . GLN A 1 436  ? 153.031 173.054 112.393 1.00 13.37  ? 1653 GLN A NE2   1 
ATOM   1914  N  N     . VAL A 1 437  ? 151.150 173.922 105.822 1.00 12.68  ? 1654 VAL A N     1 
ATOM   1915  C  CA    . VAL A 1 437  ? 150.869 173.336 104.514 1.00 12.33  ? 1654 VAL A CA    1 
ATOM   1916  C  C     . VAL A 1 437  ? 151.615 174.083 103.415 1.00 15.09  ? 1654 VAL A C     1 
ATOM   1917  O  O     . VAL A 1 437  ? 152.224 173.464 102.529 1.00 17.68  ? 1654 VAL A O     1 
ATOM   1918  C  CB    . VAL A 1 437  ? 149.351 173.312 104.260 1.00 10.31  ? 1654 VAL A CB    1 
ATOM   1919  C  CG1   . VAL A 1 437  ? 149.055 173.037 102.800 1.00 14.35  ? 1654 VAL A CG1   1 
ATOM   1920  C  CG2   . VAL A 1 437  ? 148.698 172.261 105.129 1.00 12.95  ? 1654 VAL A CG2   1 
ATOM   1921  N  N     . MET A 1 438  ? 151.592 175.419 103.458 1.00 15.49  ? 1655 MET A N     1 
ATOM   1922  C  CA    . MET A 1 438  ? 152.318 176.204 102.463 1.00 15.28  ? 1655 MET A CA    1 
ATOM   1923  C  C     . MET A 1 438  ? 153.816 175.948 102.539 1.00 15.67  ? 1655 MET A C     1 
ATOM   1924  O  O     . MET A 1 438  ? 154.488 175.848 101.504 1.00 19.23  ? 1655 MET A O     1 
ATOM   1925  C  CB    . MET A 1 438  ? 152.021 177.696 102.642 1.00 16.89  ? 1655 MET A CB    1 
ATOM   1926  C  CG    . MET A 1 438  ? 150.572 178.114 102.396 1.00 19.44  ? 1655 MET A CG    1 
ATOM   1927  S  SD    . MET A 1 438  ? 149.927 178.011 100.709 1.00 38.52  ? 1655 MET A SD    1 
ATOM   1928  C  CE    . MET A 1 438  ? 151.399 178.176 99.693  1.00 37.37  ? 1655 MET A CE    1 
ATOM   1929  N  N     . TRP A 1 439  ? 154.356 175.831 103.756 1.00 12.90  ? 1656 TRP A N     1 
ATOM   1930  C  CA    . TRP A 1 439  ? 155.776 175.551 103.912 1.00 13.19  ? 1656 TRP A CA    1 
ATOM   1931  C  C     . TRP A 1 439  ? 156.137 174.202 103.318 1.00 17.05  ? 1656 TRP A C     1 
ATOM   1932  O  O     . TRP A 1 439  ? 157.135 174.088 102.602 1.00 19.33  ? 1656 TRP A O     1 
ATOM   1933  C  CB    . TRP A 1 439  ? 156.169 175.595 105.387 1.00 13.22  ? 1656 TRP A CB    1 
ATOM   1934  C  CG    . TRP A 1 439  ? 157.453 174.875 105.679 1.00 14.43  ? 1656 TRP A CG    1 
ATOM   1935  C  CD1   . TRP A 1 439  ? 158.700 175.214 105.243 1.00 14.21  ? 1656 TRP A CD1   1 
ATOM   1936  C  CD2   . TRP A 1 439  ? 157.615 173.689 106.469 1.00 14.14  ? 1656 TRP A CD2   1 
ATOM   1937  N  NE1   . TRP A 1 439  ? 159.627 174.319 105.715 1.00 13.22  ? 1656 TRP A NE1   1 
ATOM   1938  C  CE2   . TRP A 1 439  ? 158.986 173.372 106.469 1.00 12.09  ? 1656 TRP A CE2   1 
ATOM   1939  C  CE3   . TRP A 1 439  ? 156.733 172.866 107.176 1.00 11.08  ? 1656 TRP A CE3   1 
ATOM   1940  C  CZ2   . TRP A 1 439  ? 159.495 172.271 107.147 1.00 8.82   ? 1656 TRP A CZ2   1 
ATOM   1941  C  CZ3   . TRP A 1 439  ? 157.242 171.775 107.848 1.00 7.84   ? 1656 TRP A CZ3   1 
ATOM   1942  C  CH2   . TRP A 1 439  ? 158.609 171.487 107.829 1.00 8.55   ? 1656 TRP A CH2   1 
ATOM   1943  N  N     . THR A 1 440  ? 155.327 173.173 103.591 1.00 16.99  ? 1657 THR A N     1 
ATOM   1944  C  CA    . THR A 1 440  ? 155.609 171.842 103.059 1.00 15.39  ? 1657 THR A CA    1 
ATOM   1945  C  C     . THR A 1 440  ? 155.565 171.836 101.536 1.00 18.20  ? 1657 THR A C     1 
ATOM   1946  O  O     . THR A 1 440  ? 156.470 171.302 100.880 1.00 19.85  ? 1657 THR A O     1 
ATOM   1947  C  CB    . THR A 1 440  ? 154.616 170.829 103.622 1.00 13.74  ? 1657 THR A CB    1 
ATOM   1948  O  OG1   . THR A 1 440  ? 154.738 170.774 105.047 1.00 14.40  ? 1657 THR A OG1   1 
ATOM   1949  C  CG2   . THR A 1 440  ? 154.893 169.456 103.055 1.00 14.68  ? 1657 THR A CG2   1 
ATOM   1950  N  N     . GLU A 1 441  ? 154.528 172.449 100.955 1.00 18.57  ? 1658 GLU A N     1 
ATOM   1951  C  CA    . GLU A 1 441  ? 154.404 172.471 99.499  1.00 19.68  ? 1658 GLU A CA    1 
ATOM   1952  C  C     . GLU A 1 441  ? 155.566 173.219 98.854  1.00 21.61  ? 1658 GLU A C     1 
ATOM   1953  O  O     . GLU A 1 441  ? 156.164 172.740 97.882  1.00 25.71  ? 1658 GLU A O     1 
ATOM   1954  C  CB    . GLU A 1 441  ? 153.072 173.097 99.085  1.00 18.71  ? 1658 GLU A CB    1 
ATOM   1955  C  CG    . GLU A 1 441  ? 151.837 172.355 99.572  1.00 20.48  ? 1658 GLU A CG    1 
ATOM   1956  C  CD    . GLU A 1 441  ? 152.009 170.850 99.564  1.00 25.54  ? 1658 GLU A CD    1 
ATOM   1957  O  OE1   . GLU A 1 441  ? 152.101 170.266 98.465  1.00 30.11  ? 1658 GLU A OE1   1 
ATOM   1958  O  OE2   . GLU A 1 441  ? 152.047 170.251 100.659 1.00 21.87  ? 1658 GLU A OE2   1 
ATOM   1959  N  N     . LEU A 1 442  ? 155.918 174.388 99.400  1.00 20.09  ? 1659 LEU A N     1 
ATOM   1960  C  CA    . LEU A 1 442  ? 156.982 175.184 98.799  1.00 22.11  ? 1659 LEU A CA    1 
ATOM   1961  C  C     . LEU A 1 442  ? 158.342 174.517 98.960  1.00 24.46  ? 1659 LEU A C     1 
ATOM   1962  O  O     . LEU A 1 442  ? 159.159 174.541 98.031  1.00 28.57  ? 1659 LEU A O     1 
ATOM   1963  C  CB    . LEU A 1 442  ? 156.991 176.588 99.403  1.00 21.76  ? 1659 LEU A CB    1 
ATOM   1964  C  CG    . LEU A 1 442  ? 155.854 177.503 98.942  1.00 25.55  ? 1659 LEU A CG    1 
ATOM   1965  C  CD1   . LEU A 1 442  ? 156.075 178.930 99.407  1.00 26.74  ? 1659 LEU A CD1   1 
ATOM   1966  C  CD2   . LEU A 1 442  ? 155.705 177.454 97.431  1.00 25.70  ? 1659 LEU A CD2   1 
ATOM   1967  N  N     . VAL A 1 443  ? 158.605 173.905 100.119 1.00 23.25  ? 1660 VAL A N     1 
ATOM   1968  C  CA    . VAL A 1 443  ? 159.907 173.277 100.309 1.00 25.85  ? 1660 VAL A CA    1 
ATOM   1969  C  C     . VAL A 1 443  ? 160.020 172.013 99.466  1.00 30.84  ? 1660 VAL A C     1 
ATOM   1970  O  O     . VAL A 1 443  ? 161.107 171.686 98.989  1.00 36.01  ? 1660 VAL A O     1 
ATOM   1971  C  CB    . VAL A 1 443  ? 160.192 173.007 101.801 1.00 20.31  ? 1660 VAL A CB    1 
ATOM   1972  C  CG1   . VAL A 1 443  ? 159.337 171.896 102.336 1.00 18.23  ? 1660 VAL A CG1   1 
ATOM   1973  C  CG2   . VAL A 1 443  ? 161.661 172.692 102.018 1.00 18.50  ? 1660 VAL A CG2   1 
ATOM   1974  N  N     . GLU A 1 444  ? 158.913 171.304 99.217  1.00 28.40  ? 1661 GLU A N     1 
ATOM   1975  C  CA    . GLU A 1 444  ? 158.992 170.159 98.314  1.00 27.45  ? 1661 GLU A CA    1 
ATOM   1976  C  C     . GLU A 1 444  ? 159.203 170.607 96.873  1.00 33.31  ? 1661 GLU A C     1 
ATOM   1977  O  O     . GLU A 1 444  ? 159.992 169.998 96.136  1.00 34.33  ? 1661 GLU A O     1 
ATOM   1978  C  CB    . GLU A 1 444  ? 157.735 169.303 98.433  1.00 21.62  ? 1661 GLU A CB    1 
ATOM   1979  C  CG    . GLU A 1 444  ? 157.785 168.322 99.581  1.00 18.25  ? 1661 GLU A CG    1 
ATOM   1980  C  CD    . GLU A 1 444  ? 156.517 167.516 99.708  1.00 17.92  ? 1661 GLU A CD    1 
ATOM   1981  O  OE1   . GLU A 1 444  ? 155.512 167.879 99.063  1.00 19.85  ? 1661 GLU A OE1   1 
ATOM   1982  O  OE2   . GLU A 1 444  ? 156.527 166.517 100.453 1.00 15.39  ? 1661 GLU A OE2   1 
ATOM   1983  N  N     . LYS A 1 445  ? 158.513 171.676 96.460  1.00 34.04  ? 1662 LYS A N     1 
ATOM   1984  C  CA    . LYS A 1 445  ? 158.678 172.189 95.104  1.00 37.97  ? 1662 LYS A CA    1 
ATOM   1985  C  C     . LYS A 1 445  ? 160.100 172.682 94.867  1.00 40.89  ? 1662 LYS A C     1 
ATOM   1986  O  O     . LYS A 1 445  ? 160.657 172.494 93.779  1.00 43.95  ? 1662 LYS A O     1 
ATOM   1987  C  CB    . LYS A 1 445  ? 157.671 173.307 94.842  1.00 36.88  ? 1662 LYS A CB    1 
ATOM   1988  C  CG    . LYS A 1 445  ? 157.588 173.740 93.388  1.00 42.29  ? 1662 LYS A CG    1 
ATOM   1989  C  CD    . LYS A 1 445  ? 156.603 174.884 93.205  1.00 47.81  ? 1662 LYS A CD    1 
ATOM   1990  C  CE    . LYS A 1 445  ? 156.877 176.015 94.183  1.00 42.69  ? 1662 LYS A CE    1 
ATOM   1991  N  NZ    . LYS A 1 445  ? 155.929 177.148 94.001  1.00 39.51  ? 1662 LYS A NZ    1 
ATOM   1992  N  N     . CYS A 1 446  ? 160.705 173.315 95.870  1.00 37.44  ? 1663 CYS A N     1 
ATOM   1993  C  CA    . CYS A 1 446  ? 162.087 173.755 95.743  1.00 35.42  ? 1663 CYS A CA    1 
ATOM   1994  C  C     . CYS A 1 446  ? 163.093 172.655 96.063  1.00 34.39  ? 1663 CYS A C     1 
ATOM   1995  O  O     . CYS A 1 446  ? 164.284 172.831 95.789  1.00 38.13  ? 1663 CYS A O     1 
ATOM   1996  C  CB    . CYS A 1 446  ? 162.332 174.967 96.643  1.00 38.76  ? 1663 CYS A CB    1 
ATOM   1997  S  SG    . CYS A 1 446  ? 162.726 174.567 98.353  1.00 41.16  ? 1663 CYS A SG    1 
ATOM   1998  N  N     . LEU A 1 447  ? 162.647 171.537 96.635  1.00 33.72  ? 1664 LEU A N     1 
ATOM   1999  C  CA    . LEU A 1 447  ? 163.503 170.382 96.858  1.00 40.55  ? 1664 LEU A CA    1 
ATOM   2000  C  C     . LEU A 1 447  ? 163.579 169.480 95.637  1.00 45.43  ? 1664 LEU A C     1 
ATOM   2001  O  O     . LEU A 1 447  ? 164.549 168.727 95.497  1.00 41.41  ? 1664 LEU A O     1 
ATOM   2002  C  CB    . LEU A 1 447  ? 162.995 169.588 98.065  1.00 37.87  ? 1664 LEU A CB    1 
ATOM   2003  C  CG    . LEU A 1 447  ? 163.831 168.428 98.610  1.00 35.15  ? 1664 LEU A CG    1 
ATOM   2004  C  CD1   . LEU A 1 447  ? 165.269 168.851 98.843  1.00 35.25  ? 1664 LEU A CD1   1 
ATOM   2005  C  CD2   . LEU A 1 447  ? 163.216 167.902 99.887  1.00 24.23  ? 1664 LEU A CD2   1 
ATOM   2006  N  N     . GLN A 1 448  ? 162.580 169.544 94.752  1.00 45.95  ? 1665 GLN A N     1 
ATOM   2007  C  CA    . GLN A 1 448  ? 162.674 168.830 93.483  1.00 43.54  ? 1665 GLN A CA    1 
ATOM   2008  C  C     . GLN A 1 448  ? 163.851 169.309 92.639  1.00 44.83  ? 1665 GLN A C     1 
ATOM   2009  O  O     . GLN A 1 448  ? 164.332 168.559 91.784  1.00 47.52  ? 1665 GLN A O     1 
ATOM   2010  C  CB    . GLN A 1 448  ? 161.370 168.974 92.700  1.00 41.63  ? 1665 GLN A CB    1 
ATOM   2011  C  CG    . GLN A 1 448  ? 160.265 168.044 93.175  1.00 44.29  ? 1665 GLN A CG    1 
ATOM   2012  C  CD    . GLN A 1 448  ? 158.887 168.502 92.741  1.00 50.31  ? 1665 GLN A CD    1 
ATOM   2013  O  OE1   . GLN A 1 448  ? 158.743 169.517 92.060  1.00 45.05  ? 1665 GLN A OE1   1 
ATOM   2014  N  NE2   . GLN A 1 448  ? 157.864 167.754 93.136  1.00 56.33  ? 1665 GLN A NE2   1 
ATOM   2015  N  N     . THR A 1 449  ? 164.321 170.533 92.859  1.00 45.31  ? 1666 THR A N     1 
ATOM   2016  C  CA    . THR A 1 449  ? 165.550 171.049 92.271  1.00 46.60  ? 1666 THR A CA    1 
ATOM   2017  C  C     . THR A 1 449  ? 166.528 171.408 93.388  1.00 45.78  ? 1666 THR A C     1 
ATOM   2018  O  O     . THR A 1 449  ? 166.269 171.177 94.571  1.00 45.35  ? 1666 THR A O     1 
ATOM   2019  C  CB    . THR A 1 449  ? 165.269 172.263 91.382  1.00 49.46  ? 1666 THR A CB    1 
ATOM   2020  O  OG1   . THR A 1 449  ? 164.712 173.320 92.173  1.00 52.31  ? 1666 THR A OG1   1 
ATOM   2021  C  CG2   . THR A 1 449  ? 164.293 171.899 90.275  1.00 43.30  ? 1666 THR A CG2   1 
ATOM   2022  N  N     . ASN A 1 450  ? 167.669 171.967 93.000  1.00 47.48  ? 1667 ASN A N     1 
ATOM   2023  C  CA    . ASN A 1 450  ? 168.683 172.410 93.958  1.00 51.20  ? 1667 ASN A CA    1 
ATOM   2024  C  C     . ASN A 1 450  ? 168.575 173.915 94.213  1.00 48.21  ? 1667 ASN A C     1 
ATOM   2025  O  O     . ASN A 1 450  ? 169.485 174.700 93.946  1.00 54.25  ? 1667 ASN A O     1 
ATOM   2026  C  CB    . ASN A 1 450  ? 170.076 172.007 93.471  1.00 59.49  ? 1667 ASN A CB    1 
ATOM   2027  C  CG    . ASN A 1 450  ? 170.408 172.559 92.091  1.00 61.06  ? 1667 ASN A CG    1 
ATOM   2028  O  OD1   . ASN A 1 450  ? 169.573 173.185 91.437  1.00 56.08  ? 1667 ASN A OD1   1 
ATOM   2029  N  ND2   . ASN A 1 450  ? 171.637 172.326 91.644  1.00 60.44  ? 1667 ASN A ND2   1 
ATOM   2030  N  N     . GLU A 1 451  ? 167.433 174.314 94.767  1.00 43.42  ? 1668 GLU A N     1 
ATOM   2031  C  CA    . GLU A 1 451  ? 167.146 175.721 95.025  1.00 44.24  ? 1668 GLU A CA    1 
ATOM   2032  C  C     . GLU A 1 451  ? 166.567 175.855 96.423  1.00 46.09  ? 1668 GLU A C     1 
ATOM   2033  O  O     . GLU A 1 451  ? 165.501 175.305 96.708  1.00 49.72  ? 1668 GLU A O     1 
ATOM   2034  C  CB    . GLU A 1 451  ? 166.175 176.282 93.982  1.00 46.08  ? 1668 GLU A CB    1 
ATOM   2035  C  CG    . GLU A 1 451  ? 165.512 177.590 94.377  1.00 52.29  ? 1668 GLU A CG    1 
ATOM   2036  C  CD    . GLU A 1 451  ? 164.295 177.903 93.530  1.00 55.97  ? 1668 GLU A CD    1 
ATOM   2037  O  OE1   . GLU A 1 451  ? 163.989 177.110 92.615  1.00 50.45  ? 1668 GLU A OE1   1 
ATOM   2038  O  OE2   . GLU A 1 451  ? 163.646 178.940 93.777  1.00 59.98  ? 1668 GLU A OE2   1 
ATOM   2039  N  N     . PHE A 1 452  ? 167.273 176.570 97.296  1.00 44.49  ? 1669 PHE A N     1 
ATOM   2040  C  CA    . PHE A 1 452  ? 166.786 176.798 98.654  1.00 42.00  ? 1669 PHE A CA    1 
ATOM   2041  C  C     . PHE A 1 452  ? 166.936 178.227 99.149  1.00 48.08  ? 1669 PHE A C     1 
ATOM   2042  O  O     . PHE A 1 452  ? 166.239 178.594 100.101 1.00 46.23  ? 1669 PHE A O     1 
ATOM   2043  C  CB    . PHE A 1 452  ? 167.490 175.862 99.642  1.00 38.11  ? 1669 PHE A CB    1 
ATOM   2044  C  CG    . PHE A 1 452  ? 166.779 174.561 99.849  1.00 37.07  ? 1669 PHE A CG    1 
ATOM   2045  C  CD1   . PHE A 1 452  ? 165.598 174.513 100.567 1.00 29.76  ? 1669 PHE A CD1   1 
ATOM   2046  C  CD2   . PHE A 1 452  ? 167.288 173.385 99.324  1.00 40.57  ? 1669 PHE A CD2   1 
ATOM   2047  C  CE1   . PHE A 1 452  ? 164.940 173.319 100.763 1.00 30.57  ? 1669 PHE A CE1   1 
ATOM   2048  C  CE2   . PHE A 1 452  ? 166.632 172.187 99.514  1.00 34.48  ? 1669 PHE A CE2   1 
ATOM   2049  C  CZ    . PHE A 1 452  ? 165.455 172.155 100.235 1.00 31.62  ? 1669 PHE A CZ    1 
ATOM   2050  N  N     . SER A 1 453  ? 167.809 179.045 98.557  1.00 52.20  ? 1670 SER A N     1 
ATOM   2051  C  CA    . SER A 1 453  ? 168.079 180.372 99.101  1.00 48.03  ? 1670 SER A CA    1 
ATOM   2052  C  C     . SER A 1 453  ? 166.883 181.306 98.969  1.00 43.36  ? 1670 SER A C     1 
ATOM   2053  O  O     . SER A 1 453  ? 166.678 182.164 99.833  1.00 43.07  ? 1670 SER A O     1 
ATOM   2054  C  CB    . SER A 1 453  ? 169.302 180.979 98.415  1.00 49.63  ? 1670 SER A CB    1 
ATOM   2055  O  OG    . SER A 1 453  ? 170.461 180.200 98.661  1.00 49.80  ? 1670 SER A OG    1 
ATOM   2056  N  N     . LYS A 1 454  ? 166.088 181.159 97.907  1.00 43.32  ? 1671 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 454  ? 164.951 182.052 97.700  1.00 46.36  ? 1671 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 454  ? 163.892 181.861 98.780  1.00 45.56  ? 1671 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 454  ? 163.447 182.831 99.410  1.00 46.11  ? 1671 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 454  ? 164.354 181.820 96.311  1.00 52.78  ? 1671 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 454  ? 165.295 182.064 95.121  1.00 53.37  ? 1671 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 454  ? 165.591 183.545 94.858  1.00 58.58  ? 1671 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 454  ? 166.897 184.021 95.489  1.00 56.20  ? 1671 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 454  ? 167.203 185.431 95.124  1.00 51.75  ? 1671 LYS A NZ    1 
ATOM   2065  N  N     . TYR A 1 455  ? 163.485 180.613 99.022  1.00 44.59  ? 1672 TYR A N     1 
ATOM   2066  C  CA    . TYR A 1 455  ? 162.487 180.372 100.056 1.00 41.35  ? 1672 TYR A CA    1 
ATOM   2067  C  C     . TYR A 1 455  ? 163.059 180.597 101.447 1.00 41.37  ? 1672 TYR A C     1 
ATOM   2068  O  O     . TYR A 1 455  ? 162.322 180.983 102.362 1.00 42.05  ? 1672 TYR A O     1 
ATOM   2069  C  CB    . TYR A 1 455  ? 161.916 178.961 99.936  1.00 35.50  ? 1672 TYR A CB    1 
ATOM   2070  C  CG    . TYR A 1 455  ? 160.739 178.749 100.852 1.00 30.28  ? 1672 TYR A CG    1 
ATOM   2071  C  CD1   . TYR A 1 455  ? 159.748 179.711 100.956 1.00 33.58  ? 1672 TYR A CD1   1 
ATOM   2072  C  CD2   . TYR A 1 455  ? 160.616 177.596 101.610 1.00 28.74  ? 1672 TYR A CD2   1 
ATOM   2073  C  CE1   . TYR A 1 455  ? 158.673 179.539 101.791 1.00 31.12  ? 1672 TYR A CE1   1 
ATOM   2074  C  CE2   . TYR A 1 455  ? 159.537 177.412 102.448 1.00 26.72  ? 1672 TYR A CE2   1 
ATOM   2075  C  CZ    . TYR A 1 455  ? 158.569 178.389 102.532 1.00 28.45  ? 1672 TYR A CZ    1 
ATOM   2076  O  OH    . TYR A 1 455  ? 157.488 178.225 103.362 1.00 31.79  ? 1672 TYR A OH    1 
ATOM   2077  N  N     . TRP A 1 456  ? 164.364 180.379 101.624 1.00 38.57  ? 1673 TRP A N     1 
ATOM   2078  C  CA    . TRP A 1 456  ? 164.997 180.704 102.897 1.00 35.50  ? 1673 TRP A CA    1 
ATOM   2079  C  C     . TRP A 1 456  ? 164.923 182.199 103.179 1.00 40.61  ? 1673 TRP A C     1 
ATOM   2080  O  O     . TRP A 1 456  ? 164.605 182.613 104.301 1.00 41.26  ? 1673 TRP A O     1 
ATOM   2081  C  CB    . TRP A 1 456  ? 166.449 180.234 102.894 1.00 35.46  ? 1673 TRP A CB    1 
ATOM   2082  C  CG    . TRP A 1 456  ? 167.086 180.314 104.232 1.00 38.42  ? 1673 TRP A CG    1 
ATOM   2083  C  CD1   . TRP A 1 456  ? 166.466 180.182 105.434 1.00 35.01  ? 1673 TRP A CD1   1 
ATOM   2084  C  CD2   . TRP A 1 456  ? 168.469 180.549 104.514 1.00 42.60  ? 1673 TRP A CD2   1 
ATOM   2085  N  NE1   . TRP A 1 456  ? 167.376 180.318 106.453 1.00 33.06  ? 1673 TRP A NE1   1 
ATOM   2086  C  CE2   . TRP A 1 456  ? 168.614 180.544 105.914 1.00 39.01  ? 1673 TRP A CE2   1 
ATOM   2087  C  CE3   . TRP A 1 456  ? 169.598 180.762 103.718 1.00 46.27  ? 1673 TRP A CE3   1 
ATOM   2088  C  CZ2   . TRP A 1 456  ? 169.842 180.744 106.537 1.00 41.67  ? 1673 TRP A CZ2   1 
ATOM   2089  C  CZ3   . TRP A 1 456  ? 170.817 180.961 104.339 1.00 47.69  ? 1673 TRP A CZ3   1 
ATOM   2090  C  CH2   . TRP A 1 456  ? 170.930 180.950 105.734 1.00 45.87  ? 1673 TRP A CH2   1 
ATOM   2091  N  N     . LYS A 1 457  ? 165.202 183.024 102.166 1.00 41.78  ? 1674 LYS A N     1 
ATOM   2092  C  CA    . LYS A 1 457  ? 165.086 184.470 102.324 1.00 39.02  ? 1674 LYS A CA    1 
ATOM   2093  C  C     . LYS A 1 457  ? 163.642 184.883 102.570 1.00 38.99  ? 1674 LYS A C     1 
ATOM   2094  O  O     . LYS A 1 457  ? 163.382 185.793 103.365 1.00 43.80  ? 1674 LYS A O     1 
ATOM   2095  C  CB    . LYS A 1 457  ? 165.643 185.182 101.092 1.00 42.68  ? 1674 LYS A CB    1 
ATOM   2096  C  CG    . LYS A 1 457  ? 167.159 185.176 100.993 1.00 45.84  ? 1674 LYS A CG    1 
ATOM   2097  C  CD    . LYS A 1 457  ? 167.809 185.534 102.317 1.00 46.25  ? 1674 LYS A CD    1 
ATOM   2098  C  CE    . LYS A 1 457  ? 169.288 185.828 102.135 1.00 51.44  ? 1674 LYS A CE    1 
ATOM   2099  N  NZ    . LYS A 1 457  ? 170.067 184.588 101.862 1.00 46.71  ? 1674 LYS A NZ    1 
ATOM   2100  N  N     . GLU A 1 458  ? 162.691 184.228 101.896 1.00 37.14  ? 1675 GLU A N     1 
ATOM   2101  C  CA    . GLU A 1 458  ? 161.279 184.530 102.126 1.00 38.90  ? 1675 GLU A CA    1 
ATOM   2102  C  C     . GLU A 1 458  ? 160.878 184.237 103.569 1.00 39.67  ? 1675 GLU A C     1 
ATOM   2103  O  O     . GLU A 1 458  ? 160.220 185.056 104.222 1.00 41.99  ? 1675 GLU A O     1 
ATOM   2104  C  CB    . GLU A 1 458  ? 160.406 183.732 101.159 1.00 42.96  ? 1675 GLU A CB    1 
ATOM   2105  C  CG    . GLU A 1 458  ? 160.431 184.229 99.728  1.00 50.66  ? 1675 GLU A CG    1 
ATOM   2106  C  CD    . GLU A 1 458  ? 159.252 183.721 98.921  1.00 56.13  ? 1675 GLU A CD    1 
ATOM   2107  O  OE1   . GLU A 1 458  ? 159.205 182.507 98.632  1.00 51.22  ? 1675 GLU A OE1   1 
ATOM   2108  O  OE2   . GLU A 1 458  ? 158.370 184.536 98.577  1.00 61.46  ? 1675 GLU A OE2   1 
ATOM   2109  N  N     . VAL A 1 459  ? 161.291 183.079 104.090 1.00 37.51  ? 1676 VAL A N     1 
ATOM   2110  C  CA    . VAL A 1 459  ? 160.949 182.707 105.461 1.00 34.79  ? 1676 VAL A CA    1 
ATOM   2111  C  C     . VAL A 1 459  ? 161.628 183.641 106.456 1.00 37.85  ? 1676 VAL A C     1 
ATOM   2112  O  O     . VAL A 1 459  ? 161.026 184.047 107.458 1.00 38.74  ? 1676 VAL A O     1 
ATOM   2113  C  CB    . VAL A 1 459  ? 161.311 181.231 105.712 1.00 33.86  ? 1676 VAL A CB    1 
ATOM   2114  C  CG1   . VAL A 1 459  ? 161.287 180.905 107.196 1.00 25.92  ? 1676 VAL A CG1   1 
ATOM   2115  C  CG2   . VAL A 1 459  ? 160.357 180.324 104.959 1.00 33.07  ? 1676 VAL A CG2   1 
ATOM   2116  N  N     . ASP A 1 460  ? 162.883 184.016 106.187 1.00 41.07  ? 1677 ASP A N     1 
ATOM   2117  C  CA    . ASP A 1 460  ? 163.591 184.942 107.066 1.00 37.91  ? 1677 ASP A CA    1 
ATOM   2118  C  C     . ASP A 1 460  ? 162.922 186.314 107.085 1.00 38.08  ? 1677 ASP A C     1 
ATOM   2119  O  O     . ASP A 1 460  ? 162.822 186.952 108.141 1.00 37.65  ? 1677 ASP A O     1 
ATOM   2120  C  CB    . ASP A 1 460  ? 165.049 185.057 106.626 1.00 38.68  ? 1677 ASP A CB    1 
ATOM   2121  C  CG    . ASP A 1 460  ? 165.938 185.627 107.705 1.00 49.10  ? 1677 ASP A CG    1 
ATOM   2122  O  OD1   . ASP A 1 460  ? 165.609 185.454 108.898 1.00 47.41  ? 1677 ASP A OD1   1 
ATOM   2123  O  OD2   . ASP A 1 460  ? 166.969 186.242 107.362 1.00 55.88  ? 1677 ASP A OD2   1 
ATOM   2124  N  N     . MET A 1 461  ? 162.454 186.781 105.924 1.00 38.05  ? 1678 MET A N     1 
ATOM   2125  C  CA    . MET A 1 461  ? 161.735 188.049 105.873 1.00 36.59  ? 1678 MET A CA    1 
ATOM   2126  C  C     . MET A 1 461  ? 160.410 187.963 106.619 1.00 36.14  ? 1678 MET A C     1 
ATOM   2127  O  O     . MET A 1 461  ? 160.003 188.927 107.277 1.00 41.72  ? 1678 MET A O     1 
ATOM   2128  C  CB    . MET A 1 461  ? 161.513 188.471 104.422 1.00 38.93  ? 1678 MET A CB    1 
ATOM   2129  C  CG    . MET A 1 461  ? 162.757 189.019 103.744 1.00 43.63  ? 1678 MET A CG    1 
ATOM   2130  S  SD    . MET A 1 461  ? 163.830 189.910 104.887 1.00 56.50  ? 1678 MET A SD    1 
ATOM   2131  C  CE    . MET A 1 461  ? 165.405 189.791 104.042 1.00 53.61  ? 1678 MET A CE    1 
ATOM   2132  N  N     . LYS A 1 462  ? 159.723 186.819 106.528 1.00 32.62  ? 1679 LYS A N     1 
ATOM   2133  C  CA    . LYS A 1 462  ? 158.498 186.640 107.306 1.00 33.13  ? 1679 LYS A CA    1 
ATOM   2134  C  C     . LYS A 1 462  ? 158.788 186.680 108.802 1.00 32.06  ? 1679 LYS A C     1 
ATOM   2135  O  O     . LYS A 1 462  ? 158.021 187.266 109.574 1.00 32.14  ? 1679 LYS A O     1 
ATOM   2136  C  CB    . LYS A 1 462  ? 157.813 185.323 106.940 1.00 32.53  ? 1679 LYS A CB    1 
ATOM   2137  C  CG    . LYS A 1 462  ? 157.340 185.215 105.501 1.00 36.01  ? 1679 LYS A CG    1 
ATOM   2138  C  CD    . LYS A 1 462  ? 156.616 186.461 105.035 1.00 41.78  ? 1679 LYS A CD    1 
ATOM   2139  C  CE    . LYS A 1 462  ? 156.374 186.404 103.535 1.00 45.06  ? 1679 LYS A CE    1 
ATOM   2140  N  NZ    . LYS A 1 462  ? 156.087 187.750 102.968 1.00 47.12  ? 1679 LYS A NZ    1 
ATOM   2141  N  N     . ILE A 1 463  ? 159.895 186.064 109.223 1.00 31.02  ? 1680 ILE A N     1 
ATOM   2142  C  CA    . ILE A 1 463  ? 160.279 186.074 110.635 1.00 28.63  ? 1680 ILE A CA    1 
ATOM   2143  C  C     . ILE A 1 463  ? 160.564 187.497 111.101 1.00 35.35  ? 1680 ILE A C     1 
ATOM   2144  O  O     . ILE A 1 463  ? 160.119 187.920 112.176 1.00 39.41  ? 1680 ILE A O     1 
ATOM   2145  C  CB    . ILE A 1 463  ? 161.493 185.156 110.867 1.00 30.22  ? 1680 ILE A CB    1 
ATOM   2146  C  CG1   . ILE A 1 463  ? 161.112 183.692 110.655 1.00 31.85  ? 1680 ILE A CG1   1 
ATOM   2147  C  CG2   . ILE A 1 463  ? 162.065 185.352 112.261 1.00 26.21  ? 1680 ILE A CG2   1 
ATOM   2148  C  CD1   . ILE A 1 463  ? 162.268 182.735 110.822 1.00 27.12  ? 1680 ILE A CD1   1 
ATOM   2149  N  N     . LYS A 1 464  ? 161.313 188.256 110.297 1.00 38.69  ? 1681 LYS A N     1 
ATOM   2150  C  CA    . LYS A 1 464  ? 161.644 189.628 110.673 1.00 34.47  ? 1681 LYS A CA    1 
ATOM   2151  C  C     . LYS A 1 464  ? 160.401 190.510 110.727 1.00 31.69  ? 1681 LYS A C     1 
ATOM   2152  O  O     . LYS A 1 464  ? 160.258 191.335 111.639 1.00 29.88  ? 1681 LYS A O     1 
ATOM   2153  C  CB    . LYS A 1 464  ? 162.677 190.203 109.706 1.00 38.69  ? 1681 LYS A CB    1 
ATOM   2154  C  CG    . LYS A 1 464  ? 164.111 189.962 110.138 1.00 40.04  ? 1681 LYS A CG    1 
ATOM   2155  C  CD    . LYS A 1 464  ? 165.093 190.340 109.047 1.00 40.38  ? 1681 LYS A CD    1 
ATOM   2156  C  CE    . LYS A 1 464  ? 166.520 190.058 109.481 1.00 43.97  ? 1681 LYS A CE    1 
ATOM   2157  N  NZ    . LYS A 1 464  ? 166.609 188.816 110.296 1.00 48.42  ? 1681 LYS A NZ    1 
ATOM   2158  N  N     . GLY A 1 465  ? 159.489 190.347 109.765 1.00 35.13  ? 1682 GLY A N     1 
ATOM   2159  C  CA    . GLY A 1 465  ? 158.250 191.105 109.800 1.00 37.07  ? 1682 GLY A CA    1 
ATOM   2160  C  C     . GLY A 1 465  ? 157.383 190.751 110.993 1.00 36.98  ? 1682 GLY A C     1 
ATOM   2161  O  O     . GLY A 1 465  ? 156.763 191.626 111.605 1.00 39.96  ? 1682 GLY A O     1 
ATOM   2162  N  N     . LEU A 1 466  ? 157.334 189.463 111.346 1.00 32.85  ? 1683 LEU A N     1 
ATOM   2163  C  CA    . LEU A 1 466  ? 156.585 189.048 112.525 1.00 30.98  ? 1683 LEU A CA    1 
ATOM   2164  C  C     . LEU A 1 466  ? 157.196 189.620 113.798 1.00 29.88  ? 1683 LEU A C     1 
ATOM   2165  O  O     . LEU A 1 466  ? 156.468 190.035 114.702 1.00 32.11  ? 1683 LEU A O     1 
ATOM   2166  C  CB    . LEU A 1 466  ? 156.517 187.523 112.597 1.00 28.39  ? 1683 LEU A CB    1 
ATOM   2167  C  CG    . LEU A 1 466  ? 155.429 186.860 111.752 1.00 23.91  ? 1683 LEU A CG    1 
ATOM   2168  C  CD1   . LEU A 1 466  ? 155.534 185.350 111.835 1.00 17.53  ? 1683 LEU A CD1   1 
ATOM   2169  C  CD2   . LEU A 1 466  ? 154.056 187.327 112.198 1.00 25.66  ? 1683 LEU A CD2   1 
ATOM   2170  N  N     . LEU A 1 467  ? 158.527 189.662 113.882 1.00 27.74  ? 1684 LEU A N     1 
ATOM   2171  C  CA    . LEU A 1 467  ? 159.178 190.261 115.047 1.00 29.56  ? 1684 LEU A CA    1 
ATOM   2172  C  C     . LEU A 1 467  ? 158.878 191.754 115.143 1.00 35.35  ? 1684 LEU A C     1 
ATOM   2173  O  O     . LEU A 1 467  ? 158.592 192.276 116.233 1.00 35.83  ? 1684 LEU A O     1 
ATOM   2174  C  CB    . LEU A 1 467  ? 160.686 190.019 114.979 1.00 28.05  ? 1684 LEU A CB    1 
ATOM   2175  C  CG    . LEU A 1 467  ? 161.217 188.748 115.645 1.00 25.42  ? 1684 LEU A CG    1 
ATOM   2176  C  CD1   . LEU A 1 467  ? 162.714 188.610 115.426 1.00 25.56  ? 1684 LEU A CD1   1 
ATOM   2177  C  CD2   . LEU A 1 467  ? 160.895 188.761 117.127 1.00 22.80  ? 1684 LEU A CD2   1 
ATOM   2178  N  N     . ASP A 1 468  ? 158.932 192.455 114.006 1.00 35.89  ? 1685 ASP A N     1 
ATOM   2179  C  CA    . ASP A 1 468  ? 158.629 193.883 113.995 1.00 33.41  ? 1685 ASP A CA    1 
ATOM   2180  C  C     . ASP A 1 468  ? 157.187 194.145 114.407 1.00 32.08  ? 1685 ASP A C     1 
ATOM   2181  O  O     . ASP A 1 468  ? 156.908 195.106 115.132 1.00 37.72  ? 1685 ASP A O     1 
ATOM   2182  C  CB    . ASP A 1 468  ? 158.906 194.471 112.612 1.00 39.08  ? 1685 ASP A CB    1 
ATOM   2183  C  CG    . ASP A 1 468  ? 160.386 194.659 112.345 1.00 45.20  ? 1685 ASP A CG    1 
ATOM   2184  O  OD1   . ASP A 1 468  ? 161.188 194.486 113.286 1.00 44.14  ? 1685 ASP A OD1   1 
ATOM   2185  O  OD2   . ASP A 1 468  ? 160.748 194.983 111.194 1.00 46.85  ? 1685 ASP A OD2   1 
ATOM   2186  N  N     . LYS A 1 469  ? 156.254 193.305 113.953 1.00 30.68  ? 1686 LYS A N     1 
ATOM   2187  C  CA    . LYS A 1 469  ? 154.867 193.465 114.379 1.00 32.87  ? 1686 LYS A CA    1 
ATOM   2188  C  C     . LYS A 1 469  ? 154.695 193.124 115.854 1.00 32.38  ? 1686 LYS A C     1 
ATOM   2189  O  O     . LYS A 1 469  ? 153.913 193.773 116.556 1.00 34.28  ? 1686 LYS A O     1 
ATOM   2190  C  CB    . LYS A 1 469  ? 153.942 192.605 113.525 1.00 31.92  ? 1686 LYS A CB    1 
ATOM   2191  C  CG    . LYS A 1 469  ? 152.480 192.997 113.650 1.00 31.40  ? 1686 LYS A CG    1 
ATOM   2192  C  CD    . LYS A 1 469  ? 151.577 192.033 112.913 1.00 36.63  ? 1686 LYS A CD    1 
ATOM   2193  C  CE    . LYS A 1 469  ? 152.115 191.745 111.532 1.00 38.28  ? 1686 LYS A CE    1 
ATOM   2194  N  NZ    . LYS A 1 469  ? 152.048 192.946 110.656 1.00 36.87  ? 1686 LYS A NZ    1 
ATOM   2195  N  N     . LEU A 1 470  ? 155.419 192.111 116.341 1.00 29.88  ? 1687 LEU A N     1 
ATOM   2196  C  CA    . LEU A 1 470  ? 155.346 191.729 117.747 1.00 28.71  ? 1687 LEU A CA    1 
ATOM   2197  C  C     . LEU A 1 470  ? 155.810 192.855 118.655 1.00 32.46  ? 1687 LEU A C     1 
ATOM   2198  O  O     . LEU A 1 470  ? 155.289 193.016 119.765 1.00 33.74  ? 1687 LEU A O     1 
ATOM   2199  C  CB    . LEU A 1 470  ? 156.190 190.477 117.989 1.00 27.01  ? 1687 LEU A CB    1 
ATOM   2200  C  CG    . LEU A 1 470  ? 156.346 189.979 119.427 1.00 23.11  ? 1687 LEU A CG    1 
ATOM   2201  C  CD1   . LEU A 1 470  ? 155.022 189.477 119.957 1.00 23.31  ? 1687 LEU A CD1   1 
ATOM   2202  C  CD2   . LEU A 1 470  ? 157.409 188.896 119.512 1.00 22.78  ? 1687 LEU A CD2   1 
ATOM   2203  N  N     . ASN A 1 471  ? 156.788 193.641 118.199 1.00 34.53  ? 1688 ASN A N     1 
ATOM   2204  C  CA    . ASN A 1 471  ? 157.243 194.783 118.986 1.00 35.93  ? 1688 ASN A CA    1 
ATOM   2205  C  C     . ASN A 1 471  ? 156.147 195.824 119.214 1.00 33.61  ? 1688 ASN A C     1 
ATOM   2206  O  O     . ASN A 1 471  ? 156.230 196.584 120.184 1.00 33.65  ? 1688 ASN A O     1 
ATOM   2207  C  CB    . ASN A 1 471  ? 158.449 195.442 118.313 1.00 37.21  ? 1688 ASN A CB    1 
ATOM   2208  C  CG    . ASN A 1 471  ? 159.695 194.579 118.375 1.00 37.58  ? 1688 ASN A CG    1 
ATOM   2209  O  OD1   . ASN A 1 471  ? 160.333 194.316 117.356 1.00 36.61  ? 1688 ASN A OD1   1 
ATOM   2210  N  ND2   . ASN A 1 471  ? 160.048 194.136 119.576 1.00 36.95  ? 1688 ASN A ND2   1 
ATOM   2211  N  N     . LYS A 1 472  ? 155.129 195.879 118.356 1.00 32.04  ? 1689 LYS A N     1 
ATOM   2212  C  CA    . LYS A 1 472  ? 154.110 196.928 118.423 1.00 34.25  ? 1689 LYS A CA    1 
ATOM   2213  C  C     . LYS A 1 472  ? 152.704 196.355 118.233 1.00 36.82  ? 1689 LYS A C     1 
ATOM   2214  O  O     . LYS A 1 472  ? 151.910 196.852 117.433 1.00 35.95  ? 1689 LYS A O     1 
ATOM   2215  C  CB    . LYS A 1 472  ? 154.398 198.015 117.389 1.00 32.66  ? 1689 LYS A CB    1 
ATOM   2216  C  CG    . LYS A 1 472  ? 154.735 197.486 116.003 1.00 31.74  ? 1689 LYS A CG    1 
ATOM   2217  C  CD    . LYS A 1 472  ? 154.938 198.620 115.013 1.00 35.06  ? 1689 LYS A CD    1 
ATOM   2218  C  CE    . LYS A 1 472  ? 154.983 198.107 113.583 1.00 36.09  ? 1689 LYS A CE    1 
ATOM   2219  N  NZ    . LYS A 1 472  ? 156.300 197.502 113.249 1.00 37.43  ? 1689 LYS A NZ    1 
ATOM   2220  N  N     . SER A 1 473  ? 152.367 195.301 118.975 1.00 34.34  ? 1690 SER A N     1 
ATOM   2221  C  CA    . SER A 1 473  ? 151.069 194.653 118.834 1.00 31.11  ? 1690 SER A CA    1 
ATOM   2222  C  C     . SER A 1 473  ? 150.401 194.466 120.190 1.00 31.64  ? 1690 SER A C     1 
ATOM   2223  O  O     . SER A 1 473  ? 151.018 194.624 121.246 1.00 29.96  ? 1690 SER A O     1 
ATOM   2224  C  CB    . SER A 1 473  ? 151.193 193.298 118.129 1.00 30.91  ? 1690 SER A CB    1 
ATOM   2225  O  OG    . SER A 1 473  ? 151.700 193.455 116.817 1.00 31.44  ? 1690 SER A OG    1 
ATOM   2226  N  N     . SER A 1 474  ? 149.114 194.122 120.139 1.00 32.84  ? 1691 SER A N     1 
ATOM   2227  C  CA    . SER A 1 474  ? 148.314 193.874 121.329 1.00 35.82  ? 1691 SER A CA    1 
ATOM   2228  C  C     . SER A 1 474  ? 148.605 192.481 121.885 1.00 31.68  ? 1691 SER A C     1 
ATOM   2229  O  O     . SER A 1 474  ? 149.381 191.708 121.319 1.00 30.55  ? 1691 SER A O     1 
ATOM   2230  C  CB    . SER A 1 474  ? 146.830 194.043 121.011 1.00 32.67  ? 1691 SER A CB    1 
ATOM   2231  O  OG    . SER A 1 474  ? 146.397 193.073 120.076 1.00 31.95  ? 1691 SER A OG    1 
ATOM   2232  N  N     . ASP A 1 475  ? 147.948 192.148 123.001 1.00 30.71  ? 1692 ASP A N     1 
ATOM   2233  C  CA    . ASP A 1 475  ? 148.313 190.957 123.768 1.00 31.77  ? 1692 ASP A CA    1 
ATOM   2234  C  C     . ASP A 1 475  ? 147.947 189.664 123.043 1.00 31.61  ? 1692 ASP A C     1 
ATOM   2235  O  O     . ASP A 1 475  ? 148.756 188.729 122.988 1.00 30.53  ? 1692 ASP A O     1 
ATOM   2236  C  CB    . ASP A 1 475  ? 147.653 191.007 125.145 1.00 35.12  ? 1692 ASP A CB    1 
ATOM   2237  C  CG    . ASP A 1 475  ? 146.181 191.355 125.070 1.00 38.34  ? 1692 ASP A CG    1 
ATOM   2238  O  OD1   . ASP A 1 475  ? 145.698 191.650 123.956 1.00 36.59  ? 1692 ASP A OD1   1 
ATOM   2239  O  OD2   . ASP A 1 475  ? 145.509 191.337 126.122 1.00 40.13  ? 1692 ASP A OD2   1 
ATOM   2240  N  N     . ASN A 1 476  ? 146.729 189.579 122.499 1.00 32.21  ? 1693 ASN A N     1 
ATOM   2241  C  CA    . ASN A 1 476  ? 146.347 188.386 121.750 1.00 30.23  ? 1693 ASN A CA    1 
ATOM   2242  C  C     . ASN A 1 476  ? 147.206 188.227 120.504 1.00 25.89  ? 1693 ASN A C     1 
ATOM   2243  O  O     . ASN A 1 476  ? 147.653 187.117 120.181 1.00 27.40  ? 1693 ASN A O     1 
ATOM   2244  C  CB    . ASN A 1 476  ? 144.868 188.447 121.377 1.00 33.46  ? 1693 ASN A CB    1 
ATOM   2245  C  CG    . ASN A 1 476  ? 143.971 187.921 122.476 1.00 36.56  ? 1693 ASN A CG    1 
ATOM   2246  O  OD1   . ASN A 1 476  ? 143.044 188.602 122.915 1.00 38.04  ? 1693 ASN A OD1   1 
ATOM   2247  N  ND2   . ASN A 1 476  ? 144.242 186.703 122.928 1.00 33.94  ? 1693 ASN A ND2   1 
ATOM   2248  N  N     . VAL A 1 477  ? 147.467 189.333 119.807 1.00 23.49  ? 1694 VAL A N     1 
ATOM   2249  C  CA    . VAL A 1 477  ? 148.359 189.283 118.660 1.00 22.33  ? 1694 VAL A CA    1 
ATOM   2250  C  C     . VAL A 1 477  ? 149.786 188.993 119.115 1.00 23.77  ? 1694 VAL A C     1 
ATOM   2251  O  O     . VAL A 1 477  ? 150.550 188.345 118.394 1.00 25.22  ? 1694 VAL A O     1 
ATOM   2252  C  CB    . VAL A 1 477  ? 148.243 190.591 117.853 1.00 26.78  ? 1694 VAL A CB    1 
ATOM   2253  C  CG1   . VAL A 1 477  ? 149.213 190.611 116.686 1.00 24.29  ? 1694 VAL A CG1   1 
ATOM   2254  C  CG2   . VAL A 1 477  ? 146.816 190.778 117.362 1.00 29.11  ? 1694 VAL A CG2   1 
ATOM   2255  N  N     . LYS A 1 478  ? 150.156 189.417 120.330 1.00 24.64  ? 1695 LYS A N     1 
ATOM   2256  C  CA    . LYS A 1 478  ? 151.467 189.061 120.873 1.00 24.03  ? 1695 LYS A CA    1 
ATOM   2257  C  C     . LYS A 1 478  ? 151.608 187.551 121.022 1.00 22.92  ? 1695 LYS A C     1 
ATOM   2258  O  O     . LYS A 1 478  ? 152.619 186.967 120.613 1.00 22.61  ? 1695 LYS A O     1 
ATOM   2259  C  CB    . LYS A 1 478  ? 151.691 189.739 122.226 1.00 28.53  ? 1695 LYS A CB    1 
ATOM   2260  C  CG    . LYS A 1 478  ? 152.506 191.017 122.185 1.00 32.58  ? 1695 LYS A CG    1 
ATOM   2261  C  CD    . LYS A 1 478  ? 152.015 191.993 123.242 1.00 38.10  ? 1695 LYS A CD    1 
ATOM   2262  C  CE    . LYS A 1 478  ? 152.988 193.139 123.446 1.00 43.68  ? 1695 LYS A CE    1 
ATOM   2263  N  NZ    . LYS A 1 478  ? 152.392 194.219 124.281 1.00 50.79  ? 1695 LYS A NZ    1 
ATOM   2264  N  N     . LYS A 1 479  ? 150.594 186.900 121.600 1.00 20.57  ? 1696 LYS A N     1 
ATOM   2265  C  CA    . LYS A 1 479  ? 150.639 185.448 121.755 1.00 18.46  ? 1696 LYS A CA    1 
ATOM   2266  C  C     . LYS A 1 479  ? 150.645 184.744 120.403 1.00 17.89  ? 1696 LYS A C     1 
ATOM   2267  O  O     . LYS A 1 479  ? 151.400 183.780 120.194 1.00 18.51  ? 1696 LYS A O     1 
ATOM   2268  C  CB    . LYS A 1 479  ? 149.456 184.975 122.597 1.00 20.03  ? 1696 LYS A CB    1 
ATOM   2269  C  CG    . LYS A 1 479  ? 149.336 185.667 123.939 1.00 23.99  ? 1696 LYS A CG    1 
ATOM   2270  C  CD    . LYS A 1 479  ? 148.083 185.222 124.665 1.00 27.33  ? 1696 LYS A CD    1 
ATOM   2271  C  CE    . LYS A 1 479  ? 148.410 184.275 125.804 1.00 29.93  ? 1696 LYS A CE    1 
ATOM   2272  N  NZ    . LYS A 1 479  ? 148.863 185.007 127.017 1.00 30.42  ? 1696 LYS A NZ    1 
ATOM   2273  N  N     . LYS A 1 480  ? 149.810 185.219 119.471 1.00 17.21  ? 1697 LYS A N     1 
ATOM   2274  C  CA    . LYS A 1 480  ? 149.755 184.614 118.145 1.00 14.62  ? 1697 LYS A CA    1 
ATOM   2275  C  C     . LYS A 1 480  ? 151.098 184.714 117.435 1.00 16.19  ? 1697 LYS A C     1 
ATOM   2276  O  O     . LYS A 1 480  ? 151.575 183.732 116.857 1.00 22.49  ? 1697 LYS A O     1 
ATOM   2277  C  CB    . LYS A 1 480  ? 148.665 185.281 117.307 1.00 13.35  ? 1697 LYS A CB    1 
ATOM   2278  C  CG    . LYS A 1 480  ? 147.274 184.721 117.519 1.00 13.47  ? 1697 LYS A CG    1 
ATOM   2279  C  CD    . LYS A 1 480  ? 146.291 185.336 116.539 1.00 16.50  ? 1697 LYS A CD    1 
ATOM   2280  C  CE    . LYS A 1 480  ? 144.991 185.711 117.225 1.00 22.46  ? 1697 LYS A CE    1 
ATOM   2281  N  NZ    . LYS A 1 480  ? 144.009 186.304 116.278 1.00 22.36  ? 1697 LYS A NZ    1 
ATOM   2282  N  N     . ILE A 1 481  ? 151.734 185.885 117.486 1.00 14.14  ? 1698 ILE A N     1 
ATOM   2283  C  CA    . ILE A 1 481  ? 153.013 186.054 116.809 1.00 13.43  ? 1698 ILE A CA    1 
ATOM   2284  C  C     . ILE A 1 481  ? 154.114 185.283 117.525 1.00 16.12  ? 1698 ILE A C     1 
ATOM   2285  O  O     . ILE A 1 481  ? 155.032 184.778 116.879 1.00 19.12  ? 1698 ILE A O     1 
ATOM   2286  C  CB    . ILE A 1 481  ? 153.349 187.548 116.664 1.00 17.99  ? 1698 ILE A CB    1 
ATOM   2287  C  CG1   . ILE A 1 481  ? 152.316 188.236 115.777 1.00 23.86  ? 1698 ILE A CG1   1 
ATOM   2288  C  CG2   . ILE A 1 481  ? 154.708 187.739 116.034 1.00 18.87  ? 1698 ILE A CG2   1 
ATOM   2289  C  CD1   . ILE A 1 481  ? 152.589 189.701 115.566 1.00 31.82  ? 1698 ILE A CD1   1 
ATOM   2290  N  N     . GLU A 1 482  ? 154.034 185.140 118.851 1.00 15.24  ? 1699 GLU A N     1 
ATOM   2291  C  CA    . GLU A 1 482  ? 155.022 184.329 119.563 1.00 14.19  ? 1699 GLU A CA    1 
ATOM   2292  C  C     . GLU A 1 482  ? 154.964 182.870 119.116 1.00 14.31  ? 1699 GLU A C     1 
ATOM   2293  O  O     . GLU A 1 482  ? 155.997 182.247 118.829 1.00 15.84  ? 1699 GLU A O     1 
ATOM   2294  C  CB    . GLU A 1 482  ? 154.793 184.442 121.070 1.00 15.13  ? 1699 GLU A CB    1 
ATOM   2295  C  CG    . GLU A 1 482  ? 155.481 185.631 121.719 1.00 16.62  ? 1699 GLU A CG    1 
ATOM   2296  C  CD    . GLU A 1 482  ? 154.821 186.045 123.020 1.00 16.26  ? 1699 GLU A CD    1 
ATOM   2297  O  OE1   . GLU A 1 482  ? 153.612 185.784 123.183 1.00 16.80  ? 1699 GLU A OE1   1 
ATOM   2298  O  OE2   . GLU A 1 482  ? 155.510 186.634 123.878 1.00 15.42  ? 1699 GLU A OE2   1 
ATOM   2299  N  N     . ALA A 1 483  ? 153.754 182.317 119.020 1.00 14.10  ? 1700 ALA A N     1 
ATOM   2300  C  CA    . ALA A 1 483  ? 153.621 180.928 118.588 1.00 14.00  ? 1700 ALA A CA    1 
ATOM   2301  C  C     . ALA A 1 483  ? 154.001 180.752 117.115 1.00 13.58  ? 1700 ALA A C     1 
ATOM   2302  O  O     . ALA A 1 483  ? 154.725 179.805 116.755 1.00 14.81  ? 1700 ALA A O     1 
ATOM   2303  C  CB    . ALA A 1 483  ? 152.199 180.453 118.857 1.00 14.23  ? 1700 ALA A CB    1 
ATOM   2304  N  N     . LEU A 1 484  ? 153.535 181.658 116.247 1.00 12.97  ? 1701 LEU A N     1 
ATOM   2305  C  CA    . LEU A 1 484  ? 153.951 181.624 114.849 1.00 13.28  ? 1701 LEU A CA    1 
ATOM   2306  C  C     . LEU A 1 484  ? 155.452 181.808 114.698 1.00 12.83  ? 1701 LEU A C     1 
ATOM   2307  O  O     . LEU A 1 484  ? 156.039 181.295 113.747 1.00 12.99  ? 1701 LEU A O     1 
ATOM   2308  C  CB    . LEU A 1 484  ? 153.217 182.691 114.038 1.00 11.70  ? 1701 LEU A CB    1 
ATOM   2309  C  CG    . LEU A 1 484  ? 151.921 182.334 113.309 1.00 11.56  ? 1701 LEU A CG    1 
ATOM   2310  C  CD1   . LEU A 1 484  ? 150.776 182.066 114.251 1.00 10.73  ? 1701 LEU A CD1   1 
ATOM   2311  C  CD2   . LEU A 1 484  ? 151.567 183.460 112.357 1.00 14.98  ? 1701 LEU A CD2   1 
ATOM   2312  N  N     . LEU A 1 485  ? 156.093 182.516 115.627 1.00 11.52  ? 1702 LEU A N     1 
ATOM   2313  C  CA    . LEU A 1 485  ? 157.536 182.683 115.553 1.00 12.57  ? 1702 LEU A CA    1 
ATOM   2314  C  C     . LEU A 1 485  ? 158.263 181.422 115.982 1.00 16.50  ? 1702 LEU A C     1 
ATOM   2315  O  O     . LEU A 1 485  ? 159.325 181.115 115.435 1.00 19.42  ? 1702 LEU A O     1 
ATOM   2316  C  CB    . LEU A 1 485  ? 157.971 183.871 116.403 1.00 12.06  ? 1702 LEU A CB    1 
ATOM   2317  C  CG    . LEU A 1 485  ? 158.073 185.178 115.622 1.00 14.14  ? 1702 LEU A CG    1 
ATOM   2318  C  CD1   . LEU A 1 485  ? 158.148 186.357 116.571 1.00 17.65  ? 1702 LEU A CD1   1 
ATOM   2319  C  CD2   . LEU A 1 485  ? 159.270 185.145 114.691 1.00 16.47  ? 1702 LEU A CD2   1 
ATOM   2320  N  N     . VAL A 1 486  ? 157.704 180.680 116.945 1.00 15.80  ? 1703 VAL A N     1 
ATOM   2321  C  CA    . VAL A 1 486  ? 158.223 179.344 117.244 1.00 12.86  ? 1703 VAL A CA    1 
ATOM   2322  C  C     . VAL A 1 486  ? 158.216 178.490 115.981 1.00 15.14  ? 1703 VAL A C     1 
ATOM   2323  O  O     . VAL A 1 486  ? 159.236 177.898 115.588 1.00 13.37  ? 1703 VAL A O     1 
ATOM   2324  C  CB    . VAL A 1 486  ? 157.390 178.678 118.355 1.00 11.87  ? 1703 VAL A CB    1 
ATOM   2325  C  CG1   . VAL A 1 486  ? 157.661 177.186 118.396 1.00 11.65  ? 1703 VAL A CG1   1 
ATOM   2326  C  CG2   . VAL A 1 486  ? 157.667 179.305 119.700 1.00 13.74  ? 1703 VAL A CG2   1 
ATOM   2327  N  N     . GLU A 1 487  ? 157.072 178.468 115.294 1.00 16.60  ? 1704 GLU A N     1 
ATOM   2328  C  CA    . GLU A 1 487  ? 156.947 177.627 114.106 1.00 14.30  ? 1704 GLU A CA    1 
ATOM   2329  C  C     . GLU A 1 487  ? 157.817 178.128 112.958 1.00 13.25  ? 1704 GLU A C     1 
ATOM   2330  O  O     . GLU A 1 487  ? 158.377 177.327 112.202 1.00 11.95  ? 1704 GLU A O     1 
ATOM   2331  C  CB    . GLU A 1 487  ? 155.488 177.545 113.683 1.00 11.53  ? 1704 GLU A CB    1 
ATOM   2332  C  CG    . GLU A 1 487  ? 154.624 176.956 114.761 1.00 13.48  ? 1704 GLU A CG    1 
ATOM   2333  C  CD    . GLU A 1 487  ? 154.842 175.469 114.923 1.00 15.52  ? 1704 GLU A CD    1 
ATOM   2334  O  OE1   . GLU A 1 487  ? 155.200 174.805 113.927 1.00 13.46  ? 1704 GLU A OE1   1 
ATOM   2335  O  OE2   . GLU A 1 487  ? 154.654 174.964 116.047 1.00 16.65  ? 1704 GLU A OE2   1 
ATOM   2336  N  N     . TYR A 1 488  ? 157.953 179.444 112.812 1.00 12.64  ? 1705 TYR A N     1 
ATOM   2337  C  CA    . TYR A 1 488  ? 158.741 179.976 111.711 1.00 12.71  ? 1705 TYR A CA    1 
ATOM   2338  C  C     . TYR A 1 488  ? 160.232 179.813 111.956 1.00 14.12  ? 1705 TYR A C     1 
ATOM   2339  O  O     . TYR A 1 488  ? 160.994 179.632 111.002 1.00 19.11  ? 1705 TYR A O     1 
ATOM   2340  C  CB    . TYR A 1 488  ? 158.385 181.439 111.472 1.00 12.23  ? 1705 TYR A CB    1 
ATOM   2341  C  CG    . TYR A 1 488  ? 157.400 181.628 110.346 1.00 11.92  ? 1705 TYR A CG    1 
ATOM   2342  C  CD1   . TYR A 1 488  ? 156.034 181.552 110.573 1.00 11.43  ? 1705 TYR A CD1   1 
ATOM   2343  C  CD2   . TYR A 1 488  ? 157.836 181.866 109.054 1.00 16.22  ? 1705 TYR A CD2   1 
ATOM   2344  C  CE1   . TYR A 1 488  ? 155.133 181.717 109.546 1.00 11.93  ? 1705 TYR A CE1   1 
ATOM   2345  C  CE2   . TYR A 1 488  ? 156.944 182.031 108.022 1.00 15.67  ? 1705 TYR A CE2   1 
ATOM   2346  C  CZ    . TYR A 1 488  ? 155.595 181.957 108.272 1.00 13.43  ? 1705 TYR A CZ    1 
ATOM   2347  O  OH    . TYR A 1 488  ? 154.706 182.123 107.238 1.00 19.94  ? 1705 TYR A OH    1 
ATOM   2348  N  N     . LEU A 1 489  ? 160.670 179.853 113.216 1.00 13.18  ? 1706 LEU A N     1 
ATOM   2349  C  CA    . LEU A 1 489  ? 162.048 179.487 113.510 1.00 14.71  ? 1706 LEU A CA    1 
ATOM   2350  C  C     . LEU A 1 489  ? 162.293 178.010 113.239 1.00 15.92  ? 1706 LEU A C     1 
ATOM   2351  O  O     . LEU A 1 489  ? 163.382 177.641 112.784 1.00 19.74  ? 1706 LEU A O     1 
ATOM   2352  C  CB    . LEU A 1 489  ? 162.396 179.839 114.956 1.00 15.85  ? 1706 LEU A CB    1 
ATOM   2353  C  CG    . LEU A 1 489  ? 162.556 181.328 115.265 1.00 15.06  ? 1706 LEU A CG    1 
ATOM   2354  C  CD1   . LEU A 1 489  ? 162.446 181.569 116.753 1.00 12.32  ? 1706 LEU A CD1   1 
ATOM   2355  C  CD2   . LEU A 1 489  ? 163.878 181.847 114.736 1.00 19.39  ? 1706 LEU A CD2   1 
ATOM   2356  N  N     . HIS A 1 490  ? 161.293 177.157 113.488 1.00 14.80  ? 1707 HIS A N     1 
ATOM   2357  C  CA    . HIS A 1 490  ? 161.416 175.756 113.082 1.00 14.64  ? 1707 HIS A CA    1 
ATOM   2358  C  C     . HIS A 1 490  ? 161.556 175.621 111.567 1.00 13.76  ? 1707 HIS A C     1 
ATOM   2359  O  O     . HIS A 1 490  ? 162.384 174.840 111.078 1.00 15.77  ? 1707 HIS A O     1 
ATOM   2360  C  CB    . HIS A 1 490  ? 160.212 174.960 113.575 1.00 11.66  ? 1707 HIS A CB    1 
ATOM   2361  C  CG    . HIS A 1 490  ? 160.064 173.621 112.924 1.00 8.45   ? 1707 HIS A CG    1 
ATOM   2362  N  ND1   . HIS A 1 490  ? 161.052 172.662 112.961 1.00 9.07   ? 1707 HIS A ND1   1 
ATOM   2363  C  CD2   . HIS A 1 490  ? 159.042 173.079 112.222 1.00 8.81   ? 1707 HIS A CD2   1 
ATOM   2364  C  CE1   . HIS A 1 490  ? 160.644 171.586 112.313 1.00 8.12   ? 1707 HIS A CE1   1 
ATOM   2365  N  NE2   . HIS A 1 490  ? 159.428 171.815 111.852 1.00 8.37   ? 1707 HIS A NE2   1 
ATOM   2366  N  N     . PHE A 1 491  ? 160.746 176.371 110.812 1.00 12.41  ? 1708 PHE A N     1 
ATOM   2367  C  CA    . PHE A 1 491  ? 160.828 176.335 109.351 1.00 12.47  ? 1708 PHE A CA    1 
ATOM   2368  C  C     . PHE A 1 491  ? 162.197 176.796 108.873 1.00 13.25  ? 1708 PHE A C     1 
ATOM   2369  O  O     . PHE A 1 491  ? 162.796 176.183 107.979 1.00 14.46  ? 1708 PHE A O     1 
ATOM   2370  C  CB    . PHE A 1 491  ? 159.751 177.222 108.720 1.00 11.01  ? 1708 PHE A CB    1 
ATOM   2371  C  CG    . PHE A 1 491  ? 158.334 176.751 108.933 1.00 9.35   ? 1708 PHE A CG    1 
ATOM   2372  C  CD1   . PHE A 1 491  ? 158.048 175.566 109.588 1.00 10.02  ? 1708 PHE A CD1   1 
ATOM   2373  C  CD2   . PHE A 1 491  ? 157.281 177.516 108.466 1.00 10.10  ? 1708 PHE A CD2   1 
ATOM   2374  C  CE1   . PHE A 1 491  ? 156.743 175.162 109.778 1.00 10.00  ? 1708 PHE A CE1   1 
ATOM   2375  C  CE2   . PHE A 1 491  ? 155.979 177.114 108.652 1.00 9.88   ? 1708 PHE A CE2   1 
ATOM   2376  C  CZ    . PHE A 1 491  ? 155.710 175.936 109.307 1.00 9.50   ? 1708 PHE A CZ    1 
ATOM   2377  N  N     . ASN A 1 492  ? 162.699 177.886 109.457 1.00 14.95  ? 1709 ASN A N     1 
ATOM   2378  C  CA    . ASN A 1 492  ? 164.012 178.409 109.105 1.00 18.03  ? 1709 ASN A CA    1 
ATOM   2379  C  C     . ASN A 1 492  ? 165.106 177.397 109.410 1.00 18.54  ? 1709 ASN A C     1 
ATOM   2380  O  O     . ASN A 1 492  ? 166.028 177.211 108.608 1.00 20.93  ? 1709 ASN A O     1 
ATOM   2381  C  CB    . ASN A 1 492  ? 164.257 179.714 109.861 1.00 23.03  ? 1709 ASN A CB    1 
ATOM   2382  C  CG    . ASN A 1 492  ? 165.372 180.540 109.266 1.00 27.38  ? 1709 ASN A CG    1 
ATOM   2383  O  OD1   . ASN A 1 492  ? 166.117 180.076 108.408 1.00 22.81  ? 1709 ASN A OD1   1 
ATOM   2384  N  ND2   . ASN A 1 492  ? 165.497 181.778 109.727 1.00 34.13  ? 1709 ASN A ND2   1 
ATOM   2385  N  N     . ASN A 1 493  ? 165.014 176.727 110.562 1.00 16.50  ? 1710 ASN A N     1 
ATOM   2386  C  CA    . ASN A 1 493  ? 166.004 175.717 110.922 1.00 16.37  ? 1710 ASN A CA    1 
ATOM   2387  C  C     . ASN A 1 493  ? 166.000 174.559 109.934 1.00 18.74  ? 1710 ASN A C     1 
ATOM   2388  O  O     . ASN A 1 493  ? 167.065 174.105 109.496 1.00 19.42  ? 1710 ASN A O     1 
ATOM   2389  C  CB    . ASN A 1 493  ? 165.735 175.213 112.339 1.00 17.31  ? 1710 ASN A CB    1 
ATOM   2390  C  CG    . ASN A 1 493  ? 166.672 174.101 112.748 1.00 24.64  ? 1710 ASN A CG    1 
ATOM   2391  O  OD1   . ASN A 1 493  ? 167.875 174.166 112.499 1.00 28.92  ? 1710 ASN A OD1   1 
ATOM   2392  N  ND2   . ASN A 1 493  ? 166.126 173.069 113.380 1.00 22.32  ? 1710 ASN A ND2   1 
ATOM   2393  N  N     . VAL A 1 494  ? 164.811 174.080 109.557 1.00 18.35  ? 1711 VAL A N     1 
ATOM   2394  C  CA    . VAL A 1 494  ? 164.724 172.957 108.626 1.00 15.99  ? 1711 VAL A CA    1 
ATOM   2395  C  C     . VAL A 1 494  ? 165.265 173.342 107.253 1.00 17.83  ? 1711 VAL A C     1 
ATOM   2396  O  O     . VAL A 1 494  ? 166.017 172.579 106.633 1.00 19.26  ? 1711 VAL A O     1 
ATOM   2397  C  CB    . VAL A 1 494  ? 163.276 172.443 108.547 1.00 11.38  ? 1711 VAL A CB    1 
ATOM   2398  C  CG1   . VAL A 1 494  ? 163.074 171.582 107.315 1.00 10.23  ? 1711 VAL A CG1   1 
ATOM   2399  C  CG2   . VAL A 1 494  ? 162.948 171.649 109.787 1.00 9.68   ? 1711 VAL A CG2   1 
ATOM   2400  N  N     . ILE A 1 495  ? 164.910 174.531 106.761 1.00 19.02  ? 1712 ILE A N     1 
ATOM   2401  C  CA    . ILE A 1 495  ? 165.379 174.950 105.442 1.00 17.26  ? 1712 ILE A CA    1 
ATOM   2402  C  C     . ILE A 1 495  ? 166.887 175.180 105.451 1.00 18.03  ? 1712 ILE A C     1 
ATOM   2403  O  O     . ILE A 1 495  ? 167.587 174.840 104.488 1.00 21.80  ? 1712 ILE A O     1 
ATOM   2404  C  CB    . ILE A 1 495  ? 164.603 176.196 104.976 1.00 15.20  ? 1712 ILE A CB    1 
ATOM   2405  C  CG1   . ILE A 1 495  ? 163.130 175.846 104.777 1.00 12.00  ? 1712 ILE A CG1   1 
ATOM   2406  C  CG2   . ILE A 1 495  ? 165.172 176.745 103.685 1.00 20.57  ? 1712 ILE A CG2   1 
ATOM   2407  C  CD1   . ILE A 1 495  ? 162.224 177.038 104.803 1.00 16.41  ? 1712 ILE A CD1   1 
ATOM   2408  N  N     . GLY A 1 496  ? 167.419 175.733 106.544 1.00 19.84  ? 1713 GLY A N     1 
ATOM   2409  C  CA    . GLY A 1 496  ? 168.859 175.896 106.648 1.00 24.67  ? 1713 GLY A CA    1 
ATOM   2410  C  C     . GLY A 1 496  ? 169.592 174.571 106.715 1.00 26.84  ? 1713 GLY A C     1 
ATOM   2411  O  O     . GLY A 1 496  ? 170.699 174.439 106.188 1.00 31.01  ? 1713 GLY A O     1 
ATOM   2412  N  N     . GLN A 1 497  ? 168.991 173.576 107.372 1.00 23.73  ? 1714 GLN A N     1 
ATOM   2413  C  CA    . GLN A 1 497  ? 169.578 172.240 107.382 1.00 24.75  ? 1714 GLN A CA    1 
ATOM   2414  C  C     . GLN A 1 497  ? 169.554 171.618 105.992 1.00 28.30  ? 1714 GLN A C     1 
ATOM   2415  O  O     . GLN A 1 497  ? 170.510 170.945 105.589 1.00 30.51  ? 1714 GLN A O     1 
ATOM   2416  C  CB    . GLN A 1 497  ? 168.838 171.352 108.381 1.00 20.80  ? 1714 GLN A CB    1 
ATOM   2417  C  CG    . GLN A 1 497  ? 169.218 171.597 109.826 1.00 22.53  ? 1714 GLN A CG    1 
ATOM   2418  C  CD    . GLN A 1 497  ? 168.674 170.537 110.759 1.00 22.73  ? 1714 GLN A CD    1 
ATOM   2419  O  OE1   . GLN A 1 497  ? 167.693 169.865 110.448 1.00 21.85  ? 1714 GLN A OE1   1 
ATOM   2420  N  NE2   . GLN A 1 497  ? 169.305 170.387 111.916 1.00 21.95  ? 1714 GLN A NE2   1 
ATOM   2421  N  N     . LEU A 1 498  ? 168.467 171.829 105.248 1.00 26.19  ? 1715 LEU A N     1 
ATOM   2422  C  CA    . LEU A 1 498  ? 168.349 171.245 103.916 1.00 24.75  ? 1715 LEU A CA    1 
ATOM   2423  C  C     . LEU A 1 498  ? 169.310 171.898 102.930 1.00 30.68  ? 1715 LEU A C     1 
ATOM   2424  O  O     . LEU A 1 498  ? 169.819 171.232 102.022 1.00 36.38  ? 1715 LEU A O     1 
ATOM   2425  C  CB    . LEU A 1 498  ? 166.912 171.365 103.416 1.00 21.51  ? 1715 LEU A CB    1 
ATOM   2426  C  CG    . LEU A 1 498  ? 165.902 170.417 104.060 1.00 17.15  ? 1715 LEU A CG    1 
ATOM   2427  C  CD1   . LEU A 1 498  ? 164.487 170.775 103.649 1.00 16.16  ? 1715 LEU A CD1   1 
ATOM   2428  C  CD2   . LEU A 1 498  ? 166.218 168.987 103.694 1.00 19.26  ? 1715 LEU A CD2   1 
ATOM   2429  N  N     . LYS A 1 499  ? 169.563 173.200 103.085 1.00 31.15  ? 1716 LYS A N     1 
ATOM   2430  C  CA    . LYS A 1 499  ? 170.403 173.911 102.124 1.00 34.90  ? 1716 LYS A CA    1 
ATOM   2431  C  C     . LYS A 1 499  ? 171.857 173.456 102.182 1.00 40.03  ? 1716 LYS A C     1 
ATOM   2432  O  O     . LYS A 1 499  ? 172.545 173.457 101.155 1.00 43.87  ? 1716 LYS A O     1 
ATOM   2433  C  CB    . LYS A 1 499  ? 170.311 175.419 102.363 1.00 38.17  ? 1716 LYS A CB    1 
ATOM   2434  C  CG    . LYS A 1 499  ? 170.928 176.272 101.262 1.00 39.90  ? 1716 LYS A CG    1 
ATOM   2435  C  CD    . LYS A 1 499  ? 172.262 176.866 101.686 1.00 42.71  ? 1716 LYS A CD    1 
ATOM   2436  C  CE    . LYS A 1 499  ? 172.068 178.063 102.598 1.00 45.23  ? 1716 LYS A CE    1 
ATOM   2437  N  NZ    . LYS A 1 499  ? 173.361 178.724 102.925 1.00 47.69  ? 1716 LYS A NZ    1 
ATOM   2438  N  N     . ASN A 1 500  ? 172.340 173.060 103.357 1.00 39.57  ? 1717 ASN A N     1 
ATOM   2439  C  CA    . ASN A 1 500  ? 173.747 172.716 103.528 1.00 42.75  ? 1717 ASN A CA    1 
ATOM   2440  C  C     . ASN A 1 500  ? 174.070 171.277 103.146 1.00 45.95  ? 1717 ASN A C     1 
ATOM   2441  O  O     . ASN A 1 500  ? 175.234 170.877 103.251 1.00 49.28  ? 1717 ASN A O     1 
ATOM   2442  C  CB    . ASN A 1 500  ? 174.174 172.972 104.975 1.00 44.16  ? 1717 ASN A CB    1 
ATOM   2443  C  CG    . ASN A 1 500  ? 174.312 174.448 105.288 1.00 47.50  ? 1717 ASN A CG    1 
ATOM   2444  O  OD1   . ASN A 1 500  ? 173.515 175.015 106.034 1.00 42.94  ? 1717 ASN A OD1   1 
ATOM   2445  N  ND2   . ASN A 1 500  ? 175.331 175.080 104.717 1.00 50.81  ? 1717 ASN A ND2   1 
ATOM   2446  N  N     . CYS A 1 501  ? 173.083 170.495 102.717 1.00 46.29  ? 1718 CYS A N     1 
ATOM   2447  C  CA    . CYS A 1 501  ? 173.332 169.113 102.328 1.00 47.45  ? 1718 CYS A CA    1 
ATOM   2448  C  C     . CYS A 1 501  ? 174.137 169.061 101.034 1.00 50.76  ? 1718 CYS A C     1 
ATOM   2449  O  O     . CYS A 1 501  ? 173.823 169.759 100.065 1.00 49.80  ? 1718 CYS A O     1 
ATOM   2450  C  CB    . CYS A 1 501  ? 172.011 168.366 102.163 1.00 43.18  ? 1718 CYS A CB    1 
ATOM   2451  S  SG    . CYS A 1 501  ? 171.211 167.944 103.723 1.00 50.42  ? 1718 CYS A SG    1 
ATOM   2452  N  N     . SER A 1 502  ? 175.180 168.228 101.023 1.00 53.17  ? 1719 SER A N     1 
ATOM   2453  C  CA    . SER A 1 502  ? 176.047 168.141 99.851  1.00 54.19  ? 1719 SER A CA    1 
ATOM   2454  C  C     . SER A 1 502  ? 175.378 167.379 98.714  1.00 52.48  ? 1719 SER A C     1 
ATOM   2455  O  O     . SER A 1 502  ? 175.481 167.777 97.548  1.00 50.94  ? 1719 SER A O     1 
ATOM   2456  C  CB    . SER A 1 502  ? 177.373 167.483 100.230 1.00 53.68  ? 1719 SER A CB    1 
ATOM   2457  O  OG    . SER A 1 502  ? 178.250 167.430 99.119  1.00 53.42  ? 1719 SER A OG    1 
ATOM   2458  N  N     . THR A 1 503  ? 174.691 166.285 99.028  1.00 49.59  ? 1720 THR A N     1 
ATOM   2459  C  CA    . THR A 1 503  ? 174.045 165.448 98.030  1.00 46.94  ? 1720 THR A CA    1 
ATOM   2460  C  C     . THR A 1 503  ? 172.534 165.493 98.211  1.00 45.37  ? 1720 THR A C     1 
ATOM   2461  O  O     . THR A 1 503  ? 172.025 165.830 99.283  1.00 46.69  ? 1720 THR A O     1 
ATOM   2462  C  CB    . THR A 1 503  ? 174.534 163.996 98.115  1.00 51.68  ? 1720 THR A CB    1 
ATOM   2463  O  OG1   . THR A 1 503  ? 174.245 163.468 99.415  1.00 47.75  ? 1720 THR A OG1   1 
ATOM   2464  C  CG2   . THR A 1 503  ? 176.032 163.924 97.864  1.00 56.53  ? 1720 THR A CG2   1 
ATOM   2465  N  N     . LYS A 1 504  ? 171.817 165.153 97.140  1.00 45.21  ? 1721 LYS A N     1 
ATOM   2466  C  CA    . LYS A 1 504  ? 170.359 165.163 97.202  1.00 45.26  ? 1721 LYS A CA    1 
ATOM   2467  C  C     . LYS A 1 504  ? 169.822 164.016 98.048  1.00 43.48  ? 1721 LYS A C     1 
ATOM   2468  O  O     . LYS A 1 504  ? 168.715 164.115 98.590  1.00 41.77  ? 1721 LYS A O     1 
ATOM   2469  C  CB    . LYS A 1 504  ? 169.771 165.106 95.793  1.00 45.02  ? 1721 LYS A CB    1 
ATOM   2470  C  CG    . LYS A 1 504  ? 170.342 166.142 94.836  1.00 48.67  ? 1721 LYS A CG    1 
ATOM   2471  C  CD    . LYS A 1 504  ? 170.269 167.546 95.419  1.00 54.86  ? 1721 LYS A CD    1 
ATOM   2472  C  CE    . LYS A 1 504  ? 168.889 168.152 95.245  1.00 58.31  ? 1721 LYS A CE    1 
ATOM   2473  N  NZ    . LYS A 1 504  ? 168.833 169.546 95.760  1.00 57.02  ? 1721 LYS A NZ    1 
ATOM   2474  N  N     . GLU A 1 505  ? 170.582 162.925 98.171  1.00 44.23  ? 1722 GLU A N     1 
ATOM   2475  C  CA    . GLU A 1 505  ? 170.126 161.789 98.967  1.00 41.17  ? 1722 GLU A CA    1 
ATOM   2476  C  C     . GLU A 1 505  ? 170.056 162.146 100.447 1.00 37.30  ? 1722 GLU A C     1 
ATOM   2477  O  O     . GLU A 1 505  ? 169.067 161.838 101.123 1.00 40.91  ? 1722 GLU A O     1 
ATOM   2478  C  CB    . GLU A 1 505  ? 171.046 160.588 98.742  1.00 46.10  ? 1722 GLU A CB    1 
ATOM   2479  C  CG    . GLU A 1 505  ? 170.697 159.358 99.576  1.00 50.34  ? 1722 GLU A CG    1 
ATOM   2480  C  CD    . GLU A 1 505  ? 169.208 159.059 99.603  1.00 54.39  ? 1722 GLU A CD    1 
ATOM   2481  O  OE1   . GLU A 1 505  ? 168.618 158.862 98.520  1.00 56.76  ? 1722 GLU A OE1   1 
ATOM   2482  O  OE2   . GLU A 1 505  ? 168.628 159.016 100.710 1.00 47.52  ? 1722 GLU A OE2   1 
ATOM   2483  N  N     . GLU A 1 506  ? 171.091 162.805 100.971 1.00 35.29  ? 1723 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 506  ? 171.049 163.200 102.374 1.00 36.14  ? 1723 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 506  ? 170.051 164.327 102.606 1.00 34.87  ? 1723 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 506  ? 169.490 164.437 103.700 1.00 30.51  ? 1723 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 506  ? 172.444 163.591 102.863 1.00 42.33  ? 1723 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 506  ? 173.043 164.810 102.193 1.00 48.38  ? 1723 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 506  ? 174.352 165.232 102.826 1.00 49.05  ? 1723 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 506  ? 174.729 164.645 103.862 1.00 45.25  ? 1723 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 506  ? 175.005 166.152 102.290 1.00 49.59  ? 1723 GLU A OE2   1 
ATOM   2492  N  N     . ALA A 1 507  ? 169.796 165.152 101.587 1.00 36.65  ? 1724 ALA A N     1 
ATOM   2493  C  CA    . ALA A 1 507  ? 168.738 166.152 101.697 1.00 33.83  ? 1724 ALA A CA    1 
ATOM   2494  C  C     . ALA A 1 507  ? 167.368 165.495 101.796 1.00 29.72  ? 1724 ALA A C     1 
ATOM   2495  O  O     . ALA A 1 507  ? 166.526 165.921 102.594 1.00 30.67  ? 1724 ALA A O     1 
ATOM   2496  C  CB    . ALA A 1 507  ? 168.793 167.110 100.509 1.00 31.83  ? 1724 ALA A CB    1 
ATOM   2497  N  N     . ARG A 1 508  ? 167.130 164.448 101.003 1.00 28.95  ? 1725 ARG A N     1 
ATOM   2498  C  CA    . ARG A 1 508  ? 165.875 163.708 101.105 1.00 24.99  ? 1725 ARG A CA    1 
ATOM   2499  C  C     . ARG A 1 508  ? 165.770 162.988 102.444 1.00 25.22  ? 1725 ARG A C     1 
ATOM   2500  O  O     . ARG A 1 508  ? 164.680 162.889 103.021 1.00 22.80  ? 1725 ARG A O     1 
ATOM   2501  C  CB    . ARG A 1 508  ? 165.759 162.719 99.948  1.00 28.48  ? 1725 ARG A CB    1 
ATOM   2502  C  CG    . ARG A 1 508  ? 164.353 162.213 99.700  1.00 30.87  ? 1725 ARG A CG    1 
ATOM   2503  C  CD    . ARG A 1 508  ? 164.228 161.621 98.306  1.00 42.01  ? 1725 ARG A CD    1 
ATOM   2504  N  NE    . ARG A 1 508  ? 165.354 160.754 97.978  1.00 48.26  ? 1725 ARG A NE    1 
ATOM   2505  C  CZ    . ARG A 1 508  ? 165.278 159.435 97.878  1.00 46.89  ? 1725 ARG A CZ    1 
ATOM   2506  N  NH1   . ARG A 1 508  ? 164.140 158.791 98.076  1.00 40.49  ? 1725 ARG A NH1   1 
ATOM   2507  N  NH2   . ARG A 1 508  ? 166.372 158.743 97.572  1.00 46.84  ? 1725 ARG A NH2   1 
ATOM   2508  N  N     . LEU A 1 509  ? 166.896 162.474 102.947 1.00 31.13  ? 1726 LEU A N     1 
ATOM   2509  C  CA    . LEU A 1 509  ? 166.929 161.883 104.282 1.00 26.47  ? 1726 LEU A CA    1 
ATOM   2510  C  C     . LEU A 1 509  ? 166.541 162.892 105.352 1.00 26.72  ? 1726 LEU A C     1 
ATOM   2511  O  O     . LEU A 1 509  ? 165.744 162.586 106.246 1.00 25.23  ? 1726 LEU A O     1 
ATOM   2512  C  CB    . LEU A 1 509  ? 168.323 161.326 104.569 1.00 24.64  ? 1726 LEU A CB    1 
ATOM   2513  C  CG    . LEU A 1 509  ? 168.582 160.823 105.991 1.00 25.27  ? 1726 LEU A CG    1 
ATOM   2514  C  CD1   . LEU A 1 509  ? 167.662 159.676 106.351 1.00 27.59  ? 1726 LEU A CD1   1 
ATOM   2515  C  CD2   . LEU A 1 509  ? 170.039 160.420 106.154 1.00 28.27  ? 1726 LEU A CD2   1 
ATOM   2516  N  N     . LEU A 1 510  ? 167.101 164.100 105.281 1.00 27.96  ? 1727 LEU A N     1 
ATOM   2517  C  CA    . LEU A 1 510  ? 166.833 165.105 106.301 1.00 21.65  ? 1727 LEU A CA    1 
ATOM   2518  C  C     . LEU A 1 510  ? 165.403 165.618 106.193 1.00 17.71  ? 1727 LEU A C     1 
ATOM   2519  O  O     . LEU A 1 510  ? 164.764 165.909 107.210 1.00 18.15  ? 1727 LEU A O     1 
ATOM   2520  C  CB    . LEU A 1 510  ? 167.857 166.236 106.174 1.00 22.85  ? 1727 LEU A CB    1 
ATOM   2521  C  CG    . LEU A 1 510  ? 168.221 167.178 107.329 1.00 25.60  ? 1727 LEU A CG    1 
ATOM   2522  C  CD1   . LEU A 1 510  ? 169.403 168.031 106.907 1.00 28.58  ? 1727 LEU A CD1   1 
ATOM   2523  C  CD2   . LEU A 1 510  ? 167.079 168.080 107.772 1.00 22.92  ? 1727 LEU A CD2   1 
ATOM   2524  N  N     . TRP A 1 511  ? 164.876 165.713 104.970 1.00 17.30  ? 1728 TRP A N     1 
ATOM   2525  C  CA    . TRP A 1 511  ? 163.496 166.147 104.790 1.00 15.67  ? 1728 TRP A CA    1 
ATOM   2526  C  C     . TRP A 1 511  ? 162.507 165.072 105.222 1.00 15.73  ? 1728 TRP A C     1 
ATOM   2527  O  O     . TRP A 1 511  ? 161.393 165.393 105.649 1.00 14.05  ? 1728 TRP A O     1 
ATOM   2528  C  CB    . TRP A 1 511  ? 163.265 166.543 103.331 1.00 14.97  ? 1728 TRP A CB    1 
ATOM   2529  C  CG    . TRP A 1 511  ? 161.827 166.701 102.943 1.00 11.78  ? 1728 TRP A CG    1 
ATOM   2530  C  CD1   . TRP A 1 511  ? 161.164 166.009 101.975 1.00 12.40  ? 1728 TRP A CD1   1 
ATOM   2531  C  CD2   . TRP A 1 511  ? 160.873 167.609 103.509 1.00 12.58  ? 1728 TRP A CD2   1 
ATOM   2532  N  NE1   . TRP A 1 511  ? 159.859 166.427 101.903 1.00 15.58  ? 1728 TRP A NE1   1 
ATOM   2533  C  CE2   . TRP A 1 511  ? 159.655 167.408 102.836 1.00 14.69  ? 1728 TRP A CE2   1 
ATOM   2534  C  CE3   . TRP A 1 511  ? 160.931 168.573 104.520 1.00 11.77  ? 1728 TRP A CE3   1 
ATOM   2535  C  CZ2   . TRP A 1 511  ? 158.509 168.133 103.138 1.00 14.16  ? 1728 TRP A CZ2   1 
ATOM   2536  C  CZ3   . TRP A 1 511  ? 159.790 169.285 104.822 1.00 9.69   ? 1728 TRP A CZ3   1 
ATOM   2537  C  CH2   . TRP A 1 511  ? 158.594 169.057 104.140 1.00 11.47  ? 1728 TRP A CH2   1 
ATOM   2538  N  N     . ALA A 1 512  ? 162.895 163.799 105.137 1.00 17.70  ? 1729 ALA A N     1 
ATOM   2539  C  CA    . ALA A 1 512  ? 161.999 162.727 105.553 1.00 14.66  ? 1729 ALA A CA    1 
ATOM   2540  C  C     . ALA A 1 512  ? 161.853 162.635 107.065 1.00 12.61  ? 1729 ALA A C     1 
ATOM   2541  O  O     . ALA A 1 512  ? 160.877 162.050 107.541 1.00 13.46  ? 1729 ALA A O     1 
ATOM   2542  C  CB    . ALA A 1 512  ? 162.489 161.389 105.002 1.00 17.58  ? 1729 ALA A CB    1 
ATOM   2543  N  N     . LYS A 1 513  ? 162.789 163.198 107.829 1.00 12.86  ? 1730 LYS A N     1 
ATOM   2544  C  CA    . LYS A 1 513  ? 162.760 163.066 109.281 1.00 13.24  ? 1730 LYS A CA    1 
ATOM   2545  C  C     . LYS A 1 513  ? 161.847 164.074 109.968 1.00 12.28  ? 1730 LYS A C     1 
ATOM   2546  O  O     . LYS A 1 513  ? 161.527 163.883 111.146 1.00 11.26  ? 1730 LYS A O     1 
ATOM   2547  C  CB    . LYS A 1 513  ? 164.174 163.205 109.850 1.00 17.81  ? 1730 LYS A CB    1 
ATOM   2548  C  CG    . LYS A 1 513  ? 165.053 161.985 109.649 1.00 24.61  ? 1730 LYS A CG    1 
ATOM   2549  C  CD    . LYS A 1 513  ? 166.523 162.335 109.813 1.00 27.48  ? 1730 LYS A CD    1 
ATOM   2550  C  CE    . LYS A 1 513  ? 166.981 162.140 111.249 1.00 35.03  ? 1730 LYS A CE    1 
ATOM   2551  N  NZ    . LYS A 1 513  ? 167.144 160.701 111.594 1.00 33.72  ? 1730 LYS A NZ    1 
ATOM   2552  N  N     . VAL A 1 514  ? 161.420 165.128 109.280 1.00 11.79  ? 1731 VAL A N     1 
ATOM   2553  C  CA    . VAL A 1 514  ? 160.613 166.173 109.888 1.00 9.20   ? 1731 VAL A CA    1 
ATOM   2554  C  C     . VAL A 1 514  ? 159.146 165.928 109.563 1.00 9.59   ? 1731 VAL A C     1 
ATOM   2555  O  O     . VAL A 1 514  ? 158.799 165.210 108.621 1.00 13.02  ? 1731 VAL A O     1 
ATOM   2556  C  CB    . VAL A 1 514  ? 161.056 167.579 109.429 1.00 6.31   ? 1731 VAL A CB    1 
ATOM   2557  C  CG1   . VAL A 1 514  ? 162.547 167.755 109.634 1.00 8.14   ? 1731 VAL A CG1   1 
ATOM   2558  C  CG2   . VAL A 1 514  ? 160.692 167.799 107.985 1.00 6.38   ? 1731 VAL A CG2   1 
ATOM   2559  N  N     . GLN A 1 515  ? 158.266 166.518 110.370 1.00 7.34   ? 1732 GLN A N     1 
ATOM   2560  C  CA    . GLN A 1 515  ? 156.835 166.405 110.122 1.00 7.22   ? 1732 GLN A CA    1 
ATOM   2561  C  C     . GLN A 1 515  ? 156.454 167.173 108.865 1.00 8.48   ? 1732 GLN A C     1 
ATOM   2562  O  O     . GLN A 1 515  ? 156.872 168.315 108.663 1.00 14.51  ? 1732 GLN A O     1 
ATOM   2563  C  CB    . GLN A 1 515  ? 156.035 166.922 111.316 1.00 6.07   ? 1732 GLN A CB    1 
ATOM   2564  C  CG    . GLN A 1 515  ? 155.602 165.834 112.280 1.00 6.56   ? 1732 GLN A CG    1 
ATOM   2565  C  CD    . GLN A 1 515  ? 154.547 166.302 113.255 1.00 6.62   ? 1732 GLN A CD    1 
ATOM   2566  O  OE1   . GLN A 1 515  ? 154.296 167.497 113.388 1.00 6.71   ? 1732 GLN A OE1   1 
ATOM   2567  N  NE2   . GLN A 1 515  ? 153.917 165.358 113.940 1.00 5.61   ? 1732 GLN A NE2   1 
ATOM   2568  N  N     . LYS A 1 516  ? 155.655 166.535 108.017 1.00 7.43   ? 1733 LYS A N     1 
ATOM   2569  C  CA    . LYS A 1 516  ? 155.269 167.087 106.729 1.00 9.44   ? 1733 LYS A CA    1 
ATOM   2570  C  C     . LYS A 1 516  ? 153.753 167.142 106.655 1.00 11.63  ? 1733 LYS A C     1 
ATOM   2571  O  O     . LYS A 1 516  ? 153.079 166.147 106.941 1.00 13.18  ? 1733 LYS A O     1 
ATOM   2572  C  CB    . LYS A 1 516  ? 155.841 166.244 105.589 1.00 10.35  ? 1733 LYS A CB    1 
ATOM   2573  C  CG    . LYS A 1 516  ? 157.345 166.059 105.676 1.00 9.34   ? 1733 LYS A CG    1 
ATOM   2574  C  CD    . LYS A 1 516  ? 157.845 164.998 104.716 1.00 10.77  ? 1733 LYS A CD    1 
ATOM   2575  C  CE    . LYS A 1 516  ? 157.376 163.623 105.128 1.00 10.75  ? 1733 LYS A CE    1 
ATOM   2576  N  NZ    . LYS A 1 516  ? 157.734 163.337 106.540 1.00 9.22   ? 1733 LYS A NZ    1 
ATOM   2577  N  N     . PHE A 1 517  ? 153.221 168.296 106.271 1.00 10.51  ? 1734 PHE A N     1 
ATOM   2578  C  CA    . PHE A 1 517  ? 151.788 168.552 106.299 1.00 12.79  ? 1734 PHE A CA    1 
ATOM   2579  C  C     . PHE A 1 517  ? 151.255 168.599 104.875 1.00 15.77  ? 1734 PHE A C     1 
ATOM   2580  O  O     . PHE A 1 517  ? 151.792 169.323 104.032 1.00 18.59  ? 1734 PHE A O     1 
ATOM   2581  C  CB    . PHE A 1 517  ? 151.483 169.867 107.019 1.00 11.64  ? 1734 PHE A CB    1 
ATOM   2582  C  CG    . PHE A 1 517  ? 151.647 169.805 108.516 1.00 9.74   ? 1734 PHE A CG    1 
ATOM   2583  C  CD1   . PHE A 1 517  ? 152.899 169.661 109.089 1.00 9.48   ? 1734 PHE A CD1   1 
ATOM   2584  C  CD2   . PHE A 1 517  ? 150.551 169.920 109.348 1.00 8.16   ? 1734 PHE A CD2   1 
ATOM   2585  C  CE1   . PHE A 1 517  ? 153.048 169.614 110.457 1.00 8.92   ? 1734 PHE A CE1   1 
ATOM   2586  C  CE2   . PHE A 1 517  ? 150.698 169.881 110.718 1.00 7.28   ? 1734 PHE A CE2   1 
ATOM   2587  C  CZ    . PHE A 1 517  ? 151.944 169.723 111.272 1.00 7.95   ? 1734 PHE A CZ    1 
ATOM   2588  N  N     . TYR A 1 518  ? 150.196 167.839 104.610 1.00 15.56  ? 1735 TYR A N     1 
ATOM   2589  C  CA    . TYR A 1 518  ? 149.588 167.791 103.289 1.00 17.87  ? 1735 TYR A CA    1 
ATOM   2590  C  C     . TYR A 1 518  ? 148.084 167.969 103.414 1.00 20.77  ? 1735 TYR A C     1 
ATOM   2591  O  O     . TYR A 1 518  ? 147.529 168.013 104.514 1.00 21.05  ? 1735 TYR A O     1 
ATOM   2592  C  CB    . TYR A 1 518  ? 149.891 166.470 102.573 1.00 19.08  ? 1735 TYR A CB    1 
ATOM   2593  C  CG    . TYR A 1 518  ? 151.357 166.169 102.400 1.00 16.36  ? 1735 TYR A CG    1 
ATOM   2594  C  CD1   . TYR A 1 518  ? 152.116 166.835 101.450 1.00 16.11  ? 1735 TYR A CD1   1 
ATOM   2595  C  CD2   . TYR A 1 518  ? 151.979 165.208 103.181 1.00 14.55  ? 1735 TYR A CD2   1 
ATOM   2596  C  CE1   . TYR A 1 518  ? 153.456 166.555 101.288 1.00 14.36  ? 1735 TYR A CE1   1 
ATOM   2597  C  CE2   . TYR A 1 518  ? 153.314 164.924 103.027 1.00 14.70  ? 1735 TYR A CE2   1 
ATOM   2598  C  CZ    . TYR A 1 518  ? 154.048 165.599 102.081 1.00 13.74  ? 1735 TYR A CZ    1 
ATOM   2599  O  OH    . TYR A 1 518  ? 155.383 165.313 101.929 1.00 12.51  ? 1735 TYR A OH    1 
ATOM   2600  N  N     . GLN A 1 519  ? 147.423 168.068 102.264 1.00 23.32  ? 1736 GLN A N     1 
ATOM   2601  C  CA    . GLN A 1 519  ? 145.970 168.095 102.208 1.00 27.24  ? 1736 GLN A CA    1 
ATOM   2602  C  C     . GLN A 1 519  ? 145.500 167.301 100.999 1.00 32.65  ? 1736 GLN A C     1 
ATOM   2603  O  O     . GLN A 1 519  ? 146.100 167.378 99.924  1.00 36.76  ? 1736 GLN A O     1 
ATOM   2604  C  CB    . GLN A 1 519  ? 145.428 169.528 102.141 1.00 25.20  ? 1736 GLN A CB    1 
ATOM   2605  C  CG    . GLN A 1 519  ? 146.106 170.410 101.113 1.00 27.49  ? 1736 GLN A CG    1 
ATOM   2606  C  CD    . GLN A 1 519  ? 145.239 171.578 100.697 1.00 38.42  ? 1736 GLN A CD    1 
ATOM   2607  O  OE1   . GLN A 1 519  ? 144.067 171.657 101.064 1.00 39.68  ? 1736 GLN A OE1   1 
ATOM   2608  N  NE2   . GLN A 1 519  ? 145.809 172.491 99.920  1.00 36.89  ? 1736 GLN A NE2   1 
ATOM   2609  N  N     . LYS A 1 520  ? 144.430 166.532 101.184 1.00 31.89  ? 1737 LYS A N     1 
ATOM   2610  C  CA    . LYS A 1 520  ? 143.859 165.765 100.090 1.00 37.32  ? 1737 LYS A CA    1 
ATOM   2611  C  C     . LYS A 1 520  ? 143.014 166.662 99.189  1.00 44.82  ? 1737 LYS A C     1 
ATOM   2612  O  O     . LYS A 1 520  ? 142.579 167.749 99.577  1.00 46.54  ? 1737 LYS A O     1 
ATOM   2613  C  CB    . LYS A 1 520  ? 143.010 164.610 100.620 1.00 36.96  ? 1737 LYS A CB    1 
ATOM   2614  C  CG    . LYS A 1 520  ? 143.690 163.772 101.686 1.00 32.95  ? 1737 LYS A CG    1 
ATOM   2615  C  CD    . LYS A 1 520  ? 142.779 162.660 102.178 1.00 37.23  ? 1737 LYS A CD    1 
ATOM   2616  C  CE    . LYS A 1 520  ? 143.459 161.813 103.240 1.00 33.46  ? 1737 LYS A CE    1 
ATOM   2617  N  NZ    . LYS A 1 520  ? 142.574 160.717 103.724 1.00 33.43  ? 1737 LYS A NZ    1 
ATOM   2618  N  N     . ASN A 1 521  ? 142.782 166.187 97.971  1.00 48.98  ? 1738 ASN A N     1 
ATOM   2619  C  CA    . ASN A 1 521  ? 142.010 166.925 96.980  1.00 59.91  ? 1738 ASN A CA    1 
ATOM   2620  C  C     . ASN A 1 521  ? 140.818 166.151 96.446  1.00 63.56  ? 1738 ASN A C     1 
ATOM   2621  O  O     . ASN A 1 521  ? 139.762 166.743 96.208  1.00 58.27  ? 1738 ASN A O     1 
ATOM   2622  C  CB    . ASN A 1 521  ? 142.915 167.337 95.809  1.00 68.67  ? 1738 ASN A CB    1 
ATOM   2623  C  CG    . ASN A 1 521  ? 143.801 166.204 95.332  1.00 72.92  ? 1738 ASN A CG    1 
ATOM   2624  O  OD1   . ASN A 1 521  ? 143.730 165.087 95.845  1.00 69.92  ? 1738 ASN A OD1   1 
ATOM   2625  N  ND2   . ASN A 1 521  ? 144.645 166.487 94.347  1.00 74.00  ? 1738 ASN A ND2   1 
ATOM   2626  N  N     . ASP A 1 522  ? 140.957 164.838 96.247  1.00 66.64  ? 1739 ASP A N     1 
ATOM   2627  C  CA    . ASP A 1 522  ? 139.849 164.048 95.722  1.00 69.01  ? 1739 ASP A CA    1 
ATOM   2628  C  C     . ASP A 1 522  ? 138.750 163.856 96.758  1.00 67.06  ? 1739 ASP A C     1 
ATOM   2629  O  O     . ASP A 1 522  ? 137.582 163.677 96.394  1.00 69.62  ? 1739 ASP A O     1 
ATOM   2630  C  CB    . ASP A 1 522  ? 140.353 162.690 95.235  1.00 70.22  ? 1739 ASP A CB    1 
ATOM   2631  C  CG    . ASP A 1 522  ? 140.869 161.820 96.365  1.00 75.63  ? 1739 ASP A CG    1 
ATOM   2632  O  OD1   . ASP A 1 522  ? 142.052 161.966 96.738  1.00 74.26  ? 1739 ASP A OD1   1 
ATOM   2633  O  OD2   . ASP A 1 522  ? 140.091 160.991 96.882  1.00 76.41  ? 1739 ASP A OD2   1 
ATOM   2634  N  N     . THR A 1 523  ? 139.098 163.890 98.041  1.00 62.74  ? 1740 THR A N     1 
ATOM   2635  C  CA    . THR A 1 523  ? 138.132 163.629 99.101  1.00 61.91  ? 1740 THR A CA    1 
ATOM   2636  C  C     . THR A 1 523  ? 137.256 164.856 99.315  1.00 62.22  ? 1740 THR A C     1 
ATOM   2637  O  O     . THR A 1 523  ? 137.760 165.943 99.619  1.00 61.82  ? 1740 THR A O     1 
ATOM   2638  C  CB    . THR A 1 523  ? 138.848 163.254 100.395 1.00 55.93  ? 1740 THR A CB    1 
ATOM   2639  O  OG1   . THR A 1 523  ? 139.676 164.344 100.818 1.00 48.73  ? 1740 THR A OG1   1 
ATOM   2640  C  CG2   . THR A 1 523  ? 139.711 162.020 100.184 1.00 53.72  ? 1740 THR A CG2   1 
ATOM   2641  N  N     . LEU A 1 524  ? 135.945 164.681 99.157  1.00 61.45  ? 1741 LEU A N     1 
ATOM   2642  C  CA    . LEU A 1 524  ? 134.997 165.743 99.461  1.00 60.57  ? 1741 LEU A CA    1 
ATOM   2643  C  C     . LEU A 1 524  ? 134.697 165.850 100.948 1.00 55.45  ? 1741 LEU A C     1 
ATOM   2644  O  O     . LEU A 1 524  ? 134.051 166.818 101.365 1.00 50.24  ? 1741 LEU A O     1 
ATOM   2645  C  CB    . LEU A 1 524  ? 133.697 165.529 98.683  1.00 64.85  ? 1741 LEU A CB    1 
ATOM   2646  C  CG    . LEU A 1 524  ? 133.668 166.095 97.262  1.00 69.36  ? 1741 LEU A CG    1 
ATOM   2647  C  CD1   . LEU A 1 524  ? 132.305 165.882 96.623  1.00 75.81  ? 1741 LEU A CD1   1 
ATOM   2648  C  CD2   . LEU A 1 524  ? 134.036 167.570 97.266  1.00 64.49  ? 1741 LEU A CD2   1 
ATOM   2649  N  N     . ASP A 1 525  ? 135.140 164.883 101.751 1.00 52.24  ? 1742 ASP A N     1 
ATOM   2650  C  CA    . ASP A 1 525  ? 134.982 164.968 103.197 1.00 47.30  ? 1742 ASP A CA    1 
ATOM   2651  C  C     . ASP A 1 525  ? 135.914 166.042 103.742 1.00 42.51  ? 1742 ASP A C     1 
ATOM   2652  O  O     . ASP A 1 525  ? 137.128 165.993 103.520 1.00 43.79  ? 1742 ASP A O     1 
ATOM   2653  C  CB    . ASP A 1 525  ? 135.270 163.618 103.846 1.00 43.42  ? 1742 ASP A CB    1 
ATOM   2654  C  CG    . ASP A 1 525  ? 134.800 163.554 105.286 1.00 41.48  ? 1742 ASP A CG    1 
ATOM   2655  O  OD1   . ASP A 1 525  ? 134.053 164.459 105.711 1.00 38.83  ? 1742 ASP A OD1   1 
ATOM   2656  O  OD2   . ASP A 1 525  ? 135.175 162.595 105.992 1.00 41.20  ? 1742 ASP A OD2   1 
ATOM   2657  N  N     . ASP A 1 526  ? 135.341 167.014 104.449 1.00 35.72  ? 1743 ASP A N     1 
ATOM   2658  C  CA    . ASP A 1 526  ? 136.098 168.196 104.842 1.00 33.27  ? 1743 ASP A CA    1 
ATOM   2659  C  C     . ASP A 1 526  ? 137.085 167.890 105.962 1.00 29.33  ? 1743 ASP A C     1 
ATOM   2660  O  O     . ASP A 1 526  ? 138.255 168.284 105.896 1.00 28.57  ? 1743 ASP A O     1 
ATOM   2661  C  CB    . ASP A 1 526  ? 135.132 169.303 105.260 1.00 34.49  ? 1743 ASP A CB    1 
ATOM   2662  C  CG    . ASP A 1 526  ? 134.518 170.017 104.073 1.00 41.30  ? 1743 ASP A CG    1 
ATOM   2663  O  OD1   . ASP A 1 526  ? 135.154 170.043 102.999 1.00 41.32  ? 1743 ASP A OD1   1 
ATOM   2664  O  OD2   . ASP A 1 526  ? 133.402 170.557 104.215 1.00 44.90  ? 1743 ASP A OD2   1 
ATOM   2665  N  N     . LEU A 1 527  ? 136.637 167.180 106.996 1.00 29.00  ? 1744 LEU A N     1 
ATOM   2666  C  CA    . LEU A 1 527  ? 137.423 167.044 108.215 1.00 27.23  ? 1744 LEU A CA    1 
ATOM   2667  C  C     . LEU A 1 527  ? 138.508 165.978 108.126 1.00 28.11  ? 1744 LEU A C     1 
ATOM   2668  O  O     . LEU A 1 527  ? 139.379 165.935 109.001 1.00 24.19  ? 1744 LEU A O     1 
ATOM   2669  C  CB    . LEU A 1 527  ? 136.501 166.745 109.399 1.00 24.29  ? 1744 LEU A CB    1 
ATOM   2670  C  CG    . LEU A 1 527  ? 136.127 167.941 110.278 1.00 21.55  ? 1744 LEU A CG    1 
ATOM   2671  C  CD1   . LEU A 1 527  ? 135.420 169.017 109.474 1.00 22.00  ? 1744 LEU A CD1   1 
ATOM   2672  C  CD2   . LEU A 1 527  ? 135.269 167.497 111.448 1.00 23.46  ? 1744 LEU A CD2   1 
ATOM   2673  N  N     . ASN A 1 528  ? 138.483 165.121 107.105 1.00 30.75  ? 1745 ASN A N     1 
ATOM   2674  C  CA    . ASN A 1 528  ? 139.517 164.115 106.902 1.00 26.70  ? 1745 ASN A CA    1 
ATOM   2675  C  C     . ASN A 1 528  ? 140.406 164.442 105.709 1.00 26.74  ? 1745 ASN A C     1 
ATOM   2676  O  O     . ASN A 1 528  ? 141.057 163.549 105.160 1.00 24.15  ? 1745 ASN A O     1 
ATOM   2677  C  CB    . ASN A 1 528  ? 138.891 162.731 106.728 1.00 25.38  ? 1745 ASN A CB    1 
ATOM   2678  C  CG    . ASN A 1 528  ? 138.056 162.316 107.920 1.00 26.95  ? 1745 ASN A CG    1 
ATOM   2679  O  OD1   . ASN A 1 528  ? 138.551 162.240 109.044 1.00 25.66  ? 1745 ASN A OD1   1 
ATOM   2680  N  ND2   . ASN A 1 528  ? 136.781 162.036 107.680 1.00 28.53  ? 1745 ASN A ND2   1 
ATOM   2681  N  N     . SER A 1 529  ? 140.444 165.707 105.297 1.00 27.53  ? 1746 SER A N     1 
ATOM   2682  C  CA    . SER A 1 529  ? 141.144 166.105 104.086 1.00 27.49  ? 1746 SER A CA    1 
ATOM   2683  C  C     . SER A 1 529  ? 142.610 166.443 104.311 1.00 26.41  ? 1746 SER A C     1 
ATOM   2684  O  O     . SER A 1 529  ? 143.334 166.637 103.331 1.00 27.65  ? 1746 SER A O     1 
ATOM   2685  C  CB    . SER A 1 529  ? 140.448 167.312 103.449 1.00 25.77  ? 1746 SER A CB    1 
ATOM   2686  O  OG    . SER A 1 529  ? 140.196 168.320 104.412 1.00 23.04  ? 1746 SER A OG    1 
ATOM   2687  N  N     . VAL A 1 530  ? 143.069 166.512 105.557 1.00 22.63  ? 1747 VAL A N     1 
ATOM   2688  C  CA    . VAL A 1 530  ? 144.437 166.910 105.870 1.00 18.02  ? 1747 VAL A CA    1 
ATOM   2689  C  C     . VAL A 1 530  ? 145.125 165.747 106.568 1.00 20.37  ? 1747 VAL A C     1 
ATOM   2690  O  O     . VAL A 1 530  ? 144.671 165.296 107.627 1.00 20.86  ? 1747 VAL A O     1 
ATOM   2691  C  CB    . VAL A 1 530  ? 144.476 168.174 106.743 1.00 16.66  ? 1747 VAL A CB    1 
ATOM   2692  C  CG1   . VAL A 1 530  ? 145.880 168.422 107.256 1.00 14.16  ? 1747 VAL A CG1   1 
ATOM   2693  C  CG2   . VAL A 1 530  ? 143.986 169.372 105.954 1.00 18.72  ? 1747 VAL A CG2   1 
ATOM   2694  N  N     . PHE A 1 531  ? 146.219 165.267 105.979 1.00 19.31  ? 1748 PHE A N     1 
ATOM   2695  C  CA    . PHE A 1 531  ? 147.027 164.209 106.563 1.00 14.38  ? 1748 PHE A CA    1 
ATOM   2696  C  C     . PHE A 1 531  ? 148.464 164.688 106.715 1.00 12.62  ? 1748 PHE A C     1 
ATOM   2697  O  O     . PHE A 1 531  ? 148.912 165.610 106.028 1.00 13.39  ? 1748 PHE A O     1 
ATOM   2698  C  CB    . PHE A 1 531  ? 146.971 162.918 105.727 1.00 14.80  ? 1748 PHE A CB    1 
ATOM   2699  C  CG    . PHE A 1 531  ? 147.570 163.043 104.356 1.00 17.51  ? 1748 PHE A CG    1 
ATOM   2700  C  CD1   . PHE A 1 531  ? 146.820 163.526 103.300 1.00 21.03  ? 1748 PHE A CD1   1 
ATOM   2701  C  CD2   . PHE A 1 531  ? 148.874 162.644 104.114 1.00 17.12  ? 1748 PHE A CD2   1 
ATOM   2702  C  CE1   . PHE A 1 531  ? 147.364 163.631 102.035 1.00 20.24  ? 1748 PHE A CE1   1 
ATOM   2703  C  CE2   . PHE A 1 531  ? 149.424 162.747 102.852 1.00 18.01  ? 1748 PHE A CE2   1 
ATOM   2704  C  CZ    . PHE A 1 531  ? 148.668 163.239 101.811 1.00 17.51  ? 1748 PHE A CZ    1 
ATOM   2705  N  N     . ILE A 1 532  ? 149.185 164.049 107.633 1.00 12.02  ? 1749 ILE A N     1 
ATOM   2706  C  CA    . ILE A 1 532  ? 150.479 164.528 108.106 1.00 10.74  ? 1749 ILE A CA    1 
ATOM   2707  C  C     . ILE A 1 532  ? 151.476 163.380 108.081 1.00 10.63  ? 1749 ILE A C     1 
ATOM   2708  O  O     . ILE A 1 532  ? 151.222 162.318 108.659 1.00 13.30  ? 1749 ILE A O     1 
ATOM   2709  C  CB    . ILE A 1 532  ? 150.355 165.128 109.517 1.00 8.55   ? 1749 ILE A CB    1 
ATOM   2710  C  CG1   . ILE A 1 532  ? 149.603 166.453 109.428 1.00 9.39   ? 1749 ILE A CG1   1 
ATOM   2711  C  CG2   . ILE A 1 532  ? 151.718 165.311 110.149 1.00 9.42   ? 1749 ILE A CG2   1 
ATOM   2712  C  CD1   . ILE A 1 532  ? 148.973 166.884 110.693 1.00 9.40   ? 1749 ILE A CD1   1 
ATOM   2713  N  N     . SER A 1 533  ? 152.614 163.598 107.425 1.00 7.95   ? 1750 SER A N     1 
ATOM   2714  C  CA    . SER A 1 533  ? 153.572 162.542 107.128 1.00 8.25   ? 1750 SER A CA    1 
ATOM   2715  C  C     . SER A 1 533  ? 154.869 162.763 107.894 1.00 10.85  ? 1750 SER A C     1 
ATOM   2716  O  O     . SER A 1 533  ? 155.453 163.849 107.834 1.00 13.84  ? 1750 SER A O     1 
ATOM   2717  C  CB    . SER A 1 533  ? 153.858 162.484 105.627 1.00 9.22   ? 1750 SER A CB    1 
ATOM   2718  O  OG    . SER A 1 533  ? 154.865 161.533 105.338 1.00 9.81   ? 1750 SER A OG    1 
ATOM   2719  N  N     . GLN A 1 534  ? 155.320 161.729 108.603 1.00 9.38   ? 1751 GLN A N     1 
ATOM   2720  C  CA    . GLN A 1 534  ? 156.584 161.768 109.333 1.00 7.33   ? 1751 GLN A CA    1 
ATOM   2721  C  C     . GLN A 1 534  ? 157.294 160.436 109.153 1.00 8.77   ? 1751 GLN A C     1 
ATOM   2722  O  O     . GLN A 1 534  ? 156.738 159.389 109.499 1.00 10.93  ? 1751 GLN A O     1 
ATOM   2723  C  CB    . GLN A 1 534  ? 156.360 162.059 110.820 1.00 6.74   ? 1751 GLN A CB    1 
ATOM   2724  C  CG    . GLN A 1 534  ? 157.538 161.696 111.713 1.00 7.97   ? 1751 GLN A CG    1 
ATOM   2725  C  CD    . GLN A 1 534  ? 158.574 162.797 111.810 1.00 8.25   ? 1751 GLN A CD    1 
ATOM   2726  O  OE1   . GLN A 1 534  ? 158.241 163.976 111.846 1.00 8.27   ? 1751 GLN A OE1   1 
ATOM   2727  N  NE2   . GLN A 1 534  ? 159.840 162.413 111.857 1.00 8.93   ? 1751 GLN A NE2   1 
ATOM   2728  N  N     . SER A 1 535  ? 158.516 160.486 108.612 1.00 9.04   ? 1752 SER A N     1 
ATOM   2729  C  CA    . SER A 1 535  ? 159.371 159.310 108.404 1.00 7.59   ? 1752 SER A CA    1 
ATOM   2730  C  C     . SER A 1 535  ? 158.683 158.245 107.552 1.00 8.88   ? 1752 SER A C     1 
ATOM   2731  O  O     . SER A 1 535  ? 158.838 157.046 107.785 1.00 11.43  ? 1752 SER A O     1 
ATOM   2732  C  CB    . SER A 1 535  ? 159.844 158.718 109.735 1.00 7.38   ? 1752 SER A CB    1 
ATOM   2733  O  OG    . SER A 1 535  ? 158.794 158.043 110.402 1.00 7.45   ? 1752 SER A OG    1 
ATOM   2734  N  N     . GLY A 1 536  ? 157.922 158.685 106.554 1.00 8.45   ? 1753 GLY A N     1 
ATOM   2735  C  CA    . GLY A 1 536  ? 157.265 157.763 105.650 1.00 8.42   ? 1753 GLY A CA    1 
ATOM   2736  C  C     . GLY A 1 536  ? 155.823 157.464 106.004 1.00 9.64   ? 1753 GLY A C     1 
ATOM   2737  O  O     . GLY A 1 536  ? 154.974 157.358 105.115 1.00 8.80   ? 1753 GLY A O     1 
ATOM   2738  N  N     . TYR A 1 537  ? 155.530 157.322 107.293 1.00 8.25   ? 1754 TYR A N     1 
ATOM   2739  C  CA    . TYR A 1 537  ? 154.178 157.005 107.723 1.00 7.68   ? 1754 TYR A CA    1 
ATOM   2740  C  C     . TYR A 1 537  ? 153.293 158.246 107.671 1.00 8.45   ? 1754 TYR A C     1 
ATOM   2741  O  O     . TYR A 1 537  ? 153.773 159.376 107.577 1.00 9.29   ? 1754 TYR A O     1 
ATOM   2742  C  CB    . TYR A 1 537  ? 154.180 156.426 109.136 1.00 8.73   ? 1754 TYR A CB    1 
ATOM   2743  C  CG    . TYR A 1 537  ? 155.150 155.284 109.334 1.00 11.67  ? 1754 TYR A CG    1 
ATOM   2744  C  CD1   . TYR A 1 537  ? 154.951 154.063 108.707 1.00 11.85  ? 1754 TYR A CD1   1 
ATOM   2745  C  CD2   . TYR A 1 537  ? 156.256 155.423 110.157 1.00 11.65  ? 1754 TYR A CD2   1 
ATOM   2746  C  CE1   . TYR A 1 537  ? 155.828 153.017 108.891 1.00 10.99  ? 1754 TYR A CE1   1 
ATOM   2747  C  CE2   . TYR A 1 537  ? 157.138 154.382 110.344 1.00 10.82  ? 1754 TYR A CE2   1 
ATOM   2748  C  CZ    . TYR A 1 537  ? 156.919 153.183 109.711 1.00 11.01  ? 1754 TYR A CZ    1 
ATOM   2749  O  OH    . TYR A 1 537  ? 157.798 152.145 109.901 1.00 13.67  ? 1754 TYR A OH    1 
ATOM   2750  N  N     . LEU A 1 538  ? 151.983 158.021 107.737 1.00 8.85   ? 1755 LEU A N     1 
ATOM   2751  C  CA    . LEU A 1 538  ? 150.992 159.082 107.628 1.00 7.54   ? 1755 LEU A CA    1 
ATOM   2752  C  C     . LEU A 1 538  ? 150.091 159.087 108.854 1.00 8.33   ? 1755 LEU A C     1 
ATOM   2753  O  O     . LEU A 1 538  ? 149.800 158.033 109.427 1.00 10.16  ? 1755 LEU A O     1 
ATOM   2754  C  CB    . LEU A 1 538  ? 150.139 158.916 106.368 1.00 7.86   ? 1755 LEU A CB    1 
ATOM   2755  C  CG    . LEU A 1 538  ? 150.878 158.724 105.044 1.00 9.19   ? 1755 LEU A CG    1 
ATOM   2756  C  CD1   . LEU A 1 538  ? 149.979 158.049 104.027 1.00 8.46   ? 1755 LEU A CD1   1 
ATOM   2757  C  CD2   . LEU A 1 538  ? 151.369 160.052 104.513 1.00 9.83   ? 1755 LEU A CD2   1 
ATOM   2758  N  N     . LEU A 1 539  ? 149.653 160.279 109.250 1.00 9.01   ? 1756 LEU A N     1 
ATOM   2759  C  CA    . LEU A 1 539  ? 148.707 160.464 110.340 1.00 10.39  ? 1756 LEU A CA    1 
ATOM   2760  C  C     . LEU A 1 539  ? 147.630 161.443 109.894 1.00 12.09  ? 1756 LEU A C     1 
ATOM   2761  O  O     . LEU A 1 539  ? 147.692 162.006 108.800 1.00 13.29  ? 1756 LEU A O     1 
ATOM   2762  C  CB    . LEU A 1 539  ? 149.401 160.962 111.612 1.00 7.50   ? 1756 LEU A CB    1 
ATOM   2763  C  CG    . LEU A 1 539  ? 150.352 159.959 112.260 1.00 7.84   ? 1756 LEU A CG    1 
ATOM   2764  C  CD1   . LEU A 1 539  ? 151.084 160.598 113.412 1.00 7.67   ? 1756 LEU A CD1   1 
ATOM   2765  C  CD2   . LEU A 1 539  ? 149.597 158.730 112.723 1.00 8.69   ? 1756 LEU A CD2   1 
ATOM   2766  N  N     . GLN A 1 540  ? 146.632 161.648 110.748 1.00 9.83   ? 1757 GLN A N     1 
ATOM   2767  C  CA    . GLN A 1 540  ? 145.446 162.417 110.393 1.00 11.18  ? 1757 GLN A CA    1 
ATOM   2768  C  C     . GLN A 1 540  ? 145.296 163.633 111.296 1.00 12.84  ? 1757 GLN A C     1 
ATOM   2769  O  O     . GLN A 1 540  ? 145.417 163.522 112.520 1.00 13.71  ? 1757 GLN A O     1 
ATOM   2770  C  CB    . GLN A 1 540  ? 144.194 161.544 110.483 1.00 15.74  ? 1757 GLN A CB    1 
ATOM   2771  C  CG    . GLN A 1 540  ? 143.975 160.639 109.285 1.00 15.63  ? 1757 GLN A CG    1 
ATOM   2772  C  CD    . GLN A 1 540  ? 143.255 161.338 108.154 1.00 20.37  ? 1757 GLN A CD    1 
ATOM   2773  O  OE1   . GLN A 1 540  ? 142.337 162.125 108.382 1.00 23.82  ? 1757 GLN A OE1   1 
ATOM   2774  N  NE2   . GLN A 1 540  ? 143.666 161.055 106.925 1.00 21.89  ? 1757 GLN A NE2   1 
ATOM   2775  N  N     . TYR A 1 541  ? 145.030 164.787 110.687 1.00 13.07  ? 1758 TYR A N     1 
ATOM   2776  C  CA    . TYR A 1 541  ? 144.627 165.978 111.422 1.00 10.35  ? 1758 TYR A CA    1 
ATOM   2777  C  C     . TYR A 1 541  ? 143.166 165.849 111.832 1.00 12.52  ? 1758 TYR A C     1 
ATOM   2778  O  O     . TYR A 1 541  ? 142.329 165.393 111.049 1.00 16.42  ? 1758 TYR A O     1 
ATOM   2779  C  CB    . TYR A 1 541  ? 144.821 167.222 110.554 1.00 9.86   ? 1758 TYR A CB    1 
ATOM   2780  C  CG    . TYR A 1 541  ? 145.042 168.515 111.306 1.00 11.53  ? 1758 TYR A CG    1 
ATOM   2781  C  CD1   . TYR A 1 541  ? 143.975 169.242 111.808 1.00 14.54  ? 1758 TYR A CD1   1 
ATOM   2782  C  CD2   . TYR A 1 541  ? 146.316 169.028 111.482 1.00 12.08  ? 1758 TYR A CD2   1 
ATOM   2783  C  CE1   . TYR A 1 541  ? 144.174 170.431 112.483 1.00 13.72  ? 1758 TYR A CE1   1 
ATOM   2784  C  CE2   . TYR A 1 541  ? 146.524 170.212 112.155 1.00 12.25  ? 1758 TYR A CE2   1 
ATOM   2785  C  CZ    . TYR A 1 541  ? 145.451 170.910 112.652 1.00 10.96  ? 1758 TYR A CZ    1 
ATOM   2786  O  OH    . TYR A 1 541  ? 145.660 172.090 113.323 1.00 10.26  ? 1758 TYR A OH    1 
ATOM   2787  N  N     . LYS A 1 542  ? 142.855 166.255 113.063 1.00 9.92   ? 1759 LYS A N     1 
ATOM   2788  C  CA    . LYS A 1 542  ? 141.517 166.057 113.603 1.00 10.38  ? 1759 LYS A CA    1 
ATOM   2789  C  C     . LYS A 1 542  ? 140.717 167.339 113.777 1.00 10.50  ? 1759 LYS A C     1 
ATOM   2790  O  O     . LYS A 1 542  ? 139.526 167.258 114.100 1.00 11.04  ? 1759 LYS A O     1 
ATOM   2791  C  CB    . LYS A 1 542  ? 141.591 165.319 114.947 1.00 10.96  ? 1759 LYS A CB    1 
ATOM   2792  C  CG    . LYS A 1 542  ? 141.777 163.813 114.812 1.00 11.20  ? 1759 LYS A CG    1 
ATOM   2793  C  CD    . LYS A 1 542  ? 141.065 163.259 113.587 1.00 12.73  ? 1759 LYS A CD    1 
ATOM   2794  C  CE    . LYS A 1 542  ? 141.341 161.780 113.403 1.00 15.88  ? 1759 LYS A CE    1 
ATOM   2795  N  NZ    . LYS A 1 542  ? 140.767 161.280 112.127 1.00 14.13  ? 1759 LYS A NZ    1 
ATOM   2796  N  N     . PHE A 1 543  ? 141.334 168.507 113.575 1.00 11.85  ? 1760 PHE A N     1 
ATOM   2797  C  CA    . PHE A 1 543  ? 140.646 169.803 113.555 1.00 10.32  ? 1760 PHE A CA    1 
ATOM   2798  C  C     . PHE A 1 543  ? 139.916 170.096 114.864 1.00 11.30  ? 1760 PHE A C     1 
ATOM   2799  O  O     . PHE A 1 543  ? 138.818 170.654 114.870 1.00 15.04  ? 1760 PHE A O     1 
ATOM   2800  C  CB    . PHE A 1 543  ? 139.687 169.898 112.368 1.00 11.29  ? 1760 PHE A CB    1 
ATOM   2801  C  CG    . PHE A 1 543  ? 140.375 170.010 111.043 1.00 11.64  ? 1760 PHE A CG    1 
ATOM   2802  C  CD1   . PHE A 1 543  ? 141.024 171.175 110.686 1.00 13.31  ? 1760 PHE A CD1   1 
ATOM   2803  C  CD2   . PHE A 1 543  ? 140.378 168.950 110.157 1.00 13.21  ? 1760 PHE A CD2   1 
ATOM   2804  C  CE1   . PHE A 1 543  ? 141.656 171.283 109.468 1.00 14.92  ? 1760 PHE A CE1   1 
ATOM   2805  C  CE2   . PHE A 1 543  ? 141.011 169.052 108.938 1.00 14.55  ? 1760 PHE A CE2   1 
ATOM   2806  C  CZ    . PHE A 1 543  ? 141.652 170.220 108.594 1.00 14.58  ? 1760 PHE A CZ    1 
ATOM   2807  N  N     . GLU A 1 544  ? 140.526 169.719 115.982 1.00 9.26   ? 1761 GLU A N     1 
ATOM   2808  C  CA    . GLU A 1 544  ? 140.030 170.110 117.292 1.00 9.46   ? 1761 GLU A CA    1 
ATOM   2809  C  C     . GLU A 1 544  ? 140.664 171.435 117.689 1.00 11.12  ? 1761 GLU A C     1 
ATOM   2810  O  O     . GLU A 1 544  ? 141.822 171.701 117.357 1.00 12.02  ? 1761 GLU A O     1 
ATOM   2811  C  CB    . GLU A 1 544  ? 140.342 169.039 118.338 1.00 9.04   ? 1761 GLU A CB    1 
ATOM   2812  C  CG    . GLU A 1 544  ? 139.352 167.889 118.356 1.00 11.73  ? 1761 GLU A CG    1 
ATOM   2813  C  CD    . GLU A 1 544  ? 139.884 166.666 119.075 1.00 12.52  ? 1761 GLU A CD    1 
ATOM   2814  O  OE1   . GLU A 1 544  ? 140.461 166.825 120.169 1.00 13.63  ? 1761 GLU A OE1   1 
ATOM   2815  O  OE2   . GLU A 1 544  ? 139.718 165.544 118.551 1.00 9.27   ? 1761 GLU A OE2   1 
ATOM   2816  N  N     . TYR A 1 545  ? 139.902 172.265 118.398 1.00 10.16  ? 1762 TYR A N     1 
ATOM   2817  C  CA    . TYR A 1 545  ? 140.391 173.581 118.785 1.00 9.85   ? 1762 TYR A CA    1 
ATOM   2818  C  C     . TYR A 1 545  ? 141.341 173.465 119.970 1.00 10.77  ? 1762 TYR A C     1 
ATOM   2819  O  O     . TYR A 1 545  ? 141.046 172.773 120.949 1.00 11.68  ? 1762 TYR A O     1 
ATOM   2820  C  CB    . TYR A 1 545  ? 139.231 174.513 119.127 1.00 10.43  ? 1762 TYR A CB    1 
ATOM   2821  C  CG    . TYR A 1 545  ? 139.664 175.942 119.360 1.00 13.26  ? 1762 TYR A CG    1 
ATOM   2822  C  CD1   . TYR A 1 545  ? 140.611 176.544 118.543 1.00 16.38  ? 1762 TYR A CD1   1 
ATOM   2823  C  CD2   . TYR A 1 545  ? 139.134 176.686 120.400 1.00 11.75  ? 1762 TYR A CD2   1 
ATOM   2824  C  CE1   . TYR A 1 545  ? 141.012 177.849 118.758 1.00 16.26  ? 1762 TYR A CE1   1 
ATOM   2825  C  CE2   . TYR A 1 545  ? 139.527 177.987 120.623 1.00 14.47  ? 1762 TYR A CE2   1 
ATOM   2826  C  CZ    . TYR A 1 545  ? 140.465 178.563 119.799 1.00 16.60  ? 1762 TYR A CZ    1 
ATOM   2827  O  OH    . TYR A 1 545  ? 140.858 179.860 120.018 1.00 22.81  ? 1762 TYR A OH    1 
ATOM   2828  N  N     . ILE A 1 546  ? 142.481 174.146 119.879 1.00 12.10  ? 1763 ILE A N     1 
ATOM   2829  C  CA    . ILE A 1 546  ? 143.508 174.065 120.907 1.00 11.89  ? 1763 ILE A CA    1 
ATOM   2830  C  C     . ILE A 1 546  ? 143.840 175.412 121.538 1.00 15.15  ? 1763 ILE A C     1 
ATOM   2831  O  O     . ILE A 1 546  ? 144.411 175.434 122.640 1.00 17.93  ? 1763 ILE A O     1 
ATOM   2832  C  CB    . ILE A 1 546  ? 144.793 173.408 120.357 1.00 10.73  ? 1763 ILE A CB    1 
ATOM   2833  C  CG1   . ILE A 1 546  ? 145.377 174.239 119.215 1.00 11.42  ? 1763 ILE A CG1   1 
ATOM   2834  C  CG2   . ILE A 1 546  ? 144.520 171.991 119.891 1.00 9.87   ? 1763 ILE A CG2   1 
ATOM   2835  C  CD1   . ILE A 1 546  ? 146.809 173.903 118.891 1.00 10.45  ? 1763 ILE A CD1   1 
ATOM   2836  N  N     . GLY A 1 547  ? 143.511 176.537 120.908 1.00 16.25  ? 1764 GLY A N     1 
ATOM   2837  C  CA    . GLY A 1 547  ? 143.878 177.826 121.469 1.00 16.97  ? 1764 GLY A CA    1 
ATOM   2838  C  C     . GLY A 1 547  ? 145.292 178.220 121.073 1.00 20.74  ? 1764 GLY A C     1 
ATOM   2839  O  O     . GLY A 1 547  ? 145.788 177.843 120.013 1.00 21.75  ? 1764 GLY A O     1 
ATOM   2840  N  N     . ILE A 1 548  ? 145.943 178.994 121.937 1.00 22.14  ? 1765 ILE A N     1 
ATOM   2841  C  CA    . ILE A 1 548  ? 147.361 179.301 121.752 1.00 21.41  ? 1765 ILE A CA    1 
ATOM   2842  C  C     . ILE A 1 548  ? 148.141 178.628 122.874 1.00 20.32  ? 1765 ILE A C     1 
ATOM   2843  O  O     . ILE A 1 548  ? 148.393 179.251 123.915 1.00 23.90  ? 1765 ILE A O     1 
ATOM   2844  C  CB    . ILE A 1 548  ? 147.643 180.812 121.734 1.00 20.89  ? 1765 ILE A CB    1 
ATOM   2845  C  CG1   . ILE A 1 548  ? 146.747 181.529 120.735 1.00 19.30  ? 1765 ILE A CG1   1 
ATOM   2846  C  CG2   . ILE A 1 548  ? 149.095 181.079 121.368 1.00 21.14  ? 1765 ILE A CG2   1 
ATOM   2847  C  CD1   . ILE A 1 548  ? 145.639 182.278 121.387 1.00 21.89  ? 1765 ILE A CD1   1 
ATOM   2848  N  N     . PRO A 1 549  ? 148.542 177.375 122.714 1.00 15.74  ? 1766 PRO A N     1 
ATOM   2849  C  CA    . PRO A 1 549  ? 149.327 176.715 123.754 1.00 14.28  ? 1766 PRO A CA    1 
ATOM   2850  C  C     . PRO A 1 549  ? 150.763 177.213 123.748 1.00 15.91  ? 1766 PRO A C     1 
ATOM   2851  O  O     . PRO A 1 549  ? 151.234 177.827 122.789 1.00 15.73  ? 1766 PRO A O     1 
ATOM   2852  C  CB    . PRO A 1 549  ? 149.251 175.240 123.359 1.00 12.80  ? 1766 PRO A CB    1 
ATOM   2853  C  CG    . PRO A 1 549  ? 149.158 175.283 121.872 1.00 14.37  ? 1766 PRO A CG    1 
ATOM   2854  C  CD    . PRO A 1 549  ? 148.385 176.526 121.521 1.00 15.69  ? 1766 PRO A CD    1 
ATOM   2855  N  N     . GLU A 1 550  ? 151.455 176.946 124.850 1.00 15.04  ? 1767 GLU A N     1 
ATOM   2856  C  CA    . GLU A 1 550  ? 152.870 177.293 124.946 1.00 12.80  ? 1767 GLU A CA    1 
ATOM   2857  C  C     . GLU A 1 550  ? 153.634 176.390 123.990 1.00 12.72  ? 1767 GLU A C     1 
ATOM   2858  O  O     . GLU A 1 550  ? 153.864 175.213 124.274 1.00 15.24  ? 1767 GLU A O     1 
ATOM   2859  C  CB    . GLU A 1 550  ? 153.366 177.141 126.380 1.00 12.67  ? 1767 GLU A CB    1 
ATOM   2860  C  CG    . GLU A 1 550  ? 154.771 177.674 126.612 1.00 15.53  ? 1767 GLU A CG    1 
ATOM   2861  C  CD    . GLU A 1 550  ? 155.812 176.573 126.668 1.00 16.54  ? 1767 GLU A CD    1 
ATOM   2862  O  OE1   . GLU A 1 550  ? 155.480 175.460 127.124 1.00 16.57  ? 1767 GLU A OE1   1 
ATOM   2863  O  OE2   . GLU A 1 550  ? 156.963 176.819 126.254 1.00 15.47  ? 1767 GLU A OE2   1 
ATOM   2864  N  N     . ARG A 1 551  ? 154.018 176.940 122.842 1.00 9.69   ? 1768 ARG A N     1 
ATOM   2865  C  CA    . ARG A 1 551  ? 154.589 176.132 121.775 1.00 10.26  ? 1768 ARG A CA    1 
ATOM   2866  C  C     . ARG A 1 551  ? 155.990 175.670 122.142 1.00 11.37  ? 1768 ARG A C     1 
ATOM   2867  O  O     . ARG A 1 551  ? 156.854 176.481 122.485 1.00 14.07  ? 1768 ARG A O     1 
ATOM   2868  C  CB    . ARG A 1 551  ? 154.622 176.927 120.473 1.00 11.02  ? 1768 ARG A CB    1 
ATOM   2869  C  CG    . ARG A 1 551  ? 153.259 177.142 119.847 1.00 13.72  ? 1768 ARG A CG    1 
ATOM   2870  C  CD    . ARG A 1 551  ? 152.523 175.836 119.666 1.00 12.05  ? 1768 ARG A CD    1 
ATOM   2871  N  NE    . ARG A 1 551  ? 152.863 175.197 118.402 1.00 10.46  ? 1768 ARG A NE    1 
ATOM   2872  C  CZ    . ARG A 1 551  ? 152.694 173.907 118.153 1.00 9.77   ? 1768 ARG A CZ    1 
ATOM   2873  N  NH1   . ARG A 1 551  ? 152.218 173.085 119.071 1.00 7.25   ? 1768 ARG A NH1   1 
ATOM   2874  N  NH2   . ARG A 1 551  ? 153.019 173.428 116.957 1.00 10.78  ? 1768 ARG A NH2   1 
ATOM   2875  N  N     . LEU A 1 552  ? 156.209 174.361 122.076 1.00 9.77   ? 1769 LEU A N     1 
ATOM   2876  C  CA    . LEU A 1 552  ? 157.536 173.815 122.308 1.00 8.40   ? 1769 LEU A CA    1 
ATOM   2877  C  C     . LEU A 1 552  ? 158.479 174.215 121.183 1.00 8.48   ? 1769 LEU A C     1 
ATOM   2878  O  O     . LEU A 1 552  ? 158.095 174.253 120.012 1.00 10.03  ? 1769 LEU A O     1 
ATOM   2879  C  CB    . LEU A 1 552  ? 157.479 172.294 122.419 1.00 8.23   ? 1769 LEU A CB    1 
ATOM   2880  C  CG    . LEU A 1 552  ? 157.300 171.680 123.806 1.00 10.60  ? 1769 LEU A CG    1 
ATOM   2881  C  CD1   . LEU A 1 552  ? 155.879 171.842 124.311 1.00 10.63  ? 1769 LEU A CD1   1 
ATOM   2882  C  CD2   . LEU A 1 552  ? 157.695 170.221 123.759 1.00 8.32   ? 1769 LEU A CD2   1 
ATOM   2883  N  N     . ILE A 1 553  ? 159.721 174.519 121.549 1.00 6.39   ? 1770 ILE A N     1 
ATOM   2884  C  CA    . ILE A 1 553  ? 160.739 174.824 120.555 1.00 6.12   ? 1770 ILE A CA    1 
ATOM   2885  C  C     . ILE A 1 553  ? 161.152 173.537 119.859 1.00 7.33   ? 1770 ILE A C     1 
ATOM   2886  O  O     . ILE A 1 553  ? 161.404 172.514 120.508 1.00 8.22   ? 1770 ILE A O     1 
ATOM   2887  C  CB    . ILE A 1 553  ? 161.937 175.518 121.215 1.00 8.44   ? 1770 ILE A CB    1 
ATOM   2888  C  CG1   . ILE A 1 553  ? 161.491 176.814 121.893 1.00 8.82   ? 1770 ILE A CG1   1 
ATOM   2889  C  CG2   . ILE A 1 553  ? 163.029 175.776 120.201 1.00 9.62   ? 1770 ILE A CG2   1 
ATOM   2890  C  CD1   . ILE A 1 553  ? 161.004 177.867 120.935 1.00 9.58   ? 1770 ILE A CD1   1 
ATOM   2891  N  N     . TYR A 1 554  ? 161.219 173.579 118.531 1.00 9.55   ? 1771 TYR A N     1 
ATOM   2892  C  CA    . TYR A 1 554  ? 161.519 172.395 117.730 1.00 8.70   ? 1771 TYR A CA    1 
ATOM   2893  C  C     . TYR A 1 554  ? 163.010 172.099 117.808 1.00 8.20   ? 1771 TYR A C     1 
ATOM   2894  O  O     . TYR A 1 554  ? 163.819 172.715 117.112 1.00 10.00  ? 1771 TYR A O     1 
ATOM   2895  C  CB    . TYR A 1 554  ? 161.075 172.597 116.288 1.00 7.94   ? 1771 TYR A CB    1 
ATOM   2896  C  CG    . TYR A 1 554  ? 159.588 172.457 116.081 1.00 7.92   ? 1771 TYR A CG    1 
ATOM   2897  C  CD1   . TYR A 1 554  ? 158.721 173.482 116.425 1.00 8.99   ? 1771 TYR A CD1   1 
ATOM   2898  C  CD2   . TYR A 1 554  ? 159.053 171.302 115.536 1.00 9.40   ? 1771 TYR A CD2   1 
ATOM   2899  C  CE1   . TYR A 1 554  ? 157.364 173.358 116.236 1.00 10.38  ? 1771 TYR A CE1   1 
ATOM   2900  C  CE2   . TYR A 1 554  ? 157.696 171.169 115.343 1.00 10.54  ? 1771 TYR A CE2   1 
ATOM   2901  C  CZ    . TYR A 1 554  ? 156.857 172.200 115.694 1.00 10.59  ? 1771 TYR A CZ    1 
ATOM   2902  O  OH    . TYR A 1 554  ? 155.502 172.073 115.502 1.00 9.83   ? 1771 TYR A OH    1 
ATOM   2903  N  N     . THR A 1 555  ? 163.368 171.157 118.655 1.00 7.12   ? 1772 THR A N     1 
ATOM   2904  C  CA    . THR A 1 555  ? 164.700 170.597 118.767 1.00 8.32   ? 1772 THR A CA    1 
ATOM   2905  C  C     . THR A 1 555  ? 164.765 169.272 118.025 1.00 9.39   ? 1772 THR A C     1 
ATOM   2906  O  O     . THR A 1 555  ? 163.735 168.630 117.799 1.00 9.70   ? 1772 THR A O     1 
ATOM   2907  C  CB    . THR A 1 555  ? 165.066 170.389 120.241 1.00 9.48   ? 1772 THR A CB    1 
ATOM   2908  O  OG1   . THR A 1 555  ? 164.381 169.238 120.746 1.00 13.28  ? 1772 THR A OG1   1 
ATOM   2909  C  CG2   . THR A 1 555  ? 164.657 171.591 121.052 1.00 9.13   ? 1772 THR A CG2   1 
ATOM   2910  N  N     . PRO A 1 556  ? 165.957 168.848 117.589 1.00 9.26   ? 1773 PRO A N     1 
ATOM   2911  C  CA    . PRO A 1 556  ? 166.061 167.534 116.930 1.00 8.67   ? 1773 PRO A CA    1 
ATOM   2912  C  C     . PRO A 1 556  ? 165.576 166.375 117.785 1.00 8.13   ? 1773 PRO A C     1 
ATOM   2913  O  O     . PRO A 1 556  ? 164.980 165.432 117.251 1.00 10.04  ? 1773 PRO A O     1 
ATOM   2914  C  CB    . PRO A 1 556  ? 167.558 167.428 116.619 1.00 10.83  ? 1773 PRO A CB    1 
ATOM   2915  C  CG    . PRO A 1 556  ? 167.986 168.836 116.437 1.00 9.43   ? 1773 PRO A CG    1 
ATOM   2916  C  CD    . PRO A 1 556  ? 167.187 169.642 117.423 1.00 9.97   ? 1773 PRO A CD    1 
ATOM   2917  N  N     . LEU A 1 557  ? 165.797 166.423 119.100 1.00 8.07   ? 1774 LEU A N     1 
ATOM   2918  C  CA    . LEU A 1 557  ? 165.266 165.381 119.974 1.00 9.15   ? 1774 LEU A CA    1 
ATOM   2919  C  C     . LEU A 1 557  ? 163.743 165.397 119.987 1.00 8.65   ? 1774 LEU A C     1 
ATOM   2920  O  O     . LEU A 1 557  ? 163.107 164.340 120.060 1.00 9.76   ? 1774 LEU A O     1 
ATOM   2921  C  CB    . LEU A 1 557  ? 165.816 165.544 121.390 1.00 11.54  ? 1774 LEU A CB    1 
ATOM   2922  C  CG    . LEU A 1 557  ? 165.249 164.588 122.444 1.00 14.79  ? 1774 LEU A CG    1 
ATOM   2923  C  CD1   . LEU A 1 557  ? 165.535 163.136 122.076 1.00 11.91  ? 1774 LEU A CD1   1 
ATOM   2924  C  CD2   . LEU A 1 557  ? 165.775 164.914 123.831 1.00 20.39  ? 1774 LEU A CD2   1 
ATOM   2925  N  N     . LEU A 1 558  ? 163.140 166.586 119.909 1.00 6.96   ? 1775 LEU A N     1 
ATOM   2926  C  CA    . LEU A 1 558  ? 161.685 166.673 119.831 1.00 6.41   ? 1775 LEU A CA    1 
ATOM   2927  C  C     . LEU A 1 558  ? 161.164 166.026 118.554 1.00 7.35   ? 1775 LEU A C     1 
ATOM   2928  O  O     . LEU A 1 558  ? 160.147 165.324 118.573 1.00 10.35  ? 1775 LEU A O     1 
ATOM   2929  C  CB    . LEU A 1 558  ? 161.241 168.132 119.915 1.00 6.34   ? 1775 LEU A CB    1 
ATOM   2930  C  CG    . LEU A 1 558  ? 159.739 168.394 119.839 1.00 5.38   ? 1775 LEU A CG    1 
ATOM   2931  C  CD1   . LEU A 1 558  ? 159.052 167.855 121.071 1.00 6.68   ? 1775 LEU A CD1   1 
ATOM   2932  C  CD2   . LEU A 1 558  ? 159.468 169.873 119.688 1.00 7.25   ? 1775 LEU A CD2   1 
ATOM   2933  N  N     . LEU A 1 559  ? 161.858 166.235 117.434 1.00 6.70   ? 1776 LEU A N     1 
ATOM   2934  C  CA    . LEU A 1 559  ? 161.430 165.616 116.185 1.00 6.12   ? 1776 LEU A CA    1 
ATOM   2935  C  C     . LEU A 1 559  ? 161.660 164.110 116.190 1.00 6.09   ? 1776 LEU A C     1 
ATOM   2936  O  O     . LEU A 1 559  ? 160.879 163.368 115.590 1.00 7.83   ? 1776 LEU A O     1 
ATOM   2937  C  CB    . LEU A 1 559  ? 162.144 166.266 115.004 1.00 5.55   ? 1776 LEU A CB    1 
ATOM   2938  C  CG    . LEU A 1 559  ? 161.657 167.676 114.679 1.00 5.07   ? 1776 LEU A CG    1 
ATOM   2939  C  CD1   . LEU A 1 559  ? 162.609 168.362 113.721 1.00 5.18   ? 1776 LEU A CD1   1 
ATOM   2940  C  CD2   . LEU A 1 559  ? 160.253 167.634 114.109 1.00 5.10   ? 1776 LEU A CD2   1 
ATOM   2941  N  N     . VAL A 1 560  ? 162.709 163.634 116.865 1.00 5.89   ? 1777 VAL A N     1 
ATOM   2942  C  CA    . VAL A 1 560  ? 162.903 162.190 116.992 1.00 5.73   ? 1777 VAL A CA    1 
ATOM   2943  C  C     . VAL A 1 560  ? 161.819 161.580 117.878 1.00 6.10   ? 1777 VAL A C     1 
ATOM   2944  O  O     . VAL A 1 560  ? 161.341 160.466 117.623 1.00 7.96   ? 1777 VAL A O     1 
ATOM   2945  C  CB    . VAL A 1 560  ? 164.322 161.886 117.508 1.00 6.37   ? 1777 VAL A CB    1 
ATOM   2946  C  CG1   . VAL A 1 560  ? 164.500 160.410 117.757 1.00 5.76   ? 1777 VAL A CG1   1 
ATOM   2947  C  CG2   . VAL A 1 560  ? 165.350 162.345 116.496 1.00 6.45   ? 1777 VAL A CG2   1 
ATOM   2948  N  N     . GLY A 1 561  ? 161.404 162.300 118.923 1.00 5.50   ? 1778 GLY A N     1 
ATOM   2949  C  CA    . GLY A 1 561  ? 160.262 161.858 119.709 1.00 5.25   ? 1778 GLY A CA    1 
ATOM   2950  C  C     . GLY A 1 561  ? 158.981 161.822 118.897 1.00 5.57   ? 1778 GLY A C     1 
ATOM   2951  O  O     . GLY A 1 561  ? 158.169 160.903 119.034 1.00 6.80   ? 1778 GLY A O     1 
ATOM   2952  N  N     . PHE A 1 562  ? 158.792 162.817 118.028 1.00 5.32   ? 1779 PHE A N     1 
ATOM   2953  C  CA    . PHE A 1 562  ? 157.662 162.799 117.103 1.00 5.65   ? 1779 PHE A CA    1 
ATOM   2954  C  C     . PHE A 1 562  ? 157.729 161.585 116.186 1.00 6.39   ? 1779 PHE A C     1 
ATOM   2955  O  O     . PHE A 1 562  ? 156.711 160.935 115.927 1.00 7.37   ? 1779 PHE A O     1 
ATOM   2956  C  CB    . PHE A 1 562  ? 157.642 164.079 116.268 1.00 4.87   ? 1779 PHE A CB    1 
ATOM   2957  C  CG    . PHE A 1 562  ? 157.176 165.297 117.012 1.00 6.49   ? 1779 PHE A CG    1 
ATOM   2958  C  CD1   . PHE A 1 562  ? 156.673 165.202 118.295 1.00 4.36   ? 1779 PHE A CD1   1 
ATOM   2959  C  CD2   . PHE A 1 562  ? 157.247 166.543 116.420 1.00 4.80   ? 1779 PHE A CD2   1 
ATOM   2960  C  CE1   . PHE A 1 562  ? 156.252 166.326 118.969 1.00 5.39   ? 1779 PHE A CE1   1 
ATOM   2961  C  CE2   . PHE A 1 562  ? 156.827 167.667 117.089 1.00 5.47   ? 1779 PHE A CE2   1 
ATOM   2962  C  CZ    . PHE A 1 562  ? 156.329 167.558 118.365 1.00 5.17   ? 1779 PHE A CZ    1 
ATOM   2963  N  N     . ALA A 1 563  ? 158.926 161.269 115.689 1.00 6.10   ? 1780 ALA A N     1 
ATOM   2964  C  CA    . ALA A 1 563  ? 159.094 160.138 114.782 1.00 5.63   ? 1780 ALA A CA    1 
ATOM   2965  C  C     . ALA A 1 563  ? 158.785 158.815 115.468 1.00 6.94   ? 1780 ALA A C     1 
ATOM   2966  O  O     . ALA A 1 563  ? 158.112 157.955 114.891 1.00 6.49   ? 1780 ALA A O     1 
ATOM   2967  C  CB    . ALA A 1 563  ? 160.512 160.127 114.217 1.00 7.82   ? 1780 ALA A CB    1 
ATOM   2968  N  N     . THR A 1 564  ? 159.264 158.624 116.700 1.00 5.07   ? 1781 THR A N     1 
ATOM   2969  C  CA    . THR A 1 564  ? 158.986 157.355 117.366 1.00 6.34   ? 1781 THR A CA    1 
ATOM   2970  C  C     . THR A 1 564  ? 157.529 157.261 117.807 1.00 7.33   ? 1781 THR A C     1 
ATOM   2971  O  O     . THR A 1 564  ? 156.961 156.162 117.813 1.00 9.95   ? 1781 THR A O     1 
ATOM   2972  C  CB    . THR A 1 564  ? 159.925 157.122 118.552 1.00 6.92   ? 1781 THR A CB    1 
ATOM   2973  O  OG1   . THR A 1 564  ? 159.539 155.920 119.230 1.00 6.71   ? 1781 THR A OG1   1 
ATOM   2974  C  CG2   . THR A 1 564  ? 159.875 158.258 119.532 1.00 7.18   ? 1781 THR A CG2   1 
ATOM   2975  N  N     . LEU A 1 565  ? 156.894 158.391 118.140 1.00 6.57   ? 1782 LEU A N     1 
ATOM   2976  C  CA    . LEU A 1 565  ? 155.460 158.359 118.408 1.00 6.60   ? 1782 LEU A CA    1 
ATOM   2977  C  C     . LEU A 1 565  ? 154.675 158.009 117.149 1.00 6.60   ? 1782 LEU A C     1 
ATOM   2978  O  O     . LEU A 1 565  ? 153.702 157.249 117.211 1.00 7.32   ? 1782 LEU A O     1 
ATOM   2979  C  CB    . LEU A 1 565  ? 155.003 159.700 118.979 1.00 6.31   ? 1782 LEU A CB    1 
ATOM   2980  C  CG    . LEU A 1 565  ? 155.325 159.954 120.453 1.00 5.32   ? 1782 LEU A CG    1 
ATOM   2981  C  CD1   . LEU A 1 565  ? 154.780 161.295 120.900 1.00 7.12   ? 1782 LEU A CD1   1 
ATOM   2982  C  CD2   . LEU A 1 565  ? 154.768 158.846 121.316 1.00 4.88   ? 1782 LEU A CD2   1 
ATOM   2983  N  N     . THR A 1 566  ? 155.095 158.538 115.996 1.00 6.57   ? 1783 THR A N     1 
ATOM   2984  C  CA    . THR A 1 566  ? 154.462 158.185 114.728 1.00 6.24   ? 1783 THR A CA    1 
ATOM   2985  C  C     . THR A 1 566  ? 154.635 156.702 114.420 1.00 7.36   ? 1783 THR A C     1 
ATOM   2986  O  O     . THR A 1 566  ? 153.692 156.037 113.972 1.00 8.90   ? 1783 THR A O     1 
ATOM   2987  C  CB    . THR A 1 566  ? 155.048 159.042 113.603 1.00 6.13   ? 1783 THR A CB    1 
ATOM   2988  O  OG1   . THR A 1 566  ? 154.618 160.399 113.758 1.00 6.22   ? 1783 THR A OG1   1 
ATOM   2989  C  CG2   . THR A 1 566  ? 154.604 158.540 112.244 1.00 6.44   ? 1783 THR A CG2   1 
ATOM   2990  N  N     . ASP A 1 567  ? 155.834 156.166 114.666 1.00 8.40   ? 1784 ASP A N     1 
ATOM   2991  C  CA    . ASP A 1 567  ? 156.084 154.744 114.448 1.00 9.36   ? 1784 ASP A CA    1 
ATOM   2992  C  C     . ASP A 1 567  ? 155.212 153.881 115.350 1.00 8.45   ? 1784 ASP A C     1 
ATOM   2993  O  O     . ASP A 1 567  ? 154.692 152.848 114.916 1.00 11.36  ? 1784 ASP A O     1 
ATOM   2994  C  CB    . ASP A 1 567  ? 157.557 154.424 114.688 1.00 9.41   ? 1784 ASP A CB    1 
ATOM   2995  C  CG    . ASP A 1 567  ? 158.471 155.097 113.693 1.00 11.20  ? 1784 ASP A CG    1 
ATOM   2996  O  OD1   . ASP A 1 567  ? 157.991 155.945 112.912 1.00 10.05  ? 1784 ASP A OD1   1 
ATOM   2997  O  OD2   . ASP A 1 567  ? 159.677 154.783 113.701 1.00 10.39  ? 1784 ASP A OD2   1 
ATOM   2998  N  N     . SER A 1 568  ? 155.057 154.280 116.613 1.00 7.05   ? 1785 SER A N     1 
ATOM   2999  C  CA    . SER A 1 568  ? 154.199 153.522 117.517 1.00 8.49   ? 1785 SER A CA    1 
ATOM   3000  C  C     . SER A 1 568  ? 152.737 153.602 117.095 1.00 12.65  ? 1785 SER A C     1 
ATOM   3001  O  O     . SER A 1 568  ? 152.006 152.612 117.186 1.00 15.20  ? 1785 SER A O     1 
ATOM   3002  C  CB    . SER A 1 568  ? 154.375 154.025 118.947 1.00 9.50   ? 1785 SER A CB    1 
ATOM   3003  O  OG    . SER A 1 568  ? 155.748 154.148 119.272 1.00 11.27  ? 1785 SER A OG    1 
ATOM   3004  N  N     . LEU A 1 569  ? 152.293 154.768 116.623 1.00 13.74  ? 1786 LEU A N     1 
ATOM   3005  C  CA    . LEU A 1 569  ? 150.893 154.929 116.246 1.00 10.48  ? 1786 LEU A CA    1 
ATOM   3006  C  C     . LEU A 1 569  ? 150.556 154.253 114.925 1.00 11.40  ? 1786 LEU A C     1 
ATOM   3007  O  O     . LEU A 1 569  ? 149.396 153.889 114.708 1.00 16.90  ? 1786 LEU A O     1 
ATOM   3008  C  CB    . LEU A 1 569  ? 150.532 156.410 116.160 1.00 8.37   ? 1786 LEU A CB    1 
ATOM   3009  C  CG    . LEU A 1 569  ? 150.491 157.166 117.483 1.00 8.96   ? 1786 LEU A CG    1 
ATOM   3010  C  CD1   . LEU A 1 569  ? 150.139 158.613 117.232 1.00 9.06   ? 1786 LEU A CD1   1 
ATOM   3011  C  CD2   . LEU A 1 569  ? 149.506 156.514 118.433 1.00 9.02   ? 1786 LEU A CD2   1 
ATOM   3012  N  N     . HIS A 1 570  ? 151.534 154.095 114.030 1.00 10.44  ? 1787 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 570  ? 151.235 153.566 112.703 1.00 10.82  ? 1787 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 570  ? 150.790 152.111 112.754 1.00 12.97  ? 1787 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 570  ? 149.999 151.680 111.908 1.00 14.36  ? 1787 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 570  ? 152.448 153.710 111.789 1.00 10.43  ? 1787 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 570  ? 152.225 153.181 110.408 1.00 9.80   ? 1787 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 570  ? 152.739 151.976 109.981 1.00 10.08  ? 1787 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 570  ? 151.548 153.695 109.354 1.00 10.06  ? 1787 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 570  ? 152.386 151.769 108.725 1.00 9.73   ? 1787 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 570  ? 151.663 152.798 108.321 1.00 9.68   ? 1787 HIS A NE2   1 
ATOM   3022  N  N     . GLN A 1 571  ? 151.274 151.342 113.727 1.00 13.50  ? 1788 GLN A N     1 
ATOM   3023  C  CA    . GLN A 1 571  ? 150.829 149.969 113.910 1.00 15.17  ? 1788 GLN A CA    1 
ATOM   3024  C  C     . GLN A 1 571  ? 149.900 149.823 115.102 1.00 17.69  ? 1788 GLN A C     1 
ATOM   3025  O  O     . GLN A 1 571  ? 149.768 148.721 115.644 1.00 20.11  ? 1788 GLN A O     1 
ATOM   3026  C  CB    . GLN A 1 571  ? 152.021 149.034 114.070 1.00 15.07  ? 1788 GLN A CB    1 
ATOM   3027  C  CG    . GLN A 1 571  ? 152.873 148.926 112.844 1.00 14.47  ? 1788 GLN A CG    1 
ATOM   3028  C  CD    . GLN A 1 571  ? 154.025 147.990 113.060 1.00 22.97  ? 1788 GLN A CD    1 
ATOM   3029  O  OE1   . GLN A 1 571  ? 154.208 147.461 114.146 1.00 30.18  ? 1788 GLN A OE1   1 
ATOM   3030  N  NE2   . GLN A 1 571  ? 154.822 147.796 112.037 1.00 21.69  ? 1788 GLN A NE2   1 
ATOM   3031  N  N     . LYS A 1 572  ? 149.269 150.921 115.521 1.00 15.69  ? 1789 LYS A N     1 
ATOM   3032  C  CA    . LYS A 1 572  ? 148.315 150.949 116.630 1.00 18.03  ? 1789 LYS A CA    1 
ATOM   3033  C  C     . LYS A 1 572  ? 148.934 150.438 117.928 1.00 20.89  ? 1789 LYS A C     1 
ATOM   3034  O  O     . LYS A 1 572  ? 148.249 149.854 118.769 1.00 24.12  ? 1789 LYS A O     1 
ATOM   3035  C  CB    . LYS A 1 572  ? 147.035 150.172 116.296 1.00 19.53  ? 1789 LYS A CB    1 
ATOM   3036  C  CG    . LYS A 1 572  ? 146.531 150.354 114.866 1.00 19.29  ? 1789 LYS A CG    1 
ATOM   3037  C  CD    . LYS A 1 572  ? 146.311 151.819 114.513 1.00 18.04  ? 1789 LYS A CD    1 
ATOM   3038  C  CE    . LYS A 1 572  ? 146.050 151.986 113.025 1.00 18.13  ? 1789 LYS A CE    1 
ATOM   3039  N  NZ    . LYS A 1 572  ? 146.046 153.416 112.612 1.00 17.59  ? 1789 LYS A NZ    1 
ATOM   3040  N  N     . TYR A 1 573  ? 150.236 150.650 118.094 1.00 20.36  ? 1790 TYR A N     1 
ATOM   3041  C  CA    . TYR A 1 573  ? 150.905 150.413 119.365 1.00 18.72  ? 1790 TYR A CA    1 
ATOM   3042  C  C     . TYR A 1 573  ? 150.725 151.645 120.249 1.00 19.18  ? 1790 TYR A C     1 
ATOM   3043  O  O     . TYR A 1 573  ? 149.914 152.530 119.968 1.00 23.57  ? 1790 TYR A O     1 
ATOM   3044  C  CB    . TYR A 1 573  ? 152.378 150.076 119.144 1.00 17.94  ? 1790 TYR A CB    1 
ATOM   3045  C  CG    . TYR A 1 573  ? 152.646 148.611 118.893 1.00 22.78  ? 1790 TYR A CG    1 
ATOM   3046  C  CD1   . TYR A 1 573  ? 151.907 147.898 117.959 1.00 25.52  ? 1790 TYR A CD1   1 
ATOM   3047  C  CD2   . TYR A 1 573  ? 153.627 147.937 119.603 1.00 22.67  ? 1790 TYR A CD2   1 
ATOM   3048  C  CE1   . TYR A 1 573  ? 152.146 146.557 117.732 1.00 27.71  ? 1790 TYR A CE1   1 
ATOM   3049  C  CE2   . TYR A 1 573  ? 153.869 146.598 119.388 1.00 24.26  ? 1790 TYR A CE2   1 
ATOM   3050  C  CZ    . TYR A 1 573  ? 153.130 145.913 118.449 1.00 26.64  ? 1790 TYR A CZ    1 
ATOM   3051  O  OH    . TYR A 1 573  ? 153.373 144.577 118.230 1.00 25.12  ? 1790 TYR A OH    1 
ATOM   3052  N  N     . GLY A 1 574  ? 151.469 151.712 121.339 1.00 18.56  ? 1791 GLY A N     1 
ATOM   3053  C  CA    . GLY A 1 574  ? 151.436 152.860 122.230 1.00 13.38  ? 1791 GLY A CA    1 
ATOM   3054  C  C     . GLY A 1 574  ? 152.825 153.440 122.398 1.00 12.00  ? 1791 GLY A C     1 
ATOM   3055  O  O     . GLY A 1 574  ? 153.792 152.702 122.590 1.00 18.91  ? 1791 GLY A O     1 
ATOM   3056  N  N     . GLY A 1 575  ? 152.919 154.760 122.314 1.00 7.37   ? 1792 GLY A N     1 
ATOM   3057  C  CA    . GLY A 1 575  ? 154.196 155.414 122.498 1.00 6.64   ? 1792 GLY A CA    1 
ATOM   3058  C  C     . GLY A 1 575  ? 154.566 155.551 123.958 1.00 5.91   ? 1792 GLY A C     1 
ATOM   3059  O  O     . GLY A 1 575  ? 153.800 156.111 124.745 1.00 9.49   ? 1792 GLY A O     1 
ATOM   3060  N  N     . CYS A 1 576  ? 155.734 155.047 124.334 1.00 6.11   ? 1793 CYS A N     1 
ATOM   3061  C  CA    . CYS A 1 576  ? 156.205 155.113 125.707 1.00 7.34   ? 1793 CYS A CA    1 
ATOM   3062  C  C     . CYS A 1 576  ? 157.463 155.965 125.786 1.00 8.99   ? 1793 CYS A C     1 
ATOM   3063  O  O     . CYS A 1 576  ? 158.242 156.044 124.833 1.00 12.71  ? 1793 CYS A O     1 
ATOM   3064  C  CB    . CYS A 1 576  ? 156.482 153.715 126.266 1.00 9.23   ? 1793 CYS A CB    1 
ATOM   3065  S  SG    . CYS A 1 576  ? 156.886 153.685 128.025 1.00 10.49  ? 1793 CYS A SG    1 
ATOM   3066  N  N     . PHE A 1 577  ? 157.651 156.608 126.933 1.00 6.88   ? 1794 PHE A N     1 
ATOM   3067  C  CA    . PHE A 1 577  ? 158.780 157.496 127.165 1.00 7.08   ? 1794 PHE A CA    1 
ATOM   3068  C  C     . PHE A 1 577  ? 159.351 157.211 128.542 1.00 11.73  ? 1794 PHE A C     1 
ATOM   3069  O  O     . PHE A 1 577  ? 158.605 157.158 129.524 1.00 18.20  ? 1794 PHE A O     1 
ATOM   3070  C  CB    . PHE A 1 577  ? 158.355 158.962 127.074 1.00 7.78   ? 1794 PHE A CB    1 
ATOM   3071  C  CG    . PHE A 1 577  ? 158.288 159.493 125.675 1.00 8.23   ? 1794 PHE A CG    1 
ATOM   3072  C  CD1   . PHE A 1 577  ? 159.210 159.100 124.725 1.00 7.91   ? 1794 PHE A CD1   1 
ATOM   3073  C  CD2   . PHE A 1 577  ? 157.303 160.392 125.313 1.00 7.56   ? 1794 PHE A CD2   1 
ATOM   3074  C  CE1   . PHE A 1 577  ? 159.150 159.593 123.439 1.00 7.41   ? 1794 PHE A CE1   1 
ATOM   3075  C  CE2   . PHE A 1 577  ? 157.239 160.886 124.030 1.00 7.17   ? 1794 PHE A CE2   1 
ATOM   3076  C  CZ    . PHE A 1 577  ? 158.163 160.486 123.092 1.00 6.33   ? 1794 PHE A CZ    1 
ATOM   3077  N  N     . PHE A 1 578  ? 160.668 157.035 128.621 1.00 13.80  ? 1795 PHE A N     1 
ATOM   3078  C  CA    . PHE A 1 578  ? 161.323 156.863 129.907 1.00 15.65  ? 1795 PHE A CA    1 
ATOM   3079  C  C     . PHE A 1 578  ? 162.606 157.679 129.932 1.00 16.56  ? 1795 PHE A C     1 
ATOM   3080  O  O     . PHE A 1 578  ? 163.166 158.032 128.892 1.00 18.42  ? 1795 PHE A O     1 
ATOM   3081  C  CB    . PHE A 1 578  ? 161.593 155.380 130.228 1.00 17.60  ? 1795 PHE A CB    1 
ATOM   3082  C  CG    . PHE A 1 578  ? 162.608 154.719 129.334 1.00 18.45  ? 1795 PHE A CG    1 
ATOM   3083  C  CD1   . PHE A 1 578  ? 163.956 154.723 129.661 1.00 17.85  ? 1795 PHE A CD1   1 
ATOM   3084  C  CD2   . PHE A 1 578  ? 162.209 154.058 128.188 1.00 16.48  ? 1795 PHE A CD2   1 
ATOM   3085  C  CE1   . PHE A 1 578  ? 164.884 154.110 128.846 1.00 16.29  ? 1795 PHE A CE1   1 
ATOM   3086  C  CE2   . PHE A 1 578  ? 163.134 153.443 127.369 1.00 13.92  ? 1795 PHE A CE2   1 
ATOM   3087  C  CZ    . PHE A 1 578  ? 164.471 153.468 127.701 1.00 16.08  ? 1795 PHE A CZ    1 
ATOM   3088  N  N     . GLY A 1 579  ? 163.058 157.982 131.144 1.00 19.34  ? 1796 GLY A N     1 
ATOM   3089  C  CA    . GLY A 1 579  ? 164.239 158.783 131.349 1.00 24.26  ? 1796 GLY A CA    1 
ATOM   3090  C  C     . GLY A 1 579  ? 164.224 159.440 132.712 1.00 29.12  ? 1796 GLY A C     1 
ATOM   3091  O  O     . GLY A 1 579  ? 163.443 159.070 133.594 1.00 31.81  ? 1796 GLY A O     1 
ATOM   3092  N  N     . PRO A 1 580  ? 165.094 160.424 132.918 1.00 27.30  ? 1797 PRO A N     1 
ATOM   3093  C  CA    . PRO A 1 580  ? 165.081 161.168 134.180 1.00 28.03  ? 1797 PRO A CA    1 
ATOM   3094  C  C     . PRO A 1 580  ? 163.866 162.079 134.263 1.00 28.37  ? 1797 PRO A C     1 
ATOM   3095  O  O     . PRO A 1 580  ? 163.094 162.231 133.317 1.00 30.17  ? 1797 PRO A O     1 
ATOM   3096  C  CB    . PRO A 1 580  ? 166.384 161.969 134.134 1.00 28.09  ? 1797 PRO A CB    1 
ATOM   3097  C  CG    . PRO A 1 580  ? 166.668 162.127 132.682 1.00 25.99  ? 1797 PRO A CG    1 
ATOM   3098  C  CD    . PRO A 1 580  ? 166.175 160.870 132.023 1.00 26.36  ? 1797 PRO A CD    1 
ATOM   3099  N  N     . ALA A 1 581  ? 163.700 162.689 135.432 1.00 27.82  ? 1798 ALA A N     1 
ATOM   3100  C  CA    . ALA A 1 581  ? 162.584 163.595 135.654 1.00 26.66  ? 1798 ALA A CA    1 
ATOM   3101  C  C     . ALA A 1 581  ? 162.863 164.951 135.019 1.00 25.68  ? 1798 ALA A C     1 
ATOM   3102  O  O     . ALA A 1 581  ? 163.991 165.449 135.052 1.00 26.27  ? 1798 ALA A O     1 
ATOM   3103  C  CB    . ALA A 1 581  ? 162.317 163.762 137.149 1.00 27.11  ? 1798 ALA A CB    1 
ATOM   3104  N  N     . GLY A 1 582  ? 161.822 165.545 134.441 1.00 25.17  ? 1799 GLY A N     1 
ATOM   3105  C  CA    . GLY A 1 582  ? 161.931 166.852 133.823 1.00 25.68  ? 1799 GLY A CA    1 
ATOM   3106  C  C     . GLY A 1 582  ? 162.833 166.903 132.608 1.00 24.25  ? 1799 GLY A C     1 
ATOM   3107  O  O     . GLY A 1 582  ? 163.671 167.802 132.493 1.00 22.83  ? 1799 GLY A O     1 
ATOM   3108  N  N     . THR A 1 583  ? 162.679 165.945 131.696 1.00 21.20  ? 1800 THR A N     1 
ATOM   3109  C  CA    . THR A 1 583  ? 163.499 165.885 130.492 1.00 18.32  ? 1800 THR A CA    1 
ATOM   3110  C  C     . THR A 1 583  ? 162.704 166.102 129.209 1.00 18.21  ? 1800 THR A C     1 
ATOM   3111  O  O     . THR A 1 583  ? 163.231 165.855 128.119 1.00 19.32  ? 1800 THR A O     1 
ATOM   3112  C  CB    . THR A 1 583  ? 164.247 164.552 130.430 1.00 20.55  ? 1800 THR A CB    1 
ATOM   3113  O  OG1   . THR A 1 583  ? 165.157 164.571 129.327 1.00 22.92  ? 1800 THR A OG1   1 
ATOM   3114  C  CG2   . THR A 1 583  ? 163.285 163.398 130.266 1.00 22.19  ? 1800 THR A CG2   1 
ATOM   3115  N  N     . GLY A 1 584  ? 161.460 166.564 129.303 1.00 17.54  ? 1801 GLY A N     1 
ATOM   3116  C  CA    . GLY A 1 584  ? 160.711 166.926 128.115 1.00 13.36  ? 1801 GLY A CA    1 
ATOM   3117  C  C     . GLY A 1 584  ? 159.923 165.796 127.487 1.00 13.62  ? 1801 GLY A C     1 
ATOM   3118  O  O     . GLY A 1 584  ? 159.963 165.617 126.269 1.00 11.75  ? 1801 GLY A O     1 
ATOM   3119  N  N     . LYS A 1 585  ? 159.195 165.033 128.301 1.00 14.29  ? 1802 LYS A N     1 
ATOM   3120  C  CA    . LYS A 1 585  ? 158.419 163.902 127.802 1.00 8.82   ? 1802 LYS A CA    1 
ATOM   3121  C  C     . LYS A 1 585  ? 156.944 164.257 127.643 1.00 8.40   ? 1802 LYS A C     1 
ATOM   3122  O  O     . LYS A 1 585  ? 156.377 164.119 126.552 1.00 10.49  ? 1802 LYS A O     1 
ATOM   3123  C  CB    . LYS A 1 585  ? 158.587 162.707 128.744 1.00 9.10   ? 1802 LYS A CB    1 
ATOM   3124  C  CG    . LYS A 1 585  ? 160.028 162.412 129.090 1.00 10.14  ? 1802 LYS A CG    1 
ATOM   3125  C  CD    . LYS A 1 585  ? 160.155 161.184 129.965 1.00 13.98  ? 1802 LYS A CD    1 
ATOM   3126  C  CE    . LYS A 1 585  ? 159.414 161.371 131.274 1.00 15.75  ? 1802 LYS A CE    1 
ATOM   3127  N  NZ    . LYS A 1 585  ? 160.076 162.378 132.141 1.00 18.78  ? 1802 LYS A NZ    1 
ATOM   3128  N  N     . THR A 1 586  ? 156.313 164.709 128.730 1.00 8.13   ? 1803 THR A N     1 
ATOM   3129  C  CA    . THR A 1 586  ? 154.904 165.086 128.677 1.00 7.64   ? 1803 THR A CA    1 
ATOM   3130  C  C     . THR A 1 586  ? 154.686 166.261 127.736 1.00 8.34   ? 1803 THR A C     1 
ATOM   3131  O  O     . THR A 1 586  ? 153.705 166.292 126.984 1.00 10.60  ? 1803 THR A O     1 
ATOM   3132  C  CB    . THR A 1 586  ? 154.402 165.427 130.076 1.00 11.06  ? 1803 THR A CB    1 
ATOM   3133  O  OG1   . THR A 1 586  ? 154.835 164.417 130.993 1.00 14.86  ? 1803 THR A OG1   1 
ATOM   3134  C  CG2   . THR A 1 586  ? 152.888 165.499 130.091 1.00 12.23  ? 1803 THR A CG2   1 
ATOM   3135  N  N     . GLU A 1 587  ? 155.598 167.232 127.759 1.00 9.16   ? 1804 GLU A N     1 
ATOM   3136  C  CA    . GLU A 1 587  ? 155.508 168.345 126.825 1.00 9.21   ? 1804 GLU A CA    1 
ATOM   3137  C  C     . GLU A 1 587  ? 155.690 167.883 125.386 1.00 7.95   ? 1804 GLU A C     1 
ATOM   3138  O  O     . GLU A 1 587  ? 155.059 168.434 124.481 1.00 9.57   ? 1804 GLU A O     1 
ATOM   3139  C  CB    . GLU A 1 587  ? 156.537 169.413 127.182 1.00 9.86   ? 1804 GLU A CB    1 
ATOM   3140  C  CG    . GLU A 1 587  ? 156.439 169.896 128.618 1.00 14.15  ? 1804 GLU A CG    1 
ATOM   3141  C  CD    . GLU A 1 587  ? 155.384 170.967 128.803 1.00 19.59  ? 1804 GLU A CD    1 
ATOM   3142  O  OE1   . GLU A 1 587  ? 155.599 172.103 128.331 1.00 21.89  ? 1804 GLU A OE1   1 
ATOM   3143  O  OE2   . GLU A 1 587  ? 154.339 170.673 129.421 1.00 22.40  ? 1804 GLU A OE2   1 
ATOM   3144  N  N     . THR A 1 588  ? 156.535 166.875 125.152 1.00 6.94   ? 1805 THR A N     1 
ATOM   3145  C  CA    . THR A 1 588  ? 156.698 166.345 123.800 1.00 5.54   ? 1805 THR A CA    1 
ATOM   3146  C  C     . THR A 1 588  ? 155.424 165.662 123.315 1.00 6.79   ? 1805 THR A C     1 
ATOM   3147  O  O     . THR A 1 588  ? 155.012 165.847 122.162 1.00 9.79   ? 1805 THR A O     1 
ATOM   3148  C  CB    . THR A 1 588  ? 157.882 165.378 123.757 1.00 6.05   ? 1805 THR A CB    1 
ATOM   3149  O  OG1   . THR A 1 588  ? 159.103 166.117 123.867 1.00 8.30   ? 1805 THR A OG1   1 
ATOM   3150  C  CG2   . THR A 1 588  ? 157.899 164.588 122.463 1.00 5.23   ? 1805 THR A CG2   1 
ATOM   3151  N  N     . VAL A 1 589  ? 154.773 164.891 124.190 1.00 6.80   ? 1806 VAL A N     1 
ATOM   3152  C  CA    . VAL A 1 589  ? 153.497 164.271 123.831 1.00 6.15   ? 1806 VAL A CA    1 
ATOM   3153  C  C     . VAL A 1 589  ? 152.448 165.338 123.542 1.00 6.92   ? 1806 VAL A C     1 
ATOM   3154  O  O     . VAL A 1 589  ? 151.682 165.239 122.571 1.00 8.75   ? 1806 VAL A O     1 
ATOM   3155  C  CB    . VAL A 1 589  ? 153.038 163.314 124.946 1.00 5.90   ? 1806 VAL A CB    1 
ATOM   3156  C  CG1   . VAL A 1 589  ? 151.674 162.747 124.627 1.00 7.52   ? 1806 VAL A CG1   1 
ATOM   3157  C  CG2   . VAL A 1 589  ? 154.045 162.196 125.134 1.00 5.40   ? 1806 VAL A CG2   1 
ATOM   3158  N  N     . LYS A 1 590  ? 152.407 166.383 124.372 1.00 5.43   ? 1807 LYS A N     1 
ATOM   3159  C  CA    . LYS A 1 590  ? 151.437 167.453 124.176 1.00 5.62   ? 1807 LYS A CA    1 
ATOM   3160  C  C     . LYS A 1 590  ? 151.697 168.212 122.880 1.00 6.47   ? 1807 LYS A C     1 
ATOM   3161  O  O     . LYS A 1 590  ? 150.754 168.585 122.179 1.00 12.02  ? 1807 LYS A O     1 
ATOM   3162  C  CB    . LYS A 1 590  ? 151.456 168.398 125.374 1.00 5.88   ? 1807 LYS A CB    1 
ATOM   3163  C  CG    . LYS A 1 590  ? 150.684 167.874 126.573 1.00 7.78   ? 1807 LYS A CG    1 
ATOM   3164  C  CD    . LYS A 1 590  ? 150.436 168.965 127.597 1.00 11.59  ? 1807 LYS A CD    1 
ATOM   3165  C  CE    . LYS A 1 590  ? 149.286 169.864 127.176 1.00 15.32  ? 1807 LYS A CE    1 
ATOM   3166  N  NZ    . LYS A 1 590  ? 147.967 169.181 127.284 1.00 14.47  ? 1807 LYS A NZ    1 
ATOM   3167  N  N     . ALA A 1 591  ? 152.967 168.437 122.536 1.00 5.20   ? 1808 ALA A N     1 
ATOM   3168  C  CA    . ALA A 1 591  ? 153.286 169.110 121.281 1.00 5.52   ? 1808 ALA A CA    1 
ATOM   3169  C  C     . ALA A 1 591  ? 152.948 168.244 120.076 1.00 6.56   ? 1808 ALA A C     1 
ATOM   3170  O  O     . ALA A 1 591  ? 152.533 168.768 119.038 1.00 9.80   ? 1808 ALA A O     1 
ATOM   3171  C  CB    . ALA A 1 591  ? 154.759 169.505 121.252 1.00 4.32   ? 1808 ALA A CB    1 
ATOM   3172  N  N     . PHE A 1 592  ? 153.124 166.926 120.192 1.00 5.76   ? 1809 PHE A N     1 
ATOM   3173  C  CA    . PHE A 1 592  ? 152.686 166.018 119.135 1.00 6.32   ? 1809 PHE A CA    1 
ATOM   3174  C  C     . PHE A 1 592  ? 151.181 166.123 118.925 1.00 8.00   ? 1809 PHE A C     1 
ATOM   3175  O  O     . PHE A 1 592  ? 150.701 166.238 117.788 1.00 10.73  ? 1809 PHE A O     1 
ATOM   3176  C  CB    . PHE A 1 592  ? 153.090 164.589 119.499 1.00 5.85   ? 1809 PHE A CB    1 
ATOM   3177  C  CG    . PHE A 1 592  ? 153.003 163.615 118.362 1.00 5.37   ? 1809 PHE A CG    1 
ATOM   3178  C  CD1   . PHE A 1 592  ? 153.671 163.851 117.176 1.00 6.32   ? 1809 PHE A CD1   1 
ATOM   3179  C  CD2   . PHE A 1 592  ? 152.284 162.444 118.496 1.00 5.49   ? 1809 PHE A CD2   1 
ATOM   3180  C  CE1   . PHE A 1 592  ? 153.604 162.950 116.138 1.00 5.55   ? 1809 PHE A CE1   1 
ATOM   3181  C  CE2   . PHE A 1 592  ? 152.216 161.542 117.461 1.00 6.20   ? 1809 PHE A CE2   1 
ATOM   3182  C  CZ    . PHE A 1 592  ? 152.880 161.795 116.283 1.00 6.25   ? 1809 PHE A CZ    1 
ATOM   3183  N  N     . GLY A 1 593  ? 150.424 166.118 120.024 1.00 6.57   ? 1810 GLY A N     1 
ATOM   3184  C  CA    . GLY A 1 593  ? 148.982 166.277 119.921 1.00 6.91   ? 1810 GLY A CA    1 
ATOM   3185  C  C     . GLY A 1 593  ? 148.573 167.614 119.331 1.00 9.31   ? 1810 GLY A C     1 
ATOM   3186  O  O     . GLY A 1 593  ? 147.625 167.691 118.548 1.00 12.38  ? 1810 GLY A O     1 
ATOM   3187  N  N     . GLN A 1 594  ? 149.282 168.683 119.699 1.00 7.94   ? 1811 GLN A N     1 
ATOM   3188  C  CA    . GLN A 1 594  ? 148.977 170.005 119.157 1.00 7.93   ? 1811 GLN A CA    1 
ATOM   3189  C  C     . GLN A 1 594  ? 149.261 170.078 117.663 1.00 8.02   ? 1811 GLN A C     1 
ATOM   3190  O  O     . GLN A 1 594  ? 148.465 170.641 116.905 1.00 9.93   ? 1811 GLN A O     1 
ATOM   3191  C  CB    . GLN A 1 594  ? 149.780 171.074 119.891 1.00 7.94   ? 1811 GLN A CB    1 
ATOM   3192  C  CG    . GLN A 1 594  ? 149.360 171.330 121.320 1.00 9.39   ? 1811 GLN A CG    1 
ATOM   3193  C  CD    . GLN A 1 594  ? 150.435 172.052 122.102 1.00 9.40   ? 1811 GLN A CD    1 
ATOM   3194  O  OE1   . GLN A 1 594  ? 151.380 172.590 121.525 1.00 7.64   ? 1811 GLN A OE1   1 
ATOM   3195  N  NE2   . GLN A 1 594  ? 150.303 172.061 123.421 1.00 12.38  ? 1811 GLN A NE2   1 
ATOM   3196  N  N     . ASN A 1 595  ? 150.400 169.533 117.224 1.00 7.23   ? 1812 ASN A N     1 
ATOM   3197  C  CA    . ASN A 1 595  ? 150.712 169.530 115.798 1.00 8.61   ? 1812 ASN A CA    1 
ATOM   3198  C  C     . ASN A 1 595  ? 149.722 168.689 115.010 1.00 11.07  ? 1812 ASN A C     1 
ATOM   3199  O  O     . ASN A 1 595  ? 149.427 169.004 113.852 1.00 11.22  ? 1812 ASN A O     1 
ATOM   3200  C  CB    . ASN A 1 595  ? 152.134 169.025 115.560 1.00 7.15   ? 1812 ASN A CB    1 
ATOM   3201  C  CG    . ASN A 1 595  ? 153.175 170.073 115.857 1.00 8.18   ? 1812 ASN A CG    1 
ATOM   3202  O  OD1   . ASN A 1 595  ? 152.900 171.060 116.534 1.00 9.37   ? 1812 ASN A OD1   1 
ATOM   3203  N  ND2   . ASN A 1 595  ? 154.379 169.872 115.341 1.00 8.63   ? 1812 ASN A ND2   1 
ATOM   3204  N  N     . LEU A 1 596  ? 149.197 167.623 115.611 1.00 9.89   ? 1813 LEU A N     1 
ATOM   3205  C  CA    . LEU A 1 596  ? 148.181 166.813 114.957 1.00 8.63   ? 1813 LEU A CA    1 
ATOM   3206  C  C     . LEU A 1 596  ? 146.769 167.333 115.202 1.00 12.86  ? 1813 LEU A C     1 
ATOM   3207  O  O     . LEU A 1 596  ? 145.803 166.586 115.016 1.00 16.41  ? 1813 LEU A O     1 
ATOM   3208  C  CB    . LEU A 1 596  ? 148.314 165.359 115.401 1.00 5.34   ? 1813 LEU A CB    1 
ATOM   3209  C  CG    . LEU A 1 596  ? 149.641 164.795 114.894 1.00 6.98   ? 1813 LEU A CG    1 
ATOM   3210  C  CD1   . LEU A 1 596  ? 149.887 163.436 115.430 1.00 8.93   ? 1813 LEU A CD1   1 
ATOM   3211  C  CD2   . LEU A 1 596  ? 149.645 164.727 113.398 1.00 7.82   ? 1813 LEU A CD2   1 
ATOM   3212  N  N     . GLY A 1 597  ? 146.636 168.591 115.612 1.00 10.00  ? 1814 GLY A N     1 
ATOM   3213  C  CA    . GLY A 1 597  ? 145.341 169.250 115.694 1.00 8.86   ? 1814 GLY A CA    1 
ATOM   3214  C  C     . GLY A 1 597  ? 144.370 168.651 116.685 1.00 10.67  ? 1814 GLY A C     1 
ATOM   3215  O  O     . GLY A 1 597  ? 143.185 168.493 116.368 1.00 14.70  ? 1814 GLY A O     1 
ATOM   3216  N  N     . ARG A 1 598  ? 144.838 168.317 117.883 1.00 8.70   ? 1815 ARG A N     1 
ATOM   3217  C  CA    . ARG A 1 598  ? 143.964 167.734 118.887 1.00 8.51   ? 1815 ARG A CA    1 
ATOM   3218  C  C     . ARG A 1 598  ? 144.495 168.067 120.271 1.00 9.89   ? 1815 ARG A C     1 
ATOM   3219  O  O     . ARG A 1 598  ? 145.648 168.467 120.438 1.00 11.60  ? 1815 ARG A O     1 
ATOM   3220  C  CB    . ARG A 1 598  ? 143.837 166.219 118.707 1.00 8.35   ? 1815 ARG A CB    1 
ATOM   3221  C  CG    . ARG A 1 598  ? 145.153 165.484 118.705 1.00 8.91   ? 1815 ARG A CG    1 
ATOM   3222  C  CD    . ARG A 1 598  ? 145.052 164.215 117.884 1.00 10.94  ? 1815 ARG A CD    1 
ATOM   3223  N  NE    . ARG A 1 598  ? 143.836 163.468 118.176 1.00 9.77   ? 1815 ARG A NE    1 
ATOM   3224  C  CZ    . ARG A 1 598  ? 143.441 162.395 117.506 1.00 10.06  ? 1815 ARG A CZ    1 
ATOM   3225  N  NH1   . ARG A 1 598  ? 144.131 161.928 116.479 1.00 10.12  ? 1815 ARG A NH1   1 
ATOM   3226  N  NH2   . ARG A 1 598  ? 142.320 161.780 117.870 1.00 11.75  ? 1815 ARG A NH2   1 
ATOM   3227  N  N     . VAL A 1 599  ? 143.631 167.898 121.264 1.00 9.90   ? 1816 VAL A N     1 
ATOM   3228  C  CA    . VAL A 1 599  ? 143.970 168.164 122.655 1.00 8.98   ? 1816 VAL A CA    1 
ATOM   3229  C  C     . VAL A 1 599  ? 144.265 166.833 123.331 1.00 9.45   ? 1816 VAL A C     1 
ATOM   3230  O  O     . VAL A 1 599  ? 143.388 165.966 123.428 1.00 9.28   ? 1816 VAL A O     1 
ATOM   3231  C  CB    . VAL A 1 599  ? 142.837 168.913 123.372 1.00 8.93   ? 1816 VAL A CB    1 
ATOM   3232  C  CG1   . VAL A 1 599  ? 143.123 169.008 124.858 1.00 9.87   ? 1816 VAL A CG1   1 
ATOM   3233  C  CG2   . VAL A 1 599  ? 142.662 170.293 122.770 1.00 10.37  ? 1816 VAL A CG2   1 
ATOM   3234  N  N     . VAL A 1 600  ? 145.500 166.669 123.796 1.00 10.44  ? 1817 VAL A N     1 
ATOM   3235  C  CA    . VAL A 1 600  ? 145.900 165.466 124.516 1.00 8.05   ? 1817 VAL A CA    1 
ATOM   3236  C  C     . VAL A 1 600  ? 145.475 165.637 125.969 1.00 8.32   ? 1817 VAL A C     1 
ATOM   3237  O  O     . VAL A 1 600  ? 145.991 166.505 126.676 1.00 9.43   ? 1817 VAL A O     1 
ATOM   3238  C  CB    . VAL A 1 600  ? 147.409 165.220 124.406 1.00 7.09   ? 1817 VAL A CB    1 
ATOM   3239  C  CG1   . VAL A 1 600  ? 147.846 164.158 125.392 1.00 8.55   ? 1817 VAL A CG1   1 
ATOM   3240  C  CG2   . VAL A 1 600  ? 147.777 164.806 122.999 1.00 8.96   ? 1817 VAL A CG2   1 
ATOM   3241  N  N     . VAL A 1 601  ? 144.521 164.827 126.415 1.00 8.90   ? 1818 VAL A N     1 
ATOM   3242  C  CA    . VAL A 1 601  ? 144.103 164.861 127.812 1.00 10.29  ? 1818 VAL A CA    1 
ATOM   3243  C  C     . VAL A 1 601  ? 145.169 164.159 128.646 1.00 12.33  ? 1818 VAL A C     1 
ATOM   3244  O  O     . VAL A 1 601  ? 145.609 163.052 128.319 1.00 13.92  ? 1818 VAL A O     1 
ATOM   3245  C  CB    . VAL A 1 601  ? 142.707 164.243 128.001 1.00 9.18   ? 1818 VAL A CB    1 
ATOM   3246  C  CG1   . VAL A 1 601  ? 142.638 162.793 127.529 1.00 6.54   ? 1818 VAL A CG1   1 
ATOM   3247  C  CG2   . VAL A 1 601  ? 142.261 164.377 129.446 1.00 12.96  ? 1818 VAL A CG2   1 
ATOM   3248  N  N     . VAL A 1 602  ? 145.632 164.829 129.694 1.00 13.28  ? 1819 VAL A N     1 
ATOM   3249  C  CA    . VAL A 1 602  ? 146.806 164.395 130.439 1.00 13.76  ? 1819 VAL A CA    1 
ATOM   3250  C  C     . VAL A 1 602  ? 146.363 163.837 131.781 1.00 14.94  ? 1819 VAL A C     1 
ATOM   3251  O  O     . VAL A 1 602  ? 145.663 164.512 132.546 1.00 19.58  ? 1819 VAL A O     1 
ATOM   3252  C  CB    . VAL A 1 602  ? 147.805 165.549 130.619 1.00 14.26  ? 1819 VAL A CB    1 
ATOM   3253  C  CG1   . VAL A 1 602  ? 148.801 165.227 131.716 1.00 15.24  ? 1819 VAL A CG1   1 
ATOM   3254  C  CG2   . VAL A 1 602  ? 148.525 165.820 129.312 1.00 11.25  ? 1819 VAL A CG2   1 
ATOM   3255  N  N     . PHE A 1 603  ? 146.762 162.601 132.061 1.00 12.27  ? 1820 PHE A N     1 
ATOM   3256  C  CA    . PHE A 1 603  ? 146.503 161.965 133.348 1.00 17.30  ? 1820 PHE A CA    1 
ATOM   3257  C  C     . PHE A 1 603  ? 147.630 162.354 134.296 1.00 21.90  ? 1820 PHE A C     1 
ATOM   3258  O  O     . PHE A 1 603  ? 148.719 161.779 134.246 1.00 23.23  ? 1820 PHE A O     1 
ATOM   3259  C  CB    . PHE A 1 603  ? 146.428 160.449 133.210 1.00 19.36  ? 1820 PHE A CB    1 
ATOM   3260  C  CG    . PHE A 1 603  ? 145.351 159.952 132.283 1.00 16.58  ? 1820 PHE A CG    1 
ATOM   3261  C  CD1   . PHE A 1 603  ? 145.495 160.008 130.907 1.00 15.60  ? 1820 PHE A CD1   1 
ATOM   3262  C  CD2   . PHE A 1 603  ? 144.209 159.377 132.799 1.00 17.35  ? 1820 PHE A CD2   1 
ATOM   3263  C  CE1   . PHE A 1 603  ? 144.505 159.523 130.078 1.00 18.38  ? 1820 PHE A CE1   1 
ATOM   3264  C  CE2   . PHE A 1 603  ? 143.229 158.883 131.977 1.00 20.54  ? 1820 PHE A CE2   1 
ATOM   3265  C  CZ    . PHE A 1 603  ? 143.375 158.957 130.613 1.00 19.70  ? 1820 PHE A CZ    1 
ATOM   3266  N  N     . ASN A 1 604  ? 147.376 163.326 135.171 1.00 25.63  ? 1821 ASN A N     1 
ATOM   3267  C  CA    . ASN A 1 604  ? 148.355 163.697 136.194 1.00 29.77  ? 1821 ASN A CA    1 
ATOM   3268  C  C     . ASN A 1 604  ? 148.338 162.610 137.265 1.00 41.76  ? 1821 ASN A C     1 
ATOM   3269  O  O     . ASN A 1 604  ? 147.685 162.717 138.306 1.00 48.44  ? 1821 ASN A O     1 
ATOM   3270  C  CB    . ASN A 1 604  ? 148.052 165.074 136.771 1.00 30.36  ? 1821 ASN A CB    1 
ATOM   3271  C  CG    . ASN A 1 604  ? 148.375 166.196 135.804 1.00 33.50  ? 1821 ASN A CG    1 
ATOM   3272  O  OD1   . ASN A 1 604  ? 147.487 166.917 135.349 1.00 30.56  ? 1821 ASN A OD1   1 
ATOM   3273  N  ND2   . ASN A 1 604  ? 149.653 166.348 135.481 1.00 32.96  ? 1821 ASN A ND2   1 
ATOM   3274  N  N     . CYS A 1 605  ? 149.081 161.541 136.991 1.00 40.45  ? 1822 CYS A N     1 
ATOM   3275  C  CA    . CYS A 1 605  ? 149.011 160.340 137.812 1.00 40.78  ? 1822 CYS A CA    1 
ATOM   3276  C  C     . CYS A 1 605  ? 149.739 160.537 139.135 1.00 48.87  ? 1822 CYS A C     1 
ATOM   3277  O  O     . CYS A 1 605  ? 150.900 160.958 139.165 1.00 45.75  ? 1822 CYS A O     1 
ATOM   3278  C  CB    . CYS A 1 605  ? 149.604 159.154 137.056 1.00 35.70  ? 1822 CYS A CB    1 
ATOM   3279  S  SG    . CYS A 1 605  ? 148.512 158.451 135.800 1.00 36.75  ? 1822 CYS A SG    1 
ATOM   3280  N  N     . ASP A 1 606  ? 149.049 160.223 140.226 1.00 55.30  ? 1823 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 606  ? 149.602 160.286 141.572 1.00 58.37  ? 1823 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 606  ? 148.750 159.390 142.463 1.00 61.45  ? 1823 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 606  ? 147.950 158.583 141.976 1.00 57.11  ? 1823 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 606  ? 149.652 161.731 142.081 1.00 58.15  ? 1823 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 606  ? 148.339 162.461 141.888 1.00 58.01  ? 1823 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 606  ? 147.473 161.948 141.148 1.00 53.11  ? 1823 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 606  ? 148.172 163.550 142.476 1.00 63.53  ? 1823 ASP A OD2   1 
ATOM   3288  N  N     . ASP A 1 607  ? 148.919 159.529 143.778 1.00 65.47  ? 1824 ASP A N     1 
ATOM   3289  C  CA    . ASP A 1 607  ? 148.097 158.790 144.727 1.00 68.77  ? 1824 ASP A CA    1 
ATOM   3290  C  C     . ASP A 1 607  ? 146.681 159.341 144.839 1.00 68.59  ? 1824 ASP A C     1 
ATOM   3291  O  O     . ASP A 1 607  ? 145.815 158.664 145.404 1.00 63.78  ? 1824 ASP A O     1 
ATOM   3292  C  CB    . ASP A 1 607  ? 148.758 158.792 146.107 1.00 66.28  ? 1824 ASP A CB    1 
ATOM   3293  N  N     . SER A 1 608  ? 146.426 160.544 144.320 1.00 68.84  ? 1825 SER A N     1 
ATOM   3294  C  CA    . SER A 1 608  ? 145.089 161.123 144.410 1.00 68.67  ? 1825 SER A CA    1 
ATOM   3295  C  C     . SER A 1 608  ? 144.121 160.441 143.450 1.00 65.25  ? 1825 SER A C     1 
ATOM   3296  O  O     . SER A 1 608  ? 142.946 160.244 143.782 1.00 65.54  ? 1825 SER A O     1 
ATOM   3297  C  CB    . SER A 1 608  ? 145.149 162.625 144.134 1.00 68.05  ? 1825 SER A CB    1 
ATOM   3298  O  OG    . SER A 1 608  ? 145.368 162.883 142.758 1.00 66.07  ? 1825 SER A OG    1 
ATOM   3299  N  N     . PHE A 1 609  ? 144.590 160.082 142.257 1.00 63.64  ? 1826 PHE A N     1 
ATOM   3300  C  CA    . PHE A 1 609  ? 143.743 159.431 141.262 1.00 61.11  ? 1826 PHE A CA    1 
ATOM   3301  C  C     . PHE A 1 609  ? 143.421 158.012 141.706 1.00 62.20  ? 1826 PHE A C     1 
ATOM   3302  O  O     . PHE A 1 609  ? 144.267 157.117 141.611 1.00 65.44  ? 1826 PHE A O     1 
ATOM   3303  C  CB    . PHE A 1 609  ? 144.434 159.423 139.901 1.00 56.85  ? 1826 PHE A CB    1 
ATOM   3304  C  CG    . PHE A 1 609  ? 144.053 160.574 139.017 1.00 56.90  ? 1826 PHE A CG    1 
ATOM   3305  C  CD1   . PHE A 1 609  ? 144.766 161.758 139.051 1.00 59.37  ? 1826 PHE A CD1   1 
ATOM   3306  C  CD2   . PHE A 1 609  ? 142.989 160.463 138.137 1.00 54.16  ? 1826 PHE A CD2   1 
ATOM   3307  C  CE1   . PHE A 1 609  ? 144.418 162.817 138.232 1.00 60.15  ? 1826 PHE A CE1   1 
ATOM   3308  C  CE2   . PHE A 1 609  ? 142.635 161.516 137.316 1.00 56.18  ? 1826 PHE A CE2   1 
ATOM   3309  C  CZ    . PHE A 1 609  ? 143.350 162.694 137.364 1.00 56.27  ? 1826 PHE A CZ    1 
ATOM   3310  N  N     . ASP A 1 610  ? 142.200 157.800 142.191 1.00 57.57  ? 1827 ASP A N     1 
ATOM   3311  C  CA    . ASP A 1 610  ? 141.729 156.450 142.448 1.00 56.88  ? 1827 ASP A CA    1 
ATOM   3312  C  C     . ASP A 1 610  ? 141.202 155.840 141.150 1.00 52.39  ? 1827 ASP A C     1 
ATOM   3313  O  O     . ASP A 1 610  ? 141.225 156.463 140.085 1.00 49.65  ? 1827 ASP A O     1 
ATOM   3314  C  CB    . ASP A 1 610  ? 140.685 156.446 143.565 1.00 54.64  ? 1827 ASP A CB    1 
ATOM   3315  C  CG    . ASP A 1 610  ? 139.595 157.471 143.354 1.00 53.49  ? 1827 ASP A CG    1 
ATOM   3316  O  OD1   . ASP A 1 610  ? 139.698 158.262 142.398 1.00 57.16  ? 1827 ASP A OD1   1 
ATOM   3317  O  OD2   . ASP A 1 610  ? 138.633 157.490 144.150 1.00 50.70  ? 1827 ASP A OD2   1 
ATOM   3318  N  N     . TYR A 1 611  ? 140.721 154.600 141.237 1.00 52.38  ? 1828 TYR A N     1 
ATOM   3319  C  CA    . TYR A 1 611  ? 140.550 153.799 140.030 1.00 52.49  ? 1828 TYR A CA    1 
ATOM   3320  C  C     . TYR A 1 611  ? 139.364 154.266 139.192 1.00 51.28  ? 1828 TYR A C     1 
ATOM   3321  O  O     . TYR A 1 611  ? 139.427 154.231 137.956 1.00 49.92  ? 1828 TYR A O     1 
ATOM   3322  C  CB    . TYR A 1 611  ? 140.397 152.325 140.399 1.00 55.35  ? 1828 TYR A CB    1 
ATOM   3323  C  CG    . TYR A 1 611  ? 140.092 151.441 139.216 1.00 54.02  ? 1828 TYR A CG    1 
ATOM   3324  C  CD1   . TYR A 1 611  ? 141.082 151.120 138.299 1.00 52.41  ? 1828 TYR A CD1   1 
ATOM   3325  C  CD2   . TYR A 1 611  ? 138.820 150.923 139.016 1.00 54.74  ? 1828 TYR A CD2   1 
ATOM   3326  C  CE1   . TYR A 1 611  ? 140.814 150.315 137.214 1.00 53.32  ? 1828 TYR A CE1   1 
ATOM   3327  C  CE2   . TYR A 1 611  ? 138.543 150.113 137.933 1.00 56.91  ? 1828 TYR A CE2   1 
ATOM   3328  C  CZ    . TYR A 1 611  ? 139.545 149.813 137.036 1.00 56.84  ? 1828 TYR A CZ    1 
ATOM   3329  O  OH    . TYR A 1 611  ? 139.278 149.007 135.955 1.00 57.03  ? 1828 TYR A OH    1 
ATOM   3330  N  N     . GLN A 1 612  ? 138.279 154.710 139.834 1.00 50.80  ? 1829 GLN A N     1 
ATOM   3331  C  CA    . GLN A 1 612  ? 137.042 154.928 139.088 1.00 49.02  ? 1829 GLN A CA    1 
ATOM   3332  C  C     . GLN A 1 612  ? 137.129 156.160 138.187 1.00 46.17  ? 1829 GLN A C     1 
ATOM   3333  O  O     . GLN A 1 612  ? 136.726 156.101 137.020 1.00 43.46  ? 1829 GLN A O     1 
ATOM   3334  C  CB    . GLN A 1 612  ? 135.843 154.990 140.048 1.00 49.43  ? 1829 GLN A CB    1 
ATOM   3335  C  CG    . GLN A 1 612  ? 135.603 156.289 140.810 1.00 48.91  ? 1829 GLN A CG    1 
ATOM   3336  C  CD    . GLN A 1 612  ? 136.543 156.470 141.983 1.00 53.46  ? 1829 GLN A CD    1 
ATOM   3337  O  OE1   . GLN A 1 612  ? 137.283 155.557 142.350 1.00 55.11  ? 1829 GLN A OE1   1 
ATOM   3338  N  NE2   . GLN A 1 612  ? 136.514 157.653 142.583 1.00 50.94  ? 1829 GLN A NE2   1 
ATOM   3339  N  N     . VAL A 1 613  ? 137.705 157.262 138.679 1.00 44.47  ? 1830 VAL A N     1 
ATOM   3340  C  CA    . VAL A 1 613  ? 137.847 158.455 137.847 1.00 40.98  ? 1830 VAL A CA    1 
ATOM   3341  C  C     . VAL A 1 613  ? 138.875 158.217 136.747 1.00 41.05  ? 1830 VAL A C     1 
ATOM   3342  O  O     . VAL A 1 613  ? 138.708 158.678 135.610 1.00 42.85  ? 1830 VAL A O     1 
ATOM   3343  C  CB    . VAL A 1 613  ? 138.183 159.685 138.718 1.00 40.34  ? 1830 VAL A CB    1 
ATOM   3344  C  CG1   . VAL A 1 613  ? 139.496 159.511 139.458 1.00 45.25  ? 1830 VAL A CG1   1 
ATOM   3345  C  CG2   . VAL A 1 613  ? 138.237 160.946 137.872 1.00 43.98  ? 1830 VAL A CG2   1 
ATOM   3346  N  N     . LEU A 1 614  ? 139.927 157.459 137.054 1.00 41.98  ? 1831 LEU A N     1 
ATOM   3347  C  CA    . LEU A 1 614  ? 140.978 157.192 136.081 1.00 40.65  ? 1831 LEU A CA    1 
ATOM   3348  C  C     . LEU A 1 614  ? 140.448 156.350 134.925 1.00 35.12  ? 1831 LEU A C     1 
ATOM   3349  O  O     . LEU A 1 614  ? 140.643 156.693 133.752 1.00 32.26  ? 1831 LEU A O     1 
ATOM   3350  C  CB    . LEU A 1 614  ? 142.138 156.503 136.796 1.00 42.88  ? 1831 LEU A CB    1 
ATOM   3351  C  CG    . LEU A 1 614  ? 143.438 156.161 136.090 1.00 37.31  ? 1831 LEU A CG    1 
ATOM   3352  C  CD1   . LEU A 1 614  ? 144.069 157.439 135.639 1.00 36.89  ? 1831 LEU A CD1   1 
ATOM   3353  C  CD2   . LEU A 1 614  ? 144.341 155.479 137.089 1.00 40.20  ? 1831 LEU A CD2   1 
ATOM   3354  N  N     . SER A 1 615  ? 139.722 155.273 135.240 1.00 37.27  ? 1832 SER A N     1 
ATOM   3355  C  CA    . SER A 1 615  ? 139.126 154.441 134.197 1.00 35.84  ? 1832 SER A CA    1 
ATOM   3356  C  C     . SER A 1 615  ? 138.010 155.170 133.459 1.00 35.78  ? 1832 SER A C     1 
ATOM   3357  O  O     . SER A 1 615  ? 137.823 154.963 132.252 1.00 37.62  ? 1832 SER A O     1 
ATOM   3358  C  CB    . SER A 1 615  ? 138.604 153.134 134.794 1.00 43.47  ? 1832 SER A CB    1 
ATOM   3359  O  OG    . SER A 1 615  ? 139.631 152.163 134.907 1.00 44.91  ? 1832 SER A OG    1 
ATOM   3360  N  N     . ARG A 1 616  ? 137.253 156.022 134.160 1.00 36.30  ? 1833 ARG A N     1 
ATOM   3361  C  CA    . ARG A 1 616  ? 136.220 156.814 133.497 1.00 35.35  ? 1833 ARG A CA    1 
ATOM   3362  C  C     . ARG A 1 616  ? 136.824 157.759 132.465 1.00 32.68  ? 1833 ARG A C     1 
ATOM   3363  O  O     . ARG A 1 616  ? 136.332 157.873 131.338 1.00 33.11  ? 1833 ARG A O     1 
ATOM   3364  C  CB    . ARG A 1 616  ? 135.423 157.603 134.536 1.00 36.14  ? 1833 ARG A CB    1 
ATOM   3365  C  CG    . ARG A 1 616  ? 134.146 158.200 134.003 1.00 33.51  ? 1833 ARG A CG    1 
ATOM   3366  C  CD    . ARG A 1 616  ? 133.394 158.959 135.082 1.00 36.62  ? 1833 ARG A CD    1 
ATOM   3367  N  NE    . ARG A 1 616  ? 134.255 159.841 135.863 1.00 33.09  ? 1833 ARG A NE    1 
ATOM   3368  C  CZ    . ARG A 1 616  ? 134.751 160.989 135.422 1.00 29.31  ? 1833 ARG A CZ    1 
ATOM   3369  N  NH1   . ARG A 1 616  ? 134.557 161.395 134.178 1.00 29.09  ? 1833 ARG A NH1   1 
ATOM   3370  N  NH2   . ARG A 1 616  ? 135.463 161.748 136.248 1.00 27.92  ? 1833 ARG A NH2   1 
ATOM   3371  N  N     . LEU A 1 617  ? 137.902 158.446 132.825 1.00 31.71  ? 1834 LEU A N     1 
ATOM   3372  C  CA    . LEU A 1 617  ? 138.460 159.385 131.868 1.00 27.75  ? 1834 LEU A CA    1 
ATOM   3373  C  C     . LEU A 1 617  ? 139.231 158.643 130.780 1.00 27.01  ? 1834 LEU A C     1 
ATOM   3374  O  O     . LEU A 1 617  ? 139.340 159.147 129.654 1.00 23.96  ? 1834 LEU A O     1 
ATOM   3375  C  CB    . LEU A 1 617  ? 139.310 160.418 132.610 1.00 26.14  ? 1834 LEU A CB    1 
ATOM   3376  C  CG    . LEU A 1 617  ? 139.823 161.691 131.942 1.00 27.61  ? 1834 LEU A CG    1 
ATOM   3377  C  CD1   . LEU A 1 617  ? 140.021 162.754 133.015 1.00 28.24  ? 1834 LEU A CD1   1 
ATOM   3378  C  CD2   . LEU A 1 617  ? 141.101 161.470 131.207 1.00 25.86  ? 1834 LEU A CD2   1 
ATOM   3379  N  N     . LEU A 1 618  ? 139.698 157.423 131.075 1.00 31.25  ? 1835 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 618  ? 140.240 156.544 130.041 1.00 28.53  ? 1835 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 618  ? 139.183 156.167 129.011 1.00 27.13  ? 1835 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 618  ? 139.448 156.176 127.804 1.00 31.05  ? 1835 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 618  ? 140.810 155.281 130.689 1.00 24.11  ? 1835 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 618  ? 142.321 155.170 130.846 1.00 23.10  ? 1835 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 618  ? 142.688 153.839 131.482 1.00 23.74  ? 1835 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 618  ? 142.971 155.306 129.482 1.00 21.90  ? 1835 LEU A CD2   1 
ATOM   3387  N  N     . VAL A 1 619  ? 137.983 155.813 129.468 1.00 24.48  ? 1836 VAL A N     1 
ATOM   3388  C  CA    . VAL A 1 619  ? 136.944 155.413 128.530 1.00 23.04  ? 1836 VAL A CA    1 
ATOM   3389  C  C     . VAL A 1 619  ? 136.461 156.629 127.746 1.00 25.13  ? 1836 VAL A C     1 
ATOM   3390  O  O     . VAL A 1 619  ? 136.116 156.527 126.562 1.00 24.15  ? 1836 VAL A O     1 
ATOM   3391  C  CB    . VAL A 1 619  ? 135.801 154.698 129.269 1.00 25.10  ? 1836 VAL A CB    1 
ATOM   3392  C  CG1   . VAL A 1 619  ? 134.562 154.555 128.391 1.00 25.83  ? 1836 VAL A CG1   1 
ATOM   3393  C  CG2   . VAL A 1 619  ? 136.268 153.358 129.768 1.00 34.69  ? 1836 VAL A CG2   1 
ATOM   3394  N  N     . GLY A 1 620  ? 136.443 157.801 128.388 1.00 29.00  ? 1837 GLY A N     1 
ATOM   3395  C  CA    . GLY A 1 620  ? 136.172 159.029 127.653 1.00 26.55  ? 1837 GLY A CA    1 
ATOM   3396  C  C     . GLY A 1 620  ? 137.176 159.295 126.545 1.00 22.62  ? 1837 GLY A C     1 
ATOM   3397  O  O     . GLY A 1 620  ? 136.799 159.668 125.428 1.00 20.41  ? 1837 GLY A O     1 
ATOM   3398  N  N     . ILE A 1 621  ? 138.466 159.096 126.832 1.00 22.57  ? 1838 ILE A N     1 
ATOM   3399  C  CA    . ILE A 1 621  ? 139.483 159.261 125.795 1.00 19.64  ? 1838 ILE A CA    1 
ATOM   3400  C  C     . ILE A 1 621  ? 139.326 158.210 124.702 1.00 20.02  ? 1838 ILE A C     1 
ATOM   3401  O  O     . ILE A 1 621  ? 139.643 158.468 123.535 1.00 19.07  ? 1838 ILE A O     1 
ATOM   3402  C  CB    . ILE A 1 621  ? 140.893 159.224 126.410 1.00 15.43  ? 1838 ILE A CB    1 
ATOM   3403  N  N     . THR A 1 622  ? 138.862 157.010 125.059 1.00 20.53  ? 1839 THR A N     1 
ATOM   3404  C  CA    . THR A 1 622  ? 138.598 155.978 124.060 1.00 19.45  ? 1839 THR A CA    1 
ATOM   3405  C  C     . THR A 1 622  ? 137.447 156.378 123.140 1.00 21.12  ? 1839 THR A C     1 
ATOM   3406  O  O     . THR A 1 622  ? 137.571 156.329 121.910 1.00 22.84  ? 1839 THR A O     1 
ATOM   3407  C  CB    . THR A 1 622  ? 138.290 154.650 124.757 1.00 19.41  ? 1839 THR A CB    1 
ATOM   3408  O  OG1   . THR A 1 622  ? 139.505 154.070 125.244 1.00 20.48  ? 1839 THR A OG1   1 
ATOM   3409  C  CG2   . THR A 1 622  ? 137.621 153.676 123.808 1.00 22.10  ? 1839 THR A CG2   1 
ATOM   3410  N  N     . GLN A 1 623  ? 136.325 156.800 123.725 1.00 20.05  ? 1840 GLN A N     1 
ATOM   3411  C  CA    . GLN A 1 623  ? 135.106 157.012 122.952 1.00 19.94  ? 1840 GLN A CA    1 
ATOM   3412  C  C     . GLN A 1 623  ? 135.173 158.292 122.129 1.00 19.48  ? 1840 GLN A C     1 
ATOM   3413  O  O     . GLN A 1 623  ? 134.635 158.347 121.018 1.00 16.70  ? 1840 GLN A O     1 
ATOM   3414  C  CB    . GLN A 1 623  ? 133.896 157.036 123.881 1.00 21.34  ? 1840 GLN A CB    1 
ATOM   3415  C  CG    . GLN A 1 623  ? 132.614 156.611 123.205 1.00 26.20  ? 1840 GLN A CG    1 
ATOM   3416  C  CD    . GLN A 1 623  ? 131.447 156.531 124.161 1.00 31.95  ? 1840 GLN A CD    1 
ATOM   3417  O  OE1   . GLN A 1 623  ? 131.622 156.560 125.378 1.00 35.17  ? 1840 GLN A OE1   1 
ATOM   3418  N  NE2   . GLN A 1 623  ? 130.243 156.434 123.612 1.00 38.83  ? 1840 GLN A NE2   1 
ATOM   3419  N  N     . ILE A 1 624  ? 135.811 159.337 122.663 1.00 21.71  ? 1841 ILE A N     1 
ATOM   3420  C  CA    . ILE A 1 624  ? 135.999 160.562 121.888 1.00 18.19  ? 1841 ILE A CA    1 
ATOM   3421  C  C     . ILE A 1 624  ? 136.912 160.306 120.697 1.00 19.32  ? 1841 ILE A C     1 
ATOM   3422  O  O     . ILE A 1 624  ? 136.640 160.750 119.575 1.00 22.38  ? 1841 ILE A O     1 
ATOM   3423  C  CB    . ILE A 1 624  ? 136.550 161.684 122.789 1.00 14.28  ? 1841 ILE A CB    1 
ATOM   3424  C  CG1   . ILE A 1 624  ? 135.484 162.148 123.774 1.00 17.89  ? 1841 ILE A CG1   1 
ATOM   3425  C  CG2   . ILE A 1 624  ? 137.046 162.855 121.959 1.00 13.38  ? 1841 ILE A CG2   1 
ATOM   3426  C  CD1   . ILE A 1 624  ? 134.319 162.819 123.106 1.00 19.99  ? 1841 ILE A CD1   1 
ATOM   3427  N  N     . GLY A 1 625  ? 137.989 159.562 120.915 1.00 17.66  ? 1842 GLY A N     1 
ATOM   3428  C  CA    . GLY A 1 625  ? 139.094 159.525 119.989 1.00 16.01  ? 1842 GLY A CA    1 
ATOM   3429  C  C     . GLY A 1 625  ? 140.248 160.411 120.386 1.00 12.70  ? 1842 GLY A C     1 
ATOM   3430  O  O     . GLY A 1 625  ? 141.160 160.612 119.579 1.00 12.33  ? 1842 GLY A O     1 
ATOM   3431  N  N     . ALA A 1 626  ? 140.230 160.952 121.600 1.00 11.77  ? 1843 ALA A N     1 
ATOM   3432  C  CA    . ALA A 1 626  ? 141.301 161.798 122.088 1.00 11.24  ? 1843 ALA A CA    1 
ATOM   3433  C  C     . ALA A 1 626  ? 142.469 160.942 122.559 1.00 11.84  ? 1843 ALA A C     1 
ATOM   3434  O  O     . ALA A 1 626  ? 142.382 159.716 122.647 1.00 17.02  ? 1843 ALA A O     1 
ATOM   3435  C  CB    . ALA A 1 626  ? 140.805 162.695 123.220 1.00 15.26  ? 1843 ALA A CB    1 
ATOM   3436  N  N     . TRP A 1 627  ? 143.573 161.606 122.872 1.00 9.24   ? 1844 TRP A N     1 
ATOM   3437  C  CA    . TRP A 1 627  ? 144.817 160.938 123.219 1.00 8.91   ? 1844 TRP A CA    1 
ATOM   3438  C  C     . TRP A 1 627  ? 145.108 161.126 124.697 1.00 10.74  ? 1844 TRP A C     1 
ATOM   3439  O  O     . TRP A 1 627  ? 145.145 162.257 125.188 1.00 15.39  ? 1844 TRP A O     1 
ATOM   3440  C  CB    . TRP A 1 627  ? 145.962 161.482 122.374 1.00 8.18   ? 1844 TRP A CB    1 
ATOM   3441  C  CG    . TRP A 1 627  ? 145.909 160.960 120.998 1.00 10.08  ? 1844 TRP A CG    1 
ATOM   3442  C  CD1   . TRP A 1 627  ? 145.006 160.071 120.503 1.00 12.44  ? 1844 TRP A CD1   1 
ATOM   3443  C  CD2   . TRP A 1 627  ? 146.777 161.295 119.918 1.00 9.43   ? 1844 TRP A CD2   1 
ATOM   3444  N  NE1   . TRP A 1 627  ? 145.265 159.818 119.182 1.00 12.25  ? 1844 TRP A NE1   1 
ATOM   3445  C  CE2   . TRP A 1 627  ? 146.348 160.561 118.798 1.00 10.52  ? 1844 TRP A CE2   1 
ATOM   3446  C  CE3   . TRP A 1 627  ? 147.879 162.141 119.789 1.00 7.56   ? 1844 TRP A CE3   1 
ATOM   3447  C  CZ2   . TRP A 1 627  ? 146.979 160.647 117.571 1.00 9.80   ? 1844 TRP A CZ2   1 
ATOM   3448  C  CZ3   . TRP A 1 627  ? 148.502 162.222 118.571 1.00 7.55   ? 1844 TRP A CZ3   1 
ATOM   3449  C  CH2   . TRP A 1 627  ? 148.051 161.479 117.479 1.00 8.69   ? 1844 TRP A CH2   1 
ATOM   3450  N  N     . GLY A 1 628  ? 145.312 160.020 125.401 1.00 7.81   ? 1845 GLY A N     1 
ATOM   3451  C  CA    . GLY A 1 628  ? 145.550 160.093 126.824 1.00 7.78   ? 1845 GLY A CA    1 
ATOM   3452  C  C     . GLY A 1 628  ? 146.990 159.852 127.214 1.00 8.59   ? 1845 GLY A C     1 
ATOM   3453  O  O     . GLY A 1 628  ? 147.459 158.712 127.200 1.00 13.03  ? 1845 GLY A O     1 
ATOM   3454  N  N     . CYS A 1 629  ? 147.700 160.915 127.571 1.00 8.54   ? 1846 CYS A N     1 
ATOM   3455  C  CA    . CYS A 1 629  ? 149.078 160.806 128.027 1.00 9.31   ? 1846 CYS A CA    1 
ATOM   3456  C  C     . CYS A 1 629  ? 149.083 160.483 129.514 1.00 12.14  ? 1846 CYS A C     1 
ATOM   3457  O  O     . CYS A 1 629  ? 148.587 161.271 130.326 1.00 18.14  ? 1846 CYS A O     1 
ATOM   3458  C  CB    . CYS A 1 629  ? 149.844 162.099 127.759 1.00 8.17   ? 1846 CYS A CB    1 
ATOM   3459  S  SG    . CYS A 1 629  ? 151.540 162.096 128.374 1.00 9.08   ? 1846 CYS A SG    1 
ATOM   3460  N  N     . PHE A 1 630  ? 149.638 159.326 129.871 1.00 8.78   ? 1847 PHE A N     1 
ATOM   3461  C  CA    . PHE A 1 630  ? 149.758 158.929 131.272 1.00 9.96   ? 1847 PHE A CA    1 
ATOM   3462  C  C     . PHE A 1 630  ? 151.030 159.545 131.841 1.00 12.95  ? 1847 PHE A C     1 
ATOM   3463  O  O     . PHE A 1 630  ? 152.098 158.930 131.884 1.00 20.91  ? 1847 PHE A O     1 
ATOM   3464  C  CB    . PHE A 1 630  ? 149.757 157.416 131.405 1.00 12.17  ? 1847 PHE A CB    1 
ATOM   3465  C  CG    . PHE A 1 630  ? 148.391 156.817 131.407 1.00 14.89  ? 1847 PHE A CG    1 
ATOM   3466  C  CD1   . PHE A 1 630  ? 147.710 156.610 130.222 1.00 13.91  ? 1847 PHE A CD1   1 
ATOM   3467  C  CD2   . PHE A 1 630  ? 147.781 156.470 132.598 1.00 17.02  ? 1847 PHE A CD2   1 
ATOM   3468  C  CE1   . PHE A 1 630  ? 146.448 156.061 130.228 1.00 15.19  ? 1847 PHE A CE1   1 
ATOM   3469  C  CE2   . PHE A 1 630  ? 146.522 155.922 132.608 1.00 20.55  ? 1847 PHE A CE2   1 
ATOM   3470  C  CZ    . PHE A 1 630  ? 145.856 155.717 131.424 1.00 19.65  ? 1847 PHE A CZ    1 
ATOM   3471  N  N     . ASP A 1 631  ? 150.904 160.792 132.283 1.00 12.45  ? 1848 ASP A N     1 
ATOM   3472  C  CA    . ASP A 1 631  ? 152.040 161.514 132.836 1.00 16.50  ? 1848 ASP A CA    1 
ATOM   3473  C  C     . ASP A 1 631  ? 152.469 160.888 134.156 1.00 24.01  ? 1848 ASP A C     1 
ATOM   3474  O  O     . ASP A 1 631  ? 151.651 160.719 135.065 1.00 28.86  ? 1848 ASP A O     1 
ATOM   3475  C  CB    . ASP A 1 631  ? 151.678 162.983 133.040 1.00 18.07  ? 1848 ASP A CB    1 
ATOM   3476  C  CG    . ASP A 1 631  ? 152.891 163.856 133.281 1.00 21.25  ? 1848 ASP A CG    1 
ATOM   3477  O  OD1   . ASP A 1 631  ? 154.026 163.341 133.211 1.00 22.06  ? 1848 ASP A OD1   1 
ATOM   3478  O  OD2   . ASP A 1 631  ? 152.710 165.065 133.536 1.00 22.91  ? 1848 ASP A OD2   1 
ATOM   3479  N  N     . GLU A 1 632  ? 153.759 160.552 134.252 1.00 22.57  ? 1849 GLU A N     1 
ATOM   3480  C  CA    . GLU A 1 632  ? 154.359 159.936 135.438 1.00 22.39  ? 1849 GLU A CA    1 
ATOM   3481  C  C     . GLU A 1 632  ? 153.621 158.652 135.824 1.00 24.87  ? 1849 GLU A C     1 
ATOM   3482  O  O     . GLU A 1 632  ? 153.018 158.541 136.892 1.00 33.80  ? 1849 GLU A O     1 
ATOM   3483  C  CB    . GLU A 1 632  ? 154.404 160.928 136.603 1.00 29.24  ? 1849 GLU A CB    1 
ATOM   3484  C  CG    . GLU A 1 632  ? 155.184 162.193 136.304 1.00 29.82  ? 1849 GLU A CG    1 
ATOM   3485  C  CD    . GLU A 1 632  ? 156.655 161.926 136.075 1.00 31.11  ? 1849 GLU A CD    1 
ATOM   3486  O  OE1   . GLU A 1 632  ? 157.276 161.251 136.922 1.00 32.65  ? 1849 GLU A OE1   1 
ATOM   3487  O  OE2   . GLU A 1 632  ? 157.190 162.389 135.046 1.00 28.55  ? 1849 GLU A OE2   1 
ATOM   3488  N  N     . PHE A 1 633  ? 153.676 157.674 134.917 1.00 22.00  ? 1850 PHE A N     1 
ATOM   3489  C  CA    . PHE A 1 633  ? 152.929 156.435 135.096 1.00 24.40  ? 1850 PHE A CA    1 
ATOM   3490  C  C     . PHE A 1 633  ? 153.503 155.552 136.198 1.00 33.60  ? 1850 PHE A C     1 
ATOM   3491  O  O     . PHE A 1 633  ? 152.815 154.638 136.665 1.00 38.50  ? 1850 PHE A O     1 
ATOM   3492  C  CB    . PHE A 1 633  ? 152.883 155.666 133.774 1.00 21.14  ? 1850 PHE A CB    1 
ATOM   3493  C  CG    . PHE A 1 633  ? 151.981 154.467 133.798 1.00 22.21  ? 1850 PHE A CG    1 
ATOM   3494  C  CD1   . PHE A 1 633  ? 150.622 154.611 134.015 1.00 26.17  ? 1850 PHE A CD1   1 
ATOM   3495  C  CD2   . PHE A 1 633  ? 152.491 153.197 133.603 1.00 24.21  ? 1850 PHE A CD2   1 
ATOM   3496  C  CE1   . PHE A 1 633  ? 149.789 153.510 134.040 1.00 27.61  ? 1850 PHE A CE1   1 
ATOM   3497  C  CE2   . PHE A 1 633  ? 151.664 152.093 133.626 1.00 28.61  ? 1850 PHE A CE2   1 
ATOM   3498  C  CZ    . PHE A 1 633  ? 150.311 152.251 133.844 1.00 30.92  ? 1850 PHE A CZ    1 
ATOM   3499  N  N     . ASN A 1 634  ? 154.733 155.806 136.636 1.00 35.89  ? 1851 ASN A N     1 
ATOM   3500  C  CA    . ASN A 1 634  ? 155.355 154.983 137.664 1.00 36.58  ? 1851 ASN A CA    1 
ATOM   3501  C  C     . ASN A 1 634  ? 154.946 155.382 139.076 1.00 42.51  ? 1851 ASN A C     1 
ATOM   3502  O  O     . ASN A 1 634  ? 155.363 154.719 140.031 1.00 51.43  ? 1851 ASN A O     1 
ATOM   3503  C  CB    . ASN A 1 634  ? 156.875 155.051 137.537 1.00 36.85  ? 1851 ASN A CB    1 
ATOM   3504  C  CG    . ASN A 1 634  ? 157.386 156.471 137.488 1.00 37.23  ? 1851 ASN A CG    1 
ATOM   3505  O  OD1   . ASN A 1 634  ? 156.629 157.404 137.227 1.00 35.66  ? 1851 ASN A OD1   1 
ATOM   3506  N  ND2   . ASN A 1 634  ? 158.674 156.645 137.744 1.00 41.21  ? 1851 ASN A ND2   1 
ATOM   3507  N  N     . ARG A 1 635  ? 154.152 156.437 139.234 1.00 38.90  ? 1852 ARG A N     1 
ATOM   3508  C  CA    . ARG A 1 635  ? 153.743 156.909 140.549 1.00 38.51  ? 1852 ARG A CA    1 
ATOM   3509  C  C     . ARG A 1 635  ? 152.436 156.292 141.027 1.00 41.63  ? 1852 ARG A C     1 
ATOM   3510  O  O     . ARG A 1 635  ? 151.944 156.673 142.094 1.00 46.13  ? 1852 ARG A O     1 
ATOM   3511  C  CB    . ARG A 1 635  ? 153.619 158.435 140.545 1.00 36.47  ? 1852 ARG A CB    1 
ATOM   3512  C  CG    . ARG A 1 635  ? 154.692 159.131 139.733 1.00 39.57  ? 1852 ARG A CG    1 
ATOM   3513  C  CD    . ARG A 1 635  ? 155.969 159.322 140.535 1.00 44.94  ? 1852 ARG A CD    1 
ATOM   3514  N  NE    . ARG A 1 635  ? 156.008 160.621 141.196 1.00 50.04  ? 1852 ARG A NE    1 
ATOM   3515  C  CZ    . ARG A 1 635  ? 156.353 161.756 140.603 1.00 43.47  ? 1852 ARG A CZ    1 
ATOM   3516  N  NH1   . ARG A 1 635  ? 156.710 161.791 139.329 1.00 39.17  ? 1852 ARG A NH1   1 
ATOM   3517  N  NH2   . ARG A 1 635  ? 156.344 162.885 141.306 1.00 39.09  ? 1852 ARG A NH2   1 
ATOM   3518  N  N     . LEU A 1 636  ? 151.860 155.363 140.272 1.00 38.81  ? 1853 LEU A N     1 
ATOM   3519  C  CA    . LEU A 1 636  ? 150.653 154.687 140.714 1.00 42.36  ? 1853 LEU A CA    1 
ATOM   3520  C  C     . LEU A 1 636  ? 150.973 153.664 141.800 1.00 52.29  ? 1853 LEU A C     1 
ATOM   3521  O  O     . LEU A 1 636  ? 152.098 153.170 141.916 1.00 56.41  ? 1853 LEU A O     1 
ATOM   3522  C  CB    . LEU A 1 636  ? 149.957 153.983 139.548 1.00 42.70  ? 1853 LEU A CB    1 
ATOM   3523  C  CG    . LEU A 1 636  ? 149.040 154.786 138.626 1.00 45.76  ? 1853 LEU A CG    1 
ATOM   3524  C  CD1   . LEU A 1 636  ? 149.845 155.599 137.642 1.00 38.77  ? 1853 LEU A CD1   1 
ATOM   3525  C  CD2   . LEU A 1 636  ? 148.081 153.865 137.894 1.00 47.88  ? 1853 LEU A CD2   1 
ATOM   3526  N  N     . ASP A 1 637  ? 149.960 153.349 142.602 1.00 53.62  ? 1854 ASP A N     1 
ATOM   3527  C  CA    . ASP A 1 637  ? 150.052 152.213 143.503 1.00 50.73  ? 1854 ASP A CA    1 
ATOM   3528  C  C     . ASP A 1 637  ? 150.010 150.917 142.699 1.00 47.77  ? 1854 ASP A C     1 
ATOM   3529  O  O     . ASP A 1 637  ? 149.605 150.896 141.537 1.00 48.09  ? 1854 ASP A O     1 
ATOM   3530  C  CB    . ASP A 1 637  ? 148.918 152.242 144.527 1.00 47.74  ? 1854 ASP A CB    1 
ATOM   3531  N  N     . GLU A 1 638  ? 150.444 149.825 143.334 1.00 47.55  ? 1855 GLU A N     1 
ATOM   3532  C  CA    . GLU A 1 638  ? 150.591 148.556 142.621 1.00 53.31  ? 1855 GLU A CA    1 
ATOM   3533  C  C     . GLU A 1 638  ? 149.249 148.036 142.115 1.00 52.25  ? 1855 GLU A C     1 
ATOM   3534  O  O     . GLU A 1 638  ? 149.129 147.615 140.956 1.00 52.38  ? 1855 GLU A O     1 
ATOM   3535  C  CB    . GLU A 1 638  ? 151.259 147.524 143.530 1.00 54.12  ? 1855 GLU A CB    1 
ATOM   3536  N  N     . LYS A 1 639  ? 148.222 148.072 142.970 1.00 48.90  ? 1856 LYS A N     1 
ATOM   3537  C  CA    . LYS A 1 639  ? 146.919 147.538 142.585 1.00 47.07  ? 1856 LYS A CA    1 
ATOM   3538  C  C     . LYS A 1 639  ? 146.282 148.366 141.473 1.00 47.05  ? 1856 LYS A C     1 
ATOM   3539  O  O     . LYS A 1 639  ? 145.752 147.807 140.504 1.00 45.97  ? 1856 LYS A O     1 
ATOM   3540  C  CB    . LYS A 1 639  ? 146.016 147.425 143.823 1.00 45.88  ? 1856 LYS A CB    1 
ATOM   3541  C  CG    . LYS A 1 639  ? 145.692 148.718 144.591 1.00 46.11  ? 1856 LYS A CG    1 
ATOM   3542  C  CD    . LYS A 1 639  ? 144.414 149.403 144.111 1.00 46.94  ? 1856 LYS A CD    1 
ATOM   3543  C  CE    . LYS A 1 639  ? 144.156 150.694 144.870 1.00 46.44  ? 1856 LYS A CE    1 
ATOM   3544  N  NZ    . LYS A 1 639  ? 143.017 151.457 144.290 1.00 46.30  ? 1856 LYS A NZ    1 
ATOM   3545  N  N     . VAL A 1 640  ? 146.364 149.695 141.565 1.00 47.39  ? 1857 VAL A N     1 
ATOM   3546  C  CA    . VAL A 1 640  ? 145.774 150.528 140.524 1.00 47.39  ? 1857 VAL A CA    1 
ATOM   3547  C  C     . VAL A 1 640  ? 146.605 150.458 139.249 1.00 46.09  ? 1857 VAL A C     1 
ATOM   3548  O  O     . VAL A 1 640  ? 146.053 150.506 138.143 1.00 44.69  ? 1857 VAL A O     1 
ATOM   3549  C  CB    . VAL A 1 640  ? 145.574 151.974 141.030 1.00 48.85  ? 1857 VAL A CB    1 
ATOM   3550  C  CG1   . VAL A 1 640  ? 146.895 152.655 141.337 1.00 48.69  ? 1857 VAL A CG1   1 
ATOM   3551  C  CG2   . VAL A 1 640  ? 144.769 152.789 140.027 1.00 52.92  ? 1857 VAL A CG2   1 
ATOM   3552  N  N     . LEU A 1 641  ? 147.929 150.304 139.371 1.00 47.41  ? 1858 LEU A N     1 
ATOM   3553  C  CA    . LEU A 1 641  ? 148.764 150.156 138.183 1.00 44.84  ? 1858 LEU A CA    1 
ATOM   3554  C  C     . LEU A 1 641  ? 148.412 148.883 137.429 1.00 44.90  ? 1858 LEU A C     1 
ATOM   3555  O  O     . LEU A 1 641  ? 148.283 148.905 136.204 1.00 45.06  ? 1858 LEU A O     1 
ATOM   3556  C  CB    . LEU A 1 641  ? 150.248 150.175 138.564 1.00 46.72  ? 1858 LEU A CB    1 
ATOM   3557  C  CG    . LEU A 1 641  ? 151.349 150.227 137.496 1.00 46.79  ? 1858 LEU A CG    1 
ATOM   3558  C  CD1   . LEU A 1 641  ? 152.576 150.903 138.078 1.00 47.06  ? 1858 LEU A CD1   1 
ATOM   3559  C  CD2   . LEU A 1 641  ? 151.737 148.848 136.977 1.00 43.93  ? 1858 LEU A CD2   1 
ATOM   3560  N  N     . SER A 1 642  ? 148.229 147.769 138.143 1.00 44.24  ? 1859 SER A N     1 
ATOM   3561  C  CA    . SER A 1 642  ? 147.815 146.537 137.474 1.00 43.60  ? 1859 SER A CA    1 
ATOM   3562  C  C     . SER A 1 642  ? 146.415 146.667 136.881 1.00 44.47  ? 1859 SER A C     1 
ATOM   3563  O  O     . SER A 1 642  ? 146.174 146.249 135.736 1.00 43.11  ? 1859 SER A O     1 
ATOM   3564  C  CB    . SER A 1 642  ? 147.878 145.364 138.451 1.00 43.18  ? 1859 SER A CB    1 
ATOM   3565  N  N     . ALA A 1 643  ? 145.487 147.267 137.638 1.00 46.38  ? 1860 ALA A N     1 
ATOM   3566  C  CA    . ALA A 1 643  ? 144.101 147.363 137.194 1.00 45.58  ? 1860 ALA A CA    1 
ATOM   3567  C  C     . ALA A 1 643  ? 143.968 148.212 135.936 1.00 46.70  ? 1860 ALA A C     1 
ATOM   3568  O  O     . ALA A 1 643  ? 143.176 147.887 135.044 1.00 46.17  ? 1860 ALA A O     1 
ATOM   3569  C  CB    . ALA A 1 643  ? 143.233 147.927 138.318 1.00 45.26  ? 1860 ALA A CB    1 
ATOM   3570  N  N     . VAL A 1 644  ? 144.730 149.303 135.838 1.00 45.94  ? 1861 VAL A N     1 
ATOM   3571  C  CA    . VAL A 1 644  ? 144.662 150.121 134.633 1.00 43.17  ? 1861 VAL A CA    1 
ATOM   3572  C  C     . VAL A 1 644  ? 145.622 149.650 133.548 1.00 41.53  ? 1861 VAL A C     1 
ATOM   3573  O  O     . VAL A 1 644  ? 145.424 149.993 132.376 1.00 43.79  ? 1861 VAL A O     1 
ATOM   3574  C  CB    . VAL A 1 644  ? 144.908 151.608 134.938 1.00 40.66  ? 1861 VAL A CB    1 
ATOM   3575  C  CG1   . VAL A 1 644  ? 144.016 152.051 136.077 1.00 43.54  ? 1861 VAL A CG1   1 
ATOM   3576  C  CG2   . VAL A 1 644  ? 146.374 151.873 135.238 1.00 44.14  ? 1861 VAL A CG2   1 
ATOM   3577  N  N     . SER A 1 645  ? 146.639 148.856 133.893 1.00 38.68  ? 1862 SER A N     1 
ATOM   3578  C  CA    . SER A 1 645  ? 147.442 148.214 132.864 1.00 35.89  ? 1862 SER A CA    1 
ATOM   3579  C  C     . SER A 1 645  ? 146.608 147.210 132.090 1.00 37.09  ? 1862 SER A C     1 
ATOM   3580  O  O     . SER A 1 645  ? 146.769 147.069 130.874 1.00 40.23  ? 1862 SER A O     1 
ATOM   3581  C  CB    . SER A 1 645  ? 148.661 147.539 133.490 1.00 38.70  ? 1862 SER A CB    1 
ATOM   3582  O  OG    . SER A 1 645  ? 149.438 148.470 134.222 1.00 44.77  ? 1862 SER A OG    1 
ATOM   3583  N  N     . ALA A 1 646  ? 145.696 146.520 132.781 1.00 38.15  ? 1863 ALA A N     1 
ATOM   3584  C  CA    . ALA A 1 646  ? 144.756 145.648 132.081 1.00 41.28  ? 1863 ALA A CA    1 
ATOM   3585  C  C     . ALA A 1 646  ? 143.897 146.436 131.095 1.00 40.59  ? 1863 ALA A C     1 
ATOM   3586  O  O     . ALA A 1 646  ? 143.693 146.004 129.954 1.00 41.78  ? 1863 ALA A O     1 
ATOM   3587  C  CB    . ALA A 1 646  ? 143.877 144.909 133.088 1.00 45.80  ? 1863 ALA A CB    1 
ATOM   3588  N  N     . ASN A 1 647  ? 143.408 147.610 131.509 1.00 40.57  ? 1864 ASN A N     1 
ATOM   3589  C  CA    . ASN A 1 647  ? 142.561 148.421 130.636 1.00 43.84  ? 1864 ASN A CA    1 
ATOM   3590  C  C     . ASN A 1 647  ? 143.338 148.968 129.442 1.00 38.51  ? 1864 ASN A C     1 
ATOM   3591  O  O     . ASN A 1 647  ? 142.828 148.978 128.315 1.00 36.78  ? 1864 ASN A O     1 
ATOM   3592  C  CB    . ASN A 1 647  ? 141.934 149.562 131.435 1.00 45.68  ? 1864 ASN A CB    1 
ATOM   3593  C  CG    . ASN A 1 647  ? 140.930 149.071 132.454 1.00 48.92  ? 1864 ASN A CG    1 
ATOM   3594  O  OD1   . ASN A 1 647  ? 140.564 147.896 132.463 1.00 47.76  ? 1864 ASN A OD1   1 
ATOM   3595  N  ND2   . ASN A 1 647  ? 140.478 149.968 133.322 1.00 46.56  ? 1864 ASN A ND2   1 
ATOM   3596  N  N     . ILE A 1 648  ? 144.567 149.436 129.669 1.00 37.27  ? 1865 ILE A N     1 
ATOM   3597  C  CA    . ILE A 1 648  ? 145.383 149.946 128.571 1.00 32.60  ? 1865 ILE A CA    1 
ATOM   3598  C  C     . ILE A 1 648  ? 145.754 148.820 127.612 1.00 35.61  ? 1865 ILE A C     1 
ATOM   3599  O  O     . ILE A 1 648  ? 145.795 149.016 126.391 1.00 38.78  ? 1865 ILE A O     1 
ATOM   3600  C  CB    . ILE A 1 648  ? 146.627 150.669 129.120 1.00 25.71  ? 1865 ILE A CB    1 
ATOM   3601  C  CG1   . ILE A 1 648  ? 146.215 151.882 129.950 1.00 25.95  ? 1865 ILE A CG1   1 
ATOM   3602  C  CG2   . ILE A 1 648  ? 147.532 151.128 127.996 1.00 21.79  ? 1865 ILE A CG2   1 
ATOM   3603  C  CD1   . ILE A 1 648  ? 147.336 152.443 130.787 1.00 26.47  ? 1865 ILE A CD1   1 
ATOM   3604  N  N     . GLN A 1 649  ? 146.007 147.618 128.141 1.00 33.98  ? 1866 GLN A N     1 
ATOM   3605  C  CA    . GLN A 1 649  ? 146.263 146.472 127.277 1.00 35.29  ? 1866 GLN A CA    1 
ATOM   3606  C  C     . GLN A 1 649  ? 145.038 146.129 126.443 1.00 39.63  ? 1866 GLN A C     1 
ATOM   3607  O  O     . GLN A 1 649  ? 145.161 145.784 125.264 1.00 41.62  ? 1866 GLN A O     1 
ATOM   3608  C  CB    . GLN A 1 649  ? 146.694 145.265 128.108 1.00 40.60  ? 1866 GLN A CB    1 
ATOM   3609  C  CG    . GLN A 1 649  ? 147.027 144.037 127.276 1.00 43.50  ? 1866 GLN A CG    1 
ATOM   3610  C  CD    . GLN A 1 649  ? 147.495 142.867 128.116 1.00 51.62  ? 1866 GLN A CD    1 
ATOM   3611  O  OE1   . GLN A 1 649  ? 146.945 142.595 129.183 1.00 51.90  ? 1866 GLN A OE1   1 
ATOM   3612  N  NE2   . GLN A 1 649  ? 148.512 142.163 127.635 1.00 49.70  ? 1866 GLN A NE2   1 
ATOM   3613  N  N     . GLN A 1 650  ? 143.847 146.218 127.040 1.00 41.08  ? 1867 GLN A N     1 
ATOM   3614  C  CA    . GLN A 1 650  ? 142.625 145.962 126.284 1.00 41.44  ? 1867 GLN A CA    1 
ATOM   3615  C  C     . GLN A 1 650  ? 142.431 146.997 125.183 1.00 35.83  ? 1867 GLN A C     1 
ATOM   3616  O  O     . GLN A 1 650  ? 142.048 146.653 124.058 1.00 36.53  ? 1867 GLN A O     1 
ATOM   3617  C  CB    . GLN A 1 650  ? 141.423 145.942 127.226 1.00 41.63  ? 1867 GLN A CB    1 
ATOM   3618  C  CG    . GLN A 1 650  ? 141.218 144.602 127.910 1.00 49.16  ? 1867 GLN A CG    1 
ATOM   3619  C  CD    . GLN A 1 650  ? 140.276 144.688 129.090 1.00 56.06  ? 1867 GLN A CD    1 
ATOM   3620  O  OE1   . GLN A 1 650  ? 139.088 144.955 128.928 1.00 59.26  ? 1867 GLN A OE1   1 
ATOM   3621  N  NE2   . GLN A 1 650  ? 140.804 144.472 130.290 1.00 52.57  ? 1867 GLN A NE2   1 
ATOM   3622  N  N     . ILE A 1 651  ? 142.716 148.267 125.487 1.00 35.02  ? 1868 ILE A N     1 
ATOM   3623  C  CA    . ILE A 1 651  ? 142.607 149.331 124.487 1.00 33.15  ? 1868 ILE A CA    1 
ATOM   3624  C  C     . ILE A 1 651  ? 143.576 149.081 123.337 1.00 31.34  ? 1868 ILE A C     1 
ATOM   3625  O  O     . ILE A 1 651  ? 143.209 149.169 122.158 1.00 35.08  ? 1868 ILE A O     1 
ATOM   3626  C  CB    . ILE A 1 651  ? 142.858 150.703 125.140 1.00 30.49  ? 1868 ILE A CB    1 
ATOM   3627  C  CG1   . ILE A 1 651  ? 141.666 151.122 125.996 1.00 34.32  ? 1868 ILE A CG1   1 
ATOM   3628  C  CG2   . ILE A 1 651  ? 143.139 151.762 124.090 1.00 24.28  ? 1868 ILE A CG2   1 
ATOM   3629  C  CD1   . ILE A 1 651  ? 141.893 152.412 126.744 1.00 33.15  ? 1868 ILE A CD1   1 
ATOM   3630  N  N     . GLN A 1 652  ? 144.825 148.748 123.667 1.00 30.46  ? 1869 GLN A N     1 
ATOM   3631  C  CA    . GLN A 1 652  ? 145.837 148.545 122.636 1.00 29.45  ? 1869 GLN A CA    1 
ATOM   3632  C  C     . GLN A 1 652  ? 145.543 147.307 121.798 1.00 31.69  ? 1869 GLN A C     1 
ATOM   3633  O  O     . GLN A 1 652  ? 145.758 147.312 120.581 1.00 30.17  ? 1869 GLN A O     1 
ATOM   3634  C  CB    . GLN A 1 652  ? 147.220 148.451 123.277 1.00 27.93  ? 1869 GLN A CB    1 
ATOM   3635  C  CG    . GLN A 1 652  ? 147.740 149.778 123.802 1.00 24.52  ? 1869 GLN A CG    1 
ATOM   3636  C  CD    . GLN A 1 652  ? 148.007 150.775 122.695 1.00 23.49  ? 1869 GLN A CD    1 
ATOM   3637  O  OE1   . GLN A 1 652  ? 148.291 150.397 121.561 1.00 19.05  ? 1869 GLN A OE1   1 
ATOM   3638  N  NE2   . GLN A 1 652  ? 147.912 152.058 123.018 1.00 25.18  ? 1869 GLN A NE2   1 
ATOM   3639  N  N     . ASN A 1 653  ? 145.050 146.238 122.427 1.00 33.90  ? 1870 ASN A N     1 
ATOM   3640  C  CA    . ASN A 1 653  ? 144.697 145.039 121.678 1.00 34.61  ? 1870 ASN A CA    1 
ATOM   3641  C  C     . ASN A 1 653  ? 143.478 145.269 120.797 1.00 33.46  ? 1870 ASN A C     1 
ATOM   3642  O  O     . ASN A 1 653  ? 143.375 144.673 119.720 1.00 35.75  ? 1870 ASN A O     1 
ATOM   3643  C  CB    . ASN A 1 653  ? 144.452 143.875 122.636 1.00 34.57  ? 1870 ASN A CB    1 
ATOM   3644  C  CG    . ASN A 1 653  ? 144.852 142.541 122.044 1.00 36.25  ? 1870 ASN A CG    1 
ATOM   3645  O  OD1   . ASN A 1 653  ? 144.517 142.231 120.901 1.00 32.52  ? 1870 ASN A OD1   1 
ATOM   3646  N  ND2   . ASN A 1 653  ? 145.575 141.743 122.820 1.00 39.76  ? 1870 ASN A ND2   1 
ATOM   3647  N  N     . GLY A 1 654  ? 142.544 146.114 121.236 1.00 30.57  ? 1871 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 654  ? 141.440 146.484 120.368 1.00 30.59  ? 1871 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 654  ? 141.890 147.324 119.189 1.00 29.42  ? 1871 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 654  ? 141.370 147.182 118.080 1.00 33.65  ? 1871 GLY A O     1 
ATOM   3651  N  N     . LEU A 1 655  ? 142.860 148.212 119.412 1.00 25.59  ? 1872 LEU A N     1 
ATOM   3652  C  CA    . LEU A 1 655  ? 143.340 149.062 118.328 1.00 24.58  ? 1872 LEU A CA    1 
ATOM   3653  C  C     . LEU A 1 655  ? 144.171 148.275 117.321 1.00 28.13  ? 1872 LEU A C     1 
ATOM   3654  O  O     . LEU A 1 655  ? 144.117 148.551 116.117 1.00 28.40  ? 1872 LEU A O     1 
ATOM   3655  C  CB    . LEU A 1 655  ? 144.153 150.226 118.893 1.00 25.16  ? 1872 LEU A CB    1 
ATOM   3656  C  CG    . LEU A 1 655  ? 143.388 151.317 119.642 1.00 23.43  ? 1872 LEU A CG    1 
ATOM   3657  C  CD1   . LEU A 1 655  ? 144.286 152.513 119.889 1.00 19.90  ? 1872 LEU A CD1   1 
ATOM   3658  C  CD2   . LEU A 1 655  ? 142.146 151.725 118.870 1.00 23.41  ? 1872 LEU A CD2   1 
ATOM   3659  N  N     . GLN A 1 656  ? 144.948 147.295 117.795 1.00 30.42  ? 1873 GLN A N     1 
ATOM   3660  C  CA    . GLN A 1 656  ? 145.881 146.589 116.919 1.00 29.73  ? 1873 GLN A CA    1 
ATOM   3661  C  C     . GLN A 1 656  ? 145.158 145.742 115.879 1.00 29.23  ? 1873 GLN A C     1 
ATOM   3662  O  O     . GLN A 1 656  ? 145.529 145.752 114.700 1.00 28.10  ? 1873 GLN A O     1 
ATOM   3663  C  CB    . GLN A 1 656  ? 146.820 145.714 117.747 1.00 29.08  ? 1873 GLN A CB    1 
ATOM   3664  C  CG    . GLN A 1 656  ? 147.996 146.452 118.356 1.00 28.51  ? 1873 GLN A CG    1 
ATOM   3665  C  CD    . GLN A 1 656  ? 148.872 145.546 119.197 1.00 33.61  ? 1873 GLN A CD    1 
ATOM   3666  O  OE1   . GLN A 1 656  ? 149.414 144.558 118.703 1.00 34.39  ? 1873 GLN A OE1   1 
ATOM   3667  N  NE2   . GLN A 1 656  ? 149.014 145.877 120.474 1.00 32.70  ? 1873 GLN A NE2   1 
ATOM   3668  N  N     . VAL A 1 657  ? 144.128 145.006 116.290 1.00 30.02  ? 1874 VAL A N     1 
ATOM   3669  C  CA    . VAL A 1 657  ? 143.460 144.063 115.401 1.00 30.54  ? 1874 VAL A CA    1 
ATOM   3670  C  C     . VAL A 1 657  ? 142.272 144.731 114.720 1.00 31.61  ? 1874 VAL A C     1 
ATOM   3671  O  O     . VAL A 1 657  ? 141.501 144.075 114.011 1.00 32.38  ? 1874 VAL A O     1 
ATOM   3672  C  CB    . VAL A 1 657  ? 143.019 142.802 116.165 1.00 29.00  ? 1874 VAL A CB    1 
ATOM   3673  C  CG1   . VAL A 1 657  ? 144.203 142.189 116.893 1.00 26.24  ? 1874 VAL A CG1   1 
ATOM   3674  C  CG2   . VAL A 1 657  ? 141.904 143.135 117.141 1.00 32.44  ? 1874 VAL A CG2   1 
ATOM   3675  N  N     . GLY A 1 658  ? 142.128 146.036 114.915 1.00 34.24  ? 1875 GLY A N     1 
ATOM   3676  C  CA    . GLY A 1 658  ? 141.009 146.761 114.339 1.00 35.78  ? 1875 GLY A CA    1 
ATOM   3677  C  C     . GLY A 1 658  ? 139.663 146.389 114.923 1.00 34.33  ? 1875 GLY A C     1 
ATOM   3678  O  O     . GLY A 1 658  ? 138.669 146.329 114.189 1.00 33.81  ? 1875 GLY A O     1 
ATOM   3679  N  N     . LYS A 1 659  ? 139.609 146.131 116.227 1.00 35.41  ? 1876 LYS A N     1 
ATOM   3680  C  CA    . LYS A 1 659  ? 138.350 145.822 116.884 1.00 36.16  ? 1876 LYS A CA    1 
ATOM   3681  C  C     . LYS A 1 659  ? 137.463 147.062 116.937 1.00 40.43  ? 1876 LYS A C     1 
ATOM   3682  O  O     . LYS A 1 659  ? 137.943 148.198 116.914 1.00 40.47  ? 1876 LYS A O     1 
ATOM   3683  C  CB    . LYS A 1 659  ? 138.606 145.289 118.294 1.00 34.66  ? 1876 LYS A CB    1 
ATOM   3684  C  CG    . LYS A 1 659  ? 137.474 144.454 118.870 1.00 40.11  ? 1876 LYS A CG    1 
ATOM   3685  C  CD    . LYS A 1 659  ? 137.985 143.448 119.888 1.00 45.31  ? 1876 LYS A CD    1 
ATOM   3686  C  CE    . LYS A 1 659  ? 138.428 144.131 121.171 1.00 44.23  ? 1876 LYS A CE    1 
ATOM   3687  N  NZ    . LYS A 1 659  ? 138.415 143.199 122.332 1.00 40.33  ? 1876 LYS A NZ    1 
ATOM   3688  N  N     . SER A 1 660  ? 136.152 146.834 116.999 1.00 42.05  ? 1877 SER A N     1 
ATOM   3689  C  CA    . SER A 1 660  ? 135.194 147.933 117.021 1.00 41.04  ? 1877 SER A CA    1 
ATOM   3690  C  C     . SER A 1 660  ? 134.745 148.286 118.433 1.00 38.16  ? 1877 SER A C     1 
ATOM   3691  O  O     . SER A 1 660  ? 134.526 149.463 118.735 1.00 37.39  ? 1877 SER A O     1 
ATOM   3692  C  CB    . SER A 1 660  ? 133.975 147.584 116.164 1.00 41.17  ? 1877 SER A CB    1 
ATOM   3693  O  OG    . SER A 1 660  ? 133.045 146.808 116.899 1.00 41.89  ? 1877 SER A OG    1 
ATOM   3694  N  N     . HIS A 1 661  ? 134.596 147.291 119.302 1.00 38.45  ? 1878 HIS A N     1 
ATOM   3695  C  CA    . HIS A 1 661  ? 134.146 147.501 120.669 1.00 40.35  ? 1878 HIS A CA    1 
ATOM   3696  C  C     . HIS A 1 661  ? 135.085 146.787 121.628 1.00 42.27  ? 1878 HIS A C     1 
ATOM   3697  O  O     . HIS A 1 661  ? 135.488 145.648 121.379 1.00 44.29  ? 1878 HIS A O     1 
ATOM   3698  C  CB    . HIS A 1 661  ? 132.718 146.985 120.868 1.00 46.42  ? 1878 HIS A CB    1 
ATOM   3699  C  CG    . HIS A 1 661  ? 131.662 147.868 120.282 1.00 47.26  ? 1878 HIS A CG    1 
ATOM   3700  N  ND1   . HIS A 1 661  ? 131.626 148.203 118.945 1.00 44.94  ? 1878 HIS A ND1   1 
ATOM   3701  C  CD2   . HIS A 1 661  ? 130.593 148.474 120.849 1.00 47.04  ? 1878 HIS A CD2   1 
ATOM   3702  C  CE1   . HIS A 1 661  ? 130.586 148.984 118.717 1.00 42.95  ? 1878 HIS A CE1   1 
ATOM   3703  N  NE2   . HIS A 1 661  ? 129.942 149.164 119.855 1.00 43.54  ? 1878 HIS A NE2   1 
ATOM   3704  N  N     . ILE A 1 662  ? 135.427 147.456 122.727 1.00 40.76  ? 1879 ILE A N     1 
ATOM   3705  C  CA    . ILE A 1 662  ? 136.265 146.880 123.772 1.00 44.92  ? 1879 ILE A CA    1 
ATOM   3706  C  C     . ILE A 1 662  ? 135.407 146.641 125.004 1.00 52.46  ? 1879 ILE A C     1 
ATOM   3707  O  O     . ILE A 1 662  ? 134.581 147.484 125.375 1.00 53.12  ? 1879 ILE A O     1 
ATOM   3708  C  CB    . ILE A 1 662  ? 137.477 147.771 124.110 1.00 41.23  ? 1879 ILE A CB    1 
ATOM   3709  C  CG1   . ILE A 1 662  ? 137.053 149.225 124.302 1.00 41.85  ? 1879 ILE A CG1   1 
ATOM   3710  C  CG2   . ILE A 1 662  ? 138.535 147.662 123.027 1.00 35.90  ? 1879 ILE A CG2   1 
ATOM   3711  C  CD1   . ILE A 1 662  ? 138.206 150.145 124.608 1.00 38.50  ? 1879 ILE A CD1   1 
ATOM   3712  N  N     . THR A 1 663  ? 135.593 145.482 125.629 1.00 56.34  ? 1880 THR A N     1 
ATOM   3713  C  CA    . THR A 1 663  ? 134.791 145.067 126.779 1.00 60.71  ? 1880 THR A CA    1 
ATOM   3714  C  C     . THR A 1 663  ? 135.605 145.302 128.046 1.00 59.96  ? 1880 THR A C     1 
ATOM   3715  O  O     . THR A 1 663  ? 136.289 144.406 128.541 1.00 61.69  ? 1880 THR A O     1 
ATOM   3716  C  CB    . THR A 1 663  ? 134.375 143.607 126.649 1.00 67.36  ? 1880 THR A CB    1 
ATOM   3717  O  OG1   . THR A 1 663  ? 135.542 142.776 126.630 1.00 62.97  ? 1880 THR A OG1   1 
ATOM   3718  C  CG2   . THR A 1 663  ? 133.594 143.390 125.365 1.00 66.18  ? 1880 THR A CG2   1 
ATOM   3719  N  N     . LEU A 1 664  ? 135.526 146.519 128.579 1.00 62.99  ? 1881 LEU A N     1 
ATOM   3720  C  CA    . LEU A 1 664  ? 136.159 146.830 129.851 1.00 66.36  ? 1881 LEU A CA    1 
ATOM   3721  C  C     . LEU A 1 664  ? 135.167 147.593 130.719 1.00 69.14  ? 1881 LEU A C     1 
ATOM   3722  O  O     . LEU A 1 664  ? 134.246 148.242 130.217 1.00 68.03  ? 1881 LEU A O     1 
ATOM   3723  C  CB    . LEU A 1 664  ? 137.469 147.615 129.658 1.00 64.88  ? 1881 LEU A CB    1 
ATOM   3724  C  CG    . LEU A 1 664  ? 137.505 149.027 129.075 1.00 59.95  ? 1881 LEU A CG    1 
ATOM   3725  C  CD1   . LEU A 1 664  ? 137.480 150.034 130.199 1.00 53.83  ? 1881 LEU A CD1   1 
ATOM   3726  C  CD2   . LEU A 1 664  ? 138.737 149.228 128.210 1.00 51.07  ? 1881 LEU A CD2   1 
ATOM   3727  N  N     . LEU A 1 665  ? 135.373 147.493 132.037 1.00 69.73  ? 1882 LEU A N     1 
ATOM   3728  C  CA    . LEU A 1 665  ? 134.456 148.034 133.048 1.00 70.08  ? 1882 LEU A CA    1 
ATOM   3729  C  C     . LEU A 1 665  ? 133.046 147.474 132.876 1.00 72.95  ? 1882 LEU A C     1 
ATOM   3730  O  O     . LEU A 1 665  ? 132.052 148.186 133.041 1.00 73.72  ? 1882 LEU A O     1 
ATOM   3731  C  CB    . LEU A 1 665  ? 134.440 149.565 133.037 1.00 68.15  ? 1882 LEU A CB    1 
ATOM   3732  C  CG    . LEU A 1 665  ? 135.726 150.278 133.453 1.00 60.39  ? 1882 LEU A CG    1 
ATOM   3733  C  CD1   . LEU A 1 665  ? 135.583 151.777 133.250 1.00 52.72  ? 1882 LEU A CD1   1 
ATOM   3734  C  CD2   . LEU A 1 665  ? 136.076 149.959 134.897 1.00 58.26  ? 1882 LEU A CD2   1 
ATOM   3735  N  N     . GLU A 1 666  ? 132.967 146.186 132.527 1.00 72.69  ? 1883 GLU A N     1 
ATOM   3736  C  CA    . GLU A 1 666  ? 131.722 145.427 132.396 1.00 74.69  ? 1883 GLU A CA    1 
ATOM   3737  C  C     . GLU A 1 666  ? 130.764 146.025 131.369 1.00 76.01  ? 1883 GLU A C     1 
ATOM   3738  O  O     . GLU A 1 666  ? 129.553 145.790 131.438 1.00 79.25  ? 1883 GLU A O     1 
ATOM   3739  C  CB    . GLU A 1 666  ? 131.016 145.278 133.750 1.00 77.08  ? 1883 GLU A CB    1 
ATOM   3740  N  N     . GLU A 1 667  ? 131.276 146.793 130.409 1.00 73.07  ? 1884 GLU A N     1 
ATOM   3741  C  CA    . GLU A 1 667  ? 130.449 147.382 129.368 1.00 71.48  ? 1884 GLU A CA    1 
ATOM   3742  C  C     . GLU A 1 667  ? 131.184 147.320 128.039 1.00 66.39  ? 1884 GLU A C     1 
ATOM   3743  O  O     . GLU A 1 667  ? 132.413 147.411 127.983 1.00 62.63  ? 1884 GLU A O     1 
ATOM   3744  C  CB    . GLU A 1 667  ? 130.069 148.834 129.691 1.00 73.21  ? 1884 GLU A CB    1 
ATOM   3745  C  CG    . GLU A 1 667  ? 128.976 148.968 130.738 1.00 76.13  ? 1884 GLU A CG    1 
ATOM   3746  C  CD    . GLU A 1 667  ? 127.677 148.316 130.304 1.00 77.98  ? 1884 GLU A CD    1 
ATOM   3747  O  OE1   . GLU A 1 667  ? 127.304 148.459 129.120 1.00 72.98  ? 1884 GLU A OE1   1 
ATOM   3748  O  OE2   . GLU A 1 667  ? 127.032 147.655 131.144 1.00 79.66  ? 1884 GLU A OE2   1 
ATOM   3749  N  N     . GLU A 1 668  ? 130.411 147.165 126.965 1.00 65.28  ? 1885 GLU A N     1 
ATOM   3750  C  CA    . GLU A 1 668  ? 130.963 147.066 125.614 1.00 62.70  ? 1885 GLU A CA    1 
ATOM   3751  C  C     . GLU A 1 668  ? 130.951 148.450 124.963 1.00 57.97  ? 1885 GLU A C     1 
ATOM   3752  O  O     . GLU A 1 668  ? 130.245 148.720 123.990 1.00 54.18  ? 1885 GLU A O     1 
ATOM   3753  C  CB    . GLU A 1 668  ? 130.181 146.046 124.797 1.00 63.70  ? 1885 GLU A CB    1 
ATOM   3754  C  CG    . GLU A 1 668  ? 130.945 145.474 123.619 1.00 59.91  ? 1885 GLU A CG    1 
ATOM   3755  C  CD    . GLU A 1 668  ? 130.438 144.109 123.200 1.00 63.34  ? 1885 GLU A CD    1 
ATOM   3756  O  OE1   . GLU A 1 668  ? 130.643 143.139 123.957 1.00 64.31  ? 1885 GLU A OE1   1 
ATOM   3757  O  OE2   . GLU A 1 668  ? 129.833 144.007 122.112 1.00 61.23  ? 1885 GLU A OE2   1 
ATOM   3758  N  N     . THR A 1 669  ? 131.760 149.337 125.539 1.00 57.85  ? 1886 THR A N     1 
ATOM   3759  C  CA    . THR A 1 669  ? 131.825 150.715 125.083 1.00 52.76  ? 1886 THR A CA    1 
ATOM   3760  C  C     . THR A 1 669  ? 132.395 150.784 123.667 1.00 47.28  ? 1886 THR A C     1 
ATOM   3761  O  O     . THR A 1 669  ? 133.209 149.943 123.279 1.00 48.24  ? 1886 THR A O     1 
ATOM   3762  C  CB    . THR A 1 669  ? 132.694 151.547 126.023 1.00 53.08  ? 1886 THR A CB    1 
ATOM   3763  O  OG1   . THR A 1 669  ? 134.046 151.072 125.969 1.00 47.92  ? 1886 THR A OG1   1 
ATOM   3764  C  CG2   . THR A 1 669  ? 132.188 151.433 127.452 1.00 56.55  ? 1886 THR A CG2   1 
ATOM   3765  N  N     . PRO A 1 670  ? 131.960 151.760 122.868 1.00 44.66  ? 1887 PRO A N     1 
ATOM   3766  C  CA    . PRO A 1 670  ? 132.537 151.925 121.530 1.00 41.56  ? 1887 PRO A CA    1 
ATOM   3767  C  C     . PRO A 1 670  ? 134.017 152.261 121.602 1.00 34.75  ? 1887 PRO A C     1 
ATOM   3768  O  O     . PRO A 1 670  ? 134.483 152.935 122.522 1.00 33.90  ? 1887 PRO A O     1 
ATOM   3769  C  CB    . PRO A 1 670  ? 131.732 153.085 120.932 1.00 42.25  ? 1887 PRO A CB    1 
ATOM   3770  C  CG    . PRO A 1 670  ? 130.461 153.108 121.710 1.00 44.35  ? 1887 PRO A CG    1 
ATOM   3771  C  CD    . PRO A 1 670  ? 130.821 152.666 123.094 1.00 44.59  ? 1887 PRO A CD    1 
ATOM   3772  N  N     . LEU A 1 671  ? 134.760 151.768 120.618 1.00 32.48  ? 1888 LEU A N     1 
ATOM   3773  C  CA    . LEU A 1 671  ? 136.192 152.022 120.503 1.00 30.31  ? 1888 LEU A CA    1 
ATOM   3774  C  C     . LEU A 1 671  ? 136.413 152.740 119.179 1.00 28.71  ? 1888 LEU A C     1 
ATOM   3775  O  O     . LEU A 1 671  ? 136.398 152.117 118.113 1.00 35.25  ? 1888 LEU A O     1 
ATOM   3776  C  CB    . LEU A 1 671  ? 136.998 150.728 120.584 1.00 30.37  ? 1888 LEU A CB    1 
ATOM   3777  C  CG    . LEU A 1 671  ? 138.473 150.810 120.187 1.00 25.25  ? 1888 LEU A CG    1 
ATOM   3778  C  CD1   . LEU A 1 671  ? 139.294 151.425 121.300 1.00 26.57  ? 1888 LEU A CD1   1 
ATOM   3779  C  CD2   . LEU A 1 671  ? 139.005 149.438 119.825 1.00 30.94  ? 1888 LEU A CD2   1 
ATOM   3780  N  N     . SER A 1 672  ? 136.578 154.054 119.245 1.00 23.88  ? 1889 SER A N     1 
ATOM   3781  C  CA    . SER A 1 672  ? 136.907 154.809 118.052 1.00 22.82  ? 1889 SER A CA    1 
ATOM   3782  C  C     . SER A 1 672  ? 138.310 154.434 117.584 1.00 22.35  ? 1889 SER A C     1 
ATOM   3783  O  O     . SER A 1 672  ? 139.238 154.373 118.394 1.00 22.12  ? 1889 SER A O     1 
ATOM   3784  C  CB    . SER A 1 672  ? 136.827 156.306 118.328 1.00 23.50  ? 1889 SER A CB    1 
ATOM   3785  O  OG    . SER A 1 672  ? 137.533 156.636 119.509 1.00 22.38  ? 1889 SER A OG    1 
ATOM   3786  N  N     . PRO A 1 673  ? 138.498 154.172 116.291 1.00 24.06  ? 1890 PRO A N     1 
ATOM   3787  C  CA    . PRO A 1 673  ? 139.814 153.762 115.791 1.00 23.99  ? 1890 PRO A CA    1 
ATOM   3788  C  C     . PRO A 1 673  ? 140.848 154.875 115.730 1.00 22.97  ? 1890 PRO A C     1 
ATOM   3789  O  O     . PRO A 1 673  ? 141.938 154.648 115.199 1.00 24.05  ? 1890 PRO A O     1 
ATOM   3790  C  CB    . PRO A 1 673  ? 139.494 153.243 114.380 1.00 25.87  ? 1890 PRO A CB    1 
ATOM   3791  C  CG    . PRO A 1 673  ? 138.261 153.961 113.983 1.00 27.40  ? 1890 PRO A CG    1 
ATOM   3792  C  CD    . PRO A 1 673  ? 137.470 154.170 115.236 1.00 25.26  ? 1890 PRO A CD    1 
ATOM   3793  N  N     . HIS A 1 674  ? 140.546 156.061 116.255 1.00 19.27  ? 1891 HIS A N     1 
ATOM   3794  C  CA    . HIS A 1 674  ? 141.482 157.174 116.257 1.00 18.07  ? 1891 HIS A CA    1 
ATOM   3795  C  C     . HIS A 1 674  ? 142.057 157.471 117.634 1.00 16.27  ? 1891 HIS A C     1 
ATOM   3796  O  O     . HIS A 1 674  ? 142.837 158.419 117.769 1.00 15.16  ? 1891 HIS A O     1 
ATOM   3797  C  CB    . HIS A 1 674  ? 140.804 158.430 115.700 1.00 20.74  ? 1891 HIS A CB    1 
ATOM   3798  C  CG    . HIS A 1 674  ? 140.364 158.294 114.276 1.00 26.59  ? 1891 HIS A CG    1 
ATOM   3799  N  ND1   . HIS A 1 674  ? 141.253 158.194 113.228 1.00 27.46  ? 1891 HIS A ND1   1 
ATOM   3800  C  CD2   . HIS A 1 674  ? 139.128 158.238 113.727 1.00 31.86  ? 1891 HIS A CD2   1 
ATOM   3801  C  CE1   . HIS A 1 674  ? 140.585 158.082 112.095 1.00 36.47  ? 1891 HIS A CE1   1 
ATOM   3802  N  NE2   . HIS A 1 674  ? 139.293 158.107 112.369 1.00 42.19  ? 1891 HIS A NE2   1 
ATOM   3803  N  N     . THR A 1 675  ? 141.701 156.696 118.655 1.00 16.72  ? 1892 THR A N     1 
ATOM   3804  C  CA    . THR A 1 675  ? 142.224 156.940 119.989 1.00 14.99  ? 1892 THR A CA    1 
ATOM   3805  C  C     . THR A 1 675  ? 143.659 156.436 120.102 1.00 14.89  ? 1892 THR A C     1 
ATOM   3806  O  O     . THR A 1 675  ? 144.185 155.765 119.211 1.00 21.55  ? 1892 THR A O     1 
ATOM   3807  C  CB    . THR A 1 675  ? 141.354 156.266 121.045 1.00 14.39  ? 1892 THR A CB    1 
ATOM   3808  O  OG1   . THR A 1 675  ? 141.876 156.559 122.345 1.00 13.59  ? 1892 THR A OG1   1 
ATOM   3809  C  CG2   . THR A 1 675  ? 141.361 154.767 120.850 1.00 16.13  ? 1892 THR A CG2   1 
ATOM   3810  N  N     . ALA A 1 676  ? 144.296 156.770 121.223 1.00 11.68  ? 1893 ALA A N     1 
ATOM   3811  C  CA    . ALA A 1 676  ? 145.648 156.312 121.507 1.00 12.33  ? 1893 ALA A CA    1 
ATOM   3812  C  C     . ALA A 1 676  ? 145.904 156.438 122.998 1.00 11.37  ? 1893 ALA A C     1 
ATOM   3813  O  O     . ALA A 1 676  ? 145.186 157.141 123.712 1.00 11.76  ? 1893 ALA A O     1 
ATOM   3814  C  CB    . ALA A 1 676  ? 146.697 157.101 120.717 1.00 11.03  ? 1893 ALA A CB    1 
ATOM   3815  N  N     . VAL A 1 677  ? 146.935 155.737 123.463 1.00 7.95   ? 1894 VAL A N     1 
ATOM   3816  C  CA    . VAL A 1 677  ? 147.392 155.826 124.843 1.00 8.98   ? 1894 VAL A CA    1 
ATOM   3817  C  C     . VAL A 1 677  ? 148.898 156.028 124.836 1.00 9.22   ? 1894 VAL A C     1 
ATOM   3818  O  O     . VAL A 1 677  ? 149.633 155.225 124.254 1.00 14.19  ? 1894 VAL A O     1 
ATOM   3819  C  CB    . VAL A 1 677  ? 147.029 154.571 125.660 1.00 12.10  ? 1894 VAL A CB    1 
ATOM   3820  C  CG1   . VAL A 1 677  ? 147.592 154.687 127.062 1.00 14.70  ? 1894 VAL A CG1   1 
ATOM   3821  C  CG2   . VAL A 1 677  ? 145.524 154.374 125.713 1.00 13.80  ? 1894 VAL A CG2   1 
ATOM   3822  N  N     . PHE A 1 678  ? 149.355 157.094 125.482 1.00 7.68   ? 1895 PHE A N     1 
ATOM   3823  C  CA    . PHE A 1 678  ? 150.771 157.352 125.675 1.00 6.97   ? 1895 PHE A CA    1 
ATOM   3824  C  C     . PHE A 1 678  ? 151.117 157.199 127.147 1.00 9.28   ? 1895 PHE A C     1 
ATOM   3825  O  O     . PHE A 1 678  ? 150.277 157.413 128.025 1.00 13.39  ? 1895 PHE A O     1 
ATOM   3826  C  CB    . PHE A 1 678  ? 151.156 158.752 125.200 1.00 6.70   ? 1895 PHE A CB    1 
ATOM   3827  C  CG    . PHE A 1 678  ? 150.757 159.043 123.789 1.00 6.23   ? 1895 PHE A CG    1 
ATOM   3828  C  CD1   . PHE A 1 678  ? 151.444 158.478 122.733 1.00 6.86   ? 1895 PHE A CD1   1 
ATOM   3829  C  CD2   . PHE A 1 678  ? 149.700 159.884 123.517 1.00 7.73   ? 1895 PHE A CD2   1 
ATOM   3830  C  CE1   . PHE A 1 678  ? 151.082 158.747 121.433 1.00 5.32   ? 1895 PHE A CE1   1 
ATOM   3831  C  CE2   . PHE A 1 678  ? 149.336 160.154 122.222 1.00 8.42   ? 1895 PHE A CE2   1 
ATOM   3832  C  CZ    . PHE A 1 678  ? 150.028 159.585 121.178 1.00 6.45   ? 1895 PHE A CZ    1 
ATOM   3833  N  N     . ILE A 1 679  ? 152.361 156.818 127.413 1.00 8.26   ? 1896 ILE A N     1 
ATOM   3834  C  CA    . ILE A 1 679  ? 152.830 156.609 128.776 1.00 8.41   ? 1896 ILE A CA    1 
ATOM   3835  C  C     . ILE A 1 679  ? 154.206 157.241 128.912 1.00 10.28  ? 1896 ILE A C     1 
ATOM   3836  O  O     . ILE A 1 679  ? 155.102 156.965 128.110 1.00 13.38  ? 1896 ILE A O     1 
ATOM   3837  C  CB    . ILE A 1 679  ? 152.872 155.112 129.139 1.00 9.61   ? 1896 ILE A CB    1 
ATOM   3838  C  CG1   . ILE A 1 679  ? 151.482 154.626 129.545 1.00 13.40  ? 1896 ILE A CG1   1 
ATOM   3839  C  CG2   . ILE A 1 679  ? 153.840 154.857 130.268 1.00 11.71  ? 1896 ILE A CG2   1 
ATOM   3840  C  CD1   . ILE A 1 679  ? 151.355 153.122 129.606 1.00 15.11  ? 1896 ILE A CD1   1 
ATOM   3841  N  N     . THR A 1 680  ? 154.369 158.104 129.909 1.00 9.94   ? 1897 THR A N     1 
ATOM   3842  C  CA    . THR A 1 680  ? 155.666 158.653 130.272 1.00 9.63   ? 1897 THR A CA    1 
ATOM   3843  C  C     . THR A 1 680  ? 155.958 158.264 131.711 1.00 15.24  ? 1897 THR A C     1 
ATOM   3844  O  O     . THR A 1 680  ? 155.127 158.487 132.595 1.00 20.24  ? 1897 THR A O     1 
ATOM   3845  C  CB    . THR A 1 680  ? 155.696 160.173 130.116 1.00 9.13   ? 1897 THR A CB    1 
ATOM   3846  O  OG1   . THR A 1 680  ? 154.775 160.764 131.038 1.00 12.64  ? 1897 THR A OG1   1 
ATOM   3847  C  CG2   . THR A 1 680  ? 155.312 160.569 128.702 1.00 9.77   ? 1897 THR A CG2   1 
ATOM   3848  N  N     . LEU A 1 681  ? 157.131 157.682 131.945 1.00 17.17  ? 1898 LEU A N     1 
ATOM   3849  C  CA    . LEU A 1 681  ? 157.466 157.161 133.261 1.00 21.74  ? 1898 LEU A CA    1 
ATOM   3850  C  C     . LEU A 1 681  ? 158.962 157.323 133.493 1.00 23.42  ? 1898 LEU A C     1 
ATOM   3851  O  O     . LEU A 1 681  ? 159.707 157.756 132.610 1.00 20.50  ? 1898 LEU A O     1 
ATOM   3852  C  CB    . LEU A 1 681  ? 156.994 155.705 133.403 1.00 20.76  ? 1898 LEU A CB    1 
ATOM   3853  C  CG    . LEU A 1 681  ? 157.501 154.581 132.491 1.00 16.69  ? 1898 LEU A CG    1 
ATOM   3854  C  CD1   . LEU A 1 681  ? 158.821 153.995 132.950 1.00 32.85  ? 1898 LEU A CD1   1 
ATOM   3855  C  CD2   . LEU A 1 681  ? 156.461 153.488 132.408 1.00 19.93  ? 1898 LEU A CD2   1 
ATOM   3856  N  N     . ASN A 1 682  ? 159.395 156.979 134.704 1.00 31.74  ? 1899 ASN A N     1 
ATOM   3857  C  CA    . ASN A 1 682  ? 160.792 157.113 135.114 1.00 37.04  ? 1899 ASN A CA    1 
ATOM   3858  C  C     . ASN A 1 682  ? 161.214 155.830 135.824 1.00 43.36  ? 1899 ASN A C     1 
ATOM   3859  O  O     . ASN A 1 682  ? 160.916 155.647 137.015 1.00 47.59  ? 1899 ASN A O     1 
ATOM   3860  C  CB    . ASN A 1 682  ? 160.985 158.328 136.017 1.00 36.00  ? 1899 ASN A CB    1 
ATOM   3861  C  CG    . ASN A 1 682  ? 160.231 159.546 135.528 1.00 31.44  ? 1899 ASN A CG    1 
ATOM   3862  O  OD1   . ASN A 1 682  ? 160.473 160.042 134.428 1.00 28.36  ? 1899 ASN A OD1   1 
ATOM   3863  N  ND2   . ASN A 1 682  ? 159.305 160.033 136.345 1.00 31.53  ? 1899 ASN A ND2   1 
ATOM   3864  N  N     . PRO A 1 683  ? 161.905 154.923 135.133 1.00 44.24  ? 1900 PRO A N     1 
ATOM   3865  C  CA    . PRO A 1 683  ? 162.216 153.618 135.730 1.00 49.05  ? 1900 PRO A CA    1 
ATOM   3866  C  C     . PRO A 1 683  ? 163.353 153.699 136.736 1.00 63.69  ? 1900 PRO A C     1 
ATOM   3867  O  O     . PRO A 1 683  ? 164.343 154.407 136.534 1.00 68.16  ? 1900 PRO A O     1 
ATOM   3868  C  CB    . PRO A 1 683  ? 162.621 152.759 134.522 1.00 41.14  ? 1900 PRO A CB    1 
ATOM   3869  C  CG    . PRO A 1 683  ? 162.443 153.629 133.307 1.00 37.27  ? 1900 PRO A CG    1 
ATOM   3870  C  CD    . PRO A 1 683  ? 162.468 155.043 133.783 1.00 40.87  ? 1900 PRO A CD    1 
ATOM   3871  N  N     . GLY A 1 684  ? 163.212 152.937 137.816 1.00 64.63  ? 1901 GLY A N     1 
ATOM   3872  C  CA    . GLY A 1 684  ? 164.236 152.872 138.845 1.00 62.47  ? 1901 GLY A CA    1 
ATOM   3873  C  C     . GLY A 1 684  ? 164.471 154.174 139.579 1.00 67.28  ? 1901 GLY A C     1 
ATOM   3874  O  O     . GLY A 1 684  ? 165.626 154.531 139.846 1.00 64.46  ? 1901 GLY A O     1 
ATOM   3875  N  N     . TYR A 1 685  ? 163.406 154.895 139.912 1.00 67.16  ? 1902 TYR A N     1 
ATOM   3876  C  CA    . TYR A 1 685  ? 163.534 156.181 140.584 1.00 70.85  ? 1902 TYR A CA    1 
ATOM   3877  C  C     . TYR A 1 685  ? 162.690 156.230 141.853 1.00 73.93  ? 1902 TYR A C     1 
ATOM   3878  O  O     . TYR A 1 685  ? 163.181 155.949 142.947 1.00 74.67  ? 1902 TYR A O     1 
ATOM   3879  C  CB    . TYR A 1 685  ? 163.135 157.315 139.639 1.00 62.61  ? 1902 TYR A CB    1 
ATOM   3880  C  CG    . TYR A 1 685  ? 164.221 157.701 138.661 1.00 65.22  ? 1902 TYR A CG    1 
ATOM   3881  C  CD1   . TYR A 1 685  ? 165.392 158.308 139.096 1.00 70.16  ? 1902 TYR A CD1   1 
ATOM   3882  C  CD2   . TYR A 1 685  ? 164.081 157.448 137.305 1.00 57.45  ? 1902 TYR A CD2   1 
ATOM   3883  C  CE1   . TYR A 1 685  ? 166.388 158.659 138.203 1.00 65.59  ? 1902 TYR A CE1   1 
ATOM   3884  C  CE2   . TYR A 1 685  ? 165.068 157.795 136.405 1.00 55.54  ? 1902 TYR A CE2   1 
ATOM   3885  C  CZ    . TYR A 1 685  ? 166.220 158.399 136.859 1.00 60.56  ? 1902 TYR A CZ    1 
ATOM   3886  O  OH    . TYR A 1 685  ? 167.208 158.745 135.966 1.00 57.25  ? 1902 TYR A OH    1 
ATOM   3887  N  N     . ARG A 1 688  ? 161.519 153.204 141.678 1.00 69.56  ? 1905 ARG A N     1 
ATOM   3888  C  CA    . ARG A 1 688  ? 160.341 152.992 140.846 1.00 66.14  ? 1905 ARG A CA    1 
ATOM   3889  C  C     . ARG A 1 688  ? 160.524 151.764 139.960 1.00 68.41  ? 1905 ARG A C     1 
ATOM   3890  O  O     . ARG A 1 688  ? 161.488 151.016 140.120 1.00 73.59  ? 1905 ARG A O     1 
ATOM   3891  C  CB    . ARG A 1 688  ? 160.058 154.231 139.995 1.00 62.11  ? 1905 ARG A CB    1 
ATOM   3892  C  CG    . ARG A 1 688  ? 159.413 155.377 140.763 1.00 63.05  ? 1905 ARG A CG    1 
ATOM   3893  C  CD    . ARG A 1 688  ? 158.271 154.893 141.642 1.00 60.85  ? 1905 ARG A CD    1 
ATOM   3894  N  NE    . ARG A 1 688  ? 157.649 155.984 142.384 1.00 60.92  ? 1905 ARG A NE    1 
ATOM   3895  C  CZ    . ARG A 1 688  ? 158.109 156.471 143.528 1.00 67.09  ? 1905 ARG A CZ    1 
ATOM   3896  N  NH1   . ARG A 1 688  ? 159.199 155.985 144.100 1.00 71.94  ? 1905 ARG A NH1   1 
ATOM   3897  N  NH2   . ARG A 1 688  ? 157.456 157.470 144.116 1.00 61.74  ? 1905 ARG A NH2   1 
ATOM   3898  N  N     . SER A 1 689  ? 159.600 151.557 139.029 1.00 65.71  ? 1906 SER A N     1 
ATOM   3899  C  CA    . SER A 1 689  ? 159.600 150.380 138.170 1.00 63.64  ? 1906 SER A CA    1 
ATOM   3900  C  C     . SER A 1 689  ? 159.537 150.796 136.703 1.00 60.63  ? 1906 SER A C     1 
ATOM   3901  O  O     . SER A 1 689  ? 159.435 151.978 136.366 1.00 56.81  ? 1906 SER A O     1 
ATOM   3902  C  CB    . SER A 1 689  ? 158.432 149.454 138.522 1.00 61.02  ? 1906 SER A CB    1 
ATOM   3903  O  OG    . SER A 1 689  ? 157.189 150.095 138.299 1.00 63.48  ? 1906 SER A OG    1 
ATOM   3904  N  N     . GLU A 1 690  ? 159.593 149.795 135.828 1.00 55.94  ? 1907 GLU A N     1 
ATOM   3905  C  CA    . GLU A 1 690  ? 159.521 149.959 134.387 1.00 46.97  ? 1907 GLU A CA    1 
ATOM   3906  C  C     . GLU A 1 690  ? 158.097 149.684 133.913 1.00 39.87  ? 1907 GLU A C     1 
ATOM   3907  O  O     . GLU A 1 690  ? 157.165 149.551 134.714 1.00 45.40  ? 1907 GLU A O     1 
ATOM   3908  C  CB    . GLU A 1 690  ? 160.525 149.034 133.694 1.00 44.17  ? 1907 GLU A CB    1 
ATOM   3909  C  CG    . GLU A 1 690  ? 161.956 149.180 134.171 1.00 49.91  ? 1907 GLU A CG    1 
ATOM   3910  C  CD    . GLU A 1 690  ? 162.900 148.226 133.468 1.00 49.54  ? 1907 GLU A CD    1 
ATOM   3911  O  OE1   . GLU A 1 690  ? 162.436 147.475 132.584 1.00 46.49  ? 1907 GLU A OE1   1 
ATOM   3912  O  OE2   . GLU A 1 690  ? 164.105 148.225 133.797 1.00 47.23  ? 1907 GLU A OE2   1 
ATOM   3913  N  N     . LEU A 1 691  ? 157.930 149.619 132.599 1.00 32.69  ? 1908 LEU A N     1 
ATOM   3914  C  CA    . LEU A 1 691  ? 156.644 149.252 132.028 1.00 30.70  ? 1908 LEU A CA    1 
ATOM   3915  C  C     . LEU A 1 691  ? 156.319 147.801 132.371 1.00 32.55  ? 1908 LEU A C     1 
ATOM   3916  O  O     . LEU A 1 691  ? 157.187 146.929 132.232 1.00 36.40  ? 1908 LEU A O     1 
ATOM   3917  C  CB    . LEU A 1 691  ? 156.670 149.441 130.514 1.00 26.88  ? 1908 LEU A CB    1 
ATOM   3918  C  CG    . LEU A 1 691  ? 155.330 149.607 129.802 1.00 25.27  ? 1908 LEU A CG    1 
ATOM   3919  C  CD1   . LEU A 1 691  ? 154.517 150.726 130.425 1.00 27.64  ? 1908 LEU A CD1   1 
ATOM   3920  C  CD2   . LEU A 1 691  ? 155.566 149.869 128.332 1.00 21.24  ? 1908 LEU A CD2   1 
ATOM   3921  N  N     . PRO A 1 692  ? 155.105 147.503 132.829 1.00 31.69  ? 1909 PRO A N     1 
ATOM   3922  C  CA    . PRO A 1 692  ? 154.736 146.107 133.088 1.00 32.47  ? 1909 PRO A CA    1 
ATOM   3923  C  C     . PRO A 1 692  ? 154.681 145.298 131.801 1.00 31.86  ? 1909 PRO A C     1 
ATOM   3924  O  O     . PRO A 1 692  ? 154.511 145.834 130.705 1.00 34.55  ? 1909 PRO A O     1 
ATOM   3925  C  CB    . PRO A 1 692  ? 153.353 146.214 133.740 1.00 34.67  ? 1909 PRO A CB    1 
ATOM   3926  C  CG    . PRO A 1 692  ? 152.854 147.573 133.377 1.00 32.08  ? 1909 PRO A CG    1 
ATOM   3927  C  CD    . PRO A 1 692  ? 154.065 148.442 133.275 1.00 30.43  ? 1909 PRO A CD    1 
ATOM   3928  N  N     . GLU A 1 693  ? 154.825 143.978 131.963 1.00 33.59  ? 1910 GLU A N     1 
ATOM   3929  C  CA    . GLU A 1 693  ? 155.026 143.082 130.825 1.00 38.47  ? 1910 GLU A CA    1 
ATOM   3930  C  C     . GLU A 1 693  ? 153.842 143.108 129.862 1.00 36.64  ? 1910 GLU A C     1 
ATOM   3931  O  O     . GLU A 1 693  ? 154.027 143.177 128.636 1.00 37.70  ? 1910 GLU A O     1 
ATOM   3932  C  CB    . GLU A 1 693  ? 155.269 141.659 131.326 1.00 43.91  ? 1910 GLU A CB    1 
ATOM   3933  C  CG    . GLU A 1 693  ? 156.350 141.537 132.384 1.00 45.70  ? 1910 GLU A CG    1 
ATOM   3934  C  CD    . GLU A 1 693  ? 155.785 141.536 133.790 1.00 47.42  ? 1910 GLU A CD    1 
ATOM   3935  O  OE1   . GLU A 1 693  ? 154.577 141.811 133.943 1.00 48.55  ? 1910 GLU A OE1   1 
ATOM   3936  O  OE2   . GLU A 1 693  ? 156.544 141.257 134.740 1.00 49.72  ? 1910 GLU A OE2   1 
ATOM   3937  N  N     . ASN A 1 694  ? 152.619 143.052 130.402 1.00 36.58  ? 1911 ASN A N     1 
ATOM   3938  C  CA    . ASN A 1 694  ? 151.422 143.088 129.568 1.00 37.26  ? 1911 ASN A CA    1 
ATOM   3939  C  C     . ASN A 1 694  ? 151.339 144.374 128.759 1.00 35.85  ? 1911 ASN A C     1 
ATOM   3940  O  O     . ASN A 1 694  ? 150.850 144.363 127.624 1.00 37.83  ? 1911 ASN A O     1 
ATOM   3941  C  CB    . ASN A 1 694  ? 150.175 142.913 130.436 1.00 37.57  ? 1911 ASN A CB    1 
ATOM   3942  C  CG    . ASN A 1 694  ? 150.158 143.844 131.631 1.00 34.57  ? 1911 ASN A CG    1 
ATOM   3943  O  OD1   . ASN A 1 694  ? 151.061 144.658 131.811 1.00 34.71  ? 1911 ASN A OD1   1 
ATOM   3944  N  ND2   . ASN A 1 694  ? 149.125 143.727 132.456 1.00 34.66  ? 1911 ASN A ND2   1 
ATOM   3945  N  N     . LEU A 1 695  ? 151.814 145.484 129.317 1.00 34.63  ? 1912 LEU A N     1 
ATOM   3946  C  CA    . LEU A 1 695  ? 151.957 146.709 128.549 1.00 31.38  ? 1912 LEU A CA    1 
ATOM   3947  C  C     . LEU A 1 695  ? 153.302 146.805 127.845 1.00 29.28  ? 1912 LEU A C     1 
ATOM   3948  O  O     . LEU A 1 695  ? 153.462 147.654 126.963 1.00 26.38  ? 1912 LEU A O     1 
ATOM   3949  C  CB    . LEU A 1 695  ? 151.769 147.927 129.456 1.00 26.86  ? 1912 LEU A CB    1 
ATOM   3950  C  CG    . LEU A 1 695  ? 150.363 148.120 130.018 1.00 25.63  ? 1912 LEU A CG    1 
ATOM   3951  C  CD1   . LEU A 1 695  ? 150.242 149.472 130.693 1.00 30.87  ? 1912 LEU A CD1   1 
ATOM   3952  C  CD2   . LEU A 1 695  ? 149.329 147.974 128.919 1.00 27.44  ? 1912 LEU A CD2   1 
ATOM   3953  N  N     . LYS A 1 696  ? 154.268 145.960 128.209 1.00 30.65  ? 1913 LYS A N     1 
ATOM   3954  C  CA    . LYS A 1 696  ? 155.563 145.999 127.540 1.00 31.62  ? 1913 LYS A CA    1 
ATOM   3955  C  C     . LYS A 1 696  ? 155.489 145.379 126.155 1.00 29.15  ? 1913 LYS A C     1 
ATOM   3956  O  O     . LYS A 1 696  ? 156.215 145.800 125.248 1.00 26.68  ? 1913 LYS A O     1 
ATOM   3957  C  CB    . LYS A 1 696  ? 156.618 145.284 128.384 1.00 32.87  ? 1913 LYS A CB    1 
ATOM   3958  C  CG    . LYS A 1 696  ? 158.054 145.520 127.949 1.00 32.63  ? 1913 LYS A CG    1 
ATOM   3959  C  CD    . LYS A 1 696  ? 159.038 145.222 129.074 1.00 30.23  ? 1913 LYS A CD    1 
ATOM   3960  C  CE    . LYS A 1 696  ? 158.679 143.946 129.822 1.00 35.58  ? 1913 LYS A CE    1 
ATOM   3961  N  NZ    . LYS A 1 696  ? 158.762 142.743 128.948 1.00 42.47  ? 1913 LYS A NZ    1 
ATOM   3962  N  N     . LYS A 1 697  ? 154.620 144.387 125.969 1.00 31.00  ? 1914 LYS A N     1 
ATOM   3963  C  CA    . LYS A 1 697  ? 154.500 143.768 124.654 1.00 29.47  ? 1914 LYS A CA    1 
ATOM   3964  C  C     . LYS A 1 697  ? 153.687 144.604 123.672 1.00 29.78  ? 1914 LYS A C     1 
ATOM   3965  O  O     . LYS A 1 697  ? 153.773 144.368 122.462 1.00 27.47  ? 1914 LYS A O     1 
ATOM   3966  C  CB    . LYS A 1 697  ? 153.885 142.372 124.784 1.00 27.60  ? 1914 LYS A CB    1 
ATOM   3967  C  CG    . LYS A 1 697  ? 154.245 141.411 123.652 1.00 30.14  ? 1914 LYS A CG    1 
ATOM   3968  C  CD    . LYS A 1 697  ? 155.696 141.558 123.204 1.00 35.97  ? 1914 LYS A CD    1 
ATOM   3969  C  CE    . LYS A 1 697  ? 156.657 140.848 124.146 1.00 37.81  ? 1914 LYS A CE    1 
ATOM   3970  N  NZ    . LYS A 1 697  ? 158.065 140.953 123.672 1.00 30.54  ? 1914 LYS A NZ    1 
ATOM   3971  N  N     . SER A 1 698  ? 152.918 145.583 124.153 1.00 27.72  ? 1915 SER A N     1 
ATOM   3972  C  CA    . SER A 1 698  ? 152.055 146.384 123.294 1.00 23.24  ? 1915 SER A CA    1 
ATOM   3973  C  C     . SER A 1 698  ? 152.561 147.799 123.050 1.00 21.92  ? 1915 SER A C     1 
ATOM   3974  O  O     . SER A 1 698  ? 151.950 148.524 122.259 1.00 19.64  ? 1915 SER A O     1 
ATOM   3975  C  CB    . SER A 1 698  ? 150.640 146.456 123.887 1.00 23.50  ? 1915 SER A CB    1 
ATOM   3976  O  OG    . SER A 1 698  ? 149.993 145.200 123.807 1.00 22.57  ? 1915 SER A OG    1 
ATOM   3977  N  N     . PHE A 1 699  ? 153.641 148.214 123.701 1.00 21.86  ? 1916 PHE A N     1 
ATOM   3978  C  CA    . PHE A 1 699  ? 154.158 149.569 123.597 1.00 15.38  ? 1916 PHE A CA    1 
ATOM   3979  C  C     . PHE A 1 699  ? 155.536 149.559 122.949 1.00 13.47  ? 1916 PHE A C     1 
ATOM   3980  O  O     . PHE A 1 699  ? 156.129 148.506 122.707 1.00 19.14  ? 1916 PHE A O     1 
ATOM   3981  C  CB    . PHE A 1 699  ? 154.231 150.230 124.977 1.00 17.29  ? 1916 PHE A CB    1 
ATOM   3982  C  CG    . PHE A 1 699  ? 152.944 150.860 125.420 1.00 16.19  ? 1916 PHE A CG    1 
ATOM   3983  C  CD1   . PHE A 1 699  ? 151.845 150.081 125.727 1.00 19.64  ? 1916 PHE A CD1   1 
ATOM   3984  C  CD2   . PHE A 1 699  ? 152.843 152.231 125.559 1.00 12.44  ? 1916 PHE A CD2   1 
ATOM   3985  C  CE1   . PHE A 1 699  ? 150.665 150.660 126.140 1.00 19.06  ? 1916 PHE A CE1   1 
ATOM   3986  C  CE2   . PHE A 1 699  ? 151.666 152.812 125.972 1.00 11.37  ? 1916 PHE A CE2   1 
ATOM   3987  C  CZ    . PHE A 1 699  ? 150.577 152.025 126.264 1.00 12.69  ? 1916 PHE A CZ    1 
ATOM   3988  N  N     . ARG A 1 700  ? 156.047 150.757 122.671 1.00 9.31   ? 1917 ARG A N     1 
ATOM   3989  C  CA    . ARG A 1 700  ? 157.392 150.941 122.127 1.00 10.10  ? 1917 ARG A CA    1 
ATOM   3990  C  C     . ARG A 1 700  ? 158.095 152.003 122.967 1.00 11.75  ? 1917 ARG A C     1 
ATOM   3991  O  O     . ARG A 1 700  ? 157.822 153.197 122.820 1.00 13.99  ? 1917 ARG A O     1 
ATOM   3992  C  CB    . ARG A 1 700  ? 157.350 151.341 120.656 1.00 10.51  ? 1917 ARG A CB    1 
ATOM   3993  C  CG    . ARG A 1 700  ? 157.020 150.205 119.702 1.00 18.27  ? 1917 ARG A CG    1 
ATOM   3994  C  CD    . ARG A 1 700  ? 157.871 148.959 119.942 1.00 18.18  ? 1917 ARG A CD    1 
ATOM   3995  N  NE    . ARG A 1 700  ? 159.302 149.236 120.005 1.00 14.48  ? 1917 ARG A NE    1 
ATOM   3996  C  CZ    . ARG A 1 700  ? 160.079 149.421 118.948 1.00 12.97  ? 1917 ARG A CZ    1 
ATOM   3997  N  NH1   . ARG A 1 700  ? 159.599 149.367 117.718 1.00 11.81  ? 1917 ARG A NH1   1 
ATOM   3998  N  NH2   . ARG A 1 700  ? 161.373 149.665 119.130 1.00 14.82  ? 1917 ARG A NH2   1 
ATOM   3999  N  N     . GLU A 1 701  ? 159.006 151.567 123.832 1.00 10.58  ? 1918 GLU A N     1 
ATOM   4000  C  CA    . GLU A 1 701  ? 159.678 152.473 124.750 1.00 9.63   ? 1918 GLU A CA    1 
ATOM   4001  C  C     . GLU A 1 701  ? 160.652 153.384 124.009 1.00 9.18   ? 1918 GLU A C     1 
ATOM   4002  O  O     . GLU A 1 701  ? 161.027 153.139 122.860 1.00 10.31  ? 1918 GLU A O     1 
ATOM   4003  C  CB    . GLU A 1 701  ? 160.416 151.684 125.828 1.00 14.17  ? 1918 GLU A CB    1 
ATOM   4004  C  CG    . GLU A 1 701  ? 159.521 151.182 126.944 1.00 20.24  ? 1918 GLU A CG    1 
ATOM   4005  C  CD    . GLU A 1 701  ? 159.278 149.690 126.864 1.00 27.63  ? 1918 GLU A CD    1 
ATOM   4006  O  OE1   . GLU A 1 701  ? 159.601 149.089 125.817 1.00 23.74  ? 1918 GLU A OE1   1 
ATOM   4007  O  OE2   . GLU A 1 701  ? 158.768 149.117 127.849 1.00 32.91  ? 1918 GLU A OE2   1 
ATOM   4008  N  N     . PHE A 1 702  ? 161.059 154.455 124.687 1.00 8.95   ? 1919 PHE A N     1 
ATOM   4009  C  CA    . PHE A 1 702  ? 161.984 155.420 124.113 1.00 10.33  ? 1919 PHE A CA    1 
ATOM   4010  C  C     . PHE A 1 702  ? 162.688 156.177 125.229 1.00 11.86  ? 1919 PHE A C     1 
ATOM   4011  O  O     . PHE A 1 702  ? 162.077 156.491 126.252 1.00 15.69  ? 1919 PHE A O     1 
ATOM   4012  C  CB    . PHE A 1 702  ? 161.263 156.405 123.189 1.00 9.38   ? 1919 PHE A CB    1 
ATOM   4013  C  CG    . PHE A 1 702  ? 162.190 157.201 122.326 1.00 8.88   ? 1919 PHE A CG    1 
ATOM   4014  C  CD1   . PHE A 1 702  ? 162.707 156.664 121.163 1.00 8.73   ? 1919 PHE A CD1   1 
ATOM   4015  C  CD2   . PHE A 1 702  ? 162.560 158.481 122.690 1.00 11.01  ? 1919 PHE A CD2   1 
ATOM   4016  C  CE1   . PHE A 1 702  ? 163.565 157.394 120.372 1.00 9.00   ? 1919 PHE A CE1   1 
ATOM   4017  C  CE2   . PHE A 1 702  ? 163.419 159.214 121.904 1.00 11.58  ? 1919 PHE A CE2   1 
ATOM   4018  C  CZ    . PHE A 1 702  ? 163.923 158.669 120.746 1.00 8.54   ? 1919 PHE A CZ    1 
ATOM   4019  N  N     . SER A 1 703  ? 163.964 156.483 125.014 1.00 12.31  ? 1920 SER A N     1 
ATOM   4020  C  CA    . SER A 1 703  ? 164.788 157.195 125.982 1.00 15.04  ? 1920 SER A CA    1 
ATOM   4021  C  C     . SER A 1 703  ? 165.133 158.570 125.427 1.00 18.48  ? 1920 SER A C     1 
ATOM   4022  O  O     . SER A 1 703  ? 165.681 158.678 124.325 1.00 18.93  ? 1920 SER A O     1 
ATOM   4023  C  CB    . SER A 1 703  ? 166.063 156.415 126.290 1.00 15.34  ? 1920 SER A CB    1 
ATOM   4024  O  OG    . SER A 1 703  ? 167.055 156.684 125.316 1.00 15.43  ? 1920 SER A OG    1 
ATOM   4025  N  N     . MET A 1 704  ? 164.829 159.612 126.197 1.00 19.82  ? 1921 MET A N     1 
ATOM   4026  C  CA    . MET A 1 704  ? 164.999 160.997 125.763 1.00 21.31  ? 1921 MET A CA    1 
ATOM   4027  C  C     . MET A 1 704  ? 165.651 161.820 126.874 1.00 23.44  ? 1921 MET A C     1 
ATOM   4028  O  O     . MET A 1 704  ? 165.182 162.894 127.254 1.00 23.97  ? 1921 MET A O     1 
ATOM   4029  C  CB    . MET A 1 704  ? 163.657 161.557 125.293 1.00 17.22  ? 1921 MET A CB    1 
ATOM   4030  C  CG    . MET A 1 704  ? 162.536 161.579 126.319 1.00 16.08  ? 1921 MET A CG    1 
ATOM   4031  S  SD    . MET A 1 704  ? 161.006 162.102 125.529 1.00 23.16  ? 1921 MET A SD    1 
ATOM   4032  C  CE    . MET A 1 704  ? 161.609 163.425 124.483 1.00 14.77  ? 1921 MET A CE    1 
ATOM   4033  N  N     . LYS A 1 705  ? 166.779 161.312 127.382 1.00 28.66  ? 1922 LYS A N     1 
ATOM   4034  C  CA    . LYS A 1 705  ? 167.337 161.786 128.647 1.00 35.56  ? 1922 LYS A CA    1 
ATOM   4035  C  C     . LYS A 1 705  ? 167.779 163.248 128.592 1.00 37.21  ? 1922 LYS A C     1 
ATOM   4036  O  O     . LYS A 1 705  ? 167.578 163.994 129.557 1.00 33.54  ? 1922 LYS A O     1 
ATOM   4037  C  CB    . LYS A 1 705  ? 168.508 160.894 129.060 1.00 32.17  ? 1922 LYS A CB    1 
ATOM   4038  N  N     . SER A 1 706  ? 168.380 163.682 127.485 1.00 37.47  ? 1923 SER A N     1 
ATOM   4039  C  CA    . SER A 1 706  ? 169.053 164.980 127.467 1.00 33.89  ? 1923 SER A CA    1 
ATOM   4040  C  C     . SER A 1 706  ? 168.360 165.973 126.542 1.00 29.98  ? 1923 SER A C     1 
ATOM   4041  O  O     . SER A 1 706  ? 168.514 165.885 125.314 1.00 30.84  ? 1923 SER A O     1 
ATOM   4042  C  CB    . SER A 1 706  ? 170.515 164.801 127.050 1.00 38.44  ? 1923 SER A CB    1 
ATOM   4043  O  OG    . SER A 1 706  ? 170.613 164.509 125.668 1.00 41.26  ? 1923 SER A OG    1 
ATOM   4044  N  N     . PRO A 1 707  ? 167.602 166.935 127.069 1.00 25.50  ? 1924 PRO A N     1 
ATOM   4045  C  CA    . PRO A 1 707  ? 167.072 168.004 126.215 1.00 22.29  ? 1924 PRO A CA    1 
ATOM   4046  C  C     . PRO A 1 707  ? 168.184 168.923 125.744 1.00 18.46  ? 1924 PRO A C     1 
ATOM   4047  O  O     . PRO A 1 707  ? 169.221 169.066 126.395 1.00 19.84  ? 1924 PRO A O     1 
ATOM   4048  C  CB    . PRO A 1 707  ? 166.099 168.752 127.135 1.00 16.95  ? 1924 PRO A CB    1 
ATOM   4049  C  CG    . PRO A 1 707  ? 165.820 167.813 128.257 1.00 20.95  ? 1924 PRO A CG    1 
ATOM   4050  C  CD    . PRO A 1 707  ? 167.086 167.033 128.442 1.00 25.14  ? 1924 PRO A CD    1 
ATOM   4051  N  N     . GLN A 1 708  ? 167.959 169.553 124.594 1.00 15.53  ? 1925 GLN A N     1 
ATOM   4052  C  CA    . GLN A 1 708  ? 168.885 170.562 124.082 1.00 13.00  ? 1925 GLN A CA    1 
ATOM   4053  C  C     . GLN A 1 708  ? 168.480 171.904 124.676 1.00 13.01  ? 1925 GLN A C     1 
ATOM   4054  O  O     . GLN A 1 708  ? 167.660 172.633 124.118 1.00 14.25  ? 1925 GLN A O     1 
ATOM   4055  C  CB    . GLN A 1 708  ? 168.880 170.597 122.560 1.00 11.93  ? 1925 GLN A CB    1 
ATOM   4056  C  CG    . GLN A 1 708  ? 169.676 169.488 121.895 1.00 15.66  ? 1925 GLN A CG    1 
ATOM   4057  C  CD    . GLN A 1 708  ? 168.841 168.260 121.617 1.00 16.81  ? 1925 GLN A CD    1 
ATOM   4058  O  OE1   . GLN A 1 708  ? 167.615 168.301 121.698 1.00 18.39  ? 1925 GLN A OE1   1 
ATOM   4059  N  NE2   . GLN A 1 708  ? 169.499 167.160 121.276 1.00 13.94  ? 1925 GLN A NE2   1 
ATOM   4060  N  N     . SER A 1 709  ? 169.065 172.237 125.827 1.00 12.94  ? 1926 SER A N     1 
ATOM   4061  C  CA    . SER A 1 709  ? 168.792 173.523 126.455 1.00 10.62  ? 1926 SER A CA    1 
ATOM   4062  C  C     . SER A 1 709  ? 169.456 174.682 125.729 1.00 10.36  ? 1926 SER A C     1 
ATOM   4063  O  O     . SER A 1 709  ? 169.153 175.837 126.040 1.00 13.95  ? 1926 SER A O     1 
ATOM   4064  C  CB    . SER A 1 709  ? 169.245 173.504 127.915 1.00 10.75  ? 1926 SER A CB    1 
ATOM   4065  O  OG    . SER A 1 709  ? 168.759 172.357 128.589 1.00 11.92  ? 1926 SER A OG    1 
ATOM   4066  N  N     . GLY A 1 710  ? 170.346 174.408 124.781 1.00 9.11   ? 1927 GLY A N     1 
ATOM   4067  C  CA    . GLY A 1 710  ? 170.986 175.458 124.018 1.00 10.10  ? 1927 GLY A CA    1 
ATOM   4068  C  C     . GLY A 1 710  ? 170.076 176.065 122.973 1.00 11.19  ? 1927 GLY A C     1 
ATOM   4069  O  O     . GLY A 1 710  ? 169.853 177.279 122.966 1.00 12.83  ? 1927 GLY A O     1 
ATOM   4070  N  N     . THR A 1 711  ? 169.535 175.229 122.084 1.00 11.87  ? 1928 THR A N     1 
ATOM   4071  C  CA    . THR A 1 711  ? 168.687 175.751 121.018 1.00 11.77  ? 1928 THR A CA    1 
ATOM   4072  C  C     . THR A 1 711  ? 167.331 176.208 121.544 1.00 10.95  ? 1928 THR A C     1 
ATOM   4073  O  O     . THR A 1 711  ? 166.736 177.131 120.977 1.00 15.34  ? 1928 THR A O     1 
ATOM   4074  C  CB    . THR A 1 711  ? 168.526 174.709 119.907 1.00 12.50  ? 1928 THR A CB    1 
ATOM   4075  O  OG1   . THR A 1 711  ? 167.759 175.267 118.833 1.00 15.44  ? 1928 THR A OG1   1 
ATOM   4076  C  CG2   . THR A 1 711  ? 167.848 173.452 120.417 1.00 12.41  ? 1928 THR A CG2   1 
ATOM   4077  N  N     . ILE A 1 712  ? 166.846 175.611 122.638 1.00 8.82   ? 1929 ILE A N     1 
ATOM   4078  C  CA    . ILE A 1 712  ? 165.614 176.084 123.267 1.00 9.00   ? 1929 ILE A CA    1 
ATOM   4079  C  C     . ILE A 1 712  ? 165.790 177.514 123.758 1.00 11.77  ? 1929 ILE A C     1 
ATOM   4080  O  O     . ILE A 1 712  ? 164.976 178.399 123.465 1.00 14.25  ? 1929 ILE A O     1 
ATOM   4081  C  CB    . ILE A 1 712  ? 165.206 175.149 124.419 1.00 8.76   ? 1929 ILE A CB    1 
ATOM   4082  C  CG1   . ILE A 1 712  ? 164.632 173.849 123.875 1.00 8.21   ? 1929 ILE A CG1   1 
ATOM   4083  C  CG2   . ILE A 1 712  ? 164.196 175.824 125.325 1.00 8.88   ? 1929 ILE A CG2   1 
ATOM   4084  C  CD1   . ILE A 1 712  ? 164.415 172.807 124.935 1.00 9.34   ? 1929 ILE A CD1   1 
ATOM   4085  N  N     . ALA A 1 713  ? 166.873 177.760 124.499 1.00 11.92  ? 1930 ALA A N     1 
ATOM   4086  C  CA    . ALA A 1 713  ? 167.147 179.100 125.000 1.00 10.67  ? 1930 ALA A CA    1 
ATOM   4087  C  C     . ALA A 1 713  ? 167.417 180.070 123.860 1.00 13.30  ? 1930 ALA A C     1 
ATOM   4088  O  O     . ALA A 1 713  ? 166.990 181.228 123.911 1.00 16.50  ? 1930 ALA A O     1 
ATOM   4089  C  CB    . ALA A 1 713  ? 168.327 179.067 125.967 1.00 9.73   ? 1930 ALA A CB    1 
ATOM   4090  N  N     . GLU A 1 714  ? 168.119 179.613 122.819 1.00 11.86  ? 1931 GLU A N     1 
ATOM   4091  C  CA    . GLU A 1 714  ? 168.408 180.482 121.684 1.00 13.51  ? 1931 GLU A CA    1 
ATOM   4092  C  C     . GLU A 1 714  ? 167.132 180.922 120.980 1.00 14.20  ? 1931 GLU A C     1 
ATOM   4093  O  O     . GLU A 1 714  ? 166.960 182.108 120.680 1.00 17.93  ? 1931 GLU A O     1 
ATOM   4094  C  CB    . GLU A 1 714  ? 169.346 179.774 120.708 1.00 18.90  ? 1931 GLU A CB    1 
ATOM   4095  C  CG    . GLU A 1 714  ? 169.397 180.404 119.329 1.00 25.16  ? 1931 GLU A CG    1 
ATOM   4096  C  CD    . GLU A 1 714  ? 170.274 179.628 118.364 1.00 37.48  ? 1931 GLU A CD    1 
ATOM   4097  O  OE1   . GLU A 1 714  ? 171.077 178.792 118.827 1.00 39.35  ? 1931 GLU A OE1   1 
ATOM   4098  O  OE2   . GLU A 1 714  ? 170.160 179.857 117.142 1.00 41.30  ? 1931 GLU A OE2   1 
ATOM   4099  N  N     . MET A 1 715  ? 166.207 179.990 120.746 1.00 14.40  ? 1932 MET A N     1 
ATOM   4100  C  CA    . MET A 1 715  ? 164.971 180.351 120.063 1.00 13.44  ? 1932 MET A CA    1 
ATOM   4101  C  C     . MET A 1 715  ? 164.066 181.199 120.950 1.00 13.33  ? 1932 MET A C     1 
ATOM   4102  O  O     . MET A 1 715  ? 163.408 182.121 120.459 1.00 15.24  ? 1932 MET A O     1 
ATOM   4103  C  CB    . MET A 1 715  ? 164.246 179.097 119.586 1.00 11.59  ? 1932 MET A CB    1 
ATOM   4104  C  CG    . MET A 1 715  ? 164.926 178.408 118.416 1.00 14.29  ? 1932 MET A CG    1 
ATOM   4105  S  SD    . MET A 1 715  ? 165.730 179.582 117.310 1.00 31.65  ? 1932 MET A SD    1 
ATOM   4106  C  CE    . MET A 1 715  ? 166.940 178.534 116.508 1.00 24.48  ? 1932 MET A CE    1 
ATOM   4107  N  N     . ILE A 1 716  ? 164.026 180.919 122.258 1.00 10.92  ? 1933 ILE A N     1 
ATOM   4108  C  CA    . ILE A 1 716  ? 163.213 181.739 123.154 1.00 9.50   ? 1933 ILE A CA    1 
ATOM   4109  C  C     . ILE A 1 716  ? 163.750 183.165 123.218 1.00 12.28  ? 1933 ILE A C     1 
ATOM   4110  O  O     . ILE A 1 716  ? 162.982 184.135 123.168 1.00 14.08  ? 1933 ILE A O     1 
ATOM   4111  C  CB    . ILE A 1 716  ? 163.135 181.096 124.550 1.00 7.79   ? 1933 ILE A CB    1 
ATOM   4112  C  CG1   . ILE A 1 716  ? 162.303 179.820 124.501 1.00 10.37  ? 1933 ILE A CG1   1 
ATOM   4113  C  CG2   . ILE A 1 716  ? 162.506 182.046 125.544 1.00 9.22   ? 1933 ILE A CG2   1 
ATOM   4114  C  CD1   . ILE A 1 716  ? 162.244 179.097 125.819 1.00 10.94  ? 1933 ILE A CD1   1 
ATOM   4115  N  N     . LEU A 1 717  ? 165.075 183.319 123.310 1.00 13.08  ? 1934 LEU A N     1 
ATOM   4116  C  CA    . LEU A 1 717  ? 165.675 184.649 123.332 1.00 14.17  ? 1934 LEU A CA    1 
ATOM   4117  C  C     . LEU A 1 717  ? 165.475 185.375 122.007 1.00 17.30  ? 1934 LEU A C     1 
ATOM   4118  O  O     . LEU A 1 717  ? 165.254 186.591 121.989 1.00 20.77  ? 1934 LEU A O     1 
ATOM   4119  C  CB    . LEU A 1 717  ? 167.160 184.547 123.671 1.00 14.52  ? 1934 LEU A CB    1 
ATOM   4120  C  CG    . LEU A 1 717  ? 167.486 184.285 125.139 1.00 12.52  ? 1934 LEU A CG    1 
ATOM   4121  C  CD1   . LEU A 1 717  ? 168.974 184.069 125.329 1.00 16.58  ? 1934 LEU A CD1   1 
ATOM   4122  C  CD2   . LEU A 1 717  ? 167.009 185.445 125.980 1.00 15.79  ? 1934 LEU A CD2   1 
ATOM   4123  N  N     . GLN A 1 718  ? 165.559 184.650 120.888 1.00 16.26  ? 1935 GLN A N     1 
ATOM   4124  C  CA    . GLN A 1 718  ? 165.309 185.258 119.585 1.00 14.89  ? 1935 GLN A CA    1 
ATOM   4125  C  C     . GLN A 1 718  ? 163.861 185.715 119.455 1.00 14.25  ? 1935 GLN A C     1 
ATOM   4126  O  O     . GLN A 1 718  ? 163.584 186.760 118.855 1.00 15.20  ? 1935 GLN A O     1 
ATOM   4127  C  CB    . GLN A 1 718  ? 165.672 184.267 118.480 1.00 18.21  ? 1935 GLN A CB    1 
ATOM   4128  C  CG    . GLN A 1 718  ? 165.416 184.753 117.070 1.00 20.83  ? 1935 GLN A CG    1 
ATOM   4129  C  CD    . GLN A 1 718  ? 166.348 184.108 116.066 1.00 22.97  ? 1935 GLN A CD    1 
ATOM   4130  O  OE1   . GLN A 1 718  ? 167.127 183.219 116.409 1.00 22.10  ? 1935 GLN A OE1   1 
ATOM   4131  N  NE2   . GLN A 1 718  ? 166.275 184.553 114.818 1.00 22.74  ? 1935 GLN A NE2   1 
ATOM   4132  N  N     . ILE A 1 719  ? 162.925 184.940 120.006 1.00 13.40  ? 1936 ILE A N     1 
ATOM   4133  C  CA    . ILE A 1 719  ? 161.522 185.339 120.012 1.00 14.32  ? 1936 ILE A CA    1 
ATOM   4134  C  C     . ILE A 1 719  ? 161.321 186.584 120.867 1.00 17.39  ? 1936 ILE A C     1 
ATOM   4135  O  O     . ILE A 1 719  ? 160.614 187.518 120.472 1.00 19.41  ? 1936 ILE A O     1 
ATOM   4136  C  CB    . ILE A 1 719  ? 160.648 184.168 120.496 1.00 12.77  ? 1936 ILE A CB    1 
ATOM   4137  C  CG1   . ILE A 1 719  ? 160.444 183.165 119.368 1.00 14.18  ? 1936 ILE A CG1   1 
ATOM   4138  C  CG2   . ILE A 1 719  ? 159.300 184.651 121.009 1.00 12.37  ? 1936 ILE A CG2   1 
ATOM   4139  C  CD1   . ILE A 1 719  ? 160.247 181.771 119.856 1.00 12.55  ? 1936 ILE A CD1   1 
ATOM   4140  N  N     . MET A 1 720  ? 161.956 186.628 122.039 1.00 18.77  ? 1937 MET A N     1 
ATOM   4141  C  CA    . MET A 1 720  ? 161.754 187.739 122.961 1.00 18.43  ? 1937 MET A CA    1 
ATOM   4142  C  C     . MET A 1 720  ? 162.360 189.046 122.470 1.00 20.32  ? 1937 MET A C     1 
ATOM   4143  O  O     . MET A 1 720  ? 162.073 190.095 123.055 1.00 25.27  ? 1937 MET A O     1 
ATOM   4144  C  CB    . MET A 1 720  ? 162.324 187.388 124.334 1.00 19.20  ? 1937 MET A CB    1 
ATOM   4145  C  CG    . MET A 1 720  ? 161.337 186.673 125.234 1.00 18.48  ? 1937 MET A CG    1 
ATOM   4146  S  SD    . MET A 1 720  ? 161.851 186.690 126.955 1.00 17.61  ? 1937 MET A SD    1 
ATOM   4147  C  CE    . MET A 1 720  ? 163.417 185.839 126.826 1.00 14.28  ? 1937 MET A CE    1 
ATOM   4148  N  N     . GLY A 1 721  ? 163.181 189.017 121.427 1.00 19.34  ? 1938 GLY A N     1 
ATOM   4149  C  CA    . GLY A 1 721  ? 163.682 190.229 120.820 1.00 22.68  ? 1938 GLY A CA    1 
ATOM   4150  C  C     . GLY A 1 721  ? 165.098 190.616 121.174 1.00 28.36  ? 1938 GLY A C     1 
ATOM   4151  O  O     . GLY A 1 721  ? 165.511 191.733 120.845 1.00 36.30  ? 1938 GLY A O     1 
ATOM   4152  N  N     . PHE A 1 722  ? 165.849 189.744 121.840 1.00 23.79  ? 1939 PHE A N     1 
ATOM   4153  C  CA    . PHE A 1 722  ? 167.229 190.057 122.179 1.00 26.23  ? 1939 PHE A CA    1 
ATOM   4154  C  C     . PHE A 1 722  ? 168.078 190.139 120.917 1.00 36.02  ? 1939 PHE A C     1 
ATOM   4155  O  O     . PHE A 1 722  ? 167.946 189.317 120.006 1.00 37.28  ? 1939 PHE A O     1 
ATOM   4156  C  CB    . PHE A 1 722  ? 167.798 189.002 123.125 1.00 25.81  ? 1939 PHE A CB    1 
ATOM   4157  C  CG    . PHE A 1 722  ? 167.367 189.167 124.556 1.00 27.25  ? 1939 PHE A CG    1 
ATOM   4158  C  CD1   . PHE A 1 722  ? 166.041 189.012 124.921 1.00 24.20  ? 1939 PHE A CD1   1 
ATOM   4159  C  CD2   . PHE A 1 722  ? 168.293 189.465 125.537 1.00 29.47  ? 1939 PHE A CD2   1 
ATOM   4160  C  CE1   . PHE A 1 722  ? 165.648 189.158 126.235 1.00 22.93  ? 1939 PHE A CE1   1 
ATOM   4161  C  CE2   . PHE A 1 722  ? 167.905 189.612 126.851 1.00 28.91  ? 1939 PHE A CE2   1 
ATOM   4162  C  CZ    . PHE A 1 722  ? 166.581 189.457 127.199 1.00 25.92  ? 1939 PHE A CZ    1 
ATOM   4163  N  N     . GLU A 1 723  ? 168.946 191.152 120.862 1.00 44.42  ? 1940 GLU A N     1 
ATOM   4164  C  CA    . GLU A 1 723  ? 169.780 191.352 119.680 1.00 49.22  ? 1940 GLU A CA    1 
ATOM   4165  C  C     . GLU A 1 723  ? 170.807 190.235 119.537 1.00 46.67  ? 1940 GLU A C     1 
ATOM   4166  O  O     . GLU A 1 723  ? 170.984 189.675 118.449 1.00 48.32  ? 1940 GLU A O     1 
ATOM   4167  C  CB    . GLU A 1 723  ? 170.466 192.717 119.751 1.00 54.63  ? 1940 GLU A CB    1 
ATOM   4168  C  CG    . GLU A 1 723  ? 171.673 192.863 118.838 1.00 56.98  ? 1940 GLU A CG    1 
ATOM   4169  C  CD    . GLU A 1 723  ? 172.539 194.053 119.204 1.00 61.65  ? 1940 GLU A CD    1 
ATOM   4170  O  OE1   . GLU A 1 723  ? 173.469 193.886 120.020 1.00 60.34  ? 1940 GLU A OE1   1 
ATOM   4171  O  OE2   . GLU A 1 723  ? 172.288 195.156 118.674 1.00 63.26  ? 1940 GLU A OE2   1 
ATOM   4172  N  N     . ASP A 1 724  ? 171.486 189.895 120.626 1.00 42.73  ? 1941 ASP A N     1 
ATOM   4173  C  CA    . ASP A 1 724  ? 172.425 188.777 120.663 1.00 45.53  ? 1941 ASP A CA    1 
ATOM   4174  C  C     . ASP A 1 724  ? 171.761 187.667 121.470 1.00 44.99  ? 1941 ASP A C     1 
ATOM   4175  O  O     . ASP A 1 724  ? 171.693 187.740 122.700 1.00 46.99  ? 1941 ASP A O     1 
ATOM   4176  C  CB    . ASP A 1 724  ? 173.758 189.201 121.271 1.00 45.32  ? 1941 ASP A CB    1 
ATOM   4177  C  CG    . ASP A 1 724  ? 174.906 188.310 120.840 1.00 43.67  ? 1941 ASP A CG    1 
ATOM   4178  O  OD1   . ASP A 1 724  ? 174.670 187.111 120.583 1.00 37.74  ? 1941 ASP A OD1   1 
ATOM   4179  O  OD2   . ASP A 1 724  ? 176.047 188.810 120.756 1.00 49.77  ? 1941 ASP A OD2   1 
ATOM   4180  N  N     . SER A 1 725  ? 171.269 186.644 120.777 1.00 38.13  ? 1942 SER A N     1 
ATOM   4181  C  CA    . SER A 1 725  ? 170.523 185.563 121.409 1.00 29.82  ? 1942 SER A CA    1 
ATOM   4182  C  C     . SER A 1 725  ? 171.281 184.248 121.466 1.00 29.64  ? 1942 SER A C     1 
ATOM   4183  O  O     . SER A 1 725  ? 171.185 183.538 122.466 1.00 29.63  ? 1942 SER A O     1 
ATOM   4184  C  CB    . SER A 1 725  ? 169.194 185.343 120.679 1.00 24.77  ? 1942 SER A CB    1 
ATOM   4185  O  OG    . SER A 1 725  ? 169.409 185.039 119.314 1.00 31.87  ? 1942 SER A OG    1 
ATOM   4186  N  N     . LYS A 1 726  ? 172.036 183.904 120.420 1.00 33.54  ? 1943 LYS A N     1 
ATOM   4187  C  CA    . LYS A 1 726  ? 172.760 182.635 120.410 1.00 35.35  ? 1943 LYS A CA    1 
ATOM   4188  C  C     . LYS A 1 726  ? 173.863 182.619 121.463 1.00 34.34  ? 1943 LYS A C     1 
ATOM   4189  O  O     . LYS A 1 726  ? 173.965 181.675 122.259 1.00 32.79  ? 1943 LYS A O     1 
ATOM   4190  C  CB    . LYS A 1 726  ? 173.344 182.378 119.021 1.00 37.81  ? 1943 LYS A CB    1 
ATOM   4191  C  CG    . LYS A 1 726  ? 172.329 182.452 117.892 1.00 40.61  ? 1943 LYS A CG    1 
ATOM   4192  C  CD    . LYS A 1 726  ? 172.505 183.718 117.067 1.00 41.14  ? 1943 LYS A CD    1 
ATOM   4193  C  CE    . LYS A 1 726  ? 171.668 183.671 115.800 1.00 46.00  ? 1943 LYS A CE    1 
ATOM   4194  N  NZ    . LYS A 1 726  ? 171.706 184.962 115.059 1.00 51.77  ? 1943 LYS A NZ    1 
ATOM   4195  N  N     . SER A 1 727  ? 174.698 183.662 121.480 1.00 34.91  ? 1944 SER A N     1 
ATOM   4196  C  CA    . SER A 1 727  ? 175.784 183.733 122.451 1.00 32.75  ? 1944 SER A CA    1 
ATOM   4197  C  C     . SER A 1 727  ? 175.248 183.879 123.868 1.00 30.48  ? 1944 SER A C     1 
ATOM   4198  O  O     . SER A 1 727  ? 175.804 183.300 124.808 1.00 28.80  ? 1944 SER A O     1 
ATOM   4199  C  CB    . SER A 1 727  ? 176.719 184.890 122.107 1.00 35.95  ? 1944 SER A CB    1 
ATOM   4200  O  OG    . SER A 1 727  ? 177.906 184.829 122.877 1.00 35.58  ? 1944 SER A OG    1 
ATOM   4201  N  N     . LEU A 1 728  ? 174.167 184.644 124.040 1.00 31.06  ? 1945 LEU A N     1 
ATOM   4202  C  CA    . LEU A 1 728  ? 173.551 184.768 125.357 1.00 27.62  ? 1945 LEU A CA    1 
ATOM   4203  C  C     . LEU A 1 728  ? 173.004 183.432 125.842 1.00 25.35  ? 1945 LEU A C     1 
ATOM   4204  O  O     . LEU A 1 728  ? 173.153 183.086 127.017 1.00 25.47  ? 1945 LEU A O     1 
ATOM   4205  C  CB    . LEU A 1 728  ? 172.441 185.818 125.326 1.00 26.07  ? 1945 LEU A CB    1 
ATOM   4206  C  CG    . LEU A 1 728  ? 172.824 187.220 125.797 1.00 27.27  ? 1945 LEU A CG    1 
ATOM   4207  C  CD1   . LEU A 1 728  ? 171.583 188.072 125.983 1.00 22.36  ? 1945 LEU A CD1   1 
ATOM   4208  C  CD2   . LEU A 1 728  ? 173.631 187.155 127.083 1.00 30.92  ? 1945 LEU A CD2   1 
ATOM   4209  N  N     . ALA A 1 729  ? 172.366 182.670 124.951 1.00 24.51  ? 1946 ALA A N     1 
ATOM   4210  C  CA    . ALA A 1 729  ? 171.846 181.360 125.329 1.00 21.78  ? 1946 ALA A CA    1 
ATOM   4211  C  C     . ALA A 1 729  ? 172.970 180.404 125.699 1.00 24.42  ? 1946 ALA A C     1 
ATOM   4212  O  O     . ALA A 1 729  ? 172.856 179.644 126.670 1.00 26.05  ? 1946 ALA A O     1 
ATOM   4213  C  CB    . ALA A 1 729  ? 171.014 180.782 124.191 1.00 20.34  ? 1946 ALA A CB    1 
ATOM   4214  N  N     . SER A 1 730  ? 174.064 180.425 124.932 1.00 25.22  ? 1947 SER A N     1 
ATOM   4215  C  CA    . SER A 1 730  ? 175.216 179.594 125.267 1.00 22.24  ? 1947 SER A CA    1 
ATOM   4216  C  C     . SER A 1 730  ? 175.802 179.988 126.616 1.00 22.13  ? 1947 SER A C     1 
ATOM   4217  O  O     . SER A 1 730  ? 176.167 179.121 127.419 1.00 21.71  ? 1947 SER A O     1 
ATOM   4218  C  CB    . SER A 1 730  ? 176.275 179.698 124.172 1.00 23.87  ? 1947 SER A CB    1 
ATOM   4219  O  OG    . SER A 1 730  ? 177.483 179.080 124.577 1.00 23.37  ? 1947 SER A OG    1 
ATOM   4220  N  N     . LYS A 1 731  ? 175.884 181.294 126.886 1.00 22.03  ? 1948 LYS A N     1 
ATOM   4221  C  CA    . LYS A 1 731  ? 176.389 181.768 128.171 1.00 21.20  ? 1948 LYS A CA    1 
ATOM   4222  C  C     . LYS A 1 731  ? 175.494 181.323 129.320 1.00 21.09  ? 1948 LYS A C     1 
ATOM   4223  O  O     . LYS A 1 731  ? 175.990 180.906 130.371 1.00 21.33  ? 1948 LYS A O     1 
ATOM   4224  C  CB    . LYS A 1 731  ? 176.510 183.291 128.155 1.00 23.84  ? 1948 LYS A CB    1 
ATOM   4225  C  CG    . LYS A 1 731  ? 177.818 183.815 127.597 1.00 25.82  ? 1948 LYS A CG    1 
ATOM   4226  C  CD    . LYS A 1 731  ? 177.814 185.332 127.562 1.00 29.55  ? 1948 LYS A CD    1 
ATOM   4227  C  CE    . LYS A 1 731  ? 178.707 185.862 126.456 1.00 34.43  ? 1948 LYS A CE    1 
ATOM   4228  N  NZ    . LYS A 1 731  ? 178.364 187.267 126.102 1.00 37.94  ? 1948 LYS A NZ    1 
ATOM   4229  N  N     . ILE A 1 732  ? 174.173 181.408 129.138 1.00 20.45  ? 1949 ILE A N     1 
ATOM   4230  C  CA    . ILE A 1 732  ? 173.245 181.001 130.192 1.00 17.73  ? 1949 ILE A CA    1 
ATOM   4231  C  C     . ILE A 1 732  ? 173.358 179.507 130.460 1.00 19.32  ? 1949 ILE A C     1 
ATOM   4232  O  O     . ILE A 1 732  ? 173.395 179.072 131.618 1.00 22.19  ? 1949 ILE A O     1 
ATOM   4233  C  CB    . ILE A 1 732  ? 171.802 181.399 129.827 1.00 13.88  ? 1949 ILE A CB    1 
ATOM   4234  C  CG1   . ILE A 1 732  ? 171.646 182.915 129.798 1.00 15.45  ? 1949 ILE A CG1   1 
ATOM   4235  C  CG2   . ILE A 1 732  ? 170.823 180.833 130.831 1.00 13.94  ? 1949 ILE A CG2   1 
ATOM   4236  C  CD1   . ILE A 1 732  ? 170.270 183.357 129.370 1.00 15.50  ? 1949 ILE A CD1   1 
ATOM   4237  N  N     . VAL A 1 733  ? 173.420 178.697 129.399 1.00 17.34  ? 1950 VAL A N     1 
ATOM   4238  C  CA    . VAL A 1 733  ? 173.521 177.249 129.575 1.00 15.85  ? 1950 VAL A CA    1 
ATOM   4239  C  C     . VAL A 1 733  ? 174.832 176.883 130.262 1.00 20.20  ? 1950 VAL A C     1 
ATOM   4240  O  O     . VAL A 1 733  ? 174.859 176.056 131.184 1.00 22.93  ? 1950 VAL A O     1 
ATOM   4241  C  CB    . VAL A 1 733  ? 173.367 176.536 128.219 1.00 16.95  ? 1950 VAL A CB    1 
ATOM   4242  C  CG1   . VAL A 1 733  ? 173.756 175.073 128.331 1.00 18.91  ? 1950 VAL A CG1   1 
ATOM   4243  C  CG2   . VAL A 1 733  ? 171.941 176.665 127.723 1.00 17.43  ? 1950 VAL A CG2   1 
ATOM   4244  N  N     . HIS A 1 734  ? 175.934 177.512 129.842 1.00 20.45  ? 1951 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 734  ? 177.229 177.251 130.460 1.00 21.45  ? 1951 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 734  ? 177.239 177.667 131.927 1.00 23.00  ? 1951 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 734  ? 177.776 176.951 132.780 1.00 25.96  ? 1951 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 734  ? 178.318 177.983 129.678 1.00 19.68  ? 1951 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 734  ? 179.710 177.653 130.113 1.00 20.29  ? 1951 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 734  ? 180.660 178.621 130.358 1.00 22.68  ? 1951 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 734  ? 180.320 176.464 130.327 1.00 21.86  ? 1951 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 734  ? 181.792 178.042 130.716 1.00 24.49  ? 1951 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 734  ? 181.613 176.734 130.702 1.00 23.61  ? 1951 HIS A NE2   1 
ATOM   4254  N  N     . PHE A 1 735  ? 176.643 178.820 132.239 1.00 19.36  ? 1952 PHE A N     1 
ATOM   4255  C  CA    . PHE A 1 735  ? 176.599 179.297 133.617 1.00 18.01  ? 1952 PHE A CA    1 
ATOM   4256  C  C     . PHE A 1 735  ? 175.767 178.377 134.498 1.00 19.08  ? 1952 PHE A C     1 
ATOM   4257  O  O     . PHE A 1 735  ? 176.145 178.095 135.641 1.00 24.50  ? 1952 PHE A O     1 
ATOM   4258  C  CB    . PHE A 1 735  ? 176.045 180.720 133.651 1.00 20.10  ? 1952 PHE A CB    1 
ATOM   4259  C  CG    . PHE A 1 735  ? 175.889 181.276 135.031 1.00 19.90  ? 1952 PHE A CG    1 
ATOM   4260  C  CD1   . PHE A 1 735  ? 176.994 181.478 135.835 1.00 25.07  ? 1952 PHE A CD1   1 
ATOM   4261  C  CD2   . PHE A 1 735  ? 174.640 181.599 135.524 1.00 18.55  ? 1952 PHE A CD2   1 
ATOM   4262  C  CE1   . PHE A 1 735  ? 176.856 181.991 137.105 1.00 25.14  ? 1952 PHE A CE1   1 
ATOM   4263  C  CE2   . PHE A 1 735  ? 174.497 182.112 136.794 1.00 19.41  ? 1952 PHE A CE2   1 
ATOM   4264  C  CZ    . PHE A 1 735  ? 175.608 182.308 137.583 1.00 22.29  ? 1952 PHE A CZ    1 
ATOM   4265  N  N     . LEU A 1 736  ? 174.630 177.901 133.987 1.00 18.70  ? 1953 LEU A N     1 
ATOM   4266  C  CA    . LEU A 1 736  ? 173.809 176.973 134.758 1.00 19.52  ? 1953 LEU A CA    1 
ATOM   4267  C  C     . LEU A 1 736  ? 174.524 175.642 134.958 1.00 22.61  ? 1953 LEU A C     1 
ATOM   4268  O  O     . LEU A 1 736  ? 174.411 175.027 136.026 1.00 25.97  ? 1953 LEU A O     1 
ATOM   4269  C  CB    . LEU A 1 736  ? 172.459 176.770 134.069 1.00 21.09  ? 1953 LEU A CB    1 
ATOM   4270  C  CG    . LEU A 1 736  ? 171.284 177.662 134.488 1.00 17.61  ? 1953 LEU A CG    1 
ATOM   4271  C  CD1   . LEU A 1 736  ? 170.920 177.415 135.933 1.00 18.47  ? 1953 LEU A CD1   1 
ATOM   4272  C  CD2   . LEU A 1 736  ? 171.560 179.138 134.264 1.00 14.00  ? 1953 LEU A CD2   1 
ATOM   4273  N  N     . GLU A 1 737  ? 175.279 175.189 133.951 1.00 22.99  ? 1954 GLU A N     1 
ATOM   4274  C  CA    . GLU A 1 737  ? 176.080 173.978 134.112 1.00 25.36  ? 1954 GLU A CA    1 
ATOM   4275  C  C     . GLU A 1 737  ? 177.145 174.155 135.189 1.00 28.13  ? 1954 GLU A C     1 
ATOM   4276  O  O     . GLU A 1 737  ? 177.354 173.263 136.020 1.00 27.93  ? 1954 GLU A O     1 
ATOM   4277  C  CB    . GLU A 1 737  ? 176.732 173.598 132.782 1.00 25.35  ? 1954 GLU A CB    1 
ATOM   4278  C  CG    . GLU A 1 737  ? 175.803 172.918 131.794 1.00 32.95  ? 1954 GLU A CG    1 
ATOM   4279  C  CD    . GLU A 1 737  ? 176.510 172.526 130.511 1.00 37.88  ? 1954 GLU A CD    1 
ATOM   4280  O  OE1   . GLU A 1 737  ? 177.756 172.454 130.518 1.00 36.97  ? 1954 GLU A OE1   1 
ATOM   4281  O  OE2   . GLU A 1 737  ? 175.822 172.292 129.495 1.00 40.39  ? 1954 GLU A OE2   1 
ATOM   4282  N  N     . LEU A 1 738  ? 177.825 175.304 135.190 1.00 29.06  ? 1955 LEU A N     1 
ATOM   4283  C  CA    . LEU A 1 738  ? 178.838 175.569 136.209 1.00 25.77  ? 1955 LEU A CA    1 
ATOM   4284  C  C     . LEU A 1 738  ? 178.233 175.684 137.601 1.00 24.68  ? 1955 LEU A C     1 
ATOM   4285  O  O     . LEU A 1 738  ? 178.852 175.248 138.576 1.00 27.19  ? 1955 LEU A O     1 
ATOM   4286  C  CB    . LEU A 1 738  ? 179.630 176.830 135.867 1.00 22.16  ? 1955 LEU A CB    1 
ATOM   4287  C  CG    . LEU A 1 738  ? 180.905 176.651 135.036 1.00 26.86  ? 1955 LEU A CG    1 
ATOM   4288  C  CD1   . LEU A 1 738  ? 180.683 175.855 133.764 1.00 28.11  ? 1955 LEU A CD1   1 
ATOM   4289  C  CD2   . LEU A 1 738  ? 181.503 178.006 134.710 1.00 27.95  ? 1955 LEU A CD2   1 
ATOM   4290  N  N     . LEU A 1 739  ? 177.043 176.271 137.722 1.00 22.65  ? 1956 LEU A N     1 
ATOM   4291  C  CA    . LEU A 1 739  ? 176.391 176.321 139.026 1.00 24.23  ? 1956 LEU A CA    1 
ATOM   4292  C  C     . LEU A 1 739  ? 175.954 174.935 139.482 1.00 28.51  ? 1956 LEU A C     1 
ATOM   4293  O  O     . LEU A 1 739  ? 176.006 174.626 140.677 1.00 34.22  ? 1956 LEU A O     1 
ATOM   4294  C  CB    . LEU A 1 739  ? 175.197 177.270 138.990 1.00 24.11  ? 1956 LEU A CB    1 
ATOM   4295  C  CG    . LEU A 1 739  ? 175.497 178.764 138.914 1.00 25.58  ? 1956 LEU A CG    1 
ATOM   4296  C  CD1   . LEU A 1 739  ? 174.259 179.536 139.315 1.00 23.59  ? 1956 LEU A CD1   1 
ATOM   4297  C  CD2   . LEU A 1 739  ? 176.673 179.128 139.803 1.00 26.10  ? 1956 LEU A CD2   1 
ATOM   4298  N  N     . SER A 1 740  ? 175.512 174.088 138.551 1.00 25.67  ? 1957 SER A N     1 
ATOM   4299  C  CA    . SER A 1 740  ? 175.119 172.736 138.929 1.00 27.97  ? 1957 SER A CA    1 
ATOM   4300  C  C     . SER A 1 740  ? 176.324 171.886 139.307 1.00 31.27  ? 1957 SER A C     1 
ATOM   4301  O  O     . SER A 1 740  ? 176.204 170.975 140.134 1.00 34.30  ? 1957 SER A O     1 
ATOM   4302  C  CB    . SER A 1 740  ? 174.341 172.077 137.790 1.00 30.66  ? 1957 SER A CB    1 
ATOM   4303  O  OG    . SER A 1 740  ? 173.848 170.806 138.178 1.00 38.85  ? 1957 SER A OG    1 
ATOM   4304  N  N     . SER A 1 741  ? 177.486 172.165 138.717 1.00 30.69  ? 1958 SER A N     1 
ATOM   4305  C  CA    . SER A 1 741  ? 178.681 171.373 138.980 1.00 30.28  ? 1958 SER A CA    1 
ATOM   4306  C  C     . SER A 1 741  ? 179.483 171.861 140.180 1.00 29.24  ? 1958 SER A C     1 
ATOM   4307  O  O     . SER A 1 741  ? 180.113 171.045 140.862 1.00 32.14  ? 1958 SER A O     1 
ATOM   4308  C  CB    . SER A 1 741  ? 179.583 171.362 137.743 1.00 29.68  ? 1958 SER A CB    1 
ATOM   4309  O  OG    . SER A 1 741  ? 180.852 170.810 138.045 1.00 29.89  ? 1958 SER A OG    1 
ATOM   4310  N  N     . LYS A 1 742  ? 179.477 173.163 140.459 1.00 26.65  ? 1959 LYS A N     1 
ATOM   4311  C  CA    . LYS A 1 742  ? 180.351 173.742 141.472 1.00 27.87  ? 1959 LYS A CA    1 
ATOM   4312  C  C     . LYS A 1 742  ? 179.673 173.972 142.813 1.00 31.79  ? 1959 LYS A C     1 
ATOM   4313  O  O     . LYS A 1 742  ? 180.323 173.816 143.852 1.00 34.33  ? 1959 LYS A O     1 
ATOM   4314  C  CB    . LYS A 1 742  ? 180.927 175.071 140.974 1.00 25.76  ? 1959 LYS A CB    1 
ATOM   4315  C  CG    . LYS A 1 742  ? 182.062 174.913 139.983 1.00 27.65  ? 1959 LYS A CG    1 
ATOM   4316  C  CD    . LYS A 1 742  ? 182.838 176.207 139.824 1.00 31.38  ? 1959 LYS A CD    1 
ATOM   4317  C  CE    . LYS A 1 742  ? 183.913 176.073 138.760 1.00 34.26  ? 1959 LYS A CE    1 
ATOM   4318  N  NZ    . LYS A 1 742  ? 183.687 177.003 137.621 1.00 36.85  ? 1959 LYS A NZ    1 
ATOM   4319  N  N     . CYS A 1 743  ? 178.396 174.345 142.826 1.00 29.69  ? 1960 CYS A N     1 
ATOM   4320  C  CA    . CYS A 1 743  ? 177.718 174.628 144.080 1.00 27.96  ? 1960 CYS A CA    1 
ATOM   4321  C  C     . CYS A 1 743  ? 177.475 173.339 144.861 1.00 32.51  ? 1960 CYS A C     1 
ATOM   4322  O  O     . CYS A 1 743  ? 177.651 172.226 144.356 1.00 37.56  ? 1960 CYS A O     1 
ATOM   4323  C  CB    . CYS A 1 743  ? 176.400 175.357 143.829 1.00 28.35  ? 1960 CYS A CB    1 
ATOM   4324  S  SG    . CYS A 1 743  ? 176.587 177.107 143.414 1.00 41.90  ? 1960 CYS A SG    1 
ATOM   4325  N  N     . SER A 1 744  ? 177.064 173.504 146.115 1.00 31.68  ? 1961 SER A N     1 
ATOM   4326  C  CA    . SER A 1 744  ? 176.882 172.376 147.013 1.00 31.41  ? 1961 SER A CA    1 
ATOM   4327  C  C     . SER A 1 744  ? 175.695 171.521 146.573 1.00 31.68  ? 1961 SER A C     1 
ATOM   4328  O  O     . SER A 1 744  ? 174.871 171.920 145.746 1.00 33.38  ? 1961 SER A O     1 
ATOM   4329  C  CB    . SER A 1 744  ? 176.684 172.865 148.446 1.00 30.88  ? 1961 SER A CB    1 
ATOM   4330  O  OG    . SER A 1 744  ? 177.643 173.853 148.780 1.00 31.83  ? 1961 SER A OG    1 
ATOM   4331  N  N     . SER A 1 745  ? 175.620 170.318 147.133 1.00 31.80  ? 1962 SER A N     1 
ATOM   4332  C  CA    . SER A 1 745  ? 174.571 169.365 146.776 1.00 34.34  ? 1962 SER A CA    1 
ATOM   4333  C  C     . SER A 1 745  ? 173.358 169.486 147.694 1.00 37.58  ? 1962 SER A C     1 
ATOM   4334  O  O     . SER A 1 745  ? 172.903 168.508 148.285 1.00 43.07  ? 1962 SER A O     1 
ATOM   4335  C  CB    . SER A 1 745  ? 175.131 167.948 146.796 1.00 31.64  ? 1962 SER A CB    1 
ATOM   4336  N  N     . MET A 1 746  ? 172.823 170.696 147.821 1.00 32.49  ? 1963 MET A N     1 
ATOM   4337  C  CA    . MET A 1 746  ? 171.606 170.896 148.591 1.00 30.97  ? 1963 MET A CA    1 
ATOM   4338  C  C     . MET A 1 746  ? 170.396 170.406 147.806 1.00 30.69  ? 1963 MET A C     1 
ATOM   4339  O  O     . MET A 1 746  ? 170.404 170.360 146.574 1.00 29.44  ? 1963 MET A O     1 
ATOM   4340  C  CB    . MET A 1 746  ? 171.435 172.368 148.965 1.00 31.24  ? 1963 MET A CB    1 
ATOM   4341  C  CG    . MET A 1 746  ? 172.436 172.859 149.998 1.00 32.25  ? 1963 MET A CG    1 
ATOM   4342  S  SD    . MET A 1 746  ? 172.445 174.652 150.177 1.00 32.72  ? 1963 MET A SD    1 
ATOM   4343  C  CE    . MET A 1 746  ? 173.301 174.831 151.740 1.00 21.37  ? 1963 MET A CE    1 
ATOM   4344  N  N     . ASN A 1 747  ? 169.347 170.032 148.542 1.00 32.20  ? 1964 ASN A N     1 
ATOM   4345  C  CA    . ASN A 1 747  ? 168.177 169.427 147.914 1.00 37.58  ? 1964 ASN A CA    1 
ATOM   4346  C  C     . ASN A 1 747  ? 167.384 170.429 147.085 1.00 38.48  ? 1964 ASN A C     1 
ATOM   4347  O  O     . ASN A 1 747  ? 166.798 170.056 146.063 1.00 43.55  ? 1964 ASN A O     1 
ATOM   4348  C  CB    . ASN A 1 747  ? 167.279 168.799 148.980 1.00 42.51  ? 1964 ASN A CB    1 
ATOM   4349  C  CG    . ASN A 1 747  ? 166.510 167.602 148.460 1.00 52.81  ? 1964 ASN A CG    1 
ATOM   4350  O  OD1   . ASN A 1 747  ? 166.361 167.423 147.252 1.00 51.41  ? 1964 ASN A OD1   1 
ATOM   4351  N  ND2   . ASN A 1 747  ? 166.017 166.774 149.373 1.00 58.90  ? 1964 ASN A ND2   1 
ATOM   4352  N  N     . HIS A 1 748  ? 167.352 171.696 147.498 1.00 35.82  ? 1965 HIS A N     1 
ATOM   4353  C  CA    . HIS A 1 748  ? 166.509 172.698 146.860 1.00 32.50  ? 1965 HIS A CA    1 
ATOM   4354  C  C     . HIS A 1 748  ? 167.176 173.360 145.658 1.00 29.69  ? 1965 HIS A C     1 
ATOM   4355  O  O     . HIS A 1 748  ? 166.699 174.399 145.191 1.00 28.30  ? 1965 HIS A O     1 
ATOM   4356  C  CB    . HIS A 1 748  ? 166.080 173.753 147.883 1.00 29.56  ? 1965 HIS A CB    1 
ATOM   4357  C  CG    . HIS A 1 748  ? 167.163 174.716 148.258 1.00 23.02  ? 1965 HIS A CG    1 
ATOM   4358  N  ND1   . HIS A 1 748  ? 168.073 174.459 149.261 1.00 24.11  ? 1965 HIS A ND1   1 
ATOM   4359  C  CD2   . HIS A 1 748  ? 167.473 175.942 147.775 1.00 19.87  ? 1965 HIS A CD2   1 
ATOM   4360  C  CE1   . HIS A 1 748  ? 168.901 175.482 149.373 1.00 23.41  ? 1965 HIS A CE1   1 
ATOM   4361  N  NE2   . HIS A 1 748  ? 168.557 176.396 148.484 1.00 20.46  ? 1965 HIS A NE2   1 
ATOM   4362  N  N     . TYR A 1 749  ? 168.254 172.779 145.142 1.00 29.30  ? 1966 TYR A N     1 
ATOM   4363  C  CA    . TYR A 1 749  ? 168.953 173.328 143.989 1.00 28.37  ? 1966 TYR A CA    1 
ATOM   4364  C  C     . TYR A 1 749  ? 168.440 172.665 142.717 1.00 30.18  ? 1966 TYR A C     1 
ATOM   4365  O  O     . TYR A 1 749  ? 168.568 171.447 142.551 1.00 31.49  ? 1966 TYR A O     1 
ATOM   4366  C  CB    . TYR A 1 749  ? 170.460 173.125 144.124 1.00 26.72  ? 1966 TYR A CB    1 
ATOM   4367  C  CG    . TYR A 1 749  ? 171.120 174.068 145.099 1.00 25.49  ? 1966 TYR A CG    1 
ATOM   4368  C  CD1   . TYR A 1 749  ? 170.446 175.175 145.587 1.00 27.23  ? 1966 TYR A CD1   1 
ATOM   4369  C  CD2   . TYR A 1 749  ? 172.417 173.848 145.533 1.00 27.30  ? 1966 TYR A CD2   1 
ATOM   4370  C  CE1   . TYR A 1 749  ? 171.046 176.035 146.477 1.00 26.31  ? 1966 TYR A CE1   1 
ATOM   4371  C  CE2   . TYR A 1 749  ? 173.025 174.704 146.424 1.00 27.16  ? 1966 TYR A CE2   1 
ATOM   4372  C  CZ    . TYR A 1 749  ? 172.334 175.796 146.892 1.00 24.46  ? 1966 TYR A CZ    1 
ATOM   4373  O  OH    . TYR A 1 749  ? 172.931 176.654 147.782 1.00 24.09  ? 1966 TYR A OH    1 
ATOM   4374  N  N     . HIS A 1 750  ? 167.860 173.464 141.825 1.00 27.52  ? 1967 HIS A N     1 
ATOM   4375  C  CA    . HIS A 1 750  ? 167.448 173.002 140.503 1.00 25.23  ? 1967 HIS A CA    1 
ATOM   4376  C  C     . HIS A 1 750  ? 168.013 173.970 139.475 1.00 24.53  ? 1967 HIS A C     1 
ATOM   4377  O  O     . HIS A 1 750  ? 167.583 175.126 139.404 1.00 25.60  ? 1967 HIS A O     1 
ATOM   4378  C  CB    . HIS A 1 750  ? 165.927 172.907 140.391 1.00 25.52  ? 1967 HIS A CB    1 
ATOM   4379  C  CG    . HIS A 1 750  ? 165.450 172.481 139.038 1.00 26.25  ? 1967 HIS A CG    1 
ATOM   4380  N  ND1   . HIS A 1 750  ? 166.024 171.441 138.340 1.00 26.91  ? 1967 HIS A ND1   1 
ATOM   4381  C  CD2   . HIS A 1 750  ? 164.451 172.954 138.255 1.00 25.86  ? 1967 HIS A CD2   1 
ATOM   4382  C  CE1   . HIS A 1 750  ? 165.401 171.292 137.184 1.00 24.06  ? 1967 HIS A CE1   1 
ATOM   4383  N  NE2   . HIS A 1 750  ? 164.442 172.197 137.108 1.00 25.42  ? 1967 HIS A NE2   1 
ATOM   4384  N  N     . PHE A 1 751  ? 168.974 173.499 138.680 1.00 23.99  ? 1968 PHE A N     1 
ATOM   4385  C  CA    . PHE A 1 751  ? 169.646 174.328 137.686 1.00 22.81  ? 1968 PHE A CA    1 
ATOM   4386  C  C     . PHE A 1 751  ? 169.373 173.853 136.265 1.00 22.55  ? 1968 PHE A C     1 
ATOM   4387  O  O     . PHE A 1 751  ? 170.137 174.174 135.351 1.00 25.40  ? 1968 PHE A O     1 
ATOM   4388  C  CB    . PHE A 1 751  ? 171.151 174.356 137.951 1.00 26.13  ? 1968 PHE A CB    1 
ATOM   4389  C  CG    . PHE A 1 751  ? 171.532 175.055 139.224 1.00 26.59  ? 1968 PHE A CG    1 
ATOM   4390  C  CD1   . PHE A 1 751  ? 171.524 176.435 139.304 1.00 24.02  ? 1968 PHE A CD1   1 
ATOM   4391  C  CD2   . PHE A 1 751  ? 171.907 174.328 140.340 1.00 27.49  ? 1968 PHE A CD2   1 
ATOM   4392  C  CE1   . PHE A 1 751  ? 171.876 177.077 140.470 1.00 22.88  ? 1968 PHE A CE1   1 
ATOM   4393  C  CE2   . PHE A 1 751  ? 172.262 174.966 141.510 1.00 27.99  ? 1968 PHE A CE2   1 
ATOM   4394  C  CZ    . PHE A 1 751  ? 172.246 176.342 141.574 1.00 26.28  ? 1968 PHE A CZ    1 
ATOM   4395  N  N     . GLY A 1 752  ? 168.293 173.107 136.055 1.00 21.67  ? 1969 GLY A N     1 
ATOM   4396  C  CA    . GLY A 1 752  ? 168.048 172.483 134.770 1.00 17.90  ? 1969 GLY A CA    1 
ATOM   4397  C  C     . GLY A 1 752  ? 167.395 173.385 133.745 1.00 14.74  ? 1969 GLY A C     1 
ATOM   4398  O  O     . GLY A 1 752  ? 167.825 174.523 133.543 1.00 15.35  ? 1969 GLY A O     1 
ATOM   4399  N  N     . LEU A 1 753  ? 166.354 172.877 133.086 1.00 13.15  ? 1970 LEU A N     1 
ATOM   4400  C  CA    . LEU A 1 753  ? 165.683 173.609 132.020 1.00 11.54  ? 1970 LEU A CA    1 
ATOM   4401  C  C     . LEU A 1 753  ? 164.526 174.458 132.522 1.00 12.20  ? 1970 LEU A C     1 
ATOM   4402  O  O     . LEU A 1 753  ? 164.276 175.535 131.970 1.00 14.22  ? 1970 LEU A O     1 
ATOM   4403  C  CB    . LEU A 1 753  ? 165.172 172.634 130.956 1.00 11.07  ? 1970 LEU A CB    1 
ATOM   4404  C  CG    . LEU A 1 753  ? 164.597 173.209 129.662 1.00 9.50   ? 1970 LEU A CG    1 
ATOM   4405  C  CD1   . LEU A 1 753  ? 165.495 174.294 129.101 1.00 7.46   ? 1970 LEU A CD1   1 
ATOM   4406  C  CD2   . LEU A 1 753  ? 164.393 172.103 128.645 1.00 12.50  ? 1970 LEU A CD2   1 
ATOM   4407  N  N     . ARG A 1 754  ? 163.808 173.995 133.548 1.00 12.93  ? 1971 ARG A N     1 
ATOM   4408  C  CA    . ARG A 1 754  ? 162.706 174.780 134.094 1.00 13.65  ? 1971 ARG A CA    1 
ATOM   4409  C  C     . ARG A 1 754  ? 163.208 176.073 134.725 1.00 14.63  ? 1971 ARG A C     1 
ATOM   4410  O  O     . ARG A 1 754  ? 162.591 177.130 134.556 1.00 16.97  ? 1971 ARG A O     1 
ATOM   4411  C  CB    . ARG A 1 754  ? 161.924 173.950 135.109 1.00 14.12  ? 1971 ARG A CB    1 
ATOM   4412  C  CG    . ARG A 1 754  ? 160.665 174.625 135.616 1.00 18.30  ? 1971 ARG A CG    1 
ATOM   4413  C  CD    . ARG A 1 754  ? 159.738 173.633 136.300 1.00 24.34  ? 1971 ARG A CD    1 
ATOM   4414  N  NE    . ARG A 1 754  ? 159.010 172.809 135.343 1.00 21.04  ? 1971 ARG A NE    1 
ATOM   4415  C  CZ    . ARG A 1 754  ? 159.191 171.505 135.184 1.00 17.93  ? 1971 ARG A CZ    1 
ATOM   4416  N  NH1   . ARG A 1 754  ? 160.081 170.838 135.899 1.00 17.81  ? 1971 ARG A NH1   1 
ATOM   4417  N  NH2   . ARG A 1 754  ? 158.459 170.854 134.285 1.00 16.22  ? 1971 ARG A NH2   1 
ATOM   4418  N  N     . THR A 1 755  ? 164.330 176.009 135.447 1.00 14.17  ? 1972 THR A N     1 
ATOM   4419  C  CA    . THR A 1 755  ? 164.926 177.215 136.014 1.00 14.08  ? 1972 THR A CA    1 
ATOM   4420  C  C     . THR A 1 755  ? 165.377 178.173 134.917 1.00 14.32  ? 1972 THR A C     1 
ATOM   4421  O  O     . THR A 1 755  ? 165.178 179.391 135.020 1.00 19.46  ? 1972 THR A O     1 
ATOM   4422  C  CB    . THR A 1 755  ? 166.099 176.832 136.919 1.00 16.75  ? 1972 THR A CB    1 
ATOM   4423  O  OG1   . THR A 1 755  ? 165.599 176.210 138.108 1.00 22.74  ? 1972 THR A OG1   1 
ATOM   4424  C  CG2   . THR A 1 755  ? 166.916 178.052 137.310 1.00 15.27  ? 1972 THR A CG2   1 
ATOM   4425  N  N     . LEU A 1 756  ? 165.971 177.635 133.850 1.00 11.92  ? 1973 LEU A N     1 
ATOM   4426  C  CA    . LEU A 1 756  ? 166.415 178.467 132.736 1.00 11.49  ? 1973 LEU A CA    1 
ATOM   4427  C  C     . LEU A 1 756  ? 165.238 179.156 132.057 1.00 13.31  ? 1973 LEU A C     1 
ATOM   4428  O  O     . LEU A 1 756  ? 165.306 180.348 131.734 1.00 16.87  ? 1973 LEU A O     1 
ATOM   4429  C  CB    . LEU A 1 756  ? 167.190 177.606 131.741 1.00 10.47  ? 1973 LEU A CB    1 
ATOM   4430  C  CG    . LEU A 1 756  ? 167.996 178.263 130.626 1.00 8.27   ? 1973 LEU A CG    1 
ATOM   4431  C  CD1   . LEU A 1 756  ? 169.286 177.497 130.421 1.00 12.68  ? 1973 LEU A CD1   1 
ATOM   4432  C  CD2   . LEU A 1 756  ? 167.194 178.285 129.348 1.00 9.06   ? 1973 LEU A CD2   1 
ATOM   4433  N  N     . LYS A 1 757  ? 164.140 178.428 131.851 1.00 13.21  ? 1974 LYS A N     1 
ATOM   4434  C  CA    . LYS A 1 757  ? 162.968 179.041 131.238 1.00 13.62  ? 1974 LYS A CA    1 
ATOM   4435  C  C     . LYS A 1 757  ? 162.296 180.032 132.176 1.00 15.66  ? 1974 LYS A C     1 
ATOM   4436  O  O     . LYS A 1 757  ? 161.708 181.012 131.712 1.00 18.48  ? 1974 LYS A O     1 
ATOM   4437  C  CB    . LYS A 1 757  ? 161.978 177.970 130.791 1.00 11.96  ? 1974 LYS A CB    1 
ATOM   4438  C  CG    . LYS A 1 757  ? 162.298 177.381 129.432 1.00 10.67  ? 1974 LYS A CG    1 
ATOM   4439  C  CD    . LYS A 1 757  ? 161.345 176.261 129.096 1.00 11.66  ? 1974 LYS A CD    1 
ATOM   4440  C  CE    . LYS A 1 757  ? 159.979 176.802 128.728 1.00 14.98  ? 1974 LYS A CE    1 
ATOM   4441  N  NZ    . LYS A 1 757  ? 159.904 177.168 127.291 1.00 13.43  ? 1974 LYS A NZ    1 
ATOM   4442  N  N     . GLY A 1 758  ? 162.379 179.809 133.489 1.00 14.17  ? 1975 GLY A N     1 
ATOM   4443  C  CA    . GLY A 1 758  ? 161.908 180.816 134.426 1.00 15.51  ? 1975 GLY A CA    1 
ATOM   4444  C  C     . GLY A 1 758  ? 162.721 182.094 134.353 1.00 17.18  ? 1975 GLY A C     1 
ATOM   4445  O  O     . GLY A 1 758  ? 162.171 183.197 134.414 1.00 21.05  ? 1975 GLY A O     1 
ATOM   4446  N  N     . VAL A 1 759  ? 164.041 181.959 134.209 1.00 14.95  ? 1976 VAL A N     1 
ATOM   4447  C  CA    . VAL A 1 759  ? 164.906 183.122 134.012 1.00 14.89  ? 1976 VAL A CA    1 
ATOM   4448  C  C     . VAL A 1 759  ? 164.508 183.868 132.743 1.00 15.99  ? 1976 VAL A C     1 
ATOM   4449  O  O     . VAL A 1 759  ? 164.365 185.099 132.737 1.00 17.67  ? 1976 VAL A O     1 
ATOM   4450  C  CB    . VAL A 1 759  ? 166.382 182.682 133.969 1.00 12.11  ? 1976 VAL A CB    1 
ATOM   4451  C  CG1   . VAL A 1 759  ? 167.249 183.751 133.327 1.00 11.27  ? 1976 VAL A CG1   1 
ATOM   4452  C  CG2   . VAL A 1 759  ? 166.879 182.348 135.362 1.00 15.42  ? 1976 VAL A CG2   1 
ATOM   4453  N  N     . LEU A 1 760  ? 164.297 183.124 131.655 1.00 16.39  ? 1977 LEU A N     1 
ATOM   4454  C  CA    . LEU A 1 760  ? 163.930 183.751 130.388 1.00 15.89  ? 1977 LEU A CA    1 
ATOM   4455  C  C     . LEU A 1 760  ? 162.563 184.425 130.469 1.00 19.27  ? 1977 LEU A C     1 
ATOM   4456  O  O     . LEU A 1 760  ? 162.359 185.492 129.881 1.00 22.99  ? 1977 LEU A O     1 
ATOM   4457  C  CB    . LEU A 1 760  ? 163.963 182.719 129.263 1.00 11.91  ? 1977 LEU A CB    1 
ATOM   4458  C  CG    . LEU A 1 760  ? 165.332 182.084 129.009 1.00 10.59  ? 1977 LEU A CG    1 
ATOM   4459  C  CD1   . LEU A 1 760  ? 165.284 181.121 127.839 1.00 9.64   ? 1977 LEU A CD1   1 
ATOM   4460  C  CD2   . LEU A 1 760  ? 166.386 183.149 128.787 1.00 11.24  ? 1977 LEU A CD2   1 
ATOM   4461  N  N     . ARG A 1 761  ? 161.617 183.824 131.194 1.00 17.90  ? 1978 ARG A N     1 
ATOM   4462  C  CA    . ARG A 1 761  ? 160.309 184.448 131.367 1.00 18.67  ? 1978 ARG A CA    1 
ATOM   4463  C  C     . ARG A 1 761  ? 160.406 185.709 132.214 1.00 19.72  ? 1978 ARG A C     1 
ATOM   4464  O  O     . ARG A 1 761  ? 159.688 186.684 131.968 1.00 22.70  ? 1978 ARG A O     1 
ATOM   4465  C  CB    . ARG A 1 761  ? 159.330 183.462 132.001 1.00 20.32  ? 1978 ARG A CB    1 
ATOM   4466  C  CG    . ARG A 1 761  ? 158.766 182.429 131.043 1.00 21.96  ? 1978 ARG A CG    1 
ATOM   4467  C  CD    . ARG A 1 761  ? 157.794 181.486 131.742 1.00 18.31  ? 1978 ARG A CD    1 
ATOM   4468  N  NE    . ARG A 1 761  ? 158.233 181.122 133.084 1.00 20.87  ? 1978 ARG A NE    1 
ATOM   4469  C  CZ    . ARG A 1 761  ? 157.613 181.482 134.200 1.00 24.70  ? 1978 ARG A CZ    1 
ATOM   4470  N  NH1   . ARG A 1 761  ? 156.520 182.228 134.173 1.00 20.37  ? 1978 ARG A NH1   1 
ATOM   4471  N  NH2   . ARG A 1 761  ? 158.104 181.088 135.371 1.00 30.52  ? 1978 ARG A NH2   1 
ATOM   4472  N  N     . ASN A 1 762  ? 161.283 185.708 133.218 1.00 20.09  ? 1979 ASN A N     1 
ATOM   4473  C  CA    . ASN A 1 762  ? 161.460 186.890 134.050 1.00 22.50  ? 1979 ASN A CA    1 
ATOM   4474  C  C     . ASN A 1 762  ? 162.256 187.988 133.358 1.00 25.82  ? 1979 ASN A C     1 
ATOM   4475  O  O     . ASN A 1 762  ? 162.250 189.122 133.845 1.00 27.99  ? 1979 ASN A O     1 
ATOM   4476  C  CB    . ASN A 1 762  ? 162.147 186.508 135.361 1.00 20.70  ? 1979 ASN A CB    1 
ATOM   4477  C  CG    . ASN A 1 762  ? 161.204 185.846 136.340 1.00 22.64  ? 1979 ASN A CG    1 
ATOM   4478  O  OD1   . ASN A 1 762  ? 160.443 184.950 135.978 1.00 23.25  ? 1979 ASN A OD1   1 
ATOM   4479  N  ND2   . ASN A 1 762  ? 161.253 186.281 137.591 1.00 28.22  ? 1979 ASN A ND2   1 
ATOM   4480  N  N     . CYS A 1 763  ? 162.957 187.676 132.264 1.00 22.73  ? 1980 CYS A N     1 
ATOM   4481  C  CA    . CYS A 1 763  ? 163.744 188.702 131.578 1.00 21.74  ? 1980 CYS A CA    1 
ATOM   4482  C  C     . CYS A 1 763  ? 162.877 189.826 131.014 1.00 26.42  ? 1980 CYS A C     1 
ATOM   4483  O  O     . CYS A 1 763  ? 163.272 190.995 131.064 1.00 32.77  ? 1980 CYS A O     1 
ATOM   4484  C  CB    . CYS A 1 763  ? 164.582 188.082 130.461 1.00 21.07  ? 1980 CYS A CB    1 
ATOM   4485  S  SG    . CYS A 1 763  ? 166.012 187.133 131.010 1.00 28.33  ? 1980 CYS A SG    1 
ATOM   4486  N  N     . SER A 1 764  ? 161.706 189.503 130.459 1.00 26.19  ? 1981 SER A N     1 
ATOM   4487  C  CA    . SER A 1 764  ? 160.939 190.510 129.722 1.00 30.57  ? 1981 SER A CA    1 
ATOM   4488  C  C     . SER A 1 764  ? 160.455 191.708 130.553 1.00 33.95  ? 1981 SER A C     1 
ATOM   4489  O  O     . SER A 1 764  ? 160.567 192.844 130.050 1.00 35.83  ? 1981 SER A O     1 
ATOM   4490  C  CB    . SER A 1 764  ? 159.785 189.833 128.962 1.00 33.20  ? 1981 SER A CB    1 
ATOM   4491  O  OG    . SER A 1 764  ? 158.864 189.158 129.797 1.00 35.21  ? 1981 SER A OG    1 
ATOM   4492  N  N     . PRO A 1 765  ? 159.919 191.565 131.778 1.00 33.48  ? 1982 PRO A N     1 
ATOM   4493  C  CA    . PRO A 1 765  ? 159.648 192.781 132.566 1.00 34.24  ? 1982 PRO A CA    1 
ATOM   4494  C  C     . PRO A 1 765  ? 160.906 193.562 132.892 1.00 33.84  ? 1982 PRO A C     1 
ATOM   4495  O  O     . PRO A 1 765  ? 160.847 194.787 133.058 1.00 34.66  ? 1982 PRO A O     1 
ATOM   4496  C  CB    . PRO A 1 765  ? 158.968 192.245 133.834 1.00 33.62  ? 1982 PRO A CB    1 
ATOM   4497  C  CG    . PRO A 1 765  ? 158.502 190.889 133.482 1.00 32.76  ? 1982 PRO A CG    1 
ATOM   4498  C  CD    . PRO A 1 765  ? 159.524 190.365 132.539 1.00 31.12  ? 1982 PRO A CD    1 
ATOM   4499  N  N     . LEU A 1 766  ? 162.046 192.882 132.995 1.00 33.07  ? 1983 LEU A N     1 
ATOM   4500  C  CA    . LEU A 1 766  ? 163.332 193.553 133.100 1.00 33.57  ? 1983 LEU A CA    1 
ATOM   4501  C  C     . LEU A 1 766  ? 163.846 194.033 131.749 1.00 36.21  ? 1983 LEU A C     1 
ATOM   4502  O  O     . LEU A 1 766  ? 164.702 194.920 131.712 1.00 36.54  ? 1983 LEU A O     1 
ATOM   4503  C  CB    . LEU A 1 766  ? 164.361 192.623 133.748 1.00 28.35  ? 1983 LEU A CB    1 
ATOM   4504  C  CG    . LEU A 1 766  ? 164.354 192.431 135.266 1.00 27.85  ? 1983 LEU A CG    1 
ATOM   4505  C  CD1   . LEU A 1 766  ? 163.169 191.619 135.759 1.00 31.13  ? 1983 LEU A CD1   1 
ATOM   4506  C  CD2   . LEU A 1 766  ? 165.641 191.758 135.678 1.00 28.60  ? 1983 LEU A CD2   1 
ATOM   4507  N  N     . VAL A 1 767  ? 163.365 193.454 130.644 1.00 36.15  ? 1984 VAL A N     1 
ATOM   4508  C  CA    . VAL A 1 767  ? 163.651 194.018 129.327 1.00 37.41  ? 1984 VAL A CA    1 
ATOM   4509  C  C     . VAL A 1 767  ? 163.012 195.393 129.203 1.00 37.51  ? 1984 VAL A C     1 
ATOM   4510  O  O     . VAL A 1 767  ? 163.600 196.319 128.629 1.00 38.69  ? 1984 VAL A O     1 
ATOM   4511  C  CB    . VAL A 1 767  ? 163.173 193.063 128.212 1.00 40.22  ? 1984 VAL A CB    1 
ATOM   4512  C  CG1   . VAL A 1 767  ? 163.008 193.790 126.883 1.00 39.43  ? 1984 VAL A CG1   1 
ATOM   4513  C  CG2   . VAL A 1 767  ? 164.130 191.903 128.049 1.00 37.76  ? 1984 VAL A CG2   1 
ATOM   4514  N  N     . SER A 1 768  ? 161.814 195.557 129.774 1.00 38.72  ? 1985 SER A N     1 
ATOM   4515  C  CA    . SER A 1 768  ? 161.106 196.833 129.685 1.00 44.46  ? 1985 SER A CA    1 
ATOM   4516  C  C     . SER A 1 768  ? 161.861 197.989 130.337 1.00 44.19  ? 1985 SER A C     1 
ATOM   4517  O  O     . SER A 1 768  ? 161.576 199.150 130.023 1.00 41.37  ? 1985 SER A O     1 
ATOM   4518  C  CB    . SER A 1 768  ? 159.719 196.712 130.317 1.00 45.05  ? 1985 SER A CB    1 
ATOM   4519  O  OG    . SER A 1 768  ? 159.807 196.282 131.663 1.00 45.01  ? 1985 SER A OG    1 
ATOM   4520  N  N     . GLU A 1 769  ? 162.813 197.711 131.231 1.00 42.62  ? 1986 GLU A N     1 
ATOM   4521  C  CA    . GLU A 1 769  ? 163.582 198.757 131.895 1.00 41.35  ? 1986 GLU A CA    1 
ATOM   4522  C  C     . GLU A 1 769  ? 165.060 198.728 131.520 1.00 41.46  ? 1986 GLU A C     1 
ATOM   4523  O  O     . GLU A 1 769  ? 165.598 199.736 131.055 1.00 39.91  ? 1986 GLU A O     1 
ATOM   4524  C  CB    . GLU A 1 769  ? 163.415 198.640 133.416 1.00 42.59  ? 1986 GLU A CB    1 
ATOM   4525  C  CG    . GLU A 1 769  ? 164.057 199.772 134.196 1.00 45.47  ? 1986 GLU A CG    1 
ATOM   4526  C  CD    . GLU A 1 769  ? 165.385 199.374 134.804 1.00 43.98  ? 1986 GLU A CD    1 
ATOM   4527  O  OE1   . GLU A 1 769  ? 165.498 198.225 135.278 1.00 43.79  ? 1986 GLU A OE1   1 
ATOM   4528  O  OE2   . GLU A 1 769  ? 166.317 200.206 134.804 1.00 43.22  ? 1986 GLU A OE2   1 
ATOM   4529  N  N     . PHE A 1 770  ? 165.737 197.594 131.719 1.00 40.75  ? 1987 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 770  ? 167.163 197.510 131.414 1.00 39.81  ? 1987 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 770  ? 167.415 197.512 129.911 1.00 40.22  ? 1987 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 770  ? 168.377 198.128 129.438 1.00 39.17  ? 1987 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 770  ? 167.764 196.254 132.045 1.00 37.61  ? 1987 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 770  ? 167.907 196.326 133.539 1.00 36.11  ? 1987 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 770  ? 168.847 197.158 134.120 1.00 38.03  ? 1987 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 770  ? 167.111 195.546 134.361 1.00 37.68  ? 1987 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 770  ? 168.983 197.218 135.494 1.00 38.09  ? 1987 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 770  ? 167.244 195.601 135.734 1.00 35.10  ? 1987 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 770  ? 168.180 196.440 136.301 1.00 34.78  ? 1987 PHE A CZ    1 
ATOM   4540  N  N     . GLY A 1 771  ? 166.576 196.825 129.150 1.00 39.62  ? 1988 GLY A N     1 
ATOM   4541  C  CA    . GLY A 1 771  ? 166.725 196.725 127.713 1.00 39.95  ? 1988 GLY A CA    1 
ATOM   4542  C  C     . GLY A 1 771  ? 167.126 195.325 127.277 1.00 39.34  ? 1988 GLY A C     1 
ATOM   4543  O  O     . GLY A 1 771  ? 167.519 194.473 128.073 1.00 39.47  ? 1988 GLY A O     1 
ATOM   4544  N  N     . GLU A 1 772  ? 167.017 195.103 125.967 1.00 39.24  ? 1989 GLU A N     1 
ATOM   4545  C  CA    . GLU A 1 772  ? 167.365 193.812 125.386 1.00 38.03  ? 1989 GLU A CA    1 
ATOM   4546  C  C     . GLU A 1 772  ? 168.876 193.631 125.345 1.00 38.24  ? 1989 GLU A C     1 
ATOM   4547  O  O     . GLU A 1 772  ? 169.530 194.066 124.392 1.00 41.01  ? 1989 GLU A O     1 
ATOM   4548  C  CB    . GLU A 1 772  ? 166.789 193.681 123.975 1.00 38.94  ? 1989 GLU A CB    1 
ATOM   4549  C  CG    . GLU A 1 772  ? 165.275 193.654 123.906 1.00 39.68  ? 1989 GLU A CG    1 
ATOM   4550  C  CD    . GLU A 1 772  ? 164.678 195.033 123.732 1.00 47.68  ? 1989 GLU A CD    1 
ATOM   4551  O  OE1   . GLU A 1 772  ? 165.453 196.006 123.626 1.00 57.54  ? 1989 GLU A OE1   1 
ATOM   4552  O  OE2   . GLU A 1 772  ? 163.435 195.144 123.693 1.00 50.27  ? 1989 GLU A OE2   1 
ATOM   4553  N  N     . GLY A 1 773  ? 169.441 192.988 126.358 1.00 33.39  ? 1990 GLY A N     1 
ATOM   4554  C  CA    . GLY A 1 773  ? 170.877 192.816 126.380 1.00 29.84  ? 1990 GLY A CA    1 
ATOM   4555  C  C     . GLY A 1 773  ? 171.323 191.922 127.513 1.00 27.23  ? 1990 GLY A C     1 
ATOM   4556  O  O     . GLY A 1 773  ? 170.521 191.227 128.140 1.00 27.15  ? 1990 GLY A O     1 
ATOM   4557  N  N     . GLU A 1 774  ? 172.634 191.953 127.762 1.00 26.78  ? 1991 GLU A N     1 
ATOM   4558  C  CA    . GLU A 1 774  ? 173.236 191.095 128.775 1.00 28.72  ? 1991 GLU A CA    1 
ATOM   4559  C  C     . GLU A 1 774  ? 172.857 191.521 130.187 1.00 30.53  ? 1991 GLU A C     1 
ATOM   4560  O  O     . GLU A 1 774  ? 172.750 190.670 131.080 1.00 29.24  ? 1991 GLU A O     1 
ATOM   4561  C  CB    . GLU A 1 774  ? 174.753 191.099 128.614 1.00 29.01  ? 1991 GLU A CB    1 
ATOM   4562  C  CG    . GLU A 1 774  ? 175.453 189.922 129.249 1.00 29.30  ? 1991 GLU A CG    1 
ATOM   4563  C  CD    . GLU A 1 774  ? 176.762 189.595 128.561 1.00 36.76  ? 1991 GLU A CD    1 
ATOM   4564  O  OE1   . GLU A 1 774  ? 177.017 190.152 127.472 1.00 39.62  ? 1991 GLU A OE1   1 
ATOM   4565  O  OE2   . GLU A 1 774  ? 177.540 188.787 129.109 1.00 38.46  ? 1991 GLU A OE2   1 
ATOM   4566  N  N     . LYS A 1 775  ? 172.663 192.826 130.407 1.00 32.57  ? 1992 LYS A N     1 
ATOM   4567  C  CA    . LYS A 1 775  ? 172.329 193.325 131.739 1.00 31.48  ? 1992 LYS A CA    1 
ATOM   4568  C  C     . LYS A 1 775  ? 170.999 192.766 132.222 1.00 29.44  ? 1992 LYS A C     1 
ATOM   4569  O  O     . LYS A 1 775  ? 170.850 192.430 133.403 1.00 31.38  ? 1992 LYS A O     1 
ATOM   4570  C  CB    . LYS A 1 775  ? 172.289 194.852 131.728 1.00 31.60  ? 1992 LYS A CB    1 
ATOM   4571  C  CG    . LYS A 1 775  ? 173.464 195.519 132.418 1.00 34.37  ? 1992 LYS A CG    1 
ATOM   4572  C  CD    . LYS A 1 775  ? 173.418 197.027 132.228 1.00 35.14  ? 1992 LYS A CD    1 
ATOM   4573  C  CE    . LYS A 1 775  ? 172.482 197.683 133.230 1.00 37.10  ? 1992 LYS A CE    1 
ATOM   4574  N  NZ    . LYS A 1 775  ? 172.525 199.169 133.145 1.00 26.71  ? 1992 LYS A NZ    1 
ATOM   4575  N  N     . THR A 1 776  ? 170.021 192.661 131.319 1.00 26.25  ? 1993 THR A N     1 
ATOM   4576  C  CA    . THR A 1 776  ? 168.726 192.097 131.680 1.00 25.12  ? 1993 THR A CA    1 
ATOM   4577  C  C     . THR A 1 776  ? 168.856 190.644 132.111 1.00 25.75  ? 1993 THR A C     1 
ATOM   4578  O  O     . THR A 1 776  ? 168.256 190.230 133.109 1.00 27.76  ? 1993 THR A O     1 
ATOM   4579  C  CB    . THR A 1 776  ? 167.763 192.213 130.503 1.00 28.41  ? 1993 THR A CB    1 
ATOM   4580  O  OG1   . THR A 1 776  ? 167.610 193.590 130.144 1.00 38.45  ? 1993 THR A OG1   1 
ATOM   4581  C  CG2   . THR A 1 776  ? 166.419 191.648 130.873 1.00 28.26  ? 1993 THR A CG2   1 
ATOM   4582  N  N     . VAL A 1 777  ? 169.647 189.859 131.377 1.00 25.55  ? 1994 VAL A N     1 
ATOM   4583  C  CA    . VAL A 1 777  ? 169.836 188.453 131.719 1.00 23.08  ? 1994 VAL A CA    1 
ATOM   4584  C  C     . VAL A 1 777  ? 170.553 188.318 133.058 1.00 22.64  ? 1994 VAL A C     1 
ATOM   4585  O  O     . VAL A 1 777  ? 170.186 187.480 133.891 1.00 19.16  ? 1994 VAL A O     1 
ATOM   4586  C  CB    . VAL A 1 777  ? 170.588 187.736 130.582 1.00 19.35  ? 1994 VAL A CB    1 
ATOM   4587  C  CG1   . VAL A 1 777  ? 171.244 186.465 131.078 1.00 16.79  ? 1994 VAL A CG1   1 
ATOM   4588  C  CG2   . VAL A 1 777  ? 169.639 187.429 129.440 1.00 18.89  ? 1994 VAL A CG2   1 
ATOM   4589  N  N     . VAL A 1 778  ? 171.564 189.159 133.298 1.00 24.28  ? 1995 VAL A N     1 
ATOM   4590  C  CA    . VAL A 1 778  ? 172.298 189.109 134.563 1.00 22.76  ? 1995 VAL A CA    1 
ATOM   4591  C  C     . VAL A 1 778  ? 171.380 189.452 135.732 1.00 25.49  ? 1995 VAL A C     1 
ATOM   4592  O  O     . VAL A 1 778  ? 171.372 188.765 136.762 1.00 26.17  ? 1995 VAL A O     1 
ATOM   4593  C  CB    . VAL A 1 778  ? 173.517 190.046 134.509 1.00 23.88  ? 1995 VAL A CB    1 
ATOM   4594  C  CG1   . VAL A 1 778  ? 174.128 190.205 135.886 1.00 23.79  ? 1995 VAL A CG1   1 
ATOM   4595  C  CG2   . VAL A 1 778  ? 174.546 189.511 133.538 1.00 26.72  ? 1995 VAL A CG2   1 
ATOM   4596  N  N     . GLU A 1 779  ? 170.580 190.511 135.586 1.00 25.70  ? 1996 GLU A N     1 
ATOM   4597  C  CA    . GLU A 1 779  ? 169.697 190.912 136.676 1.00 23.62  ? 1996 GLU A CA    1 
ATOM   4598  C  C     . GLU A 1 779  ? 168.570 189.910 136.891 1.00 21.46  ? 1996 GLU A C     1 
ATOM   4599  O  O     . GLU A 1 779  ? 168.141 189.703 138.031 1.00 23.53  ? 1996 GLU A O     1 
ATOM   4600  C  CB    . GLU A 1 779  ? 169.137 192.308 136.415 1.00 28.28  ? 1996 GLU A CB    1 
ATOM   4601  C  CG    . GLU A 1 779  ? 170.172 193.415 136.516 1.00 34.73  ? 1996 GLU A CG    1 
ATOM   4602  C  CD    . GLU A 1 779  ? 170.654 193.647 137.936 1.00 40.98  ? 1996 GLU A CD    1 
ATOM   4603  O  OE1   . GLU A 1 779  ? 169.897 193.348 138.884 1.00 41.64  ? 1996 GLU A OE1   1 
ATOM   4604  O  OE2   . GLU A 1 779  ? 171.792 194.132 138.104 1.00 45.33  ? 1996 GLU A OE2   1 
ATOM   4605  N  N     . SER A 1 780  ? 168.089 189.266 135.825 1.00 20.13  ? 1997 SER A N     1 
ATOM   4606  C  CA    . SER A 1 780  ? 167.085 188.221 135.993 1.00 17.91  ? 1997 SER A CA    1 
ATOM   4607  C  C     . SER A 1 780  ? 167.674 186.998 136.683 1.00 16.73  ? 1997 SER A C     1 
ATOM   4608  O  O     . SER A 1 780  ? 166.997 186.347 137.488 1.00 16.72  ? 1997 SER A O     1 
ATOM   4609  C  CB    . SER A 1 780  ? 166.493 187.839 134.640 1.00 17.73  ? 1997 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 780  ? 165.889 186.562 134.701 1.00 15.95  ? 1997 SER A OG    1 
ATOM   4611  N  N     . LEU A 1 781  ? 168.933 186.669 136.380 1.00 17.57  ? 1998 LEU A N     1 
ATOM   4612  C  CA    . LEU A 1 781  ? 169.606 185.583 137.085 1.00 17.58  ? 1998 LEU A CA    1 
ATOM   4613  C  C     . LEU A 1 781  ? 169.787 185.920 138.559 1.00 16.78  ? 1998 LEU A C     1 
ATOM   4614  O  O     . LEU A 1 781  ? 169.680 185.042 139.422 1.00 17.28  ? 1998 LEU A O     1 
ATOM   4615  C  CB    . LEU A 1 781  ? 170.957 185.291 136.434 1.00 16.56  ? 1998 LEU A CB    1 
ATOM   4616  C  CG    . LEU A 1 781  ? 170.955 184.489 135.133 1.00 12.40  ? 1998 LEU A CG    1 
ATOM   4617  C  CD1   . LEU A 1 781  ? 172.262 184.688 134.391 1.00 13.84  ? 1998 LEU A CD1   1 
ATOM   4618  C  CD2   . LEU A 1 781  ? 170.719 183.018 135.409 1.00 12.08  ? 1998 LEU A CD2   1 
ATOM   4619  N  N     . LYS A 1 782  ? 170.071 187.188 138.861 1.00 15.85  ? 1999 LYS A N     1 
ATOM   4620  C  CA    . LYS A 1 782  ? 170.182 187.610 140.254 1.00 14.90  ? 1999 LYS A CA    1 
ATOM   4621  C  C     . LYS A 1 782  ? 168.832 187.556 140.963 1.00 15.99  ? 1999 LYS A C     1 
ATOM   4622  O  O     . LYS A 1 782  ? 168.762 187.221 142.149 1.00 15.96  ? 1999 LYS A O     1 
ATOM   4623  C  CB    . LYS A 1 782  ? 170.768 189.019 140.332 1.00 18.22  ? 1999 LYS A CB    1 
ATOM   4624  C  CG    . LYS A 1 782  ? 172.241 189.100 139.983 1.00 22.45  ? 1999 LYS A CG    1 
ATOM   4625  C  CD    . LYS A 1 782  ? 172.715 190.541 139.933 1.00 26.27  ? 1999 LYS A CD    1 
ATOM   4626  C  CE    . LYS A 1 782  ? 174.191 190.625 139.586 1.00 28.34  ? 1999 LYS A CE    1 
ATOM   4627  N  NZ    . LYS A 1 782  ? 174.760 191.969 139.875 1.00 28.01  ? 1999 LYS A NZ    1 
ATOM   4628  N  N     . ARG A 1 783  ? 167.753 187.899 140.262 1.00 19.46  ? 2000 ARG A N     1 
ATOM   4629  C  CA    . ARG A 1 783  ? 166.438 187.907 140.894 1.00 17.53  ? 2000 ARG A CA    1 
ATOM   4630  C  C     . ARG A 1 783  ? 165.857 186.509 141.063 1.00 16.80  ? 2000 ARG A C     1 
ATOM   4631  O  O     . ARG A 1 783  ? 165.079 186.280 141.994 1.00 16.74  ? 2000 ARG A O     1 
ATOM   4632  C  CB    . ARG A 1 783  ? 165.470 188.776 140.090 1.00 13.97  ? 2000 ARG A CB    1 
ATOM   4633  C  CG    . ARG A 1 783  ? 165.432 190.222 140.537 1.00 15.46  ? 2000 ARG A CG    1 
ATOM   4634  C  CD    . ARG A 1 783  ? 164.836 191.119 139.473 1.00 18.79  ? 2000 ARG A CD    1 
ATOM   4635  N  NE    . ARG A 1 783  ? 165.418 192.455 139.506 1.00 22.96  ? 2000 ARG A NE    1 
ATOM   4636  C  CZ    . ARG A 1 783  ? 164.784 193.556 139.127 1.00 26.29  ? 2000 ARG A CZ    1 
ATOM   4637  N  NH1   . ARG A 1 783  ? 163.539 193.519 138.684 1.00 25.44  ? 2000 ARG A NH1   1 
ATOM   4638  N  NH2   . ARG A 1 783  ? 165.416 194.724 139.197 1.00 28.45  ? 2000 ARG A NH2   1 
ATOM   4639  N  N     . VAL A 1 784  ? 166.209 185.572 140.190 1.00 15.63  ? 2001 VAL A N     1 
ATOM   4640  C  CA    . VAL A 1 784  ? 165.587 184.251 140.172 1.00 15.24  ? 2001 VAL A CA    1 
ATOM   4641  C  C     . VAL A 1 784  ? 166.414 183.223 140.936 1.00 18.93  ? 2001 VAL A C     1 
ATOM   4642  O  O     . VAL A 1 784  ? 165.884 182.479 141.760 1.00 19.87  ? 2001 VAL A O     1 
ATOM   4643  C  CB    . VAL A 1 784  ? 165.342 183.803 138.714 1.00 18.72  ? 2001 VAL A CB    1 
ATOM   4644  C  CG1   . VAL A 1 784  ? 164.942 182.340 138.663 1.00 19.14  ? 2001 VAL A CG1   1 
ATOM   4645  C  CG2   . VAL A 1 784  ? 164.270 184.666 138.077 1.00 20.96  ? 2001 VAL A CG2   1 
ATOM   4646  N  N     . ILE A 1 785  ? 167.718 183.174 140.684 1.00 18.56  ? 2002 ILE A N     1 
ATOM   4647  C  CA    . ILE A 1 785  ? 168.550 182.097 141.212 1.00 15.88  ? 2002 ILE A CA    1 
ATOM   4648  C  C     . ILE A 1 785  ? 169.201 182.480 142.536 1.00 14.65  ? 2002 ILE A C     1 
ATOM   4649  O  O     . ILE A 1 785  ? 169.214 181.680 143.474 1.00 19.04  ? 2002 ILE A O     1 
ATOM   4650  C  CB    . ILE A 1 785  ? 169.600 181.697 140.156 1.00 18.31  ? 2002 ILE A CB    1 
ATOM   4651  C  CG1   . ILE A 1 785  ? 168.911 181.060 138.948 1.00 21.21  ? 2002 ILE A CG1   1 
ATOM   4652  C  CG2   . ILE A 1 785  ? 170.632 180.752 140.748 1.00 17.91  ? 2002 ILE A CG2   1 
ATOM   4653  C  CD1   . ILE A 1 785  ? 169.858 180.405 137.972 1.00 19.75  ? 2002 ILE A CD1   1 
ATOM   4654  N  N     . LEU A 1 786  ? 169.734 183.700 142.622 1.00 13.78  ? 2003 LEU A N     1 
ATOM   4655  C  CA    . LEU A 1 786  ? 170.508 184.114 143.792 1.00 12.99  ? 2003 LEU A CA    1 
ATOM   4656  C  C     . LEU A 1 786  ? 169.779 184.024 145.134 1.00 14.55  ? 2003 LEU A C     1 
ATOM   4657  O  O     . LEU A 1 786  ? 170.452 183.719 146.134 1.00 18.01  ? 2003 LEU A O     1 
ATOM   4658  C  CB    . LEU A 1 786  ? 171.045 185.534 143.574 1.00 13.17  ? 2003 LEU A CB    1 
ATOM   4659  C  CG    . LEU A 1 786  ? 172.204 185.957 144.471 1.00 12.78  ? 2003 LEU A CG    1 
ATOM   4660  C  CD1   . LEU A 1 786  ? 173.256 184.873 144.482 1.00 17.24  ? 2003 LEU A CD1   1 
ATOM   4661  C  CD2   . LEU A 1 786  ? 172.792 187.276 144.009 1.00 15.24  ? 2003 LEU A CD2   1 
ATOM   4662  N  N     . PRO A 1 787  ? 168.472 184.311 145.258 1.00 12.94  ? 2004 PRO A N     1 
ATOM   4663  C  CA    . PRO A 1 787  ? 167.820 184.109 146.564 1.00 11.92  ? 2004 PRO A CA    1 
ATOM   4664  C  C     . PRO A 1 787  ? 167.918 182.695 147.110 1.00 12.40  ? 2004 PRO A C     1 
ATOM   4665  O  O     . PRO A 1 787  ? 167.996 182.525 148.332 1.00 16.66  ? 2004 PRO A O     1 
ATOM   4666  C  CB    . PRO A 1 787  ? 166.365 184.496 146.280 1.00 13.48  ? 2004 PRO A CB    1 
ATOM   4667  C  CG    . PRO A 1 787  ? 166.480 185.551 145.280 1.00 15.27  ? 2004 PRO A CG    1 
ATOM   4668  C  CD    . PRO A 1 787  ? 167.612 185.132 144.381 1.00 15.79  ? 2004 PRO A CD    1 
ATOM   4669  N  N     . SER A 1 788  ? 167.930 181.677 146.258 1.00 12.65  ? 2005 SER A N     1 
ATOM   4670  C  CA    . SER A 1 788  ? 167.919 180.302 146.741 1.00 14.49  ? 2005 SER A CA    1 
ATOM   4671  C  C     . SER A 1 788  ? 169.300 179.776 147.115 1.00 16.10  ? 2005 SER A C     1 
ATOM   4672  O  O     . SER A 1 788  ? 169.400 178.631 147.567 1.00 17.66  ? 2005 SER A O     1 
ATOM   4673  C  CB    . SER A 1 788  ? 167.286 179.386 145.690 1.00 16.62  ? 2005 SER A CB    1 
ATOM   4674  O  OG    . SER A 1 788  ? 167.954 179.500 144.446 1.00 20.81  ? 2005 SER A OG    1 
ATOM   4675  N  N     . LEU A 1 789  ? 170.356 180.565 146.953 1.00 15.73  ? 2006 LEU A N     1 
ATOM   4676  C  CA    . LEU A 1 789  ? 171.716 180.115 147.211 1.00 18.41  ? 2006 LEU A CA    1 
ATOM   4677  C  C     . LEU A 1 789  ? 172.192 180.562 148.589 1.00 19.78  ? 2006 LEU A C     1 
ATOM   4678  O  O     . LEU A 1 789  ? 171.697 181.535 149.162 1.00 19.53  ? 2006 LEU A O     1 
ATOM   4679  C  CB    . LEU A 1 789  ? 172.674 180.637 146.138 1.00 19.66  ? 2006 LEU A CB    1 
ATOM   4680  C  CG    . LEU A 1 789  ? 172.318 180.331 144.684 1.00 15.22  ? 2006 LEU A CG    1 
ATOM   4681  C  CD1   . LEU A 1 789  ? 173.391 180.861 143.753 1.00 14.45  ? 2006 LEU A CD1   1 
ATOM   4682  C  CD2   . LEU A 1 789  ? 172.121 178.841 144.486 1.00 16.89  ? 2006 LEU A CD2   1 
ATOM   4683  N  N     . GLY A 1 790  ? 173.179 179.835 149.112 1.00 21.38  ? 2007 GLY A N     1 
ATOM   4684  C  CA    . GLY A 1 790  ? 173.730 180.113 150.426 1.00 22.31  ? 2007 GLY A CA    1 
ATOM   4685  C  C     . GLY A 1 790  ? 174.766 181.219 150.434 1.00 30.18  ? 2007 GLY A C     1 
ATOM   4686  O  O     . GLY A 1 790  ? 174.575 182.254 149.791 1.00 33.14  ? 2007 GLY A O     1 
ATOM   4687  N  N     . ASP A 1 791  ? 175.864 181.019 151.167 1.00 32.99  ? 2008 ASP A N     1 
ATOM   4688  C  CA    . ASP A 1 791  ? 176.934 182.010 151.268 1.00 36.01  ? 2008 ASP A CA    1 
ATOM   4689  C  C     . ASP A 1 791  ? 178.118 181.667 150.369 1.00 37.37  ? 2008 ASP A C     1 
ATOM   4690  O  O     . ASP A 1 791  ? 178.504 182.466 149.508 1.00 36.65  ? 2008 ASP A O     1 
ATOM   4691  C  CB    . ASP A 1 791  ? 177.389 182.138 152.727 1.00 36.74  ? 2008 ASP A CB    1 
ATOM   4692  C  CG    . ASP A 1 791  ? 176.729 183.298 153.444 1.00 39.87  ? 2008 ASP A CG    1 
ATOM   4693  O  OD1   . ASP A 1 791  ? 175.927 184.013 152.808 1.00 38.70  ? 2008 ASP A OD1   1 
ATOM   4694  O  OD2   . ASP A 1 791  ? 177.010 183.492 154.646 1.00 36.45  ? 2008 ASP A OD2   1 
ATOM   4695  N  N     . THR A 1 792  ? 178.710 180.484 150.560 1.00 38.06  ? 2009 THR A N     1 
ATOM   4696  C  CA    . THR A 1 792  ? 179.736 180.012 149.635 1.00 38.01  ? 2009 THR A CA    1 
ATOM   4697  C  C     . THR A 1 792  ? 179.160 179.842 148.238 1.00 36.32  ? 2009 THR A C     1 
ATOM   4698  O  O     . THR A 1 792  ? 179.833 180.117 147.236 1.00 36.37  ? 2009 THR A O     1 
ATOM   4699  C  CB    . THR A 1 792  ? 180.329 178.694 150.132 1.00 34.09  ? 2009 THR A CB    1 
ATOM   4700  O  OG1   . THR A 1 792  ? 180.557 178.772 151.544 1.00 35.93  ? 2009 THR A OG1   1 
ATOM   4701  C  CG2   . THR A 1 792  ? 181.643 178.400 149.426 1.00 31.36  ? 2009 THR A CG2   1 
ATOM   4702  N  N     . ASP A 1 793  ? 177.906 179.395 148.157 1.00 32.01  ? 2010 ASP A N     1 
ATOM   4703  C  CA    . ASP A 1 793  ? 177.217 179.335 146.876 1.00 28.83  ? 2010 ASP A CA    1 
ATOM   4704  C  C     . ASP A 1 793  ? 177.047 180.726 146.280 1.00 31.58  ? 2010 ASP A C     1 
ATOM   4705  O  O     . ASP A 1 793  ? 177.111 180.894 145.059 1.00 36.03  ? 2010 ASP A O     1 
ATOM   4706  C  CB    . ASP A 1 793  ? 175.865 178.650 147.050 1.00 27.36  ? 2010 ASP A CB    1 
ATOM   4707  C  CG    . ASP A 1 793  ? 176.001 177.218 147.515 1.00 30.41  ? 2010 ASP A CG    1 
ATOM   4708  O  OD1   . ASP A 1 793  ? 177.003 176.570 147.151 1.00 37.96  ? 2010 ASP A OD1   1 
ATOM   4709  O  OD2   . ASP A 1 793  ? 175.116 176.743 148.254 1.00 28.10  ? 2010 ASP A OD2   1 
ATOM   4710  N  N     . GLU A 1 794  ? 176.837 181.739 147.126 1.00 28.90  ? 2011 GLU A N     1 
ATOM   4711  C  CA    . GLU A 1 794  ? 176.755 183.109 146.624 1.00 28.46  ? 2011 GLU A CA    1 
ATOM   4712  C  C     . GLU A 1 794  ? 178.095 183.575 146.072 1.00 32.11  ? 2011 GLU A C     1 
ATOM   4713  O  O     . GLU A 1 794  ? 178.142 184.267 145.048 1.00 32.08  ? 2011 GLU A O     1 
ATOM   4714  C  CB    . GLU A 1 794  ? 176.279 184.055 147.725 1.00 32.50  ? 2011 GLU A CB    1 
ATOM   4715  C  CG    . GLU A 1 794  ? 175.611 185.324 147.212 1.00 34.98  ? 2011 GLU A CG    1 
ATOM   4716  C  CD    . GLU A 1 794  ? 176.602 186.394 146.788 1.00 35.81  ? 2011 GLU A CD    1 
ATOM   4717  O  OE1   . GLU A 1 794  ? 177.743 186.386 147.294 1.00 39.51  ? 2011 GLU A OE1   1 
ATOM   4718  O  OE2   . GLU A 1 794  ? 176.240 187.240 145.944 1.00 33.91  ? 2011 GLU A OE2   1 
ATOM   4719  N  N     . LEU A 1 795  ? 179.193 183.224 146.748 1.00 34.11  ? 2012 LEU A N     1 
ATOM   4720  C  CA    . LEU A 1 795  ? 180.517 183.566 146.230 1.00 34.50  ? 2012 LEU A CA    1 
ATOM   4721  C  C     . LEU A 1 795  ? 180.786 182.874 144.900 1.00 35.27  ? 2012 LEU A C     1 
ATOM   4722  O  O     . LEU A 1 795  ? 181.347 183.479 143.977 1.00 35.42  ? 2012 LEU A O     1 
ATOM   4723  C  CB    . LEU A 1 795  ? 181.599 183.208 147.250 1.00 33.51  ? 2012 LEU A CB    1 
ATOM   4724  C  CG    . LEU A 1 795  ? 182.009 184.260 148.286 1.00 36.04  ? 2012 LEU A CG    1 
ATOM   4725  C  CD1   . LEU A 1 795  ? 182.616 185.466 147.586 1.00 37.41  ? 2012 LEU A CD1   1 
ATOM   4726  C  CD2   . LEU A 1 795  ? 180.863 184.685 149.192 1.00 34.70  ? 2012 LEU A CD2   1 
ATOM   4727  N  N     . VAL A 1 796  ? 180.385 181.605 144.784 1.00 34.36  ? 2013 VAL A N     1 
ATOM   4728  C  CA    . VAL A 1 796  ? 180.520 180.881 143.522 1.00 31.37  ? 2013 VAL A CA    1 
ATOM   4729  C  C     . VAL A 1 796  ? 179.691 181.550 142.431 1.00 32.32  ? 2013 VAL A C     1 
ATOM   4730  O  O     . VAL A 1 796  ? 180.159 181.731 141.299 1.00 34.61  ? 2013 VAL A O     1 
ATOM   4731  C  CB    . VAL A 1 796  ? 180.126 179.404 143.713 1.00 31.06  ? 2013 VAL A CB    1 
ATOM   4732  C  CG1   . VAL A 1 796  ? 179.976 178.704 142.373 1.00 31.47  ? 2013 VAL A CG1   1 
ATOM   4733  C  CG2   . VAL A 1 796  ? 181.159 178.690 144.569 1.00 38.50  ? 2013 VAL A CG2   1 
ATOM   4734  N  N     . PHE A 1 797  ? 178.454 181.937 142.760 1.00 31.96  ? 2014 PHE A N     1 
ATOM   4735  C  CA    . PHE A 1 797  ? 177.589 182.625 141.806 1.00 25.63  ? 2014 PHE A CA    1 
ATOM   4736  C  C     . PHE A 1 797  ? 178.232 183.913 141.318 1.00 27.21  ? 2014 PHE A C     1 
ATOM   4737  O  O     . PHE A 1 797  ? 178.264 184.182 140.114 1.00 32.30  ? 2014 PHE A O     1 
ATOM   4738  C  CB    . PHE A 1 797  ? 176.228 182.911 142.450 1.00 21.86  ? 2014 PHE A CB    1 
ATOM   4739  C  CG    . PHE A 1 797  ? 175.224 183.559 141.522 1.00 20.41  ? 2014 PHE A CG    1 
ATOM   4740  C  CD1   . PHE A 1 797  ? 175.178 184.938 141.364 1.00 19.51  ? 2014 PHE A CD1   1 
ATOM   4741  C  CD2   . PHE A 1 797  ? 174.311 182.788 140.827 1.00 20.97  ? 2014 PHE A CD2   1 
ATOM   4742  C  CE1   . PHE A 1 797  ? 174.257 185.525 140.520 1.00 17.18  ? 2014 PHE A CE1   1 
ATOM   4743  C  CE2   . PHE A 1 797  ? 173.385 183.375 139.983 1.00 18.22  ? 2014 PHE A CE2   1 
ATOM   4744  C  CZ    . PHE A 1 797  ? 173.362 184.743 139.830 1.00 16.30  ? 2014 PHE A CZ    1 
ATOM   4745  N  N     . LYS A 1 798  ? 178.754 184.720 142.242 1.00 26.92  ? 2015 LYS A N     1 
ATOM   4746  C  CA    . LYS A 1 798  ? 179.349 185.995 141.855 1.00 30.73  ? 2015 LYS A CA    1 
ATOM   4747  C  C     . LYS A 1 798  ? 180.603 185.794 141.013 1.00 32.78  ? 2015 LYS A C     1 
ATOM   4748  O  O     . LYS A 1 798  ? 180.804 186.499 140.015 1.00 32.65  ? 2015 LYS A O     1 
ATOM   4749  C  CB    . LYS A 1 798  ? 179.661 186.829 143.095 1.00 32.78  ? 2015 LYS A CB    1 
ATOM   4750  C  CG    . LYS A 1 798  ? 179.687 188.327 142.838 1.00 31.47  ? 2015 LYS A CG    1 
ATOM   4751  C  CD    . LYS A 1 798  ? 178.471 188.774 142.040 1.00 29.24  ? 2015 LYS A CD    1 
ATOM   4752  C  CE    . LYS A 1 798  ? 177.234 188.866 142.919 1.00 28.28  ? 2015 LYS A CE    1 
ATOM   4753  N  NZ    . LYS A 1 798  ? 176.091 189.492 142.202 1.00 25.97  ? 2015 LYS A NZ    1 
ATOM   4754  N  N     . ASP A 1 799  ? 181.445 184.825 141.385 1.00 33.86  ? 2016 ASP A N     1 
ATOM   4755  C  CA    . ASP A 1 799  ? 182.671 184.576 140.631 1.00 36.45  ? 2016 ASP A CA    1 
ATOM   4756  C  C     . ASP A 1 799  ? 182.360 184.108 139.213 1.00 38.34  ? 2016 ASP A C     1 
ATOM   4757  O  O     . ASP A 1 799  ? 182.927 184.621 138.241 1.00 37.82  ? 2016 ASP A O     1 
ATOM   4758  C  CB    . ASP A 1 799  ? 183.534 183.549 141.366 1.00 36.70  ? 2016 ASP A CB    1 
ATOM   4759  C  CG    . ASP A 1 799  ? 184.624 182.963 140.488 1.00 46.22  ? 2016 ASP A CG    1 
ATOM   4760  O  OD1   . ASP A 1 799  ? 184.805 181.728 140.511 1.00 52.44  ? 2016 ASP A OD1   1 
ATOM   4761  O  OD2   . ASP A 1 799  ? 185.318 183.736 139.793 1.00 50.31  ? 2016 ASP A OD2   1 
ATOM   4762  N  N     . GLU A 1 800  ? 181.444 183.144 139.070 1.00 37.61  ? 2017 GLU A N     1 
ATOM   4763  C  CA    . GLU A 1 800  ? 181.121 182.648 137.736 1.00 32.53  ? 2017 GLU A CA    1 
ATOM   4764  C  C     . GLU A 1 800  ? 180.348 183.677 136.920 1.00 29.48  ? 2017 GLU A C     1 
ATOM   4765  O  O     . GLU A 1 800  ? 180.485 183.712 135.693 1.00 31.16  ? 2017 GLU A O     1 
ATOM   4766  C  CB    . GLU A 1 800  ? 180.336 181.339 137.820 1.00 28.99  ? 2017 GLU A CB    1 
ATOM   4767  C  CG    . GLU A 1 800  ? 180.992 180.243 138.654 1.00 36.47  ? 2017 GLU A CG    1 
ATOM   4768  C  CD    . GLU A 1 800  ? 182.424 179.945 138.249 1.00 36.61  ? 2017 GLU A CD    1 
ATOM   4769  O  OE1   . GLU A 1 800  ? 182.726 179.952 137.038 1.00 38.85  ? 2017 GLU A OE1   1 
ATOM   4770  O  OE2   . GLU A 1 800  ? 183.253 179.696 139.149 1.00 33.55  ? 2017 GLU A OE2   1 
ATOM   4771  N  N     . LEU A 1 801  ? 179.540 184.518 137.569 1.00 27.73  ? 2018 LEU A N     1 
ATOM   4772  C  CA    . LEU A 1 801  ? 178.844 185.576 136.848 1.00 28.38  ? 2018 LEU A CA    1 
ATOM   4773  C  C     . LEU A 1 801  ? 179.820 186.621 136.328 1.00 34.17  ? 2018 LEU A C     1 
ATOM   4774  O  O     . LEU A 1 801  ? 179.653 187.134 135.216 1.00 36.09  ? 2018 LEU A O     1 
ATOM   4775  C  CB    . LEU A 1 801  ? 177.799 186.224 137.751 1.00 25.65  ? 2018 LEU A CB    1 
ATOM   4776  C  CG    . LEU A 1 801  ? 176.585 186.830 137.052 1.00 23.64  ? 2018 LEU A CG    1 
ATOM   4777  C  CD1   . LEU A 1 801  ? 175.750 185.745 136.403 1.00 23.84  ? 2018 LEU A CD1   1 
ATOM   4778  C  CD2   . LEU A 1 801  ? 175.755 187.626 138.036 1.00 25.42  ? 2018 LEU A CD2   1 
ATOM   4779  N  N     . SER A 1 802  ? 180.840 186.958 137.122 1.00 35.19  ? 2019 SER A N     1 
ATOM   4780  C  CA    . SER A 1 802  ? 181.853 187.896 136.652 1.00 37.02  ? 2019 SER A CA    1 
ATOM   4781  C  C     . SER A 1 802  ? 182.712 187.277 135.556 1.00 36.68  ? 2019 SER A C     1 
ATOM   4782  O  O     . SER A 1 802  ? 183.134 187.972 134.624 1.00 36.15  ? 2019 SER A O     1 
ATOM   4783  C  CB    . SER A 1 802  ? 182.719 188.360 137.820 1.00 37.65  ? 2019 SER A CB    1 
ATOM   4784  O  OG    . SER A 1 802  ? 181.950 189.083 138.765 1.00 40.72  ? 2019 SER A OG    1 
ATOM   4785  N  N     . LYS A 1 803  ? 182.983 185.973 135.651 1.00 34.64  ? 2020 LYS A N     1 
ATOM   4786  C  CA    . LYS A 1 803  ? 183.829 185.320 134.656 1.00 33.91  ? 2020 LYS A CA    1 
ATOM   4787  C  C     . LYS A 1 803  ? 183.108 185.155 133.323 1.00 33.72  ? 2020 LYS A C     1 
ATOM   4788  O  O     . LYS A 1 803  ? 183.684 185.428 132.264 1.00 32.39  ? 2020 LYS A O     1 
ATOM   4789  C  CB    . LYS A 1 803  ? 184.300 183.966 135.184 1.00 34.82  ? 2020 LYS A CB    1 
ATOM   4790  C  CG    . LYS A 1 803  ? 185.391 183.319 134.353 1.00 39.13  ? 2020 LYS A CG    1 
ATOM   4791  C  CD    . LYS A 1 803  ? 185.732 181.937 134.883 1.00 43.06  ? 2020 LYS A CD    1 
ATOM   4792  C  CE    . LYS A 1 803  ? 184.674 180.919 134.492 1.00 40.56  ? 2020 LYS A CE    1 
ATOM   4793  N  NZ    . LYS A 1 803  ? 184.939 179.585 135.097 1.00 40.64  ? 2020 LYS A NZ    1 
ATOM   4794  N  N     . ILE A 1 804  ? 181.851 184.715 133.350 1.00 33.75  ? 2021 ILE A N     1 
ATOM   4795  C  CA    . ILE A 1 804  ? 181.130 184.428 132.112 1.00 32.99  ? 2021 ILE A CA    1 
ATOM   4796  C  C     . ILE A 1 804  ? 180.494 185.693 131.551 1.00 32.67  ? 2021 ILE A C     1 
ATOM   4797  O  O     . ILE A 1 804  ? 180.790 186.112 130.427 1.00 35.06  ? 2021 ILE A O     1 
ATOM   4798  C  CB    . ILE A 1 804  ? 180.076 183.331 132.345 1.00 26.61  ? 2021 ILE A CB    1 
ATOM   4799  C  CG1   . ILE A 1 804  ? 180.745 182.041 132.811 1.00 29.63  ? 2021 ILE A CG1   1 
ATOM   4800  C  CG2   . ILE A 1 804  ? 179.278 183.087 131.079 1.00 25.48  ? 2021 ILE A CG2   1 
ATOM   4801  C  CD1   . ILE A 1 804  ? 179.842 181.158 133.629 1.00 27.23  ? 2021 ILE A CD1   1 
ATOM   4802  N  N     . PHE A 1 805  ? 179.606 186.312 132.321 1.00 28.13  ? 2022 PHE A N     1 
ATOM   4803  C  CA    . PHE A 1 805  ? 178.933 187.518 131.870 1.00 27.19  ? 2022 PHE A CA    1 
ATOM   4804  C  C     . PHE A 1 805  ? 179.814 188.739 132.101 1.00 30.35  ? 2022 PHE A C     1 
ATOM   4805  O  O     . PHE A 1 805  ? 180.696 188.742 132.964 1.00 32.29  ? 2022 PHE A O     1 
ATOM   4806  C  CB    . PHE A 1 805  ? 177.597 187.686 132.593 1.00 26.72  ? 2022 PHE A CB    1 
ATOM   4807  C  CG    . PHE A 1 805  ? 176.557 186.680 132.185 1.00 23.24  ? 2022 PHE A CG    1 
ATOM   4808  C  CD1   . PHE A 1 805  ? 175.747 186.908 131.088 1.00 21.86  ? 2022 PHE A CD1   1 
ATOM   4809  C  CD2   . PHE A 1 805  ? 176.390 185.508 132.900 1.00 22.20  ? 2022 PHE A CD2   1 
ATOM   4810  C  CE1   . PHE A 1 805  ? 174.792 185.987 130.711 1.00 19.82  ? 2022 PHE A CE1   1 
ATOM   4811  C  CE2   . PHE A 1 805  ? 175.433 184.584 132.529 1.00 17.84  ? 2022 PHE A CE2   1 
ATOM   4812  C  CZ    . PHE A 1 805  ? 174.634 184.825 131.433 1.00 16.96  ? 2022 PHE A CZ    1 
ATOM   4813  N  N     . ASP A 1 806  ? 179.570 189.786 131.309 1.00 30.94  ? 2023 ASP A N     1 
ATOM   4814  C  CA    . ASP A 1 806  ? 180.381 190.994 131.420 1.00 35.85  ? 2023 ASP A CA    1 
ATOM   4815  C  C     . ASP A 1 806  ? 180.026 191.792 132.669 1.00 34.54  ? 2023 ASP A C     1 
ATOM   4816  O  O     . ASP A 1 806  ? 180.915 192.319 133.349 1.00 33.22  ? 2023 ASP A O     1 
ATOM   4817  C  CB    . ASP A 1 806  ? 180.225 191.852 130.163 1.00 37.50  ? 2023 ASP A CB    1 
ATOM   4818  C  CG    . ASP A 1 806  ? 178.773 192.075 129.777 1.00 37.14  ? 2023 ASP A CG    1 
ATOM   4819  O  OD1   . ASP A 1 806  ? 177.873 191.725 130.569 1.00 37.63  ? 2023 ASP A OD1   1 
ATOM   4820  O  OD2   . ASP A 1 806  ? 178.531 192.606 128.673 1.00 35.42  ? 2023 ASP A OD2   1 
ATOM   4821  N  N     . SER A 1 807  ? 178.740 191.893 132.986 1.00 33.32  ? 2024 SER A N     1 
ATOM   4822  C  CA    . SER A 1 807  ? 178.296 192.652 134.148 1.00 33.17  ? 2024 SER A CA    1 
ATOM   4823  C  C     . SER A 1 807  ? 177.450 191.791 135.078 1.00 31.89  ? 2024 SER A C     1 
ATOM   4824  O  O     . SER A 1 807  ? 177.641 191.803 136.294 1.00 30.33  ? 2024 SER A O     1 
ATOM   4825  C  CB    . SER A 1 807  ? 177.505 193.886 133.710 1.00 32.73  ? 2024 SER A CB    1 
ATOM   4826  O  OG    . SER A 1 807  ? 176.915 194.533 134.824 1.00 35.64  ? 2024 SER A OG    1 
ATOM   4827  N  N     . SER A 1 814  ? 164.307 202.570 140.766 1.00 68.55  ? 2031 SER A N     1 
ATOM   4828  C  CA    . SER A 1 814  ? 164.357 201.408 141.644 1.00 65.64  ? 2031 SER A CA    1 
ATOM   4829  C  C     . SER A 1 814  ? 164.647 201.819 143.083 1.00 55.74  ? 2031 SER A C     1 
ATOM   4830  O  O     . SER A 1 814  ? 164.354 201.080 144.021 1.00 52.30  ? 2031 SER A O     1 
ATOM   4831  C  CB    . SER A 1 814  ? 165.413 200.414 141.157 1.00 67.63  ? 2031 SER A CB    1 
ATOM   4832  O  OG    . SER A 1 814  ? 166.692 201.021 141.088 1.00 68.43  ? 2031 SER A OG    1 
ATOM   4833  N  N     . LYS A 1 815  ? 165.227 203.008 143.250 1.00 55.24  ? 2032 LYS A N     1 
ATOM   4834  C  CA    . LYS A 1 815  ? 165.565 203.517 144.573 1.00 52.49  ? 2032 LYS A CA    1 
ATOM   4835  C  C     . LYS A 1 815  ? 164.357 204.031 145.343 1.00 48.67  ? 2032 LYS A C     1 
ATOM   4836  O  O     . LYS A 1 815  ? 164.482 204.298 146.544 1.00 49.81  ? 2032 LYS A O     1 
ATOM   4837  C  CB    . LYS A 1 815  ? 166.609 204.629 144.456 1.00 55.03  ? 2032 LYS A CB    1 
ATOM   4838  C  CG    . LYS A 1 815  ? 167.883 204.217 143.732 1.00 56.65  ? 2032 LYS A CG    1 
ATOM   4839  C  CD    . LYS A 1 815  ? 168.614 203.105 144.472 1.00 56.57  ? 2032 LYS A CD    1 
ATOM   4840  C  CE    . LYS A 1 815  ? 168.677 201.826 143.648 1.00 54.07  ? 2032 LYS A CE    1 
ATOM   4841  N  NZ    . LYS A 1 815  ? 169.318 200.714 144.401 1.00 52.63  ? 2032 LYS A NZ    1 
ATOM   4842  N  N     . ALA A 1 816  ? 163.204 204.186 144.687 1.00 45.84  ? 2033 ALA A N     1 
ATOM   4843  C  CA    . ALA A 1 816  ? 162.002 204.618 145.392 1.00 48.51  ? 2033 ALA A CA    1 
ATOM   4844  C  C     . ALA A 1 816  ? 161.568 203.581 146.418 1.00 49.50  ? 2033 ALA A C     1 
ATOM   4845  O  O     . ALA A 1 816  ? 161.249 203.919 147.565 1.00 52.44  ? 2033 ALA A O     1 
ATOM   4846  C  CB    . ALA A 1 816  ? 160.878 204.892 144.392 1.00 51.93  ? 2033 ALA A CB    1 
ATOM   4847  N  N     . ILE A 1 817  ? 161.577 202.303 146.032 1.00 47.76  ? 2034 ILE A N     1 
ATOM   4848  C  CA    . ILE A 1 817  ? 161.198 201.260 146.977 1.00 46.33  ? 2034 ILE A CA    1 
ATOM   4849  C  C     . ILE A 1 817  ? 162.277 201.071 148.037 1.00 42.98  ? 2034 ILE A C     1 
ATOM   4850  O  O     . ILE A 1 817  ? 161.974 200.676 149.164 1.00 43.26  ? 2034 ILE A O     1 
ATOM   4851  C  CB    . ILE A 1 817  ? 160.867 199.945 146.242 1.00 41.14  ? 2034 ILE A CB    1 
ATOM   4852  C  CG1   . ILE A 1 817  ? 160.057 199.020 147.152 1.00 32.62  ? 2034 ILE A CG1   1 
ATOM   4853  C  CG2   . ILE A 1 817  ? 162.125 199.248 145.744 1.00 40.37  ? 2034 ILE A CG2   1 
ATOM   4854  C  CD1   . ILE A 1 817  ? 158.699 199.559 147.517 1.00 35.19  ? 2034 ILE A CD1   1 
ATOM   4855  N  N     . VAL A 1 818  ? 163.535 201.387 147.722 1.00 43.83  ? 2035 VAL A N     1 
ATOM   4856  C  CA    . VAL A 1 818  ? 164.594 201.315 148.727 1.00 41.19  ? 2035 VAL A CA    1 
ATOM   4857  C  C     . VAL A 1 818  ? 164.392 202.391 149.788 1.00 41.32  ? 2035 VAL A C     1 
ATOM   4858  O  O     . VAL A 1 818  ? 164.482 202.126 150.995 1.00 42.22  ? 2035 VAL A O     1 
ATOM   4859  C  CB    . VAL A 1 818  ? 165.974 201.432 148.056 1.00 41.16  ? 2035 VAL A CB    1 
ATOM   4860  C  CG1   . VAL A 1 818  ? 167.059 201.679 149.091 1.00 38.41  ? 2035 VAL A CG1   1 
ATOM   4861  C  CG2   . VAL A 1 818  ? 166.276 200.180 147.258 1.00 42.36  ? 2035 VAL A CG2   1 
ATOM   4862  N  N     . GLN A 1 819  ? 164.099 203.619 149.352 1.00 42.78  ? 2036 GLN A N     1 
ATOM   4863  C  CA    . GLN A 1 819  ? 163.813 204.697 150.293 1.00 43.21  ? 2036 GLN A CA    1 
ATOM   4864  C  C     . GLN A 1 819  ? 162.562 204.400 151.110 1.00 44.66  ? 2036 GLN A C     1 
ATOM   4865  O  O     . GLN A 1 819  ? 162.518 204.673 152.316 1.00 48.74  ? 2036 GLN A O     1 
ATOM   4866  C  CB    . GLN A 1 819  ? 163.662 206.020 149.541 1.00 43.44  ? 2036 GLN A CB    1 
ATOM   4867  C  CG    . GLN A 1 819  ? 163.653 207.249 150.432 1.00 43.29  ? 2036 GLN A CG    1 
ATOM   4868  C  CD    . GLN A 1 819  ? 164.663 207.164 151.557 1.00 44.96  ? 2036 GLN A CD    1 
ATOM   4869  O  OE1   . GLN A 1 819  ? 165.872 207.146 151.322 1.00 44.02  ? 2036 GLN A OE1   1 
ATOM   4870  N  NE2   . GLN A 1 819  ? 164.173 207.113 152.790 1.00 43.71  ? 2036 GLN A NE2   1 
ATOM   4871  N  N     . CYS A 1 820  ? 161.537 203.829 150.473 1.00 40.77  ? 2037 CYS A N     1 
ATOM   4872  C  CA    . CYS A 1 820  ? 160.315 203.505 151.199 1.00 37.71  ? 2037 CYS A CA    1 
ATOM   4873  C  C     . CYS A 1 820  ? 160.544 202.375 152.196 1.00 40.78  ? 2037 CYS A C     1 
ATOM   4874  O  O     . CYS A 1 820  ? 159.965 202.381 153.288 1.00 44.41  ? 2037 CYS A O     1 
ATOM   4875  C  CB    . CYS A 1 820  ? 159.206 203.145 150.218 1.00 38.98  ? 2037 CYS A CB    1 
ATOM   4876  S  SG    . CYS A 1 820  ? 157.593 203.039 150.989 1.00 48.69  ? 2037 CYS A SG    1 
ATOM   4877  N  N     . LEU A 1 821  ? 161.384 201.398 151.842 1.00 41.15  ? 2038 LEU A N     1 
ATOM   4878  C  CA    . LEU A 1 821  ? 161.743 200.337 152.777 1.00 36.01  ? 2038 LEU A CA    1 
ATOM   4879  C  C     . LEU A 1 821  ? 162.504 200.891 153.971 1.00 33.99  ? 2038 LEU A C     1 
ATOM   4880  O  O     . LEU A 1 821  ? 162.261 200.483 155.111 1.00 34.10  ? 2038 LEU A O     1 
ATOM   4881  C  CB    . LEU A 1 821  ? 162.575 199.268 152.066 1.00 31.40  ? 2038 LEU A CB    1 
ATOM   4882  C  CG    . LEU A 1 821  ? 161.838 198.080 151.449 1.00 27.79  ? 2038 LEU A CG    1 
ATOM   4883  C  CD1   . LEU A 1 821  ? 162.732 197.361 150.463 1.00 32.92  ? 2038 LEU A CD1   1 
ATOM   4884  C  CD2   . LEU A 1 821  ? 161.388 197.127 152.533 1.00 23.96  ? 2038 LEU A CD2   1 
ATOM   4885  N  N     . LYS A 1 822  ? 163.429 201.824 153.727 1.00 33.08  ? 2039 LYS A N     1 
ATOM   4886  C  CA    . LYS A 1 822  ? 164.151 202.453 154.829 1.00 32.74  ? 2039 LYS A CA    1 
ATOM   4887  C  C     . LYS A 1 822  ? 163.206 203.231 155.738 1.00 34.33  ? 2039 LYS A C     1 
ATOM   4888  O  O     . LYS A 1 822  ? 163.321 203.168 156.969 1.00 38.17  ? 2039 LYS A O     1 
ATOM   4889  C  CB    . LYS A 1 822  ? 165.244 203.369 154.284 1.00 30.44  ? 2039 LYS A CB    1 
ATOM   4890  C  CG    . LYS A 1 822  ? 166.489 202.636 153.823 1.00 32.56  ? 2039 LYS A CG    1 
ATOM   4891  C  CD    . LYS A 1 822  ? 167.521 203.602 153.269 1.00 35.46  ? 2039 LYS A CD    1 
ATOM   4892  C  CE    . LYS A 1 822  ? 168.732 202.863 152.728 1.00 34.93  ? 2039 LYS A CE    1 
ATOM   4893  N  NZ    . LYS A 1 822  ? 169.290 201.910 153.725 1.00 34.77  ? 2039 LYS A NZ    1 
ATOM   4894  N  N     . ASP A 1 823  ? 162.255 203.961 155.146 1.00 35.24  ? 2040 ASP A N     1 
ATOM   4895  C  CA    . ASP A 1 823  ? 161.288 204.710 155.944 1.00 36.99  ? 2040 ASP A CA    1 
ATOM   4896  C  C     . ASP A 1 823  ? 160.402 203.779 156.765 1.00 36.01  ? 2040 ASP A C     1 
ATOM   4897  O  O     . ASP A 1 823  ? 160.146 204.038 157.948 1.00 35.82  ? 2040 ASP A O     1 
ATOM   4898  C  CB    . ASP A 1 823  ? 160.437 205.598 155.036 1.00 40.37  ? 2040 ASP A CB    1 
ATOM   4899  C  CG    . ASP A 1 823  ? 161.239 206.713 154.392 1.00 45.76  ? 2040 ASP A CG    1 
ATOM   4900  O  OD1   . ASP A 1 823  ? 162.409 206.909 154.783 1.00 47.07  ? 2040 ASP A OD1   1 
ATOM   4901  O  OD2   . ASP A 1 823  ? 160.699 207.394 153.496 1.00 46.12  ? 2040 ASP A OD2   1 
ATOM   4902  N  N     . ALA A 1 824  ? 159.939 202.681 156.163 1.00 34.75  ? 2041 ALA A N     1 
ATOM   4903  C  CA    . ALA A 1 824  ? 159.087 201.741 156.885 1.00 34.53  ? 2041 ALA A CA    1 
ATOM   4904  C  C     . ALA A 1 824  ? 159.856 201.032 157.993 1.00 32.79  ? 2041 ALA A C     1 
ATOM   4905  O  O     . ALA A 1 824  ? 159.302 200.766 159.067 1.00 36.93  ? 2041 ALA A O     1 
ATOM   4906  C  CB    . ALA A 1 824  ? 158.484 200.725 155.916 1.00 30.22  ? 2041 ALA A CB    1 
ATOM   4907  N  N     . GLY A 1 825  ? 161.127 200.713 157.753 1.00 27.91  ? 2042 GLY A N     1 
ATOM   4908  C  CA    . GLY A 1 825  ? 161.932 200.098 158.792 1.00 24.62  ? 2042 GLY A CA    1 
ATOM   4909  C  C     . GLY A 1 825  ? 162.203 201.032 159.954 1.00 24.06  ? 2042 GLY A C     1 
ATOM   4910  O  O     . GLY A 1 825  ? 162.155 200.620 161.115 1.00 24.70  ? 2042 GLY A O     1 
ATOM   4911  N  N     . GLN A 1 826  ? 162.497 202.302 159.661 1.00 26.87  ? 2043 GLN A N     1 
ATOM   4912  C  CA    . GLN A 1 826  ? 162.662 203.271 160.738 1.00 28.33  ? 2043 GLN A CA    1 
ATOM   4913  C  C     . GLN A 1 826  ? 161.352 203.516 161.474 1.00 27.96  ? 2043 GLN A C     1 
ATOM   4914  O  O     . GLN A 1 826  ? 161.364 203.835 162.668 1.00 28.83  ? 2043 GLN A O     1 
ATOM   4915  C  CB    . GLN A 1 826  ? 163.228 204.580 160.190 1.00 29.72  ? 2043 GLN A CB    1 
ATOM   4916  C  CG    . GLN A 1 826  ? 164.699 204.495 159.821 1.00 28.64  ? 2043 GLN A CG    1 
ATOM   4917  C  CD    . GLN A 1 826  ? 165.485 203.619 160.778 1.00 28.19  ? 2043 GLN A CD    1 
ATOM   4918  O  OE1   . GLN A 1 826  ? 165.665 203.962 161.947 1.00 27.36  ? 2043 GLN A OE1   1 
ATOM   4919  N  NE2   . GLN A 1 826  ? 165.956 202.479 160.286 1.00 26.68  ? 2043 GLN A NE2   1 
ATOM   4920  N  N     . ARG A 1 827  ? 160.219 203.376 160.783 1.00 27.47  ? 2044 ARG A N     1 
ATOM   4921  C  CA    . ARG A 1 827  ? 158.932 203.416 161.466 1.00 29.33  ? 2044 ARG A CA    1 
ATOM   4922  C  C     . ARG A 1 827  ? 158.755 202.213 162.386 1.00 27.84  ? 2044 ARG A C     1 
ATOM   4923  O  O     . ARG A 1 827  ? 158.197 202.339 163.482 1.00 30.68  ? 2044 ARG A O     1 
ATOM   4924  C  CB    . ARG A 1 827  ? 157.797 203.477 160.445 1.00 29.48  ? 2044 ARG A CB    1 
ATOM   4925  C  CG    . ARG A 1 827  ? 156.450 203.833 161.045 1.00 31.95  ? 2044 ARG A CG    1 
ATOM   4926  C  CD    . ARG A 1 827  ? 155.368 203.919 159.982 1.00 35.08  ? 2044 ARG A CD    1 
ATOM   4927  N  NE    . ARG A 1 827  ? 154.534 202.724 159.964 1.00 41.48  ? 2044 ARG A NE    1 
ATOM   4928  C  CZ    . ARG A 1 827  ? 153.648 202.442 159.019 1.00 48.67  ? 2044 ARG A CZ    1 
ATOM   4929  N  NH1   . ARG A 1 827  ? 153.445 203.257 157.998 1.00 45.76  ? 2044 ARG A NH1   1 
ATOM   4930  N  NH2   . ARG A 1 827  ? 152.946 201.316 159.104 1.00 46.77  ? 2044 ARG A NH2   1 
ATOM   4931  N  N     . SER A 1 828  ? 159.223 201.040 161.960 1.00 22.69  ? 2045 SER A N     1 
ATOM   4932  C  CA    . SER A 1 828  ? 159.020 199.809 162.714 1.00 21.13  ? 2045 SER A CA    1 
ATOM   4933  C  C     . SER A 1 828  ? 160.105 199.544 163.750 1.00 20.52  ? 2045 SER A C     1 
ATOM   4934  O  O     . SER A 1 828  ? 159.983 198.580 164.513 1.00 16.95  ? 2045 SER A O     1 
ATOM   4935  C  CB    . SER A 1 828  ? 158.933 198.614 161.759 1.00 21.09  ? 2045 SER A CB    1 
ATOM   4936  O  OG    . SER A 1 828  ? 157.980 198.844 160.735 1.00 25.21  ? 2045 SER A OG    1 
ATOM   4937  N  N     . GLY A 1 829  ? 161.154 200.362 163.801 1.00 20.75  ? 2046 GLY A N     1 
ATOM   4938  C  CA    . GLY A 1 829  ? 162.215 200.200 164.771 1.00 17.80  ? 2046 GLY A CA    1 
ATOM   4939  C  C     . GLY A 1 829  ? 163.423 199.430 164.281 1.00 17.57  ? 2046 GLY A C     1 
ATOM   4940  O  O     . GLY A 1 829  ? 164.463 199.455 164.949 1.00 16.24  ? 2046 GLY A O     1 
ATOM   4941  N  N     . PHE A 1 830  ? 163.318 198.752 163.141 1.00 17.45  ? 2047 PHE A N     1 
ATOM   4942  C  CA    . PHE A 1 830  ? 164.424 197.968 162.617 1.00 15.07  ? 2047 PHE A CA    1 
ATOM   4943  C  C     . PHE A 1 830  ? 165.521 198.881 162.072 1.00 20.50  ? 2047 PHE A C     1 
ATOM   4944  O  O     . PHE A 1 830  ? 165.332 200.084 161.870 1.00 27.26  ? 2047 PHE A O     1 
ATOM   4945  C  CB    . PHE A 1 830  ? 163.935 197.019 161.526 1.00 14.69  ? 2047 PHE A CB    1 
ATOM   4946  C  CG    . PHE A 1 830  ? 162.871 196.064 161.983 1.00 15.05  ? 2047 PHE A CG    1 
ATOM   4947  C  CD1   . PHE A 1 830  ? 162.905 195.523 163.255 1.00 15.76  ? 2047 PHE A CD1   1 
ATOM   4948  C  CD2   . PHE A 1 830  ? 161.839 195.704 161.139 1.00 15.51  ? 2047 PHE A CD2   1 
ATOM   4949  C  CE1   . PHE A 1 830  ? 161.928 194.643 163.675 1.00 13.09  ? 2047 PHE A CE1   1 
ATOM   4950  C  CE2   . PHE A 1 830  ? 160.862 194.827 161.554 1.00 15.91  ? 2047 PHE A CE2   1 
ATOM   4951  C  CZ    . PHE A 1 830  ? 160.907 194.296 162.824 1.00 12.85  ? 2047 PHE A CZ    1 
ATOM   4952  N  N     . SER A 1 831  ? 166.688 198.288 161.833 1.00 19.37  ? 2048 SER A N     1 
ATOM   4953  C  CA    . SER A 1 831  ? 167.853 198.997 161.322 1.00 23.21  ? 2048 SER A CA    1 
ATOM   4954  C  C     . SER A 1 831  ? 168.294 198.362 160.013 1.00 25.51  ? 2048 SER A C     1 
ATOM   4955  O  O     . SER A 1 831  ? 168.431 197.137 159.927 1.00 25.20  ? 2048 SER A O     1 
ATOM   4956  C  CB    . SER A 1 831  ? 169.000 198.974 162.332 1.00 22.93  ? 2048 SER A CB    1 
ATOM   4957  O  OG    . SER A 1 831  ? 170.236 199.247 161.698 1.00 24.93  ? 2048 SER A OG    1 
ATOM   4958  N  N     . MET A 1 832  ? 168.521 199.197 159.001 1.00 27.54  ? 2049 MET A N     1 
ATOM   4959  C  CA    . MET A 1 832  ? 168.843 198.737 157.651 1.00 26.90  ? 2049 MET A CA    1 
ATOM   4960  C  C     . MET A 1 832  ? 170.330 198.436 157.534 1.00 28.60  ? 2049 MET A C     1 
ATOM   4961  O  O     . MET A 1 832  ? 171.127 199.270 157.104 1.00 31.43  ? 2049 MET A O     1 
ATOM   4962  C  CB    . MET A 1 832  ? 168.405 199.768 156.619 1.00 26.21  ? 2049 MET A CB    1 
ATOM   4963  C  CG    . MET A 1 832  ? 166.906 199.861 156.475 1.00 28.90  ? 2049 MET A CG    1 
ATOM   4964  S  SD    . MET A 1 832  ? 166.221 198.200 156.384 1.00 27.64  ? 2049 MET A SD    1 
ATOM   4965  C  CE    . MET A 1 832  ? 164.641 198.428 157.174 1.00 19.87  ? 2049 MET A CE    1 
ATOM   4966  N  N     . SER A 1 833  ? 170.705 197.220 157.918 1.00 25.92  ? 2050 SER A N     1 
ATOM   4967  C  CA    . SER A 1 833  ? 172.020 196.713 157.571 1.00 26.35  ? 2050 SER A CA    1 
ATOM   4968  C  C     . SER A 1 833  ? 172.055 196.356 156.086 1.00 28.28  ? 2050 SER A C     1 
ATOM   4969  O  O     . SER A 1 833  ? 171.023 196.282 155.414 1.00 27.32  ? 2050 SER A O     1 
ATOM   4970  C  CB    . SER A 1 833  ? 172.372 195.498 158.428 1.00 26.82  ? 2050 SER A CB    1 
ATOM   4971  O  OG    . SER A 1 833  ? 173.591 194.912 158.002 1.00 24.27  ? 2050 SER A OG    1 
ATOM   4972  N  N     . GLU A 1 834  ? 173.268 196.148 155.568 1.00 30.31  ? 2051 GLU A N     1 
ATOM   4973  C  CA    . GLU A 1 834  ? 173.413 195.827 154.152 1.00 29.54  ? 2051 GLU A CA    1 
ATOM   4974  C  C     . GLU A 1 834  ? 172.780 194.482 153.816 1.00 26.96  ? 2051 GLU A C     1 
ATOM   4975  O  O     . GLU A 1 834  ? 172.094 194.352 152.796 1.00 27.65  ? 2051 GLU A O     1 
ATOM   4976  C  CB    . GLU A 1 834  ? 174.889 195.842 153.758 1.00 31.70  ? 2051 GLU A CB    1 
ATOM   4977  C  CG    . GLU A 1 834  ? 175.510 197.229 153.757 1.00 42.00  ? 2051 GLU A CG    1 
ATOM   4978  C  CD    . GLU A 1 834  ? 174.912 198.137 152.698 1.00 44.37  ? 2051 GLU A CD    1 
ATOM   4979  O  OE1   . GLU A 1 834  ? 174.572 197.638 151.605 1.00 44.21  ? 2051 GLU A OE1   1 
ATOM   4980  O  OE2   . GLU A 1 834  ? 174.781 199.352 152.960 1.00 42.81  ? 2051 GLU A OE2   1 
ATOM   4981  N  N     . GLU A 1 835  ? 172.991 193.475 154.667 1.00 23.58  ? 2052 GLU A N     1 
ATOM   4982  C  CA    . GLU A 1 835  ? 172.382 192.170 154.435 1.00 21.80  ? 2052 GLU A CA    1 
ATOM   4983  C  C     . GLU A 1 835  ? 170.864 192.242 154.532 1.00 21.52  ? 2052 GLU A C     1 
ATOM   4984  O  O     . GLU A 1 835  ? 170.155 191.635 153.720 1.00 25.08  ? 2052 GLU A O     1 
ATOM   4985  C  CB    . GLU A 1 835  ? 172.935 191.150 155.428 1.00 19.95  ? 2052 GLU A CB    1 
ATOM   4986  C  CG    . GLU A 1 835  ? 172.299 189.777 155.321 1.00 24.90  ? 2052 GLU A CG    1 
ATOM   4987  C  CD    . GLU A 1 835  ? 173.075 188.844 154.415 1.00 31.67  ? 2052 GLU A CD    1 
ATOM   4988  O  OE1   . GLU A 1 835  ? 174.039 189.303 153.769 1.00 29.64  ? 2052 GLU A OE1   1 
ATOM   4989  O  OE2   . GLU A 1 835  ? 172.715 187.650 154.343 1.00 32.32  ? 2052 GLU A OE2   1 
ATOM   4990  N  N     . PHE A 1 836  ? 170.349 192.984 155.514 1.00 20.38  ? 2053 PHE A N     1 
ATOM   4991  C  CA    . PHE A 1 836  ? 168.904 193.094 155.677 1.00 18.88  ? 2053 PHE A CA    1 
ATOM   4992  C  C     . PHE A 1 836  ? 168.266 193.826 154.505 1.00 19.57  ? 2053 PHE A C     1 
ATOM   4993  O  O     . PHE A 1 836  ? 167.207 193.418 154.017 1.00 19.56  ? 2053 PHE A O     1 
ATOM   4994  C  CB    . PHE A 1 836  ? 168.573 193.803 156.987 1.00 17.99  ? 2053 PHE A CB    1 
ATOM   4995  C  CG    . PHE A 1 836  ? 167.113 193.807 157.314 1.00 14.62  ? 2053 PHE A CG    1 
ATOM   4996  C  CD1   . PHE A 1 836  ? 166.360 192.658 157.178 1.00 14.65  ? 2053 PHE A CD1   1 
ATOM   4997  C  CD2   . PHE A 1 836  ? 166.491 194.960 157.749 1.00 15.45  ? 2053 PHE A CD2   1 
ATOM   4998  C  CE1   . PHE A 1 836  ? 165.017 192.659 157.478 1.00 14.55  ? 2053 PHE A CE1   1 
ATOM   4999  C  CE2   . PHE A 1 836  ? 165.148 194.965 158.048 1.00 16.51  ? 2053 PHE A CE2   1 
ATOM   5000  C  CZ    . PHE A 1 836  ? 164.410 193.813 157.912 1.00 14.08  ? 2053 PHE A CZ    1 
ATOM   5001  N  N     . LEU A 1 837  ? 168.895 194.907 154.040 1.00 20.69  ? 2054 LEU A N     1 
ATOM   5002  C  CA    . LEU A 1 837  ? 168.373 195.622 152.880 1.00 21.24  ? 2054 LEU A CA    1 
ATOM   5003  C  C     . LEU A 1 837  ? 168.439 194.760 151.627 1.00 23.57  ? 2054 LEU A C     1 
ATOM   5004  O  O     . LEU A 1 837  ? 167.512 194.778 150.808 1.00 27.97  ? 2054 LEU A O     1 
ATOM   5005  C  CB    . LEU A 1 837  ? 169.138 196.926 152.676 1.00 24.35  ? 2054 LEU A CB    1 
ATOM   5006  C  CG    . LEU A 1 837  ? 168.420 197.970 151.822 1.00 26.58  ? 2054 LEU A CG    1 
ATOM   5007  C  CD1   . LEU A 1 837  ? 167.150 198.436 152.511 1.00 28.46  ? 2054 LEU A CD1   1 
ATOM   5008  C  CD2   . LEU A 1 837  ? 169.340 199.142 151.537 1.00 33.13  ? 2054 LEU A CD2   1 
ATOM   5009  N  N     . LYS A 1 838  ? 169.524 193.997 151.466 1.00 22.37  ? 2055 LYS A N     1 
ATOM   5010  C  CA    . LYS A 1 838  ? 169.638 193.094 150.326 1.00 20.66  ? 2055 LYS A CA    1 
ATOM   5011  C  C     . LYS A 1 838  ? 168.531 192.049 150.336 1.00 19.35  ? 2055 LYS A C     1 
ATOM   5012  O  O     . LYS A 1 838  ? 167.897 191.796 149.305 1.00 20.37  ? 2055 LYS A O     1 
ATOM   5013  C  CB    . LYS A 1 838  ? 171.010 192.419 150.329 1.00 18.69  ? 2055 LYS A CB    1 
ATOM   5014  C  CG    . LYS A 1 838  ? 171.151 191.293 149.323 1.00 18.41  ? 2055 LYS A CG    1 
ATOM   5015  C  CD    . LYS A 1 838  ? 172.556 190.715 149.329 1.00 19.79  ? 2055 LYS A CD    1 
ATOM   5016  C  CE    . LYS A 1 838  ? 172.733 189.708 150.450 1.00 19.94  ? 2055 LYS A CE    1 
ATOM   5017  N  NZ    . LYS A 1 838  ? 173.989 188.924 150.301 1.00 22.25  ? 2055 LYS A NZ    1 
ATOM   5018  N  N     . LYS A 1 839  ? 168.262 191.454 151.501 1.00 17.02  ? 2056 LYS A N     1 
ATOM   5019  C  CA    . LYS A 1 839  ? 167.223 190.434 151.577 1.00 14.14  ? 2056 LYS A CA    1 
ATOM   5020  C  C     . LYS A 1 839  ? 165.829 191.027 151.413 1.00 17.02  ? 2056 LYS A C     1 
ATOM   5021  O  O     . LYS A 1 839  ? 164.957 190.386 150.817 1.00 20.18  ? 2056 LYS A O     1 
ATOM   5022  C  CB    . LYS A 1 839  ? 167.333 189.672 152.894 1.00 13.80  ? 2056 LYS A CB    1 
ATOM   5023  C  CG    . LYS A 1 839  ? 168.561 188.780 152.969 1.00 16.72  ? 2056 LYS A CG    1 
ATOM   5024  C  CD    . LYS A 1 839  ? 168.430 187.589 152.037 1.00 14.70  ? 2056 LYS A CD    1 
ATOM   5025  C  CE    . LYS A 1 839  ? 169.632 186.670 152.139 1.00 12.56  ? 2056 LYS A CE    1 
ATOM   5026  N  NZ    . LYS A 1 839  ? 169.489 185.494 151.242 1.00 9.97   ? 2056 LYS A NZ    1 
ATOM   5027  N  N     . CYS A 1 840  ? 165.602 192.245 151.914 1.00 17.59  ? 2057 CYS A N     1 
ATOM   5028  C  CA    . CYS A 1 840  ? 164.318 192.906 151.696 1.00 17.33  ? 2057 CYS A CA    1 
ATOM   5029  C  C     . CYS A 1 840  ? 164.085 193.196 150.217 1.00 23.27  ? 2057 CYS A C     1 
ATOM   5030  O  O     . CYS A 1 840  ? 162.987 192.960 149.697 1.00 24.98  ? 2057 CYS A O     1 
ATOM   5031  C  CB    . CYS A 1 840  ? 164.244 194.197 152.510 1.00 13.98  ? 2057 CYS A CB    1 
ATOM   5032  S  SG    . CYS A 1 840  ? 163.988 193.954 154.275 1.00 20.02  ? 2057 CYS A SG    1 
ATOM   5033  N  N     . MET A 1 841  ? 165.109 193.705 149.522 1.00 24.12  ? 2058 MET A N     1 
ATOM   5034  C  CA    . MET A 1 841  ? 164.980 193.948 148.088 1.00 21.31  ? 2058 MET A CA    1 
ATOM   5035  C  C     . MET A 1 841  ? 164.761 192.651 147.322 1.00 22.50  ? 2058 MET A C     1 
ATOM   5036  O  O     . MET A 1 841  ? 163.956 192.609 146.384 1.00 29.63  ? 2058 MET A O     1 
ATOM   5037  C  CB    . MET A 1 841  ? 166.214 194.673 147.556 1.00 23.99  ? 2058 MET A CB    1 
ATOM   5038  C  CG    . MET A 1 841  ? 166.380 196.092 148.057 1.00 27.80  ? 2058 MET A CG    1 
ATOM   5039  S  SD    . MET A 1 841  ? 167.904 196.838 147.449 1.00 56.21  ? 2058 MET A SD    1 
ATOM   5040  C  CE    . MET A 1 841  ? 167.514 197.038 145.713 1.00 49.18  ? 2058 MET A CE    1 
ATOM   5041  N  N     . GLN A 1 842  ? 165.476 191.587 147.698 1.00 17.00  ? 2059 GLN A N     1 
ATOM   5042  C  CA    . GLN A 1 842  ? 165.295 190.300 147.033 1.00 17.07  ? 2059 GLN A CA    1 
ATOM   5043  C  C     . GLN A 1 842  ? 163.874 189.787 147.214 1.00 20.42  ? 2059 GLN A C     1 
ATOM   5044  O  O     . GLN A 1 842  ? 163.231 189.360 146.249 1.00 23.75  ? 2059 GLN A O     1 
ATOM   5045  C  CB    . GLN A 1 842  ? 166.304 189.283 147.566 1.00 17.25  ? 2059 GLN A CB    1 
ATOM   5046  C  CG    . GLN A 1 842  ? 167.716 189.476 147.045 1.00 16.83  ? 2059 GLN A CG    1 
ATOM   5047  C  CD    . GLN A 1 842  ? 168.667 188.406 147.532 1.00 15.47  ? 2059 GLN A CD    1 
ATOM   5048  O  OE1   . GLN A 1 842  ? 168.302 187.560 148.346 1.00 17.14  ? 2059 GLN A OE1   1 
ATOM   5049  N  NE2   . GLN A 1 842  ? 169.898 188.444 147.043 1.00 14.14  ? 2059 GLN A NE2   1 
ATOM   5050  N  N     . PHE A 1 843  ? 163.351 189.860 148.442 1.00 20.67  ? 2060 PHE A N     1 
ATOM   5051  C  CA    . PHE A 1 843  ? 161.996 189.383 148.695 1.00 20.13  ? 2060 PHE A CA    1 
ATOM   5052  C  C     . PHE A 1 843  ? 160.960 190.225 147.964 1.00 22.15  ? 2060 PHE A C     1 
ATOM   5053  O  O     . PHE A 1 843  ? 159.980 189.685 147.447 1.00 27.55  ? 2060 PHE A O     1 
ATOM   5054  C  CB    . PHE A 1 843  ? 161.700 189.365 150.193 1.00 17.25  ? 2060 PHE A CB    1 
ATOM   5055  C  CG    . PHE A 1 843  ? 160.276 189.018 150.518 1.00 14.95  ? 2060 PHE A CG    1 
ATOM   5056  C  CD1   . PHE A 1 843  ? 159.828 187.714 150.424 1.00 15.28  ? 2060 PHE A CD1   1 
ATOM   5057  C  CD2   . PHE A 1 843  ? 159.385 189.995 150.914 1.00 15.48  ? 2060 PHE A CD2   1 
ATOM   5058  C  CE1   . PHE A 1 843  ? 158.516 187.396 150.722 1.00 16.55  ? 2060 PHE A CE1   1 
ATOM   5059  C  CE2   . PHE A 1 843  ? 158.073 189.684 151.210 1.00 14.67  ? 2060 PHE A CE2   1 
ATOM   5060  C  CZ    . PHE A 1 843  ? 157.640 188.384 151.114 1.00 15.84  ? 2060 PHE A CZ    1 
ATOM   5061  N  N     . TYR A 1 844  ? 161.154 191.546 147.906 1.00 20.84  ? 2061 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 844  ? 160.192 192.397 147.209 1.00 20.88  ? 2061 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 844  ? 160.197 192.129 145.706 1.00 27.03  ? 2061 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 844  ? 159.144 191.869 145.105 1.00 29.79  ? 2061 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 844  ? 160.497 193.866 147.495 1.00 19.07  ? 2061 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 844  ? 159.791 194.823 146.567 1.00 23.40  ? 2061 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 844  ? 158.413 194.974 146.616 1.00 25.74  ? 2061 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 844  ? 160.500 195.573 145.642 1.00 29.11  ? 2061 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 844  ? 157.761 195.848 145.770 1.00 28.73  ? 2061 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 844  ? 159.856 196.446 144.789 1.00 30.95  ? 2061 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 844  ? 158.488 196.582 144.861 1.00 32.27  ? 2061 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 844  ? 157.843 197.452 144.014 1.00 38.09  ? 2061 TYR A OH    1 
ATOM   5073  N  N     . TYR A 1 845  ? 161.382 192.154 145.084 1.00 28.38  ? 2062 TYR A N     1 
ATOM   5074  C  CA    . TYR A 1 845  ? 161.488 191.896 143.652 1.00 23.25  ? 2062 TYR A CA    1 
ATOM   5075  C  C     . TYR A 1 845  ? 161.092 190.475 143.290 1.00 22.51  ? 2062 TYR A C     1 
ATOM   5076  O  O     . TYR A 1 845  ? 160.766 190.210 142.129 1.00 24.46  ? 2062 TYR A O     1 
ATOM   5077  C  CB    . TYR A 1 845  ? 162.914 192.156 143.168 1.00 19.66  ? 2062 TYR A CB    1 
ATOM   5078  C  CG    . TYR A 1 845  ? 163.289 193.613 143.081 1.00 22.62  ? 2062 TYR A CG    1 
ATOM   5079  C  CD1   . TYR A 1 845  ? 162.325 194.586 142.873 1.00 26.67  ? 2062 TYR A CD1   1 
ATOM   5080  C  CD2   . TYR A 1 845  ? 164.611 194.014 143.198 1.00 28.34  ? 2062 TYR A CD2   1 
ATOM   5081  C  CE1   . TYR A 1 845  ? 162.666 195.920 142.790 1.00 31.53  ? 2062 TYR A CE1   1 
ATOM   5082  C  CE2   . TYR A 1 845  ? 164.963 195.345 143.116 1.00 34.39  ? 2062 TYR A CE2   1 
ATOM   5083  C  CZ    . TYR A 1 845  ? 163.986 196.294 142.912 1.00 38.19  ? 2062 TYR A CZ    1 
ATOM   5084  O  OH    . TYR A 1 845  ? 164.332 197.623 142.830 1.00 51.17  ? 2062 TYR A OH    1 
ATOM   5085  N  N     . MET A 1 846  ? 161.115 189.558 144.252 1.00 21.98  ? 2063 MET A N     1 
ATOM   5086  C  CA    . MET A 1 846  ? 160.782 188.170 143.988 1.00 24.93  ? 2063 MET A CA    1 
ATOM   5087  C  C     . MET A 1 846  ? 159.305 187.872 144.209 1.00 27.90  ? 2063 MET A C     1 
ATOM   5088  O  O     . MET A 1 846  ? 158.730 187.057 143.480 1.00 33.33  ? 2063 MET A O     1 
ATOM   5089  C  CB    . MET A 1 846  ? 161.670 187.292 144.868 1.00 24.94  ? 2063 MET A CB    1 
ATOM   5090  C  CG    . MET A 1 846  ? 161.227 185.885 145.070 1.00 27.37  ? 2063 MET A CG    1 
ATOM   5091  S  SD    . MET A 1 846  ? 162.605 184.964 145.750 1.00 51.11  ? 2063 MET A SD    1 
ATOM   5092  C  CE    . MET A 1 846  ? 161.818 183.392 145.965 1.00 25.44  ? 2063 MET A CE    1 
ATOM   5093  N  N     . GLN A 1 847  ? 158.668 188.530 145.179 1.00 26.12  ? 2064 GLN A N     1 
ATOM   5094  C  CA    . GLN A 1 847  ? 157.219 188.474 145.312 1.00 25.59  ? 2064 GLN A CA    1 
ATOM   5095  C  C     . GLN A 1 847  ? 156.513 189.318 144.266 1.00 32.97  ? 2064 GLN A C     1 
ATOM   5096  O  O     . GLN A 1 847  ? 155.286 189.222 144.148 1.00 39.62  ? 2064 GLN A O     1 
ATOM   5097  C  CB    . GLN A 1 847  ? 156.785 188.934 146.707 1.00 23.65  ? 2064 GLN A CB    1 
ATOM   5098  C  CG    . GLN A 1 847  ? 156.894 190.434 146.941 1.00 22.11  ? 2064 GLN A CG    1 
ATOM   5099  C  CD    . GLN A 1 847  ? 155.572 191.152 146.779 1.00 24.85  ? 2064 GLN A CD    1 
ATOM   5100  O  OE1   . GLN A 1 847  ? 154.509 190.573 146.995 1.00 30.64  ? 2064 GLN A OE1   1 
ATOM   5101  N  NE2   . GLN A 1 847  ? 155.631 192.419 146.394 1.00 23.85  ? 2064 GLN A NE2   1 
ATOM   5102  N  N     . LYS A 1 848  ? 157.254 190.166 143.543 1.00 32.47  ? 2065 LYS A N     1 
ATOM   5103  C  CA    . LYS A 1 848  ? 156.683 190.877 142.402 1.00 27.97  ? 2065 LYS A CA    1 
ATOM   5104  C  C     . LYS A 1 848  ? 156.048 189.924 141.396 1.00 27.65  ? 2065 LYS A C     1 
ATOM   5105  O  O     . LYS A 1 848  ? 155.009 190.237 140.804 1.00 24.67  ? 2065 LYS A O     1 
ATOM   5106  C  CB    . LYS A 1 848  ? 157.767 191.712 141.720 1.00 25.71  ? 2065 LYS A CB    1 
ATOM   5107  C  CG    . LYS A 1 848  ? 157.239 192.705 140.711 1.00 27.91  ? 2065 LYS A CG    1 
ATOM   5108  C  CD    . LYS A 1 848  ? 156.528 193.849 141.395 1.00 34.11  ? 2065 LYS A CD    1 
ATOM   5109  C  CE    . LYS A 1 848  ? 157.522 194.750 142.097 1.00 32.47  ? 2065 LYS A CE    1 
ATOM   5110  N  NZ    . LYS A 1 848  ? 158.417 195.443 141.131 1.00 34.56  ? 2065 LYS A NZ    1 
ATOM   5111  N  N     . THR A 1 849  ? 156.650 188.754 141.193 1.00 30.64  ? 2066 THR A N     1 
ATOM   5112  C  CA    . THR A 1 849  ? 156.187 187.796 140.194 1.00 35.23  ? 2066 THR A CA    1 
ATOM   5113  C  C     . THR A 1 849  ? 155.587 186.530 140.782 1.00 34.81  ? 2066 THR A C     1 
ATOM   5114  O  O     . THR A 1 849  ? 154.549 186.068 140.303 1.00 38.78  ? 2066 THR A O     1 
ATOM   5115  C  CB    . THR A 1 849  ? 157.341 187.409 139.262 1.00 32.09  ? 2066 THR A CB    1 
ATOM   5116  O  OG1   . THR A 1 849  ? 158.319 186.661 139.995 1.00 33.09  ? 2066 THR A OG1   1 
ATOM   5117  C  CG2   . THR A 1 849  ? 157.996 188.652 138.680 1.00 28.23  ? 2066 THR A CG2   1 
ATOM   5118  N  N     . GLN A 1 850  ? 156.208 185.952 141.806 1.00 34.29  ? 2067 GLN A N     1 
ATOM   5119  C  CA    . GLN A 1 850  ? 155.771 184.676 142.355 1.00 38.87  ? 2067 GLN A CA    1 
ATOM   5120  C  C     . GLN A 1 850  ? 154.700 184.895 143.417 1.00 46.48  ? 2067 GLN A C     1 
ATOM   5121  O  O     . GLN A 1 850  ? 154.819 185.785 144.263 1.00 46.14  ? 2067 GLN A O     1 
ATOM   5122  C  CB    . GLN A 1 850  ? 156.964 183.918 142.942 1.00 38.24  ? 2067 GLN A CB    1 
ATOM   5123  C  CG    . GLN A 1 850  ? 156.604 182.710 143.780 1.00 41.55  ? 2067 GLN A CG    1 
ATOM   5124  C  CD    . GLN A 1 850  ? 155.745 181.712 143.030 1.00 48.35  ? 2067 GLN A CD    1 
ATOM   5125  O  OE1   . GLN A 1 850  ? 154.560 181.554 143.320 1.00 47.30  ? 2067 GLN A OE1   1 
ATOM   5126  N  NE2   . GLN A 1 850  ? 156.341 181.032 142.059 1.00 51.84  ? 2067 GLN A NE2   1 
ATOM   5127  N  N     . GLN A 1 851  ? 153.650 184.074 143.363 1.00 51.66  ? 2068 GLN A N     1 
ATOM   5128  C  CA    . GLN A 1 851  ? 152.488 184.230 144.227 1.00 48.50  ? 2068 GLN A CA    1 
ATOM   5129  C  C     . GLN A 1 851  ? 152.627 183.545 145.581 1.00 43.94  ? 2068 GLN A C     1 
ATOM   5130  O  O     . GLN A 1 851  ? 151.758 183.734 146.436 1.00 43.62  ? 2068 GLN A O     1 
ATOM   5131  C  CB    . GLN A 1 851  ? 151.234 183.695 143.525 1.00 54.50  ? 2068 GLN A CB    1 
ATOM   5132  C  CG    . GLN A 1 851  ? 150.811 184.494 142.306 1.00 55.40  ? 2068 GLN A CG    1 
ATOM   5133  C  CD    . GLN A 1 851  ? 149.809 185.578 142.643 1.00 59.58  ? 2068 GLN A CD    1 
ATOM   5134  O  OE1   . GLN A 1 851  ? 148.688 185.293 143.065 1.00 59.46  ? 2068 GLN A OE1   1 
ATOM   5135  N  NE2   . GLN A 1 851  ? 150.207 186.831 142.457 1.00 62.00  ? 2068 GLN A NE2   1 
ATOM   5136  N  N     . ALA A 1 852  ? 153.674 182.755 145.803 1.00 41.18  ? 2069 ALA A N     1 
ATOM   5137  C  CA    . ALA A 1 852  ? 153.851 182.096 147.095 1.00 38.89  ? 2069 ALA A CA    1 
ATOM   5138  C  C     . ALA A 1 852  ? 155.327 181.836 147.335 1.00 37.47  ? 2069 ALA A C     1 
ATOM   5139  O  O     . ALA A 1 852  ? 155.975 181.156 146.535 1.00 42.02  ? 2069 ALA A O     1 
ATOM   5140  C  CB    . ALA A 1 852  ? 153.063 180.794 147.165 1.00 41.70  ? 2069 ALA A CB    1 
ATOM   5141  N  N     . LEU A 1 853  ? 155.841 182.345 148.448 1.00 29.47  ? 2070 LEU A N     1 
ATOM   5142  C  CA    . LEU A 1 853  ? 157.264 182.334 148.736 1.00 26.36  ? 2070 LEU A CA    1 
ATOM   5143  C  C     . LEU A 1 853  ? 157.564 181.436 149.928 1.00 24.83  ? 2070 LEU A C     1 
ATOM   5144  O  O     . LEU A 1 853  ? 156.713 181.217 150.793 1.00 25.91  ? 2070 LEU A O     1 
ATOM   5145  C  CB    . LEU A 1 853  ? 157.765 183.750 149.022 1.00 23.88  ? 2070 LEU A CB    1 
ATOM   5146  C  CG    . LEU A 1 853  ? 157.483 184.763 147.916 1.00 29.71  ? 2070 LEU A CG    1 
ATOM   5147  C  CD1   . LEU A 1 853  ? 156.298 185.641 148.286 1.00 27.29  ? 2070 LEU A CD1   1 
ATOM   5148  C  CD2   . LEU A 1 853  ? 158.709 185.602 147.650 1.00 27.87  ? 2070 LEU A CD2   1 
ATOM   5149  N  N     . ILE A 1 854  ? 158.785 180.911 149.959 1.00 23.25  ? 2071 ILE A N     1 
ATOM   5150  C  CA    . ILE A 1 854  ? 159.290 180.143 151.089 1.00 18.58  ? 2071 ILE A CA    1 
ATOM   5151  C  C     . ILE A 1 854  ? 160.518 180.863 151.621 1.00 19.11  ? 2071 ILE A C     1 
ATOM   5152  O  O     . ILE A 1 854  ? 161.520 180.998 150.908 1.00 23.68  ? 2071 ILE A O     1 
ATOM   5153  C  CB    . ILE A 1 854  ? 159.633 178.696 150.701 1.00 20.97  ? 2071 ILE A CB    1 
ATOM   5154  C  CG1   . ILE A 1 854  ? 158.494 178.064 149.903 1.00 29.08  ? 2071 ILE A CG1   1 
ATOM   5155  C  CG2   . ILE A 1 854  ? 159.904 177.872 151.941 1.00 23.12  ? 2071 ILE A CG2   1 
ATOM   5156  C  CD1   . ILE A 1 854  ? 158.723 176.606 149.570 1.00 33.93  ? 2071 ILE A CD1   1 
ATOM   5157  N  N     . LEU A 1 855  ? 160.442 181.326 152.863 1.00 16.09  ? 2072 LEU A N     1 
ATOM   5158  C  CA    . LEU A 1 855  ? 161.566 181.965 153.533 1.00 13.84  ? 2072 LEU A CA    1 
ATOM   5159  C  C     . LEU A 1 855  ? 162.196 180.945 154.470 1.00 15.52  ? 2072 LEU A C     1 
ATOM   5160  O  O     . LEU A 1 855  ? 161.545 180.476 155.409 1.00 20.13  ? 2072 LEU A O     1 
ATOM   5161  C  CB    . LEU A 1 855  ? 161.113 183.206 154.303 1.00 9.83   ? 2072 LEU A CB    1 
ATOM   5162  C  CG    . LEU A 1 855  ? 160.816 184.474 153.500 1.00 9.06   ? 2072 LEU A CG    1 
ATOM   5163  C  CD1   . LEU A 1 855  ? 159.381 184.490 153.021 1.00 12.21  ? 2072 LEU A CD1   1 
ATOM   5164  C  CD2   . LEU A 1 855  ? 161.102 185.708 154.328 1.00 10.37  ? 2072 LEU A CD2   1 
ATOM   5165  N  N     . VAL A 1 856  ? 163.453 180.595 154.214 1.00 12.29  ? 2073 VAL A N     1 
ATOM   5166  C  CA    . VAL A 1 856  ? 164.139 179.541 154.949 1.00 13.28  ? 2073 VAL A CA    1 
ATOM   5167  C  C     . VAL A 1 856  ? 165.367 180.138 155.617 1.00 14.38  ? 2073 VAL A C     1 
ATOM   5168  O  O     . VAL A 1 856  ? 166.117 180.892 154.987 1.00 14.59  ? 2073 VAL A O     1 
ATOM   5169  C  CB    . VAL A 1 856  ? 164.534 178.369 154.033 1.00 18.35  ? 2073 VAL A CB    1 
ATOM   5170  C  CG1   . VAL A 1 856  ? 165.099 177.224 154.852 1.00 19.89  ? 2073 VAL A CG1   1 
ATOM   5171  C  CG2   . VAL A 1 856  ? 163.346 177.905 153.223 1.00 24.62  ? 2073 VAL A CG2   1 
ATOM   5172  N  N     . GLY A 1 857  ? 165.565 179.805 156.884 1.00 17.28  ? 2074 GLY A N     1 
ATOM   5173  C  CA    . GLY A 1 857  ? 166.728 180.272 157.611 1.00 16.22  ? 2074 GLY A CA    1 
ATOM   5174  C  C     . GLY A 1 857  ? 166.604 179.893 159.069 1.00 16.17  ? 2074 GLY A C     1 
ATOM   5175  O  O     . GLY A 1 857  ? 165.515 179.578 159.561 1.00 15.00  ? 2074 GLY A O     1 
ATOM   5176  N  N     . LYS A 1 858  ? 167.744 179.941 159.755 1.00 15.31  ? 2075 LYS A N     1 
ATOM   5177  C  CA    . LYS A 1 858  ? 167.802 179.552 161.156 1.00 14.06  ? 2075 LYS A CA    1 
ATOM   5178  C  C     . LYS A 1 858  ? 166.942 180.482 162.006 1.00 14.26  ? 2075 LYS A C     1 
ATOM   5179  O  O     . LYS A 1 858  ? 166.655 181.620 161.631 1.00 16.59  ? 2075 LYS A O     1 
ATOM   5180  C  CB    . LYS A 1 858  ? 169.245 179.567 161.657 1.00 13.20  ? 2075 LYS A CB    1 
ATOM   5181  C  CG    . LYS A 1 858  ? 170.043 180.777 161.205 1.00 14.76  ? 2075 LYS A CG    1 
ATOM   5182  C  CD    . LYS A 1 858  ? 171.390 180.838 161.903 1.00 18.90  ? 2075 LYS A CD    1 
ATOM   5183  C  CE    . LYS A 1 858  ? 172.277 179.676 161.490 1.00 29.14  ? 2075 LYS A CE    1 
ATOM   5184  N  NZ    . LYS A 1 858  ? 173.538 179.631 162.280 1.00 32.65  ? 2075 LYS A NZ    1 
ATOM   5185  N  N     . ALA A 1 859  ? 166.516 179.974 163.159 1.00 10.84  ? 2076 ALA A N     1 
ATOM   5186  C  CA    . ALA A 1 859  ? 165.608 180.727 164.013 1.00 11.09  ? 2076 ALA A CA    1 
ATOM   5187  C  C     . ALA A 1 859  ? 166.300 181.960 164.578 1.00 10.25  ? 2076 ALA A C     1 
ATOM   5188  O  O     . ALA A 1 859  ? 167.380 181.867 165.167 1.00 10.61  ? 2076 ALA A O     1 
ATOM   5189  C  CB    . ALA A 1 859  ? 165.093 179.845 165.143 1.00 11.74  ? 2076 ALA A CB    1 
ATOM   5190  N  N     . GLY A 1 860  ? 165.669 183.116 164.401 1.00 9.22   ? 2077 GLY A N     1 
ATOM   5191  C  CA    . GLY A 1 860  ? 166.240 184.375 164.823 1.00 10.36  ? 2077 GLY A CA    1 
ATOM   5192  C  C     . GLY A 1 860  ? 166.982 185.136 163.750 1.00 10.69  ? 2077 GLY A C     1 
ATOM   5193  O  O     . GLY A 1 860  ? 167.545 186.195 164.047 1.00 10.05  ? 2077 GLY A O     1 
ATOM   5194  N  N     . CYS A 1 861  ? 167.000 184.635 162.514 1.00 10.15  ? 2078 CYS A N     1 
ATOM   5195  C  CA    . CYS A 1 861  ? 167.763 185.274 161.450 1.00 10.29  ? 2078 CYS A CA    1 
ATOM   5196  C  C     . CYS A 1 861  ? 167.088 186.519 160.892 1.00 14.18  ? 2078 CYS A C     1 
ATOM   5197  O  O     . CYS A 1 861  ? 167.782 187.385 160.352 1.00 18.10  ? 2078 CYS A O     1 
ATOM   5198  C  CB    . CYS A 1 861  ? 168.022 184.284 160.317 1.00 10.57  ? 2078 CYS A CB    1 
ATOM   5199  S  SG    . CYS A 1 861  ? 166.550 183.849 159.395 1.00 17.25  ? 2078 CYS A SG    1 
ATOM   5200  N  N     . GLY A 1 862  ? 165.766 186.639 161.004 1.00 12.67  ? 2079 GLY A N     1 
ATOM   5201  C  CA    . GLY A 1 862  ? 165.109 187.847 160.543 1.00 11.23  ? 2079 GLY A CA    1 
ATOM   5202  C  C     . GLY A 1 862  ? 164.095 187.697 159.427 1.00 10.54  ? 2079 GLY A C     1 
ATOM   5203  O  O     . GLY A 1 862  ? 163.965 188.597 158.595 1.00 11.59  ? 2079 GLY A O     1 
ATOM   5204  N  N     . LYS A 1 863  ? 163.371 186.577 159.386 1.00 8.76   ? 2080 LYS A N     1 
ATOM   5205  C  CA    . LYS A 1 863  ? 162.410 186.355 158.308 1.00 8.05   ? 2080 LYS A CA    1 
ATOM   5206  C  C     . LYS A 1 863  ? 161.139 187.177 158.504 1.00 8.60   ? 2080 LYS A C     1 
ATOM   5207  O  O     . LYS A 1 863  ? 160.688 187.869 157.580 1.00 11.25  ? 2080 LYS A O     1 
ATOM   5208  C  CB    . LYS A 1 863  ? 162.072 184.870 158.210 1.00 9.34   ? 2080 LYS A CB    1 
ATOM   5209  C  CG    . LYS A 1 863  ? 163.271 183.980 158.010 1.00 10.99  ? 2080 LYS A CG    1 
ATOM   5210  C  CD    . LYS A 1 863  ? 162.927 182.532 158.271 1.00 10.77  ? 2080 LYS A CD    1 
ATOM   5211  C  CE    . LYS A 1 863  ? 163.324 182.133 159.674 1.00 9.81   ? 2080 LYS A CE    1 
ATOM   5212  N  NZ    . LYS A 1 863  ? 163.075 180.694 159.931 1.00 16.74  ? 2080 LYS A NZ    1 
ATOM   5213  N  N     . THR A 1 864  ? 160.533 187.092 159.693 1.00 8.71   ? 2081 THR A N     1 
ATOM   5214  C  CA    . THR A 1 864  ? 159.295 187.823 159.952 1.00 9.10   ? 2081 THR A CA    1 
ATOM   5215  C  C     . THR A 1 864  ? 159.515 189.324 159.860 1.00 9.19   ? 2081 THR A C     1 
ATOM   5216  O  O     . THR A 1 864  ? 158.676 190.047 159.312 1.00 12.36  ? 2081 THR A O     1 
ATOM   5217  C  CB    . THR A 1 864  ? 158.732 187.459 161.324 1.00 10.15  ? 2081 THR A CB    1 
ATOM   5218  O  OG1   . THR A 1 864  ? 158.730 186.037 161.484 1.00 11.71  ? 2081 THR A OG1   1 
ATOM   5219  C  CG2   . THR A 1 864  ? 157.312 187.973 161.465 1.00 10.50  ? 2081 THR A CG2   1 
ATOM   5220  N  N     . ALA A 1 865  ? 160.644 189.806 160.379 1.00 8.56   ? 2082 ALA A N     1 
ATOM   5221  C  CA    . ALA A 1 865  ? 160.984 191.216 160.236 1.00 9.50   ? 2082 ALA A CA    1 
ATOM   5222  C  C     . ALA A 1 865  ? 161.132 191.596 158.771 1.00 11.04  ? 2082 ALA A C     1 
ATOM   5223  O  O     . ALA A 1 865  ? 160.668 192.662 158.353 1.00 12.30  ? 2082 ALA A O     1 
ATOM   5224  C  CB    . ALA A 1 865  ? 162.267 191.524 161.001 1.00 12.64  ? 2082 ALA A CB    1 
ATOM   5225  N  N     . THR A 1 866  ? 161.747 190.717 157.973 1.00 12.00  ? 2083 THR A N     1 
ATOM   5226  C  CA    . THR A 1 866  ? 161.926 190.985 156.549 1.00 11.31  ? 2083 THR A CA    1 
ATOM   5227  C  C     . THR A 1 866  ? 160.587 191.154 155.844 1.00 11.44  ? 2083 THR A C     1 
ATOM   5228  O  O     . THR A 1 866  ? 160.349 192.169 155.177 1.00 12.99  ? 2083 THR A O     1 
ATOM   5229  C  CB    . THR A 1 866  ? 162.719 189.854 155.895 1.00 10.92  ? 2083 THR A CB    1 
ATOM   5230  O  OG1   . THR A 1 866  ? 164.077 189.890 156.347 1.00 10.80  ? 2083 THR A OG1   1 
ATOM   5231  C  CG2   . THR A 1 866  ? 162.691 189.986 154.384 1.00 12.26  ? 2083 THR A CG2   1 
ATOM   5232  N  N     . TRP A 1 867  ? 159.683 190.182 156.000 1.00 10.57  ? 2084 TRP A N     1 
ATOM   5233  C  CA    . TRP A 1 867  ? 158.458 190.288 155.219 1.00 11.66  ? 2084 TRP A CA    1 
ATOM   5234  C  C     . TRP A 1 867  ? 157.485 191.304 155.804 1.00 14.23  ? 2084 TRP A C     1 
ATOM   5235  O  O     . TRP A 1 867  ? 156.723 191.913 155.046 1.00 18.08  ? 2084 TRP A O     1 
ATOM   5236  C  CB    . TRP A 1 867  ? 157.802 188.915 155.019 1.00 11.18  ? 2084 TRP A CB    1 
ATOM   5237  C  CG    . TRP A 1 867  ? 157.256 188.191 156.207 1.00 10.55  ? 2084 TRP A CG    1 
ATOM   5238  C  CD1   . TRP A 1 867  ? 157.802 187.098 156.805 1.00 11.36  ? 2084 TRP A CD1   1 
ATOM   5239  C  CD2   . TRP A 1 867  ? 156.009 188.431 156.875 1.00 11.83  ? 2084 TRP A CD2   1 
ATOM   5240  N  NE1   . TRP A 1 867  ? 157.002 186.670 157.834 1.00 13.71  ? 2084 TRP A NE1   1 
ATOM   5241  C  CE2   . TRP A 1 867  ? 155.894 187.472 157.897 1.00 13.77  ? 2084 TRP A CE2   1 
ATOM   5242  C  CE3   . TRP A 1 867  ? 154.993 189.376 156.725 1.00 13.30  ? 2084 TRP A CE3   1 
ATOM   5243  C  CZ2   . TRP A 1 867  ? 154.807 187.433 158.764 1.00 15.13  ? 2084 TRP A CZ2   1 
ATOM   5244  C  CZ3   . TRP A 1 867  ? 153.915 189.335 157.586 1.00 15.58  ? 2084 TRP A CZ3   1 
ATOM   5245  C  CH2   . TRP A 1 867  ? 153.831 188.372 158.592 1.00 14.72  ? 2084 TRP A CH2   1 
ATOM   5246  N  N     . LYS A 1 868  ? 157.520 191.556 157.117 1.00 12.99  ? 2085 LYS A N     1 
ATOM   5247  C  CA    . LYS A 1 868  ? 156.703 192.634 157.665 1.00 11.72  ? 2085 LYS A CA    1 
ATOM   5248  C  C     . LYS A 1 868  ? 157.191 193.995 157.186 1.00 13.77  ? 2085 LYS A C     1 
ATOM   5249  O  O     . LYS A 1 868  ? 156.377 194.865 156.851 1.00 20.59  ? 2085 LYS A O     1 
ATOM   5250  C  CB    . LYS A 1 868  ? 156.693 192.572 159.190 1.00 11.98  ? 2085 LYS A CB    1 
ATOM   5251  C  CG    . LYS A 1 868  ? 155.739 191.534 159.755 1.00 15.06  ? 2085 LYS A CG    1 
ATOM   5252  C  CD    . LYS A 1 868  ? 155.641 191.630 161.267 1.00 17.62  ? 2085 LYS A CD    1 
ATOM   5253  C  CE    . LYS A 1 868  ? 154.676 190.595 161.817 1.00 25.16  ? 2085 LYS A CE    1 
ATOM   5254  N  NZ    . LYS A 1 868  ? 153.284 190.834 161.348 1.00 25.56  ? 2085 LYS A NZ    1 
ATOM   5255  N  N     . THR A 1 869  ? 158.512 194.195 157.128 1.00 12.12  ? 2086 THR A N     1 
ATOM   5256  C  CA    . THR A 1 869  ? 159.050 195.442 156.598 1.00 14.30  ? 2086 THR A CA    1 
ATOM   5257  C  C     . THR A 1 869  ? 158.688 195.616 155.131 1.00 14.80  ? 2086 THR A C     1 
ATOM   5258  O  O     . THR A 1 869  ? 158.311 196.713 154.704 1.00 18.72  ? 2086 THR A O     1 
ATOM   5259  C  CB    . THR A 1 869  ? 160.567 195.477 156.778 1.00 16.62  ? 2086 THR A CB    1 
ATOM   5260  O  OG1   . THR A 1 869  ? 160.890 195.260 158.155 1.00 19.08  ? 2086 THR A OG1   1 
ATOM   5261  C  CG2   . THR A 1 869  ? 161.127 196.819 156.345 1.00 18.17  ? 2086 THR A CG2   1 
ATOM   5262  N  N     . VAL A 1 870  ? 158.783 194.538 154.347 1.00 14.12  ? 2087 VAL A N     1 
ATOM   5263  C  CA    . VAL A 1 870  ? 158.458 194.628 152.926 1.00 15.80  ? 2087 VAL A CA    1 
ATOM   5264  C  C     . VAL A 1 870  ? 156.979 194.944 152.726 1.00 20.48  ? 2087 VAL A C     1 
ATOM   5265  O  O     . VAL A 1 870  ? 156.621 195.776 151.886 1.00 25.66  ? 2087 VAL A O     1 
ATOM   5266  C  CB    . VAL A 1 870  ? 158.870 193.337 152.198 1.00 14.39  ? 2087 VAL A CB    1 
ATOM   5267  C  CG1   . VAL A 1 870  ? 158.269 193.300 150.806 1.00 16.34  ? 2087 VAL A CG1   1 
ATOM   5268  C  CG2   . VAL A 1 870  ? 160.381 193.245 152.118 1.00 16.93  ? 2087 VAL A CG2   1 
ATOM   5269  N  N     . ILE A 1 871  ? 156.098 194.296 153.495 1.00 18.73  ? 2088 ILE A N     1 
ATOM   5270  C  CA    . ILE A 1 871  ? 154.666 194.557 153.366 1.00 18.65  ? 2088 ILE A CA    1 
ATOM   5271  C  C     . ILE A 1 871  ? 154.324 195.987 153.782 1.00 21.32  ? 2088 ILE A C     1 
ATOM   5272  O  O     . ILE A 1 871  ? 153.533 196.665 153.112 1.00 26.90  ? 2088 ILE A O     1 
ATOM   5273  C  CB    . ILE A 1 871  ? 153.862 193.511 154.159 1.00 17.75  ? 2088 ILE A CB    1 
ATOM   5274  C  CG1   . ILE A 1 871  ? 153.890 192.170 153.431 1.00 20.82  ? 2088 ILE A CG1   1 
ATOM   5275  C  CG2   . ILE A 1 871  ? 152.441 193.960 154.394 1.00 24.37  ? 2088 ILE A CG2   1 
ATOM   5276  C  CD1   . ILE A 1 871  ? 153.227 191.059 154.193 1.00 21.42  ? 2088 ILE A CD1   1 
ATOM   5277  N  N     . ASP A 1 872  ? 154.919 196.477 154.874 1.00 19.03  ? 2089 ASP A N     1 
ATOM   5278  C  CA    . ASP A 1 872  ? 154.676 197.859 155.282 1.00 21.82  ? 2089 ASP A CA    1 
ATOM   5279  C  C     . ASP A 1 872  ? 155.166 198.842 154.225 1.00 26.54  ? 2089 ASP A C     1 
ATOM   5280  O  O     . ASP A 1 872  ? 154.476 199.819 153.903 1.00 32.76  ? 2089 ASP A O     1 
ATOM   5281  C  CB    . ASP A 1 872  ? 155.350 198.138 156.625 1.00 27.61  ? 2089 ASP A CB    1 
ATOM   5282  C  CG    . ASP A 1 872  ? 154.550 197.611 157.801 1.00 32.14  ? 2089 ASP A CG    1 
ATOM   5283  O  OD1   . ASP A 1 872  ? 153.364 197.271 157.612 1.00 33.10  ? 2089 ASP A OD1   1 
ATOM   5284  O  OD2   . ASP A 1 872  ? 155.107 197.542 158.916 1.00 30.85  ? 2089 ASP A OD2   1 
ATOM   5285  N  N     . ALA A 1 873  ? 156.348 198.588 153.657 1.00 25.35  ? 2090 ALA A N     1 
ATOM   5286  C  CA    . ALA A 1 873  ? 156.881 199.474 152.630 1.00 25.90  ? 2090 ALA A CA    1 
ATOM   5287  C  C     . ALA A 1 873  ? 156.038 199.432 151.365 1.00 26.43  ? 2090 ALA A C     1 
ATOM   5288  O  O     . ALA A 1 873  ? 155.852 200.457 150.708 1.00 31.27  ? 2090 ALA A O     1 
ATOM   5289  C  CB    . ALA A 1 873  ? 158.326 199.106 152.317 1.00 27.83  ? 2090 ALA A CB    1 
ATOM   5290  N  N     . MET A 1 874  ? 155.522 198.259 151.001 1.00 25.69  ? 2091 MET A N     1 
ATOM   5291  C  CA    . MET A 1 874  ? 154.671 198.173 149.821 1.00 28.06  ? 2091 MET A CA    1 
ATOM   5292  C  C     . MET A 1 874  ? 153.351 198.898 150.043 1.00 33.42  ? 2091 MET A C     1 
ATOM   5293  O  O     . MET A 1 874  ? 152.825 199.533 149.122 1.00 36.51  ? 2091 MET A O     1 
ATOM   5294  C  CB    . MET A 1 874  ? 154.431 196.714 149.446 1.00 23.27  ? 2091 MET A CB    1 
ATOM   5295  C  CG    . MET A 1 874  ? 155.586 196.081 148.692 1.00 21.50  ? 2091 MET A CG    1 
ATOM   5296  S  SD    . MET A 1 874  ? 155.375 194.310 148.442 1.00 28.35  ? 2091 MET A SD    1 
ATOM   5297  C  CE    . MET A 1 874  ? 153.593 194.186 148.438 1.00 30.86  ? 2091 MET A CE    1 
ATOM   5298  N  N     . ALA A 1 875  ? 152.805 198.819 151.261 1.00 33.54  ? 2092 ALA A N     1 
ATOM   5299  C  CA    . ALA A 1 875  ? 151.596 199.573 151.582 1.00 32.40  ? 2092 ALA A CA    1 
ATOM   5300  C  C     . ALA A 1 875  ? 151.840 201.074 151.494 1.00 33.51  ? 2092 ALA A C     1 
ATOM   5301  O  O     . ALA A 1 875  ? 150.994 201.818 150.984 1.00 37.05  ? 2092 ALA A O     1 
ATOM   5302  C  CB    . ALA A 1 875  ? 151.092 199.199 152.974 1.00 33.60  ? 2092 ALA A CB    1 
ATOM   5303  N  N     . ILE A 1 876  ? 152.986 201.540 151.995 1.00 33.00  ? 2093 ILE A N     1 
ATOM   5304  C  CA    . ILE A 1 876  ? 153.289 202.968 151.930 1.00 33.98  ? 2093 ILE A CA    1 
ATOM   5305  C  C     . ILE A 1 876  ? 153.551 203.402 150.489 1.00 35.77  ? 2093 ILE A C     1 
ATOM   5306  O  O     . ILE A 1 876  ? 153.136 204.489 150.068 1.00 38.95  ? 2093 ILE A O     1 
ATOM   5307  C  CB    . ILE A 1 876  ? 154.474 203.304 152.856 1.00 33.81  ? 2093 ILE A CB    1 
ATOM   5308  C  CG1   . ILE A 1 876  ? 154.121 202.998 154.311 1.00 32.47  ? 2093 ILE A CG1   1 
ATOM   5309  C  CG2   . ILE A 1 876  ? 154.869 204.768 152.730 1.00 35.02  ? 2093 ILE A CG2   1 
ATOM   5310  C  CD1   . ILE A 1 876  ? 155.329 202.750 155.187 1.00 35.49  ? 2093 ILE A CD1   1 
ATOM   5311  N  N     . PHE A 1 877  ? 154.215 202.554 149.702 1.00 33.80  ? 2094 PHE A N     1 
ATOM   5312  C  CA    . PHE A 1 877  ? 154.668 202.940 148.370 1.00 35.59  ? 2094 PHE A CA    1 
ATOM   5313  C  C     . PHE A 1 877  ? 153.541 202.865 147.345 1.00 41.81  ? 2094 PHE A C     1 
ATOM   5314  O  O     . PHE A 1 877  ? 153.204 203.868 146.706 1.00 44.96  ? 2094 PHE A O     1 
ATOM   5315  C  CB    . PHE A 1 877  ? 155.846 202.050 147.955 1.00 36.40  ? 2094 PHE A CB    1 
ATOM   5316  C  CG    . PHE A 1 877  ? 156.131 202.053 146.480 1.00 38.50  ? 2094 PHE A CG    1 
ATOM   5317  C  CD1   . PHE A 1 877  ? 156.714 203.153 145.875 1.00 41.81  ? 2094 PHE A CD1   1 
ATOM   5318  C  CD2   . PHE A 1 877  ? 155.843 200.942 145.703 1.00 36.07  ? 2094 PHE A CD2   1 
ATOM   5319  C  CE1   . PHE A 1 877  ? 156.986 203.153 144.521 1.00 46.40  ? 2094 PHE A CE1   1 
ATOM   5320  C  CE2   . PHE A 1 877  ? 156.115 200.936 144.350 1.00 37.88  ? 2094 PHE A CE2   1 
ATOM   5321  C  CZ    . PHE A 1 877  ? 156.686 202.042 143.758 1.00 45.79  ? 2094 PHE A CZ    1 
ATOM   5322  N  N     . ASP A 1 878  ? 152.959 201.677 147.164 1.00 40.90  ? 2095 ASP A N     1 
ATOM   5323  C  CA    . ASP A 1 878  ? 151.889 201.514 146.184 1.00 40.79  ? 2095 ASP A CA    1 
ATOM   5324  C  C     . ASP A 1 878  ? 150.643 202.292 146.583 1.00 43.14  ? 2095 ASP A C     1 
ATOM   5325  O  O     . ASP A 1 878  ? 149.959 202.863 145.725 1.00 45.65  ? 2095 ASP A O     1 
ATOM   5326  C  CB    . ASP A 1 878  ? 151.561 200.032 146.009 1.00 39.50  ? 2095 ASP A CB    1 
ATOM   5327  C  CG    . ASP A 1 878  ? 152.617 199.292 145.215 1.00 40.30  ? 2095 ASP A CG    1 
ATOM   5328  O  OD1   . ASP A 1 878  ? 153.157 199.879 144.257 1.00 48.21  ? 2095 ASP A OD1   1 
ATOM   5329  O  OD2   . ASP A 1 878  ? 152.911 198.127 145.550 1.00 36.01  ? 2095 ASP A OD2   1 
ATOM   5330  N  N     . GLY A 1 879  ? 150.333 202.329 147.876 1.00 43.97  ? 2096 GLY A N     1 
ATOM   5331  C  CA    . GLY A 1 879  ? 149.134 202.956 148.377 1.00 47.60  ? 2096 GLY A CA    1 
ATOM   5332  C  C     . GLY A 1 879  ? 148.027 201.987 148.731 1.00 49.16  ? 2096 GLY A C     1 
ATOM   5333  O  O     . GLY A 1 879  ? 147.082 202.375 149.428 1.00 50.90  ? 2096 GLY A O     1 
ATOM   5334  N  N     . HIS A 1 880  ? 148.116 200.744 148.265 1.00 47.36  ? 2097 HIS A N     1 
ATOM   5335  C  CA    . HIS A 1 880  ? 147.154 199.725 148.652 1.00 50.49  ? 2097 HIS A CA    1 
ATOM   5336  C  C     . HIS A 1 880  ? 147.316 199.373 150.124 1.00 53.49  ? 2097 HIS A C     1 
ATOM   5337  O  O     . HIS A 1 880  ? 148.434 199.278 150.636 1.00 52.49  ? 2097 HIS A O     1 
ATOM   5338  C  CB    . HIS A 1 880  ? 147.335 198.469 147.802 1.00 51.56  ? 2097 HIS A CB    1 
ATOM   5339  C  CG    . HIS A 1 880  ? 146.556 198.481 146.525 1.00 59.80  ? 2097 HIS A CG    1 
ATOM   5340  N  ND1   . HIS A 1 880  ? 145.974 197.347 146.001 1.00 65.11  ? 2097 HIS A ND1   1 
ATOM   5341  C  CD2   . HIS A 1 880  ? 146.261 199.487 145.669 1.00 60.40  ? 2097 HIS A CD2   1 
ATOM   5342  C  CE1   . HIS A 1 880  ? 145.355 197.654 144.875 1.00 65.80  ? 2097 HIS A CE1   1 
ATOM   5343  N  NE2   . HIS A 1 880  ? 145.513 198.946 144.651 1.00 61.94  ? 2097 HIS A NE2   1 
ATOM   5344  N  N     . ALA A 1 881  ? 146.193 199.187 150.808 1.00 53.44  ? 2098 ALA A N     1 
ATOM   5345  C  CA    . ALA A 1 881  ? 146.238 198.678 152.168 1.00 53.46  ? 2098 ALA A CA    1 
ATOM   5346  C  C     . ALA A 1 881  ? 146.650 197.212 152.158 1.00 51.47  ? 2098 ALA A C     1 
ATOM   5347  O  O     . ALA A 1 881  ? 146.480 196.502 151.164 1.00 51.39  ? 2098 ALA A O     1 
ATOM   5348  C  CB    . ALA A 1 881  ? 144.881 198.840 152.851 1.00 57.61  ? 2098 ALA A CB    1 
ATOM   5349  N  N     . ASN A 1 882  ? 147.209 196.761 153.276 1.00 50.19  ? 2099 ASN A N     1 
ATOM   5350  C  CA    . ASN A 1 882  ? 147.695 195.395 153.394 1.00 45.91  ? 2099 ASN A CA    1 
ATOM   5351  C  C     . ASN A 1 882  ? 147.076 194.742 154.617 1.00 44.19  ? 2099 ASN A C     1 
ATOM   5352  O  O     . ASN A 1 882  ? 147.127 195.300 155.717 1.00 43.78  ? 2099 ASN A O     1 
ATOM   5353  C  CB    . ASN A 1 882  ? 149.220 195.359 153.487 1.00 39.69  ? 2099 ASN A CB    1 
ATOM   5354  C  CG    . ASN A 1 882  ? 149.883 195.497 152.137 1.00 40.59  ? 2099 ASN A CG    1 
ATOM   5355  O  OD1   . ASN A 1 882  ? 149.303 195.147 151.112 1.00 43.98  ? 2099 ASN A OD1   1 
ATOM   5356  N  ND2   . ASN A 1 882  ? 151.105 196.007 152.125 1.00 38.95  ? 2099 ASN A ND2   1 
ATOM   5357  N  N     . VAL A 1 883  ? 146.499 193.562 154.421 1.00 41.30  ? 2100 VAL A N     1 
ATOM   5358  C  CA    . VAL A 1 883  ? 145.912 192.781 155.500 1.00 42.08  ? 2100 VAL A CA    1 
ATOM   5359  C  C     . VAL A 1 883  ? 146.688 191.477 155.599 1.00 39.16  ? 2100 VAL A C     1 
ATOM   5360  O  O     . VAL A 1 883  ? 146.840 190.762 154.602 1.00 36.90  ? 2100 VAL A O     1 
ATOM   5361  C  CB    . VAL A 1 883  ? 144.414 192.521 155.262 1.00 41.46  ? 2100 VAL A CB    1 
ATOM   5362  C  CG1   . VAL A 1 883  ? 143.795 191.820 156.460 1.00 41.30  ? 2100 VAL A CG1   1 
ATOM   5363  C  CG2   . VAL A 1 883  ? 143.692 193.819 154.946 1.00 44.73  ? 2100 VAL A CG2   1 
ATOM   5364  N  N     . VAL A 1 884  ? 147.193 191.180 156.794 1.00 37.80  ? 2101 VAL A N     1 
ATOM   5365  C  CA    . VAL A 1 884  ? 148.090 190.055 157.015 1.00 31.58  ? 2101 VAL A CA    1 
ATOM   5366  C  C     . VAL A 1 884  ? 147.422 189.055 157.946 1.00 29.13  ? 2101 VAL A C     1 
ATOM   5367  O  O     . VAL A 1 884  ? 146.624 189.419 158.815 1.00 36.24  ? 2101 VAL A O     1 
ATOM   5368  C  CB    . VAL A 1 884  ? 149.447 190.513 157.592 1.00 32.66  ? 2101 VAL A CB    1 
ATOM   5369  C  CG1   . VAL A 1 884  ? 150.237 191.272 156.544 1.00 32.15  ? 2101 VAL A CG1   1 
ATOM   5370  C  CG2   . VAL A 1 884  ? 149.232 191.383 158.818 1.00 35.42  ? 2101 VAL A CG2   1 
ATOM   5371  N  N     . TYR A 1 885  ? 147.746 187.781 157.747 1.00 23.21  ? 2102 TYR A N     1 
ATOM   5372  C  CA    . TYR A 1 885  ? 147.253 186.711 158.602 1.00 27.26  ? 2102 TYR A CA    1 
ATOM   5373  C  C     . TYR A 1 885  ? 148.365 185.698 158.816 1.00 27.85  ? 2102 TYR A C     1 
ATOM   5374  O  O     . TYR A 1 885  ? 149.018 185.278 157.857 1.00 27.83  ? 2102 TYR A O     1 
ATOM   5375  C  CB    . TYR A 1 885  ? 146.018 186.039 157.991 1.00 27.14  ? 2102 TYR A CB    1 
ATOM   5376  C  CG    . TYR A 1 885  ? 144.773 186.888 158.092 1.00 34.07  ? 2102 TYR A CG    1 
ATOM   5377  C  CD1   . TYR A 1 885  ? 144.215 187.187 159.328 1.00 38.36  ? 2102 TYR A CD1   1 
ATOM   5378  C  CD2   . TYR A 1 885  ? 144.167 187.408 156.956 1.00 35.85  ? 2102 TYR A CD2   1 
ATOM   5379  C  CE1   . TYR A 1 885  ? 143.081 187.969 159.431 1.00 40.13  ? 2102 TYR A CE1   1 
ATOM   5380  C  CE2   . TYR A 1 885  ? 143.034 188.194 157.049 1.00 39.82  ? 2102 TYR A CE2   1 
ATOM   5381  C  CZ    . TYR A 1 885  ? 142.495 188.470 158.288 1.00 41.80  ? 2102 TYR A CZ    1 
ATOM   5382  O  OH    . TYR A 1 885  ? 141.367 189.250 158.387 1.00 44.75  ? 2102 TYR A OH    1 
ATOM   5383  N  N     . VAL A 1 886  ? 148.576 185.312 160.070 1.00 24.89  ? 2103 VAL A N     1 
ATOM   5384  C  CA    . VAL A 1 886  ? 149.636 184.387 160.448 1.00 20.07  ? 2103 VAL A CA    1 
ATOM   5385  C  C     . VAL A 1 886  ? 148.981 183.104 160.936 1.00 22.06  ? 2103 VAL A C     1 
ATOM   5386  O  O     . VAL A 1 886  ? 148.154 183.132 161.856 1.00 29.17  ? 2103 VAL A O     1 
ATOM   5387  C  CB    . VAL A 1 886  ? 150.550 184.987 161.526 1.00 20.81  ? 2103 VAL A CB    1 
ATOM   5388  C  CG1   . VAL A 1 886  ? 151.727 184.074 161.782 1.00 25.00  ? 2103 VAL A CG1   1 
ATOM   5389  C  CG2   . VAL A 1 886  ? 151.020 186.371 161.109 1.00 19.06  ? 2103 VAL A CG2   1 
ATOM   5390  N  N     . ILE A 1 887  ? 149.343 181.982 160.320 1.00 19.31  ? 2104 ILE A N     1 
ATOM   5391  C  CA    . ILE A 1 887  ? 148.731 180.688 160.604 1.00 21.86  ? 2104 ILE A CA    1 
ATOM   5392  C  C     . ILE A 1 887  ? 149.851 179.671 160.766 1.00 24.85  ? 2104 ILE A C     1 
ATOM   5393  O  O     . ILE A 1 887  ? 150.477 179.272 159.777 1.00 28.91  ? 2104 ILE A O     1 
ATOM   5394  C  CB    . ILE A 1 887  ? 147.754 180.244 159.502 1.00 24.38  ? 2104 ILE A CB    1 
ATOM   5395  C  CG1   . ILE A 1 887  ? 146.545 181.182 159.410 1.00 28.58  ? 2104 ILE A CG1   1 
ATOM   5396  C  CG2   . ILE A 1 887  ? 147.285 178.817 159.743 1.00 29.45  ? 2104 ILE A CG2   1 
ATOM   5397  C  CD1   . ILE A 1 887  ? 146.692 182.314 158.408 1.00 26.59  ? 2104 ILE A CD1   1 
ATOM   5398  N  N     . ASP A 1 888  ? 150.108 179.250 162.001 1.00 26.15  ? 2105 ASP A N     1 
ATOM   5399  C  CA    . ASP A 1 888  ? 151.056 178.167 162.222 1.00 28.34  ? 2105 ASP A CA    1 
ATOM   5400  C  C     . ASP A 1 888  ? 150.448 176.855 161.741 1.00 28.88  ? 2105 ASP A C     1 
ATOM   5401  O  O     . ASP A 1 888  ? 149.330 176.498 162.125 1.00 32.78  ? 2105 ASP A O     1 
ATOM   5402  C  CB    . ASP A 1 888  ? 151.436 178.079 163.698 1.00 30.12  ? 2105 ASP A CB    1 
ATOM   5403  C  CG    . ASP A 1 888  ? 152.311 179.232 164.146 1.00 27.00  ? 2105 ASP A CG    1 
ATOM   5404  O  OD1   . ASP A 1 888  ? 152.338 180.266 163.447 1.00 24.09  ? 2105 ASP A OD1   1 
ATOM   5405  O  OD2   . ASP A 1 888  ? 152.972 179.102 165.198 1.00 23.91  ? 2105 ASP A OD2   1 
ATOM   5406  N  N     . THR A 1 889  ? 151.184 176.144 160.888 1.00 28.56  ? 2106 THR A N     1 
ATOM   5407  C  CA    . THR A 1 889  ? 150.625 174.985 160.199 1.00 35.17  ? 2106 THR A CA    1 
ATOM   5408  C  C     . THR A 1 889  ? 150.408 173.810 161.147 1.00 45.29  ? 2106 THR A C     1 
ATOM   5409  O  O     . THR A 1 889  ? 149.326 173.213 161.172 1.00 53.93  ? 2106 THR A O     1 
ATOM   5410  C  CB    . THR A 1 889  ? 151.541 174.576 159.045 1.00 34.94  ? 2106 THR A CB    1 
ATOM   5411  O  OG1   . THR A 1 889  ? 151.776 175.706 158.196 1.00 33.52  ? 2106 THR A OG1   1 
ATOM   5412  C  CG2   . THR A 1 889  ? 150.909 173.465 158.229 1.00 38.42  ? 2106 THR A CG2   1 
ATOM   5413  N  N     . LYS A 1 890  ? 151.423 173.468 161.943 1.00 40.99  ? 2107 LYS A N     1 
ATOM   5414  C  CA    . LYS A 1 890  ? 151.412 172.198 162.660 1.00 41.23  ? 2107 LYS A CA    1 
ATOM   5415  C  C     . LYS A 1 890  ? 150.547 172.206 163.914 1.00 41.80  ? 2107 LYS A C     1 
ATOM   5416  O  O     . LYS A 1 890  ? 150.192 171.129 164.403 1.00 43.41  ? 2107 LYS A O     1 
ATOM   5417  C  CB    . LYS A 1 890  ? 152.840 171.793 163.028 1.00 40.40  ? 2107 LYS A CB    1 
ATOM   5418  C  CG    . LYS A 1 890  ? 153.744 171.611 161.826 1.00 41.86  ? 2107 LYS A CG    1 
ATOM   5419  C  CD    . LYS A 1 890  ? 153.149 170.605 160.860 1.00 52.67  ? 2107 LYS A CD    1 
ATOM   5420  C  CE    . LYS A 1 890  ? 153.265 169.190 161.392 1.00 55.84  ? 2107 LYS A CE    1 
ATOM   5421  N  NZ    . LYS A 1 890  ? 154.655 168.677 161.292 1.00 55.91  ? 2107 LYS A NZ    1 
ATOM   5422  N  N     . VAL A 1 891  ? 150.207 173.379 164.452 1.00 36.65  ? 2108 VAL A N     1 
ATOM   5423  C  CA    . VAL A 1 891  ? 149.383 173.414 165.657 1.00 35.55  ? 2108 VAL A CA    1 
ATOM   5424  C  C     . VAL A 1 891  ? 147.951 172.985 165.345 1.00 43.89  ? 2108 VAL A C     1 
ATOM   5425  O  O     . VAL A 1 891  ? 147.322 172.266 166.131 1.00 46.47  ? 2108 VAL A O     1 
ATOM   5426  C  CB    . VAL A 1 891  ? 149.455 174.805 166.318 1.00 29.73  ? 2108 VAL A CB    1 
ATOM   5427  C  CG1   . VAL A 1 891  ? 149.094 175.901 165.344 1.00 33.36  ? 2108 VAL A CG1   1 
ATOM   5428  C  CG2   . VAL A 1 891  ? 148.555 174.866 167.534 1.00 30.24  ? 2108 VAL A CG2   1 
ATOM   5429  N  N     . LEU A 1 892  ? 147.423 173.385 164.190 1.00 47.08  ? 2109 LEU A N     1 
ATOM   5430  C  CA    . LEU A 1 892  ? 146.096 172.964 163.767 1.00 48.54  ? 2109 LEU A CA    1 
ATOM   5431  C  C     . LEU A 1 892  ? 146.184 171.695 162.931 1.00 55.88  ? 2109 LEU A C     1 
ATOM   5432  O  O     . LEU A 1 892  ? 147.039 171.574 162.050 1.00 57.21  ? 2109 LEU A O     1 
ATOM   5433  C  CB    . LEU A 1 892  ? 145.390 174.057 162.960 1.00 44.25  ? 2109 LEU A CB    1 
ATOM   5434  C  CG    . LEU A 1 892  ? 144.676 175.209 163.674 1.00 47.04  ? 2109 LEU A CG    1 
ATOM   5435  C  CD1   . LEU A 1 892  ? 145.643 176.213 164.264 1.00 47.82  ? 2109 LEU A CD1   1 
ATOM   5436  C  CD2   . LEU A 1 892  ? 143.711 175.896 162.724 1.00 60.33  ? 2109 LEU A CD2   1 
ATOM   5437  N  N     . THR A 1 893  ? 145.295 170.750 163.217 1.00 57.52  ? 2110 THR A N     1 
ATOM   5438  C  CA    . THR A 1 893  ? 145.179 169.564 162.385 1.00 63.23  ? 2110 THR A CA    1 
ATOM   5439  C  C     . THR A 1 893  ? 144.505 169.916 161.061 1.00 67.57  ? 2110 THR A C     1 
ATOM   5440  O  O     . THR A 1 893  ? 143.916 170.988 160.898 1.00 67.17  ? 2110 THR A O     1 
ATOM   5441  C  CB    . THR A 1 893  ? 144.391 168.472 163.107 1.00 64.04  ? 2110 THR A CB    1 
ATOM   5442  O  OG1   . THR A 1 893  ? 144.345 167.295 162.291 1.00 64.37  ? 2110 THR A OG1   1 
ATOM   5443  C  CG2   . THR A 1 893  ? 142.973 168.940 163.399 1.00 64.58  ? 2110 THR A CG2   1 
ATOM   5444  N  N     . LYS A 1 894  ? 144.604 168.992 160.102 1.00 66.88  ? 2111 LYS A N     1 
ATOM   5445  C  CA    . LYS A 1 894  ? 144.075 169.262 158.769 1.00 68.09  ? 2111 LYS A CA    1 
ATOM   5446  C  C     . LYS A 1 894  ? 142.555 169.341 158.763 1.00 68.86  ? 2111 LYS A C     1 
ATOM   5447  O  O     . LYS A 1 894  ? 141.982 170.078 157.953 1.00 72.37  ? 2111 LYS A O     1 
ATOM   5448  C  CB    . LYS A 1 894  ? 144.554 168.200 157.783 1.00 70.89  ? 2111 LYS A CB    1 
ATOM   5449  C  CG    . LYS A 1 894  ? 146.012 168.342 157.417 1.00 71.96  ? 2111 LYS A CG    1 
ATOM   5450  C  CD    . LYS A 1 894  ? 146.407 167.364 156.338 1.00 76.65  ? 2111 LYS A CD    1 
ATOM   5451  C  CE    . LYS A 1 894  ? 145.842 167.751 154.986 1.00 84.49  ? 2111 LYS A CE    1 
ATOM   5452  N  NZ    . LYS A 1 894  ? 146.402 166.908 153.894 1.00 84.85  ? 2111 LYS A NZ    1 
ATOM   5453  N  N     . GLU A 1 895  ? 141.889 168.592 159.645 1.00 68.02  ? 2112 GLU A N     1 
ATOM   5454  C  CA    . GLU A 1 895  ? 140.442 168.725 159.777 1.00 69.98  ? 2112 GLU A CA    1 
ATOM   5455  C  C     . GLU A 1 895  ? 140.064 170.119 160.261 1.00 67.69  ? 2112 GLU A C     1 
ATOM   5456  O  O     . GLU A 1 895  ? 139.059 170.689 159.821 1.00 69.02  ? 2112 GLU A O     1 
ATOM   5457  C  CB    . GLU A 1 895  ? 139.901 167.657 160.726 1.00 67.58  ? 2112 GLU A CB    1 
ATOM   5458  N  N     . SER A 1 896  ? 140.858 170.683 161.172 1.00 64.23  ? 2113 SER A N     1 
ATOM   5459  C  CA    . SER A 1 896  ? 140.630 172.053 161.613 1.00 63.38  ? 2113 SER A CA    1 
ATOM   5460  C  C     . SER A 1 896  ? 141.107 173.070 160.585 1.00 62.21  ? 2113 SER A C     1 
ATOM   5461  O  O     . SER A 1 896  ? 140.560 174.176 160.516 1.00 63.36  ? 2113 SER A O     1 
ATOM   5462  C  CB    . SER A 1 896  ? 141.328 172.297 162.951 1.00 66.43  ? 2113 SER A CB    1 
ATOM   5463  O  OG    . SER A 1 896  ? 141.017 173.581 163.461 1.00 69.16  ? 2113 SER A OG    1 
ATOM   5464  N  N     . LEU A 1 897  ? 142.126 172.728 159.795 1.00 61.46  ? 2114 LEU A N     1 
ATOM   5465  C  CA    . LEU A 1 897  ? 142.663 173.676 158.824 1.00 64.97  ? 2114 LEU A CA    1 
ATOM   5466  C  C     . LEU A 1 897  ? 141.749 173.836 157.614 1.00 69.78  ? 2114 LEU A C     1 
ATOM   5467  O  O     . LEU A 1 897  ? 141.519 174.960 157.154 1.00 68.08  ? 2114 LEU A O     1 
ATOM   5468  C  CB    . LEU A 1 897  ? 144.060 173.237 158.382 1.00 64.68  ? 2114 LEU A CB    1 
ATOM   5469  C  CG    . LEU A 1 897  ? 144.939 174.300 157.716 1.00 63.42  ? 2114 LEU A CG    1 
ATOM   5470  C  CD1   . LEU A 1 897  ? 144.896 175.610 158.487 1.00 53.57  ? 2114 LEU A CD1   1 
ATOM   5471  C  CD2   . LEU A 1 897  ? 146.370 173.803 157.586 1.00 60.54  ? 2114 LEU A CD2   1 
ATOM   5472  N  N     . TYR A 1 898  ? 141.214 172.734 157.091 1.00 73.90  ? 2115 TYR A N     1 
ATOM   5473  C  CA    . TYR A 1 898  ? 140.423 172.747 155.867 1.00 72.55  ? 2115 TYR A CA    1 
ATOM   5474  C  C     . TYR A 1 898  ? 138.950 172.450 156.102 1.00 73.81  ? 2115 TYR A C     1 
ATOM   5475  O  O     . TYR A 1 898  ? 138.088 173.221 155.674 1.00 76.05  ? 2115 TYR A O     1 
ATOM   5476  C  CB    . TYR A 1 898  ? 140.999 171.739 154.863 1.00 72.90  ? 2115 TYR A CB    1 
ATOM   5477  C  CG    . TYR A 1 898  ? 142.470 171.931 154.580 1.00 71.74  ? 2115 TYR A CG    1 
ATOM   5478  C  CD1   . TYR A 1 898  ? 142.944 173.115 154.030 1.00 71.79  ? 2115 TYR A CD1   1 
ATOM   5479  C  CD2   . TYR A 1 898  ? 143.386 170.928 154.865 1.00 69.36  ? 2115 TYR A CD2   1 
ATOM   5480  C  CE1   . TYR A 1 898  ? 144.291 173.294 153.770 1.00 72.05  ? 2115 TYR A CE1   1 
ATOM   5481  C  CE2   . TYR A 1 898  ? 144.732 171.098 154.609 1.00 72.89  ? 2115 TYR A CE2   1 
ATOM   5482  C  CZ    . TYR A 1 898  ? 145.179 172.281 154.062 1.00 75.33  ? 2115 TYR A CZ    1 
ATOM   5483  O  OH    . TYR A 1 898  ? 146.521 172.447 153.809 1.00 72.52  ? 2115 TYR A OH    1 
ATOM   5484  N  N     . GLY A 1 899  ? 138.636 171.346 156.768 1.00 75.94  ? 2116 GLY A N     1 
ATOM   5485  C  CA    . GLY A 1 899  ? 137.255 170.975 157.023 1.00 83.36  ? 2116 GLY A CA    1 
ATOM   5486  C  C     . GLY A 1 899  ? 136.977 169.542 156.615 1.00 90.56  ? 2116 GLY A C     1 
ATOM   5487  O  O     . GLY A 1 899  ? 137.595 169.000 155.695 1.00 91.82  ? 2116 GLY A O     1 
ATOM   5488  N  N     . SER A 1 900  ? 136.027 168.919 157.309 1.00 97.39  ? 2117 SER A N     1 
ATOM   5489  C  CA    . SER A 1 900  ? 135.726 167.513 157.086 1.00 104.69 ? 2117 SER A CA    1 
ATOM   5490  C  C     . SER A 1 900  ? 134.248 167.259 157.343 1.00 109.77 ? 2117 SER A C     1 
ATOM   5491  O  O     . SER A 1 900  ? 133.559 168.059 157.982 1.00 110.48 ? 2117 SER A O     1 
ATOM   5492  C  CB    . SER A 1 900  ? 136.584 166.608 157.978 1.00 104.05 ? 2117 SER A CB    1 
ATOM   5493  O  OG    . SER A 1 900  ? 136.462 166.973 159.342 1.00 105.38 ? 2117 SER A OG    1 
ATOM   5494  N  N     . MET A 1 901  ? 133.772 166.126 156.832 1.00 112.94 ? 2118 MET A N     1 
ATOM   5495  C  CA    . MET A 1 901  ? 132.389 165.717 157.012 1.00 117.06 ? 2118 MET A CA    1 
ATOM   5496  C  C     . MET A 1 901  ? 132.141 165.255 158.447 1.00 123.00 ? 2118 MET A C     1 
ATOM   5497  O  O     . MET A 1 901  ? 133.045 165.194 159.285 1.00 121.44 ? 2118 MET A O     1 
ATOM   5498  C  CB    . MET A 1 901  ? 132.032 164.583 156.050 1.00 118.48 ? 2118 MET A CB    1 
ATOM   5499  C  CG    . MET A 1 901  ? 132.039 164.933 154.568 1.00 120.08 ? 2118 MET A CG    1 
ATOM   5500  S  SD    . MET A 1 901  ? 130.838 166.194 154.100 1.00 124.53 ? 2118 MET A SD    1 
ATOM   5501  C  CE    . MET A 1 901  ? 131.891 167.628 153.930 1.00 111.74 ? 2118 MET A CE    1 
ATOM   5502  N  N     . LEU A 1 902  ? 130.882 164.929 158.721 1.00 128.12 ? 2119 LEU A N     1 
ATOM   5503  C  CA    . LEU A 1 902  ? 130.488 164.247 159.944 1.00 131.78 ? 2119 LEU A CA    1 
ATOM   5504  C  C     . LEU A 1 902  ? 130.114 162.809 159.612 1.00 134.39 ? 2119 LEU A C     1 
ATOM   5505  O  O     . LEU A 1 902  ? 129.444 162.549 158.609 1.00 132.16 ? 2119 LEU A O     1 
ATOM   5506  C  CB    . LEU A 1 902  ? 129.311 164.948 160.624 1.00 132.54 ? 2119 LEU A CB    1 
ATOM   5507  C  CG    . LEU A 1 902  ? 129.584 166.051 161.652 1.00 132.18 ? 2119 LEU A CG    1 
ATOM   5508  C  CD1   . LEU A 1 902  ? 130.392 165.502 162.819 1.00 132.43 ? 2119 LEU A CD1   1 
ATOM   5509  C  CD2   . LEU A 1 902  ? 130.276 167.256 161.031 1.00 126.22 ? 2119 LEU A CD2   1 
ATOM   5510  N  N     . LYS A 1 903  ? 130.555 161.877 160.458 1.00 138.47 ? 2120 LYS A N     1 
ATOM   5511  C  CA    . LYS A 1 903  ? 130.293 160.461 160.226 1.00 139.52 ? 2120 LYS A CA    1 
ATOM   5512  C  C     . LYS A 1 903  ? 128.820 160.095 160.363 1.00 141.19 ? 2120 LYS A C     1 
ATOM   5513  O  O     . LYS A 1 903  ? 128.431 159.004 159.933 1.00 140.91 ? 2120 LYS A O     1 
ATOM   5514  C  CB    . LYS A 1 903  ? 131.124 159.611 161.189 1.00 138.84 ? 2120 LYS A CB    1 
ATOM   5515  N  N     . ALA A 1 904  ? 127.999 160.968 160.941 1.00 143.25 ? 2121 ALA A N     1 
ATOM   5516  C  CA    . ALA A 1 904  ? 126.582 160.701 161.146 1.00 144.83 ? 2121 ALA A CA    1 
ATOM   5517  C  C     . ALA A 1 904  ? 125.664 161.636 160.376 1.00 143.81 ? 2121 ALA A C     1 
ATOM   5518  O  O     . ALA A 1 904  ? 124.581 161.221 159.960 1.00 143.08 ? 2121 ALA A O     1 
ATOM   5519  C  CB    . ALA A 1 904  ? 126.244 160.783 162.638 1.00 146.03 ? 2121 ALA A CB    1 
ATOM   5520  N  N     . THR A 1 905  ? 126.063 162.895 160.173 1.00 142.44 ? 2122 THR A N     1 
ATOM   5521  C  CA    . THR A 1 905  ? 125.218 163.865 159.493 1.00 141.03 ? 2122 THR A CA    1 
ATOM   5522  C  C     . THR A 1 905  ? 125.757 164.310 158.141 1.00 136.29 ? 2122 THR A C     1 
ATOM   5523  O  O     . THR A 1 905  ? 124.969 164.776 157.311 1.00 133.42 ? 2122 THR A O     1 
ATOM   5524  C  CB    . THR A 1 905  ? 125.015 165.110 160.371 1.00 143.07 ? 2122 THR A CB    1 
ATOM   5525  O  OG1   . THR A 1 905  ? 126.242 165.840 160.467 1.00 137.40 ? 2122 THR A OG1   1 
ATOM   5526  C  CG2   . THR A 1 905  ? 124.572 164.706 161.770 1.00 147.31 ? 2122 THR A CG2   1 
ATOM   5527  N  N     . LEU A 1 906  ? 127.066 164.169 157.905 1.00 135.50 ? 2123 LEU A N     1 
ATOM   5528  C  CA    . LEU A 1 906  ? 127.727 164.599 156.667 1.00 132.22 ? 2123 LEU A CA    1 
ATOM   5529  C  C     . LEU A 1 906  ? 127.467 166.078 156.378 1.00 130.25 ? 2123 LEU A C     1 
ATOM   5530  O  O     . LEU A 1 906  ? 126.987 166.453 155.307 1.00 127.94 ? 2123 LEU A O     1 
ATOM   5531  C  CB    . LEU A 1 906  ? 127.319 163.727 155.472 1.00 132.02 ? 2123 LEU A CB    1 
ATOM   5532  C  CG    . LEU A 1 906  ? 127.946 162.338 155.293 1.00 131.63 ? 2123 LEU A CG    1 
ATOM   5533  C  CD1   . LEU A 1 906  ? 127.434 161.326 156.311 1.00 134.43 ? 2123 LEU A CD1   1 
ATOM   5534  C  CD2   . LEU A 1 906  ? 127.723 161.836 153.874 1.00 131.31 ? 2123 LEU A CD2   1 
ATOM   5535  N  N     . GLU A 1 907  ? 127.792 166.922 157.353 1.00 128.39 ? 2124 GLU A N     1 
ATOM   5536  C  CA    . GLU A 1 907  ? 127.643 168.365 157.230 1.00 125.10 ? 2124 GLU A CA    1 
ATOM   5537  C  C     . GLU A 1 907  ? 129.019 169.013 157.208 1.00 117.74 ? 2124 GLU A C     1 
ATOM   5538  O  O     . GLU A 1 907  ? 129.829 168.793 158.114 1.00 114.84 ? 2124 GLU A O     1 
ATOM   5539  C  CB    . GLU A 1 907  ? 126.805 168.931 158.379 1.00 128.55 ? 2124 GLU A CB    1 
ATOM   5540  C  CG    . GLU A 1 907  ? 125.305 168.842 158.149 1.00 130.96 ? 2124 GLU A CG    1 
ATOM   5541  C  CD    . GLU A 1 907  ? 124.875 169.501 156.853 1.00 127.99 ? 2124 GLU A CD    1 
ATOM   5542  O  OE1   . GLU A 1 907  ? 124.879 170.749 156.789 1.00 123.99 ? 2124 GLU A OE1   1 
ATOM   5543  O  OE2   . GLU A 1 907  ? 124.533 168.773 155.898 1.00 126.40 ? 2124 GLU A OE2   1 
ATOM   5544  N  N     . TRP A 1 908  ? 129.278 169.805 156.172 1.00 115.12 ? 2125 TRP A N     1 
ATOM   5545  C  CA    . TRP A 1 908  ? 130.571 170.455 156.022 1.00 110.24 ? 2125 TRP A CA    1 
ATOM   5546  C  C     . TRP A 1 908  ? 130.760 171.537 157.079 1.00 110.39 ? 2125 TRP A C     1 
ATOM   5547  O  O     . TRP A 1 908  ? 129.847 172.314 157.369 1.00 112.14 ? 2125 TRP A O     1 
ATOM   5548  C  CB    . TRP A 1 908  ? 130.696 171.055 154.621 1.00 105.38 ? 2125 TRP A CB    1 
ATOM   5549  C  CG    . TRP A 1 908  ? 131.821 172.035 154.461 1.00 100.39 ? 2125 TRP A CG    1 
ATOM   5550  C  CD1   . TRP A 1 908  ? 131.743 173.394 154.555 1.00 97.62  ? 2125 TRP A CD1   1 
ATOM   5551  C  CD2   . TRP A 1 908  ? 133.189 171.732 154.162 1.00 98.78  ? 2125 TRP A CD2   1 
ATOM   5552  N  NE1   . TRP A 1 908  ? 132.977 173.954 154.343 1.00 96.59  ? 2125 TRP A NE1   1 
ATOM   5553  C  CE2   . TRP A 1 908  ? 133.882 172.955 154.098 1.00 96.60  ? 2125 TRP A CE2   1 
ATOM   5554  C  CE3   . TRP A 1 908  ? 133.895 170.545 153.947 1.00 96.77  ? 2125 TRP A CE3   1 
ATOM   5555  C  CZ2   . TRP A 1 908  ? 135.247 173.026 153.829 1.00 93.55  ? 2125 TRP A CZ2   1 
ATOM   5556  C  CZ3   . TRP A 1 908  ? 135.249 170.617 153.679 1.00 93.62  ? 2125 TRP A CZ3   1 
ATOM   5557  C  CH2   . TRP A 1 908  ? 135.910 171.848 153.622 1.00 93.55  ? 2125 TRP A CH2   1 
ATOM   5558  N  N     . ARG A 1 909  ? 131.957 171.578 157.658 1.00 106.81 ? 2126 ARG A N     1 
ATOM   5559  C  CA    . ARG A 1 909  ? 132.355 172.621 158.593 1.00 101.32 ? 2126 ARG A CA    1 
ATOM   5560  C  C     . ARG A 1 909  ? 133.606 173.296 158.054 1.00 94.10  ? 2126 ARG A C     1 
ATOM   5561  O  O     . ARG A 1 909  ? 134.573 172.617 157.694 1.00 92.42  ? 2126 ARG A O     1 
ATOM   5562  C  CB    . ARG A 1 909  ? 132.616 172.051 159.989 1.00 103.34 ? 2126 ARG A CB    1 
ATOM   5563  C  CG    . ARG A 1 909  ? 131.375 171.533 160.693 1.00 109.91 ? 2126 ARG A CG    1 
ATOM   5564  C  CD    . ARG A 1 909  ? 131.701 171.058 162.100 1.00 112.63 ? 2126 ARG A CD    1 
ATOM   5565  N  NE    . ARG A 1 909  ? 132.521 169.852 162.093 1.00 113.39 ? 2126 ARG A NE    1 
ATOM   5566  C  CZ    . ARG A 1 909  ? 133.777 169.800 162.515 1.00 113.55 ? 2126 ARG A CZ    1 
ATOM   5567  N  NH1   . ARG A 1 909  ? 134.390 170.869 162.996 1.00 115.52 ? 2126 ARG A NH1   1 
ATOM   5568  N  NH2   . ARG A 1 909  ? 134.434 168.645 162.454 1.00 109.22 ? 2126 ARG A NH2   1 
ATOM   5569  N  N     . ASP A 1 910  ? 133.585 174.624 157.996 1.00 92.99  ? 2127 ASP A N     1 
ATOM   5570  C  CA    . ASP A 1 910  ? 134.683 175.365 157.390 1.00 88.69  ? 2127 ASP A CA    1 
ATOM   5571  C  C     . ASP A 1 910  ? 135.927 175.318 158.268 1.00 87.65  ? 2127 ASP A C     1 
ATOM   5572  O  O     . ASP A 1 910  ? 135.864 175.589 159.471 1.00 88.76  ? 2127 ASP A O     1 
ATOM   5573  C  CB    . ASP A 1 910  ? 134.273 176.816 157.148 1.00 85.40  ? 2127 ASP A CB    1 
ATOM   5574  C  CG    . ASP A 1 910  ? 133.637 177.022 155.792 1.00 87.06  ? 2127 ASP A CG    1 
ATOM   5575  O  OD1   . ASP A 1 910  ? 133.731 176.107 154.947 1.00 89.13  ? 2127 ASP A OD1   1 
ATOM   5576  O  OD2   . ASP A 1 910  ? 133.044 178.098 155.570 1.00 89.34  ? 2127 ASP A OD2   1 
ATOM   5577  N  N     . GLY A 1 911  ? 137.060 174.975 157.660 1.00 82.17  ? 2128 GLY A N     1 
ATOM   5578  C  CA    . GLY A 1 911  ? 138.341 175.120 158.312 1.00 74.23  ? 2128 GLY A CA    1 
ATOM   5579  C  C     . GLY A 1 911  ? 138.806 176.559 158.276 1.00 70.28  ? 2128 GLY A C     1 
ATOM   5580  O  O     . GLY A 1 911  ? 138.150 177.440 157.725 1.00 72.93  ? 2128 GLY A O     1 
ATOM   5581  N  N     . LEU A 1 912  ? 139.972 176.796 158.879 1.00 66.63  ? 2129 LEU A N     1 
ATOM   5582  C  CA    . LEU A 1 912  ? 140.486 178.159 158.987 1.00 65.93  ? 2129 LEU A CA    1 
ATOM   5583  C  C     . LEU A 1 912  ? 140.838 178.734 157.618 1.00 68.52  ? 2129 LEU A C     1 
ATOM   5584  O  O     . LEU A 1 912  ? 140.408 179.843 157.267 1.00 68.46  ? 2129 LEU A O     1 
ATOM   5585  C  CB    . LEU A 1 912  ? 141.701 178.177 159.915 1.00 59.42  ? 2129 LEU A CB    1 
ATOM   5586  C  CG    . LEU A 1 912  ? 142.555 179.443 159.974 1.00 53.15  ? 2129 LEU A CG    1 
ATOM   5587  C  CD1   . LEU A 1 912  ? 141.732 180.639 160.418 1.00 51.91  ? 2129 LEU A CD1   1 
ATOM   5588  C  CD2   . LEU A 1 912  ? 143.735 179.228 160.905 1.00 45.19  ? 2129 LEU A CD2   1 
ATOM   5589  N  N     . PHE A 1 913  ? 141.613 177.985 156.828 1.00 66.58  ? 2130 PHE A N     1 
ATOM   5590  C  CA    . PHE A 1 913  ? 142.050 178.476 155.525 1.00 62.03  ? 2130 PHE A CA    1 
ATOM   5591  C  C     . PHE A 1 913  ? 140.873 178.630 154.570 1.00 67.26  ? 2130 PHE A C     1 
ATOM   5592  O  O     . PHE A 1 913  ? 140.785 179.622 153.833 1.00 68.68  ? 2130 PHE A O     1 
ATOM   5593  C  CB    . PHE A 1 913  ? 143.106 177.534 154.947 1.00 57.66  ? 2130 PHE A CB    1 
ATOM   5594  C  CG    . PHE A 1 913  ? 143.798 178.071 153.731 1.00 55.67  ? 2130 PHE A CG    1 
ATOM   5595  C  CD1   . PHE A 1 913  ? 144.024 179.430 153.592 1.00 52.73  ? 2130 PHE A CD1   1 
ATOM   5596  C  CD2   . PHE A 1 913  ? 144.239 177.218 152.735 1.00 56.77  ? 2130 PHE A CD2   1 
ATOM   5597  C  CE1   . PHE A 1 913  ? 144.666 179.927 152.477 1.00 51.64  ? 2130 PHE A CE1   1 
ATOM   5598  C  CE2   . PHE A 1 913  ? 144.883 177.712 151.617 1.00 57.38  ? 2130 PHE A CE2   1 
ATOM   5599  C  CZ    . PHE A 1 913  ? 145.096 179.069 151.488 1.00 53.44  ? 2130 PHE A CZ    1 
ATOM   5600  N  N     . THR A 1 914  ? 139.947 177.669 154.581 1.00 68.61  ? 2131 THR A N     1 
ATOM   5601  C  CA    . THR A 1 914  ? 138.758 177.784 153.745 1.00 69.22  ? 2131 THR A CA    1 
ATOM   5602  C  C     . THR A 1 914  ? 137.888 178.956 154.181 1.00 70.50  ? 2131 THR A C     1 
ATOM   5603  O  O     . THR A 1 914  ? 137.315 179.651 153.336 1.00 71.87  ? 2131 THR A O     1 
ATOM   5604  C  CB    . THR A 1 914  ? 137.964 176.480 153.773 1.00 71.95  ? 2131 THR A CB    1 
ATOM   5605  O  OG1   . THR A 1 914  ? 137.536 176.204 155.112 1.00 77.29  ? 2131 THR A OG1   1 
ATOM   5606  C  CG2   . THR A 1 914  ? 138.823 175.332 153.267 1.00 74.32  ? 2131 THR A CG2   1 
ATOM   5607  N  N     . SER A 1 915  ? 137.791 179.203 155.491 1.00 71.31  ? 2132 SER A N     1 
ATOM   5608  C  CA    . SER A 1 915  ? 136.996 180.329 155.977 1.00 70.42  ? 2132 SER A CA    1 
ATOM   5609  C  C     . SER A 1 915  ? 137.582 181.659 155.524 1.00 71.77  ? 2132 SER A C     1 
ATOM   5610  O  O     . SER A 1 915  ? 136.851 182.533 155.043 1.00 76.44  ? 2132 SER A O     1 
ATOM   5611  C  CB    . SER A 1 915  ? 136.888 180.294 157.500 1.00 69.43  ? 2132 SER A CB    1 
ATOM   5612  O  OG    . SER A 1 915  ? 136.445 181.541 158.006 1.00 67.03  ? 2132 SER A OG    1 
ATOM   5613  N  N     . ILE A 1 916  ? 138.900 181.837 155.667 1.00 69.59  ? 2133 ILE A N     1 
ATOM   5614  C  CA    . ILE A 1 916  ? 139.492 183.114 155.276 1.00 71.22  ? 2133 ILE A CA    1 
ATOM   5615  C  C     . ILE A 1 916  ? 139.439 183.289 153.759 1.00 72.41  ? 2133 ILE A C     1 
ATOM   5616  O  O     . ILE A 1 916  ? 139.197 184.397 153.258 1.00 73.18  ? 2133 ILE A O     1 
ATOM   5617  C  CB    . ILE A 1 916  ? 140.922 183.262 155.839 1.00 68.98  ? 2133 ILE A CB    1 
ATOM   5618  C  CG1   . ILE A 1 916  ? 141.524 184.617 155.453 1.00 64.27  ? 2133 ILE A CG1   1 
ATOM   5619  C  CG2   . ILE A 1 916  ? 141.835 182.148 155.384 1.00 64.22  ? 2133 ILE A CG2   1 
ATOM   5620  C  CD1   . ILE A 1 916  ? 140.670 185.804 155.837 1.00 61.32  ? 2133 ILE A CD1   1 
ATOM   5621  N  N     . LEU A 1 917  ? 139.614 182.201 153.001 1.00 72.06  ? 2134 LEU A N     1 
ATOM   5622  C  CA    . LEU A 1 917  ? 139.525 182.321 151.550 1.00 72.39  ? 2134 LEU A CA    1 
ATOM   5623  C  C     . LEU A 1 917  ? 138.103 182.631 151.096 1.00 77.24  ? 2134 LEU A C     1 
ATOM   5624  O  O     . LEU A 1 917  ? 137.906 183.408 150.159 1.00 78.42  ? 2134 LEU A O     1 
ATOM   5625  C  CB    . LEU A 1 917  ? 140.035 181.055 150.876 1.00 65.67  ? 2134 LEU A CB    1 
ATOM   5626  C  CG    . LEU A 1 917  ? 140.221 181.263 149.376 1.00 66.93  ? 2134 LEU A CG    1 
ATOM   5627  C  CD1   . LEU A 1 917  ? 141.169 182.418 149.107 1.00 64.08  ? 2134 LEU A CD1   1 
ATOM   5628  C  CD2   . LEU A 1 917  ? 140.724 180.011 148.749 1.00 72.72  ? 2134 LEU A CD2   1 
ATOM   5629  N  N     . ARG A 1 918  ? 137.097 182.038 151.741 1.00 76.70  ? 2135 ARG A N     1 
ATOM   5630  C  CA    . ARG A 1 918  ? 135.718 182.368 151.400 1.00 75.60  ? 2135 ARG A CA    1 
ATOM   5631  C  C     . ARG A 1 918  ? 135.390 183.809 151.776 1.00 77.36  ? 2135 ARG A C     1 
ATOM   5632  O  O     . ARG A 1 918  ? 134.682 184.505 151.037 1.00 80.93  ? 2135 ARG A O     1 
ATOM   5633  C  CB    . ARG A 1 918  ? 134.766 181.394 152.090 1.00 76.76  ? 2135 ARG A CB    1 
ATOM   5634  C  CG    . ARG A 1 918  ? 133.440 181.210 151.378 1.00 80.29  ? 2135 ARG A CG    1 
ATOM   5635  C  CD    . ARG A 1 918  ? 132.530 180.270 152.151 1.00 78.98  ? 2135 ARG A CD    1 
ATOM   5636  N  NE    . ARG A 1 918  ? 133.158 178.975 152.391 1.00 83.87  ? 2135 ARG A NE    1 
ATOM   5637  C  CZ    . ARG A 1 918  ? 133.249 178.005 151.492 1.00 83.19  ? 2135 ARG A CZ    1 
ATOM   5638  N  NH1   . ARG A 1 918  ? 132.749 178.139 150.275 1.00 82.75  ? 2135 ARG A NH1   1 
ATOM   5639  N  NH2   . ARG A 1 918  ? 133.857 176.869 151.823 1.00 83.87  ? 2135 ARG A NH2   1 
ATOM   5640  N  N     . ARG A 1 919  ? 135.912 184.275 152.915 1.00 77.02  ? 2136 ARG A N     1 
ATOM   5641  C  CA    . ARG A 1 919  ? 135.669 185.647 153.344 1.00 77.90  ? 2136 ARG A CA    1 
ATOM   5642  C  C     . ARG A 1 919  ? 136.331 186.661 152.419 1.00 81.25  ? 2136 ARG A C     1 
ATOM   5643  O  O     . ARG A 1 919  ? 135.812 187.771 152.254 1.00 82.46  ? 2136 ARG A O     1 
ATOM   5644  C  CB    . ARG A 1 919  ? 136.156 185.837 154.781 1.00 76.34  ? 2136 ARG A CB    1 
ATOM   5645  C  CG    . ARG A 1 919  ? 135.203 185.286 155.831 1.00 75.56  ? 2136 ARG A CG    1 
ATOM   5646  C  CD    . ARG A 1 919  ? 135.826 185.285 157.218 1.00 73.01  ? 2136 ARG A CD    1 
ATOM   5647  N  NE    . ARG A 1 919  ? 136.088 186.635 157.700 1.00 76.04  ? 2136 ARG A NE    1 
ATOM   5648  C  CZ    . ARG A 1 919  ? 137.269 187.060 158.128 1.00 72.22  ? 2136 ARG A CZ    1 
ATOM   5649  N  NH1   . ARG A 1 919  ? 138.316 186.254 158.179 1.00 66.07  ? 2136 ARG A NH1   1 
ATOM   5650  N  NH2   . ARG A 1 919  ? 137.400 188.323 158.522 1.00 69.95  ? 2136 ARG A NH2   1 
ATOM   5651  N  N     . VAL A 1 920  ? 137.467 186.313 151.812 1.00 78.31  ? 2137 VAL A N     1 
ATOM   5652  C  CA    . VAL A 1 920  ? 138.065 187.223 150.838 1.00 78.18  ? 2137 VAL A CA    1 
ATOM   5653  C  C     . VAL A 1 920  ? 137.517 187.018 149.427 1.00 82.26  ? 2137 VAL A C     1 
ATOM   5654  O  O     . VAL A 1 920  ? 137.661 187.913 148.583 1.00 83.51  ? 2137 VAL A O     1 
ATOM   5655  C  CB    . VAL A 1 920  ? 139.601 187.117 150.823 1.00 73.62  ? 2137 VAL A CB    1 
ATOM   5656  C  CG1   . VAL A 1 920  ? 140.159 187.346 152.217 1.00 73.04  ? 2137 VAL A CG1   1 
ATOM   5657  C  CG2   . VAL A 1 920  ? 140.052 185.781 150.271 1.00 69.12  ? 2137 VAL A CG2   1 
ATOM   5658  N  N     . ASN A 1 921  ? 136.896 185.870 149.147 1.00 81.98  ? 2138 ASN A N     1 
ATOM   5659  C  CA    . ASN A 1 921  ? 136.223 185.684 147.865 1.00 82.19  ? 2138 ASN A CA    1 
ATOM   5660  C  C     . ASN A 1 921  ? 134.920 186.469 147.808 1.00 85.14  ? 2138 ASN A C     1 
ATOM   5661  O  O     . ASN A 1 921  ? 134.619 187.108 146.794 1.00 87.36  ? 2138 ASN A O     1 
ATOM   5662  C  CB    . ASN A 1 921  ? 135.955 184.198 147.620 1.00 80.91  ? 2138 ASN A CB    1 
ATOM   5663  C  CG    . ASN A 1 921  ? 136.981 183.562 146.705 1.00 83.85  ? 2138 ASN A CG    1 
ATOM   5664  O  OD1   . ASN A 1 921  ? 137.805 184.249 146.103 1.00 82.55  ? 2138 ASN A OD1   1 
ATOM   5665  N  ND2   . ASN A 1 921  ? 136.931 182.239 146.592 1.00 81.80  ? 2138 ASN A ND2   1 
ATOM   5666  N  N     . ASP A 1 922  ? 134.133 186.427 148.886 1.00 86.31  ? 2139 ASP A N     1 
ATOM   5667  C  CA    . ASP A 1 922  ? 132.836 187.097 148.882 1.00 87.66  ? 2139 ASP A CA    1 
ATOM   5668  C  C     . ASP A 1 922  ? 132.993 188.613 148.854 1.00 88.77  ? 2139 ASP A C     1 
ATOM   5669  O  O     . ASP A 1 922  ? 132.346 189.295 148.050 1.00 89.46  ? 2139 ASP A O     1 
ATOM   5670  C  CB    . ASP A 1 922  ? 132.017 186.663 150.098 1.00 89.82  ? 2139 ASP A CB    1 
ATOM   5671  C  CG    . ASP A 1 922  ? 131.466 185.258 149.956 1.00 94.67  ? 2139 ASP A CG    1 
ATOM   5672  O  OD1   . ASP A 1 922  ? 132.020 184.478 149.154 1.00 92.34  ? 2139 ASP A OD1   1 
ATOM   5673  O  OD2   . ASP A 1 922  ? 130.477 184.934 150.647 1.00 95.45  ? 2139 ASP A OD2   1 
ATOM   5674  N  N     . ASP A 1 923  ? 133.863 189.150 149.712 1.00 89.44  ? 2140 ASP A N     1 
ATOM   5675  C  CA    . ASP A 1 923  ? 134.085 190.590 149.868 1.00 89.80  ? 2140 ASP A CA    1 
ATOM   5676  C  C     . ASP A 1 923  ? 132.769 191.322 150.138 1.00 93.35  ? 2140 ASP A C     1 
ATOM   5677  O  O     . ASP A 1 923  ? 132.328 192.180 149.371 1.00 92.36  ? 2140 ASP A O     1 
ATOM   5678  C  CB    . ASP A 1 923  ? 134.806 191.173 148.649 1.00 88.06  ? 2140 ASP A CB    1 
ATOM   5679  C  CG    . ASP A 1 923  ? 135.415 192.532 148.930 1.00 90.19  ? 2140 ASP A CG    1 
ATOM   5680  O  OD1   . ASP A 1 923  ? 135.756 192.801 150.101 1.00 90.53  ? 2140 ASP A OD1   1 
ATOM   5681  O  OD2   . ASP A 1 923  ? 135.552 193.332 147.981 1.00 90.64  ? 2140 ASP A OD2   1 
ATOM   5682  N  N     . ILE A 1 924  ? 132.139 190.946 151.252 1.00 95.03  ? 2141 ILE A N     1 
ATOM   5683  C  CA    . ILE A 1 924  ? 130.824 191.484 151.592 1.00 94.37  ? 2141 ILE A CA    1 
ATOM   5684  C  C     . ILE A 1 924  ? 130.919 192.973 151.909 1.00 92.07  ? 2141 ILE A C     1 
ATOM   5685  O  O     . ILE A 1 924  ? 130.148 193.786 151.387 1.00 91.62  ? 2141 ILE A O     1 
ATOM   5686  C  CB    . ILE A 1 924  ? 130.215 190.692 152.763 1.00 92.87  ? 2141 ILE A CB    1 
ATOM   5687  C  CG1   . ILE A 1 924  ? 129.829 189.283 152.308 1.00 94.50  ? 2141 ILE A CG1   1 
ATOM   5688  C  CG2   . ILE A 1 924  ? 129.009 191.419 153.339 1.00 94.28  ? 2141 ILE A CG2   1 
ATOM   5689  C  CD1   . ILE A 1 924  ? 128.819 189.257 151.184 1.00 97.02  ? 2141 ILE A CD1   1 
ATOM   5690  N  N     . THR A 1 925  ? 131.872 193.351 152.761 1.00 92.16  ? 2142 THR A N     1 
ATOM   5691  C  CA    . THR A 1 925  ? 132.033 194.753 153.131 1.00 94.10  ? 2142 THR A CA    1 
ATOM   5692  C  C     . THR A 1 925  ? 132.631 195.575 151.995 1.00 93.33  ? 2142 THR A C     1 
ATOM   5693  O  O     . THR A 1 925  ? 132.243 196.733 151.799 1.00 91.89  ? 2142 THR A O     1 
ATOM   5694  C  CB    . THR A 1 925  ? 132.903 194.860 154.388 1.00 92.75  ? 2142 THR A CB    1 
ATOM   5695  O  OG1   . THR A 1 925  ? 132.304 194.103 155.448 1.00 91.89  ? 2142 THR A OG1   1 
ATOM   5696  C  CG2   . THR A 1 925  ? 133.041 196.308 154.841 1.00 90.10  ? 2142 THR A CG2   1 
ATOM   5697  N  N     . GLY A 1 926  ? 133.537 194.990 151.219 1.00 91.85  ? 2143 GLY A N     1 
ATOM   5698  C  CA    . GLY A 1 926  ? 134.237 195.706 150.176 1.00 89.93  ? 2143 GLY A CA    1 
ATOM   5699  C  C     . GLY A 1 926  ? 135.673 196.060 150.491 1.00 87.47  ? 2143 GLY A C     1 
ATOM   5700  O  O     . GLY A 1 926  ? 136.291 196.804 149.722 1.00 86.95  ? 2143 GLY A O     1 
ATOM   5701  N  N     . THR A 1 927  ? 136.220 195.559 151.599 1.00 86.67  ? 2144 THR A N     1 
ATOM   5702  C  CA    . THR A 1 927  ? 137.609 195.846 151.940 1.00 85.13  ? 2144 THR A CA    1 
ATOM   5703  C  C     . THR A 1 927  ? 138.571 195.117 151.007 1.00 83.98  ? 2144 THR A C     1 
ATOM   5704  O  O     . THR A 1 927  ? 139.574 195.690 150.566 1.00 84.27  ? 2144 THR A O     1 
ATOM   5705  C  CB    . THR A 1 927  ? 137.870 195.466 153.401 1.00 90.68  ? 2144 THR A CB    1 
ATOM   5706  O  OG1   . THR A 1 927  ? 137.182 196.383 154.261 1.00 96.30  ? 2144 THR A OG1   1 
ATOM   5707  C  CG2   . THR A 1 927  ? 139.359 195.501 153.726 1.00 85.97  ? 2144 THR A CG2   1 
ATOM   5708  N  N     . PHE A 1 928  ? 138.258 193.869 150.658 1.00 84.95  ? 2145 PHE A N     1 
ATOM   5709  C  CA    . PHE A 1 928  ? 139.174 192.998 149.935 1.00 83.59  ? 2145 PHE A CA    1 
ATOM   5710  C  C     . PHE A 1 928  ? 139.105 193.172 148.421 1.00 85.53  ? 2145 PHE A C     1 
ATOM   5711  O  O     . PHE A 1 928  ? 139.470 192.247 147.686 1.00 83.07  ? 2145 PHE A O     1 
ATOM   5712  C  CB    . PHE A 1 928  ? 138.911 191.537 150.304 1.00 81.73  ? 2145 PHE A CB    1 
ATOM   5713  C  CG    . PHE A 1 928  ? 138.997 191.260 151.776 1.00 83.75  ? 2145 PHE A CG    1 
ATOM   5714  C  CD1   . PHE A 1 928  ? 139.994 191.837 152.544 1.00 82.27  ? 2145 PHE A CD1   1 
ATOM   5715  C  CD2   . PHE A 1 928  ? 138.081 190.425 152.393 1.00 82.94  ? 2145 PHE A CD2   1 
ATOM   5716  C  CE1   . PHE A 1 928  ? 140.077 191.584 153.901 1.00 76.99  ? 2145 PHE A CE1   1 
ATOM   5717  C  CE2   . PHE A 1 928  ? 138.159 190.167 153.749 1.00 79.51  ? 2145 PHE A CE2   1 
ATOM   5718  C  CZ    . PHE A 1 928  ? 139.158 190.748 154.504 1.00 76.02  ? 2145 PHE A CZ    1 
ATOM   5719  N  N     . LYS A 1 929  ? 138.641 194.324 147.935 1.00 86.38  ? 2146 LYS A N     1 
ATOM   5720  C  CA    . LYS A 1 929  ? 138.708 194.598 146.505 1.00 85.21  ? 2146 LYS A CA    1 
ATOM   5721  C  C     . LYS A 1 929  ? 139.923 195.435 146.131 1.00 82.34  ? 2146 LYS A C     1 
ATOM   5722  O  O     . LYS A 1 929  ? 140.373 195.379 144.981 1.00 82.68  ? 2146 LYS A O     1 
ATOM   5723  C  CB    . LYS A 1 929  ? 137.430 195.300 146.028 1.00 85.79  ? 2146 LYS A CB    1 
ATOM   5724  C  CG    . LYS A 1 929  ? 137.348 196.785 146.354 1.00 87.74  ? 2146 LYS A CG    1 
ATOM   5725  C  CD    . LYS A 1 929  ? 135.912 197.250 146.525 1.00 89.17  ? 2146 LYS A CD    1 
ATOM   5726  C  CE    . LYS A 1 929  ? 135.860 198.679 147.039 1.00 88.97  ? 2146 LYS A CE    1 
ATOM   5727  N  NZ    . LYS A 1 929  ? 136.784 198.890 148.187 1.00 84.40  ? 2146 LYS A NZ    1 
ATOM   5728  N  N     . ASN A 1 930  ? 140.469 196.204 147.072 1.00 75.49  ? 2147 ASN A N     1 
ATOM   5729  C  CA    . ASN A 1 930  ? 141.612 197.070 146.806 1.00 74.61  ? 2147 ASN A CA    1 
ATOM   5730  C  C     . ASN A 1 930  ? 142.636 196.957 147.924 1.00 73.24  ? 2147 ASN A C     1 
ATOM   5731  O  O     . ASN A 1 930  ? 143.162 197.961 148.413 1.00 75.10  ? 2147 ASN A O     1 
ATOM   5732  C  CB    . ASN A 1 930  ? 141.174 198.522 146.624 1.00 79.23  ? 2147 ASN A CB    1 
ATOM   5733  C  CG    . ASN A 1 930  ? 140.414 198.741 145.333 1.00 89.29  ? 2147 ASN A CG    1 
ATOM   5734  O  OD1   . ASN A 1 930  ? 139.296 199.255 145.336 1.00 90.33  ? 2147 ASN A OD1   1 
ATOM   5735  N  ND2   . ASN A 1 930  ? 141.020 198.350 144.217 1.00 91.16  ? 2147 ASN A ND2   1 
ATOM   5736  N  N     . SER A 1 931  ? 142.933 195.730 148.345 1.00 68.33  ? 2148 SER A N     1 
ATOM   5737  C  CA    . SER A 1 931  ? 143.925 195.500 149.383 1.00 62.81  ? 2148 SER A CA    1 
ATOM   5738  C  C     . SER A 1 931  ? 144.559 194.136 149.167 1.00 58.04  ? 2148 SER A C     1 
ATOM   5739  O  O     . SER A 1 931  ? 143.864 193.166 148.851 1.00 60.67  ? 2148 SER A O     1 
ATOM   5740  C  CB    . SER A 1 931  ? 143.302 195.584 150.781 1.00 63.09  ? 2148 SER A CB    1 
ATOM   5741  O  OG    . SER A 1 931  ? 142.395 194.518 150.999 1.00 66.94  ? 2148 SER A OG    1 
ATOM   5742  N  N     . ARG A 1 932  ? 145.879 194.071 149.329 1.00 54.33  ? 2149 ARG A N     1 
ATOM   5743  C  CA    . ARG A 1 932  ? 146.589 192.805 149.226 1.00 48.79  ? 2149 ARG A CA    1 
ATOM   5744  C  C     . ARG A 1 932  ? 146.350 191.983 150.481 1.00 45.27  ? 2149 ARG A C     1 
ATOM   5745  O  O     . ARG A 1 932  ? 146.424 192.501 151.600 1.00 47.26  ? 2149 ARG A O     1 
ATOM   5746  C  CB    . ARG A 1 932  ? 148.085 193.028 149.024 1.00 46.82  ? 2149 ARG A CB    1 
ATOM   5747  C  CG    . ARG A 1 932  ? 148.450 193.657 147.702 1.00 47.71  ? 2149 ARG A CG    1 
ATOM   5748  C  CD    . ARG A 1 932  ? 149.730 194.454 147.821 1.00 41.74  ? 2149 ARG A CD    1 
ATOM   5749  N  NE    . ARG A 1 932  ? 150.265 194.793 146.509 1.00 45.21  ? 2149 ARG A NE    1 
ATOM   5750  C  CZ    . ARG A 1 932  ? 150.806 195.962 146.199 1.00 49.43  ? 2149 ARG A CZ    1 
ATOM   5751  N  NH1   . ARG A 1 932  ? 150.903 196.936 147.089 1.00 45.55  ? 2149 ARG A NH1   1 
ATOM   5752  N  NH2   . ARG A 1 932  ? 151.262 196.159 144.966 1.00 50.03  ? 2149 ARG A NH2   1 
ATOM   5753  N  N     . ILE A 1 933  ? 146.073 190.700 150.289 1.00 39.05  ? 2150 ILE A N     1 
ATOM   5754  C  CA    . ILE A 1 933  ? 145.779 189.766 151.367 1.00 40.14  ? 2150 ILE A CA    1 
ATOM   5755  C  C     . ILE A 1 933  ? 146.865 188.696 151.407 1.00 37.63  ? 2150 ILE A C     1 
ATOM   5756  O  O     . ILE A 1 933  ? 147.183 188.075 150.385 1.00 38.84  ? 2150 ILE A O     1 
ATOM   5757  C  CB    . ILE A 1 933  ? 144.352 189.187 151.222 1.00 43.58  ? 2150 ILE A CB    1 
ATOM   5758  C  CG1   . ILE A 1 933  ? 143.893 188.451 152.491 1.00 44.95  ? 2150 ILE A CG1   1 
ATOM   5759  C  CG2   . ILE A 1 933  ? 144.135 188.446 149.908 1.00 45.65  ? 2150 ILE A CG2   1 
ATOM   5760  C  CD1   . ILE A 1 933  ? 143.989 189.258 153.748 1.00 42.96  ? 2150 ILE A CD1   1 
ATOM   5761  N  N     . TRP A 1 934  ? 147.479 188.534 152.577 1.00 34.90  ? 2151 TRP A N     1 
ATOM   5762  C  CA    . TRP A 1 934  ? 148.576 187.601 152.786 1.00 27.91  ? 2151 TRP A CA    1 
ATOM   5763  C  C     . TRP A 1 934  ? 148.149 186.525 153.770 1.00 29.00  ? 2151 TRP A C     1 
ATOM   5764  O  O     . TRP A 1 934  ? 147.451 186.809 154.747 1.00 37.29  ? 2151 TRP A O     1 
ATOM   5765  C  CB    . TRP A 1 934  ? 149.823 188.304 153.333 1.00 30.07  ? 2151 TRP A CB    1 
ATOM   5766  C  CG    . TRP A 1 934  ? 150.124 189.627 152.712 1.00 32.03  ? 2151 TRP A CG    1 
ATOM   5767  C  CD1   . TRP A 1 934  ? 149.635 190.841 153.092 1.00 35.27  ? 2151 TRP A CD1   1 
ATOM   5768  C  CD2   . TRP A 1 934  ? 151.007 189.876 151.616 1.00 28.02  ? 2151 TRP A CD2   1 
ATOM   5769  N  NE1   . TRP A 1 934  ? 150.149 191.830 152.291 1.00 34.52  ? 2151 TRP A NE1   1 
ATOM   5770  C  CE2   . TRP A 1 934  ? 150.995 191.261 151.376 1.00 30.41  ? 2151 TRP A CE2   1 
ATOM   5771  C  CE3   . TRP A 1 934  ? 151.797 189.061 150.807 1.00 26.98  ? 2151 TRP A CE3   1 
ATOM   5772  C  CZ2   . TRP A 1 934  ? 151.744 191.844 150.364 1.00 30.60  ? 2151 TRP A CZ2   1 
ATOM   5773  C  CZ3   . TRP A 1 934  ? 152.540 189.640 149.808 1.00 25.13  ? 2151 TRP A CZ3   1 
ATOM   5774  C  CH2   . TRP A 1 934  ? 152.509 191.018 149.592 1.00 27.05  ? 2151 TRP A CH2   1 
ATOM   5775  N  N     . VAL A 1 935  ? 148.570 185.292 153.514 1.00 23.62  ? 2152 VAL A N     1 
ATOM   5776  C  CA    . VAL A 1 935  ? 148.385 184.185 154.444 1.00 25.09  ? 2152 VAL A CA    1 
ATOM   5777  C  C     . VAL A 1 935  ? 149.768 183.617 154.724 1.00 26.99  ? 2152 VAL A C     1 
ATOM   5778  O  O     . VAL A 1 935  ? 150.359 182.948 153.867 1.00 31.52  ? 2152 VAL A O     1 
ATOM   5779  C  CB    . VAL A 1 935  ? 147.435 183.113 153.894 1.00 24.84  ? 2152 VAL A CB    1 
ATOM   5780  C  CG1   . VAL A 1 935  ? 147.457 181.871 154.772 1.00 26.15  ? 2152 VAL A CG1   1 
ATOM   5781  C  CG2   . VAL A 1 935  ? 146.026 183.662 153.805 1.00 32.98  ? 2152 VAL A CG2   1 
ATOM   5782  N  N     . VAL A 1 936  ? 150.293 183.896 155.911 1.00 21.47  ? 2153 VAL A N     1 
ATOM   5783  C  CA    . VAL A 1 936  ? 151.645 183.508 156.287 1.00 17.63  ? 2153 VAL A CA    1 
ATOM   5784  C  C     . VAL A 1 936  ? 151.571 182.194 157.045 1.00 19.30  ? 2153 VAL A C     1 
ATOM   5785  O  O     . VAL A 1 936  ? 150.985 182.128 158.132 1.00 25.95  ? 2153 VAL A O     1 
ATOM   5786  C  CB    . VAL A 1 936  ? 152.322 184.595 157.135 1.00 18.88  ? 2153 VAL A CB    1 
ATOM   5787  C  CG1   . VAL A 1 936  ? 153.701 184.141 157.572 1.00 19.00  ? 2153 VAL A CG1   1 
ATOM   5788  C  CG2   . VAL A 1 936  ? 152.403 185.896 156.356 1.00 17.89  ? 2153 VAL A CG2   1 
ATOM   5789  N  N     . PHE A 1 937  ? 152.159 181.144 156.475 1.00 18.81  ? 2154 PHE A N     1 
ATOM   5790  C  CA    . PHE A 1 937  ? 152.235 179.848 157.148 1.00 22.38  ? 2154 PHE A CA    1 
ATOM   5791  C  C     . PHE A 1 937  ? 153.532 179.779 157.954 1.00 22.16  ? 2154 PHE A C     1 
ATOM   5792  O  O     . PHE A 1 937  ? 154.496 179.096 157.609 1.00 22.03  ? 2154 PHE A O     1 
ATOM   5793  C  CB    . PHE A 1 937  ? 152.130 178.713 156.139 1.00 25.56  ? 2154 PHE A CB    1 
ATOM   5794  C  CG    . PHE A 1 937  ? 150.718 178.346 155.787 1.00 29.28  ? 2154 PHE A CG    1 
ATOM   5795  C  CD1   . PHE A 1 937  ? 149.860 177.841 156.748 1.00 32.83  ? 2154 PHE A CD1   1 
ATOM   5796  C  CD2   . PHE A 1 937  ? 150.249 178.504 154.495 1.00 31.27  ? 2154 PHE A CD2   1 
ATOM   5797  C  CE1   . PHE A 1 937  ? 148.562 177.502 156.428 1.00 37.84  ? 2154 PHE A CE1   1 
ATOM   5798  C  CE2   . PHE A 1 937  ? 148.952 178.166 154.170 1.00 37.16  ? 2154 PHE A CE2   1 
ATOM   5799  C  CZ    . PHE A 1 937  ? 148.108 177.664 155.137 1.00 41.39  ? 2154 PHE A CZ    1 
ATOM   5800  N  N     . ASP A 1 938  ? 153.526 180.510 159.069 1.00 19.82  ? 2155 ASP A N     1 
ATOM   5801  C  CA    . ASP A 1 938  ? 154.716 180.716 159.895 1.00 19.73  ? 2155 ASP A CA    1 
ATOM   5802  C  C     . ASP A 1 938  ? 154.991 179.473 160.742 1.00 22.39  ? 2155 ASP A C     1 
ATOM   5803  O  O     . ASP A 1 938  ? 154.916 179.481 161.972 1.00 26.79  ? 2155 ASP A O     1 
ATOM   5804  C  CB    . ASP A 1 938  ? 154.536 181.952 160.765 1.00 18.28  ? 2155 ASP A CB    1 
ATOM   5805  C  CG    . ASP A 1 938  ? 155.849 182.592 161.155 1.00 17.93  ? 2155 ASP A CG    1 
ATOM   5806  O  OD1   . ASP A 1 938  ? 156.777 181.861 161.556 1.00 19.04  ? 2155 ASP A OD1   1 
ATOM   5807  O  OD2   . ASP A 1 938  ? 155.949 183.832 161.066 1.00 15.31  ? 2155 ASP A OD2   1 
ATOM   5808  N  N     . SER A 1 939  ? 155.334 178.389 160.054 1.00 23.49  ? 2156 SER A N     1 
ATOM   5809  C  CA    . SER A 1 939  ? 155.690 177.128 160.694 1.00 28.64  ? 2156 SER A CA    1 
ATOM   5810  C  C     . SER A 1 939  ? 156.450 176.282 159.679 1.00 31.93  ? 2156 SER A C     1 
ATOM   5811  O  O     . SER A 1 939  ? 156.829 176.763 158.607 1.00 32.64  ? 2156 SER A O     1 
ATOM   5812  C  CB    . SER A 1 939  ? 154.450 176.403 161.227 1.00 30.96  ? 2156 SER A CB    1 
ATOM   5813  O  OG    . SER A 1 939  ? 154.808 175.410 162.171 1.00 28.86  ? 2156 SER A OG    1 
ATOM   5814  N  N     . ASP A 1 940  ? 156.662 175.014 160.014 1.00 31.53  ? 2157 ASP A N     1 
ATOM   5815  C  CA    . ASP A 1 940  ? 157.450 174.115 159.185 1.00 35.27  ? 2157 ASP A CA    1 
ATOM   5816  C  C     . ASP A 1 940  ? 156.575 173.435 158.140 1.00 41.87  ? 2157 ASP A C     1 
ATOM   5817  O  O     . ASP A 1 940  ? 155.426 173.075 158.414 1.00 45.75  ? 2157 ASP A O     1 
ATOM   5818  C  CB    . ASP A 1 940  ? 158.136 173.061 160.054 1.00 39.60  ? 2157 ASP A CB    1 
ATOM   5819  C  CG    . ASP A 1 940  ? 159.174 173.658 160.982 1.00 36.85  ? 2157 ASP A CG    1 
ATOM   5820  O  OD1   . ASP A 1 940  ? 159.755 174.705 160.631 1.00 29.37  ? 2157 ASP A OD1   1 
ATOM   5821  O  OD2   . ASP A 1 940  ? 159.408 173.082 162.065 1.00 41.72  ? 2157 ASP A OD2   1 
ATOM   5822  N  N     . LEU A 1 941  ? 157.123 173.272 156.936 1.00 45.49  ? 2158 LEU A N     1 
ATOM   5823  C  CA    . LEU A 1 941  ? 156.441 172.510 155.898 1.00 56.97  ? 2158 LEU A CA    1 
ATOM   5824  C  C     . LEU A 1 941  ? 156.286 171.050 156.304 1.00 62.81  ? 2158 LEU A C     1 
ATOM   5825  O  O     . LEU A 1 941  ? 157.133 170.474 156.991 1.00 63.60  ? 2158 LEU A O     1 
ATOM   5826  C  CB    . LEU A 1 941  ? 157.191 172.588 154.567 1.00 60.06  ? 2158 LEU A CB    1 
ATOM   5827  C  CG    . LEU A 1 941  ? 156.801 173.654 153.538 1.00 54.87  ? 2158 LEU A CG    1 
ATOM   5828  C  CD1   . LEU A 1 941  ? 155.383 173.412 153.046 1.00 55.15  ? 2158 LEU A CD1   1 
ATOM   5829  C  CD2   . LEU A 1 941  ? 156.934 175.050 154.082 1.00 43.07  ? 2158 LEU A CD2   1 
ATOM   5830  N  N     . ASP A 1 942  ? 155.181 170.455 155.866 1.00 67.60  ? 2159 ASP A N     1 
ATOM   5831  C  CA    . ASP A 1 942  ? 154.865 169.066 156.133 1.00 75.96  ? 2159 ASP A CA    1 
ATOM   5832  C  C     . ASP A 1 942  ? 154.404 168.402 154.843 1.00 77.38  ? 2159 ASP A C     1 
ATOM   5833  O  O     . ASP A 1 942  ? 153.617 168.992 154.094 1.00 76.16  ? 2159 ASP A O     1 
ATOM   5834  C  CB    . ASP A 1 942  ? 153.771 168.965 157.204 1.00 75.39  ? 2159 ASP A CB    1 
ATOM   5835  C  CG    . ASP A 1 942  ? 153.634 167.574 157.768 1.00 79.17  ? 2159 ASP A CG    1 
ATOM   5836  O  OD1   . ASP A 1 942  ? 152.975 166.729 157.127 1.00 81.19  ? 2159 ASP A OD1   1 
ATOM   5837  O  OD2   . ASP A 1 942  ? 154.179 167.330 158.862 1.00 78.22  ? 2159 ASP A OD2   1 
ATOM   5838  N  N     . PRO A 1 943  ? 154.881 167.183 154.548 1.00 78.18  ? 2160 PRO A N     1 
ATOM   5839  C  CA    . PRO A 1 943  ? 154.512 166.530 153.282 1.00 82.01  ? 2160 PRO A CA    1 
ATOM   5840  C  C     . PRO A 1 943  ? 153.032 166.196 153.197 1.00 81.84  ? 2160 PRO A C     1 
ATOM   5841  O  O     . PRO A 1 943  ? 152.355 166.534 152.220 1.00 83.29  ? 2160 PRO A O     1 
ATOM   5842  C  CB    . PRO A 1 943  ? 155.363 165.251 153.274 1.00 78.71  ? 2160 PRO A CB    1 
ATOM   5843  C  CG    . PRO A 1 943  ? 156.363 165.409 154.364 1.00 76.42  ? 2160 PRO A CG    1 
ATOM   5844  C  CD    . PRO A 1 943  ? 155.807 166.371 155.353 1.00 73.67  ? 2160 PRO A CD    1 
ATOM   5845  N  N     . GLU A 1 944  ? 152.526 165.521 154.228 1.00 79.00  ? 2161 GLU A N     1 
ATOM   5846  C  CA    . GLU A 1 944  ? 151.124 165.129 154.258 1.00 79.13  ? 2161 GLU A CA    1 
ATOM   5847  C  C     . GLU A 1 944  ? 150.209 166.344 154.378 1.00 79.84  ? 2161 GLU A C     1 
ATOM   5848  O  O     . GLU A 1 944  ? 149.048 166.274 153.963 1.00 82.13  ? 2161 GLU A O     1 
ATOM   5849  C  CB    . GLU A 1 944  ? 150.953 164.084 155.381 1.00 81.77  ? 2161 GLU A CB    1 
ATOM   5850  C  CG    . GLU A 1 944  ? 149.640 163.279 155.479 1.00 86.58  ? 2161 GLU A CG    1 
ATOM   5851  C  CD    . GLU A 1 944  ? 148.430 164.075 155.911 1.00 89.62  ? 2161 GLU A CD    1 
ATOM   5852  O  OE1   . GLU A 1 944  ? 147.300 163.560 155.786 1.00 91.98  ? 2161 GLU A OE1   1 
ATOM   5853  O  OE2   . GLU A 1 944  ? 148.612 165.160 156.489 1.00 87.56  ? 2161 GLU A OE2   1 
ATOM   5854  N  N     . TYR A 1 945  ? 150.717 167.464 154.899 1.00 79.26  ? 2162 TYR A N     1 
ATOM   5855  C  CA    . TYR A 1 945  ? 149.957 168.709 154.877 1.00 80.89  ? 2162 TYR A CA    1 
ATOM   5856  C  C     . TYR A 1 945  ? 149.979 169.363 153.499 1.00 78.02  ? 2162 TYR A C     1 
ATOM   5857  O  O     . TYR A 1 945  ? 148.982 169.965 153.083 1.00 75.55  ? 2162 TYR A O     1 
ATOM   5858  C  CB    . TYR A 1 945  ? 150.502 169.683 155.921 1.00 81.02  ? 2162 TYR A CB    1 
ATOM   5859  C  CG    . TYR A 1 945  ? 149.953 169.488 157.316 1.00 77.11  ? 2162 TYR A CG    1 
ATOM   5860  C  CD1   . TYR A 1 945  ? 150.343 168.407 158.096 1.00 72.87  ? 2162 TYR A CD1   1 
ATOM   5861  C  CD2   . TYR A 1 945  ? 149.045 170.390 157.853 1.00 73.08  ? 2162 TYR A CD2   1 
ATOM   5862  C  CE1   . TYR A 1 945  ? 149.843 168.232 159.371 1.00 72.21  ? 2162 TYR A CE1   1 
ATOM   5863  C  CE2   . TYR A 1 945  ? 148.540 170.223 159.126 1.00 67.53  ? 2162 TYR A CE2   1 
ATOM   5864  C  CZ    . TYR A 1 945  ? 148.941 169.142 159.880 1.00 70.37  ? 2162 TYR A CZ    1 
ATOM   5865  O  OH    . TYR A 1 945  ? 148.439 168.973 161.149 1.00 69.43  ? 2162 TYR A OH    1 
ATOM   5866  N  N     . VAL A 1 946  ? 151.102 169.267 152.776 1.00 78.43  ? 2163 VAL A N     1 
ATOM   5867  C  CA    . VAL A 1 946  ? 151.220 169.955 151.490 1.00 79.56  ? 2163 VAL A CA    1 
ATOM   5868  C  C     . VAL A 1 946  ? 150.650 169.121 150.347 1.00 81.66  ? 2163 VAL A C     1 
ATOM   5869  O  O     . VAL A 1 946  ? 150.512 169.631 149.223 1.00 82.38  ? 2163 VAL A O     1 
ATOM   5870  C  CB    . VAL A 1 946  ? 152.689 170.349 151.207 1.00 83.38  ? 2163 VAL A CB    1 
ATOM   5871  C  CG1   . VAL A 1 946  ? 153.531 169.140 150.820 1.00 79.79  ? 2163 VAL A CG1   1 
ATOM   5872  C  CG2   . VAL A 1 946  ? 152.799 171.490 150.185 1.00 82.17  ? 2163 VAL A CG2   1 
ATOM   5873  N  N     . GLU A 1 947  ? 150.292 167.857 150.595 1.00 83.25  ? 2164 GLU A N     1 
ATOM   5874  C  CA    . GLU A 1 947  ? 149.575 167.096 149.575 1.00 83.00  ? 2164 GLU A CA    1 
ATOM   5875  C  C     . GLU A 1 947  ? 148.219 167.718 149.258 1.00 85.65  ? 2164 GLU A C     1 
ATOM   5876  O  O     . GLU A 1 947  ? 147.747 167.625 148.120 1.00 91.13  ? 2164 GLU A O     1 
ATOM   5877  C  CB    . GLU A 1 947  ? 149.400 165.641 150.008 1.00 85.09  ? 2164 GLU A CB    1 
ATOM   5878  C  CG    . GLU A 1 947  ? 150.694 164.851 150.063 1.00 86.26  ? 2164 GLU A CG    1 
ATOM   5879  C  CD    . GLU A 1 947  ? 151.325 164.668 148.697 1.00 88.35  ? 2164 GLU A CD    1 
ATOM   5880  O  OE1   . GLU A 1 947  ? 150.578 164.577 147.700 1.00 94.27  ? 2164 GLU A OE1   1 
ATOM   5881  O  OE2   . GLU A 1 947  ? 152.570 164.622 148.619 1.00 84.86  ? 2164 GLU A OE2   1 
ATOM   5882  N  N     . ALA A 1 948  ? 147.581 168.352 150.242 1.00 85.17  ? 2165 ALA A N     1 
ATOM   5883  C  CA    . ALA A 1 948  ? 146.361 169.112 150.005 1.00 84.65  ? 2165 ALA A CA    1 
ATOM   5884  C  C     . ALA A 1 948  ? 146.634 170.561 149.623 1.00 80.82  ? 2165 ALA A C     1 
ATOM   5885  O  O     . ALA A 1 948  ? 145.697 171.281 149.264 1.00 77.53  ? 2165 ALA A O     1 
ATOM   5886  C  CB    . ALA A 1 948  ? 145.462 169.071 151.245 1.00 82.81  ? 2165 ALA A CB    1 
ATOM   5887  N  N     . MET A 1 949  ? 147.890 170.999 149.695 1.00 80.57  ? 2166 MET A N     1 
ATOM   5888  C  CA    . MET A 1 949  ? 148.284 172.349 149.321 1.00 83.82  ? 2166 MET A CA    1 
ATOM   5889  C  C     . MET A 1 949  ? 148.804 172.431 147.892 1.00 87.59  ? 2166 MET A C     1 
ATOM   5890  O  O     . MET A 1 949  ? 148.911 173.535 147.348 1.00 90.96  ? 2166 MET A O     1 
ATOM   5891  C  CB    . MET A 1 949  ? 149.367 172.854 150.288 1.00 83.12  ? 2166 MET A CB    1 
ATOM   5892  C  CG    . MET A 1 949  ? 149.532 174.361 150.404 1.00 75.41  ? 2166 MET A CG    1 
ATOM   5893  S  SD    . MET A 1 949  ? 147.999 175.295 150.300 1.00 66.20  ? 2166 MET A SD    1 
ATOM   5894  C  CE    . MET A 1 949  ? 147.333 175.048 151.942 1.00 67.44  ? 2166 MET A CE    1 
ATOM   5895  N  N     . ASN A 1 950  ? 149.138 171.286 147.290 1.00 85.33  ? 2167 ASN A N     1 
ATOM   5896  C  CA    . ASN A 1 950  ? 149.729 171.270 145.953 1.00 86.22  ? 2167 ASN A CA    1 
ATOM   5897  C  C     . ASN A 1 950  ? 148.770 171.819 144.902 1.00 87.44  ? 2167 ASN A C     1 
ATOM   5898  O  O     . ASN A 1 950  ? 149.158 172.641 144.063 1.00 84.60  ? 2167 ASN A O     1 
ATOM   5899  C  CB    . ASN A 1 950  ? 150.155 169.847 145.593 1.00 85.82  ? 2167 ASN A CB    1 
ATOM   5900  C  CG    . ASN A 1 950  ? 151.479 169.804 144.860 1.00 89.42  ? 2167 ASN A CG    1 
ATOM   5901  O  OD1   . ASN A 1 950  ? 152.320 170.688 145.022 1.00 93.67  ? 2167 ASN A OD1   1 
ATOM   5902  N  ND2   . ASN A 1 950  ? 151.671 168.775 144.044 1.00 86.72  ? 2167 ASN A ND2   1 
ATOM   5903  N  N     . SER A 1 951  ? 147.512 171.368 144.923 1.00 91.26  ? 2168 SER A N     1 
ATOM   5904  C  CA    . SER A 1 951  ? 146.539 171.859 143.951 1.00 91.40  ? 2168 SER A CA    1 
ATOM   5905  C  C     . SER A 1 951  ? 146.207 173.325 144.189 1.00 90.43  ? 2168 SER A C     1 
ATOM   5906  O  O     . SER A 1 951  ? 145.887 174.050 143.240 1.00 91.13  ? 2168 SER A O     1 
ATOM   5907  C  CB    . SER A 1 951  ? 145.269 171.012 143.997 1.00 91.33  ? 2168 SER A CB    1 
ATOM   5908  O  OG    . SER A 1 951  ? 144.305 171.495 143.077 1.00 87.26  ? 2168 SER A OG    1 
ATOM   5909  N  N     . VAL A 1 952  ? 146.274 173.770 145.445 1.00 92.53  ? 2169 VAL A N     1 
ATOM   5910  C  CA    . VAL A 1 952  ? 146.166 175.192 145.751 1.00 91.81  ? 2169 VAL A CA    1 
ATOM   5911  C  C     . VAL A 1 952  ? 147.313 175.955 145.107 1.00 90.84  ? 2169 VAL A C     1 
ATOM   5912  O  O     . VAL A 1 952  ? 147.129 177.050 144.563 1.00 91.96  ? 2169 VAL A O     1 
ATOM   5913  C  CB    . VAL A 1 952  ? 146.139 175.399 147.275 1.00 90.56  ? 2169 VAL A CB    1 
ATOM   5914  C  CG1   . VAL A 1 952  ? 145.734 176.819 147.622 1.00 88.88  ? 2169 VAL A CG1   1 
ATOM   5915  C  CG2   . VAL A 1 952  ? 145.230 174.374 147.940 1.00 86.17  ? 2169 VAL A CG2   1 
ATOM   5916  N  N     . LEU A 1 953  ? 148.515 175.390 145.167 1.00 88.91  ? 2170 LEU A N     1 
ATOM   5917  C  CA    . LEU A 1 953  ? 149.702 175.987 144.573 1.00 88.33  ? 2170 LEU A CA    1 
ATOM   5918  C  C     . LEU A 1 953  ? 149.853 175.674 143.093 1.00 92.39  ? 2170 LEU A C     1 
ATOM   5919  O  O     . LEU A 1 953  ? 150.804 176.160 142.471 1.00 93.39  ? 2170 LEU A O     1 
ATOM   5920  C  CB    . LEU A 1 953  ? 150.954 175.525 145.321 1.00 88.39  ? 2170 LEU A CB    1 
ATOM   5921  C  CG    . LEU A 1 953  ? 151.410 176.401 146.485 1.00 82.22  ? 2170 LEU A CG    1 
ATOM   5922  C  CD1   . LEU A 1 953  ? 151.754 177.746 145.905 1.00 81.14  ? 2170 LEU A CD1   1 
ATOM   5923  C  CD2   . LEU A 1 953  ? 150.376 176.539 147.587 1.00 82.54  ? 2170 LEU A CD2   1 
ATOM   5924  N  N     . ASP A 1 954  ? 148.954 174.881 142.519 1.00 96.37  ? 2171 ASP A N     1 
ATOM   5925  C  CA    . ASP A 1 954  ? 149.050 174.540 141.110 1.00 99.33  ? 2171 ASP A CA    1 
ATOM   5926  C  C     . ASP A 1 954  ? 148.706 175.752 140.245 1.00 99.17  ? 2171 ASP A C     1 
ATOM   5927  O  O     . ASP A 1 954  ? 148.226 176.783 140.725 1.00 95.60  ? 2171 ASP A O     1 
ATOM   5928  C  CB    . ASP A 1 954  ? 148.129 173.365 140.783 1.00 98.96  ? 2171 ASP A CB    1 
ATOM   5929  C  CG    . ASP A 1 954  ? 148.612 172.561 139.593 1.00 98.27  ? 2171 ASP A CG    1 
ATOM   5930  O  OD1   . ASP A 1 954  ? 149.712 172.861 139.082 1.00 98.51  ? 2171 ASP A OD1   1 
ATOM   5931  O  OD2   . ASP A 1 954  ? 147.893 171.632 139.169 1.00 98.09  ? 2171 ASP A OD2   1 
ATOM   5932  N  N     . ASP A 1 955  ? 148.966 175.615 138.942 1.00 101.22 ? 2172 ASP A N     1 
ATOM   5933  C  CA    . ASP A 1 955  ? 148.700 176.692 137.995 1.00 103.50 ? 2172 ASP A CA    1 
ATOM   5934  C  C     . ASP A 1 955  ? 147.218 177.027 137.887 1.00 102.75 ? 2172 ASP A C     1 
ATOM   5935  O  O     . ASP A 1 955  ? 146.876 178.125 137.437 1.00 102.72 ? 2172 ASP A O     1 
ATOM   5936  C  CB    . ASP A 1 955  ? 149.250 176.321 136.617 1.00 103.39 ? 2172 ASP A CB    1 
ATOM   5937  C  CG    . ASP A 1 955  ? 148.801 174.945 136.160 1.00 106.84 ? 2172 ASP A CG    1 
ATOM   5938  O  OD1   . ASP A 1 955  ? 148.131 174.242 136.945 1.00 101.57 ? 2172 ASP A OD1   1 
ATOM   5939  O  OD2   . ASP A 1 955  ? 149.118 174.566 135.013 1.00 116.12 ? 2172 ASP A OD2   1 
ATOM   5940  N  N     . ASN A 1 956  ? 146.336 176.108 138.284 1.00 99.01  ? 2173 ASN A N     1 
ATOM   5941  C  CA    . ASN A 1 956  ? 144.905 176.377 138.216 1.00 97.84  ? 2173 ASN A CA    1 
ATOM   5942  C  C     . ASN A 1 956  ? 144.468 177.396 139.262 1.00 97.72  ? 2173 ASN A C     1 
ATOM   5943  O  O     . ASN A 1 956  ? 143.434 178.051 139.082 1.00 95.63  ? 2173 ASN A O     1 
ATOM   5944  C  CB    . ASN A 1 956  ? 144.124 175.076 138.390 1.00 95.60  ? 2173 ASN A CB    1 
ATOM   5945  C  CG    . ASN A 1 956  ? 144.345 174.105 137.250 1.00 101.24 ? 2173 ASN A CG    1 
ATOM   5946  O  OD1   . ASN A 1 956  ? 144.382 174.497 136.084 1.00 106.76 ? 2173 ASN A OD1   1 
ATOM   5947  N  ND2   . ASN A 1 956  ? 144.493 172.828 137.581 1.00 102.24 ? 2173 ASN A ND2   1 
ATOM   5948  N  N     . LYS A 1 957  ? 145.244 177.546 140.342 1.00 96.05  ? 2174 LYS A N     1 
ATOM   5949  C  CA    . LYS A 1 957  ? 144.900 178.409 141.479 1.00 92.28  ? 2174 LYS A CA    1 
ATOM   5950  C  C     . LYS A 1 957  ? 143.523 178.059 142.040 1.00 89.18  ? 2174 LYS A C     1 
ATOM   5951  O  O     . LYS A 1 957  ? 142.689 178.929 142.297 1.00 86.50  ? 2174 LYS A O     1 
ATOM   5952  C  CB    . LYS A 1 957  ? 144.983 179.892 141.104 1.00 89.88  ? 2174 LYS A CB    1 
ATOM   5953  C  CG    . LYS A 1 957  ? 146.250 180.281 140.357 1.00 88.57  ? 2174 LYS A CG    1 
ATOM   5954  C  CD    . LYS A 1 957  ? 147.495 179.978 141.176 1.00 87.70  ? 2174 LYS A CD    1 
ATOM   5955  C  CE    . LYS A 1 957  ? 147.577 180.861 142.410 1.00 82.61  ? 2174 LYS A CE    1 
ATOM   5956  N  NZ    . LYS A 1 957  ? 148.348 180.212 143.508 1.00 86.88  ? 2174 LYS A NZ    1 
ATOM   5957  N  N     . ILE A 1 958  ? 143.286 176.764 142.231 1.00 88.82  ? 2175 ILE A N     1 
ATOM   5958  C  CA    . ILE A 1 958  ? 141.988 176.241 142.633 1.00 90.15  ? 2175 ILE A CA    1 
ATOM   5959  C  C     . ILE A 1 958  ? 142.202 175.363 143.861 1.00 92.31  ? 2175 ILE A C     1 
ATOM   5960  O  O     . ILE A 1 958  ? 143.293 174.816 144.052 1.00 92.99  ? 2175 ILE A O     1 
ATOM   5961  C  CB    . ILE A 1 958  ? 141.325 175.455 141.481 1.00 93.72  ? 2175 ILE A CB    1 
ATOM   5962  C  CG1   . ILE A 1 958  ? 139.858 175.147 141.770 1.00 89.70  ? 2175 ILE A CG1   1 
ATOM   5963  C  CG2   . ILE A 1 958  ? 142.065 174.154 141.207 1.00 95.14  ? 2175 ILE A CG2   1 
ATOM   5964  C  CD1   . ILE A 1 958  ? 139.114 174.675 140.542 1.00 80.08  ? 2175 ILE A CD1   1 
ATOM   5965  N  N     . LEU A 1 959  ? 141.184 175.262 144.711 1.00 90.20  ? 2176 LEU A N     1 
ATOM   5966  C  CA    . LEU A 1 959  ? 141.291 174.440 145.909 1.00 89.50  ? 2176 LEU A CA    1 
ATOM   5967  C  C     . LEU A 1 959  ? 140.379 173.226 145.816 1.00 91.45  ? 2176 LEU A C     1 
ATOM   5968  O  O     . LEU A 1 959  ? 139.228 173.324 145.384 1.00 95.00  ? 2176 LEU A O     1 
ATOM   5969  C  CB    . LEU A 1 959  ? 140.954 175.246 147.165 1.00 89.20  ? 2176 LEU A CB    1 
ATOM   5970  C  CG    . LEU A 1 959  ? 142.031 176.182 147.723 1.00 88.09  ? 2176 LEU A CG    1 
ATOM   5971  C  CD1   . LEU A 1 959  ? 142.235 177.411 146.849 1.00 89.54  ? 2176 LEU A CD1   1 
ATOM   5972  C  CD2   . LEU A 1 959  ? 141.720 176.567 149.163 1.00 79.69  ? 2176 LEU A CD2   1 
ATOM   5973  N  N     . THR A 1 960  ? 140.904 172.078 146.232 1.00 89.99  ? 2177 THR A N     1 
ATOM   5974  C  CA    . THR A 1 960  ? 140.164 170.825 146.218 1.00 92.37  ? 2177 THR A CA    1 
ATOM   5975  C  C     . THR A 1 960  ? 139.574 170.589 147.602 1.00 94.61  ? 2177 THR A C     1 
ATOM   5976  O  O     . THR A 1 960  ? 140.306 170.546 148.597 1.00 92.99  ? 2177 THR A O     1 
ATOM   5977  C  CB    . THR A 1 960  ? 141.065 169.660 145.807 1.00 90.38  ? 2177 THR A CB    1 
ATOM   5978  O  OG1   . THR A 1 960  ? 142.125 169.512 146.759 1.00 90.72  ? 2177 THR A OG1   1 
ATOM   5979  C  CG2   . THR A 1 960  ? 141.662 169.911 144.433 1.00 89.22  ? 2177 THR A CG2   1 
ATOM   5980  N  N     . LEU A 1 961  ? 138.255 170.443 147.661 1.00 96.46  ? 2178 LEU A N     1 
ATOM   5981  C  CA    . LEU A 1 961  ? 137.521 170.236 148.894 1.00 97.99  ? 2178 LEU A CA    1 
ATOM   5982  C  C     . LEU A 1 961  ? 136.691 168.961 148.796 1.00 101.39 ? 2178 LEU A C     1 
ATOM   5983  O  O     . LEU A 1 961  ? 136.290 168.562 147.697 1.00 102.81 ? 2178 LEU A O     1 
ATOM   5984  C  CB    . LEU A 1 961  ? 136.597 171.425 149.196 1.00 96.03  ? 2178 LEU A CB    1 
ATOM   5985  C  CG    . LEU A 1 961  ? 137.109 172.552 150.099 1.00 89.22  ? 2178 LEU A CG    1 
ATOM   5986  C  CD1   . LEU A 1 961  ? 138.326 173.246 149.506 1.00 86.59  ? 2178 LEU A CD1   1 
ATOM   5987  C  CD2   . LEU A 1 961  ? 136.000 173.557 150.370 1.00 89.61  ? 2178 LEU A CD2   1 
ATOM   5988  N  N     . PRO A 1 962  ? 136.445 168.284 149.922 1.00 102.52 ? 2179 PRO A N     1 
ATOM   5989  C  CA    . PRO A 1 962  ? 135.640 167.051 149.874 1.00 100.97 ? 2179 PRO A CA    1 
ATOM   5990  C  C     . PRO A 1 962  ? 134.219 167.256 149.376 1.00 99.54  ? 2179 PRO A C     1 
ATOM   5991  O  O     . PRO A 1 962  ? 133.667 166.357 148.730 1.00 99.11  ? 2179 PRO A O     1 
ATOM   5992  C  CB    . PRO A 1 962  ? 135.661 166.568 151.331 1.00 105.01 ? 2179 PRO A CB    1 
ATOM   5993  C  CG    . PRO A 1 962  ? 136.902 167.168 151.907 1.00 106.03 ? 2179 PRO A CG    1 
ATOM   5994  C  CD    . PRO A 1 962  ? 137.028 168.510 151.255 1.00 103.32 ? 2179 PRO A CD    1 
ATOM   5995  N  N     . ASN A 1 963  ? 133.607 168.409 149.649 1.00 98.79  ? 2180 ASN A N     1 
ATOM   5996  C  CA    . ASN A 1 963  ? 132.222 168.635 149.255 1.00 100.44 ? 2180 ASN A CA    1 
ATOM   5997  C  C     . ASN A 1 963  ? 132.066 168.998 147.784 1.00 100.41 ? 2180 ASN A C     1 
ATOM   5998  O  O     . ASN A 1 963  ? 130.935 169.018 147.286 1.00 99.77  ? 2180 ASN A O     1 
ATOM   5999  C  CB    . ASN A 1 963  ? 131.594 169.730 150.124 1.00 100.45 ? 2180 ASN A CB    1 
ATOM   6000  C  CG    . ASN A 1 963  ? 132.236 171.089 149.913 1.00 98.13  ? 2180 ASN A CG    1 
ATOM   6001  O  OD1   . ASN A 1 963  ? 133.364 171.191 149.433 1.00 99.28  ? 2180 ASN A OD1   1 
ATOM   6002  N  ND2   . ASN A 1 963  ? 131.513 172.144 150.271 1.00 93.60  ? 2180 ASN A ND2   1 
ATOM   6003  N  N     . GLY A 1 964  ? 133.159 169.283 147.080 1.00 97.96  ? 2181 GLY A N     1 
ATOM   6004  C  CA    . GLY A 1 964  ? 133.099 169.640 145.679 1.00 96.40  ? 2181 GLY A CA    1 
ATOM   6005  C  C     . GLY A 1 964  ? 133.211 171.119 145.380 1.00 96.51  ? 2181 GLY A C     1 
ATOM   6006  O  O     . GLY A 1 964  ? 133.264 171.489 144.200 1.00 97.49  ? 2181 GLY A O     1 
ATOM   6007  N  N     . GLU A 1 965  ? 133.243 171.973 146.399 1.00 93.41  ? 2182 GLU A N     1 
ATOM   6008  C  CA    . GLU A 1 965  ? 133.384 173.404 146.172 1.00 92.13  ? 2182 GLU A CA    1 
ATOM   6009  C  C     . GLU A 1 965  ? 134.785 173.731 145.666 1.00 93.66  ? 2182 GLU A C     1 
ATOM   6010  O  O     . GLU A 1 965  ? 135.782 173.189 146.150 1.00 93.43  ? 2182 GLU A O     1 
ATOM   6011  C  CB    . GLU A 1 965  ? 133.088 174.176 147.460 1.00 90.11  ? 2182 GLU A CB    1 
ATOM   6012  C  CG    . GLU A 1 965  ? 133.381 175.672 147.396 1.00 88.22  ? 2182 GLU A CG    1 
ATOM   6013  C  CD    . GLU A 1 965  ? 132.263 176.473 146.752 1.00 86.16  ? 2182 GLU A CD    1 
ATOM   6014  O  OE1   . GLU A 1 965  ? 131.256 175.870 146.324 1.00 87.32  ? 2182 GLU A OE1   1 
ATOM   6015  O  OE2   . GLU A 1 965  ? 132.393 177.713 146.671 1.00 85.14  ? 2182 GLU A OE2   1 
ATOM   6016  N  N     . ARG A 1 966  ? 134.854 174.620 144.677 1.00 92.62  ? 2183 ARG A N     1 
ATOM   6017  C  CA    . ARG A 1 966  ? 136.112 175.068 144.089 1.00 89.92  ? 2183 ARG A CA    1 
ATOM   6018  C  C     . ARG A 1 966  ? 136.261 176.562 144.353 1.00 86.35  ? 2183 ARG A C     1 
ATOM   6019  O  O     . ARG A 1 966  ? 135.414 177.359 143.935 1.00 83.67  ? 2183 ARG A O     1 
ATOM   6020  C  CB    . ARG A 1 966  ? 136.148 174.764 142.595 1.00 94.62  ? 2183 ARG A CB    1 
ATOM   6021  C  CG    . ARG A 1 966  ? 135.817 173.321 142.241 1.00 96.60  ? 2183 ARG A CG    1 
ATOM   6022  C  CD    . ARG A 1 966  ? 137.009 172.402 142.469 1.00 92.14  ? 2183 ARG A CD    1 
ATOM   6023  N  NE    . ARG A 1 966  ? 136.989 171.787 143.790 1.00 92.80  ? 2183 ARG A NE    1 
ATOM   6024  C  CZ    . ARG A 1 966  ? 136.307 170.692 144.094 1.00 92.34  ? 2183 ARG A CZ    1 
ATOM   6025  N  NH1   . ARG A 1 966  ? 135.574 170.061 143.191 1.00 94.99  ? 2183 ARG A NH1   1 
ATOM   6026  N  NH2   . ARG A 1 966  ? 136.362 170.216 145.334 1.00 91.64  ? 2183 ARG A NH2   1 
ATOM   6027  N  N     . LEU A 1 967  ? 137.340 176.938 145.039 1.00 87.62  ? 2184 LEU A N     1 
ATOM   6028  C  CA    . LEU A 1 967  ? 137.562 178.323 145.428 1.00 86.26  ? 2184 LEU A CA    1 
ATOM   6029  C  C     . LEU A 1 967  ? 138.708 178.911 144.624 1.00 82.74  ? 2184 LEU A C     1 
ATOM   6030  O  O     . LEU A 1 967  ? 139.838 178.404 144.715 1.00 82.93  ? 2184 LEU A O     1 
ATOM   6031  C  CB    . LEU A 1 967  ? 137.862 178.420 146.919 1.00 87.34  ? 2184 LEU A CB    1 
ATOM   6032  C  CG    . LEU A 1 967  ? 136.740 178.025 147.883 1.00 86.28  ? 2184 LEU A CG    1 
ATOM   6033  C  CD1   . LEU A 1 967  ? 136.918 176.596 148.375 1.00 86.05  ? 2184 LEU A CD1   1 
ATOM   6034  C  CD2   . LEU A 1 967  ? 136.682 178.992 149.053 1.00 79.60  ? 2184 LEU A CD2   1 
ATOM   6035  N  N     . PRO A 1 968  ? 138.480 179.954 143.832 1.00 82.44  ? 2185 PRO A N     1 
ATOM   6036  C  CA    . PRO A 1 968  ? 139.582 180.577 143.096 1.00 84.51  ? 2185 PRO A CA    1 
ATOM   6037  C  C     . PRO A 1 968  ? 140.464 181.411 144.011 1.00 82.85  ? 2185 PRO A C     1 
ATOM   6038  O  O     . PRO A 1 968  ? 140.063 181.842 145.094 1.00 80.52  ? 2185 PRO A O     1 
ATOM   6039  C  CB    . PRO A 1 968  ? 138.866 181.454 142.067 1.00 85.10  ? 2185 PRO A CB    1 
ATOM   6040  C  CG    . PRO A 1 968  ? 137.588 181.822 142.739 1.00 85.88  ? 2185 PRO A CG    1 
ATOM   6041  C  CD    . PRO A 1 968  ? 137.195 180.630 143.581 1.00 84.36  ? 2185 PRO A CD    1 
ATOM   6042  N  N     . ILE A 1 969  ? 141.687 181.639 143.551 1.00 78.59  ? 2186 ILE A N     1 
ATOM   6043  C  CA    . ILE A 1 969  ? 142.683 182.432 144.263 1.00 71.23  ? 2186 ILE A CA    1 
ATOM   6044  C  C     . ILE A 1 969  ? 142.873 183.744 143.511 1.00 66.62  ? 2186 ILE A C     1 
ATOM   6045  O  O     . ILE A 1 969  ? 143.295 183.728 142.347 1.00 66.65  ? 2186 ILE A O     1 
ATOM   6046  C  CB    . ILE A 1 969  ? 144.015 181.680 144.403 1.00 72.30  ? 2186 ILE A CB    1 
ATOM   6047  C  CG1   . ILE A 1 969  ? 143.827 180.424 145.251 1.00 76.34  ? 2186 ILE A CG1   1 
ATOM   6048  C  CG2   . ILE A 1 969  ? 145.078 182.584 144.997 1.00 67.07  ? 2186 ILE A CG2   1 
ATOM   6049  C  CD1   . ILE A 1 969  ? 145.014 179.503 145.225 1.00 82.97  ? 2186 ILE A CD1   1 
ATOM   6050  N  N     . PRO A 1 970  ? 142.572 184.887 144.118 1.00 63.53  ? 2187 PRO A N     1 
ATOM   6051  C  CA    . PRO A 1 970  ? 142.800 186.175 143.454 1.00 61.28  ? 2187 PRO A CA    1 
ATOM   6052  C  C     . PRO A 1 970  ? 144.284 186.443 143.280 1.00 61.74  ? 2187 PRO A C     1 
ATOM   6053  O  O     . PRO A 1 970  ? 145.115 185.824 143.961 1.00 63.92  ? 2187 PRO A O     1 
ATOM   6054  C  CB    . PRO A 1 970  ? 142.158 187.188 144.418 1.00 59.17  ? 2187 PRO A CB    1 
ATOM   6055  C  CG    . PRO A 1 970  ? 141.237 186.385 145.275 1.00 61.75  ? 2187 PRO A CG    1 
ATOM   6056  C  CD    . PRO A 1 970  ? 141.874 185.041 145.404 1.00 62.50  ? 2187 PRO A CD    1 
ATOM   6057  N  N     . PRO A 1 971  ? 144.659 187.335 142.357 1.00 63.27  ? 2188 PRO A N     1 
ATOM   6058  C  CA    . PRO A 1 971  ? 146.087 187.657 142.187 1.00 65.59  ? 2188 PRO A CA    1 
ATOM   6059  C  C     . PRO A 1 971  ? 146.737 188.248 143.427 1.00 58.21  ? 2188 PRO A C     1 
ATOM   6060  O  O     . PRO A 1 971  ? 147.932 188.019 143.655 1.00 52.98  ? 2188 PRO A O     1 
ATOM   6061  C  CB    . PRO A 1 971  ? 146.085 188.657 141.021 1.00 68.22  ? 2188 PRO A CB    1 
ATOM   6062  C  CG    . PRO A 1 971  ? 144.806 188.403 140.299 1.00 66.23  ? 2188 PRO A CG    1 
ATOM   6063  C  CD    . PRO A 1 971  ? 143.820 188.013 141.354 1.00 62.37  ? 2188 PRO A CD    1 
ATOM   6064  N  N     . ASN A 1 972  ? 145.995 188.998 144.238 1.00 55.66  ? 2189 ASN A N     1 
ATOM   6065  C  CA    . ASN A 1 972  ? 146.544 189.624 145.432 1.00 52.81  ? 2189 ASN A CA    1 
ATOM   6066  C  C     . ASN A 1 972  ? 146.467 188.727 146.662 1.00 51.03  ? 2189 ASN A C     1 
ATOM   6067  O  O     . ASN A 1 972  ? 146.663 189.215 147.780 1.00 50.91  ? 2189 ASN A O     1 
ATOM   6068  C  CB    . ASN A 1 972  ? 145.829 190.950 145.708 1.00 53.48  ? 2189 ASN A CB    1 
ATOM   6069  C  CG    . ASN A 1 972  ? 144.349 190.771 145.975 1.00 52.93  ? 2189 ASN A CG    1 
ATOM   6070  O  OD1   . ASN A 1 972  ? 143.737 189.806 145.520 1.00 51.75  ? 2189 ASN A OD1   1 
ATOM   6071  N  ND2   . ASN A 1 972  ? 143.764 191.705 146.715 1.00 54.47  ? 2189 ASN A ND2   1 
ATOM   6072  N  N     . PHE A 1 973  ? 146.187 187.437 146.486 1.00 48.83  ? 2190 PHE A N     1 
ATOM   6073  C  CA    . PHE A 1 973  ? 146.138 186.475 147.589 1.00 44.10  ? 2190 PHE A CA    1 
ATOM   6074  C  C     . PHE A 1 973  ? 147.442 185.687 147.550 1.00 41.36  ? 2190 PHE A C     1 
ATOM   6075  O  O     . PHE A 1 973  ? 147.539 184.639 146.912 1.00 40.92  ? 2190 PHE A O     1 
ATOM   6076  C  CB    . PHE A 1 973  ? 144.914 185.573 147.466 1.00 47.37  ? 2190 PHE A CB    1 
ATOM   6077  C  CG    . PHE A 1 973  ? 144.739 184.609 148.608 1.00 42.67  ? 2190 PHE A CG    1 
ATOM   6078  C  CD1   . PHE A 1 973  ? 144.133 185.012 149.784 1.00 42.56  ? 2190 PHE A CD1   1 
ATOM   6079  C  CD2   . PHE A 1 973  ? 145.152 183.295 148.494 1.00 44.82  ? 2190 PHE A CD2   1 
ATOM   6080  C  CE1   . PHE A 1 973  ? 143.962 184.136 150.831 1.00 47.98  ? 2190 PHE A CE1   1 
ATOM   6081  C  CE2   . PHE A 1 973  ? 144.978 182.410 149.539 1.00 46.20  ? 2190 PHE A CE2   1 
ATOM   6082  C  CZ    . PHE A 1 973  ? 144.384 182.833 150.709 1.00 46.12  ? 2190 PHE A CZ    1 
ATOM   6083  N  N     . ARG A 1 974  ? 148.455 186.201 148.241 1.00 39.39  ? 2191 ARG A N     1 
ATOM   6084  C  CA    . ARG A 1 974  ? 149.803 185.650 148.188 1.00 36.35  ? 2191 ARG A CA    1 
ATOM   6085  C  C     . ARG A 1 974  ? 150.120 184.923 149.488 1.00 28.82  ? 2191 ARG A C     1 
ATOM   6086  O  O     . ARG A 1 974  ? 150.055 185.516 150.569 1.00 29.33  ? 2191 ARG A O     1 
ATOM   6087  C  CB    . ARG A 1 974  ? 150.831 186.749 147.917 1.00 36.24  ? 2191 ARG A CB    1 
ATOM   6088  C  CG    . ARG A 1 974  ? 151.131 186.947 146.437 1.00 43.32  ? 2191 ARG A CG    1 
ATOM   6089  C  CD    . ARG A 1 974  ? 151.834 188.263 146.160 1.00 39.35  ? 2191 ARG A CD    1 
ATOM   6090  N  NE    . ARG A 1 974  ? 150.949 189.411 146.303 1.00 37.93  ? 2191 ARG A NE    1 
ATOM   6091  C  CZ    . ARG A 1 974  ? 151.058 190.525 145.594 1.00 40.75  ? 2191 ARG A CZ    1 
ATOM   6092  N  NH1   . ARG A 1 974  ? 152.005 190.674 144.683 1.00 37.67  ? 2191 ARG A NH1   1 
ATOM   6093  N  NH2   . ARG A 1 974  ? 150.195 191.515 145.803 1.00 42.53  ? 2191 ARG A NH2   1 
ATOM   6094  N  N     . ILE A 1 975  ? 150.466 183.642 149.372 1.00 26.78  ? 2192 ILE A N     1 
ATOM   6095  C  CA    . ILE A 1 975  ? 150.882 182.832 150.511 1.00 24.95  ? 2192 ILE A CA    1 
ATOM   6096  C  C     . ILE A 1 975  ? 152.345 183.116 150.823 1.00 26.29  ? 2192 ILE A C     1 
ATOM   6097  O  O     . ILE A 1 975  ? 153.143 183.421 149.933 1.00 31.10  ? 2192 ILE A O     1 
ATOM   6098  C  CB    . ILE A 1 975  ? 150.648 181.336 150.216 1.00 28.31  ? 2192 ILE A CB    1 
ATOM   6099  C  CG1   . ILE A 1 975  ? 149.267 181.123 149.599 1.00 33.85  ? 2192 ILE A CG1   1 
ATOM   6100  C  CG2   . ILE A 1 975  ? 150.786 180.493 151.477 1.00 28.86  ? 2192 ILE A CG2   1 
ATOM   6101  C  CD1   . ILE A 1 975  ? 148.140 181.248 150.591 1.00 37.06  ? 2192 ILE A CD1   1 
ATOM   6102  N  N     . LEU A 1 976  ? 152.701 183.041 152.103 1.00 22.64  ? 2193 LEU A N     1 
ATOM   6103  C  CA    . LEU A 1 976  ? 154.090 183.105 152.535 1.00 18.01  ? 2193 LEU A CA    1 
ATOM   6104  C  C     . LEU A 1 976  ? 154.376 181.948 153.474 1.00 20.12  ? 2193 LEU A C     1 
ATOM   6105  O  O     . LEU A 1 976  ? 153.510 181.539 154.252 1.00 26.60  ? 2193 LEU A O     1 
ATOM   6106  C  CB    . LEU A 1 976  ? 154.424 184.424 153.239 1.00 15.89  ? 2193 LEU A CB    1 
ATOM   6107  C  CG    . LEU A 1 976  ? 154.769 185.651 152.398 1.00 15.47  ? 2193 LEU A CG    1 
ATOM   6108  C  CD1   . LEU A 1 976  ? 153.558 186.212 151.706 1.00 18.54  ? 2193 LEU A CD1   1 
ATOM   6109  C  CD2   . LEU A 1 976  ? 155.398 186.706 153.275 1.00 18.61  ? 2193 LEU A CD2   1 
ATOM   6110  N  N     . PHE A 1 977  ? 155.592 181.423 153.395 1.00 17.44  ? 2194 PHE A N     1 
ATOM   6111  C  CA    . PHE A 1 977  ? 156.057 180.370 154.282 1.00 18.99  ? 2194 PHE A CA    1 
ATOM   6112  C  C     . PHE A 1 977  ? 157.279 180.868 155.036 1.00 19.87  ? 2194 PHE A C     1 
ATOM   6113  O  O     . PHE A 1 977  ? 158.031 181.706 154.531 1.00 23.51  ? 2194 PHE A O     1 
ATOM   6114  C  CB    . PHE A 1 977  ? 156.398 179.100 153.504 1.00 22.04  ? 2194 PHE A CB    1 
ATOM   6115  C  CG    . PHE A 1 977  ? 155.199 178.389 152.951 1.00 24.24  ? 2194 PHE A CG    1 
ATOM   6116  C  CD1   . PHE A 1 977  ? 154.457 177.534 153.745 1.00 28.89  ? 2194 PHE A CD1   1 
ATOM   6117  C  CD2   . PHE A 1 977  ? 154.815 178.577 151.636 1.00 26.44  ? 2194 PHE A CD2   1 
ATOM   6118  C  CE1   . PHE A 1 977  ? 153.354 176.876 153.236 1.00 34.21  ? 2194 PHE A CE1   1 
ATOM   6119  C  CE2   . PHE A 1 977  ? 153.713 177.923 151.121 1.00 30.24  ? 2194 PHE A CE2   1 
ATOM   6120  C  CZ    . PHE A 1 977  ? 152.982 177.072 151.923 1.00 33.03  ? 2194 PHE A CZ    1 
ATOM   6121  N  N     . GLU A 1 978  ? 157.473 180.357 156.248 1.00 18.74  ? 2195 GLU A N     1 
ATOM   6122  C  CA    . GLU A 1 978  ? 158.592 180.771 157.093 1.00 17.55  ? 2195 GLU A CA    1 
ATOM   6123  C  C     . GLU A 1 978  ? 159.061 179.544 157.867 1.00 21.40  ? 2195 GLU A C     1 
ATOM   6124  O  O     . GLU A 1 978  ? 158.431 179.149 158.851 1.00 25.84  ? 2195 GLU A O     1 
ATOM   6125  C  CB    . GLU A 1 978  ? 158.183 181.899 158.028 1.00 14.10  ? 2195 GLU A CB    1 
ATOM   6126  C  CG    . GLU A 1 978  ? 159.315 182.443 158.863 1.00 13.42  ? 2195 GLU A CG    1 
ATOM   6127  C  CD    . GLU A 1 978  ? 158.962 183.758 159.515 1.00 13.31  ? 2195 GLU A CD    1 
ATOM   6128  O  OE1   . GLU A 1 978  ? 158.871 184.772 158.795 1.00 12.70  ? 2195 GLU A OE1   1 
ATOM   6129  O  OE2   . GLU A 1 978  ? 158.784 183.785 160.751 1.00 12.69  ? 2195 GLU A OE2   1 
ATOM   6130  N  N     . THR A 1 979  ? 160.161 178.950 157.425 1.00 19.84  ? 2196 THR A N     1 
ATOM   6131  C  CA    . THR A 1 979  ? 160.665 177.706 157.988 1.00 21.33  ? 2196 THR A CA    1 
ATOM   6132  C  C     . THR A 1 979  ? 162.084 177.891 158.509 1.00 21.75  ? 2196 THR A C     1 
ATOM   6133  O  O     . THR A 1 979  ? 162.693 178.954 158.373 1.00 24.53  ? 2196 THR A O     1 
ATOM   6134  C  CB    . THR A 1 979  ? 160.638 176.587 156.947 1.00 24.59  ? 2196 THR A CB    1 
ATOM   6135  O  OG1   . THR A 1 979  ? 161.459 176.954 155.833 1.00 22.92  ? 2196 THR A OG1   1 
ATOM   6136  C  CG2   . THR A 1 979  ? 159.237 176.356 156.468 1.00 29.75  ? 2196 THR A CG2   1 
ATOM   6137  N  N     . ASP A 1 980  ? 162.606 176.824 159.112 1.00 22.48  ? 2197 ASP A N     1 
ATOM   6138  C  CA    . ASP A 1 980  ? 164.003 176.749 159.499 1.00 22.18  ? 2197 ASP A CA    1 
ATOM   6139  C  C     . ASP A 1 980  ? 164.744 175.567 158.889 1.00 27.33  ? 2197 ASP A C     1 
ATOM   6140  O  O     . ASP A 1 980  ? 165.977 175.533 158.958 1.00 29.53  ? 2197 ASP A O     1 
ATOM   6141  C  CB    . ASP A 1 980  ? 164.137 176.715 161.032 1.00 25.39  ? 2197 ASP A CB    1 
ATOM   6142  C  CG    . ASP A 1 980  ? 163.457 175.510 161.666 1.00 35.67  ? 2197 ASP A CG    1 
ATOM   6143  O  OD1   . ASP A 1 980  ? 162.823 174.708 160.948 1.00 37.93  ? 2197 ASP A OD1   1 
ATOM   6144  O  OD2   . ASP A 1 980  ? 163.561 175.363 162.902 1.00 34.85  ? 2197 ASP A OD2   1 
ATOM   6145  N  N     . ASN A 1 981  ? 164.035 174.606 158.303 1.00 31.90  ? 2198 ASN A N     1 
ATOM   6146  C  CA    . ASN A 1 981  ? 164.661 173.482 157.625 1.00 36.76  ? 2198 ASN A CA    1 
ATOM   6147  C  C     . ASN A 1 981  ? 163.706 172.964 156.561 1.00 41.84  ? 2198 ASN A C     1 
ATOM   6148  O  O     . ASN A 1 981  ? 162.493 173.174 156.633 1.00 44.25  ? 2198 ASN A O     1 
ATOM   6149  C  CB    . ASN A 1 981  ? 165.036 172.365 158.607 1.00 40.49  ? 2198 ASN A CB    1 
ATOM   6150  C  CG    . ASN A 1 981  ? 166.137 171.464 158.077 1.00 46.95  ? 2198 ASN A CG    1 
ATOM   6151  O  OD1   . ASN A 1 981  ? 166.139 171.086 156.905 1.00 48.58  ? 2198 ASN A OD1   1 
ATOM   6152  N  ND2   . ASN A 1 981  ? 167.083 171.117 158.942 1.00 46.88  ? 2198 ASN A ND2   1 
ATOM   6153  N  N     . LEU A 1 982  ? 164.270 172.274 155.574 1.00 46.33  ? 2199 LEU A N     1 
ATOM   6154  C  CA    . LEU A 1 982  ? 163.519 171.710 154.457 1.00 54.55  ? 2199 LEU A CA    1 
ATOM   6155  C  C     . LEU A 1 982  ? 163.803 170.221 154.332 1.00 57.10  ? 2199 LEU A C     1 
ATOM   6156  O  O     . LEU A 1 982  ? 164.056 169.694 153.247 1.00 59.29  ? 2199 LEU A O     1 
ATOM   6157  C  CB    . LEU A 1 982  ? 163.856 172.432 153.157 1.00 52.41  ? 2199 LEU A CB    1 
ATOM   6158  C  CG    . LEU A 1 982  ? 163.341 173.862 153.004 1.00 42.46  ? 2199 LEU A CG    1 
ATOM   6159  C  CD1   . LEU A 1 982  ? 164.047 174.542 151.852 1.00 31.56  ? 2199 LEU A CD1   1 
ATOM   6160  C  CD2   . LEU A 1 982  ? 161.842 173.874 152.791 1.00 45.52  ? 2199 LEU A CD2   1 
ATOM   6161  N  N     . ASP A 1 983  ? 163.769 169.520 155.467 1.00 58.23  ? 2200 ASP A N     1 
ATOM   6162  C  CA    . ASP A 1 983  ? 164.115 168.103 155.473 1.00 63.66  ? 2200 ASP A CA    1 
ATOM   6163  C  C     . ASP A 1 983  ? 163.030 167.254 154.821 1.00 67.08  ? 2200 ASP A C     1 
ATOM   6164  O  O     . ASP A 1 983  ? 163.335 166.285 154.115 1.00 71.91  ? 2200 ASP A O     1 
ATOM   6165  C  CB    . ASP A 1 983  ? 164.384 167.638 156.906 1.00 64.98  ? 2200 ASP A CB    1 
ATOM   6166  C  CG    . ASP A 1 983  ? 163.198 167.861 157.827 1.00 66.85  ? 2200 ASP A CG    1 
ATOM   6167  O  OD1   . ASP A 1 983  ? 162.313 168.670 157.478 1.00 68.49  ? 2200 ASP A OD1   1 
ATOM   6168  O  OD2   . ASP A 1 983  ? 163.149 167.223 158.899 1.00 65.97  ? 2200 ASP A OD2   1 
ATOM   6169  N  N     . HIS A 1 984  ? 161.761 167.597 155.040 1.00 64.18  ? 2201 HIS A N     1 
ATOM   6170  C  CA    . HIS A 1 984  ? 160.644 166.806 154.540 1.00 67.67  ? 2201 HIS A CA    1 
ATOM   6171  C  C     . HIS A 1 984  ? 159.909 167.476 153.386 1.00 70.00  ? 2201 HIS A C     1 
ATOM   6172  O  O     . HIS A 1 984  ? 158.787 167.076 153.065 1.00 73.85  ? 2201 HIS A O     1 
ATOM   6173  C  CB    . HIS A 1 984  ? 159.665 166.494 155.674 1.00 70.42  ? 2201 HIS A CB    1 
ATOM   6174  C  CG    . HIS A 1 984  ? 160.212 165.557 156.706 1.00 72.34  ? 2201 HIS A CG    1 
ATOM   6175  N  ND1   . HIS A 1 984  ? 161.558 165.288 156.826 1.00 71.39  ? 2201 HIS A ND1   1 
ATOM   6176  C  CD2   . HIS A 1 984  ? 159.597 164.837 157.674 1.00 74.15  ? 2201 HIS A CD2   1 
ATOM   6177  C  CE1   . HIS A 1 984  ? 161.748 164.437 157.818 1.00 71.76  ? 2201 HIS A CE1   1 
ATOM   6178  N  NE2   . HIS A 1 984  ? 160.574 164.146 158.349 1.00 73.13  ? 2201 HIS A NE2   1 
ATOM   6179  N  N     . THR A 1 985  ? 160.508 168.481 152.755 1.00 71.06  ? 2202 THR A N     1 
ATOM   6180  C  CA    . THR A 1 985  ? 159.887 169.153 151.622 1.00 76.16  ? 2202 THR A CA    1 
ATOM   6181  C  C     . THR A 1 985  ? 160.280 168.435 150.336 1.00 75.32  ? 2202 THR A C     1 
ATOM   6182  O  O     . THR A 1 985  ? 161.471 168.271 150.048 1.00 69.90  ? 2202 THR A O     1 
ATOM   6183  C  CB    . THR A 1 985  ? 160.298 170.623 151.570 1.00 72.44  ? 2202 THR A CB    1 
ATOM   6184  O  OG1   . THR A 1 985  ? 159.786 171.300 152.725 1.00 71.56  ? 2202 THR A OG1   1 
ATOM   6185  C  CG2   . THR A 1 985  ? 159.749 171.287 150.319 1.00 69.74  ? 2202 THR A CG2   1 
ATOM   6186  N  N     . THR A 1 986  ? 159.278 168.003 149.574 1.00 78.13  ? 2203 THR A N     1 
ATOM   6187  C  CA    . THR A 1 986  ? 159.526 167.301 148.328 1.00 77.66  ? 2203 THR A CA    1 
ATOM   6188  C  C     . THR A 1 986  ? 160.080 168.262 147.275 1.00 72.90  ? 2203 THR A C     1 
ATOM   6189  O  O     . THR A 1 986  ? 159.780 169.458 147.297 1.00 71.82  ? 2203 THR A O     1 
ATOM   6190  C  CB    . THR A 1 986  ? 158.241 166.658 147.813 1.00 79.65  ? 2203 THR A CB    1 
ATOM   6191  O  OG1   . THR A 1 986  ? 157.287 167.680 147.501 1.00 75.17  ? 2203 THR A OG1   1 
ATOM   6192  C  CG2   . THR A 1 986  ? 157.653 165.732 148.866 1.00 77.26  ? 2203 THR A CG2   1 
ATOM   6193  N  N     . PRO A 1 987  ? 160.894 167.761 146.340 1.00 68.31  ? 2204 PRO A N     1 
ATOM   6194  C  CA    . PRO A 1 987  ? 161.407 168.623 145.262 1.00 65.60  ? 2204 PRO A CA    1 
ATOM   6195  C  C     . PRO A 1 987  ? 160.350 169.101 144.276 1.00 69.15  ? 2204 PRO A C     1 
ATOM   6196  O  O     . PRO A 1 987  ? 160.695 169.821 143.333 1.00 68.39  ? 2204 PRO A O     1 
ATOM   6197  C  CB    . PRO A 1 987  ? 162.440 167.727 144.562 1.00 64.65  ? 2204 PRO A CB    1 
ATOM   6198  C  CG    . PRO A 1 987  ? 162.832 166.725 145.591 1.00 62.37  ? 2204 PRO A CG    1 
ATOM   6199  C  CD    . PRO A 1 987  ? 161.585 166.461 146.375 1.00 69.78  ? 2204 PRO A CD    1 
ATOM   6200  N  N     . ALA A 1 988  ? 159.083 168.720 144.442 1.00 72.51  ? 2205 ALA A N     1 
ATOM   6201  C  CA    . ALA A 1 988  ? 158.032 169.239 143.577 1.00 75.62  ? 2205 ALA A CA    1 
ATOM   6202  C  C     . ALA A 1 988  ? 157.653 170.671 143.930 1.00 75.92  ? 2205 ALA A C     1 
ATOM   6203  O  O     . ALA A 1 988  ? 157.181 171.413 143.061 1.00 75.65  ? 2205 ALA A O     1 
ATOM   6204  C  CB    . ALA A 1 988  ? 156.797 168.340 143.650 1.00 78.12  ? 2205 ALA A CB    1 
ATOM   6205  N  N     . THR A 1 989  ? 157.847 171.076 145.185 1.00 75.03  ? 2206 THR A N     1 
ATOM   6206  C  CA    . THR A 1 989  ? 157.427 172.391 145.648 1.00 75.81  ? 2206 THR A CA    1 
ATOM   6207  C  C     . THR A 1 989  ? 158.577 173.376 145.821 1.00 70.41  ? 2206 THR A C     1 
ATOM   6208  O  O     . THR A 1 989  ? 158.321 174.552 146.098 1.00 73.77  ? 2206 THR A O     1 
ATOM   6209  C  CB    . THR A 1 989  ? 156.669 172.267 146.975 1.00 81.58  ? 2206 THR A CB    1 
ATOM   6210  O  OG1   . THR A 1 989  ? 157.485 171.577 147.929 1.00 80.42  ? 2206 THR A OG1   1 
ATOM   6211  C  CG2   . THR A 1 989  ? 155.373 171.499 146.777 1.00 81.13  ? 2206 THR A CG2   1 
ATOM   6212  N  N     . ILE A 1 990  ? 159.829 172.932 145.677 1.00 66.44  ? 2207 ILE A N     1 
ATOM   6213  C  CA    . ILE A 1 990  ? 160.951 173.862 145.783 1.00 64.50  ? 2207 ILE A CA    1 
ATOM   6214  C  C     . ILE A 1 990  ? 160.980 174.812 144.592 1.00 67.04  ? 2207 ILE A C     1 
ATOM   6215  O  O     . ILE A 1 990  ? 161.401 175.967 144.722 1.00 64.11  ? 2207 ILE A O     1 
ATOM   6216  C  CB    . ILE A 1 990  ? 162.282 173.099 145.928 1.00 63.06  ? 2207 ILE A CB    1 
ATOM   6217  C  CG1   . ILE A 1 990  ? 162.454 172.096 144.786 1.00 64.53  ? 2207 ILE A CG1   1 
ATOM   6218  C  CG2   . ILE A 1 990  ? 162.353 172.404 147.279 1.00 62.27  ? 2207 ILE A CG2   1 
ATOM   6219  C  CD1   . ILE A 1 990  ? 163.806 171.431 144.740 1.00 52.66  ? 2207 ILE A CD1   1 
ATOM   6220  N  N     . THR A 1 991  ? 160.551 174.348 143.417 1.00 67.94  ? 2208 THR A N     1 
ATOM   6221  C  CA    . THR A 1 991  ? 160.489 175.189 142.231 1.00 69.79  ? 2208 THR A CA    1 
ATOM   6222  C  C     . THR A 1 991  ? 159.082 175.676 141.918 1.00 66.11  ? 2208 THR A C     1 
ATOM   6223  O  O     . THR A 1 991  ? 158.935 176.703 141.247 1.00 61.75  ? 2208 THR A O     1 
ATOM   6224  C  CB    . THR A 1 991  ? 161.054 174.441 141.013 1.00 68.84  ? 2208 THR A CB    1 
ATOM   6225  O  OG1   . THR A 1 991  ? 160.976 175.279 139.853 1.00 70.04  ? 2208 THR A OG1   1 
ATOM   6226  C  CG2   . THR A 1 991  ? 160.287 173.148 140.762 1.00 66.62  ? 2208 THR A CG2   1 
ATOM   6227  N  N     . ARG A 1 992  ? 158.051 174.965 142.380 1.00 67.75  ? 2209 ARG A N     1 
ATOM   6228  C  CA    . ARG A 1 992  ? 156.687 175.460 142.238 1.00 72.00  ? 2209 ARG A CA    1 
ATOM   6229  C  C     . ARG A 1 992  ? 156.472 176.709 143.083 1.00 68.16  ? 2209 ARG A C     1 
ATOM   6230  O  O     . ARG A 1 992  ? 155.845 177.675 142.631 1.00 64.48  ? 2209 ARG A O     1 
ATOM   6231  C  CB    . ARG A 1 992  ? 155.697 174.359 142.620 1.00 74.69  ? 2209 ARG A CB    1 
ATOM   6232  C  CG    . ARG A 1 992  ? 154.316 174.845 143.012 1.00 77.42  ? 2209 ARG A CG    1 
ATOM   6233  C  CD    . ARG A 1 992  ? 153.429 173.679 143.411 1.00 82.94  ? 2209 ARG A CD    1 
ATOM   6234  N  NE    . ARG A 1 992  ? 153.668 172.499 142.588 1.00 82.50  ? 2209 ARG A NE    1 
ATOM   6235  C  CZ    . ARG A 1 992  ? 153.032 172.235 141.455 1.00 84.20  ? 2209 ARG A CZ    1 
ATOM   6236  N  NH1   . ARG A 1 992  ? 152.112 173.053 140.971 1.00 82.86  ? 2209 ARG A NH1   1 
ATOM   6237  N  NH2   . ARG A 1 992  ? 153.327 171.121 140.791 1.00 89.34  ? 2209 ARG A NH2   1 
ATOM   6238  N  N     . CYS A 1 993  ? 157.002 176.714 144.302 1.00 67.58  ? 2210 CYS A N     1 
ATOM   6239  C  CA    . CYS A 1 993  ? 156.975 177.873 145.179 1.00 58.58  ? 2210 CYS A CA    1 
ATOM   6240  C  C     . CYS A 1 993  ? 158.322 178.580 145.137 1.00 50.41  ? 2210 CYS A C     1 
ATOM   6241  O  O     . CYS A 1 993  ? 159.367 177.950 144.960 1.00 49.26  ? 2210 CYS A O     1 
ATOM   6242  C  CB    . CYS A 1 993  ? 156.658 177.465 146.619 1.00 59.50  ? 2210 CYS A CB    1 
ATOM   6243  S  SG    . CYS A 1 993  ? 155.071 176.645 146.845 1.00 82.70  ? 2210 CYS A SG    1 
ATOM   6244  N  N     . GLY A 1 994  ? 158.289 179.899 145.288 1.00 43.12  ? 2211 GLY A N     1 
ATOM   6245  C  CA    . GLY A 1 994  ? 159.526 180.651 145.376 1.00 40.58  ? 2211 GLY A CA    1 
ATOM   6246  C  C     . GLY A 1 994  ? 160.245 180.363 146.683 1.00 37.05  ? 2211 GLY A C     1 
ATOM   6247  O  O     . GLY A 1 994  ? 159.632 180.265 147.746 1.00 38.16  ? 2211 GLY A O     1 
ATOM   6248  N  N     . LEU A 1 995  ? 161.566 180.223 146.600 1.00 34.68  ? 2212 LEU A N     1 
ATOM   6249  C  CA    . LEU A 1 995  ? 162.394 179.915 147.758 1.00 26.02  ? 2212 LEU A CA    1 
ATOM   6250  C  C     . LEU A 1 995  ? 163.378 181.051 147.990 1.00 22.46  ? 2212 LEU A C     1 
ATOM   6251  O  O     . LEU A 1 995  ? 164.168 181.383 147.100 1.00 24.34  ? 2212 LEU A O     1 
ATOM   6252  C  CB    . LEU A 1 995  ? 163.136 178.592 147.559 1.00 24.04  ? 2212 LEU A CB    1 
ATOM   6253  C  CG    . LEU A 1 995  ? 163.753 177.951 148.799 1.00 21.94  ? 2212 LEU A CG    1 
ATOM   6254  C  CD1   . LEU A 1 995  ? 163.589 176.448 148.724 1.00 30.50  ? 2212 LEU A CD1   1 
ATOM   6255  C  CD2   . LEU A 1 995  ? 165.218 178.320 148.940 1.00 21.46  ? 2212 LEU A CD2   1 
ATOM   6256  N  N     . LEU A 1 996  ? 163.333 181.637 149.182 1.00 19.20  ? 2213 LEU A N     1 
ATOM   6257  C  CA    . LEU A 1 996  ? 164.304 182.629 149.622 1.00 14.09  ? 2213 LEU A CA    1 
ATOM   6258  C  C     . LEU A 1 996  ? 165.077 182.048 150.797 1.00 14.22  ? 2213 LEU A C     1 
ATOM   6259  O  O     . LEU A 1 996  ? 164.476 181.512 151.734 1.00 16.80  ? 2213 LEU A O     1 
ATOM   6260  C  CB    . LEU A 1 996  ? 163.615 183.937 150.019 1.00 9.22   ? 2213 LEU A CB    1 
ATOM   6261  C  CG    . LEU A 1 996  ? 164.461 185.016 150.693 1.00 9.45   ? 2213 LEU A CG    1 
ATOM   6262  C  CD1   . LEU A 1 996  ? 165.648 185.389 149.834 1.00 11.77  ? 2213 LEU A CD1   1 
ATOM   6263  C  CD2   . LEU A 1 996  ? 163.619 186.240 150.979 1.00 10.85  ? 2213 LEU A CD2   1 
ATOM   6264  N  N     . TRP A 1 997  ? 166.400 182.146 150.744 1.00 12.24  ? 2214 TRP A N     1 
ATOM   6265  C  CA    . TRP A 1 997  ? 167.273 181.484 151.704 1.00 11.40  ? 2214 TRP A CA    1 
ATOM   6266  C  C     . TRP A 1 997  ? 167.968 182.522 152.572 1.00 14.55  ? 2214 TRP A C     1 
ATOM   6267  O  O     . TRP A 1 997  ? 168.599 183.448 152.054 1.00 14.92  ? 2214 TRP A O     1 
ATOM   6268  C  CB    . TRP A 1 997  ? 168.307 180.618 150.986 1.00 13.34  ? 2214 TRP A CB    1 
ATOM   6269  C  CG    . TRP A 1 997  ? 169.180 179.832 151.903 1.00 15.05  ? 2214 TRP A CG    1 
ATOM   6270  C  CD1   . TRP A 1 997  ? 170.388 180.208 152.408 1.00 17.75  ? 2214 TRP A CD1   1 
ATOM   6271  C  CD2   . TRP A 1 997  ? 168.921 178.521 152.413 1.00 14.49  ? 2214 TRP A CD2   1 
ATOM   6272  N  NE1   . TRP A 1 997  ? 170.894 179.216 153.210 1.00 18.40  ? 2214 TRP A NE1   1 
ATOM   6273  C  CE2   . TRP A 1 997  ? 170.012 178.169 153.229 1.00 16.19  ? 2214 TRP A CE2   1 
ATOM   6274  C  CE3   . TRP A 1 997  ? 167.870 177.614 152.264 1.00 15.08  ? 2214 TRP A CE3   1 
ATOM   6275  C  CZ2   . TRP A 1 997  ? 170.081 176.948 153.893 1.00 15.18  ? 2214 TRP A CZ2   1 
ATOM   6276  C  CZ3   . TRP A 1 997  ? 167.943 176.403 152.922 1.00 16.25  ? 2214 TRP A CZ3   1 
ATOM   6277  C  CH2   . TRP A 1 997  ? 169.038 176.081 153.728 1.00 15.64  ? 2214 TRP A CH2   1 
ATOM   6278  N  N     . PHE A 1 998  ? 167.848 182.361 153.887 1.00 16.55  ? 2215 PHE A N     1 
ATOM   6279  C  CA    . PHE A 1 998  ? 168.500 183.222 154.872 1.00 15.24  ? 2215 PHE A CA    1 
ATOM   6280  C  C     . PHE A 1 998  ? 169.670 182.438 155.461 1.00 17.73  ? 2215 PHE A C     1 
ATOM   6281  O  O     . PHE A 1 998  ? 169.519 181.710 156.442 1.00 18.59  ? 2215 PHE A O     1 
ATOM   6282  C  CB    . PHE A 1 998  ? 167.522 183.660 155.952 1.00 9.28   ? 2215 PHE A CB    1 
ATOM   6283  C  CG    . PHE A 1 998  ? 166.704 184.860 155.581 1.00 8.12   ? 2215 PHE A CG    1 
ATOM   6284  C  CD1   . PHE A 1 998  ? 167.185 186.136 155.807 1.00 10.79  ? 2215 PHE A CD1   1 
ATOM   6285  C  CD2   . PHE A 1 998  ? 165.453 184.712 155.013 1.00 8.23   ? 2215 PHE A CD2   1 
ATOM   6286  C  CE1   . PHE A 1 998  ? 166.435 187.243 155.471 1.00 12.85  ? 2215 PHE A CE1   1 
ATOM   6287  C  CE2   . PHE A 1 998  ? 164.701 185.814 154.674 1.00 8.68   ? 2215 PHE A CE2   1 
ATOM   6288  C  CZ    . PHE A 1 998  ? 165.193 187.081 154.903 1.00 10.67  ? 2215 PHE A CZ    1 
ATOM   6289  N  N     . SER A 1 999  ? 170.845 182.592 154.849 1.00 16.91  ? 2216 SER A N     1 
ATOM   6290  C  CA    . SER A 1 999  ? 172.015 181.839 155.281 1.00 18.58  ? 2216 SER A CA    1 
ATOM   6291  C  C     . SER A 1 999  ? 172.621 182.388 156.566 1.00 19.09  ? 2216 SER A C     1 
ATOM   6292  O  O     . SER A 1 999  ? 173.241 181.632 157.321 1.00 21.98  ? 2216 SER A O     1 
ATOM   6293  C  CB    . SER A 1 999  ? 173.068 181.830 154.173 1.00 26.23  ? 2216 SER A CB    1 
ATOM   6294  O  OG    . SER A 1 999  ? 173.572 183.133 153.941 1.00 30.24  ? 2216 SER A OG    1 
ATOM   6295  N  N     . THR A 1 1000 ? 172.459 183.681 156.835 1.00 17.28  ? 2217 THR A N     1 
ATOM   6296  C  CA    . THR A 1 1000 ? 173.071 184.294 158.004 1.00 18.92  ? 2217 THR A CA    1 
ATOM   6297  C  C     . THR A 1 1000 ? 172.148 185.376 158.544 1.00 20.13  ? 2217 THR A C     1 
ATOM   6298  O  O     . THR A 1 1000 ? 171.164 185.759 157.906 1.00 19.48  ? 2217 THR A O     1 
ATOM   6299  C  CB    . THR A 1 1000 ? 174.450 184.878 157.680 1.00 20.52  ? 2217 THR A CB    1 
ATOM   6300  O  OG1   . THR A 1 1000 ? 175.115 185.241 158.895 1.00 21.01  ? 2217 THR A OG1   1 
ATOM   6301  C  CG2   . THR A 1 1000 ? 174.311 186.111 156.806 1.00 21.35  ? 2217 THR A CG2   1 
ATOM   6302  N  N     . ASP A 1 1001 ? 172.479 185.859 159.739 1.00 18.77  ? 2218 ASP A N     1 
ATOM   6303  C  CA    . ASP A 1 1001 ? 171.698 186.903 160.384 1.00 16.18  ? 2218 ASP A CA    1 
ATOM   6304  C  C     . ASP A 1 1001 ? 171.766 188.202 159.591 1.00 19.08  ? 2218 ASP A C     1 
ATOM   6305  O  O     . ASP A 1 1001 ? 172.767 188.509 158.939 1.00 21.63  ? 2218 ASP A O     1 
ATOM   6306  C  CB    . ASP A 1 1001 ? 172.198 187.144 161.807 1.00 14.80  ? 2218 ASP A CB    1 
ATOM   6307  C  CG    . ASP A 1 1001 ? 172.081 185.916 162.682 1.00 15.65  ? 2218 ASP A CG    1 
ATOM   6308  O  OD1   . ASP A 1 1001 ? 171.733 184.840 162.152 1.00 16.49  ? 2218 ASP A OD1   1 
ATOM   6309  O  OD2   . ASP A 1 1001 ? 172.337 186.025 163.899 1.00 13.18  ? 2218 ASP A OD2   1 
ATOM   6310  N  N     . VAL A 1 1002 ? 170.684 188.969 159.656 1.00 17.82  ? 2219 VAL A N     1 
ATOM   6311  C  CA    . VAL A 1 1002 ? 170.589 190.237 158.951 1.00 17.54  ? 2219 VAL A CA    1 
ATOM   6312  C  C     . VAL A 1 1002 ? 170.996 191.404 159.850 1.00 17.40  ? 2219 VAL A C     1 
ATOM   6313  O  O     . VAL A 1 1002 ? 170.707 192.557 159.537 1.00 16.29  ? 2219 VAL A O     1 
ATOM   6314  C  CB    . VAL A 1 1002 ? 169.185 190.453 158.372 1.00 18.83  ? 2219 VAL A CB    1 
ATOM   6315  C  CG1   . VAL A 1 1002 ? 168.863 189.380 157.346 1.00 19.61  ? 2219 VAL A CG1   1 
ATOM   6316  C  CG2   . VAL A 1 1002 ? 168.153 190.472 159.484 1.00 15.68  ? 2219 VAL A CG2   1 
ATOM   6317  N  N     . CYS A 1 1003 ? 171.664 191.121 160.965 1.00 19.59  ? 2220 CYS A N     1 
ATOM   6318  C  CA    . CYS A 1 1003 ? 171.988 192.144 161.943 1.00 20.57  ? 2220 CYS A CA    1 
ATOM   6319  C  C     . CYS A 1 1003 ? 173.345 191.869 162.566 1.00 25.89  ? 2220 CYS A C     1 
ATOM   6320  O  O     . CYS A 1 1003 ? 173.865 190.752 162.522 1.00 26.44  ? 2220 CYS A O     1 
ATOM   6321  C  CB    . CYS A 1 1003 ? 170.944 192.211 163.059 1.00 17.33  ? 2220 CYS A CB    1 
ATOM   6322  S  SG    . CYS A 1 1003 ? 169.368 192.837 162.534 1.00 15.48  ? 2220 CYS A SG    1 
ATOM   6323  N  N     . SER A 1 1004 ? 173.913 192.920 163.143 1.00 24.77  ? 2221 SER A N     1 
ATOM   6324  C  CA    . SER A 1 1004 ? 174.942 192.772 164.150 1.00 23.55  ? 2221 SER A CA    1 
ATOM   6325  C  C     . SER A 1 1004 ? 174.261 192.574 165.501 1.00 25.10  ? 2221 SER A C     1 
ATOM   6326  O  O     . SER A 1 1004 ? 173.035 192.630 165.622 1.00 28.49  ? 2221 SER A O     1 
ATOM   6327  C  CB    . SER A 1 1004 ? 175.868 193.985 164.155 1.00 26.20  ? 2221 SER A CB    1 
ATOM   6328  O  OG    . SER A 1 1004 ? 175.122 195.189 164.197 1.00 26.23  ? 2221 SER A OG    1 
ATOM   6329  N  N     . ILE A 1 1005 ? 175.061 192.324 166.534 1.00 22.81  ? 2222 ILE A N     1 
ATOM   6330  C  CA    . ILE A 1 1005 ? 174.511 192.235 167.881 1.00 20.35  ? 2222 ILE A CA    1 
ATOM   6331  C  C     . ILE A 1 1005 ? 174.067 193.613 168.365 1.00 22.98  ? 2222 ILE A C     1 
ATOM   6332  O  O     . ILE A 1 1005 ? 173.012 193.758 169.000 1.00 23.46  ? 2222 ILE A O     1 
ATOM   6333  C  CB    . ILE A 1 1005 ? 175.533 191.582 168.834 1.00 21.28  ? 2222 ILE A CB    1 
ATOM   6334  C  CG1   . ILE A 1 1005 ? 175.828 190.127 168.436 1.00 21.12  ? 2222 ILE A CG1   1 
ATOM   6335  C  CG2   . ILE A 1 1005 ? 175.047 191.626 170.252 1.00 25.42  ? 2222 ILE A CG2   1 
ATOM   6336  C  CD1   . ILE A 1 1005 ? 176.977 189.927 167.460 1.00 22.68  ? 2222 ILE A CD1   1 
ATOM   6337  N  N     . SER A 1 1006 ? 174.845 194.649 168.041 1.00 23.56  ? 2223 SER A N     1 
ATOM   6338  C  CA    . SER A 1 1006 ? 174.535 196.000 168.500 1.00 27.52  ? 2223 SER A CA    1 
ATOM   6339  C  C     . SER A 1 1006 ? 173.236 196.522 167.894 1.00 25.03  ? 2223 SER A C     1 
ATOM   6340  O  O     . SER A 1 1006 ? 172.480 197.238 168.562 1.00 25.47  ? 2223 SER A O     1 
ATOM   6341  C  CB    . SER A 1 1006 ? 175.694 196.936 168.172 1.00 28.77  ? 2223 SER A CB    1 
ATOM   6342  O  OG    . SER A 1 1006 ? 175.969 196.928 166.784 1.00 26.03  ? 2223 SER A OG    1 
ATOM   6343  N  N     . SER A 1 1007 ? 172.967 196.193 166.628 1.00 22.41  ? 2224 SER A N     1 
ATOM   6344  C  CA    . SER A 1 1007 ? 171.744 196.665 165.986 1.00 22.39  ? 2224 SER A CA    1 
ATOM   6345  C  C     . SER A 1 1007 ? 170.502 196.063 166.633 1.00 21.71  ? 2224 SER A C     1 
ATOM   6346  O  O     . SER A 1 1007 ? 169.513 196.770 166.871 1.00 22.45  ? 2224 SER A O     1 
ATOM   6347  C  CB    . SER A 1 1007 ? 171.780 196.342 164.494 1.00 23.46  ? 2224 SER A CB    1 
ATOM   6348  O  OG    . SER A 1 1007 ? 170.514 196.566 163.902 1.00 22.85  ? 2224 SER A OG    1 
ATOM   6349  N  N     . LYS A 1 1008 ? 170.534 194.761 166.927 1.00 19.82  ? 2225 LYS A N     1 
ATOM   6350  C  CA    . LYS A 1 1008 ? 169.414 194.145 167.628 1.00 17.17  ? 2225 LYS A CA    1 
ATOM   6351  C  C     . LYS A 1 1008 ? 169.290 194.697 169.041 1.00 20.71  ? 2225 LYS A C     1 
ATOM   6352  O  O     . LYS A 1 1008 ? 168.174 194.870 169.544 1.00 21.97  ? 2225 LYS A O     1 
ATOM   6353  C  CB    . LYS A 1 1008 ? 169.565 192.624 167.652 1.00 13.95  ? 2225 LYS A CB    1 
ATOM   6354  C  CG    . LYS A 1 1008 ? 168.541 191.925 168.535 1.00 12.43  ? 2225 LYS A CG    1 
ATOM   6355  C  CD    . LYS A 1 1008 ? 168.158 190.552 168.034 1.00 15.50  ? 2225 LYS A CD    1 
ATOM   6356  C  CE    . LYS A 1 1008 ? 166.982 190.011 168.831 1.00 12.61  ? 2225 LYS A CE    1 
ATOM   6357  N  NZ    . LYS A 1 1008 ? 166.896 188.527 168.792 1.00 11.86  ? 2225 LYS A NZ    1 
ATOM   6358  N  N     . ILE A 1 1009 ? 170.421 195.002 169.686 1.00 20.91  ? 2226 ILE A N     1 
ATOM   6359  C  CA    . ILE A 1 1009 ? 170.379 195.620 171.012 1.00 19.75  ? 2226 ILE A CA    1 
ATOM   6360  C  C     . ILE A 1 1009 ? 169.657 196.962 170.950 1.00 22.15  ? 2226 ILE A C     1 
ATOM   6361  O  O     . ILE A 1 1009 ? 168.787 197.256 171.778 1.00 24.05  ? 2226 ILE A O     1 
ATOM   6362  C  CB    . ILE A 1 1009 ? 171.802 195.764 171.583 1.00 18.67  ? 2226 ILE A CB    1 
ATOM   6363  C  CG1   . ILE A 1 1009 ? 172.246 194.460 172.239 1.00 17.16  ? 2226 ILE A CG1   1 
ATOM   6364  C  CG2   . ILE A 1 1009 ? 171.885 196.902 172.587 1.00 24.82  ? 2226 ILE A CG2   1 
ATOM   6365  C  CD1   . ILE A 1 1009 ? 173.689 194.456 172.656 1.00 19.32  ? 2226 ILE A CD1   1 
ATOM   6366  N  N     . ASP A 1 1010 ? 169.987 197.780 169.946 1.00 21.84  ? 2227 ASP A N     1 
ATOM   6367  C  CA    . ASP A 1 1010 ? 169.351 199.088 169.807 1.00 23.64  ? 2227 ASP A CA    1 
ATOM   6368  C  C     . ASP A 1 1010 ? 167.861 198.964 169.505 1.00 21.52  ? 2227 ASP A C     1 
ATOM   6369  O  O     . ASP A 1 1010 ? 167.044 199.705 170.069 1.00 23.06  ? 2227 ASP A O     1 
ATOM   6370  C  CB    . ASP A 1 1010 ? 170.051 199.897 168.717 1.00 25.67  ? 2227 ASP A CB    1 
ATOM   6371  C  CG    . ASP A 1 1010 ? 171.428 200.367 169.135 1.00 31.73  ? 2227 ASP A CG    1 
ATOM   6372  O  OD1   . ASP A 1 1010 ? 171.869 200.007 170.247 1.00 32.20  ? 2227 ASP A OD1   1 
ATOM   6373  O  OD2   . ASP A 1 1010 ? 172.069 201.100 168.354 1.00 34.82  ? 2227 ASP A OD2   1 
ATOM   6374  N  N     . HIS A 1 1011 ? 167.488 198.039 168.614 1.00 18.85  ? 2228 HIS A N     1 
ATOM   6375  C  CA    . HIS A 1 1011 ? 166.072 197.859 168.300 1.00 18.65  ? 2228 HIS A CA    1 
ATOM   6376  C  C     . HIS A 1 1011 ? 165.291 197.374 169.513 1.00 22.22  ? 2228 HIS A C     1 
ATOM   6377  O  O     . HIS A 1 1011 ? 164.174 197.840 169.768 1.00 26.85  ? 2228 HIS A O     1 
ATOM   6378  C  CB    . HIS A 1 1011 ? 165.891 196.878 167.146 1.00 14.78  ? 2228 HIS A CB    1 
ATOM   6379  C  CG    . HIS A 1 1011 ? 164.497 196.345 167.036 1.00 13.27  ? 2228 HIS A CG    1 
ATOM   6380  N  ND1   . HIS A 1 1011 ? 164.181 195.023 167.262 1.00 12.80  ? 2228 HIS A ND1   1 
ATOM   6381  C  CD2   . HIS A 1 1011 ? 163.330 196.963 166.737 1.00 15.91  ? 2228 HIS A CD2   1 
ATOM   6382  C  CE1   . HIS A 1 1011 ? 162.881 194.850 167.102 1.00 12.90  ? 2228 HIS A CE1   1 
ATOM   6383  N  NE2   . HIS A 1 1011 ? 162.342 196.011 166.781 1.00 14.59  ? 2228 HIS A NE2   1 
ATOM   6384  N  N     . LEU A 1 1012 ? 165.860 196.429 170.266 1.00 20.02  ? 2229 LEU A N     1 
ATOM   6385  C  CA    . LEU A 1 1012 ? 165.204 195.935 171.470 1.00 19.64  ? 2229 LEU A CA    1 
ATOM   6386  C  C     . LEU A 1 1012 ? 165.057 197.038 172.506 1.00 24.24  ? 2229 LEU A C     1 
ATOM   6387  O  O     . LEU A 1 1012 ? 164.018 197.141 173.169 1.00 25.33  ? 2229 LEU A O     1 
ATOM   6388  C  CB    . LEU A 1 1012 ? 165.994 194.765 172.046 1.00 15.12  ? 2229 LEU A CB    1 
ATOM   6389  C  CG    . LEU A 1 1012 ? 165.859 193.431 171.325 1.00 12.82  ? 2229 LEU A CG    1 
ATOM   6390  C  CD1   . LEU A 1 1012 ? 166.966 192.516 171.780 1.00 14.19  ? 2229 LEU A CD1   1 
ATOM   6391  C  CD2   . LEU A 1 1012 ? 164.501 192.811 171.594 1.00 14.70  ? 2229 LEU A CD2   1 
ATOM   6392  N  N     . LEU A 1 1013 ? 166.090 197.872 172.655 1.00 22.27  ? 2230 LEU A N     1 
ATOM   6393  C  CA    . LEU A 1 1013 ? 166.016 198.994 173.583 1.00 24.63  ? 2230 LEU A CA    1 
ATOM   6394  C  C     . LEU A 1 1013 ? 164.893 199.946 173.200 1.00 30.71  ? 2230 LEU A C     1 
ATOM   6395  O  O     . LEU A 1 1013 ? 164.091 200.342 174.049 1.00 34.21  ? 2230 LEU A O     1 
ATOM   6396  C  CB    . LEU A 1 1013 ? 167.355 199.730 173.622 1.00 25.47  ? 2230 LEU A CB    1 
ATOM   6397  C  CG    . LEU A 1 1013 ? 168.478 199.118 174.457 1.00 23.53  ? 2230 LEU A CG    1 
ATOM   6398  C  CD1   . LEU A 1 1013 ? 169.782 199.834 174.182 1.00 30.44  ? 2230 LEU A CD1   1 
ATOM   6399  C  CD2   . LEU A 1 1013 ? 168.143 199.191 175.929 1.00 29.21  ? 2230 LEU A CD2   1 
ATOM   6400  N  N     . ASN A 1 1014 ? 164.805 200.302 171.914 1.00 31.97  ? 2231 ASN A N     1 
ATOM   6401  C  CA    . ASN A 1 1014 ? 163.769 201.239 171.478 1.00 34.06  ? 2231 ASN A CA    1 
ATOM   6402  C  C     . ASN A 1 1014 ? 162.371 200.647 171.634 1.00 34.74  ? 2231 ASN A C     1 
ATOM   6403  O  O     . ASN A 1 1014 ? 161.440 201.345 172.057 1.00 39.22  ? 2231 ASN A O     1 
ATOM   6404  C  CB    . ASN A 1 1014 ? 164.016 201.660 170.031 1.00 30.95  ? 2231 ASN A CB    1 
ATOM   6405  C  CG    . ASN A 1 1014 ? 165.128 202.682 169.906 1.00 34.81  ? 2231 ASN A CG    1 
ATOM   6406  O  OD1   . ASN A 1 1014 ? 166.120 202.629 170.632 1.00 33.01  ? 2231 ASN A OD1   1 
ATOM   6407  N  ND2   . ASN A 1 1014 ? 164.964 203.625 168.986 1.00 38.20  ? 2231 ASN A ND2   1 
ATOM   6408  N  N     . LYS A 1 1015 ? 162.207 199.363 171.305 1.00 31.18  ? 2232 LYS A N     1 
ATOM   6409  C  CA    . LYS A 1 1015 ? 160.911 198.711 171.473 1.00 30.98  ? 2232 LYS A CA    1 
ATOM   6410  C  C     . LYS A 1 1015 ? 160.504 198.657 172.942 1.00 39.99  ? 2232 LYS A C     1 
ATOM   6411  O  O     . LYS A 1 1015 ? 159.339 198.900 173.282 1.00 43.84  ? 2232 LYS A O     1 
ATOM   6412  C  CB    . LYS A 1 1015 ? 160.954 197.307 170.872 1.00 28.79  ? 2232 LYS A CB    1 
ATOM   6413  C  CG    . LYS A 1 1015 ? 159.686 196.501 171.070 1.00 32.76  ? 2232 LYS A CG    1 
ATOM   6414  C  CD    . LYS A 1 1015 ? 159.818 195.120 170.454 1.00 34.62  ? 2232 LYS A CD    1 
ATOM   6415  C  CE    . LYS A 1 1015 ? 159.346 194.043 171.414 1.00 36.39  ? 2232 LYS A CE    1 
ATOM   6416  N  NZ    . LYS A 1 1015 ? 157.867 194.056 171.572 1.00 40.76  ? 2232 LYS A NZ    1 
ATOM   6417  N  N     . SER A 1 1016 ? 161.454 198.350 173.829 1.00 39.67  ? 2233 SER A N     1 
ATOM   6418  C  CA    . SER A 1 1016 ? 161.149 198.303 175.254 1.00 39.99  ? 2233 SER A CA    1 
ATOM   6419  C  C     . SER A 1 1016 ? 160.863 199.689 175.823 1.00 41.88  ? 2233 SER A C     1 
ATOM   6420  O  O     . SER A 1 1016 ? 160.053 199.817 176.748 1.00 42.97  ? 2233 SER A O     1 
ATOM   6421  C  CB    . SER A 1 1016 ? 162.298 197.633 176.004 1.00 37.67  ? 2233 SER A CB    1 
ATOM   6422  O  OG    . SER A 1 1016 ? 163.505 198.351 175.828 1.00 37.89  ? 2233 SER A OG    1 
ATOM   6423  N  N     . TYR A 1 1017 ? 161.523 200.729 175.302 1.00 37.45  ? 2234 TYR A N     1 
ATOM   6424  C  CA    . TYR A 1 1017 ? 161.188 202.093 175.704 1.00 36.36  ? 2234 TYR A CA    1 
ATOM   6425  C  C     . TYR A 1 1017 ? 159.769 202.447 175.286 1.00 43.17  ? 2234 TYR A C     1 
ATOM   6426  O  O     . TYR A 1 1017 ? 159.002 203.021 176.068 1.00 45.74  ? 2234 TYR A O     1 
ATOM   6427  C  CB    . TYR A 1 1017 ? 162.164 203.097 175.091 1.00 36.28  ? 2234 TYR A CB    1 
ATOM   6428  C  CG    . TYR A 1 1017 ? 163.609 202.929 175.480 1.00 37.92  ? 2234 TYR A CG    1 
ATOM   6429  C  CD1   . TYR A 1 1017 ? 163.970 202.393 176.707 1.00 37.99  ? 2234 TYR A CD1   1 
ATOM   6430  C  CD2   . TYR A 1 1017 ? 164.617 203.321 174.612 1.00 39.68  ? 2234 TYR A CD2   1 
ATOM   6431  C  CE1   . TYR A 1 1017 ? 165.301 202.244 177.051 1.00 42.20  ? 2234 TYR A CE1   1 
ATOM   6432  C  CE2   . TYR A 1 1017 ? 165.940 203.171 174.941 1.00 41.26  ? 2234 TYR A CE2   1 
ATOM   6433  C  CZ    . TYR A 1 1017 ? 166.280 202.640 176.160 1.00 43.45  ? 2234 TYR A CZ    1 
ATOM   6434  O  OH    . TYR A 1 1017 ? 167.611 202.505 176.470 1.00 44.54  ? 2234 TYR A OH    1 
ATOM   6435  N  N     . GLU A 1 1018 ? 159.405 202.121 174.043 1.00 44.46  ? 2235 GLU A N     1 
ATOM   6436  C  CA    . GLU A 1 1018 ? 158.054 202.395 173.569 1.00 46.90  ? 2235 GLU A CA    1 
ATOM   6437  C  C     . GLU A 1 1018 ? 157.008 201.558 174.291 1.00 50.46  ? 2235 GLU A C     1 
ATOM   6438  O  O     . GLU A 1 1018 ? 155.836 201.947 174.322 1.00 55.09  ? 2235 GLU A O     1 
ATOM   6439  C  CB    . GLU A 1 1018 ? 157.964 202.159 172.061 1.00 49.41  ? 2235 GLU A CB    1 
ATOM   6440  C  CG    . GLU A 1 1018 ? 158.247 203.400 171.232 1.00 50.29  ? 2235 GLU A CG    1 
ATOM   6441  C  CD    . GLU A 1 1018 ? 158.050 203.168 169.749 1.00 62.86  ? 2235 GLU A CD    1 
ATOM   6442  O  OE1   . GLU A 1 1018 ? 157.705 202.031 169.364 1.00 63.88  ? 2235 GLU A OE1   1 
ATOM   6443  O  OE2   . GLU A 1 1018 ? 158.239 204.123 168.967 1.00 64.50  ? 2235 GLU A OE2   1 
ATOM   6444  N  N     . ALA A 1 1019 ? 157.401 200.417 174.862 1.00 50.29  ? 2236 ALA A N     1 
ATOM   6445  C  CA    . ALA A 1 1019 ? 156.474 199.645 175.682 1.00 53.12  ? 2236 ALA A CA    1 
ATOM   6446  C  C     . ALA A 1 1019 ? 156.115 200.377 176.969 1.00 51.63  ? 2236 ALA A C     1 
ATOM   6447  O  O     . ALA A 1 1019 ? 155.011 200.196 177.495 1.00 54.82  ? 2236 ALA A O     1 
ATOM   6448  C  CB    . ALA A 1 1019 ? 157.067 198.273 176.001 1.00 53.19  ? 2236 ALA A CB    1 
ATOM   6449  N  N     . LEU A 1 1020 ? 157.027 201.195 177.489 1.00 50.37  ? 2237 LEU A N     1 
ATOM   6450  C  CA    . LEU A 1 1020 ? 156.793 201.936 178.725 1.00 53.34  ? 2237 LEU A CA    1 
ATOM   6451  C  C     . LEU A 1 1020 ? 155.703 202.987 178.546 1.00 54.29  ? 2237 LEU A C     1 
ATOM   6452  O  O     . LEU A 1 1020 ? 155.994 204.162 178.324 1.00 53.33  ? 2237 LEU A O     1 
ATOM   6453  C  CB    . LEU A 1 1020 ? 158.085 202.604 179.202 1.00 52.10  ? 2237 LEU A CB    1 
ATOM   6454  C  CG    . LEU A 1 1020 ? 159.187 201.694 179.746 1.00 46.58  ? 2237 LEU A CG    1 
ATOM   6455  C  CD1   . LEU A 1 1020 ? 160.316 202.517 180.350 1.00 42.34  ? 2237 LEU A CD1   1 
ATOM   6456  C  CD2   . LEU A 1 1020 ? 158.622 200.725 180.768 1.00 41.57  ? 2237 LEU A CD2   1 
ATOM   6457  N  N     . PHE A 1 1027 ? 159.485 213.882 182.486 1.00 95.00  ? 2244 PHE A N     1 
ATOM   6458  C  CA    . PHE A 1 1027 ? 160.830 214.432 182.366 1.00 99.96  ? 2244 PHE A CA    1 
ATOM   6459  C  C     . PHE A 1 1027 ? 161.869 213.371 182.711 1.00 95.94  ? 2244 PHE A C     1 
ATOM   6460  O  O     . PHE A 1 1027 ? 163.044 213.498 182.365 1.00 94.91  ? 2244 PHE A O     1 
ATOM   6461  C  CB    . PHE A 1 1027 ? 160.991 215.658 183.270 1.00 105.61 ? 2244 PHE A CB    1 
ATOM   6462  C  CG    . PHE A 1 1027 ? 162.287 216.392 183.074 1.00 111.14 ? 2244 PHE A CG    1 
ATOM   6463  C  CD1   . PHE A 1 1027 ? 162.531 217.093 181.904 1.00 114.80 ? 2244 PHE A CD1   1 
ATOM   6464  C  CD2   . PHE A 1 1027 ? 163.260 216.385 184.061 1.00 106.70 ? 2244 PHE A CD2   1 
ATOM   6465  C  CE1   . PHE A 1 1027 ? 163.722 217.771 181.720 1.00 113.72 ? 2244 PHE A CE1   1 
ATOM   6466  C  CE2   . PHE A 1 1027 ? 164.453 217.061 183.884 1.00 107.36 ? 2244 PHE A CE2   1 
ATOM   6467  C  CZ    . PHE A 1 1027 ? 164.684 217.754 182.711 1.00 111.53 ? 2244 PHE A CZ    1 
ATOM   6468  N  N     . GLU A 1 1028 ? 161.425 212.316 183.397 1.00 90.74  ? 2245 GLU A N     1 
ATOM   6469  C  CA    . GLU A 1 1028 ? 162.317 211.219 183.748 1.00 86.32  ? 2245 GLU A CA    1 
ATOM   6470  C  C     . GLU A 1 1028 ? 162.479 210.210 182.620 1.00 83.69  ? 2245 GLU A C     1 
ATOM   6471  O  O     . GLU A 1 1028 ? 163.470 209.470 182.609 1.00 79.08  ? 2245 GLU A O     1 
ATOM   6472  C  CB    . GLU A 1 1028 ? 161.806 210.504 185.002 1.00 85.84  ? 2245 GLU A CB    1 
ATOM   6473  C  CG    . GLU A 1 1028 ? 160.404 209.934 184.857 1.00 84.48  ? 2245 GLU A CG    1 
ATOM   6474  C  CD    . GLU A 1 1028 ? 159.862 209.371 186.157 1.00 80.07  ? 2245 GLU A CD    1 
ATOM   6475  O  OE1   . GLU A 1 1028 ? 160.601 209.372 187.163 1.00 83.00  ? 2245 GLU A OE1   1 
ATOM   6476  O  OE2   . GLU A 1 1028 ? 158.695 208.926 186.170 1.00 73.29  ? 2245 GLU A OE2   1 
ATOM   6477  N  N     . LEU A 1 1029 ? 161.541 210.175 181.671 1.00 85.01  ? 2246 LEU A N     1 
ATOM   6478  C  CA    . LEU A 1 1029 ? 161.579 209.159 180.624 1.00 84.23  ? 2246 LEU A CA    1 
ATOM   6479  C  C     . LEU A 1 1029 ? 162.767 209.365 179.691 1.00 81.33  ? 2246 LEU A C     1 
ATOM   6480  O  O     . LEU A 1 1029 ? 163.453 208.401 179.334 1.00 78.03  ? 2246 LEU A O     1 
ATOM   6481  C  CB    . LEU A 1 1029 ? 160.255 209.164 179.851 1.00 81.35  ? 2246 LEU A CB    1 
ATOM   6482  C  CG    . LEU A 1 1029 ? 159.918 208.084 178.815 1.00 81.76  ? 2246 LEU A CG    1 
ATOM   6483  C  CD1   . LEU A 1 1029 ? 158.411 207.921 178.734 1.00 82.42  ? 2246 LEU A CD1   1 
ATOM   6484  C  CD2   . LEU A 1 1029 ? 160.466 208.405 177.428 1.00 81.06  ? 2246 LEU A CD2   1 
ATOM   6485  N  N     . ASP A 1 1030 ? 163.034 210.612 179.292 1.00 79.52  ? 2247 ASP A N     1 
ATOM   6486  C  CA    . ASP A 1 1030 ? 164.105 210.861 178.331 1.00 77.57  ? 2247 ASP A CA    1 
ATOM   6487  C  C     . ASP A 1 1030 ? 165.479 210.616 178.943 1.00 71.63  ? 2247 ASP A C     1 
ATOM   6488  O  O     . ASP A 1 1030 ? 166.343 210.002 178.307 1.00 69.61  ? 2247 ASP A O     1 
ATOM   6489  C  CB    . ASP A 1 1030 ? 164.006 212.286 177.787 1.00 78.59  ? 2247 ASP A CB    1 
ATOM   6490  C  CG    . ASP A 1 1030 ? 164.446 212.385 176.339 1.00 83.79  ? 2247 ASP A CG    1 
ATOM   6491  O  OD1   . ASP A 1 1030 ? 163.857 213.192 175.591 1.00 87.34  ? 2247 ASP A OD1   1 
ATOM   6492  O  OD2   . ASP A 1 1030 ? 165.379 211.652 175.949 1.00 82.97  ? 2247 ASP A OD2   1 
ATOM   6493  N  N     . LYS A 1 1031 ? 165.701 211.081 180.175 1.00 71.06  ? 2248 LYS A N     1 
ATOM   6494  C  CA    . LYS A 1 1031 ? 166.976 210.818 180.836 1.00 70.49  ? 2248 LYS A CA    1 
ATOM   6495  C  C     . LYS A 1 1031 ? 167.143 209.334 181.136 1.00 69.73  ? 2248 LYS A C     1 
ATOM   6496  O  O     . LYS A 1 1031 ? 168.253 208.796 181.033 1.00 68.25  ? 2248 LYS A O     1 
ATOM   6497  C  CB    . LYS A 1 1031 ? 167.095 211.654 182.112 1.00 77.91  ? 2248 LYS A CB    1 
ATOM   6498  C  CG    . LYS A 1 1031 ? 165.893 211.571 183.034 1.00 81.11  ? 2248 LYS A CG    1 
ATOM   6499  C  CD    . LYS A 1 1031 ? 166.077 212.404 184.291 1.00 80.13  ? 2248 LYS A CD    1 
ATOM   6500  C  CE    . LYS A 1 1031 ? 166.945 211.688 185.311 1.00 74.25  ? 2248 LYS A CE    1 
ATOM   6501  N  NZ    . LYS A 1 1031 ? 166.980 212.412 186.612 1.00 69.12  ? 2248 LYS A NZ    1 
ATOM   6502  N  N     . LEU A 1 1032 ? 166.048 208.654 181.488 1.00 72.40  ? 2249 LEU A N     1 
ATOM   6503  C  CA    . LEU A 1 1032 ? 166.091 207.212 181.704 1.00 70.57  ? 2249 LEU A CA    1 
ATOM   6504  C  C     . LEU A 1 1032 ? 166.508 206.486 180.430 1.00 67.16  ? 2249 LEU A C     1 
ATOM   6505  O  O     . LEU A 1 1032 ? 167.386 205.612 180.451 1.00 64.33  ? 2249 LEU A O     1 
ATOM   6506  C  CB    . LEU A 1 1032 ? 164.716 206.733 182.171 1.00 71.54  ? 2249 LEU A CB    1 
ATOM   6507  C  CG    . LEU A 1 1032 ? 164.573 205.361 182.817 1.00 63.12  ? 2249 LEU A CG    1 
ATOM   6508  C  CD1   . LEU A 1 1032 ? 165.058 205.448 184.249 1.00 59.08  ? 2249 LEU A CD1   1 
ATOM   6509  C  CD2   . LEU A 1 1032 ? 163.130 204.890 182.758 1.00 61.40  ? 2249 LEU A CD2   1 
ATOM   6510  N  N     . LYS A 1 1033 ? 165.893 206.862 179.304 1.00 65.65  ? 2250 LYS A N     1 
ATOM   6511  C  CA    . LYS A 1 1033 ? 166.235 206.283 178.010 1.00 58.64  ? 2250 LYS A CA    1 
ATOM   6512  C  C     . LYS A 1 1033 ? 167.691 206.544 177.652 1.00 59.56  ? 2250 LYS A C     1 
ATOM   6513  O  O     . LYS A 1 1033 ? 168.396 205.636 177.193 1.00 56.99  ? 2250 LYS A O     1 
ATOM   6514  C  CB    . LYS A 1 1033 ? 165.306 206.852 176.937 1.00 55.18  ? 2250 LYS A CB    1 
ATOM   6515  C  CG    . LYS A 1 1033 ? 165.769 206.624 175.512 1.00 52.55  ? 2250 LYS A CG    1 
ATOM   6516  C  CD    . LYS A 1 1033 ? 164.794 207.218 174.510 1.00 50.77  ? 2250 LYS A CD    1 
ATOM   6517  C  CE    . LYS A 1 1033 ? 165.227 206.931 173.082 1.00 46.82  ? 2250 LYS A CE    1 
ATOM   6518  N  NZ    . LYS A 1 1033 ? 166.487 207.641 172.729 1.00 48.19  ? 2250 LYS A NZ    1 
ATOM   6519  N  N     . ASP A 1 1034 ? 168.161 207.776 177.869 1.00 63.73  ? 2251 ASP A N     1 
ATOM   6520  C  CA    . ASP A 1 1034 ? 169.545 208.113 177.555 1.00 61.66  ? 2251 ASP A CA    1 
ATOM   6521  C  C     . ASP A 1 1034 ? 170.520 207.282 178.377 1.00 57.93  ? 2251 ASP A C     1 
ATOM   6522  O  O     . ASP A 1 1034 ? 171.500 206.758 177.837 1.00 58.63  ? 2251 ASP A O     1 
ATOM   6523  C  CB    . ASP A 1 1034 ? 169.792 209.604 177.785 1.00 63.32  ? 2251 ASP A CB    1 
ATOM   6524  C  CG    . ASP A 1 1034 ? 169.005 210.480 176.831 1.00 66.50  ? 2251 ASP A CG    1 
ATOM   6525  O  OD1   . ASP A 1 1034 ? 168.653 210.001 175.733 1.00 64.75  ? 2251 ASP A OD1   1 
ATOM   6526  O  OD2   . ASP A 1 1034 ? 168.740 211.649 177.179 1.00 68.59  ? 2251 ASP A OD2   1 
ATOM   6527  N  N     . LEU A 1 1035 ? 170.260 207.137 179.680 1.00 57.71  ? 2252 LEU A N     1 
ATOM   6528  C  CA    . LEU A 1 1035 ? 171.161 206.370 180.538 1.00 59.16  ? 2252 LEU A CA    1 
ATOM   6529  C  C     . LEU A 1 1035 ? 171.187 204.896 180.148 1.00 59.47  ? 2252 LEU A C     1 
ATOM   6530  O  O     . LEU A 1 1035 ? 172.265 204.295 180.025 1.00 61.44  ? 2252 LEU A O     1 
ATOM   6531  C  CB    . LEU A 1 1035 ? 170.759 206.532 182.004 1.00 63.33  ? 2252 LEU A CB    1 
ATOM   6532  C  CG    . LEU A 1 1035 ? 170.915 207.917 182.632 1.00 67.01  ? 2252 LEU A CG    1 
ATOM   6533  C  CD1   . LEU A 1 1035 ? 170.339 207.933 184.038 1.00 65.23  ? 2252 LEU A CD1   1 
ATOM   6534  C  CD2   . LEU A 1 1035 ? 172.376 208.338 182.641 1.00 68.01  ? 2252 LEU A CD2   1 
ATOM   6535  N  N     . ILE A 1 1036 ? 170.009 204.297 179.936 1.00 57.47  ? 2253 ILE A N     1 
ATOM   6536  C  CA    . ILE A 1 1036 ? 169.961 202.881 179.577 1.00 51.41  ? 2253 ILE A CA    1 
ATOM   6537  C  C     . ILE A 1 1036 ? 170.630 202.649 178.226 1.00 52.28  ? 2253 ILE A C     1 
ATOM   6538  O  O     . ILE A 1 1036 ? 171.322 201.643 178.025 1.00 46.43  ? 2253 ILE A O     1 
ATOM   6539  C  CB    . ILE A 1 1036 ? 168.508 202.367 179.587 1.00 47.61  ? 2253 ILE A CB    1 
ATOM   6540  C  CG1   . ILE A 1 1036 ? 167.875 202.548 180.963 1.00 49.42  ? 2253 ILE A CG1   1 
ATOM   6541  C  CG2   . ILE A 1 1036 ? 168.458 200.895 179.232 1.00 46.50  ? 2253 ILE A CG2   1 
ATOM   6542  C  CD1   . ILE A 1 1036 ? 166.417 202.149 181.002 1.00 44.63  ? 2253 ILE A CD1   1 
ATOM   6543  N  N     . SER A 1 1037 ? 170.458 203.585 177.287 1.00 57.77  ? 2254 SER A N     1 
ATOM   6544  C  CA    . SER A 1 1037 ? 171.020 203.401 175.953 1.00 53.94  ? 2254 SER A CA    1 
ATOM   6545  C  C     . SER A 1 1037 ? 172.536 203.571 175.948 1.00 56.08  ? 2254 SER A C     1 
ATOM   6546  O  O     . SER A 1 1037 ? 173.254 202.749 175.366 1.00 56.34  ? 2254 SER A O     1 
ATOM   6547  C  CB    . SER A 1 1037 ? 170.365 204.372 174.973 1.00 51.26  ? 2254 SER A CB    1 
ATOM   6548  O  OG    . SER A 1 1037 ? 169.002 204.042 174.774 1.00 48.86  ? 2254 SER A OG    1 
ATOM   6549  N  N     . ASP A 1 1038 ? 173.053 204.625 176.588 1.00 56.61  ? 2255 ASP A N     1 
ATOM   6550  C  CA    . ASP A 1 1038 ? 174.490 204.852 176.488 1.00 56.65  ? 2255 ASP A CA    1 
ATOM   6551  C  C     . ASP A 1 1038 ? 175.291 203.995 177.458 1.00 58.54  ? 2255 ASP A C     1 
ATOM   6552  O  O     . ASP A 1 1038 ? 176.513 203.892 177.301 1.00 60.03  ? 2255 ASP A O     1 
ATOM   6553  C  CB    . ASP A 1 1038 ? 174.843 206.339 176.681 1.00 57.94  ? 2255 ASP A CB    1 
ATOM   6554  C  CG    . ASP A 1 1038 ? 174.516 206.875 178.071 1.00 62.02  ? 2255 ASP A CG    1 
ATOM   6555  O  OD1   . ASP A 1 1038 ? 173.983 206.140 178.922 1.00 60.64  ? 2255 ASP A OD1   1 
ATOM   6556  O  OD2   . ASP A 1 1038 ? 174.800 208.066 178.313 1.00 63.63  ? 2255 ASP A OD2   1 
ATOM   6557  N  N     . SER A 1 1039 ? 174.642 203.377 178.450 1.00 57.75  ? 2256 SER A N     1 
ATOM   6558  C  CA    . SER A 1 1039 ? 175.364 202.436 179.298 1.00 56.38  ? 2256 SER A CA    1 
ATOM   6559  C  C     . SER A 1 1039 ? 175.690 201.128 178.584 1.00 52.58  ? 2256 SER A C     1 
ATOM   6560  O  O     . SER A 1 1039 ? 176.470 200.332 179.117 1.00 46.21  ? 2256 SER A O     1 
ATOM   6561  C  CB    . SER A 1 1039 ? 174.562 202.158 180.567 1.00 56.32  ? 2256 SER A CB    1 
ATOM   6562  O  OG    . SER A 1 1039 ? 174.248 203.363 181.243 1.00 57.03  ? 2256 SER A OG    1 
ATOM   6563  N  N     . PHE A 1 1040 ? 175.116 200.887 177.402 1.00 52.21  ? 2257 PHE A N     1 
ATOM   6564  C  CA    . PHE A 1 1040 ? 175.443 199.713 176.590 1.00 51.56  ? 2257 PHE A CA    1 
ATOM   6565  C  C     . PHE A 1 1040 ? 176.612 200.067 175.673 1.00 60.00  ? 2257 PHE A C     1 
ATOM   6566  O  O     . PHE A 1 1040 ? 176.448 200.392 174.495 1.00 58.74  ? 2257 PHE A O     1 
ATOM   6567  C  CB    . PHE A 1 1040 ? 174.226 199.255 175.793 1.00 43.03  ? 2257 PHE A CB    1 
ATOM   6568  C  CG    . PHE A 1 1040 ? 173.405 198.199 176.480 1.00 38.63  ? 2257 PHE A CG    1 
ATOM   6569  C  CD1   . PHE A 1 1040 ? 173.709 196.857 176.327 1.00 32.18  ? 2257 PHE A CD1   1 
ATOM   6570  C  CD2   . PHE A 1 1040 ? 172.320 198.548 177.267 1.00 36.89  ? 2257 PHE A CD2   1 
ATOM   6571  C  CE1   . PHE A 1 1040 ? 172.953 195.884 176.952 1.00 23.04  ? 2257 PHE A CE1   1 
ATOM   6572  C  CE2   . PHE A 1 1040 ? 171.561 197.579 177.894 1.00 26.64  ? 2257 PHE A CE2   1 
ATOM   6573  C  CZ    . PHE A 1 1040 ? 171.878 196.246 177.736 1.00 18.98  ? 2257 PHE A CZ    1 
ATOM   6574  N  N     . ASP A 1 1041 ? 177.818 199.999 176.233 1.00 65.62  ? 2258 ASP A N     1 
ATOM   6575  C  CA    . ASP A 1 1041 ? 179.042 200.317 175.499 1.00 64.02  ? 2258 ASP A CA    1 
ATOM   6576  C  C     . ASP A 1 1041 ? 179.526 199.067 174.768 1.00 60.87  ? 2258 ASP A C     1 
ATOM   6577  O  O     . ASP A 1 1041 ? 180.075 198.150 175.385 1.00 60.47  ? 2258 ASP A O     1 
ATOM   6578  C  CB    . ASP A 1 1041 ? 180.107 200.867 176.445 1.00 65.65  ? 2258 ASP A CB    1 
ATOM   6579  C  CG    . ASP A 1 1041 ? 180.205 200.081 177.741 1.00 65.73  ? 2258 ASP A CG    1 
ATOM   6580  O  OD1   . ASP A 1 1041 ? 179.341 199.210 177.979 1.00 66.94  ? 2258 ASP A OD1   1 
ATOM   6581  O  OD2   . ASP A 1 1041 ? 181.146 200.335 178.520 1.00 65.29  ? 2258 ASP A OD2   1 
ATOM   6582  N  N     . MET A 1 1042 ? 179.350 199.052 173.442 1.00 57.08  ? 2259 MET A N     1 
ATOM   6583  C  CA    . MET A 1 1042 ? 179.516 197.839 172.645 1.00 57.32  ? 2259 MET A CA    1 
ATOM   6584  C  C     . MET A 1 1042 ? 180.949 197.309 172.657 1.00 62.63  ? 2259 MET A C     1 
ATOM   6585  O  O     . MET A 1 1042 ? 181.158 196.120 172.393 1.00 61.09  ? 2259 MET A O     1 
ATOM   6586  C  CB    . MET A 1 1042 ? 179.057 198.123 171.204 1.00 57.22  ? 2259 MET A CB    1 
ATOM   6587  C  CG    . MET A 1 1042 ? 179.078 196.962 170.186 1.00 58.69  ? 2259 MET A CG    1 
ATOM   6588  S  SD    . MET A 1 1042 ? 178.617 195.287 170.707 1.00 65.42  ? 2259 MET A SD    1 
ATOM   6589  C  CE    . MET A 1 1042 ? 177.059 195.551 171.559 1.00 49.97  ? 2259 MET A CE    1 
ATOM   6590  N  N     . ALA A 1 1043 ? 181.933 198.155 172.984 1.00 66.42  ? 2260 ALA A N     1 
ATOM   6591  C  CA    . ALA A 1 1043 ? 183.333 197.739 172.926 1.00 66.95  ? 2260 ALA A CA    1 
ATOM   6592  C  C     . ALA A 1 1043 ? 183.625 196.600 173.898 1.00 66.51  ? 2260 ALA A C     1 
ATOM   6593  O  O     . ALA A 1 1043 ? 184.316 195.637 173.545 1.00 60.69  ? 2260 ALA A O     1 
ATOM   6594  C  CB    . ALA A 1 1043 ? 184.244 198.933 173.209 1.00 61.66  ? 2260 ALA A CB    1 
ATOM   6595  N  N     . SER A 1 1044 ? 183.108 196.687 175.123 1.00 65.33  ? 2261 SER A N     1 
ATOM   6596  C  CA    . SER A 1 1044 ? 183.245 195.598 176.081 1.00 62.59  ? 2261 SER A CA    1 
ATOM   6597  C  C     . SER A 1 1044 ? 182.193 194.516 175.887 1.00 60.72  ? 2261 SER A C     1 
ATOM   6598  O  O     . SER A 1 1044 ? 182.468 193.335 176.147 1.00 62.15  ? 2261 SER A O     1 
ATOM   6599  C  CB    . SER A 1 1044 ? 183.167 196.139 177.511 1.00 65.02  ? 2261 SER A CB    1 
ATOM   6600  O  OG    . SER A 1 1044 ? 184.368 196.798 177.872 1.00 68.24  ? 2261 SER A OG    1 
ATOM   6601  N  N     . LEU A 1 1045 ? 180.996 194.898 175.435 1.00 58.49  ? 2262 LEU A N     1 
ATOM   6602  C  CA    . LEU A 1 1045 ? 179.935 193.923 175.203 1.00 56.40  ? 2262 LEU A CA    1 
ATOM   6603  C  C     . LEU A 1 1045 ? 180.313 192.906 174.134 1.00 57.38  ? 2262 LEU A C     1 
ATOM   6604  O  O     . LEU A 1 1045 ? 179.904 191.746 174.225 1.00 55.98  ? 2262 LEU A O     1 
ATOM   6605  C  CB    . LEU A 1 1045 ? 178.632 194.633 174.826 1.00 54.05  ? 2262 LEU A CB    1 
ATOM   6606  C  CG    . LEU A 1 1045 ? 177.667 195.095 175.927 1.00 50.21  ? 2262 LEU A CG    1 
ATOM   6607  C  CD1   . LEU A 1 1045 ? 177.112 193.882 176.633 1.00 50.02  ? 2262 LEU A CD1   1 
ATOM   6608  C  CD2   . LEU A 1 1045 ? 178.298 196.030 176.941 1.00 53.24  ? 2262 LEU A CD2   1 
ATOM   6609  N  N     . THR A 1 1046 ? 181.084 193.311 173.121 1.00 59.00  ? 2263 THR A N     1 
ATOM   6610  C  CA    . THR A 1 1046 ? 181.507 192.365 172.091 1.00 60.26  ? 2263 THR A CA    1 
ATOM   6611  C  C     . THR A 1 1046 ? 182.359 191.251 172.689 1.00 59.60  ? 2263 THR A C     1 
ATOM   6612  O  O     . THR A 1 1046 ? 182.128 190.061 172.428 1.00 61.47  ? 2263 THR A O     1 
ATOM   6613  C  CB    . THR A 1 1046 ? 182.278 193.096 170.991 1.00 65.40  ? 2263 THR A CB    1 
ATOM   6614  O  OG1   . THR A 1 1046 ? 181.496 194.193 170.504 1.00 66.99  ? 2263 THR A OG1   1 
ATOM   6615  C  CG2   . THR A 1 1046 ? 182.587 192.151 169.841 1.00 64.60  ? 2263 THR A CG2   1 
ATOM   6616  N  N     . ASN A 1 1047 ? 183.332 191.623 173.525 1.00 60.19  ? 2264 ASN A N     1 
ATOM   6617  C  CA    . ASN A 1 1047 ? 184.138 190.627 174.220 1.00 61.78  ? 2264 ASN A CA    1 
ATOM   6618  C  C     . ASN A 1 1047 ? 183.294 189.802 175.180 1.00 60.02  ? 2264 ASN A C     1 
ATOM   6619  O  O     . ASN A 1 1047 ? 183.546 188.606 175.352 1.00 58.37  ? 2264 ASN A O     1 
ATOM   6620  C  CB    . ASN A 1 1047 ? 185.285 191.307 174.967 1.00 63.40  ? 2264 ASN A CB    1 
ATOM   6621  C  CG    . ASN A 1 1047 ? 186.232 192.036 174.038 1.00 68.53  ? 2264 ASN A CG    1 
ATOM   6622  O  OD1   . ASN A 1 1047 ? 186.515 193.219 174.224 1.00 70.84  ? 2264 ASN A OD1   1 
ATOM   6623  N  ND2   . ASN A 1 1047 ? 186.728 191.331 173.028 1.00 68.38  ? 2264 ASN A ND2   1 
ATOM   6624  N  N     . ILE A 1 1048 ? 182.277 190.415 175.792 1.00 58.81  ? 2265 ILE A N     1 
ATOM   6625  C  CA    . ILE A 1 1048 ? 181.417 189.687 176.725 1.00 56.47  ? 2265 ILE A CA    1 
ATOM   6626  C  C     . ILE A 1 1048 ? 180.621 188.607 175.998 1.00 54.36  ? 2265 ILE A C     1 
ATOM   6627  O  O     . ILE A 1 1048 ? 180.529 187.465 176.459 1.00 55.51  ? 2265 ILE A O     1 
ATOM   6628  C  CB    . ILE A 1 1048 ? 180.497 190.669 177.470 1.00 52.35  ? 2265 ILE A CB    1 
ATOM   6629  C  CG1   . ILE A 1 1048 ? 181.304 191.420 178.521 1.00 55.11  ? 2265 ILE A CG1   1 
ATOM   6630  C  CG2   . ILE A 1 1048 ? 179.329 189.943 178.120 1.00 47.24  ? 2265 ILE A CG2   1 
ATOM   6631  C  CD1   . ILE A 1 1048 ? 180.667 192.686 178.945 1.00 52.95  ? 2265 ILE A CD1   1 
ATOM   6632  N  N     . PHE A 1 1049 ? 180.038 188.950 174.850 1.00 50.28  ? 2266 PHE A N     1 
ATOM   6633  C  CA    . PHE A 1 1049 ? 179.272 187.966 174.089 1.00 49.09  ? 2266 PHE A CA    1 
ATOM   6634  C  C     . PHE A 1 1049 ? 180.177 186.873 173.524 1.00 54.34  ? 2266 PHE A C     1 
ATOM   6635  O  O     . PHE A 1 1049 ? 179.816 185.685 173.542 1.00 55.43  ? 2266 PHE A O     1 
ATOM   6636  C  CB    . PHE A 1 1049 ? 178.481 188.657 172.974 1.00 50.94  ? 2266 PHE A CB    1 
ATOM   6637  C  CG    . PHE A 1 1049 ? 177.416 189.601 173.476 1.00 51.72  ? 2266 PHE A CG    1 
ATOM   6638  C  CD1   . PHE A 1 1049 ? 176.499 189.190 174.428 1.00 48.15  ? 2266 PHE A CD1   1 
ATOM   6639  C  CD2   . PHE A 1 1049 ? 177.322 190.893 172.987 1.00 45.46  ? 2266 PHE A CD2   1 
ATOM   6640  C  CE1   . PHE A 1 1049 ? 175.521 190.056 174.892 1.00 37.79  ? 2266 PHE A CE1   1 
ATOM   6641  C  CE2   . PHE A 1 1049 ? 176.355 191.763 173.459 1.00 40.25  ? 2266 PHE A CE2   1 
ATOM   6642  C  CZ    . PHE A 1 1049 ? 175.450 191.339 174.405 1.00 35.64  ? 2266 PHE A CZ    1 
ATOM   6643  N  N     . THR A 1 1050 ? 181.367 187.249 173.036 1.00 58.17  ? 2267 THR A N     1 
ATOM   6644  C  CA    . THR A 1 1050 ? 182.286 186.246 172.508 1.00 56.94  ? 2267 THR A CA    1 
ATOM   6645  C  C     . THR A 1 1050 ? 182.914 185.392 173.604 1.00 59.21  ? 2267 THR A C     1 
ATOM   6646  O  O     . THR A 1 1050 ? 183.440 184.316 173.304 1.00 60.22  ? 2267 THR A O     1 
ATOM   6647  C  CB    . THR A 1 1050 ? 183.384 186.907 171.676 1.00 56.28  ? 2267 THR A CB    1 
ATOM   6648  O  OG1   . THR A 1 1050 ? 184.026 187.927 172.448 1.00 57.29  ? 2267 THR A OG1   1 
ATOM   6649  C  CG2   . THR A 1 1050 ? 182.797 187.523 170.413 1.00 54.85  ? 2267 THR A CG2   1 
ATOM   6650  N  N     . CYS A 1 1051 ? 182.895 185.850 174.855 1.00 60.34  ? 2268 CYS A N     1 
ATOM   6651  C  CA    . CYS A 1 1051 ? 183.327 185.032 175.980 1.00 60.69  ? 2268 CYS A CA    1 
ATOM   6652  C  C     . CYS A 1 1051 ? 182.170 184.322 176.671 1.00 59.52  ? 2268 CYS A C     1 
ATOM   6653  O  O     . CYS A 1 1051 ? 182.407 183.505 177.565 1.00 63.92  ? 2268 CYS A O     1 
ATOM   6654  C  CB    . CYS A 1 1051 ? 184.081 185.897 176.997 1.00 59.68  ? 2268 CYS A CB    1 
ATOM   6655  S  SG    . CYS A 1 1051 ? 185.227 184.992 178.064 1.00 72.78  ? 2268 CYS A SG    1 
ATOM   6656  N  N     . SER A 1 1052 ? 180.930 184.634 176.298 1.00 59.48  ? 2269 SER A N     1 
ATOM   6657  C  CA    . SER A 1 1052 ? 179.773 183.913 176.807 1.00 56.60  ? 2269 SER A CA    1 
ATOM   6658  C  C     . SER A 1 1052 ? 179.299 182.816 175.868 1.00 55.76  ? 2269 SER A C     1 
ATOM   6659  O  O     . SER A 1 1052 ? 178.573 181.918 176.309 1.00 52.19  ? 2269 SER A O     1 
ATOM   6660  C  CB    . SER A 1 1052 ? 178.609 184.874 177.057 1.00 50.14  ? 2269 SER A CB    1 
ATOM   6661  O  OG    . SER A 1 1052 ? 178.116 185.398 175.837 1.00 50.73  ? 2269 SER A OG    1 
ATOM   6662  N  N     . ASN A 1 1053 ? 179.668 182.878 174.585 1.00 59.60  ? 2270 ASN A N     1 
ATOM   6663  C  CA    . ASN A 1 1053 ? 179.257 181.810 173.676 1.00 60.66  ? 2270 ASN A CA    1 
ATOM   6664  C  C     . ASN A 1 1053 ? 179.950 180.486 173.990 1.00 60.66  ? 2270 ASN A C     1 
ATOM   6665  O  O     . ASN A 1 1053 ? 179.356 179.419 173.802 1.00 59.30  ? 2270 ASN A O     1 
ATOM   6666  C  CB    . ASN A 1 1053 ? 179.508 182.211 172.217 1.00 59.29  ? 2270 ASN A CB    1 
ATOM   6667  C  CG    . ASN A 1 1053 ? 180.951 182.618 171.940 1.00 61.08  ? 2270 ASN A CG    1 
ATOM   6668  O  OD1   . ASN A 1 1053 ? 181.895 182.106 172.543 1.00 65.62  ? 2270 ASN A OD1   1 
ATOM   6669  N  ND2   . ASN A 1 1053 ? 181.124 183.534 170.997 1.00 56.33  ? 2270 ASN A ND2   1 
ATOM   6670  N  N     . ASP A 1 1054 ? 181.198 180.532 174.464 1.00 59.60  ? 2271 ASP A N     1 
ATOM   6671  C  CA    . ASP A 1 1054 ? 182.008 179.325 174.591 1.00 62.55  ? 2271 ASP A CA    1 
ATOM   6672  C  C     . ASP A 1 1054 ? 181.614 178.445 175.771 1.00 63.85  ? 2271 ASP A C     1 
ATOM   6673  O  O     . ASP A 1 1054 ? 181.894 177.241 175.740 1.00 65.09  ? 2271 ASP A O     1 
ATOM   6674  C  CB    . ASP A 1 1054 ? 183.490 179.694 174.706 1.00 64.38  ? 2271 ASP A CB    1 
ATOM   6675  C  CG    . ASP A 1 1054 ? 183.865 180.187 176.091 1.00 65.16  ? 2271 ASP A CG    1 
ATOM   6676  O  OD1   . ASP A 1 1054 ? 183.065 180.924 176.701 1.00 62.15  ? 2271 ASP A OD1   1 
ATOM   6677  O  OD2   . ASP A 1 1054 ? 184.961 179.832 176.572 1.00 67.36  ? 2271 ASP A OD2   1 
ATOM   6678  N  N     . LEU A 1 1055 ? 180.993 179.008 176.805 1.00 62.18  ? 2272 LEU A N     1 
ATOM   6679  C  CA    . LEU A 1 1055 ? 180.668 178.239 177.998 1.00 60.56  ? 2272 LEU A CA    1 
ATOM   6680  C  C     . LEU A 1 1055 ? 179.609 177.183 177.690 1.00 60.32  ? 2272 LEU A C     1 
ATOM   6681  O  O     . LEU A 1 1055 ? 178.863 177.276 176.713 1.00 63.16  ? 2272 LEU A O     1 
ATOM   6682  C  CB    . LEU A 1 1055 ? 180.186 179.162 179.117 1.00 57.85  ? 2272 LEU A CB    1 
ATOM   6683  C  CG    . LEU A 1 1055 ? 181.097 180.349 179.436 1.00 57.18  ? 2272 LEU A CG    1 
ATOM   6684  C  CD1   . LEU A 1 1055 ? 180.434 181.290 180.428 1.00 53.66  ? 2272 LEU A CD1   1 
ATOM   6685  C  CD2   . LEU A 1 1055 ? 182.437 179.867 179.965 1.00 57.36  ? 2272 LEU A CD2   1 
ATOM   6686  N  N     . VAL A 1 1056 ? 179.557 176.160 178.538 1.00 54.83  ? 2273 VAL A N     1 
ATOM   6687  C  CA    . VAL A 1 1056 ? 178.672 175.023 178.311 1.00 56.50  ? 2273 VAL A CA    1 
ATOM   6688  C  C     . VAL A 1 1056 ? 177.253 175.443 178.682 1.00 54.68  ? 2273 VAL A C     1 
ATOM   6689  O  O     . VAL A 1 1056 ? 176.919 175.570 179.863 1.00 48.41  ? 2273 VAL A O     1 
ATOM   6690  C  CB    . VAL A 1 1056 ? 179.117 173.794 179.111 1.00 58.26  ? 2273 VAL A CB    1 
ATOM   6691  C  CG1   . VAL A 1 1056 ? 178.114 172.660 178.950 1.00 60.36  ? 2273 VAL A CG1   1 
ATOM   6692  C  CG2   . VAL A 1 1056 ? 180.505 173.351 178.673 1.00 57.77  ? 2273 VAL A CG2   1 
ATOM   6693  N  N     . HIS A 1 1057 ? 176.417 175.661 177.671 1.00 52.70  ? 2274 HIS A N     1 
ATOM   6694  C  CA    . HIS A 1 1057 ? 175.022 176.036 177.859 1.00 46.96  ? 2274 HIS A CA    1 
ATOM   6695  C  C     . HIS A 1 1057 ? 174.140 174.826 177.589 1.00 47.90  ? 2274 HIS A C     1 
ATOM   6696  O  O     . HIS A 1 1057 ? 174.314 174.140 176.576 1.00 45.72  ? 2274 HIS A O     1 
ATOM   6697  C  CB    . HIS A 1 1057 ? 174.626 177.189 176.933 1.00 43.97  ? 2274 HIS A CB    1 
ATOM   6698  C  CG    . HIS A 1 1057 ? 175.546 178.368 177.000 1.00 45.36  ? 2274 HIS A CG    1 
ATOM   6699  N  ND1   . HIS A 1 1057 ? 175.682 179.143 178.132 1.00 43.44  ? 2274 HIS A ND1   1 
ATOM   6700  C  CD2   . HIS A 1 1057 ? 176.358 178.919 176.068 1.00 49.00  ? 2274 HIS A CD2   1 
ATOM   6701  C  CE1   . HIS A 1 1057 ? 176.550 180.111 177.899 1.00 44.65  ? 2274 HIS A CE1   1 
ATOM   6702  N  NE2   . HIS A 1 1057 ? 176.975 179.998 176.654 1.00 50.73  ? 2274 HIS A NE2   1 
ATOM   6703  N  N     . ILE A 1 1058 ? 173.198 174.569 178.490 1.00 44.94  ? 2275 ILE A N     1 
ATOM   6704  C  CA    . ILE A 1 1058 ? 172.260 173.460 178.359 1.00 41.12  ? 2275 ILE A CA    1 
ATOM   6705  C  C     . ILE A 1 1058 ? 170.941 173.996 177.828 1.00 38.60  ? 2275 ILE A C     1 
ATOM   6706  O  O     . ILE A 1 1058 ? 170.495 175.080 178.227 1.00 40.51  ? 2275 ILE A O     1 
ATOM   6707  C  CB    . ILE A 1 1058 ? 172.085 172.723 179.699 1.00 36.26  ? 2275 ILE A CB    1 
ATOM   6708  C  CG1   . ILE A 1 1058 ? 173.456 172.548 180.355 1.00 41.57  ? 2275 ILE A CG1   1 
ATOM   6709  C  CG2   . ILE A 1 1058 ? 171.401 171.384 179.489 1.00 35.84  ? 2275 ILE A CG2   1 
ATOM   6710  C  CD1   . ILE A 1 1058 ? 173.456 171.674 181.575 1.00 35.76  ? 2275 ILE A CD1   1 
ATOM   6711  N  N     . LEU A 1 1059 ? 170.322 173.234 176.923 1.00 37.42  ? 2276 LEU A N     1 
ATOM   6712  C  CA    . LEU A 1 1059 ? 169.305 173.730 175.994 1.00 34.72  ? 2276 LEU A CA    1 
ATOM   6713  C  C     . LEU A 1 1059 ? 169.871 174.905 175.200 1.00 37.21  ? 2276 LEU A C     1 
ATOM   6714  O  O     . LEU A 1 1059 ? 169.437 176.051 175.319 1.00 31.44  ? 2276 LEU A O     1 
ATOM   6715  C  CB    . LEU A 1 1059 ? 167.997 174.096 176.705 1.00 29.36  ? 2276 LEU A CB    1 
ATOM   6716  C  CG    . LEU A 1 1059 ? 167.171 172.910 177.203 1.00 27.15  ? 2276 LEU A CG    1 
ATOM   6717  C  CD1   . LEU A 1 1059 ? 166.183 173.343 178.263 1.00 23.34  ? 2276 LEU A CD1   1 
ATOM   6718  C  CD2   . LEU A 1 1059 ? 166.447 172.254 176.043 1.00 23.58  ? 2276 LEU A CD2   1 
ATOM   6719  N  N     . GLY A 1 1060 ? 170.884 174.585 174.396 1.00 40.83  ? 2277 GLY A N     1 
ATOM   6720  C  CA    . GLY A 1 1060 ? 171.685 175.564 173.690 1.00 34.32  ? 2277 GLY A CA    1 
ATOM   6721  C  C     . GLY A 1 1060 ? 170.924 176.493 172.771 1.00 29.88  ? 2277 GLY A C     1 
ATOM   6722  O  O     . GLY A 1 1060 ? 170.410 176.081 171.727 1.00 28.53  ? 2277 GLY A O     1 
ATOM   6723  N  N     . VAL A 1 1061 ? 170.853 177.759 173.165 1.00 27.72  ? 2278 VAL A N     1 
ATOM   6724  C  CA    . VAL A 1 1061 ? 170.248 178.822 172.375 1.00 24.56  ? 2278 VAL A CA    1 
ATOM   6725  C  C     . VAL A 1 1061 ? 171.362 179.770 171.955 1.00 23.93  ? 2278 VAL A C     1 
ATOM   6726  O  O     . VAL A 1 1061 ? 172.252 180.080 172.755 1.00 28.04  ? 2278 VAL A O     1 
ATOM   6727  C  CB    . VAL A 1 1061 ? 169.147 179.544 173.179 1.00 18.17  ? 2278 VAL A CB    1 
ATOM   6728  C  CG1   . VAL A 1 1061 ? 168.758 180.851 172.533 1.00 15.72  ? 2278 VAL A CG1   1 
ATOM   6729  C  CG2   . VAL A 1 1061 ? 167.930 178.650 173.309 1.00 14.66  ? 2278 VAL A CG2   1 
ATOM   6730  N  N     . ARG A 1 1062 ? 171.330 180.199 170.691 1.00 19.61  ? 2279 ARG A N     1 
ATOM   6731  C  CA    . ARG A 1 1062 ? 172.413 180.980 170.106 1.00 19.89  ? 2279 ARG A CA    1 
ATOM   6732  C  C     . ARG A 1 1062 ? 172.648 182.276 170.878 1.00 21.21  ? 2279 ARG A C     1 
ATOM   6733  O  O     . ARG A 1 1062 ? 171.777 182.778 171.594 1.00 21.10  ? 2279 ARG A O     1 
ATOM   6734  C  CB    . ARG A 1 1062 ? 172.109 181.315 168.647 1.00 19.61  ? 2279 ARG A CB    1 
ATOM   6735  C  CG    . ARG A 1 1062 ? 171.695 180.137 167.791 1.00 21.16  ? 2279 ARG A CG    1 
ATOM   6736  C  CD    . ARG A 1 1062 ? 171.732 180.516 166.320 1.00 19.08  ? 2279 ARG A CD    1 
ATOM   6737  N  NE    . ARG A 1 1062 ? 170.635 181.408 165.961 1.00 12.61  ? 2279 ARG A NE    1 
ATOM   6738  C  CZ    . ARG A 1 1062 ? 170.793 182.608 165.420 1.00 11.66  ? 2279 ARG A CZ    1 
ATOM   6739  N  NH1   . ARG A 1 1062 ? 171.993 183.098 165.162 1.00 11.93  ? 2279 ARG A NH1   1 
ATOM   6740  N  NH2   . ARG A 1 1062 ? 169.718 183.335 165.133 1.00 11.76  ? 2279 ARG A NH2   1 
ATOM   6741  N  N     . THR A 1 1063 ? 173.860 182.815 170.722 1.00 20.76  ? 2280 THR A N     1 
ATOM   6742  C  CA    . THR A 1 1063 ? 174.220 184.050 171.407 1.00 21.01  ? 2280 THR A CA    1 
ATOM   6743  C  C     . THR A 1 1063 ? 173.414 185.230 170.881 1.00 19.11  ? 2280 THR A C     1 
ATOM   6744  O  O     . THR A 1 1063 ? 173.122 186.164 171.634 1.00 20.62  ? 2280 THR A O     1 
ATOM   6745  C  CB    . THR A 1 1063 ? 175.721 184.306 171.255 1.00 28.27  ? 2280 THR A CB    1 
ATOM   6746  O  OG1   . THR A 1 1063 ? 176.443 183.149 171.694 1.00 33.41  ? 2280 THR A OG1   1 
ATOM   6747  C  CG2   . THR A 1 1063 ? 176.164 185.500 172.089 1.00 33.89  ? 2280 THR A CG2   1 
ATOM   6748  N  N     . PHE A 1 1064 ? 173.013 185.187 169.608 1.00 17.66  ? 2281 PHE A N     1 
ATOM   6749  C  CA    . PHE A 1 1064 ? 172.201 186.250 169.028 1.00 16.84  ? 2281 PHE A CA    1 
ATOM   6750  C  C     . PHE A 1 1064 ? 170.780 186.269 169.580 1.00 15.43  ? 2281 PHE A C     1 
ATOM   6751  O  O     . PHE A 1 1064 ? 170.082 187.275 169.420 1.00 14.68  ? 2281 PHE A O     1 
ATOM   6752  C  CB    . PHE A 1 1064 ? 172.174 186.098 167.504 1.00 15.60  ? 2281 PHE A CB    1 
ATOM   6753  C  CG    . PHE A 1 1064 ? 171.575 187.271 166.777 1.00 14.18  ? 2281 PHE A CG    1 
ATOM   6754  C  CD1   . PHE A 1 1064 ? 172.297 188.437 166.600 1.00 17.67  ? 2281 PHE A CD1   1 
ATOM   6755  C  CD2   . PHE A 1 1064 ? 170.295 187.198 166.254 1.00 15.43  ? 2281 PHE A CD2   1 
ATOM   6756  C  CE1   . PHE A 1 1064 ? 171.750 189.513 165.927 1.00 16.41  ? 2281 PHE A CE1   1 
ATOM   6757  C  CE2   . PHE A 1 1064 ? 169.742 188.269 165.579 1.00 15.14  ? 2281 PHE A CE2   1 
ATOM   6758  C  CZ    . PHE A 1 1064 ? 170.471 189.427 165.416 1.00 14.41  ? 2281 PHE A CZ    1 
ATOM   6759  N  N     . ASN A 1 1065 ? 170.341 185.197 170.236 1.00 13.56  ? 2282 ASN A N     1 
ATOM   6760  C  CA    . ASN A 1 1065 ? 168.971 185.088 170.716 1.00 11.91  ? 2282 ASN A CA    1 
ATOM   6761  C  C     . ASN A 1 1065 ? 168.834 185.303 172.219 1.00 14.50  ? 2282 ASN A C     1 
ATOM   6762  O  O     . ASN A 1 1065 ? 167.716 185.239 172.736 1.00 16.05  ? 2282 ASN A O     1 
ATOM   6763  C  CB    . ASN A 1 1065 ? 168.395 183.724 170.338 1.00 12.62  ? 2282 ASN A CB    1 
ATOM   6764  C  CG    . ASN A 1 1065 ? 168.317 183.525 168.843 1.00 15.84  ? 2282 ASN A CG    1 
ATOM   6765  O  OD1   . ASN A 1 1065 ? 168.546 184.456 168.073 1.00 16.59  ? 2282 ASN A OD1   1 
ATOM   6766  N  ND2   . ASN A 1 1065 ? 168.001 182.307 168.421 1.00 14.35  ? 2282 ASN A ND2   1 
ATOM   6767  N  N     . LYS A 1 1066 ? 169.934 185.544 172.932 1.00 13.04  ? 2283 LYS A N     1 
ATOM   6768  C  CA    . LYS A 1 1066 ? 169.881 185.923 174.338 1.00 12.62  ? 2283 LYS A CA    1 
ATOM   6769  C  C     . LYS A 1 1066 ? 169.697 187.423 174.527 1.00 13.86  ? 2283 LYS A C     1 
ATOM   6770  O  O     . LYS A 1 1066 ? 169.476 187.880 175.661 1.00 18.77  ? 2283 LYS A O     1 
ATOM   6771  C  CB    . LYS A 1 1066 ? 171.162 185.476 175.049 1.00 16.69  ? 2283 LYS A CB    1 
ATOM   6772  C  CG    . LYS A 1 1066 ? 171.542 184.025 174.806 1.00 20.35  ? 2283 LYS A CG    1 
ATOM   6773  C  CD    . LYS A 1 1066 ? 170.947 183.113 175.864 1.00 25.47  ? 2283 LYS A CD    1 
ATOM   6774  C  CE    . LYS A 1 1066 ? 171.350 181.666 175.644 1.00 25.27  ? 2283 LYS A CE    1 
ATOM   6775  N  NZ    . LYS A 1 1066 ? 172.725 181.395 176.137 1.00 28.34  ? 2283 LYS A NZ    1 
ATOM   6776  N  N     . LEU A 1 1067 ? 169.788 188.185 173.435 1.00 11.96  ? 2284 LEU A N     1 
ATOM   6777  C  CA    . LEU A 1 1067 ? 169.725 189.638 173.505 1.00 10.82  ? 2284 LEU A CA    1 
ATOM   6778  C  C     . LEU A 1 1067 ? 168.367 190.114 173.990 1.00 13.04  ? 2284 LEU A C     1 
ATOM   6779  O  O     . LEU A 1 1067 ? 168.281 191.115 174.710 1.00 17.12  ? 2284 LEU A O     1 
ATOM   6780  C  CB    . LEU A 1 1067 ? 170.030 190.236 172.136 1.00 10.03  ? 2284 LEU A CB    1 
ATOM   6781  C  CG    . LEU A 1 1067 ? 171.479 190.467 171.725 1.00 10.77  ? 2284 LEU A CG    1 
ATOM   6782  C  CD1   . LEU A 1 1067 ? 172.167 189.181 171.367 1.00 12.96  ? 2284 LEU A CD1   1 
ATOM   6783  C  CD2   . LEU A 1 1067 ? 171.474 191.372 170.536 1.00 16.28  ? 2284 LEU A CD2   1 
ATOM   6784  N  N     . GLU A 1 1068 ? 167.295 189.427 173.588 1.00 11.69  ? 2285 GLU A N     1 
ATOM   6785  C  CA    . GLU A 1 1068 ? 165.960 189.824 174.019 1.00 12.30  ? 2285 GLU A CA    1 
ATOM   6786  C  C     . GLU A 1 1068 ? 165.836 189.735 175.531 1.00 14.51  ? 2285 GLU A C     1 
ATOM   6787  O  O     . GLU A 1 1068 ? 165.386 190.684 176.185 1.00 18.15  ? 2285 GLU A O     1 
ATOM   6788  C  CB    . GLU A 1 1068 ? 164.908 188.954 173.332 1.00 13.39  ? 2285 GLU A CB    1 
ATOM   6789  C  CG    . GLU A 1 1068 ? 165.138 188.791 171.838 1.00 14.44  ? 2285 GLU A CG    1 
ATOM   6790  C  CD    . GLU A 1 1068 ? 164.430 187.582 171.261 1.00 14.28  ? 2285 GLU A CD    1 
ATOM   6791  O  OE1   . GLU A 1 1068 ? 163.740 186.874 172.023 1.00 15.61  ? 2285 GLU A OE1   1 
ATOM   6792  O  OE2   . GLU A 1 1068 ? 164.573 187.338 170.045 1.00 12.85  ? 2285 GLU A OE2   1 
ATOM   6793  N  N     . THR A 1 1069 ? 166.299 188.623 176.107 1.00 13.84  ? 2286 THR A N     1 
ATOM   6794  C  CA    . THR A 1 1069 ? 166.274 188.461 177.556 1.00 14.13  ? 2286 THR A CA    1 
ATOM   6795  C  C     . THR A 1 1069 ? 167.117 189.525 178.243 1.00 14.44  ? 2286 THR A C     1 
ATOM   6796  O  O     . THR A 1 1069 ? 166.651 190.188 179.175 1.00 14.49  ? 2286 THR A O     1 
ATOM   6797  C  CB    . THR A 1 1069 ? 166.770 187.068 177.941 1.00 14.85  ? 2286 THR A CB    1 
ATOM   6798  O  OG1   . THR A 1 1069 ? 165.883 186.076 177.410 1.00 15.61  ? 2286 THR A OG1   1 
ATOM   6799  C  CG2   . THR A 1 1069 ? 166.826 186.933 179.450 1.00 13.04  ? 2286 THR A CG2   1 
ATOM   6800  N  N     . ALA A 1 1070 ? 168.352 189.725 177.771 1.00 15.20  ? 2287 ALA A N     1 
ATOM   6801  C  CA    . ALA A 1 1070 ? 169.252 190.667 178.437 1.00 15.35  ? 2287 ALA A CA    1 
ATOM   6802  C  C     . ALA A 1 1070 ? 168.695 192.088 178.411 1.00 16.24  ? 2287 ALA A C     1 
ATOM   6803  O  O     . ALA A 1 1070 ? 168.564 192.738 179.460 1.00 18.64  ? 2287 ALA A O     1 
ATOM   6804  C  CB    . ALA A 1 1070 ? 170.634 190.621 177.787 1.00 14.72  ? 2287 ALA A CB    1 
ATOM   6805  N  N     . VAL A 1 1071 ? 168.328 192.571 177.221 1.00 15.14  ? 2288 VAL A N     1 
ATOM   6806  C  CA    . VAL A 1 1071 ? 167.872 193.947 177.074 1.00 15.38  ? 2288 VAL A CA    1 
ATOM   6807  C  C     . VAL A 1 1071 ? 166.552 194.164 177.801 1.00 20.82  ? 2288 VAL A C     1 
ATOM   6808  O  O     . VAL A 1 1071 ? 166.382 195.164 178.513 1.00 28.19  ? 2288 VAL A O     1 
ATOM   6809  C  CB    . VAL A 1 1071 ? 167.763 194.310 175.583 1.00 14.65  ? 2288 VAL A CB    1 
ATOM   6810  C  CG1   . VAL A 1 1071 ? 167.148 195.680 175.422 1.00 23.37  ? 2288 VAL A CG1   1 
ATOM   6811  C  CG2   . VAL A 1 1071 ? 169.130 194.264 174.931 1.00 14.49  ? 2288 VAL A CG2   1 
ATOM   6812  N  N     . GLN A 1 1072 ? 165.600 193.236 177.649 1.00 18.10  ? 2289 GLN A N     1 
ATOM   6813  C  CA    . GLN A 1 1072 ? 164.297 193.416 178.274 1.00 18.68  ? 2289 GLN A CA    1 
ATOM   6814  C  C     . GLN A 1 1072 ? 164.395 193.343 179.793 1.00 20.60  ? 2289 GLN A C     1 
ATOM   6815  O  O     . GLN A 1 1072 ? 163.728 194.110 180.497 1.00 22.33  ? 2289 GLN A O     1 
ATOM   6816  C  CB    . GLN A 1 1072 ? 163.326 192.374 177.727 1.00 17.80  ? 2289 GLN A CB    1 
ATOM   6817  C  CG    . GLN A 1 1072 ? 161.886 192.584 178.112 1.00 22.08  ? 2289 GLN A CG    1 
ATOM   6818  C  CD    . GLN A 1 1072 ? 160.960 191.658 177.355 1.00 29.40  ? 2289 GLN A CD    1 
ATOM   6819  O  OE1   . GLN A 1 1072 ? 161.405 190.850 176.540 1.00 28.95  ? 2289 GLN A OE1   1 
ATOM   6820  N  NE2   . GLN A 1 1072 ? 159.665 191.767 177.621 1.00 29.89  ? 2289 GLN A NE2   1 
ATOM   6821  N  N     . LEU A 1 1073 ? 165.248 192.455 180.317 1.00 18.90  ? 2290 LEU A N     1 
ATOM   6822  C  CA    . LEU A 1 1073 ? 165.433 192.360 181.760 1.00 19.83  ? 2290 LEU A CA    1 
ATOM   6823  C  C     . LEU A 1 1073 ? 166.040 193.641 182.315 1.00 21.52  ? 2290 LEU A C     1 
ATOM   6824  O  O     . LEU A 1 1073 ? 165.576 194.168 183.334 1.00 21.71  ? 2290 LEU A O     1 
ATOM   6825  C  CB    . LEU A 1 1073 ? 166.314 191.151 182.090 1.00 17.89  ? 2290 LEU A CB    1 
ATOM   6826  C  CG    . LEU A 1 1073 ? 166.366 190.573 183.509 1.00 15.32  ? 2290 LEU A CG    1 
ATOM   6827  C  CD1   . LEU A 1 1073 ? 166.737 189.108 183.441 1.00 14.04  ? 2290 LEU A CD1   1 
ATOM   6828  C  CD2   . LEU A 1 1073 ? 167.344 191.301 184.409 1.00 17.68  ? 2290 LEU A CD2   1 
ATOM   6829  N  N     . ALA A 1 1074 ? 167.080 194.163 181.653 1.00 21.43  ? 2291 ALA A N     1 
ATOM   6830  C  CA    . ALA A 1 1074 ? 167.708 195.390 182.135 1.00 19.87  ? 2291 ALA A CA    1 
ATOM   6831  C  C     . ALA A 1 1074 ? 166.739 196.564 182.090 1.00 23.79  ? 2291 ALA A C     1 
ATOM   6832  O  O     . ALA A 1 1074 ? 166.650 197.347 183.049 1.00 29.44  ? 2291 ALA A O     1 
ATOM   6833  C  CB    . ALA A 1 1074 ? 168.960 195.696 181.316 1.00 19.38  ? 2291 ALA A CB    1 
ATOM   6834  N  N     . VAL A 1 1075 ? 165.984 196.686 180.994 1.00 26.32  ? 2292 VAL A N     1 
ATOM   6835  C  CA    . VAL A 1 1075 ? 165.036 197.788 180.855 1.00 30.50  ? 2292 VAL A CA    1 
ATOM   6836  C  C     . VAL A 1 1075 ? 163.948 197.699 181.918 1.00 28.67  ? 2292 VAL A C     1 
ATOM   6837  O  O     . VAL A 1 1075 ? 163.579 198.709 182.529 1.00 28.97  ? 2292 VAL A O     1 
ATOM   6838  C  CB    . VAL A 1 1075 ? 164.449 197.811 179.432 1.00 27.94  ? 2292 VAL A CB    1 
ATOM   6839  C  CG1   . VAL A 1 1075 ? 163.199 198.673 179.377 1.00 31.38  ? 2292 VAL A CG1   1 
ATOM   6840  C  CG2   . VAL A 1 1075 ? 165.487 198.322 178.449 1.00 25.40  ? 2292 VAL A CG2   1 
ATOM   6841  N  N     . HIS A 1 1076 ? 163.433 196.493 182.177 1.00 26.90  ? 2293 HIS A N     1 
ATOM   6842  C  CA    . HIS A 1 1076 ? 162.389 196.363 183.187 1.00 29.27  ? 2293 HIS A CA    1 
ATOM   6843  C  C     . HIS A 1 1076 ? 162.928 196.616 184.590 1.00 32.44  ? 2293 HIS A C     1 
ATOM   6844  O  O     . HIS A 1 1076 ? 162.211 197.151 185.440 1.00 35.97  ? 2293 HIS A O     1 
ATOM   6845  C  CB    . HIS A 1 1076 ? 161.732 194.988 183.119 1.00 31.99  ? 2293 HIS A CB    1 
ATOM   6846  C  CG    . HIS A 1 1076 ? 160.802 194.719 184.260 1.00 27.75  ? 2293 HIS A CG    1 
ATOM   6847  N  ND1   . HIS A 1 1076 ? 159.513 195.204 184.296 1.00 23.66  ? 2293 HIS A ND1   1 
ATOM   6848  C  CD2   . HIS A 1 1076 ? 160.982 194.041 185.418 1.00 25.29  ? 2293 HIS A CD2   1 
ATOM   6849  C  CE1   . HIS A 1 1076 ? 158.934 194.823 185.420 1.00 22.81  ? 2293 HIS A CE1   1 
ATOM   6850  N  NE2   . HIS A 1 1076 ? 159.804 194.117 186.119 1.00 22.68  ? 2293 HIS A NE2   1 
ATOM   6851  N  N     . LEU A 1 1077 ? 164.184 196.243 184.857 1.00 31.85  ? 2294 LEU A N     1 
ATOM   6852  C  CA    . LEU A 1 1077 ? 164.771 196.533 186.164 1.00 31.36  ? 2294 LEU A CA    1 
ATOM   6853  C  C     . LEU A 1 1077 ? 164.876 198.037 186.398 1.00 34.47  ? 2294 LEU A C     1 
ATOM   6854  O  O     . LEU A 1 1077 ? 164.497 198.545 187.465 1.00 36.60  ? 2294 LEU A O     1 
ATOM   6855  C  CB    . LEU A 1 1077 ? 166.147 195.876 186.282 1.00 27.93  ? 2294 LEU A CB    1 
ATOM   6856  C  CG    . LEU A 1 1077 ? 166.196 194.369 186.529 1.00 23.81  ? 2294 LEU A CG    1 
ATOM   6857  C  CD1   . LEU A 1 1077 ? 167.590 193.953 186.958 1.00 22.61  ? 2294 LEU A CD1   1 
ATOM   6858  C  CD2   . LEU A 1 1077 ? 165.169 193.959 187.568 1.00 28.00  ? 2294 LEU A CD2   1 
ATOM   6859  N  N     . ILE A 1 1078 ? 165.368 198.771 185.397 1.00 34.69  ? 2295 ILE A N     1 
ATOM   6860  C  CA    . ILE A 1 1078 ? 165.480 200.218 185.557 1.00 36.59  ? 2295 ILE A CA    1 
ATOM   6861  C  C     . ILE A 1 1078 ? 164.096 200.862 185.626 1.00 38.57  ? 2295 ILE A C     1 
ATOM   6862  O  O     . ILE A 1 1078 ? 163.880 201.821 186.377 1.00 46.28  ? 2295 ILE A O     1 
ATOM   6863  C  CB    . ILE A 1 1078 ? 166.343 200.825 184.438 1.00 39.99  ? 2295 ILE A CB    1 
ATOM   6864  C  CG1   . ILE A 1 1078 ? 167.653 200.052 184.285 1.00 35.32  ? 2295 ILE A CG1   1 
ATOM   6865  C  CG2   . ILE A 1 1078 ? 166.674 202.264 184.751 1.00 47.11  ? 2295 ILE A CG2   1 
ATOM   6866  C  CD1   . ILE A 1 1078 ? 168.601 200.213 185.441 1.00 39.52  ? 2295 ILE A CD1   1 
ATOM   6867  N  N     . SER A 1 1079 ? 163.131 200.338 184.866 1.00 35.63  ? 2296 SER A N     1 
ATOM   6868  C  CA    . SER A 1 1079 ? 161.779 200.887 184.915 1.00 42.98  ? 2296 SER A CA    1 
ATOM   6869  C  C     . SER A 1 1079 ? 161.068 200.541 186.217 1.00 43.88  ? 2296 SER A C     1 
ATOM   6870  O  O     . SER A 1 1079 ? 160.089 201.200 186.579 1.00 43.92  ? 2296 SER A O     1 
ATOM   6871  C  CB    . SER A 1 1079 ? 160.961 200.385 183.727 1.00 47.66  ? 2296 SER A CB    1 
ATOM   6872  O  OG    . SER A 1 1079 ? 159.579 200.613 183.935 1.00 41.58  ? 2296 SER A OG    1 
ATOM   6873  N  N     . SER A 1 1080 ? 161.510 199.491 186.909 1.00 44.33  ? 2297 SER A N     1 
ATOM   6874  C  CA    . SER A 1 1080 ? 160.968 199.208 188.232 1.00 45.39  ? 2297 SER A CA    1 
ATOM   6875  C  C     . SER A 1 1080 ? 161.595 200.104 189.291 1.00 46.36  ? 2297 SER A C     1 
ATOM   6876  O  O     . SER A 1 1080 ? 160.923 200.486 190.255 1.00 46.65  ? 2297 SER A O     1 
ATOM   6877  C  CB    . SER A 1 1080 ? 161.179 197.737 188.584 1.00 45.82  ? 2297 SER A CB    1 
ATOM   6878  O  OG    . SER A 1 1080 ? 162.507 197.502 189.013 1.00 53.00  ? 2297 SER A OG    1 
ATOM   6879  N  N     . TYR A 1 1081 ? 162.871 200.447 189.132 1.00 47.66  ? 2298 TYR A N     1 
ATOM   6880  C  CA    . TYR A 1 1081 ? 163.551 201.308 190.093 1.00 48.94  ? 2298 TYR A CA    1 
ATOM   6881  C  C     . TYR A 1 1081 ? 163.465 202.795 189.744 1.00 56.04  ? 2298 TYR A C     1 
ATOM   6882  O  O     . TYR A 1 1081 ? 164.092 203.611 190.427 1.00 60.90  ? 2298 TYR A O     1 
ATOM   6883  C  CB    . TYR A 1 1081 ? 165.016 200.890 190.227 1.00 48.01  ? 2298 TYR A CB    1 
ATOM   6884  C  CG    . TYR A 1 1081 ? 165.223 199.667 191.088 1.00 48.83  ? 2298 TYR A CG    1 
ATOM   6885  C  CD1   . TYR A 1 1081 ? 164.217 199.205 191.925 1.00 46.54  ? 2298 TYR A CD1   1 
ATOM   6886  C  CD2   . TYR A 1 1081 ? 166.422 198.970 191.058 1.00 53.91  ? 2298 TYR A CD2   1 
ATOM   6887  C  CE1   . TYR A 1 1081 ? 164.402 198.086 192.712 1.00 50.17  ? 2298 TYR A CE1   1 
ATOM   6888  C  CE2   . TYR A 1 1081 ? 166.615 197.849 191.839 1.00 52.58  ? 2298 TYR A CE2   1 
ATOM   6889  C  CZ    . TYR A 1 1081 ? 165.603 197.412 192.665 1.00 54.07  ? 2298 TYR A CZ    1 
ATOM   6890  O  OH    . TYR A 1 1081 ? 165.792 196.296 193.446 1.00 61.00  ? 2298 TYR A OH    1 
ATOM   6891  N  N     . ARG A 1 1082 ? 162.718 203.159 188.695 1.00 58.27  ? 2299 ARG A N     1 
ATOM   6892  C  CA    . ARG A 1 1082 ? 162.597 204.557 188.279 1.00 61.07  ? 2299 ARG A CA    1 
ATOM   6893  C  C     . ARG A 1 1082 ? 162.022 205.477 189.354 1.00 68.99  ? 2299 ARG A C     1 
ATOM   6894  O  O     . ARG A 1 1082 ? 162.224 206.693 189.271 1.00 70.27  ? 2299 ARG A O     1 
ATOM   6895  C  CB    . ARG A 1 1082 ? 161.709 204.665 187.035 1.00 61.76  ? 2299 ARG A CB    1 
ATOM   6896  C  CG    . ARG A 1 1082 ? 160.256 204.280 187.295 1.00 62.25  ? 2299 ARG A CG    1 
ATOM   6897  C  CD    . ARG A 1 1082 ? 159.378 204.338 186.050 1.00 60.11  ? 2299 ARG A CD    1 
ATOM   6898  N  NE    . ARG A 1 1082 ? 159.180 205.692 185.549 1.00 65.88  ? 2299 ARG A NE    1 
ATOM   6899  C  CZ    . ARG A 1 1082 ? 158.682 205.978 184.354 1.00 69.15  ? 2299 ARG A CZ    1 
ATOM   6900  N  NH1   . ARG A 1 1082 ? 158.315 205.027 183.511 1.00 63.24  ? 2299 ARG A NH1   1 
ATOM   6901  N  NH2   . ARG A 1 1082 ? 158.541 207.252 183.998 1.00 74.93  ? 2299 ARG A NH2   1 
ATOM   6902  N  N     . GLN A 1 1083 ? 161.298 204.938 190.341 1.00 71.20  ? 2300 GLN A N     1 
ATOM   6903  C  CA    . GLN A 1 1083 ? 160.578 205.789 191.287 1.00 73.03  ? 2300 GLN A CA    1 
ATOM   6904  C  C     . GLN A 1 1083 ? 161.525 206.617 192.149 1.00 74.82  ? 2300 GLN A C     1 
ATOM   6905  O  O     . GLN A 1 1083 ? 161.257 207.794 192.415 1.00 78.84  ? 2300 GLN A O     1 
ATOM   6906  C  CB    . GLN A 1 1083 ? 159.660 204.943 192.169 1.00 75.16  ? 2300 GLN A CB    1 
ATOM   6907  C  CG    . GLN A 1 1083 ? 158.735 204.018 191.399 1.00 80.31  ? 2300 GLN A CG    1 
ATOM   6908  C  CD    . GLN A 1 1083 ? 157.605 204.764 190.722 1.00 83.84  ? 2300 GLN A CD    1 
ATOM   6909  O  OE1   . GLN A 1 1083 ? 157.113 205.769 191.238 1.00 88.99  ? 2300 GLN A OE1   1 
ATOM   6910  N  NE2   . GLN A 1 1083 ? 157.185 204.277 189.561 1.00 75.24  ? 2300 GLN A NE2   1 
ATOM   6911  N  N     . TRP A 1 1084 ? 162.633 206.029 192.592 1.00 74.83  ? 2301 TRP A N     1 
ATOM   6912  C  CA    . TRP A 1 1084 ? 163.558 206.699 193.504 1.00 79.93  ? 2301 TRP A CA    1 
ATOM   6913  C  C     . TRP A 1 1084 ? 164.822 207.172 192.797 1.00 81.27  ? 2301 TRP A C     1 
ATOM   6914  O  O     . TRP A 1 1084 ? 165.918 207.107 193.360 1.00 81.47  ? 2301 TRP A O     1 
ATOM   6915  C  CB    . TRP A 1 1084 ? 163.910 205.777 194.666 1.00 80.91  ? 2301 TRP A CB    1 
ATOM   6916  C  CG    . TRP A 1 1084 ? 162.758 205.493 195.574 1.00 83.92  ? 2301 TRP A CG    1 
ATOM   6917  C  CD1   . TRP A 1 1084 ? 162.378 206.214 196.668 1.00 88.76  ? 2301 TRP A CD1   1 
ATOM   6918  C  CD2   . TRP A 1 1084 ? 161.841 204.398 195.477 1.00 83.68  ? 2301 TRP A CD2   1 
ATOM   6919  N  NE1   . TRP A 1 1084 ? 161.276 205.641 197.253 1.00 91.44  ? 2301 TRP A NE1   1 
ATOM   6920  C  CE2   . TRP A 1 1084 ? 160.927 204.523 196.541 1.00 89.05  ? 2301 TRP A CE2   1 
ATOM   6921  C  CE3   . TRP A 1 1084 ? 161.704 203.324 194.593 1.00 82.33  ? 2301 TRP A CE3   1 
ATOM   6922  C  CZ2   . TRP A 1 1084 ? 159.889 203.616 196.744 1.00 88.87  ? 2301 TRP A CZ2   1 
ATOM   6923  C  CZ3   . TRP A 1 1084 ? 160.672 202.426 194.795 1.00 83.69  ? 2301 TRP A CZ3   1 
ATOM   6924  C  CH2   . TRP A 1 1084 ? 159.779 202.577 195.862 1.00 86.17  ? 2301 TRP A CH2   1 
ATOM   6925  N  N     . PHE A 1 1085 ? 164.701 207.654 191.560 1.00 80.58  ? 2302 PHE A N     1 
ATOM   6926  C  CA    . PHE A 1 1085 ? 165.859 208.065 190.778 1.00 81.31  ? 2302 PHE A CA    1 
ATOM   6927  C  C     . PHE A 1 1085 ? 166.048 209.575 190.710 1.00 89.31  ? 2302 PHE A C     1 
ATOM   6928  O  O     . PHE A 1 1085 ? 167.101 210.028 190.249 1.00 93.99  ? 2302 PHE A O     1 
ATOM   6929  C  CB    . PHE A 1 1085 ? 165.760 207.509 189.352 1.00 74.26  ? 2302 PHE A CB    1 
ATOM   6930  C  CG    . PHE A 1 1085 ? 166.215 206.085 189.223 1.00 70.69  ? 2302 PHE A CG    1 
ATOM   6931  C  CD1   . PHE A 1 1085 ? 166.760 205.414 190.307 1.00 71.34  ? 2302 PHE A CD1   1 
ATOM   6932  C  CD2   . PHE A 1 1085 ? 166.108 205.420 188.014 1.00 68.08  ? 2302 PHE A CD2   1 
ATOM   6933  C  CE1   . PHE A 1 1085 ? 167.184 204.104 190.187 1.00 64.68  ? 2302 PHE A CE1   1 
ATOM   6934  C  CE2   . PHE A 1 1085 ? 166.529 204.111 187.888 1.00 63.13  ? 2302 PHE A CE2   1 
ATOM   6935  C  CZ    . PHE A 1 1085 ? 167.070 203.454 188.975 1.00 59.46  ? 2302 PHE A CZ    1 
ATOM   6936  N  N     . GLN A 1 1086 ? 165.069 210.362 191.152 1.00 91.51  ? 2303 GLN A N     1 
ATOM   6937  C  CA    . GLN A 1 1086 ? 165.175 211.812 191.061 1.00 92.96  ? 2303 GLN A CA    1 
ATOM   6938  C  C     . GLN A 1 1086 ? 166.018 212.422 192.172 1.00 91.89  ? 2303 GLN A C     1 
ATOM   6939  O  O     . GLN A 1 1086 ? 166.296 213.625 192.124 1.00 89.85  ? 2303 GLN A O     1 
ATOM   6940  C  CB    . GLN A 1 1086 ? 163.782 212.445 191.076 1.00 93.86  ? 2303 GLN A CB    1 
ATOM   6941  C  CG    . GLN A 1 1086 ? 163.040 212.282 192.393 1.00 92.31  ? 2303 GLN A CG    1 
ATOM   6942  C  CD    . GLN A 1 1086 ? 162.136 211.066 192.408 1.00 87.57  ? 2303 GLN A CD    1 
ATOM   6943  O  OE1   . GLN A 1 1086 ? 161.941 210.411 191.384 1.00 85.83  ? 2303 GLN A OE1   1 
ATOM   6944  N  NE2   . GLN A 1 1086 ? 161.578 210.757 193.572 1.00 84.18  ? 2303 GLN A NE2   1 
ATOM   6945  N  N     . ASN A 1 1087 ? 166.431 211.635 193.162 1.00 91.09  ? 2304 ASN A N     1 
ATOM   6946  C  CA    . ASN A 1 1087 ? 167.140 212.141 194.333 1.00 93.36  ? 2304 ASN A CA    1 
ATOM   6947  C  C     . ASN A 1 1087 ? 168.416 211.344 194.578 1.00 93.33  ? 2304 ASN A C     1 
ATOM   6948  O  O     . ASN A 1 1087 ? 168.712 210.920 195.697 1.00 95.95  ? 2304 ASN A O     1 
ATOM   6949  C  CB    . ASN A 1 1087 ? 166.233 212.117 195.561 1.00 95.84  ? 2304 ASN A CB    1 
ATOM   6950  C  CG    . ASN A 1 1087 ? 165.507 210.797 195.725 1.00 93.80  ? 2304 ASN A CG    1 
ATOM   6951  O  OD1   . ASN A 1 1087 ? 165.726 209.855 194.964 1.00 90.32  ? 2304 ASN A OD1   1 
ATOM   6952  N  ND2   . ASN A 1 1087 ? 164.632 210.724 196.721 1.00 92.73  ? 2304 ASN A ND2   1 
ATOM   6953  N  N     . LEU A 1 1088 ? 169.194 211.127 193.520 1.00 90.87  ? 2305 LEU A N     1 
ATOM   6954  C  CA    . LEU A 1 1088 ? 170.479 210.455 193.635 1.00 93.38  ? 2305 LEU A CA    1 
ATOM   6955  C  C     . LEU A 1 1088 ? 171.474 211.103 192.684 1.00 92.75  ? 2305 LEU A C     1 
ATOM   6956  O  O     . LEU A 1 1088 ? 171.097 211.656 191.648 1.00 91.16  ? 2305 LEU A O     1 
ATOM   6957  C  CB    . LEU A 1 1088 ? 170.364 208.953 193.339 1.00 94.28  ? 2305 LEU A CB    1 
ATOM   6958  C  CG    . LEU A 1 1088 ? 171.374 208.040 194.040 1.00 88.44  ? 2305 LEU A CG    1 
ATOM   6959  C  CD1   . LEU A 1 1088 ? 171.535 208.422 195.505 1.00 85.65  ? 2305 LEU A CD1   1 
ATOM   6960  C  CD2   . LEU A 1 1088 ? 170.968 206.580 193.906 1.00 81.31  ? 2305 LEU A CD2   1 
ATOM   6961  N  N     . ASP A 1 1089 ? 172.751 211.026 193.049 1.00 94.22  ? 2306 ASP A N     1 
ATOM   6962  C  CA    . ASP A 1 1089 ? 173.804 211.611 192.235 1.00 94.56  ? 2306 ASP A CA    1 
ATOM   6963  C  C     . ASP A 1 1089 ? 174.055 210.759 190.993 1.00 92.89  ? 2306 ASP A C     1 
ATOM   6964  O  O     . ASP A 1 1089 ? 173.614 209.611 190.887 1.00 89.16  ? 2306 ASP A O     1 
ATOM   6965  C  CB    . ASP A 1 1089 ? 175.088 211.766 193.049 1.00 92.69  ? 2306 ASP A CB    1 
ATOM   6966  C  CG    . ASP A 1 1089 ? 175.466 210.499 193.786 1.00 95.00  ? 2306 ASP A CG    1 
ATOM   6967  O  OD1   . ASP A 1 1089 ? 174.592 209.925 194.469 1.00 97.91  ? 2306 ASP A OD1   1 
ATOM   6968  O  OD2   . ASP A 1 1089 ? 176.637 210.076 193.684 1.00 96.88  ? 2306 ASP A OD2   1 
ATOM   6969  N  N     . ASP A 1 1090 ? 174.779 211.347 190.035 1.00 93.32  ? 2307 ASP A N     1 
ATOM   6970  C  CA    . ASP A 1 1090 ? 175.030 210.667 188.769 1.00 88.44  ? 2307 ASP A CA    1 
ATOM   6971  C  C     . ASP A 1 1090 ? 175.952 209.467 188.941 1.00 84.80  ? 2307 ASP A C     1 
ATOM   6972  O  O     . ASP A 1 1090 ? 175.801 208.471 188.227 1.00 81.15  ? 2307 ASP A O     1 
ATOM   6973  C  CB    . ASP A 1 1090 ? 175.619 211.645 187.753 1.00 90.28  ? 2307 ASP A CB    1 
ATOM   6974  C  CG    . ASP A 1 1090 ? 175.314 211.251 186.321 1.00 88.94  ? 2307 ASP A CG    1 
ATOM   6975  O  OD1   . ASP A 1 1090 ? 174.752 210.156 186.108 1.00 81.39  ? 2307 ASP A OD1   1 
ATOM   6976  O  OD2   . ASP A 1 1090 ? 175.633 212.038 185.406 1.00 92.61  ? 2307 ASP A OD2   1 
ATOM   6977  N  N     . LYS A 1 1091 ? 176.904 209.539 189.874 1.00 86.80  ? 2308 LYS A N     1 
ATOM   6978  C  CA    . LYS A 1 1091 ? 177.815 208.419 190.096 1.00 84.91  ? 2308 LYS A CA    1 
ATOM   6979  C  C     . LYS A 1 1091 ? 177.076 207.206 190.652 1.00 82.97  ? 2308 LYS A C     1 
ATOM   6980  O  O     . LYS A 1 1091 ? 177.244 206.083 190.160 1.00 78.50  ? 2308 LYS A O     1 
ATOM   6981  C  CB    . LYS A 1 1091 ? 178.941 208.844 191.038 1.00 82.74  ? 2308 LYS A CB    1 
ATOM   6982  C  CG    . LYS A 1 1091 ? 180.096 207.860 191.117 1.00 82.80  ? 2308 LYS A CG    1 
ATOM   6983  C  CD    . LYS A 1 1091 ? 180.816 207.741 189.786 1.00 87.70  ? 2308 LYS A CD    1 
ATOM   6984  C  CE    . LYS A 1 1091 ? 182.207 207.156 189.968 1.00 92.50  ? 2308 LYS A CE    1 
ATOM   6985  N  NZ    . LYS A 1 1091 ? 182.179 205.872 190.719 1.00 90.93  ? 2308 LYS A NZ    1 
ATOM   6986  N  N     . SER A 1 1092 ? 176.237 207.417 191.670 1.00 84.48  ? 2309 SER A N     1 
ATOM   6987  C  CA    . SER A 1 1092 ? 175.507 206.304 192.271 1.00 84.61  ? 2309 SER A CA    1 
ATOM   6988  C  C     . SER A 1 1092 ? 174.457 205.747 191.317 1.00 77.80  ? 2309 SER A C     1 
ATOM   6989  O  O     . SER A 1 1092 ? 174.254 204.529 191.254 1.00 76.07  ? 2309 SER A O     1 
ATOM   6990  C  CB    . SER A 1 1092 ? 174.861 206.748 193.582 1.00 90.51  ? 2309 SER A CB    1 
ATOM   6991  O  OG    . SER A 1 1092 ? 175.842 206.985 194.577 1.00 91.53  ? 2309 SER A OG    1 
ATOM   6992  N  N     . LEU A 1 1093 ? 173.781 206.623 190.569 1.00 77.11  ? 2310 LEU A N     1 
ATOM   6993  C  CA    . LEU A 1 1093 ? 172.815 206.161 189.577 1.00 72.65  ? 2310 LEU A CA    1 
ATOM   6994  C  C     . LEU A 1 1093 ? 173.496 205.369 188.467 1.00 67.66  ? 2310 LEU A C     1 
ATOM   6995  O  O     . LEU A 1 1093 ? 172.973 204.342 188.017 1.00 63.78  ? 2310 LEU A O     1 
ATOM   6996  C  CB    . LEU A 1 1093 ? 172.051 207.351 188.997 1.00 73.84  ? 2310 LEU A CB    1 
ATOM   6997  C  CG    . LEU A 1 1093 ? 170.789 207.021 188.202 1.00 64.98  ? 2310 LEU A CG    1 
ATOM   6998  C  CD1   . LEU A 1 1093 ? 169.960 205.991 188.932 1.00 65.52  ? 2310 LEU A CD1   1 
ATOM   6999  C  CD2   . LEU A 1 1093 ? 169.975 208.279 187.948 1.00 65.84  ? 2310 LEU A CD2   1 
ATOM   7000  N  N     . LYS A 1 1094 ? 174.667 205.829 188.020 1.00 69.98  ? 2311 LYS A N     1 
ATOM   7001  C  CA    . LYS A 1 1094 ? 175.421 205.099 187.009 1.00 65.15  ? 2311 LYS A CA    1 
ATOM   7002  C  C     . LYS A 1 1094 ? 175.872 203.744 187.533 1.00 63.90  ? 2311 LYS A C     1 
ATOM   7003  O  O     . LYS A 1 1094 ? 175.831 202.747 186.806 1.00 63.59  ? 2311 LYS A O     1 
ATOM   7004  C  CB    . LYS A 1 1094 ? 176.622 205.928 186.555 1.00 71.77  ? 2311 LYS A CB    1 
ATOM   7005  C  CG    . LYS A 1 1094 ? 177.417 205.318 185.414 1.00 71.37  ? 2311 LYS A CG    1 
ATOM   7006  C  CD    . LYS A 1 1094 ? 178.559 206.234 185.000 1.00 71.27  ? 2311 LYS A CD    1 
ATOM   7007  C  CE    . LYS A 1 1094 ? 179.313 205.679 183.805 1.00 69.90  ? 2311 LYS A CE    1 
ATOM   7008  N  NZ    . LYS A 1 1094 ? 178.676 206.083 182.522 1.00 64.93  ? 2311 LYS A NZ    1 
ATOM   7009  N  N     . ASP A 1 1095 ? 176.292 203.685 188.801 1.00 65.02  ? 2312 ASP A N     1 
ATOM   7010  C  CA    . ASP A 1 1095 ? 176.691 202.410 189.393 1.00 66.96  ? 2312 ASP A CA    1 
ATOM   7011  C  C     . ASP A 1 1095 ? 175.510 201.451 189.516 1.00 64.26  ? 2312 ASP A C     1 
ATOM   7012  O  O     . ASP A 1 1095 ? 175.654 200.250 189.261 1.00 61.41  ? 2312 ASP A O     1 
ATOM   7013  C  CB    . ASP A 1 1095 ? 177.337 202.646 190.757 1.00 73.36  ? 2312 ASP A CB    1 
ATOM   7014  C  CG    . ASP A 1 1095 ? 178.849 202.712 190.682 1.00 77.64  ? 2312 ASP A CG    1 
ATOM   7015  O  OD1   . ASP A 1 1095 ? 179.393 202.626 189.561 1.00 79.95  ? 2312 ASP A OD1   1 
ATOM   7016  O  OD2   . ASP A 1 1095 ? 179.495 202.849 191.742 1.00 78.89  ? 2312 ASP A OD2   1 
ATOM   7017  N  N     . VAL A 1 1096 ? 174.337 201.961 189.904 1.00 62.50  ? 2313 VAL A N     1 
ATOM   7018  C  CA    . VAL A 1 1096 ? 173.146 201.118 190.014 1.00 55.93  ? 2313 VAL A CA    1 
ATOM   7019  C  C     . VAL A 1 1096 ? 172.740 200.582 188.646 1.00 53.33  ? 2313 VAL A C     1 
ATOM   7020  O  O     . VAL A 1 1096 ? 172.430 199.390 188.491 1.00 53.79  ? 2313 VAL A O     1 
ATOM   7021  C  CB    . VAL A 1 1096 ? 172.001 201.906 190.679 1.00 52.93  ? 2313 VAL A CB    1 
ATOM   7022  C  CG1   . VAL A 1 1096 ? 170.656 201.251 190.408 1.00 51.69  ? 2313 VAL A CG1   1 
ATOM   7023  C  CG2   . VAL A 1 1096 ? 172.242 202.024 192.173 1.00 60.10  ? 2313 VAL A CG2   1 
ATOM   7024  N  N     . ILE A 1 1097 ? 172.745 201.451 187.632 1.00 52.37  ? 2314 ILE A N     1 
ATOM   7025  C  CA    . ILE A 1 1097 ? 172.401 201.034 186.275 1.00 48.29  ? 2314 ILE A CA    1 
ATOM   7026  C  C     . ILE A 1 1097 ? 173.400 200.003 185.765 1.00 43.70  ? 2314 ILE A C     1 
ATOM   7027  O  O     . ILE A 1 1097 ? 173.022 199.003 185.141 1.00 44.21  ? 2314 ILE A O     1 
ATOM   7028  C  CB    . ILE A 1 1097 ? 172.320 202.268 185.356 1.00 48.69  ? 2314 ILE A CB    1 
ATOM   7029  C  CG1   . ILE A 1 1097 ? 170.996 202.995 185.580 1.00 48.18  ? 2314 ILE A CG1   1 
ATOM   7030  C  CG2   . ILE A 1 1097 ? 172.462 201.881 183.895 1.00 48.63  ? 2314 ILE A CG2   1 
ATOM   7031  C  CD1   . ILE A 1 1097 ? 170.876 204.284 184.827 1.00 51.83  ? 2314 ILE A CD1   1 
ATOM   7032  N  N     . THR A 1 1098 ? 174.688 200.219 186.040 1.00 43.87  ? 2315 THR A N     1 
ATOM   7033  C  CA    . THR A 1 1098 ? 175.710 199.270 185.620 1.00 44.82  ? 2315 THR A CA    1 
ATOM   7034  C  C     . THR A 1 1098 ? 175.535 197.922 186.305 1.00 47.01  ? 2315 THR A C     1 
ATOM   7035  O  O     . THR A 1 1098 ? 175.694 196.875 185.670 1.00 50.16  ? 2315 THR A O     1 
ATOM   7036  C  CB    . THR A 1 1098 ? 177.095 199.844 185.908 1.00 57.02  ? 2315 THR A CB    1 
ATOM   7037  O  OG1   . THR A 1 1098 ? 177.199 201.150 185.328 1.00 59.02  ? 2315 THR A OG1   1 
ATOM   7038  C  CG2   . THR A 1 1098 ? 178.170 198.950 185.327 1.00 55.87  ? 2315 THR A CG2   1 
ATOM   7039  N  N     . LEU A 1 1099 ? 175.196 197.926 187.598 1.00 45.45  ? 2316 LEU A N     1 
ATOM   7040  C  CA    . LEU A 1 1099 ? 174.964 196.671 188.309 1.00 46.38  ? 2316 LEU A CA    1 
ATOM   7041  C  C     . LEU A 1 1099 ? 173.771 195.922 187.730 1.00 43.34  ? 2316 LEU A C     1 
ATOM   7042  O  O     . LEU A 1 1099 ? 173.822 194.698 187.559 1.00 41.99  ? 2316 LEU A O     1 
ATOM   7043  C  CB    . LEU A 1 1099 ? 174.773 196.942 189.806 1.00 50.34  ? 2316 LEU A CB    1 
ATOM   7044  C  CG    . LEU A 1 1099 ? 174.680 195.776 190.805 1.00 55.25  ? 2316 LEU A CG    1 
ATOM   7045  C  CD1   . LEU A 1 1099 ? 175.175 196.199 192.172 1.00 69.89  ? 2316 LEU A CD1   1 
ATOM   7046  C  CD2   . LEU A 1 1099 ? 173.248 195.260 190.951 1.00 43.02  ? 2316 LEU A CD2   1 
ATOM   7047  N  N     . LEU A 1 1100 ? 172.684 196.634 187.429 1.00 39.50  ? 2317 LEU A N     1 
ATOM   7048  C  CA    . LEU A 1 1100 ? 171.510 195.959 186.883 1.00 32.18  ? 2317 LEU A CA    1 
ATOM   7049  C  C     . LEU A 1 1100 ? 171.779 195.418 185.481 1.00 33.00  ? 2317 LEU A C     1 
ATOM   7050  O  O     . LEU A 1 1100 ? 171.304 194.332 185.129 1.00 30.86  ? 2317 LEU A O     1 
ATOM   7051  C  CB    . LEU A 1 1100 ? 170.310 196.903 186.893 1.00 29.64  ? 2317 LEU A CB    1 
ATOM   7052  C  CG    . LEU A 1 1100 ? 169.826 197.244 188.307 1.00 33.40  ? 2317 LEU A CG    1 
ATOM   7053  C  CD1   . LEU A 1 1100 ? 168.472 197.921 188.285 1.00 33.79  ? 2317 LEU A CD1   1 
ATOM   7054  C  CD2   . LEU A 1 1100 ? 169.784 196.004 189.187 1.00 35.41  ? 2317 LEU A CD2   1 
ATOM   7055  N  N     . ILE A 1 1101 ? 172.556 196.146 184.676 1.00 37.90  ? 2318 ILE A N     1 
ATOM   7056  C  CA    . ILE A 1 1101 ? 172.925 195.647 183.353 1.00 33.62  ? 2318 ILE A CA    1 
ATOM   7057  C  C     . ILE A 1 1101 ? 173.835 194.428 183.468 1.00 34.87  ? 2318 ILE A C     1 
ATOM   7058  O  O     . ILE A 1 1101 ? 173.695 193.461 182.707 1.00 37.59  ? 2318 ILE A O     1 
ATOM   7059  C  CB    . ILE A 1 1101 ? 173.564 196.772 182.518 1.00 29.10  ? 2318 ILE A CB    1 
ATOM   7060  C  CG1   . ILE A 1 1101 ? 172.505 197.805 182.147 1.00 28.39  ? 2318 ILE A CG1   1 
ATOM   7061  C  CG2   . ILE A 1 1101 ? 174.226 196.228 181.268 1.00 28.04  ? 2318 ILE A CG2   1 
ATOM   7062  C  CD1   . ILE A 1 1101 ? 173.070 199.030 181.513 1.00 30.65  ? 2318 ILE A CD1   1 
ATOM   7063  N  N     . LYS A 1 1102 ? 174.768 194.444 184.424 1.00 34.48  ? 2319 LYS A N     1 
ATOM   7064  C  CA    . LYS A 1 1102 ? 175.615 193.276 184.654 1.00 36.42  ? 2319 LYS A CA    1 
ATOM   7065  C  C     . LYS A 1 1102 ? 174.784 192.074 185.076 1.00 36.80  ? 2319 LYS A C     1 
ATOM   7066  O  O     . LYS A 1 1102 ? 175.039 190.947 184.636 1.00 35.58  ? 2319 LYS A O     1 
ATOM   7067  C  CB    . LYS A 1 1102 ? 176.668 193.588 185.717 1.00 41.22  ? 2319 LYS A CB    1 
ATOM   7068  C  CG    . LYS A 1 1102 ? 177.800 194.480 185.247 1.00 45.21  ? 2319 LYS A CG    1 
ATOM   7069  C  CD    . LYS A 1 1102 ? 178.563 195.049 186.428 1.00 50.76  ? 2319 LYS A CD    1 
ATOM   7070  C  CE    . LYS A 1 1102 ? 179.904 195.609 185.997 1.00 59.09  ? 2319 LYS A CE    1 
ATOM   7071  N  NZ    . LYS A 1 1102 ? 180.323 196.767 186.830 1.00 69.90  ? 2319 LYS A NZ    1 
ATOM   7072  N  N     . ARG A 1 1103 ? 173.781 192.299 185.927 1.00 32.54  ? 2320 ARG A N     1 
ATOM   7073  C  CA    . ARG A 1 1103 ? 172.907 191.213 186.357 1.00 30.71  ? 2320 ARG A CA    1 
ATOM   7074  C  C     . ARG A 1 1103 ? 172.099 190.657 185.193 1.00 31.18  ? 2320 ARG A C     1 
ATOM   7075  O  O     . ARG A 1 1103 ? 171.948 189.436 185.059 1.00 34.29  ? 2320 ARG A O     1 
ATOM   7076  C  CB    . ARG A 1 1103 ? 171.990 191.706 187.474 1.00 31.82  ? 2320 ARG A CB    1 
ATOM   7077  C  CG    . ARG A 1 1103 ? 170.724 190.903 187.657 1.00 28.86  ? 2320 ARG A CG    1 
ATOM   7078  C  CD    . ARG A 1 1103 ? 170.141 191.159 189.025 1.00 28.52  ? 2320 ARG A CD    1 
ATOM   7079  N  NE    . ARG A 1 1103 ? 169.097 190.200 189.354 1.00 28.79  ? 2320 ARG A NE    1 
ATOM   7080  C  CZ    . ARG A 1 1103 ? 168.190 190.383 190.301 1.00 34.61  ? 2320 ARG A CZ    1 
ATOM   7081  N  NH1   . ARG A 1 1103 ? 168.175 191.480 191.040 1.00 36.02  ? 2320 ARG A NH1   1 
ATOM   7082  N  NH2   . ARG A 1 1103 ? 167.274 189.443 190.511 1.00 34.07  ? 2320 ARG A NH2   1 
ATOM   7083  N  N     . SER A 1 1104 ? 171.581 191.541 184.335 1.00 29.20  ? 2321 SER A N     1 
ATOM   7084  C  CA    . SER A 1 1104 ? 170.839 191.094 183.161 1.00 24.97  ? 2321 SER A CA    1 
ATOM   7085  C  C     . SER A 1 1104 ? 171.720 190.270 182.232 1.00 23.29  ? 2321 SER A C     1 
ATOM   7086  O  O     . SER A 1 1104 ? 171.307 189.208 181.755 1.00 25.14  ? 2321 SER A O     1 
ATOM   7087  C  CB    . SER A 1 1104 ? 170.262 192.297 182.418 1.00 24.41  ? 2321 SER A CB    1 
ATOM   7088  O  OG    . SER A 1 1104 ? 171.270 192.977 181.692 1.00 26.68  ? 2321 SER A OG    1 
ATOM   7089  N  N     . LEU A 1 1105 ? 172.945 190.735 181.981 1.00 24.56  ? 2322 LEU A N     1 
ATOM   7090  C  CA    . LEU A 1 1105 ? 173.857 189.991 181.119 1.00 26.69  ? 2322 LEU A CA    1 
ATOM   7091  C  C     . LEU A 1 1105 ? 174.218 188.640 181.724 1.00 27.41  ? 2322 LEU A C     1 
ATOM   7092  O  O     . LEU A 1 1105 ? 174.274 187.631 181.012 1.00 30.43  ? 2322 LEU A O     1 
ATOM   7093  C  CB    . LEU A 1 1105 ? 175.117 190.815 180.853 1.00 29.80  ? 2322 LEU A CB    1 
ATOM   7094  C  CG    . LEU A 1 1105 ? 174.924 192.070 180.004 1.00 26.20  ? 2322 LEU A CG    1 
ATOM   7095  C  CD1   . LEU A 1 1105 ? 176.020 193.082 180.280 1.00 27.54  ? 2322 LEU A CD1   1 
ATOM   7096  C  CD2   . LEU A 1 1105 ? 174.883 191.701 178.537 1.00 26.51  ? 2322 LEU A CD2   1 
ATOM   7097  N  N     . LEU A 1 1106 ? 174.456 188.597 183.038 1.00 26.50  ? 2323 LEU A N     1 
ATOM   7098  C  CA    . LEU A 1 1106 ? 174.842 187.344 183.680 1.00 28.20  ? 2323 LEU A CA    1 
ATOM   7099  C  C     . LEU A 1 1106 ? 173.702 186.333 183.668 1.00 31.55  ? 2323 LEU A C     1 
ATOM   7100  O  O     . LEU A 1 1106 ? 173.924 185.147 183.395 1.00 29.46  ? 2323 LEU A O     1 
ATOM   7101  C  CB    . LEU A 1 1106 ? 175.307 187.611 185.111 1.00 27.85  ? 2323 LEU A CB    1 
ATOM   7102  C  CG    . LEU A 1 1106 ? 175.480 186.389 186.015 1.00 28.48  ? 2323 LEU A CG    1 
ATOM   7103  C  CD1   . LEU A 1 1106 ? 176.556 185.454 185.479 1.00 32.63  ? 2323 LEU A CD1   1 
ATOM   7104  C  CD2   . LEU A 1 1106 ? 175.790 186.812 187.440 1.00 32.09  ? 2323 LEU A CD2   1 
ATOM   7105  N  N     . TYR A 1 1107 ? 172.477 186.774 183.948 1.00 30.59  ? 2324 TYR A N     1 
ATOM   7106  C  CA    . TYR A 1 1107 ? 171.343 185.860 184.001 1.00 21.68  ? 2324 TYR A CA    1 
ATOM   7107  C  C     . TYR A 1 1107 ? 170.655 185.682 182.656 1.00 21.18  ? 2324 TYR A C     1 
ATOM   7108  O  O     . TYR A 1 1107 ? 169.645 184.975 182.585 1.00 21.44  ? 2324 TYR A O     1 
ATOM   7109  C  CB    . TYR A 1 1107 ? 170.333 186.332 185.047 1.00 18.45  ? 2324 TYR A CB    1 
ATOM   7110  C  CG    . TYR A 1 1107 ? 170.849 186.205 186.460 1.00 21.73  ? 2324 TYR A CG    1 
ATOM   7111  C  CD1   . TYR A 1 1107 ? 171.195 184.968 186.983 1.00 23.74  ? 2324 TYR A CD1   1 
ATOM   7112  C  CD2   . TYR A 1 1107 ? 171.006 187.323 187.265 1.00 25.94  ? 2324 TYR A CD2   1 
ATOM   7113  C  CE1   . TYR A 1 1107 ? 171.674 184.847 188.273 1.00 25.92  ? 2324 TYR A CE1   1 
ATOM   7114  C  CE2   . TYR A 1 1107 ? 171.485 187.213 188.555 1.00 31.11  ? 2324 TYR A CE2   1 
ATOM   7115  C  CZ    . TYR A 1 1107 ? 171.817 185.973 189.054 1.00 32.59  ? 2324 TYR A CZ    1 
ATOM   7116  O  OH    . TYR A 1 1107 ? 172.294 185.863 190.339 1.00 35.87  ? 2324 TYR A OH    1 
ATOM   7117  N  N     . ALA A 1 1108 ? 171.163 186.310 181.596 1.00 23.87  ? 2325 ALA A N     1 
ATOM   7118  C  CA    . ALA A 1 1108 ? 170.704 186.027 180.241 1.00 22.81  ? 2325 ALA A CA    1 
ATOM   7119  C  C     . ALA A 1 1108 ? 171.696 185.167 179.469 1.00 25.47  ? 2325 ALA A C     1 
ATOM   7120  O  O     . ALA A 1 1108 ? 171.332 184.107 178.954 1.00 30.04  ? 2325 ALA A O     1 
ATOM   7121  C  CB    . ALA A 1 1108 ? 170.454 187.338 179.489 1.00 20.78  ? 2325 ALA A CB    1 
ATOM   7122  N  N     . LEU A 1 1109 ? 172.951 185.613 179.375 1.00 24.56  ? 2326 LEU A N     1 
ATOM   7123  C  CA    . LEU A 1 1109 ? 173.929 184.918 178.544 1.00 25.75  ? 2326 LEU A CA    1 
ATOM   7124  C  C     . LEU A 1 1109 ? 174.326 183.577 179.147 1.00 27.68  ? 2326 LEU A C     1 
ATOM   7125  O  O     . LEU A 1 1109 ? 174.341 182.554 178.453 1.00 30.91  ? 2326 LEU A O     1 
ATOM   7126  C  CB    . LEU A 1 1109 ? 175.156 185.803 178.341 1.00 29.60  ? 2326 LEU A CB    1 
ATOM   7127  C  CG    . LEU A 1 1109 ? 174.820 187.154 177.716 1.00 38.39  ? 2326 LEU A CG    1 
ATOM   7128  C  CD1   . LEU A 1 1109 ? 175.989 188.114 177.827 1.00 39.15  ? 2326 LEU A CD1   1 
ATOM   7129  C  CD2   . LEU A 1 1109 ? 174.398 186.963 176.271 1.00 39.35  ? 2326 LEU A CD2   1 
ATOM   7130  N  N     . ALA A 1 1110 ? 174.652 183.559 180.437 1.00 26.16  ? 2327 ALA A N     1 
ATOM   7131  C  CA    . ALA A 1 1110 ? 175.072 182.336 181.108 1.00 27.36  ? 2327 ALA A CA    1 
ATOM   7132  C  C     . ALA A 1 1110 ? 174.165 182.001 182.283 1.00 30.05  ? 2327 ALA A C     1 
ATOM   7133  O  O     . ALA A 1 1110 ? 174.602 181.392 183.259 1.00 38.92  ? 2327 ALA A O     1 
ATOM   7134  C  CB    . ALA A 1 1110 ? 176.525 182.430 181.566 1.00 33.03  ? 2327 ALA A CB    1 
ATOM   7135  N  N     . GLY A 1 1111 ? 172.895 182.398 182.204 1.00 27.01  ? 2328 GLY A N     1 
ATOM   7136  C  CA    . GLY A 1 1111 ? 171.918 181.882 183.141 1.00 24.89  ? 2328 GLY A CA    1 
ATOM   7137  C  C     . GLY A 1 1111 ? 171.578 180.428 182.905 1.00 23.97  ? 2328 GLY A C     1 
ATOM   7138  O  O     . GLY A 1 1111 ? 170.962 179.796 183.769 1.00 23.05  ? 2328 GLY A O     1 
ATOM   7139  N  N     . ASP A 1 1112 ? 171.975 179.884 181.755 1.00 26.09  ? 2329 ASP A N     1 
ATOM   7140  C  CA    . ASP A 1 1112 ? 171.753 178.488 181.385 1.00 25.97  ? 2329 ASP A CA    1 
ATOM   7141  C  C     . ASP A 1 1112 ? 173.023 177.655 181.507 1.00 32.32  ? 2329 ASP A C     1 
ATOM   7142  O  O     . ASP A 1 1112 ? 173.257 176.746 180.706 1.00 34.86  ? 2329 ASP A O     1 
ATOM   7143  C  CB    . ASP A 1 1112 ? 171.196 178.403 179.969 1.00 28.18  ? 2329 ASP A CB    1 
ATOM   7144  C  CG    . ASP A 1 1112 ? 172.108 179.043 178.938 1.00 31.67  ? 2329 ASP A CG    1 
ATOM   7145  O  OD1   . ASP A 1 1112 ? 173.062 179.746 179.329 1.00 34.32  ? 2329 ASP A OD1   1 
ATOM   7146  O  OD2   . ASP A 1 1112 ? 171.868 178.844 177.730 1.00 34.26  ? 2329 ASP A OD2   1 
ATOM   7147  N  N     . SER A 1 1113 ? 173.863 177.946 182.495 1.00 29.41  ? 2330 SER A N     1 
ATOM   7148  C  CA    . SER A 1 1113 ? 175.119 177.240 182.682 1.00 29.72  ? 2330 SER A CA    1 
ATOM   7149  C  C     . SER A 1 1113 ? 175.252 176.822 184.139 1.00 30.60  ? 2330 SER A C     1 
ATOM   7150  O  O     . SER A 1 1113 ? 174.421 177.157 184.986 1.00 29.13  ? 2330 SER A O     1 
ATOM   7151  C  CB    . SER A 1 1113 ? 176.315 178.103 182.262 1.00 34.85  ? 2330 SER A CB    1 
ATOM   7152  O  OG    . SER A 1 1113 ? 176.202 179.413 182.784 1.00 35.95  ? 2330 SER A OG    1 
ATOM   7153  N  N     . THR A 1 1114 ? 176.321 176.082 184.422 1.00 38.08  ? 2331 THR A N     1 
ATOM   7154  C  CA    . THR A 1 1114 ? 176.556 175.556 185.758 1.00 38.58  ? 2331 THR A CA    1 
ATOM   7155  C  C     . THR A 1 1114 ? 176.984 176.678 186.703 1.00 43.75  ? 2331 THR A C     1 
ATOM   7156  O  O     . THR A 1 1114 ? 177.141 177.839 186.314 1.00 44.51  ? 2331 THR A O     1 
ATOM   7157  C  CB    . THR A 1 1114 ? 177.610 174.454 185.715 1.00 37.61  ? 2331 THR A CB    1 
ATOM   7158  O  OG1   . THR A 1 1114 ? 178.897 175.032 185.463 1.00 40.48  ? 2331 THR A OG1   1 
ATOM   7159  C  CG2   . THR A 1 1114 ? 177.291 173.459 184.612 1.00 33.33  ? 2331 THR A CG2   1 
ATOM   7160  N  N     . GLY A 1 1115 ? 177.161 176.318 187.976 1.00 46.97  ? 2332 GLY A N     1 
ATOM   7161  C  CA    . GLY A 1 1115 ? 177.603 177.298 188.955 1.00 50.96  ? 2332 GLY A CA    1 
ATOM   7162  C  C     . GLY A 1 1115 ? 179.004 177.808 188.679 1.00 54.62  ? 2332 GLY A C     1 
ATOM   7163  O  O     . GLY A 1 1115 ? 179.252 179.016 188.705 1.00 55.70  ? 2332 GLY A O     1 
ATOM   7164  N  N     . GLU A 1 1116 ? 179.935 176.893 188.390 1.00 55.65  ? 2333 GLU A N     1 
ATOM   7165  C  CA    . GLU A 1 1116 ? 181.322 177.281 188.140 1.00 58.28  ? 2333 GLU A CA    1 
ATOM   7166  C  C     . GLU A 1 1116 ? 181.444 178.128 186.879 1.00 58.34  ? 2333 GLU A C     1 
ATOM   7167  O  O     . GLU A 1 1116 ? 182.225 179.089 186.838 1.00 58.02  ? 2333 GLU A O     1 
ATOM   7168  C  CB    . GLU A 1 1116 ? 182.202 176.034 188.038 1.00 55.23  ? 2333 GLU A CB    1 
ATOM   7169  C  CG    . GLU A 1 1116 ? 182.670 175.486 189.378 1.00 62.28  ? 2333 GLU A CG    1 
ATOM   7170  C  CD    . GLU A 1 1116 ? 181.559 174.801 190.153 1.00 68.66  ? 2333 GLU A CD    1 
ATOM   7171  O  OE1   . GLU A 1 1116 ? 180.603 174.308 189.519 1.00 65.19  ? 2333 GLU A OE1   1 
ATOM   7172  O  OE2   . GLU A 1 1116 ? 181.644 174.755 191.398 1.00 68.51  ? 2333 GLU A OE2   1 
ATOM   7173  N  N     . SER A 1 1117 ? 180.680 177.785 185.839 1.00 50.95  ? 2334 SER A N     1 
ATOM   7174  C  CA    . SER A 1 1117 ? 180.649 178.619 184.644 1.00 46.41  ? 2334 SER A CA    1 
ATOM   7175  C  C     . SER A 1 1117 ? 180.055 179.987 184.942 1.00 47.35  ? 2334 SER A C     1 
ATOM   7176  O  O     . SER A 1 1117 ? 180.471 180.984 184.346 1.00 53.44  ? 2334 SER A O     1 
ATOM   7177  C  CB    . SER A 1 1117 ? 179.861 177.922 183.537 1.00 46.88  ? 2334 SER A CB    1 
ATOM   7178  O  OG    . SER A 1 1117 ? 180.631 176.895 182.937 1.00 48.90  ? 2334 SER A OG    1 
ATOM   7179  N  N     . GLN A 1 1118 ? 179.095 180.059 185.869 1.00 45.25  ? 2335 GLN A N     1 
ATOM   7180  C  CA    . GLN A 1 1118 ? 178.569 181.354 186.287 1.00 45.23  ? 2335 GLN A CA    1 
ATOM   7181  C  C     . GLN A 1 1118 ? 179.632 182.180 187.002 1.00 49.07  ? 2335 GLN A C     1 
ATOM   7182  O  O     . GLN A 1 1118 ? 179.711 183.397 186.804 1.00 50.28  ? 2335 GLN A O     1 
ATOM   7183  C  CB    . GLN A 1 1118 ? 177.340 181.165 187.176 1.00 43.58  ? 2335 GLN A CB    1 
ATOM   7184  C  CG    . GLN A 1 1118 ? 176.021 181.180 186.419 1.00 36.81  ? 2335 GLN A CG    1 
ATOM   7185  C  CD    . GLN A 1 1118 ? 174.828 181.427 187.321 1.00 30.92  ? 2335 GLN A CD    1 
ATOM   7186  O  OE1   . GLN A 1 1118 ? 174.888 182.241 188.241 1.00 29.71  ? 2335 GLN A OE1   1 
ATOM   7187  N  NE2   . GLN A 1 1118 ? 173.733 180.727 187.057 1.00 27.29  ? 2335 GLN A NE2   1 
ATOM   7188  N  N     . ARG A 1 1119 ? 180.458 181.540 187.839 1.00 50.45  ? 2336 ARG A N     1 
ATOM   7189  C  CA    . ARG A 1 1119 ? 181.564 182.257 188.475 1.00 54.60  ? 2336 ARG A CA    1 
ATOM   7190  C  C     . ARG A 1 1119 ? 182.567 182.760 187.442 1.00 54.10  ? 2336 ARG A C     1 
ATOM   7191  O  O     . ARG A 1 1119 ? 183.053 183.894 187.534 1.00 55.55  ? 2336 ARG A O     1 
ATOM   7192  C  CB    . ARG A 1 1119 ? 182.270 181.367 189.500 1.00 61.99  ? 2336 ARG A CB    1 
ATOM   7193  C  CG    . ARG A 1 1119 ? 181.352 180.562 190.396 1.00 62.28  ? 2336 ARG A CG    1 
ATOM   7194  C  CD    . ARG A 1 1119 ? 181.996 180.244 191.738 1.00 64.29  ? 2336 ARG A CD    1 
ATOM   7195  N  NE    . ARG A 1 1119 ? 181.867 181.334 192.698 1.00 67.44  ? 2336 ARG A NE    1 
ATOM   7196  C  CZ    . ARG A 1 1119 ? 180.752 181.631 193.353 1.00 74.46  ? 2336 ARG A CZ    1 
ATOM   7197  N  NH1   . ARG A 1 1119 ? 179.640 180.934 193.182 1.00 76.69  ? 2336 ARG A NH1   1 
ATOM   7198  N  NH2   . ARG A 1 1119 ? 180.756 182.650 194.208 1.00 76.17  ? 2336 ARG A NH2   1 
ATOM   7199  N  N     . ALA A 1 1120 ? 182.892 181.926 186.450 1.00 52.02  ? 2337 ALA A N     1 
ATOM   7200  C  CA    . ALA A 1 1120 ? 183.811 182.357 185.400 1.00 54.87  ? 2337 ALA A CA    1 
ATOM   7201  C  C     . ALA A 1 1120 ? 183.234 183.524 184.604 1.00 53.14  ? 2337 ALA A C     1 
ATOM   7202  O  O     . ALA A 1 1120 ? 183.941 184.494 184.299 1.00 53.34  ? 2337 ALA A O     1 
ATOM   7203  C  CB    . ALA A 1 1120 ? 184.141 181.186 184.475 1.00 57.02  ? 2337 ALA A CB    1 
ATOM   7204  N  N     . PHE A 1 1121 ? 181.940 183.460 184.285 1.00 53.22  ? 2338 PHE A N     1 
ATOM   7205  C  CA    . PHE A 1 1121 ? 181.321 184.528 183.512 1.00 51.17  ? 2338 PHE A CA    1 
ATOM   7206  C  C     . PHE A 1 1121 ? 181.213 185.816 184.317 1.00 50.45  ? 2338 PHE A C     1 
ATOM   7207  O  O     . PHE A 1 1121 ? 181.356 186.907 183.759 1.00 51.95  ? 2338 PHE A O     1 
ATOM   7208  C  CB    . PHE A 1 1121 ? 179.945 184.101 183.008 1.00 45.50  ? 2338 PHE A CB    1 
ATOM   7209  C  CG    . PHE A 1 1121 ? 179.350 185.060 182.023 1.00 40.07  ? 2338 PHE A CG    1 
ATOM   7210  C  CD1   . PHE A 1 1121 ? 180.110 185.541 180.973 1.00 42.24  ? 2338 PHE A CD1   1 
ATOM   7211  C  CD2   . PHE A 1 1121 ? 178.044 185.496 182.153 1.00 37.04  ? 2338 PHE A CD2   1 
ATOM   7212  C  CE1   . PHE A 1 1121 ? 179.578 186.429 180.068 1.00 40.78  ? 2338 PHE A CE1   1 
ATOM   7213  C  CE2   . PHE A 1 1121 ? 177.502 186.377 181.242 1.00 34.24  ? 2338 PHE A CE2   1 
ATOM   7214  C  CZ    . PHE A 1 1121 ? 178.273 186.847 180.202 1.00 35.92  ? 2338 PHE A CZ    1 
ATOM   7215  N  N     . ILE A 1 1122 ? 180.950 185.723 185.623 1.00 48.47  ? 2339 ILE A N     1 
ATOM   7216  C  CA    . ILE A 1 1122 ? 180.882 186.952 186.407 1.00 51.69  ? 2339 ILE A CA    1 
ATOM   7217  C  C     . ILE A 1 1122 ? 182.276 187.537 186.605 1.00 58.65  ? 2339 ILE A C     1 
ATOM   7218  O  O     . ILE A 1 1122 ? 182.433 188.763 186.671 1.00 62.51  ? 2339 ILE A O     1 
ATOM   7219  C  CB    . ILE A 1 1122 ? 180.131 186.735 187.737 1.00 52.31  ? 2339 ILE A CB    1 
ATOM   7220  C  CG1   . ILE A 1 1122 ? 179.808 188.083 188.376 1.00 56.97  ? 2339 ILE A CG1   1 
ATOM   7221  C  CG2   . ILE A 1 1122 ? 180.924 185.900 188.714 1.00 52.97  ? 2339 ILE A CG2   1 
ATOM   7222  C  CD1   . ILE A 1 1122 ? 178.852 188.905 187.571 1.00 54.82  ? 2339 ILE A CD1   1 
ATOM   7223  N  N     . GLN A 1 1123 ? 183.313 186.692 186.658 1.00 57.53  ? 2340 GLN A N     1 
ATOM   7224  C  CA    . GLN A 1 1123 ? 184.678 187.210 186.646 1.00 57.44  ? 2340 GLN A CA    1 
ATOM   7225  C  C     . GLN A 1 1123 ? 184.967 187.959 185.350 1.00 58.62  ? 2340 GLN A C     1 
ATOM   7226  O  O     . GLN A 1 1123 ? 185.540 189.056 185.368 1.00 60.28  ? 2340 GLN A O     1 
ATOM   7227  C  CB    . GLN A 1 1123 ? 185.673 186.066 186.840 1.00 60.05  ? 2340 GLN A CB    1 
ATOM   7228  C  CG    . GLN A 1 1123 ? 187.122 186.506 186.929 1.00 64.55  ? 2340 GLN A CG    1 
ATOM   7229  C  CD    . GLN A 1 1123 ? 188.020 185.427 187.500 1.00 67.53  ? 2340 GLN A CD    1 
ATOM   7230  O  OE1   . GLN A 1 1123 ? 187.598 184.285 187.679 1.00 71.25  ? 2340 GLN A OE1   1 
ATOM   7231  N  NE2   . GLN A 1 1123 ? 189.265 185.785 187.789 1.00 62.35  ? 2340 GLN A NE2   1 
ATOM   7232  N  N     . THR A 1 1124 ? 184.543 187.391 184.216 1.00 56.95  ? 2341 THR A N     1 
ATOM   7233  C  CA    . THR A 1 1124 ? 184.718 188.059 182.928 1.00 53.04  ? 2341 THR A CA    1 
ATOM   7234  C  C     . THR A 1 1124 ? 183.946 189.377 182.872 1.00 56.11  ? 2341 THR A C     1 
ATOM   7235  O  O     . THR A 1 1124 ? 184.460 190.387 182.375 1.00 59.99  ? 2341 THR A O     1 
ATOM   7236  C  CB    . THR A 1 1124 ? 184.283 187.121 181.799 1.00 50.21  ? 2341 THR A CB    1 
ATOM   7237  O  OG1   . THR A 1 1124 ? 185.246 186.070 181.653 1.00 54.51  ? 2341 THR A OG1   1 
ATOM   7238  C  CG2   . THR A 1 1124 ? 184.158 187.863 180.478 1.00 51.00  ? 2341 THR A CG2   1 
ATOM   7239  N  N     . ILE A 1 1125 ? 182.715 189.385 183.391 1.00 59.01  ? 2342 ILE A N     1 
ATOM   7240  C  CA    . ILE A 1 1125 ? 181.890 190.593 183.387 1.00 62.24  ? 2342 ILE A CA    1 
ATOM   7241  C  C     . ILE A 1 1125 ? 182.535 191.686 184.229 1.00 61.06  ? 2342 ILE A C     1 
ATOM   7242  O  O     . ILE A 1 1125 ? 182.626 192.846 183.808 1.00 60.60  ? 2342 ILE A O     1 
ATOM   7243  C  CB    . ILE A 1 1125 ? 180.467 190.273 183.880 1.00 55.41  ? 2342 ILE A CB    1 
ATOM   7244  C  CG1   . ILE A 1 1125 ? 179.674 189.531 182.810 1.00 49.37  ? 2342 ILE A CG1   1 
ATOM   7245  C  CG2   . ILE A 1 1125 ? 179.730 191.535 184.282 1.00 54.36  ? 2342 ILE A CG2   1 
ATOM   7246  C  CD1   . ILE A 1 1125 ? 178.285 189.168 183.260 1.00 44.42  ? 2342 ILE A CD1   1 
ATOM   7247  N  N     . ASN A 1 1126 ? 182.996 191.332 185.432 1.00 59.16  ? 2343 ASN A N     1 
ATOM   7248  C  CA    . ASN A 1 1126 ? 183.652 192.315 186.285 1.00 62.76  ? 2343 ASN A CA    1 
ATOM   7249  C  C     . ASN A 1 1126 ? 184.958 192.807 185.675 1.00 71.54  ? 2343 ASN A C     1 
ATOM   7250  O  O     . ASN A 1 1126 ? 185.340 193.963 185.887 1.00 80.79  ? 2343 ASN A O     1 
ATOM   7251  C  CB    . ASN A 1 1126 ? 183.906 191.727 187.673 1.00 65.14  ? 2343 ASN A CB    1 
ATOM   7252  C  CG    . ASN A 1 1126 ? 182.623 191.390 188.410 1.00 69.92  ? 2343 ASN A CG    1 
ATOM   7253  O  OD1   . ASN A 1 1126 ? 182.522 190.351 189.061 1.00 65.93  ? 2343 ASN A OD1   1 
ATOM   7254  N  ND2   . ASN A 1 1126 ? 181.635 192.271 188.311 1.00 70.62  ? 2343 ASN A ND2   1 
ATOM   7255  N  N     . THR A 1 1127 ? 185.650 191.954 184.916 1.00 67.89  ? 2344 THR A N     1 
ATOM   7256  C  CA    . THR A 1 1127 ? 186.904 192.371 184.297 1.00 67.16  ? 2344 THR A CA    1 
ATOM   7257  C  C     . THR A 1 1127 ? 186.666 193.327 183.132 1.00 64.96  ? 2344 THR A C     1 
ATOM   7258  O  O     . THR A 1 1127 ? 187.353 194.347 183.006 1.00 65.09  ? 2344 THR A O     1 
ATOM   7259  C  CB    . THR A 1 1127 ? 187.688 191.145 183.828 1.00 65.15  ? 2344 THR A CB    1 
ATOM   7260  O  OG1   . THR A 1 1127 ? 187.696 190.155 184.864 1.00 64.81  ? 2344 THR A OG1   1 
ATOM   7261  C  CG2   . THR A 1 1127 ? 189.118 191.526 183.487 1.00 66.82  ? 2344 THR A CG2   1 
ATOM   7262  N  N     . TYR A 1 1128 ? 185.693 193.018 182.271 1.00 64.73  ? 2345 TYR A N     1 
ATOM   7263  C  CA    . TYR A 1 1128 ? 185.614 193.696 180.980 1.00 65.62  ? 2345 TYR A CA    1 
ATOM   7264  C  C     . TYR A 1 1128 ? 184.947 195.066 181.059 1.00 69.76  ? 2345 TYR A C     1 
ATOM   7265  O  O     . TYR A 1 1128 ? 185.284 195.950 180.263 1.00 70.24  ? 2345 TYR A O     1 
ATOM   7266  C  CB    . TYR A 1 1128 ? 184.900 192.804 179.964 1.00 60.95  ? 2345 TYR A CB    1 
ATOM   7267  C  CG    . TYR A 1 1128 ? 185.790 191.710 179.410 1.00 58.02  ? 2345 TYR A CG    1 
ATOM   7268  C  CD1   . TYR A 1 1128 ? 187.139 191.650 179.744 1.00 58.85  ? 2345 TYR A CD1   1 
ATOM   7269  C  CD2   . TYR A 1 1128 ? 185.285 190.736 178.561 1.00 57.48  ? 2345 TYR A CD2   1 
ATOM   7270  C  CE1   . TYR A 1 1128 ? 187.957 190.656 179.248 1.00 58.17  ? 2345 TYR A CE1   1 
ATOM   7271  C  CE2   . TYR A 1 1128 ? 186.099 189.735 178.058 1.00 60.56  ? 2345 TYR A CE2   1 
ATOM   7272  C  CZ    . TYR A 1 1128 ? 187.433 189.701 178.406 1.00 59.60  ? 2345 TYR A CZ    1 
ATOM   7273  O  OH    . TYR A 1 1128 ? 188.248 188.709 177.910 1.00 57.42  ? 2345 TYR A OH    1 
ATOM   7274  N  N     . PHE A 1 1129 ? 183.999 195.268 181.980 1.00 69.49  ? 2346 PHE A N     1 
ATOM   7275  C  CA    . PHE A 1 1129 ? 183.505 196.623 182.217 1.00 69.32  ? 2346 PHE A CA    1 
ATOM   7276  C  C     . PHE A 1 1129 ? 184.591 197.531 182.775 1.00 74.47  ? 2346 PHE A C     1 
ATOM   7277  O  O     . PHE A 1 1129 ? 184.661 198.711 182.412 1.00 72.81  ? 2346 PHE A O     1 
ATOM   7278  C  CB    . PHE A 1 1129 ? 182.318 196.627 183.181 1.00 68.50  ? 2346 PHE A CB    1 
ATOM   7279  C  CG    . PHE A 1 1129 ? 180.987 196.371 182.532 1.00 61.31  ? 2346 PHE A CG    1 
ATOM   7280  C  CD1   . PHE A 1 1129 ? 179.915 197.198 182.820 1.00 61.28  ? 2346 PHE A CD1   1 
ATOM   7281  C  CD2   . PHE A 1 1129 ? 180.791 195.313 181.668 1.00 57.53  ? 2346 PHE A CD2   1 
ATOM   7282  C  CE1   . PHE A 1 1129 ? 178.680 196.989 182.251 1.00 60.40  ? 2346 PHE A CE1   1 
ATOM   7283  C  CE2   . PHE A 1 1129 ? 179.550 195.101 181.097 1.00 57.78  ? 2346 PHE A CE2   1 
ATOM   7284  C  CZ    . PHE A 1 1129 ? 178.497 195.939 181.388 1.00 58.28  ? 2346 PHE A CZ    1 
ATOM   7285  N  N     . GLY A 1 1130 ? 185.437 197.006 183.649 1.00 78.90  ? 2347 GLY A N     1 
ATOM   7286  C  CA    . GLY A 1 1130 ? 186.372 197.810 184.401 1.00 85.03  ? 2347 GLY A CA    1 
ATOM   7287  C  C     . GLY A 1 1130 ? 186.015 197.855 185.878 1.00 86.20  ? 2347 GLY A C     1 
ATOM   7288  O  O     . GLY A 1 1130 ? 184.888 197.569 186.291 1.00 82.59  ? 2347 GLY A O     1 
ATOM   7289  N  N     . HIS A 1 1131 ? 187.003 198.221 186.688 1.00 90.01  ? 2348 HIS A N     1 
ATOM   7290  C  CA    . HIS A 1 1131 ? 186.847 198.200 188.135 1.00 89.77  ? 2348 HIS A CA    1 
ATOM   7291  C  C     . HIS A 1 1131 ? 186.325 199.513 188.702 1.00 89.71  ? 2348 HIS A C     1 
ATOM   7292  O  O     . HIS A 1 1131 ? 186.092 199.596 189.913 1.00 86.86  ? 2348 HIS A O     1 
ATOM   7293  C  CB    . HIS A 1 1131 ? 188.180 197.844 188.795 1.00 89.76  ? 2348 HIS A CB    1 
ATOM   7294  C  CG    . HIS A 1 1131 ? 188.648 196.455 188.489 1.00 94.44  ? 2348 HIS A CG    1 
ATOM   7295  N  ND1   . HIS A 1 1131 ? 189.422 196.158 187.387 1.00 98.10  ? 2348 HIS A ND1   1 
ATOM   7296  C  CD2   . HIS A 1 1131 ? 188.445 195.282 189.134 1.00 95.89  ? 2348 HIS A CD2   1 
ATOM   7297  C  CE1   . HIS A 1 1131 ? 189.678 194.862 187.369 1.00 96.77  ? 2348 HIS A CE1   1 
ATOM   7298  N  NE2   . HIS A 1 1131 ? 189.097 194.308 188.418 1.00 98.18  ? 2348 HIS A NE2   1 
ATOM   7299  N  N     . ASP A 1 1132 ? 186.134 200.536 187.866 1.00 91.01  ? 2349 ASP A N     1 
ATOM   7300  C  CA    . ASP A 1 1132 ? 185.584 201.793 188.361 1.00 92.58  ? 2349 ASP A CA    1 
ATOM   7301  C  C     . ASP A 1 1132 ? 184.091 201.679 188.640 1.00 90.12  ? 2349 ASP A C     1 
ATOM   7302  O  O     . ASP A 1 1132 ? 183.572 202.374 189.522 1.00 88.43  ? 2349 ASP A O     1 
ATOM   7303  C  CB    . ASP A 1 1132 ? 185.855 202.919 187.362 1.00 92.98  ? 2349 ASP A CB    1 
ATOM   7304  C  CG    . ASP A 1 1132 ? 185.079 202.754 186.070 1.00 92.55  ? 2349 ASP A CG    1 
ATOM   7305  O  OD1   . ASP A 1 1132 ? 185.124 201.652 185.484 1.00 90.53  ? 2349 ASP A OD1   1 
ATOM   7306  O  OD2   . ASP A 1 1132 ? 184.420 203.725 185.643 1.00 90.93  ? 2349 ASP A OD2   1 
ATOM   7307  N  N     . SER A 1 1133 ? 183.390 200.818 187.910 1.00 88.39  ? 2350 SER A N     1 
ATOM   7308  C  CA    . SER A 1 1133 ? 181.964 200.632 188.110 1.00 83.96  ? 2350 SER A CA    1 
ATOM   7309  C  C     . SER A 1 1133 ? 181.708 199.688 189.280 1.00 85.04  ? 2350 SER A C     1 
ATOM   7310  O  O     . SER A 1 1133 ? 182.621 199.054 189.817 1.00 86.25  ? 2350 SER A O     1 
ATOM   7311  C  CB    . SER A 1 1133 ? 181.312 200.089 186.841 1.00 78.54  ? 2350 SER A CB    1 
ATOM   7312  O  OG    . SER A 1 1133 ? 181.696 198.745 186.611 1.00 78.49  ? 2350 SER A OG    1 
ATOM   7313  N  N     . GLN A 1 1134 ? 180.443 199.611 189.683 1.00 81.07  ? 2351 GLN A N     1 
ATOM   7314  C  CA    . GLN A 1 1134 ? 180.051 198.712 190.760 1.00 80.44  ? 2351 GLN A CA    1 
ATOM   7315  C  C     . GLN A 1 1134 ? 180.262 197.267 190.329 1.00 78.19  ? 2351 GLN A C     1 
ATOM   7316  O  O     . GLN A 1 1134 ? 179.895 196.879 189.216 1.00 81.73  ? 2351 GLN A O     1 
ATOM   7317  C  CB    . GLN A 1 1134 ? 178.591 198.954 191.142 1.00 76.19  ? 2351 GLN A CB    1 
ATOM   7318  C  CG    . GLN A 1 1134 ? 178.191 198.387 192.494 1.00 77.09  ? 2351 GLN A CG    1 
ATOM   7319  C  CD    . GLN A 1 1134 ? 176.949 199.054 193.057 1.00 77.18  ? 2351 GLN A CD    1 
ATOM   7320  O  OE1   . GLN A 1 1134 ? 176.014 199.370 192.322 1.00 72.81  ? 2351 GLN A OE1   1 
ATOM   7321  N  NE2   . GLN A 1 1134 ? 176.932 199.268 194.367 1.00 77.08  ? 2351 GLN A NE2   1 
ATOM   7322  N  N     . GLU A 1 1135 ? 180.860 196.471 191.211 1.00 75.12  ? 2352 GLU A N     1 
ATOM   7323  C  CA    . GLU A 1 1135 ? 181.205 195.088 190.901 1.00 74.06  ? 2352 GLU A CA    1 
ATOM   7324  C  C     . GLU A 1 1135 ? 180.058 194.189 191.343 1.00 74.12  ? 2352 GLU A C     1 
ATOM   7325  O  O     . GLU A 1 1135 ? 179.785 194.061 192.540 1.00 74.16  ? 2352 GLU A O     1 
ATOM   7326  C  CB    . GLU A 1 1135 ? 182.506 194.689 191.591 1.00 73.16  ? 2352 GLU A CB    1 
ATOM   7327  C  CG    . GLU A 1 1135 ? 183.697 195.551 191.220 1.00 79.06  ? 2352 GLU A CG    1 
ATOM   7328  C  CD    . GLU A 1 1135 ? 183.994 196.607 192.266 1.00 83.72  ? 2352 GLU A CD    1 
ATOM   7329  O  OE1   . GLU A 1 1135 ? 183.103 197.438 192.542 1.00 81.53  ? 2352 GLU A OE1   1 
ATOM   7330  O  OE2   . GLU A 1 1135 ? 185.115 196.604 192.814 1.00 85.28  ? 2352 GLU A OE2   1 
ATOM   7331  N  N     . LEU A 1 1136 ? 179.389 193.563 190.380 1.00 72.66  ? 2353 LEU A N     1 
ATOM   7332  C  CA    . LEU A 1 1136 ? 178.329 192.617 190.696 1.00 70.48  ? 2353 LEU A CA    1 
ATOM   7333  C  C     . LEU A 1 1136 ? 178.956 191.312 191.167 1.00 73.85  ? 2353 LEU A C     1 
ATOM   7334  O  O     . LEU A 1 1136 ? 179.707 190.673 190.422 1.00 72.73  ? 2353 LEU A O     1 
ATOM   7335  C  CB    . LEU A 1 1136 ? 177.437 192.375 189.484 1.00 62.28  ? 2353 LEU A CB    1 
ATOM   7336  C  CG    . LEU A 1 1136 ? 176.419 191.251 189.683 1.00 58.87  ? 2353 LEU A CG    1 
ATOM   7337  C  CD1   . LEU A 1 1136 ? 175.291 191.694 190.598 1.00 62.09  ? 2353 LEU A CD1   1 
ATOM   7338  C  CD2   . LEU A 1 1136 ? 175.877 190.788 188.357 1.00 53.12  ? 2353 LEU A CD2   1 
ATOM   7339  N  N     . SER A 1 1137 ? 178.652 190.920 192.398 1.00 74.35  ? 2354 SER A N     1 
ATOM   7340  C  CA    . SER A 1 1137 ? 179.185 189.702 192.979 1.00 70.20  ? 2354 SER A CA    1 
ATOM   7341  C  C     . SER A 1 1137 ? 178.169 188.572 192.839 1.00 68.73  ? 2354 SER A C     1 
ATOM   7342  O  O     . SER A 1 1137 ? 177.100 188.728 192.245 1.00 68.92  ? 2354 SER A O     1 
ATOM   7343  C  CB    . SER A 1 1137 ? 179.567 189.929 194.442 1.00 74.04  ? 2354 SER A CB    1 
ATOM   7344  O  OG    . SER A 1 1137 ? 180.529 190.963 194.563 1.00 80.94  ? 2354 SER A OG    1 
ATOM   7345  N  N     . ASP A 1 1138 ? 178.522 187.412 193.396 1.00 72.89  ? 2355 ASP A N     1 
ATOM   7346  C  CA    . ASP A 1 1138 ? 177.661 186.237 193.326 1.00 76.65  ? 2355 ASP A CA    1 
ATOM   7347  C  C     . ASP A 1 1138 ? 176.346 186.431 194.070 1.00 75.89  ? 2355 ASP A C     1 
ATOM   7348  O  O     . ASP A 1 1138 ? 175.369 185.737 193.768 1.00 72.36  ? 2355 ASP A O     1 
ATOM   7349  C  CB    . ASP A 1 1138 ? 178.411 185.023 193.884 1.00 82.43  ? 2355 ASP A CB    1 
ATOM   7350  C  CG    . ASP A 1 1138 ? 177.673 183.717 193.658 1.00 84.90  ? 2355 ASP A CG    1 
ATOM   7351  O  OD1   . ASP A 1 1138 ? 176.824 183.355 194.500 1.00 82.66  ? 2355 ASP A OD1   1 
ATOM   7352  O  OD2   . ASP A 1 1138 ? 177.947 183.048 192.639 1.00 87.32  ? 2355 ASP A OD2   1 
ATOM   7353  N  N     . TYR A 1 1139 ? 176.289 187.369 195.019 1.00 75.82  ? 2356 TYR A N     1 
ATOM   7354  C  CA    . TYR A 1 1139 ? 175.108 187.546 195.856 1.00 78.48  ? 2356 TYR A CA    1 
ATOM   7355  C  C     . TYR A 1 1139 ? 174.703 189.011 195.986 1.00 75.95  ? 2356 TYR A C     1 
ATOM   7356  O  O     . TYR A 1 1139 ? 173.998 189.365 196.934 1.00 77.77  ? 2356 TYR A O     1 
ATOM   7357  C  CB    . TYR A 1 1139 ? 175.347 186.946 197.243 1.00 81.14  ? 2356 TYR A CB    1 
ATOM   7358  C  CG    . TYR A 1 1139 ? 176.746 187.180 197.772 1.00 83.01  ? 2356 TYR A CG    1 
ATOM   7359  C  CD1   . TYR A 1 1139 ? 177.091 188.386 198.370 1.00 83.48  ? 2356 TYR A CD1   1 
ATOM   7360  C  CD2   . TYR A 1 1139 ? 177.720 186.194 197.676 1.00 82.51  ? 2356 TYR A CD2   1 
ATOM   7361  C  CE1   . TYR A 1 1139 ? 178.368 188.604 198.853 1.00 86.54  ? 2356 TYR A CE1   1 
ATOM   7362  C  CE2   . TYR A 1 1139 ? 178.999 186.403 198.157 1.00 85.06  ? 2356 TYR A CE2   1 
ATOM   7363  C  CZ    . TYR A 1 1139 ? 179.317 187.609 198.744 1.00 88.57  ? 2356 TYR A CZ    1 
ATOM   7364  O  OH    . TYR A 1 1139 ? 180.589 187.821 199.225 1.00 90.57  ? 2356 TYR A OH    1 
ATOM   7365  N  N     . SER A 1 1140 ? 175.122 189.866 195.057 1.00 72.85  ? 2357 SER A N     1 
ATOM   7366  C  CA    . SER A 1 1140 ? 174.816 191.285 195.163 1.00 70.08  ? 2357 SER A CA    1 
ATOM   7367  C  C     . SER A 1 1140 ? 173.346 191.551 194.859 1.00 65.25  ? 2357 SER A C     1 
ATOM   7368  O  O     . SER A 1 1140 ? 172.780 191.004 193.910 1.00 63.69  ? 2357 SER A O     1 
ATOM   7369  C  CB    . SER A 1 1140 ? 175.699 192.093 194.217 1.00 70.74  ? 2357 SER A CB    1 
ATOM   7370  O  OG    . SER A 1 1140 ? 175.268 193.441 194.152 1.00 68.28  ? 2357 SER A OG    1 
ATOM   7371  N  N     . THR A 1 1141 ? 172.730 192.401 195.679 1.00 70.71  ? 2358 THR A N     1 
ATOM   7372  C  CA    . THR A 1 1141 ? 171.328 192.762 195.535 1.00 69.75  ? 2358 THR A CA    1 
ATOM   7373  C  C     . THR A 1 1141 ? 171.169 194.232 195.899 1.00 72.49  ? 2358 THR A C     1 
ATOM   7374  O  O     . THR A 1 1141 ? 171.947 194.778 196.684 1.00 75.39  ? 2358 THR A O     1 
ATOM   7375  C  CB    . THR A 1 1141 ? 170.425 191.889 196.425 1.00 67.83  ? 2358 THR A CB    1 
ATOM   7376  O  OG1   . THR A 1 1141 ? 170.882 190.533 196.384 1.00 68.47  ? 2358 THR A OG1   1 
ATOM   7377  C  CG2   . THR A 1 1141 ? 168.981 191.922 195.940 1.00 62.61  ? 2358 THR A CG2   1 
ATOM   7378  N  N     . ILE A 1 1142 ? 170.156 194.869 195.318 1.00 72.42  ? 2359 ILE A N     1 
ATOM   7379  C  CA    . ILE A 1 1142 ? 169.880 196.285 195.530 1.00 73.32  ? 2359 ILE A CA    1 
ATOM   7380  C  C     . ILE A 1 1142 ? 168.660 196.397 196.434 1.00 73.22  ? 2359 ILE A C     1 
ATOM   7381  O  O     . ILE A 1 1142 ? 167.600 195.837 196.130 1.00 69.74  ? 2359 ILE A O     1 
ATOM   7382  C  CB    . ILE A 1 1142 ? 169.653 197.019 194.200 1.00 68.86  ? 2359 ILE A CB    1 
ATOM   7383  C  CG1   . ILE A 1 1142 ? 170.978 197.198 193.456 1.00 67.18  ? 2359 ILE A CG1   1 
ATOM   7384  C  CG2   . ILE A 1 1142 ? 169.004 198.368 194.440 1.00 64.18  ? 2359 ILE A CG2   1 
ATOM   7385  C  CD1   . ILE A 1 1142 ? 171.982 198.052 194.195 1.00 69.78  ? 2359 ILE A CD1   1 
ATOM   7386  N  N     . VAL A 1 1143 ? 168.810 197.116 197.546 1.00 79.98  ? 2360 VAL A N     1 
ATOM   7387  C  CA    . VAL A 1 1143 ? 167.710 197.373 198.464 1.00 80.58  ? 2360 VAL A CA    1 
ATOM   7388  C  C     . VAL A 1 1143 ? 167.489 198.878 198.552 1.00 80.81  ? 2360 VAL A C     1 
ATOM   7389  O  O     . VAL A 1 1143 ? 168.401 199.682 198.344 1.00 80.89  ? 2360 VAL A O     1 
ATOM   7390  C  CB    . VAL A 1 1143 ? 167.955 196.776 199.866 1.00 78.10  ? 2360 VAL A CB    1 
ATOM   7391  C  CG1   . VAL A 1 1143 ? 168.082 195.263 199.785 1.00 76.29  ? 2360 VAL A CG1   1 
ATOM   7392  C  CG2   . VAL A 1 1143 ? 169.189 197.392 200.505 1.00 77.72  ? 2360 VAL A CG2   1 
ATOM   7393  N  N     . ILE A 1 1144 ? 166.252 199.251 198.857 1.00 82.05  ? 2361 ILE A N     1 
ATOM   7394  C  CA    . ILE A 1 1144 ? 165.879 200.656 198.949 1.00 85.27  ? 2361 ILE A CA    1 
ATOM   7395  C  C     . ILE A 1 1144 ? 166.024 201.151 200.382 1.00 86.65  ? 2361 ILE A C     1 
ATOM   7396  O  O     . ILE A 1 1144 ? 165.884 202.344 200.654 1.00 87.84  ? 2361 ILE A O     1 
ATOM   7397  C  CB    . ILE A 1 1144 ? 164.449 200.882 198.436 1.00 86.42  ? 2361 ILE A CB    1 
ATOM   7398  C  CG1   . ILE A 1 1144 ? 163.523 199.772 198.939 1.00 86.02  ? 2361 ILE A CG1   1 
ATOM   7399  C  CG2   . ILE A 1 1144 ? 164.433 200.947 196.916 1.00 85.19  ? 2361 ILE A CG2   1 
ATOM   7400  C  CD1   . ILE A 1 1144 ? 162.060 200.018 198.645 1.00 87.65  ? 2361 ILE A CD1   1 
ATOM   7401  N  N     . LEU A 1 1149 ? 168.543 203.482 198.328 1.00 74.79  ? 2366 LEU A N     1 
ATOM   7402  C  CA    . LEU A 1 1149 ? 169.294 202.716 197.340 1.00 74.95  ? 2366 LEU A CA    1 
ATOM   7403  C  C     . LEU A 1 1149 ? 170.701 202.441 197.855 1.00 73.60  ? 2366 LEU A C     1 
ATOM   7404  O  O     . LEU A 1 1149 ? 171.494 203.366 198.032 1.00 76.21  ? 2366 LEU A O     1 
ATOM   7405  C  CB    . LEU A 1 1149 ? 169.358 203.457 195.999 1.00 80.13  ? 2366 LEU A CB    1 
ATOM   7406  C  CG    . LEU A 1 1149 ? 168.192 203.351 195.006 1.00 79.15  ? 2366 LEU A CG    1 
ATOM   7407  C  CD1   . LEU A 1 1149 ? 168.019 201.920 194.524 1.00 72.55  ? 2366 LEU A CD1   1 
ATOM   7408  C  CD2   . LEU A 1 1149 ? 166.886 203.893 195.565 1.00 79.39  ? 2366 LEU A CD2   1 
ATOM   7409  N  N     . SER A 1 1150 ? 171.010 201.169 198.096 1.00 74.67  ? 2367 SER A N     1 
ATOM   7410  C  CA    . SER A 1 1150 ? 172.300 200.808 198.663 1.00 79.94  ? 2367 SER A CA    1 
ATOM   7411  C  C     . SER A 1 1150 ? 172.680 199.399 198.231 1.00 79.53  ? 2367 SER A C     1 
ATOM   7412  O  O     . SER A 1 1150 ? 171.825 198.577 197.890 1.00 75.23  ? 2367 SER A O     1 
ATOM   7413  C  CB    . SER A 1 1150 ? 172.284 200.905 200.193 1.00 82.34  ? 2367 SER A CB    1 
ATOM   7414  O  OG    . SER A 1 1150 ? 171.326 200.022 200.748 1.00 84.34  ? 2367 SER A OG    1 
ATOM   7415  N  N     . PHE A 1 1151 ? 173.984 199.139 198.246 1.00 84.36  ? 2368 PHE A N     1 
ATOM   7416  C  CA    . PHE A 1 1151 ? 174.496 197.800 197.993 1.00 85.62  ? 2368 PHE A CA    1 
ATOM   7417  C  C     . PHE A 1 1151 ? 174.116 196.889 199.156 1.00 86.92  ? 2368 PHE A C     1 
ATOM   7418  O  O     . PHE A 1 1151 ? 174.229 197.268 200.325 1.00 89.99  ? 2368 PHE A O     1 
ATOM   7419  C  CB    . PHE A 1 1151 ? 176.019 197.864 197.791 1.00 85.78  ? 2368 PHE A CB    1 
ATOM   7420  C  CG    . PHE A 1 1151 ? 176.668 196.555 197.386 1.00 87.17  ? 2368 PHE A CG    1 
ATOM   7421  C  CD1   . PHE A 1 1151 ? 176.846 195.514 198.290 1.00 84.39  ? 2368 PHE A CD1   1 
ATOM   7422  C  CD2   . PHE A 1 1151 ? 177.105 196.375 196.083 1.00 88.33  ? 2368 PHE A CD2   1 
ATOM   7423  C  CE1   . PHE A 1 1151 ? 177.443 194.330 197.902 1.00 85.80  ? 2368 PHE A CE1   1 
ATOM   7424  C  CE2   . PHE A 1 1151 ? 177.702 195.190 195.690 1.00 87.12  ? 2368 PHE A CE2   1 
ATOM   7425  C  CZ    . PHE A 1 1151 ? 177.870 194.167 196.601 1.00 85.22  ? 2368 PHE A CZ    1 
ATOM   7426  N  N     . SER A 1 1152 ? 173.664 195.682 198.829 1.00 82.37  ? 2369 SER A N     1 
ATOM   7427  C  CA    . SER A 1 1152 ? 173.248 194.713 199.834 1.00 81.24  ? 2369 SER A CA    1 
ATOM   7428  C  C     . SER A 1 1152 ? 173.692 193.326 199.383 1.00 79.56  ? 2369 SER A C     1 
ATOM   7429  O  O     . SER A 1 1152 ? 174.489 193.178 198.452 1.00 80.59  ? 2369 SER A O     1 
ATOM   7430  C  CB    . SER A 1 1152 ? 171.733 194.784 200.067 1.00 81.61  ? 2369 SER A CB    1 
ATOM   7431  O  OG    . SER A 1 1152 ? 171.324 193.855 201.056 1.00 85.78  ? 2369 SER A OG    1 
ATOM   7432  N  N     . SER A 1 1153 ? 173.170 192.303 200.054 1.00 80.23  ? 2370 SER A N     1 
ATOM   7433  C  CA    . SER A 1 1153 ? 173.489 190.924 199.719 1.00 79.01  ? 2370 SER A CA    1 
ATOM   7434  C  C     . SER A 1 1153 ? 172.290 190.044 200.039 1.00 75.71  ? 2370 SER A C     1 
ATOM   7435  O  O     . SER A 1 1153 ? 171.428 190.403 200.844 1.00 75.18  ? 2370 SER A O     1 
ATOM   7436  C  CB    . SER A 1 1153 ? 174.734 190.435 200.469 1.00 81.78  ? 2370 SER A CB    1 
ATOM   7437  O  OG    . SER A 1 1153 ? 175.913 190.981 199.905 1.00 77.62  ? 2370 SER A OG    1 
ATOM   7438  N  N     . PHE A 1 1154 ? 172.248 188.879 199.391 1.00 76.57  ? 2371 PHE A N     1 
ATOM   7439  C  CA    . PHE A 1 1154 ? 171.150 187.939 199.586 1.00 76.44  ? 2371 PHE A CA    1 
ATOM   7440  C  C     . PHE A 1 1154 ? 171.232 187.200 200.914 1.00 81.91  ? 2371 PHE A C     1 
ATOM   7441  O  O     . PHE A 1 1154 ? 170.215 186.675 201.378 1.00 81.88  ? 2371 PHE A O     1 
ATOM   7442  C  CB    . PHE A 1 1154 ? 171.120 186.922 198.442 1.00 69.19  ? 2371 PHE A CB    1 
ATOM   7443  C  CG    . PHE A 1 1154 ? 170.258 187.336 197.283 1.00 61.39  ? 2371 PHE A CG    1 
ATOM   7444  C  CD1   . PHE A 1 1154 ? 168.925 187.659 197.474 1.00 55.83  ? 2371 PHE A CD1   1 
ATOM   7445  C  CD2   . PHE A 1 1154 ? 170.782 187.398 196.002 1.00 58.52  ? 2371 PHE A CD2   1 
ATOM   7446  C  CE1   . PHE A 1 1154 ? 168.130 188.039 196.409 1.00 49.53  ? 2371 PHE A CE1   1 
ATOM   7447  C  CE2   . PHE A 1 1154 ? 169.992 187.779 194.933 1.00 54.75  ? 2371 PHE A CE2   1 
ATOM   7448  C  CZ    . PHE A 1 1154 ? 168.665 188.100 195.137 1.00 48.10  ? 2371 PHE A CZ    1 
ATOM   7449  N  N     . CYS A 1 1155 ? 172.412 187.154 201.536 1.00 83.38  ? 2372 CYS A N     1 
ATOM   7450  C  CA    . CYS A 1 1155 ? 172.615 186.368 202.748 1.00 85.54  ? 2372 CYS A CA    1 
ATOM   7451  C  C     . CYS A 1 1155 ? 171.900 186.937 203.967 1.00 82.38  ? 2372 CYS A C     1 
ATOM   7452  O  O     . CYS A 1 1155 ? 171.769 186.226 204.969 1.00 80.75  ? 2372 CYS A O     1 
ATOM   7453  C  CB    . CYS A 1 1155 ? 174.112 186.247 203.041 1.00 88.43  ? 2372 CYS A CB    1 
ATOM   7454  S  SG    . CYS A 1 1155 ? 175.128 185.880 201.591 1.00 87.64  ? 2372 CYS A SG    1 
ATOM   7455  N  N     . SER A 1 1156 ? 171.436 188.185 203.915 1.00 84.32  ? 2373 SER A N     1 
ATOM   7456  C  CA    . SER A 1 1156 ? 170.802 188.833 205.055 1.00 86.10  ? 2373 SER A CA    1 
ATOM   7457  C  C     . SER A 1 1156 ? 169.288 188.939 204.903 1.00 85.17  ? 2373 SER A C     1 
ATOM   7458  O  O     . SER A 1 1156 ? 168.671 189.821 205.510 1.00 84.02  ? 2373 SER A O     1 
ATOM   7459  C  CB    . SER A 1 1156 ? 171.410 190.219 205.276 1.00 87.71  ? 2373 SER A CB    1 
ATOM   7460  O  OG    . SER A 1 1156 ? 170.929 191.148 204.320 1.00 86.65  ? 2373 SER A OG    1 
ATOM   7461  N  N     . GLU A 1 1157 ? 168.680 188.065 204.104 1.00 83.43  ? 2374 GLU A N     1 
ATOM   7462  C  CA    . GLU A 1 1157 ? 167.243 188.094 203.869 1.00 86.17  ? 2374 GLU A CA    1 
ATOM   7463  C  C     . GLU A 1 1157 ? 166.546 186.812 204.295 1.00 81.77  ? 2374 GLU A C     1 
ATOM   7464  O  O     . GLU A 1 1157 ? 165.377 186.867 204.681 1.00 79.46  ? 2374 GLU A O     1 
ATOM   7465  C  CB    . GLU A 1 1157 ? 166.976 188.401 202.379 1.00 87.34  ? 2374 GLU A CB    1 
ATOM   7466  C  CG    . GLU A 1 1157 ? 165.540 188.778 201.912 1.00 87.26  ? 2374 GLU A CG    1 
ATOM   7467  C  CD    . GLU A 1 1157 ? 164.489 187.671 201.948 1.00 83.85  ? 2374 GLU A CD    1 
ATOM   7468  O  OE1   . GLU A 1 1157 ? 163.294 188.002 201.809 1.00 82.72  ? 2374 GLU A OE1   1 
ATOM   7469  O  OE2   . GLU A 1 1157 ? 164.839 186.475 201.996 1.00 79.55  ? 2374 GLU A OE2   1 
ATOM   7470  N  N     . ILE A 1 1158 ? 167.247 185.680 204.273 1.00 80.33  ? 2375 ILE A N     1 
ATOM   7471  C  CA    . ILE A 1 1158 ? 166.617 184.361 204.435 1.00 75.21  ? 2375 ILE A CA    1 
ATOM   7472  C  C     . ILE A 1 1158 ? 165.981 184.248 205.818 1.00 74.17  ? 2375 ILE A C     1 
ATOM   7473  O  O     . ILE A 1 1158 ? 166.614 184.613 206.830 1.00 72.80  ? 2375 ILE A O     1 
ATOM   7474  C  CB    . ILE A 1 1158 ? 167.648 183.239 204.203 1.00 69.74  ? 2375 ILE A CB    1 
ATOM   7475  C  CG1   . ILE A 1 1158 ? 168.909 183.462 205.043 1.00 72.18  ? 2375 ILE A CG1   1 
ATOM   7476  C  CG2   . ILE A 1 1158 ? 168.020 183.153 202.735 1.00 59.46  ? 2375 ILE A CG2   1 
ATOM   7477  C  CD1   . ILE A 1 1158 ? 169.852 182.285 205.043 1.00 63.53  ? 2375 ILE A CD1   1 
ATOM   7478  N  N     . PRO A 1 1159 ? 164.731 183.791 205.923 1.00 71.55  ? 2376 PRO A N     1 
ATOM   7479  C  CA    . PRO A 1 1159 ? 164.114 183.623 207.244 1.00 71.11  ? 2376 PRO A CA    1 
ATOM   7480  C  C     . PRO A 1 1159 ? 164.337 182.232 207.814 1.00 71.05  ? 2376 PRO A C     1 
ATOM   7481  O  O     . PRO A 1 1159 ? 164.210 181.232 207.101 1.00 70.32  ? 2376 PRO A O     1 
ATOM   7482  C  CB    . PRO A 1 1159 ? 162.630 183.890 206.969 1.00 68.10  ? 2376 PRO A CB    1 
ATOM   7483  C  CG    . PRO A 1 1159 ? 162.435 183.541 205.516 1.00 65.99  ? 2376 PRO A CG    1 
ATOM   7484  C  CD    . PRO A 1 1159 ? 163.782 183.525 204.829 1.00 67.41  ? 2376 PRO A CD    1 
ATOM   7485  N  N     . SER A 1 1160 ? 164.672 182.156 209.101 1.00 72.19  ? 2377 SER A N     1 
ATOM   7486  C  CA    . SER A 1 1160 ? 164.870 180.872 209.772 1.00 76.39  ? 2377 SER A CA    1 
ATOM   7487  C  C     . SER A 1 1160 ? 163.514 180.388 210.275 1.00 77.02  ? 2377 SER A C     1 
ATOM   7488  O  O     . SER A 1 1160 ? 163.140 180.562 211.436 1.00 73.99  ? 2377 SER A O     1 
ATOM   7489  C  CB    . SER A 1 1160 ? 165.885 181.004 210.900 1.00 82.10  ? 2377 SER A CB    1 
ATOM   7490  O  OG    . SER A 1 1160 ? 167.145 181.423 210.404 1.00 88.81  ? 2377 SER A OG    1 
ATOM   7491  N  N     . VAL A 1 1161 ? 162.767 179.765 209.369 1.00 81.09  ? 2378 VAL A N     1 
ATOM   7492  C  CA    . VAL A 1 1161 ? 161.418 179.305 209.673 1.00 79.33  ? 2378 VAL A CA    1 
ATOM   7493  C  C     . VAL A 1 1161 ? 161.499 178.042 210.522 1.00 74.30  ? 2378 VAL A C     1 
ATOM   7494  O  O     . VAL A 1 1161 ? 162.403 177.213 210.354 1.00 74.66  ? 2378 VAL A O     1 
ATOM   7495  C  CB    . VAL A 1 1161 ? 160.619 179.085 208.372 1.00 72.65  ? 2378 VAL A CB    1 
ATOM   7496  C  CG1   . VAL A 1 1161 ? 161.231 177.976 207.521 1.00 59.08  ? 2378 VAL A CG1   1 
ATOM   7497  C  CG2   . VAL A 1 1161 ? 159.148 178.807 208.668 1.00 77.88  ? 2378 VAL A CG2   1 
ATOM   7498  N  N     . SER A 1 1162 ? 160.578 177.913 211.471 1.00 73.05  ? 2379 SER A N     1 
ATOM   7499  C  CA    . SER A 1 1162 ? 160.534 176.773 212.381 1.00 75.93  ? 2379 SER A CA    1 
ATOM   7500  C  C     . SER A 1 1162 ? 159.212 176.042 212.176 1.00 79.10  ? 2379 SER A C     1 
ATOM   7501  O  O     . SER A 1 1162 ? 158.211 176.356 212.825 1.00 77.49  ? 2379 SER A O     1 
ATOM   7502  C  CB    . SER A 1 1162 ? 160.700 177.227 213.828 1.00 79.66  ? 2379 SER A CB    1 
ATOM   7503  O  OG    . SER A 1 1162 ? 159.451 177.578 214.398 1.00 79.99  ? 2379 SER A OG    1 
ATOM   7504  N  N     . LEU A 1 1163 ? 159.212 175.069 211.270 1.00 85.23  ? 2380 LEU A N     1 
ATOM   7505  C  CA    . LEU A 1 1163 ? 158.058 174.203 211.101 1.00 83.02  ? 2380 LEU A CA    1 
ATOM   7506  C  C     . LEU A 1 1163 ? 157.953 173.238 212.277 1.00 81.81  ? 2380 LEU A C     1 
ATOM   7507  O  O     . LEU A 1 1163 ? 158.950 172.878 212.909 1.00 79.70  ? 2380 LEU A O     1 
ATOM   7508  C  CB    . LEU A 1 1163 ? 158.142 173.421 209.786 1.00 79.40  ? 2380 LEU A CB    1 
ATOM   7509  C  CG    . LEU A 1 1163 ? 159.126 172.257 209.612 1.00 78.03  ? 2380 LEU A CG    1 
ATOM   7510  C  CD1   . LEU A 1 1163 ? 158.729 171.430 208.403 1.00 69.76  ? 2380 LEU A CD1   1 
ATOM   7511  C  CD2   . LEU A 1 1163 ? 160.562 172.734 209.454 1.00 66.63  ? 2380 LEU A CD2   1 
ATOM   7512  N  N     . GLU A 1 1164 ? 156.726 172.817 212.573 1.00 81.24  ? 2381 GLU A N     1 
ATOM   7513  C  CA    . GLU A 1 1164 ? 156.538 171.857 213.648 1.00 83.58  ? 2381 GLU A CA    1 
ATOM   7514  C  C     . GLU A 1 1164 ? 156.835 170.445 213.145 1.00 82.52  ? 2381 GLU A C     1 
ATOM   7515  O  O     . GLU A 1 1164 ? 157.325 170.240 212.031 1.00 82.63  ? 2381 GLU A O     1 
ATOM   7516  C  CB    . GLU A 1 1164 ? 155.131 171.962 214.237 1.00 84.44  ? 2381 GLU A CB    1 
ATOM   7517  C  CG    . GLU A 1 1164 ? 153.994 171.505 213.337 1.00 88.19  ? 2381 GLU A CG    1 
ATOM   7518  C  CD    . GLU A 1 1164 ? 153.497 172.590 212.406 1.00 94.46  ? 2381 GLU A CD    1 
ATOM   7519  O  OE1   . GLU A 1 1164 ? 154.203 173.604 212.219 1.00 92.28  ? 2381 GLU A OE1   1 
ATOM   7520  O  OE2   . GLU A 1 1164 ? 152.379 172.434 211.875 1.00 96.82  ? 2381 GLU A OE2   1 
ATOM   7521  N  N     . ALA A 1 1165 ? 156.542 169.458 213.993 1.00 81.54  ? 2382 ALA A N     1 
ATOM   7522  C  CA    . ALA A 1 1165 ? 156.947 168.083 213.718 1.00 76.29  ? 2382 ALA A CA    1 
ATOM   7523  C  C     . ALA A 1 1165 ? 156.220 167.506 212.507 1.00 76.24  ? 2382 ALA A C     1 
ATOM   7524  O  O     . ALA A 1 1165 ? 156.840 166.880 211.640 1.00 75.18  ? 2382 ALA A O     1 
ATOM   7525  C  CB    . ALA A 1 1165 ? 156.707 167.219 214.955 1.00 73.13  ? 2382 ALA A CB    1 
ATOM   7526  N  N     . HIS A 1 1166 ? 154.905 167.709 212.426 1.00 74.22  ? 2383 HIS A N     1 
ATOM   7527  C  CA    . HIS A 1 1166 ? 154.078 167.006 211.454 1.00 75.45  ? 2383 HIS A CA    1 
ATOM   7528  C  C     . HIS A 1 1166 ? 153.895 167.767 210.142 1.00 73.36  ? 2383 HIS A C     1 
ATOM   7529  O  O     . HIS A 1 1166 ? 152.925 167.507 209.423 1.00 73.22  ? 2383 HIS A O     1 
ATOM   7530  C  CB    . HIS A 1 1166 ? 152.713 166.675 212.061 1.00 80.76  ? 2383 HIS A CB    1 
ATOM   7531  C  CG    . HIS A 1 1166 ? 152.118 167.789 212.864 1.00 89.83  ? 2383 HIS A CG    1 
ATOM   7532  N  ND1   . HIS A 1 1166 ? 152.104 167.788 214.242 1.00 87.93  ? 2383 HIS A ND1   1 
ATOM   7533  C  CD2   . HIS A 1 1166 ? 151.515 168.939 212.481 1.00 93.60  ? 2383 HIS A CD2   1 
ATOM   7534  C  CE1   . HIS A 1 1166 ? 151.517 168.890 214.674 1.00 93.27  ? 2383 HIS A CE1   1 
ATOM   7535  N  NE2   . HIS A 1 1166 ? 151.150 169.605 213.626 1.00 92.47  ? 2383 HIS A NE2   1 
ATOM   7536  N  N     . GLU A 1 1167 ? 154.791 168.695 209.811 1.00 71.89  ? 2384 GLU A N     1 
ATOM   7537  C  CA    . GLU A 1 1167 ? 154.777 169.281 208.476 1.00 78.06  ? 2384 GLU A CA    1 
ATOM   7538  C  C     . GLU A 1 1167 ? 155.809 168.665 207.542 1.00 71.08  ? 2384 GLU A C     1 
ATOM   7539  O  O     . GLU A 1 1167 ? 155.984 169.163 206.425 1.00 63.55  ? 2384 GLU A O     1 
ATOM   7540  C  CB    . GLU A 1 1167 ? 154.980 170.801 208.531 1.00 84.81  ? 2384 GLU A CB    1 
ATOM   7541  C  CG    . GLU A 1 1167 ? 153.794 171.547 209.106 1.00 88.10  ? 2384 GLU A CG    1 
ATOM   7542  C  CD    . GLU A 1 1167 ? 153.997 173.049 209.128 1.00 87.40  ? 2384 GLU A CD    1 
ATOM   7543  O  OE1   . GLU A 1 1167 ? 155.113 173.505 208.815 1.00 87.03  ? 2384 GLU A OE1   1 
ATOM   7544  O  OE2   . GLU A 1 1167 ? 153.035 173.777 209.452 1.00 84.92  ? 2384 GLU A OE2   1 
ATOM   7545  N  N     . VAL A 1 1168 ? 156.502 167.607 207.970 1.00 68.79  ? 2385 VAL A N     1 
ATOM   7546  C  CA    . VAL A 1 1168 ? 157.348 166.852 207.049 1.00 64.51  ? 2385 VAL A CA    1 
ATOM   7547  C  C     . VAL A 1 1168 ? 156.543 165.902 206.177 1.00 65.06  ? 2385 VAL A C     1 
ATOM   7548  O  O     . VAL A 1 1168 ? 157.053 165.447 205.146 1.00 66.14  ? 2385 VAL A O     1 
ATOM   7549  C  CB    . VAL A 1 1168 ? 158.435 166.069 207.808 1.00 60.52  ? 2385 VAL A CB    1 
ATOM   7550  C  CG1   . VAL A 1 1168 ? 159.444 167.028 208.425 1.00 52.40  ? 2385 VAL A CG1   1 
ATOM   7551  C  CG2   . VAL A 1 1168 ? 157.807 165.190 208.875 1.00 64.26  ? 2385 VAL A CG2   1 
ATOM   7552  N  N     . MET A 1 1169 ? 155.301 165.587 206.557 1.00 63.66  ? 2386 MET A N     1 
ATOM   7553  C  CA    . MET A 1 1169 ? 154.416 164.864 205.649 1.00 65.91  ? 2386 MET A CA    1 
ATOM   7554  C  C     . MET A 1 1169 ? 154.023 165.711 204.448 1.00 70.26  ? 2386 MET A C     1 
ATOM   7555  O  O     . MET A 1 1169 ? 153.820 165.172 203.354 1.00 70.65  ? 2386 MET A O     1 
ATOM   7556  C  CB    . MET A 1 1169 ? 153.152 164.393 206.368 1.00 66.05  ? 2386 MET A CB    1 
ATOM   7557  C  CG    . MET A 1 1169 ? 153.336 163.853 207.770 1.00 71.47  ? 2386 MET A CG    1 
ATOM   7558  S  SD    . MET A 1 1169 ? 154.300 162.332 207.761 1.00 81.46  ? 2386 MET A SD    1 
ATOM   7559  C  CE    . MET A 1 1169 ? 153.858 161.657 209.355 1.00 76.06  ? 2386 MET A CE    1 
ATOM   7560  N  N     . ARG A 1 1170 ? 153.897 167.017 204.628 1.00 67.70  ? 2387 ARG A N     1 
ATOM   7561  C  CA    . ARG A 1 1170 ? 153.467 167.881 203.537 1.00 63.37  ? 2387 ARG A CA    1 
ATOM   7562  C  C     . ARG A 1 1170 ? 154.591 168.017 202.520 1.00 64.48  ? 2387 ARG A C     1 
ATOM   7563  O  O     . ARG A 1 1170 ? 155.686 168.470 202.878 1.00 63.19  ? 2387 ARG A O     1 
ATOM   7564  C  CB    . ARG A 1 1170 ? 153.060 169.249 204.068 1.00 62.07  ? 2387 ARG A CB    1 
ATOM   7565  C  CG    . ARG A 1 1170 ? 151.722 169.267 204.785 1.00 66.05  ? 2387 ARG A CG    1 
ATOM   7566  C  CD    . ARG A 1 1170 ? 150.899 170.478 204.372 1.00 68.28  ? 2387 ARG A CD    1 
ATOM   7567  N  NE    . ARG A 1 1170 ? 150.766 170.586 202.924 1.00 70.13  ? 2387 ARG A NE    1 
ATOM   7568  C  CZ    . ARG A 1 1170 ? 149.979 169.820 202.180 1.00 69.11  ? 2387 ARG A CZ    1 
ATOM   7569  N  NH1   . ARG A 1 1170 ? 149.201 168.895 202.719 1.00 71.97  ? 2387 ARG A NH1   1 
ATOM   7570  N  NH2   . ARG A 1 1170 ? 149.963 169.995 200.861 1.00 67.03  ? 2387 ARG A NH2   1 
ATOM   7571  N  N     . PRO A 1 1171 ? 154.376 167.643 201.256 1.00 63.63  ? 2388 PRO A N     1 
ATOM   7572  C  CA    . PRO A 1 1171 ? 155.470 167.679 200.277 1.00 60.34  ? 2388 PRO A CA    1 
ATOM   7573  C  C     . PRO A 1 1171 ? 155.797 169.065 199.750 1.00 60.11  ? 2388 PRO A C     1 
ATOM   7574  O  O     . PRO A 1 1171 ? 156.802 169.209 199.041 1.00 63.51  ? 2388 PRO A O     1 
ATOM   7575  C  CB    . PRO A 1 1171 ? 154.951 166.779 199.148 1.00 58.73  ? 2388 PRO A CB    1 
ATOM   7576  C  CG    . PRO A 1 1171 ? 153.470 166.880 199.243 1.00 58.55  ? 2388 PRO A CG    1 
ATOM   7577  C  CD    . PRO A 1 1171 ? 153.136 167.081 200.694 1.00 62.05  ? 2388 PRO A CD    1 
ATOM   7578  N  N     . ASP A 1 1172 ? 154.997 170.082 200.063 1.00 57.75  ? 2389 ASP A N     1 
ATOM   7579  C  CA    . ASP A 1 1172 ? 155.187 171.415 199.508 1.00 58.65  ? 2389 ASP A CA    1 
ATOM   7580  C  C     . ASP A 1 1172 ? 155.836 172.385 200.485 1.00 52.98  ? 2389 ASP A C     1 
ATOM   7581  O  O     . ASP A 1 1172 ? 155.914 173.581 200.190 1.00 50.81  ? 2389 ASP A O     1 
ATOM   7582  C  CB    . ASP A 1 1172 ? 153.851 171.982 199.027 1.00 64.01  ? 2389 ASP A CB    1 
ATOM   7583  C  CG    . ASP A 1 1172 ? 152.787 171.957 200.102 1.00 67.28  ? 2389 ASP A CG    1 
ATOM   7584  O  OD1   . ASP A 1 1172 ? 152.708 172.927 200.885 1.00 65.68  ? 2389 ASP A OD1   1 
ATOM   7585  O  OD2   . ASP A 1 1172 ? 152.025 170.971 200.160 1.00 70.44  ? 2389 ASP A OD2   1 
ATOM   7586  N  N     . ILE A 1 1173 ? 156.303 171.908 201.633 1.00 51.59  ? 2390 ILE A N     1 
ATOM   7587  C  CA    . ILE A 1 1173 ? 156.987 172.772 202.589 1.00 51.49  ? 2390 ILE A CA    1 
ATOM   7588  C  C     . ILE A 1 1173 ? 158.384 173.063 202.061 1.00 50.60  ? 2390 ILE A C     1 
ATOM   7589  O  O     . ILE A 1 1173 ? 159.182 172.145 201.844 1.00 52.33  ? 2390 ILE A O     1 
ATOM   7590  C  CB    . ILE A 1 1173 ? 157.043 172.131 203.982 1.00 54.79  ? 2390 ILE A CB    1 
ATOM   7591  C  CG1   . ILE A 1 1173 ? 155.640 171.754 204.459 1.00 63.99  ? 2390 ILE A CG1   1 
ATOM   7592  C  CG2   . ILE A 1 1173 ? 157.713 173.069 204.974 1.00 51.08  ? 2390 ILE A CG2   1 
ATOM   7593  C  CD1   . ILE A 1 1173 ? 154.653 172.901 204.448 1.00 64.64  ? 2390 ILE A CD1   1 
ATOM   7594  N  N     . VAL A 1 1174 ? 158.684 174.341 201.852 1.00 45.71  ? 2391 VAL A N     1 
ATOM   7595  C  CA    . VAL A 1 1174 ? 159.956 174.772 201.287 1.00 40.38  ? 2391 VAL A CA    1 
ATOM   7596  C  C     . VAL A 1 1174 ? 160.786 175.379 202.404 1.00 36.42  ? 2391 VAL A C     1 
ATOM   7597  O  O     . VAL A 1 1174 ? 160.344 176.320 203.076 1.00 33.84  ? 2391 VAL A O     1 
ATOM   7598  C  CB    . VAL A 1 1174 ? 159.759 175.783 200.149 1.00 37.32  ? 2391 VAL A CB    1 
ATOM   7599  C  CG1   . VAL A 1 1174 ? 161.100 176.153 199.527 1.00 34.62  ? 2391 VAL A CG1   1 
ATOM   7600  C  CG2   . VAL A 1 1174 ? 158.797 175.237 199.117 1.00 38.68  ? 2391 VAL A CG2   1 
ATOM   7601  N  N     . ILE A 1 1175 ? 161.986 174.844 202.604 1.00 36.94  ? 2392 ILE A N     1 
ATOM   7602  C  CA    . ILE A 1 1175 ? 162.945 175.401 203.551 1.00 36.97  ? 2392 ILE A CA    1 
ATOM   7603  C  C     . ILE A 1 1175 ? 163.765 176.450 202.803 1.00 38.07  ? 2392 ILE A C     1 
ATOM   7604  O  O     . ILE A 1 1175 ? 164.533 176.083 201.898 1.00 38.32  ? 2392 ILE A O     1 
ATOM   7605  C  CB    . ILE A 1 1175 ? 163.845 174.312 204.146 1.00 39.21  ? 2392 ILE A CB    1 
ATOM   7606  C  CG1   . ILE A 1 1175 ? 163.025 173.353 205.014 1.00 36.20  ? 2392 ILE A CG1   1 
ATOM   7607  C  CG2   . ILE A 1 1175 ? 164.974 174.934 204.943 1.00 42.47  ? 2392 ILE A CG2   1 
ATOM   7608  C  CD1   . ILE A 1 1175 ? 162.111 174.035 206.010 1.00 34.84  ? 2392 ILE A CD1   1 
ATOM   7609  N  N     . PRO A 1 1176 ? 163.628 177.735 203.125 1.00 35.98  ? 2393 PRO A N     1 
ATOM   7610  C  CA    . PRO A 1 1176 ? 164.325 178.765 202.344 1.00 35.42  ? 2393 PRO A CA    1 
ATOM   7611  C  C     . PRO A 1 1176 ? 165.818 178.767 202.632 1.00 34.18  ? 2393 PRO A C     1 
ATOM   7612  O  O     . PRO A 1 1176 ? 166.246 178.728 203.787 1.00 36.55  ? 2393 PRO A O     1 
ATOM   7613  C  CB    . PRO A 1 1176 ? 163.660 180.068 202.801 1.00 39.09  ? 2393 PRO A CB    1 
ATOM   7614  C  CG    . PRO A 1 1176 ? 163.120 179.760 204.151 1.00 41.26  ? 2393 PRO A CG    1 
ATOM   7615  C  CD    . PRO A 1 1176 ? 162.721 178.317 204.127 1.00 37.79  ? 2393 PRO A CD    1 
ATOM   7616  N  N     . THR A 1 1177 ? 166.608 178.808 201.564 1.00 33.70  ? 2394 THR A N     1 
ATOM   7617  C  CA    . THR A 1 1177 ? 168.052 178.954 201.673 1.00 36.14  ? 2394 THR A CA    1 
ATOM   7618  C  C     . THR A 1 1177 ? 168.500 180.129 200.813 1.00 36.81  ? 2394 THR A C     1 
ATOM   7619  O  O     . THR A 1 1177 ? 167.660 180.853 200.270 1.00 38.56  ? 2394 THR A O     1 
ATOM   7620  C  CB    . THR A 1 1177 ? 168.763 177.663 201.258 1.00 37.59  ? 2394 THR A CB    1 
ATOM   7621  O  OG1   . THR A 1 1177 ? 170.167 177.780 201.514 1.00 38.72  ? 2394 THR A OG1   1 
ATOM   7622  C  CG2   . THR A 1 1177 ? 168.538 177.373 199.782 1.00 37.18  ? 2394 THR A CG2   1 
ATOM   7623  N  N     . ILE A 1 1178 ? 169.811 180.340 200.697 1.00 38.14  ? 2395 ILE A N     1 
ATOM   7624  C  CA    . ILE A 1 1178 ? 170.318 181.432 199.869 1.00 39.02  ? 2395 ILE A CA    1 
ATOM   7625  C  C     . ILE A 1 1178 ? 169.980 181.189 198.403 1.00 36.01  ? 2395 ILE A C     1 
ATOM   7626  O  O     . ILE A 1 1178 ? 169.517 182.093 197.694 1.00 34.21  ? 2395 ILE A O     1 
ATOM   7627  C  CB    . ILE A 1 1178 ? 171.834 181.602 200.078 1.00 42.02  ? 2395 ILE A CB    1 
ATOM   7628  C  CG1   . ILE A 1 1178 ? 172.139 181.968 201.533 1.00 49.19  ? 2395 ILE A CG1   1 
ATOM   7629  C  CG2   . ILE A 1 1178 ? 172.391 182.656 199.134 1.00 38.03  ? 2395 ILE A CG2   1 
ATOM   7630  C  CD1   . ILE A 1 1178 ? 172.686 180.818 202.356 1.00 42.49  ? 2395 ILE A CD1   1 
ATOM   7631  N  N     . ASP A 1 1179 ? 170.194 179.957 197.934 1.00 34.24  ? 2396 ASP A N     1 
ATOM   7632  C  CA    . ASP A 1 1179 ? 169.944 179.630 196.535 1.00 31.01  ? 2396 ASP A CA    1 
ATOM   7633  C  C     . ASP A 1 1179 ? 168.463 179.726 196.193 1.00 29.16  ? 2396 ASP A C     1 
ATOM   7634  O  O     . ASP A 1 1179 ? 168.106 180.167 195.096 1.00 31.07  ? 2396 ASP A O     1 
ATOM   7635  C  CB    . ASP A 1 1179 ? 170.476 178.233 196.221 1.00 30.77  ? 2396 ASP A CB    1 
ATOM   7636  C  CG    . ASP A 1 1179 ? 171.988 178.180 196.202 1.00 28.33  ? 2396 ASP A CG    1 
ATOM   7637  O  OD1   . ASP A 1 1179 ? 172.621 179.181 196.597 1.00 29.54  ? 2396 ASP A OD1   1 
ATOM   7638  O  OD2   . ASP A 1 1179 ? 172.543 177.140 195.793 1.00 26.36  ? 2396 ASP A OD2   1 
ATOM   7639  N  N     . THR A 1 1180 ? 167.587 179.316 197.115 1.00 27.86  ? 2397 THR A N     1 
ATOM   7640  C  CA    . THR A 1 1180 ? 166.151 179.405 196.865 1.00 29.12  ? 2397 THR A CA    1 
ATOM   7641  C  C     . THR A 1 1180 ? 165.705 180.853 196.709 1.00 35.26  ? 2397 THR A C     1 
ATOM   7642  O  O     . THR A 1 1180 ? 164.927 181.176 195.804 1.00 40.61  ? 2397 THR A O     1 
ATOM   7643  C  CB    . THR A 1 1180 ? 165.379 178.724 197.995 1.00 32.65  ? 2397 THR A CB    1 
ATOM   7644  O  OG1   . THR A 1 1180 ? 165.715 177.332 198.032 1.00 37.85  ? 2397 THR A OG1   1 
ATOM   7645  C  CG2   . THR A 1 1180 ? 163.879 178.870 197.790 1.00 28.64  ? 2397 THR A CG2   1 
ATOM   7646  N  N     . ILE A 1 1181 ? 166.211 181.745 197.564 1.00 34.29  ? 2398 ILE A N     1 
ATOM   7647  C  CA    . ILE A 1 1181 ? 165.852 183.157 197.470 1.00 32.59  ? 2398 ILE A CA    1 
ATOM   7648  C  C     . ILE A 1 1181 ? 166.425 183.778 196.201 1.00 31.17  ? 2398 ILE A C     1 
ATOM   7649  O  O     . ILE A 1 1181 ? 165.754 184.570 195.529 1.00 36.50  ? 2398 ILE A O     1 
ATOM   7650  C  CB    . ILE A 1 1181 ? 166.306 183.908 198.735 1.00 37.87  ? 2398 ILE A CB    1 
ATOM   7651  C  CG1   . ILE A 1 1181 ? 165.607 183.330 199.967 1.00 41.98  ? 2398 ILE A CG1   1 
ATOM   7652  C  CG2   . ILE A 1 1181 ? 166.030 185.398 198.617 1.00 46.84  ? 2398 ILE A CG2   1 
ATOM   7653  C  CD1   . ILE A 1 1181 ? 164.097 183.442 199.924 1.00 40.46  ? 2398 ILE A CD1   1 
ATOM   7654  N  N     . LYS A 1 1182 ? 167.662 183.422 195.844 1.00 26.91  ? 2399 LYS A N     1 
ATOM   7655  C  CA    . LYS A 1 1182 ? 168.257 183.931 194.610 1.00 28.57  ? 2399 LYS A CA    1 
ATOM   7656  C  C     . LYS A 1 1182 ? 167.454 183.499 193.387 1.00 25.76  ? 2399 LYS A C     1 
ATOM   7657  O  O     . LYS A 1 1182 ? 167.159 184.311 192.497 1.00 23.48  ? 2399 LYS A O     1 
ATOM   7658  C  CB    . LYS A 1 1182 ? 169.701 183.449 194.496 1.00 28.23  ? 2399 LYS A CB    1 
ATOM   7659  C  CG    . LYS A 1 1182 ? 170.380 183.831 193.198 1.00 24.62  ? 2399 LYS A CG    1 
ATOM   7660  C  CD    . LYS A 1 1182 ? 171.732 183.154 193.066 1.00 23.25  ? 2399 LYS A CD    1 
ATOM   7661  C  CE    . LYS A 1 1182 ? 171.586 181.741 192.527 1.00 22.31  ? 2399 LYS A CE    1 
ATOM   7662  N  NZ    . LYS A 1 1182 ? 172.906 181.085 192.318 1.00 20.42  ? 2399 LYS A NZ    1 
ATOM   7663  N  N     . HIS A 1 1183 ? 167.076 182.219 193.338 1.00 27.17  ? 2400 HIS A N     1 
ATOM   7664  C  CA    . HIS A 1 1183 ? 166.325 181.705 192.201 1.00 22.45  ? 2400 HIS A CA    1 
ATOM   7665  C  C     . HIS A 1 1183 ? 164.925 182.297 192.150 1.00 20.76  ? 2400 HIS A C     1 
ATOM   7666  O  O     . HIS A 1 1183 ? 164.420 182.597 191.066 1.00 24.30  ? 2400 HIS A O     1 
ATOM   7667  C  CB    . HIS A 1 1183 ? 166.273 180.179 192.251 1.00 20.70  ? 2400 HIS A CB    1 
ATOM   7668  C  CG    . HIS A 1 1183 ? 167.530 179.518 191.776 1.00 21.79  ? 2400 HIS A CG    1 
ATOM   7669  N  ND1   . HIS A 1 1183 ? 168.039 179.711 190.510 1.00 20.13  ? 2400 HIS A ND1   1 
ATOM   7670  C  CD2   . HIS A 1 1183 ? 168.385 178.674 192.400 1.00 23.98  ? 2400 HIS A CD2   1 
ATOM   7671  C  CE1   . HIS A 1 1183 ? 169.151 179.011 190.374 1.00 21.37  ? 2400 HIS A CE1   1 
ATOM   7672  N  NE2   . HIS A 1 1183 ? 169.383 178.373 191.506 1.00 24.93  ? 2400 HIS A NE2   1 
ATOM   7673  N  N     . GLU A 1 1184 ? 164.290 182.503 193.307 1.00 20.39  ? 2401 GLU A N     1 
ATOM   7674  C  CA    . GLU A 1 1184 ? 162.972 183.130 193.308 1.00 25.45  ? 2401 GLU A CA    1 
ATOM   7675  C  C     . GLU A 1 1184 ? 163.049 184.590 192.875 1.00 26.50  ? 2401 GLU A C     1 
ATOM   7676  O  O     . GLU A 1 1184 ? 162.153 185.082 192.182 1.00 24.09  ? 2401 GLU A O     1 
ATOM   7677  C  CB    . GLU A 1 1184 ? 162.323 183.010 194.686 1.00 27.99  ? 2401 GLU A CB    1 
ATOM   7678  C  CG    . GLU A 1 1184 ? 160.931 183.630 194.754 1.00 34.15  ? 2401 GLU A CG    1 
ATOM   7679  C  CD    . GLU A 1 1184 ? 160.141 183.193 195.969 1.00 40.61  ? 2401 GLU A CD    1 
ATOM   7680  O  OE1   . GLU A 1 1184 ? 160.225 182.005 196.337 1.00 40.03  ? 2401 GLU A OE1   1 
ATOM   7681  O  OE2   . GLU A 1 1184 ? 159.429 184.037 196.551 1.00 40.61  ? 2401 GLU A OE2   1 
ATOM   7682  N  N     . LYS A 1 1185 ? 164.114 185.298 193.256 1.00 26.06  ? 2402 LYS A N     1 
ATOM   7683  C  CA    . LYS A 1 1185 ? 164.247 186.694 192.850 1.00 25.10  ? 2402 LYS A CA    1 
ATOM   7684  C  C     . LYS A 1 1185 ? 164.469 186.812 191.347 1.00 28.85  ? 2402 LYS A C     1 
ATOM   7685  O  O     . LYS A 1 1185 ? 163.839 187.644 190.679 1.00 30.33  ? 2402 LYS A O     1 
ATOM   7686  C  CB    . LYS A 1 1185 ? 165.388 187.357 193.619 1.00 30.64  ? 2402 LYS A CB    1 
ATOM   7687  C  CG    . LYS A 1 1185 ? 165.587 188.824 193.289 1.00 34.29  ? 2402 LYS A CG    1 
ATOM   7688  C  CD    . LYS A 1 1185 ? 164.567 189.692 194.008 1.00 44.38  ? 2402 LYS A CD    1 
ATOM   7689  C  CE    . LYS A 1 1185 ? 164.965 191.159 193.980 1.00 46.98  ? 2402 LYS A CE    1 
ATOM   7690  N  NZ    . LYS A 1 1185 ? 164.566 191.864 195.230 1.00 42.33  ? 2402 LYS A NZ    1 
ATOM   7691  N  N     . ILE A 1 1186 ? 165.358 185.981 190.791 1.00 30.87  ? 2403 ILE A N     1 
ATOM   7692  C  CA    . ILE A 1 1186 ? 165.576 186.045 189.347 1.00 24.06  ? 2403 ILE A CA    1 
ATOM   7693  C  C     . ILE A 1 1186 ? 164.343 185.544 188.598 1.00 19.01  ? 2403 ILE A C     1 
ATOM   7694  O  O     . ILE A 1 1186 ? 164.030 186.036 187.506 1.00 22.16  ? 2403 ILE A O     1 
ATOM   7695  C  CB    . ILE A 1 1186 ? 166.861 185.291 188.942 1.00 18.51  ? 2403 ILE A CB    1 
ATOM   7696  C  CG1   . ILE A 1 1186 ? 167.205 185.556 187.475 1.00 21.77  ? 2403 ILE A CG1   1 
ATOM   7697  C  CG2   . ILE A 1 1186 ? 166.742 183.803 189.181 1.00 18.91  ? 2403 ILE A CG2   1 
ATOM   7698  C  CD1   . ILE A 1 1186 ? 167.195 187.020 187.096 1.00 25.60  ? 2403 ILE A CD1   1 
ATOM   7699  N  N     . PHE A 1 1187 ? 163.595 184.608 189.187 1.00 15.84  ? 2404 PHE A N     1 
ATOM   7700  C  CA    . PHE A 1 1187 ? 162.343 184.166 188.591 1.00 15.86  ? 2404 PHE A CA    1 
ATOM   7701  C  C     . PHE A 1 1187 ? 161.311 185.280 188.565 1.00 18.67  ? 2404 PHE A C     1 
ATOM   7702  O  O     . PHE A 1 1187 ? 160.606 185.449 187.568 1.00 24.26  ? 2404 PHE A O     1 
ATOM   7703  C  CB    . PHE A 1 1187 ? 161.800 182.966 189.357 1.00 17.85  ? 2404 PHE A CB    1 
ATOM   7704  C  CG    . PHE A 1 1187 ? 160.754 182.210 188.617 1.00 16.31  ? 2404 PHE A CG    1 
ATOM   7705  C  CD1   . PHE A 1 1187 ? 160.935 181.876 187.290 1.00 19.93  ? 2404 PHE A CD1   1 
ATOM   7706  C  CD2   . PHE A 1 1187 ? 159.573 181.858 189.240 1.00 16.58  ? 2404 PHE A CD2   1 
ATOM   7707  C  CE1   . PHE A 1 1187 ? 159.963 181.188 186.604 1.00 22.51  ? 2404 PHE A CE1   1 
ATOM   7708  C  CE2   . PHE A 1 1187 ? 158.598 181.171 188.558 1.00 23.19  ? 2404 PHE A CE2   1 
ATOM   7709  C  CZ    . PHE A 1 1187 ? 158.794 180.838 187.236 1.00 25.59  ? 2404 PHE A CZ    1 
ATOM   7710  N  N     . TYR A 1 1188 ? 161.203 186.042 189.655 1.00 19.66  ? 2405 TYR A N     1 
ATOM   7711  C  CA    . TYR A 1 1188 ? 160.279 187.171 189.688 1.00 23.91  ? 2405 TYR A CA    1 
ATOM   7712  C  C     . TYR A 1 1188 ? 160.669 188.227 188.666 1.00 22.53  ? 2405 TYR A C     1 
ATOM   7713  O  O     . TYR A 1 1188 ? 159.804 188.791 187.988 1.00 19.56  ? 2405 TYR A O     1 
ATOM   7714  C  CB    . TYR A 1 1188 ? 160.243 187.783 191.087 1.00 27.21  ? 2405 TYR A CB    1 
ATOM   7715  C  CG    . TYR A 1 1188 ? 159.340 187.068 192.061 1.00 27.43  ? 2405 TYR A CG    1 
ATOM   7716  C  CD1   . TYR A 1 1188 ? 158.248 186.334 191.621 1.00 24.96  ? 2405 TYR A CD1   1 
ATOM   7717  C  CD2   . TYR A 1 1188 ? 159.583 187.129 193.426 1.00 32.57  ? 2405 TYR A CD2   1 
ATOM   7718  C  CE1   . TYR A 1 1188 ? 157.423 185.683 192.515 1.00 27.31  ? 2405 TYR A CE1   1 
ATOM   7719  C  CE2   . TYR A 1 1188 ? 158.767 186.482 194.325 1.00 34.19  ? 2405 TYR A CE2   1 
ATOM   7720  C  CZ    . TYR A 1 1188 ? 157.690 185.761 193.866 1.00 34.02  ? 2405 TYR A CZ    1 
ATOM   7721  O  OH    . TYR A 1 1188 ? 156.880 185.115 194.768 1.00 38.34  ? 2405 TYR A OH    1 
ATOM   7722  N  N     . ASP A 1 1189 ? 161.969 188.507 188.544 1.00 24.87  ? 2406 ASP A N     1 
ATOM   7723  C  CA    . ASP A 1 1189 ? 162.427 189.486 187.561 1.00 22.38  ? 2406 ASP A CA    1 
ATOM   7724  C  C     . ASP A 1 1189 ? 162.106 189.041 186.139 1.00 24.06  ? 2406 ASP A C     1 
ATOM   7725  O  O     . ASP A 1 1189 ? 161.595 189.829 185.333 1.00 22.29  ? 2406 ASP A O     1 
ATOM   7726  C  CB    . ASP A 1 1189 ? 163.926 189.722 187.723 1.00 23.48  ? 2406 ASP A CB    1 
ATOM   7727  C  CG    . ASP A 1 1189 ? 164.250 190.582 188.922 1.00 27.80  ? 2406 ASP A CG    1 
ATOM   7728  O  OD1   . ASP A 1 1189 ? 163.526 191.571 189.157 1.00 30.90  ? 2406 ASP A OD1   1 
ATOM   7729  O  OD2   . ASP A 1 1189 ? 165.220 190.264 189.637 1.00 29.27  ? 2406 ASP A OD2   1 
ATOM   7730  N  N     . LEU A 1 1190 ? 162.372 187.771 185.820 1.00 23.41  ? 2407 LEU A N     1 
ATOM   7731  C  CA    . LEU A 1 1190 ? 162.131 187.284 184.465 1.00 18.72  ? 2407 LEU A CA    1 
ATOM   7732  C  C     . LEU A 1 1190 ? 160.645 187.124 184.172 1.00 23.52  ? 2407 LEU A C     1 
ATOM   7733  O  O     . LEU A 1 1190 ? 160.228 187.234 183.015 1.00 29.43  ? 2407 LEU A O     1 
ATOM   7734  C  CB    . LEU A 1 1190 ? 162.861 185.963 184.249 1.00 12.86  ? 2407 LEU A CB    1 
ATOM   7735  C  CG    . LEU A 1 1190 ? 164.270 186.114 183.689 1.00 14.72  ? 2407 LEU A CG    1 
ATOM   7736  C  CD1   . LEU A 1 1190 ? 164.986 184.780 183.673 1.00 15.16  ? 2407 LEU A CD1   1 
ATOM   7737  C  CD2   . LEU A 1 1190 ? 164.191 186.703 182.296 1.00 15.63  ? 2407 LEU A CD2   1 
ATOM   7738  N  N     . LEU A 1 1191 ? 159.835 186.855 185.193 1.00 20.62  ? 2408 LEU A N     1 
ATOM   7739  C  CA    . LEU A 1 1191 ? 158.395 186.785 184.992 1.00 18.36  ? 2408 LEU A CA    1 
ATOM   7740  C  C     . LEU A 1 1191 ? 157.802 188.172 184.788 1.00 22.14  ? 2408 LEU A C     1 
ATOM   7741  O  O     . LEU A 1 1191 ? 156.988 188.378 183.881 1.00 24.53  ? 2408 LEU A O     1 
ATOM   7742  C  CB    . LEU A 1 1191 ? 157.749 186.088 186.185 1.00 21.33  ? 2408 LEU A CB    1 
ATOM   7743  C  CG    . LEU A 1 1191 ? 156.360 185.486 186.019 1.00 22.25  ? 2408 LEU A CG    1 
ATOM   7744  C  CD1   . LEU A 1 1191 ? 156.414 184.280 185.109 1.00 19.74  ? 2408 LEU A CD1   1 
ATOM   7745  C  CD2   . LEU A 1 1191 ? 155.847 185.099 187.381 1.00 19.82  ? 2408 LEU A CD2   1 
ATOM   7746  N  N     . ASN A 1 1192 ? 158.202 189.137 185.620 1.00 22.39  ? 2409 ASN A N     1 
ATOM   7747  C  CA    . ASN A 1 1192 ? 157.707 190.502 185.503 1.00 22.37  ? 2409 ASN A CA    1 
ATOM   7748  C  C     . ASN A 1 1192 ? 158.219 191.193 184.249 1.00 24.20  ? 2409 ASN A C     1 
ATOM   7749  O  O     . ASN A 1 1192 ? 157.584 192.138 183.772 1.00 23.72  ? 2409 ASN A O     1 
ATOM   7750  C  CB    . ASN A 1 1192 ? 158.108 191.303 186.743 1.00 20.57  ? 2409 ASN A CB    1 
ATOM   7751  C  CG    . ASN A 1 1192 ? 157.126 192.408 187.074 1.00 19.65  ? 2409 ASN A CG    1 
ATOM   7752  O  OD1   . ASN A 1 1192 ? 156.377 192.872 186.216 1.00 23.27  ? 2409 ASN A OD1   1 
ATOM   7753  N  ND2   . ASN A 1 1192 ? 157.128 192.838 188.330 1.00 20.84  ? 2409 ASN A ND2   1 
ATOM   7754  N  N     . SER A 1 1193 ? 159.339 190.733 183.695 1.00 22.88  ? 2410 SER A N     1 
ATOM   7755  C  CA    . SER A 1 1193 ? 159.926 191.338 182.510 1.00 22.76  ? 2410 SER A CA    1 
ATOM   7756  C  C     . SER A 1 1193 ? 159.223 190.931 181.219 1.00 23.19  ? 2410 SER A C     1 
ATOM   7757  O  O     . SER A 1 1193 ? 159.799 191.139 180.145 1.00 24.15  ? 2410 SER A O     1 
ATOM   7758  C  CB    . SER A 1 1193 ? 161.413 190.985 182.429 1.00 22.42  ? 2410 SER A CB    1 
ATOM   7759  O  OG    . SER A 1 1193 ? 161.928 191.241 181.137 1.00 24.93  ? 2410 SER A OG    1 
ATOM   7760  N  N     . LYS A 1 1194 ? 158.014 190.367 181.307 1.00 23.04  ? 2411 LYS A N     1 
ATOM   7761  C  CA    . LYS A 1 1194 ? 157.245 189.906 180.148 1.00 22.33  ? 2411 LYS A CA    1 
ATOM   7762  C  C     . LYS A 1 1194 ? 158.041 188.896 179.326 1.00 20.21  ? 2411 LYS A C     1 
ATOM   7763  O  O     . LYS A 1 1194 ? 158.100 188.973 178.097 1.00 19.74  ? 2411 LYS A O     1 
ATOM   7764  C  CB    . LYS A 1 1194 ? 156.788 191.081 179.278 1.00 23.80  ? 2411 LYS A CB    1 
ATOM   7765  C  CG    . LYS A 1 1194 ? 155.873 192.069 179.987 1.00 27.30  ? 2411 LYS A CG    1 
ATOM   7766  C  CD    . LYS A 1 1194 ? 154.447 191.552 180.077 1.00 24.65  ? 2411 LYS A CD    1 
ATOM   7767  C  CE    . LYS A 1 1194 ? 153.733 192.120 181.293 1.00 22.56  ? 2411 LYS A CE    1 
ATOM   7768  N  NZ    . LYS A 1 1194 ? 153.746 191.174 182.440 1.00 26.59  ? 2411 LYS A NZ    1 
ATOM   7769  N  N     . ARG A 1 1195 ? 158.662 187.942 180.015 1.00 19.15  ? 2412 ARG A N     1 
ATOM   7770  C  CA    . ARG A 1 1195 ? 159.559 186.980 179.396 1.00 14.75  ? 2412 ARG A CA    1 
ATOM   7771  C  C     . ARG A 1 1195 ? 159.258 185.594 179.947 1.00 11.66  ? 2412 ARG A C     1 
ATOM   7772  O  O     . ARG A 1 1195 ? 158.839 185.446 181.097 1.00 13.28  ? 2412 ARG A O     1 
ATOM   7773  C  CB    . ARG A 1 1195 ? 161.026 187.363 179.655 1.00 13.88  ? 2412 ARG A CB    1 
ATOM   7774  C  CG    . ARG A 1 1195 ? 162.053 186.547 178.899 1.00 13.65  ? 2412 ARG A CG    1 
ATOM   7775  C  CD    . ARG A 1 1195 ? 162.463 187.230 177.610 1.00 14.99  ? 2412 ARG A CD    1 
ATOM   7776  N  NE    . ARG A 1 1195 ? 163.461 186.453 176.887 1.00 14.97  ? 2412 ARG A NE    1 
ATOM   7777  C  CZ    . ARG A 1 1195 ? 163.361 186.107 175.611 1.00 13.12  ? 2412 ARG A CZ    1 
ATOM   7778  N  NH1   . ARG A 1 1195 ? 162.319 186.463 174.880 1.00 12.55  ? 2412 ARG A NH1   1 
ATOM   7779  N  NH2   . ARG A 1 1195 ? 164.331 185.387 175.057 1.00 11.73  ? 2412 ARG A NH2   1 
ATOM   7780  N  N     . GLY A 1 1196 ? 159.461 184.577 179.111 1.00 11.06  ? 2413 GLY A N     1 
ATOM   7781  C  CA    . GLY A 1 1196 ? 159.279 183.213 179.552 1.00 9.88   ? 2413 GLY A CA    1 
ATOM   7782  C  C     . GLY A 1 1196 ? 160.530 182.633 180.186 1.00 10.58  ? 2413 GLY A C     1 
ATOM   7783  O  O     . GLY A 1 1196 ? 161.652 183.061 179.927 1.00 13.17  ? 2413 GLY A O     1 
ATOM   7784  N  N     . ILE A 1 1197 ? 160.322 181.633 181.038 1.00 8.60   ? 2414 ILE A N     1 
ATOM   7785  C  CA    . ILE A 1 1197 ? 161.397 180.991 181.783 1.00 8.87   ? 2414 ILE A CA    1 
ATOM   7786  C  C     . ILE A 1 1197 ? 161.381 179.502 181.470 1.00 11.13  ? 2414 ILE A C     1 
ATOM   7787  O  O     . ILE A 1 1197 ? 160.311 178.892 181.380 1.00 14.62  ? 2414 ILE A O     1 
ATOM   7788  C  CB    . ILE A 1 1197 ? 161.265 181.231 183.304 1.00 9.80   ? 2414 ILE A CB    1 
ATOM   7789  C  CG1   . ILE A 1 1197 ? 161.398 182.714 183.643 1.00 12.04  ? 2414 ILE A CG1   1 
ATOM   7790  C  CG2   . ILE A 1 1197 ? 162.327 180.474 184.074 1.00 10.14  ? 2414 ILE A CG2   1 
ATOM   7791  C  CD1   . ILE A 1 1197 ? 160.088 183.453 183.779 1.00 14.36  ? 2414 ILE A CD1   1 
ATOM   7792  N  N     . ILE A 1 1198 ? 162.561 178.915 181.289 1.00 10.37  ? 2415 ILE A N     1 
ATOM   7793  C  CA    . ILE A 1 1198 ? 162.704 177.468 181.184 1.00 9.42   ? 2415 ILE A CA    1 
ATOM   7794  C  C     . ILE A 1 1198 ? 163.636 177.018 182.299 1.00 12.19  ? 2415 ILE A C     1 
ATOM   7795  O  O     . ILE A 1 1198 ? 164.760 177.522 182.416 1.00 14.34  ? 2415 ILE A O     1 
ATOM   7796  C  CB    . ILE A 1 1198 ? 163.227 177.040 179.805 1.00 9.34   ? 2415 ILE A CB    1 
ATOM   7797  C  CG1   . ILE A 1 1198 ? 162.097 177.089 178.778 1.00 9.35   ? 2415 ILE A CG1   1 
ATOM   7798  C  CG2   . ILE A 1 1198 ? 163.788 175.638 179.862 1.00 11.27  ? 2415 ILE A CG2   1 
ATOM   7799  C  CD1   . ILE A 1 1198 ? 162.522 176.701 177.385 1.00 10.29  ? 2415 ILE A CD1   1 
ATOM   7800  N  N     . LEU A 1 1199 ? 163.165 176.082 183.123 1.00 12.12  ? 2416 LEU A N     1 
ATOM   7801  C  CA    . LEU A 1 1199 ? 163.901 175.606 184.295 1.00 10.87  ? 2416 LEU A CA    1 
ATOM   7802  C  C     . LEU A 1 1199 ? 164.474 174.228 183.977 1.00 14.86  ? 2416 LEU A C     1 
ATOM   7803  O  O     . LEU A 1 1199 ? 163.876 173.201 184.291 1.00 20.87  ? 2416 LEU A O     1 
ATOM   7804  C  CB    . LEU A 1 1199 ? 162.993 175.559 185.519 1.00 9.20   ? 2416 LEU A CB    1 
ATOM   7805  C  CG    . LEU A 1 1199 ? 162.223 176.817 185.922 1.00 9.12   ? 2416 LEU A CG    1 
ATOM   7806  C  CD1   . LEU A 1 1199 ? 161.079 176.456 186.848 1.00 11.07  ? 2416 LEU A CD1   1 
ATOM   7807  C  CD2   . LEU A 1 1199 ? 163.136 177.826 186.587 1.00 10.80  ? 2416 LEU A CD2   1 
ATOM   7808  N  N     . CYS A 1 1200 ? 165.650 174.204 183.359 1.00 14.85  ? 2417 CYS A N     1 
ATOM   7809  C  CA    . CYS A 1 1200 ? 166.315 172.952 183.027 1.00 16.33  ? 2417 CYS A CA    1 
ATOM   7810  C  C     . CYS A 1 1200 ? 167.154 172.485 184.208 1.00 20.41  ? 2417 CYS A C     1 
ATOM   7811  O  O     . CYS A 1 1200 ? 167.901 173.272 184.795 1.00 24.46  ? 2417 CYS A O     1 
ATOM   7812  C  CB    . CYS A 1 1200 ? 167.196 173.116 181.790 1.00 16.28  ? 2417 CYS A CB    1 
ATOM   7813  S  SG    . CYS A 1 1200 ? 167.849 171.564 181.141 1.00 32.35  ? 2417 CYS A SG    1 
ATOM   7814  N  N     . GLY A 1 1201 ? 167.032 171.205 184.552 1.00 23.44  ? 2418 GLY A N     1 
ATOM   7815  C  CA    . GLY A 1 1201 ? 167.772 170.655 185.662 1.00 30.06  ? 2418 GLY A CA    1 
ATOM   7816  C  C     . GLY A 1 1201 ? 167.563 169.167 185.867 1.00 32.25  ? 2418 GLY A C     1 
ATOM   7817  O  O     . GLY A 1 1201 ? 166.610 168.568 185.357 1.00 34.36  ? 2418 GLY A O     1 
ATOM   7818  N  N     . PRO A 1 1202 ? 168.456 168.546 186.633 1.00 24.91  ? 2419 PRO A N     1 
ATOM   7819  C  CA    . PRO A 1 1202 ? 168.369 167.102 186.882 1.00 25.83  ? 2419 PRO A CA    1 
ATOM   7820  C  C     . PRO A 1 1202 ? 167.168 166.765 187.748 1.00 27.66  ? 2419 PRO A C     1 
ATOM   7821  O  O     . PRO A 1 1202 ? 166.575 167.662 188.365 1.00 28.66  ? 2419 PRO A O     1 
ATOM   7822  C  CB    . PRO A 1 1202 ? 169.687 166.794 187.609 1.00 28.56  ? 2419 PRO A CB    1 
ATOM   7823  C  CG    . PRO A 1 1202 ? 170.112 168.094 188.189 1.00 27.18  ? 2419 PRO A CG    1 
ATOM   7824  C  CD    . PRO A 1 1202 ? 169.673 169.133 187.216 1.00 23.17  ? 2419 PRO A CD    1 
ATOM   7825  N  N     . PRO A 1 1203 ? 166.760 165.494 187.795 1.00 28.15  ? 2420 PRO A N     1 
ATOM   7826  C  CA    . PRO A 1 1203 ? 165.639 165.109 188.665 1.00 29.39  ? 2420 PRO A CA    1 
ATOM   7827  C  C     . PRO A 1 1203 ? 165.943 165.368 190.133 1.00 30.99  ? 2420 PRO A C     1 
ATOM   7828  O  O     . PRO A 1 1203 ? 167.022 165.040 190.631 1.00 30.53  ? 2420 PRO A O     1 
ATOM   7829  C  CB    . PRO A 1 1203 ? 165.473 163.612 188.383 1.00 31.05  ? 2420 PRO A CB    1 
ATOM   7830  C  CG    . PRO A 1 1203 ? 166.069 163.407 187.045 1.00 33.82  ? 2420 PRO A CG    1 
ATOM   7831  C  CD    . PRO A 1 1203 ? 167.201 164.375 186.945 1.00 29.79  ? 2420 PRO A CD    1 
ATOM   7832  N  N     . GLY A 1 1204 ? 164.972 165.953 190.828 1.00 30.13  ? 2421 GLY A N     1 
ATOM   7833  C  CA    . GLY A 1 1204 ? 165.129 166.273 192.230 1.00 28.20  ? 2421 GLY A CA    1 
ATOM   7834  C  C     . GLY A 1 1204 ? 165.980 167.486 192.522 1.00 27.50  ? 2421 GLY A C     1 
ATOM   7835  O  O     . GLY A 1 1204 ? 166.376 167.680 193.676 1.00 30.82  ? 2421 GLY A O     1 
ATOM   7836  N  N     . SER A 1 1205 ? 166.274 168.311 191.518 1.00 24.91  ? 2422 SER A N     1 
ATOM   7837  C  CA    . SER A 1 1205 ? 167.099 169.492 191.730 1.00 22.48  ? 2422 SER A CA    1 
ATOM   7838  C  C     . SER A 1 1205 ? 166.339 170.636 192.380 1.00 22.57  ? 2422 SER A C     1 
ATOM   7839  O  O     . SER A 1 1205 ? 166.969 171.575 192.877 1.00 24.73  ? 2422 SER A O     1 
ATOM   7840  C  CB    . SER A 1 1205 ? 167.685 169.971 190.405 1.00 24.23  ? 2422 SER A CB    1 
ATOM   7841  O  OG    . SER A 1 1205 ? 168.089 171.324 190.501 1.00 22.51  ? 2422 SER A OG    1 
ATOM   7842  N  N     . GLY A 1 1206 ? 165.012 170.586 192.385 1.00 24.06  ? 2423 GLY A N     1 
ATOM   7843  C  CA    . GLY A 1 1206 ? 164.228 171.667 192.944 1.00 22.27  ? 2423 GLY A CA    1 
ATOM   7844  C  C     . GLY A 1 1206 ? 163.602 172.546 191.883 1.00 20.87  ? 2423 GLY A C     1 
ATOM   7845  O  O     . GLY A 1 1206 ? 163.608 173.771 192.007 1.00 23.37  ? 2423 GLY A O     1 
ATOM   7846  N  N     . LYS A 1 1207 ? 163.072 171.938 190.824 1.00 18.82  ? 2424 LYS A N     1 
ATOM   7847  C  CA    . LYS A 1 1207 ? 162.441 172.720 189.767 1.00 16.69  ? 2424 LYS A CA    1 
ATOM   7848  C  C     . LYS A 1 1207 ? 160.991 173.036 190.116 1.00 17.54  ? 2424 LYS A C     1 
ATOM   7849  O  O     . LYS A 1 1207 ? 160.609 174.207 190.225 1.00 20.45  ? 2424 LYS A O     1 
ATOM   7850  C  CB    . LYS A 1 1207 ? 162.539 171.970 188.438 1.00 15.96  ? 2424 LYS A CB    1 
ATOM   7851  C  CG    . LYS A 1 1207 ? 163.963 171.589 188.071 1.00 19.12  ? 2424 LYS A CG    1 
ATOM   7852  C  CD    . LYS A 1 1207 ? 164.043 170.988 186.683 1.00 18.42  ? 2424 LYS A CD    1 
ATOM   7853  C  CE    . LYS A 1 1207 ? 163.566 169.550 186.672 1.00 22.60  ? 2424 LYS A CE    1 
ATOM   7854  N  NZ    . LYS A 1 1207 ? 164.642 168.624 187.107 1.00 26.87  ? 2424 LYS A NZ    1 
ATOM   7855  N  N     . THR A 1 1208 ? 160.177 171.996 190.314 1.00 16.19  ? 2425 THR A N     1 
ATOM   7856  C  CA    . THR A 1 1208 ? 158.804 172.198 190.766 1.00 14.69  ? 2425 THR A CA    1 
ATOM   7857  C  C     . THR A 1 1208 ? 158.771 172.857 192.139 1.00 16.85  ? 2425 THR A C     1 
ATOM   7858  O  O     . THR A 1 1208 ? 157.895 173.685 192.420 1.00 21.00  ? 2425 THR A O     1 
ATOM   7859  C  CB    . THR A 1 1208 ? 158.059 170.861 190.796 1.00 14.62  ? 2425 THR A CB    1 
ATOM   7860  O  OG1   . THR A 1 1208 ? 158.140 170.238 189.508 1.00 15.96  ? 2425 THR A OG1   1 
ATOM   7861  C  CG2   . THR A 1 1208 ? 156.597 171.059 191.158 1.00 13.64  ? 2425 THR A CG2   1 
ATOM   7862  N  N     . MET A 1 1209 ? 159.736 172.522 192.998 1.00 18.28  ? 2426 MET A N     1 
ATOM   7863  C  CA    . MET A 1 1209 ? 159.735 173.046 194.359 1.00 19.36  ? 2426 MET A CA    1 
ATOM   7864  C  C     . MET A 1 1209 ? 159.957 174.556 194.367 1.00 21.85  ? 2426 MET A C     1 
ATOM   7865  O  O     . MET A 1 1209 ? 159.168 175.304 194.956 1.00 22.21  ? 2426 MET A O     1 
ATOM   7866  C  CB    . MET A 1 1209 ? 160.803 172.327 195.186 1.00 21.61  ? 2426 MET A CB    1 
ATOM   7867  C  CG    . MET A 1 1209 ? 160.793 172.662 196.659 1.00 28.57  ? 2426 MET A CG    1 
ATOM   7868  S  SD    . MET A 1 1209 ? 159.233 172.133 197.389 1.00 48.79  ? 2426 MET A SD    1 
ATOM   7869  C  CE    . MET A 1 1209 ? 159.418 170.361 197.382 1.00 32.63  ? 2426 MET A CE    1 
ATOM   7870  N  N     . ILE A 1 1210 ? 161.008 175.024 193.687 1.00 21.52  ? 2427 ILE A N     1 
ATOM   7871  C  CA    . ILE A 1 1210 ? 161.280 176.459 193.626 1.00 18.49  ? 2427 ILE A CA    1 
ATOM   7872  C  C     . ILE A 1 1210 ? 160.204 177.173 192.817 1.00 20.74  ? 2427 ILE A C     1 
ATOM   7873  O  O     . ILE A 1 1210 ? 159.811 178.297 193.147 1.00 30.65  ? 2427 ILE A O     1 
ATOM   7874  C  CB    . ILE A 1 1210 ? 162.693 176.716 193.069 1.00 17.63  ? 2427 ILE A CB    1 
ATOM   7875  C  CG1   . ILE A 1 1210 ? 163.747 176.233 194.064 1.00 24.87  ? 2427 ILE A CG1   1 
ATOM   7876  C  CG2   . ILE A 1 1210 ? 162.921 178.189 192.784 1.00 20.34  ? 2427 ILE A CG2   1 
ATOM   7877  C  CD1   . ILE A 1 1210 ? 165.159 176.298 193.532 1.00 22.10  ? 2427 ILE A CD1   1 
ATOM   7878  N  N     . MET A 1 1211 ? 159.698 176.528 191.761 1.00 18.62  ? 2428 MET A N     1 
ATOM   7879  C  CA    . MET A 1 1211 ? 158.552 177.040 191.010 1.00 19.61  ? 2428 MET A CA    1 
ATOM   7880  C  C     . MET A 1 1211 ? 157.363 177.391 191.900 1.00 20.94  ? 2428 MET A C     1 
ATOM   7881  O  O     . MET A 1 1211 ? 156.921 178.549 191.954 1.00 26.01  ? 2428 MET A O     1 
ATOM   7882  C  CB    . MET A 1 1211 ? 158.134 176.005 189.970 1.00 20.25  ? 2428 MET A CB    1 
ATOM   7883  C  CG    . MET A 1 1211 ? 156.992 176.464 189.111 1.00 20.11  ? 2428 MET A CG    1 
ATOM   7884  S  SD    . MET A 1 1211 ? 157.337 177.864 188.063 1.00 28.88  ? 2428 MET A SD    1 
ATOM   7885  C  CE    . MET A 1 1211 ? 155.670 178.472 187.879 1.00 17.89  ? 2428 MET A CE    1 
ATOM   7886  N  N     . ASN A 1 1212 ? 156.813 176.390 192.586 1.00 19.52  ? 2429 ASN A N     1 
ATOM   7887  C  CA    . ASN A 1 1212 ? 155.615 176.630 193.374 1.00 22.25  ? 2429 ASN A CA    1 
ATOM   7888  C  C     . ASN A 1 1212 ? 155.913 177.408 194.647 1.00 27.63  ? 2429 ASN A C     1 
ATOM   7889  O  O     . ASN A 1 1212 ? 155.001 178.031 195.198 1.00 30.83  ? 2429 ASN A O     1 
ATOM   7890  C  CB    . ASN A 1 1212 ? 154.921 175.308 193.687 1.00 22.88  ? 2429 ASN A CB    1 
ATOM   7891  C  CG    . ASN A 1 1212 ? 154.040 174.838 192.548 1.00 21.43  ? 2429 ASN A CG    1 
ATOM   7892  O  OD1   . ASN A 1 1212 ? 154.200 175.277 191.410 1.00 17.52  ? 2429 ASN A OD1   1 
ATOM   7893  N  ND2   . ASN A 1 1212 ? 153.105 173.946 192.847 1.00 26.03  ? 2429 ASN A ND2   1 
ATOM   7894  N  N     . ASN A 1 1213 ? 157.164 177.414 195.116 1.00 28.21  ? 2430 ASN A N     1 
ATOM   7895  C  CA    . ASN A 1 1213 ? 157.536 178.333 196.184 1.00 28.21  ? 2430 ASN A CA    1 
ATOM   7896  C  C     . ASN A 1 1213 ? 157.508 179.775 195.700 1.00 29.31  ? 2430 ASN A C     1 
ATOM   7897  O  O     . ASN A 1 1213 ? 157.112 180.680 196.443 1.00 35.53  ? 2430 ASN A O     1 
ATOM   7898  C  CB    . ASN A 1 1213 ? 158.919 177.978 196.724 1.00 27.76  ? 2430 ASN A CB    1 
ATOM   7899  C  CG    . ASN A 1 1213 ? 159.356 178.891 197.850 1.00 32.78  ? 2430 ASN A CG    1 
ATOM   7900  O  OD1   . ASN A 1 1213 ? 160.395 179.543 197.767 1.00 33.09  ? 2430 ASN A OD1   1 
ATOM   7901  N  ND2   . ASN A 1 1213 ? 158.558 178.949 198.907 1.00 37.62  ? 2430 ASN A ND2   1 
ATOM   7902  N  N     . ALA A 1 1214 ? 157.930 180.007 194.457 1.00 25.81  ? 2431 ALA A N     1 
ATOM   7903  C  CA    . ALA A 1 1214 ? 157.983 181.363 193.931 1.00 24.79  ? 2431 ALA A CA    1 
ATOM   7904  C  C     . ALA A 1 1214 ? 156.588 181.897 193.648 1.00 28.99  ? 2431 ALA A C     1 
ATOM   7905  O  O     . ALA A 1 1214 ? 156.274 183.044 193.981 1.00 33.73  ? 2431 ALA A O     1 
ATOM   7906  C  CB    . ALA A 1 1214 ? 158.844 181.399 192.671 1.00 22.60  ? 2431 ALA A CB    1 
ATOM   7907  N  N     . LEU A 1 1215 ? 155.730 181.082 193.043 1.00 26.49  ? 2432 LEU A N     1 
ATOM   7908  C  CA    . LEU A 1 1215 ? 154.373 181.524 192.731 1.00 27.60  ? 2432 LEU A CA    1 
ATOM   7909  C  C     . LEU A 1 1215 ? 153.319 180.790 193.554 1.00 29.77  ? 2432 LEU A C     1 
ATOM   7910  O  O     . LEU A 1 1215 ? 152.241 180.447 193.068 1.00 24.36  ? 2432 LEU A O     1 
ATOM   7911  C  CB    . LEU A 1 1215 ? 154.088 181.419 191.239 1.00 19.71  ? 2432 LEU A CB    1 
ATOM   7912  C  CG    . LEU A 1 1215 ? 155.173 182.072 190.390 1.00 22.19  ? 2432 LEU A CG    1 
ATOM   7913  C  CD1   . LEU A 1 1215 ? 154.935 181.820 188.925 1.00 21.98  ? 2432 LEU A CD1   1 
ATOM   7914  C  CD2   . LEU A 1 1215 ? 155.214 183.563 190.679 1.00 22.27  ? 2432 LEU A CD2   1 
ATOM   7915  N  N     . ARG A 1 1216 ? 153.641 180.546 194.817 1.00 32.55  ? 2433 ARG A N     1 
ATOM   7916  C  CA    . ARG A 1 1216 ? 152.665 180.287 195.862 1.00 34.49  ? 2433 ARG A CA    1 
ATOM   7917  C  C     . ARG A 1 1216 ? 152.708 181.343 196.953 1.00 33.85  ? 2433 ARG A C     1 
ATOM   7918  O  O     . ARG A 1 1216 ? 151.678 181.624 197.571 1.00 34.65  ? 2433 ARG A O     1 
ATOM   7919  C  CB    . ARG A 1 1216 ? 152.902 178.895 196.473 1.00 36.74  ? 2433 ARG A CB    1 
ATOM   7920  C  CG    . ARG A 1 1216 ? 151.921 178.470 197.557 1.00 38.82  ? 2433 ARG A CG    1 
ATOM   7921  C  CD    . ARG A 1 1216 ? 152.357 177.162 198.203 1.00 43.14  ? 2433 ARG A CD    1 
ATOM   7922  N  NE    . ARG A 1 1216 ? 153.472 177.351 199.125 1.00 50.18  ? 2433 ARG A NE    1 
ATOM   7923  C  CZ    . ARG A 1 1216 ? 154.734 177.057 198.843 1.00 42.00  ? 2433 ARG A CZ    1 
ATOM   7924  N  NH1   . ARG A 1 1216 ? 155.078 176.535 197.678 1.00 38.63  ? 2433 ARG A NH1   1 
ATOM   7925  N  NH2   . ARG A 1 1216 ? 155.673 177.291 199.755 1.00 39.57  ? 2433 ARG A NH2   1 
ATOM   7926  N  N     . ASN A 1 1217 ? 153.867 181.961 197.171 1.00 31.73  ? 2434 ASN A N     1 
ATOM   7927  C  CA    . ASN A 1 1217 ? 154.031 183.063 198.105 1.00 32.91  ? 2434 ASN A CA    1 
ATOM   7928  C  C     . ASN A 1 1217 ? 153.813 184.422 197.456 1.00 36.33  ? 2434 ASN A C     1 
ATOM   7929  O  O     . ASN A 1 1217 ? 153.999 185.447 198.120 1.00 39.43  ? 2434 ASN A O     1 
ATOM   7930  C  CB    . ASN A 1 1217 ? 155.428 183.017 198.730 1.00 32.67  ? 2434 ASN A CB    1 
ATOM   7931  C  CG    . ASN A 1 1217 ? 155.645 181.781 199.574 1.00 38.85  ? 2434 ASN A CG    1 
ATOM   7932  O  OD1   . ASN A 1 1217 ? 155.014 180.748 199.354 1.00 39.16  ? 2434 ASN A OD1   1 
ATOM   7933  N  ND2   . ASN A 1 1217 ? 156.539 181.881 200.550 1.00 42.20  ? 2434 ASN A ND2   1 
ATOM   7934  N  N     . SER A 1 1218 ? 153.434 184.457 196.181 1.00 34.42  ? 2435 SER A N     1 
ATOM   7935  C  CA    . SER A 1 1218 ? 153.224 185.701 195.456 1.00 34.56  ? 2435 SER A CA    1 
ATOM   7936  C  C     . SER A 1 1218 ? 151.741 186.034 195.387 1.00 32.49  ? 2435 SER A C     1 
ATOM   7937  O  O     . SER A 1 1218 ? 150.903 185.154 195.166 1.00 28.64  ? 2435 SER A O     1 
ATOM   7938  C  CB    . SER A 1 1218 ? 153.795 185.613 194.040 1.00 32.25  ? 2435 SER A CB    1 
ATOM   7939  O  OG    . SER A 1 1218 ? 153.672 186.854 193.370 1.00 33.60  ? 2435 SER A OG    1 
ATOM   7940  N  N     . SER A 1 1219 ? 151.424 187.312 195.580 1.00 33.65  ? 2436 SER A N     1 
ATOM   7941  C  CA    . SER A 1 1219 ? 150.060 187.808 195.474 1.00 32.34  ? 2436 SER A CA    1 
ATOM   7942  C  C     . SER A 1 1219 ? 149.768 188.442 194.121 1.00 32.38  ? 2436 SER A C     1 
ATOM   7943  O  O     . SER A 1 1219 ? 148.667 188.962 193.921 1.00 33.38  ? 2436 SER A O     1 
ATOM   7944  C  CB    . SER A 1 1219 ? 149.780 188.821 196.588 1.00 30.68  ? 2436 SER A CB    1 
ATOM   7945  O  OG    . SER A 1 1219 ? 150.497 190.024 196.373 1.00 27.52  ? 2436 SER A OG    1 
ATOM   7946  N  N     . LEU A 1 1220 ? 150.721 188.410 193.190 1.00 29.59  ? 2437 LEU A N     1 
ATOM   7947  C  CA    . LEU A 1 1220 ? 150.549 189.027 191.884 1.00 25.21  ? 2437 LEU A CA    1 
ATOM   7948  C  C     . LEU A 1 1220 ? 150.499 188.011 190.748 1.00 25.29  ? 2437 LEU A C     1 
ATOM   7949  O  O     . LEU A 1 1220 ? 150.126 188.375 189.628 1.00 26.12  ? 2437 LEU A O     1 
ATOM   7950  C  CB    . LEU A 1 1220 ? 151.680 190.044 191.644 1.00 25.89  ? 2437 LEU A CB    1 
ATOM   7951  C  CG    . LEU A 1 1220 ? 151.752 190.950 190.409 1.00 31.02  ? 2437 LEU A CG    1 
ATOM   7952  C  CD1   . LEU A 1 1220 ? 150.391 191.547 190.086 1.00 31.98  ? 2437 LEU A CD1   1 
ATOM   7953  C  CD2   . LEU A 1 1220 ? 152.782 192.050 190.612 1.00 32.60  ? 2437 LEU A CD2   1 
ATOM   7954  N  N     . TYR A 1 1221 ? 150.831 186.746 191.002 1.00 24.05  ? 2438 TYR A N     1 
ATOM   7955  C  CA    . TYR A 1 1221 ? 150.777 185.723 189.967 1.00 18.32  ? 2438 TYR A CA    1 
ATOM   7956  C  C     . TYR A 1 1221 ? 150.151 184.453 190.526 1.00 17.23  ? 2438 TYR A C     1 
ATOM   7957  O  O     . TYR A 1 1221 ? 150.197 184.199 191.731 1.00 21.24  ? 2438 TYR A O     1 
ATOM   7958  C  CB    . TYR A 1 1221 ? 152.168 185.418 189.400 1.00 19.46  ? 2438 TYR A CB    1 
ATOM   7959  C  CG    . TYR A 1 1221 ? 152.854 186.608 188.762 1.00 23.12  ? 2438 TYR A CG    1 
ATOM   7960  C  CD1   . TYR A 1 1221 ? 153.635 187.471 189.517 1.00 23.75  ? 2438 TYR A CD1   1 
ATOM   7961  C  CD2   . TYR A 1 1221 ? 152.721 186.866 187.405 1.00 22.36  ? 2438 TYR A CD2   1 
ATOM   7962  C  CE1   . TYR A 1 1221 ? 154.264 188.558 188.941 1.00 18.86  ? 2438 TYR A CE1   1 
ATOM   7963  C  CE2   . TYR A 1 1221 ? 153.349 187.951 186.819 1.00 19.08  ? 2438 TYR A CE2   1 
ATOM   7964  C  CZ    . TYR A 1 1221 ? 154.117 188.792 187.593 1.00 18.86  ? 2438 TYR A CZ    1 
ATOM   7965  O  OH    . TYR A 1 1221 ? 154.743 189.874 187.020 1.00 20.16  ? 2438 TYR A OH    1 
ATOM   7966  N  N     . ASP A 1 1222 ? 149.563 183.658 189.632 1.00 15.24  ? 2439 ASP A N     1 
ATOM   7967  C  CA    . ASP A 1 1222 ? 148.964 182.377 189.983 1.00 15.74  ? 2439 ASP A CA    1 
ATOM   7968  C  C     . ASP A 1 1222 ? 149.433 181.309 189.006 1.00 17.86  ? 2439 ASP A C     1 
ATOM   7969  O  O     . ASP A 1 1222 ? 149.829 181.603 187.876 1.00 20.77  ? 2439 ASP A O     1 
ATOM   7970  C  CB    . ASP A 1 1222 ? 147.432 182.435 189.979 1.00 15.76  ? 2439 ASP A CB    1 
ATOM   7971  C  CG    . ASP A 1 1222 ? 146.882 183.354 191.042 1.00 24.11  ? 2439 ASP A CG    1 
ATOM   7972  O  OD1   . ASP A 1 1222 ? 147.404 183.331 192.176 1.00 25.15  ? 2439 ASP A OD1   1 
ATOM   7973  O  OD2   . ASP A 1 1222 ? 145.919 184.090 190.746 1.00 29.44  ? 2439 ASP A OD2   1 
ATOM   7974  N  N     . VAL A 1 1223 ? 149.371 180.057 189.450 1.00 15.81  ? 2440 VAL A N     1 
ATOM   7975  C  CA    . VAL A 1 1223 ? 149.901 178.922 188.704 1.00 14.99  ? 2440 VAL A CA    1 
ATOM   7976  C  C     . VAL A 1 1223 ? 148.747 178.101 188.151 1.00 15.85  ? 2440 VAL A C     1 
ATOM   7977  O  O     . VAL A 1 1223 ? 147.796 177.784 188.875 1.00 18.11  ? 2440 VAL A O     1 
ATOM   7978  C  CB    . VAL A 1 1223 ? 150.805 178.040 189.582 1.00 15.16  ? 2440 VAL A CB    1 
ATOM   7979  C  CG1   . VAL A 1 1223 ? 151.394 176.898 188.771 1.00 13.08  ? 2440 VAL A CG1   1 
ATOM   7980  C  CG2   . VAL A 1 1223 ? 151.901 178.858 190.192 1.00 14.96  ? 2440 VAL A CG2   1 
ATOM   7981  N  N     . VAL A 1 1224 ? 148.829 177.767 186.866 1.00 16.17  ? 2441 VAL A N     1 
ATOM   7982  C  CA    . VAL A 1 1224 ? 148.108 176.621 186.329 1.00 16.35  ? 2441 VAL A CA    1 
ATOM   7983  C  C     . VAL A 1 1224 ? 149.161 175.595 185.936 1.00 15.90  ? 2441 VAL A C     1 
ATOM   7984  O  O     . VAL A 1 1224 ? 149.654 175.596 184.804 1.00 17.20  ? 2441 VAL A O     1 
ATOM   7985  C  CB    . VAL A 1 1224 ? 147.220 177.004 185.134 1.00 18.63  ? 2441 VAL A CB    1 
ATOM   7986  C  CG1   . VAL A 1 1224 ? 146.304 175.851 184.771 1.00 27.34  ? 2441 VAL A CG1   1 
ATOM   7987  C  CG2   . VAL A 1 1224 ? 146.410 178.235 185.461 1.00 23.24  ? 2441 VAL A CG2   1 
ATOM   7988  N  N     . GLY A 1 1225 ? 149.511 174.715 186.870 1.00 16.15  ? 2442 GLY A N     1 
ATOM   7989  C  CA    . GLY A 1 1225 ? 150.604 173.789 186.639 1.00 13.95  ? 2442 GLY A CA    1 
ATOM   7990  C  C     . GLY A 1 1225 ? 150.162 172.606 185.797 1.00 14.05  ? 2442 GLY A C     1 
ATOM   7991  O  O     . GLY A 1 1225 ? 149.096 172.028 186.006 1.00 16.60  ? 2442 GLY A O     1 
ATOM   7992  N  N     . ILE A 1 1226 ? 151.000 172.252 184.827 1.00 13.51  ? 2443 ILE A N     1 
ATOM   7993  C  CA    . ILE A 1 1226 ? 150.746 171.126 183.939 1.00 15.13  ? 2443 ILE A CA    1 
ATOM   7994  C  C     . ILE A 1 1226 ? 151.977 170.233 183.925 1.00 17.14  ? 2443 ILE A C     1 
ATOM   7995  O  O     . ILE A 1 1226 ? 153.110 170.721 183.863 1.00 18.88  ? 2443 ILE A O     1 
ATOM   7996  C  CB    . ILE A 1 1226 ? 150.402 171.579 182.503 1.00 14.20  ? 2443 ILE A CB    1 
ATOM   7997  C  CG1   . ILE A 1 1226 ? 149.386 172.719 182.508 1.00 14.41  ? 2443 ILE A CG1   1 
ATOM   7998  C  CG2   . ILE A 1 1226 ? 149.836 170.424 181.707 1.00 17.20  ? 2443 ILE A CG2   1 
ATOM   7999  C  CD1   . ILE A 1 1226 ? 149.246 173.402 181.171 1.00 19.51  ? 2443 ILE A CD1   1 
ATOM   8000  N  N     . ASN A 1 1227 ? 151.754 168.925 183.998 1.00 16.83  ? 2444 ASN A N     1 
ATOM   8001  C  CA    . ASN A 1 1227 ? 152.782 167.929 183.737 1.00 21.38  ? 2444 ASN A CA    1 
ATOM   8002  C  C     . ASN A 1 1227 ? 152.497 167.310 182.378 1.00 22.70  ? 2444 ASN A C     1 
ATOM   8003  O  O     . ASN A 1 1227 ? 151.369 166.883 182.112 1.00 25.87  ? 2444 ASN A O     1 
ATOM   8004  C  CB    . ASN A 1 1227 ? 152.805 166.855 184.828 1.00 32.76  ? 2444 ASN A CB    1 
ATOM   8005  C  CG    . ASN A 1 1227 ? 154.073 166.015 184.803 1.00 36.57  ? 2444 ASN A CG    1 
ATOM   8006  O  OD1   . ASN A 1 1227 ? 154.471 165.491 183.762 1.00 29.33  ? 2444 ASN A OD1   1 
ATOM   8007  N  ND2   . ASN A 1 1227 ? 154.712 165.881 185.959 1.00 42.88  ? 2444 ASN A ND2   1 
ATOM   8008  N  N     . PHE A 1 1228 ? 153.509 167.265 181.524 1.00 23.10  ? 2445 PHE A N     1 
ATOM   8009  C  CA    . PHE A 1 1228 ? 153.338 166.785 180.163 1.00 27.13  ? 2445 PHE A CA    1 
ATOM   8010  C  C     . PHE A 1 1228 ? 153.702 165.309 180.058 1.00 34.62  ? 2445 PHE A C     1 
ATOM   8011  O  O     . PHE A 1 1228 ? 154.396 164.747 180.908 1.00 35.59  ? 2445 PHE A O     1 
ATOM   8012  C  CB    . PHE A 1 1228 ? 154.181 167.608 179.187 1.00 27.43  ? 2445 PHE A CB    1 
ATOM   8013  C  CG    . PHE A 1 1228 ? 153.563 168.925 178.816 1.00 26.12  ? 2445 PHE A CG    1 
ATOM   8014  C  CD1   . PHE A 1 1228 ? 152.213 169.155 179.017 1.00 24.49  ? 2445 PHE A CD1   1 
ATOM   8015  C  CD2   . PHE A 1 1228 ? 154.334 169.935 178.267 1.00 24.53  ? 2445 PHE A CD2   1 
ATOM   8016  C  CE1   . PHE A 1 1228 ? 151.645 170.365 178.674 1.00 20.73  ? 2445 PHE A CE1   1 
ATOM   8017  C  CE2   . PHE A 1 1228 ? 153.770 171.146 177.925 1.00 22.95  ? 2445 PHE A CE2   1 
ATOM   8018  C  CZ    . PHE A 1 1228 ? 152.425 171.362 178.131 1.00 18.04  ? 2445 PHE A CZ    1 
ATOM   8019  N  N     . SER A 1 1229 ? 153.214 164.688 178.987 1.00 38.86  ? 2446 SER A N     1 
ATOM   8020  C  CA    . SER A 1 1229 ? 153.366 163.262 178.745 1.00 43.61  ? 2446 SER A CA    1 
ATOM   8021  C  C     . SER A 1 1229 ? 153.697 163.051 177.274 1.00 43.89  ? 2446 SER A C     1 
ATOM   8022  O  O     . SER A 1 1229 ? 153.780 164.002 176.491 1.00 43.46  ? 2446 SER A O     1 
ATOM   8023  C  CB    . SER A 1 1229 ? 152.099 162.495 179.138 1.00 44.64  ? 2446 SER A CB    1 
ATOM   8024  O  OG    . SER A 1 1229 ? 150.981 162.913 178.377 1.00 43.73  ? 2446 SER A OG    1 
ATOM   8025  N  N     . LYS A 1 1230 ? 153.899 161.783 176.905 1.00 40.48  ? 2447 LYS A N     1 
ATOM   8026  C  CA    . LYS A 1 1230 ? 154.201 161.449 175.517 1.00 38.74  ? 2447 LYS A CA    1 
ATOM   8027  C  C     . LYS A 1 1230 ? 153.041 161.802 174.596 1.00 41.04  ? 2447 LYS A C     1 
ATOM   8028  O  O     . LYS A 1 1230 ? 153.246 162.353 173.508 1.00 42.88  ? 2447 LYS A O     1 
ATOM   8029  C  CB    . LYS A 1 1230 ? 154.542 159.964 175.402 1.00 40.76  ? 2447 LYS A CB    1 
ATOM   8030  C  CG    . LYS A 1 1230 ? 155.997 159.635 175.681 1.00 39.75  ? 2447 LYS A CG    1 
ATOM   8031  C  CD    . LYS A 1 1230 ? 156.920 160.421 174.771 1.00 41.79  ? 2447 LYS A CD    1 
ATOM   8032  C  CE    . LYS A 1 1230 ? 158.376 160.105 175.055 1.00 40.89  ? 2447 LYS A CE    1 
ATOM   8033  N  NZ    . LYS A 1 1230 ? 158.920 160.965 176.139 1.00 42.53  ? 2447 LYS A NZ    1 
ATOM   8034  N  N     . ASP A 1 1231 ? 151.816 161.496 175.014 1.00 42.15  ? 2448 ASP A N     1 
ATOM   8035  C  CA    . ASP A 1 1231 ? 150.620 161.768 174.218 1.00 44.81  ? 2448 ASP A CA    1 
ATOM   8036  C  C     . ASP A 1 1231 ? 149.930 162.997 174.801 1.00 43.60  ? 2448 ASP A C     1 
ATOM   8037  O  O     . ASP A 1 1231 ? 148.980 162.891 175.576 1.00 45.92  ? 2448 ASP A O     1 
ATOM   8038  C  CB    . ASP A 1 1231 ? 149.695 160.556 174.200 1.00 46.18  ? 2448 ASP A CB    1 
ATOM   8039  N  N     . THR A 1 1232 ? 150.413 164.175 174.415 1.00 42.56  ? 2449 THR A N     1 
ATOM   8040  C  CA    . THR A 1 1232 ? 149.817 165.441 174.815 1.00 43.48  ? 2449 THR A CA    1 
ATOM   8041  C  C     . THR A 1 1232 ? 149.302 166.178 173.591 1.00 44.87  ? 2449 THR A C     1 
ATOM   8042  O  O     . THR A 1 1232 ? 149.917 166.137 172.521 1.00 44.96  ? 2449 THR A O     1 
ATOM   8043  C  CB    . THR A 1 1232 ? 150.813 166.329 175.568 1.00 40.00  ? 2449 THR A CB    1 
ATOM   8044  O  OG1   . THR A 1 1232 ? 152.091 166.285 174.921 1.00 46.47  ? 2449 THR A OG1   1 
ATOM   8045  C  CG2   . THR A 1 1232 ? 150.940 165.886 177.004 1.00 36.21  ? 2449 THR A CG2   1 
ATOM   8046  N  N     . THR A 1 1233 ? 148.170 166.852 173.758 1.00 44.70  ? 2450 THR A N     1 
ATOM   8047  C  CA    . THR A 1 1233 ? 147.518 167.582 172.687 1.00 43.69  ? 2450 THR A CA    1 
ATOM   8048  C  C     . THR A 1 1233 ? 147.349 169.043 173.081 1.00 37.98  ? 2450 THR A C     1 
ATOM   8049  O  O     . THR A 1 1233 ? 147.603 169.443 174.220 1.00 37.29  ? 2450 THR A O     1 
ATOM   8050  C  CB    . THR A 1 1233 ? 146.152 166.971 172.350 1.00 46.63  ? 2450 THR A CB    1 
ATOM   8051  O  OG1   . THR A 1 1233 ? 145.300 167.041 173.500 1.00 45.34  ? 2450 THR A OG1   1 
ATOM   8052  C  CG2   . THR A 1 1233 ? 146.300 165.519 171.920 1.00 45.59  ? 2450 THR A CG2   1 
ATOM   8053  N  N     . THR A 1 1234 ? 146.917 169.841 172.103 1.00 37.92  ? 2451 THR A N     1 
ATOM   8054  C  CA    . THR A 1 1234 ? 146.616 171.245 172.355 1.00 38.58  ? 2451 THR A CA    1 
ATOM   8055  C  C     . THR A 1 1234 ? 145.429 171.404 173.295 1.00 43.08  ? 2451 THR A C     1 
ATOM   8056  O  O     . THR A 1 1234 ? 145.406 172.329 174.114 1.00 48.59  ? 2451 THR A O     1 
ATOM   8057  C  CB    . THR A 1 1234 ? 146.346 171.959 171.030 1.00 32.23  ? 2451 THR A CB    1 
ATOM   8058  O  OG1   . THR A 1 1234 ? 147.387 171.647 170.095 1.00 32.73  ? 2451 THR A OG1   1 
ATOM   8059  C  CG2   . THR A 1 1234 ? 146.274 173.460 171.224 1.00 24.91  ? 2451 THR A CG2   1 
ATOM   8060  N  N     . GLU A 1 1235 ? 144.446 170.505 173.204 1.00 40.90  ? 2452 GLU A N     1 
ATOM   8061  C  CA    . GLU A 1 1235 ? 143.245 170.614 174.022 1.00 42.53  ? 2452 GLU A CA    1 
ATOM   8062  C  C     . GLU A 1 1235 ? 143.513 170.347 175.497 1.00 46.79  ? 2452 GLU A C     1 
ATOM   8063  O  O     . GLU A 1 1235 ? 142.703 170.750 176.338 1.00 49.16  ? 2452 GLU A O     1 
ATOM   8064  C  CB    . GLU A 1 1235 ? 142.165 169.663 173.500 1.00 41.02  ? 2452 GLU A CB    1 
ATOM   8065  C  CG    . GLU A 1 1235 ? 141.685 169.965 172.080 1.00 45.43  ? 2452 GLU A CG    1 
ATOM   8066  C  CD    . GLU A 1 1235 ? 142.583 169.389 170.998 1.00 42.95  ? 2452 GLU A CD    1 
ATOM   8067  O  OE1   . GLU A 1 1235 ? 143.614 168.773 171.336 1.00 41.46  ? 2452 GLU A OE1   1 
ATOM   8068  O  OE2   . GLU A 1 1235 ? 142.260 169.559 169.804 1.00 41.01  ? 2452 GLU A OE2   1 
ATOM   8069  N  N     . HIS A 1 1236 ? 144.618 169.676 175.831 1.00 46.18  ? 2453 HIS A N     1 
ATOM   8070  C  CA    . HIS A 1 1236 ? 144.992 169.521 177.235 1.00 47.93  ? 2453 HIS A CA    1 
ATOM   8071  C  C     . HIS A 1 1236 ? 145.299 170.871 177.873 1.00 48.20  ? 2453 HIS A C     1 
ATOM   8072  O  O     . HIS A 1 1236 ? 144.873 171.146 179.001 1.00 51.37  ? 2453 HIS A O     1 
ATOM   8073  C  CB    . HIS A 1 1236 ? 146.196 168.588 177.362 1.00 47.53  ? 2453 HIS A CB    1 
ATOM   8074  C  CG    . HIS A 1 1236 ? 145.881 167.150 177.091 1.00 48.02  ? 2453 HIS A CG    1 
ATOM   8075  N  ND1   . HIS A 1 1236 ? 146.858 166.186 176.967 1.00 47.19  ? 2453 HIS A ND1   1 
ATOM   8076  C  CD2   . HIS A 1 1236 ? 144.699 166.512 176.922 1.00 48.94  ? 2453 HIS A CD2   1 
ATOM   8077  C  CE1   . HIS A 1 1236 ? 146.291 165.016 176.732 1.00 45.95  ? 2453 HIS A CE1   1 
ATOM   8078  N  NE2   . HIS A 1 1236 ? 144.982 165.186 176.700 1.00 48.75  ? 2453 HIS A NE2   1 
ATOM   8079  N  N     . ILE A 1 1237 ? 146.034 171.727 177.160 1.00 41.69  ? 2454 ILE A N     1 
ATOM   8080  C  CA    . ILE A 1 1237 ? 146.368 173.048 177.681 1.00 39.42  ? 2454 ILE A CA    1 
ATOM   8081  C  C     . ILE A 1 1237 ? 145.113 173.896 177.839 1.00 46.39  ? 2454 ILE A C     1 
ATOM   8082  O  O     . ILE A 1 1237 ? 144.956 174.620 178.829 1.00 50.28  ? 2454 ILE A O     1 
ATOM   8083  C  CB    . ILE A 1 1237 ? 147.405 173.725 176.768 1.00 34.63  ? 2454 ILE A CB    1 
ATOM   8084  C  CG1   . ILE A 1 1237 ? 148.642 172.839 176.625 1.00 31.59  ? 2454 ILE A CG1   1 
ATOM   8085  C  CG2   . ILE A 1 1237 ? 147.793 175.085 177.314 1.00 35.35  ? 2454 ILE A CG2   1 
ATOM   8086  C  CD1   . ILE A 1 1237 ? 149.763 173.481 175.845 1.00 25.09  ? 2454 ILE A CD1   1 
ATOM   8087  N  N     . LEU A 1 1238 ? 144.193 173.814 176.875 1.00 48.83  ? 2455 LEU A N     1 
ATOM   8088  C  CA    . LEU A 1 1238 ? 142.951 174.577 176.974 1.00 53.89  ? 2455 LEU A CA    1 
ATOM   8089  C  C     . LEU A 1 1238 ? 142.074 174.059 178.108 1.00 56.41  ? 2455 LEU A C     1 
ATOM   8090  O  O     . LEU A 1 1238 ? 141.392 174.843 178.780 1.00 56.15  ? 2455 LEU A O     1 
ATOM   8091  C  CB    . LEU A 1 1238 ? 142.192 174.536 175.647 1.00 49.85  ? 2455 LEU A CB    1 
ATOM   8092  C  CG    . LEU A 1 1238 ? 142.561 175.549 174.558 1.00 48.79  ? 2455 LEU A CG    1 
ATOM   8093  C  CD1   . LEU A 1 1238 ? 142.350 176.969 175.062 1.00 49.46  ? 2455 LEU A CD1   1 
ATOM   8094  C  CD2   . LEU A 1 1238 ? 143.972 175.357 174.022 1.00 34.58  ? 2455 LEU A CD2   1 
ATOM   8095  N  N     . SER A 1 1239 ? 142.076 172.744 178.334 1.00 54.45  ? 2456 SER A N     1 
ATOM   8096  C  CA    . SER A 1 1239 ? 141.355 172.188 179.474 1.00 56.44  ? 2456 SER A CA    1 
ATOM   8097  C  C     . SER A 1 1239 ? 141.966 172.653 180.790 1.00 57.74  ? 2456 SER A C     1 
ATOM   8098  O  O     . SER A 1 1239 ? 141.243 172.903 181.761 1.00 62.62  ? 2456 SER A O     1 
ATOM   8099  C  CB    . SER A 1 1239 ? 141.344 170.662 179.392 1.00 57.50  ? 2456 SER A CB    1 
ATOM   8100  O  OG    . SER A 1 1239 ? 142.650 170.133 179.540 1.00 53.58  ? 2456 SER A OG    1 
ATOM   8101  N  N     . ALA A 1 1240 ? 143.297 172.756 180.844 1.00 52.24  ? 2457 ALA A N     1 
ATOM   8102  C  CA    . ALA A 1 1240 ? 143.952 173.286 182.036 1.00 50.03  ? 2457 ALA A CA    1 
ATOM   8103  C  C     . ALA A 1 1240 ? 143.595 174.751 182.257 1.00 54.29  ? 2457 ALA A C     1 
ATOM   8104  O  O     . ALA A 1 1240 ? 143.386 175.183 183.397 1.00 55.79  ? 2457 ALA A O     1 
ATOM   8105  C  CB    . ALA A 1 1240 ? 145.466 173.113 181.926 1.00 44.64  ? 2457 ALA A CB    1 
ATOM   8106  N  N     . LEU A 1 1241 ? 143.513 175.529 181.179 1.00 52.63  ? 2458 LEU A N     1 
ATOM   8107  C  CA    . LEU A 1 1241 ? 143.140 176.935 181.277 1.00 52.76  ? 2458 LEU A CA    1 
ATOM   8108  C  C     . LEU A 1 1241 ? 141.640 177.149 181.426 1.00 56.72  ? 2458 LEU A C     1 
ATOM   8109  O  O     . LEU A 1 1241 ? 141.217 178.296 181.603 1.00 56.24  ? 2458 LEU A O     1 
ATOM   8110  C  CB    . LEU A 1 1241 ? 143.628 177.709 180.050 1.00 51.36  ? 2458 LEU A CB    1 
ATOM   8111  C  CG    . LEU A 1 1241 ? 145.131 177.815 179.799 1.00 47.86  ? 2458 LEU A CG    1 
ATOM   8112  C  CD1   . LEU A 1 1241 ? 145.419 177.833 178.306 1.00 42.18  ? 2458 LEU A CD1   1 
ATOM   8113  C  CD2   . LEU A 1 1241 ? 145.692 179.057 180.468 1.00 47.59  ? 2458 LEU A CD2   1 
ATOM   8114  N  N     . HIS A 1 1242 ? 140.833 176.087 181.342 1.00 60.12  ? 2459 HIS A N     1 
ATOM   8115  C  CA    . HIS A 1 1242 ? 139.380 176.245 181.347 1.00 66.42  ? 2459 HIS A CA    1 
ATOM   8116  C  C     . HIS A 1 1242 ? 138.883 176.815 182.672 1.00 66.73  ? 2459 HIS A C     1 
ATOM   8117  O  O     . HIS A 1 1242 ? 138.019 177.699 182.686 1.00 65.32  ? 2459 HIS A O     1 
ATOM   8118  C  CB    . HIS A 1 1242 ? 138.720 174.895 181.025 1.00 69.85  ? 2459 HIS A CB    1 
ATOM   8119  C  CG    . HIS A 1 1242 ? 137.222 174.878 181.146 1.00 77.80  ? 2459 HIS A CG    1 
ATOM   8120  N  ND1   . HIS A 1 1242 ? 136.552 175.055 182.338 1.00 79.36  ? 2459 HIS A ND1   1 
ATOM   8121  C  CD2   . HIS A 1 1242 ? 136.265 174.703 180.204 1.00 82.23  ? 2459 HIS A CD2   1 
ATOM   8122  C  CE1   . HIS A 1 1242 ? 135.250 174.989 182.127 1.00 78.11  ? 2459 HIS A CE1   1 
ATOM   8123  N  NE2   . HIS A 1 1242 ? 135.049 174.776 180.840 1.00 82.02  ? 2459 HIS A NE2   1 
ATOM   8124  N  N     . ARG A 1 1243 ? 139.410 176.328 183.791 1.00 63.17  ? 2460 ARG A N     1 
ATOM   8125  C  CA    . ARG A 1 1243 ? 138.905 176.727 185.098 1.00 66.37  ? 2460 ARG A CA    1 
ATOM   8126  C  C     . ARG A 1 1243 ? 139.577 177.979 185.647 1.00 64.48  ? 2460 ARG A C     1 
ATOM   8127  O  O     . ARG A 1 1243 ? 139.198 178.440 186.728 1.00 65.70  ? 2460 ARG A O     1 
ATOM   8128  C  CB    . ARG A 1 1243 ? 139.059 175.577 186.099 1.00 73.63  ? 2460 ARG A CB    1 
ATOM   8129  C  CG    . ARG A 1 1243 ? 140.491 175.140 186.350 1.00 72.97  ? 2460 ARG A CG    1 
ATOM   8130  C  CD    . ARG A 1 1243 ? 140.562 174.194 187.538 1.00 71.55  ? 2460 ARG A CD    1 
ATOM   8131  N  NE    . ARG A 1 1243 ? 140.526 174.911 188.807 1.00 73.69  ? 2460 ARG A NE    1 
ATOM   8132  C  CZ    . ARG A 1 1243 ? 140.062 174.406 189.942 1.00 86.99  ? 2460 ARG A CZ    1 
ATOM   8133  N  NH1   . ARG A 1 1243 ? 139.584 173.174 190.005 1.00 95.42  ? 2460 ARG A NH1   1 
ATOM   8134  N  NH2   . ARG A 1 1243 ? 140.076 175.156 191.039 1.00 90.98  ? 2460 ARG A NH2   1 
ATOM   8135  N  N     . HIS A 1 1244 ? 140.556 178.540 184.937 1.00 60.35  ? 2461 HIS A N     1 
ATOM   8136  C  CA    . HIS A 1 1244 ? 141.249 179.736 185.391 1.00 56.51  ? 2461 HIS A CA    1 
ATOM   8137  C  C     . HIS A 1 1244 ? 141.127 180.920 184.444 1.00 54.59  ? 2461 HIS A C     1 
ATOM   8138  O  O     . HIS A 1 1244 ? 141.493 182.034 184.834 1.00 52.59  ? 2461 HIS A O     1 
ATOM   8139  C  CB    . HIS A 1 1244 ? 142.740 179.438 185.619 1.00 49.01  ? 2461 HIS A CB    1 
ATOM   8140  C  CG    . HIS A 1 1244 ? 143.000 178.462 186.722 1.00 52.79  ? 2461 HIS A CG    1 
ATOM   8141  N  ND1   . HIS A 1 1244 ? 143.341 177.148 186.488 1.00 52.53  ? 2461 HIS A ND1   1 
ATOM   8142  C  CD2   . HIS A 1 1244 ? 142.973 178.609 188.068 1.00 55.04  ? 2461 HIS A CD2   1 
ATOM   8143  C  CE1   . HIS A 1 1244 ? 143.511 176.526 187.641 1.00 52.41  ? 2461 HIS A CE1   1 
ATOM   8144  N  NE2   . HIS A 1 1244 ? 143.293 177.390 188.615 1.00 58.07  ? 2461 HIS A NE2   1 
ATOM   8145  N  N     . THR A 1 1245 ? 140.629 180.721 183.227 1.00 54.76  ? 2462 THR A N     1 
ATOM   8146  C  CA    . THR A 1 1245 ? 140.526 181.784 182.239 1.00 51.99  ? 2462 THR A CA    1 
ATOM   8147  C  C     . THR A 1 1245 ? 139.086 181.927 181.765 1.00 54.59  ? 2462 THR A C     1 
ATOM   8148  O  O     . THR A 1 1245 ? 138.293 180.983 181.817 1.00 56.93  ? 2462 THR A O     1 
ATOM   8149  C  CB    . THR A 1 1245 ? 141.430 181.521 181.031 1.00 50.91  ? 2462 THR A CB    1 
ATOM   8150  O  OG1   . THR A 1 1245 ? 141.092 180.257 180.450 1.00 54.28  ? 2462 THR A OG1   1 
ATOM   8151  C  CG2   . THR A 1 1245 ? 142.884 181.498 181.451 1.00 48.67  ? 2462 THR A CG2   1 
ATOM   8152  N  N     . ASN A 1 1246 ? 138.757 183.130 181.298 1.00 50.81  ? 2463 ASN A N     1 
ATOM   8153  C  CA    . ASN A 1 1246 ? 137.445 183.423 180.745 1.00 48.90  ? 2463 ASN A CA    1 
ATOM   8154  C  C     . ASN A 1 1246 ? 137.601 184.117 179.400 1.00 45.78  ? 2463 ASN A C     1 
ATOM   8155  O  O     . ASN A 1 1246 ? 138.591 184.810 179.151 1.00 46.97  ? 2463 ASN A O     1 
ATOM   8156  C  CB    . ASN A 1 1246 ? 136.608 184.294 181.699 1.00 48.82  ? 2463 ASN A CB    1 
ATOM   8157  C  CG    . ASN A 1 1246 ? 137.038 185.749 181.698 1.00 48.27  ? 2463 ASN A CG    1 
ATOM   8158  O  OD1   . ASN A 1 1246 ? 138.228 186.058 181.714 1.00 45.39  ? 2463 ASN A OD1   1 
ATOM   8159  N  ND2   . ASN A 1 1246 ? 136.065 186.651 181.684 1.00 50.18  ? 2463 ASN A ND2   1 
ATOM   8160  N  N     . TYR A 1 1247 ? 136.615 183.914 178.531 1.00 42.52  ? 2464 TYR A N     1 
ATOM   8161  C  CA    . TYR A 1 1247 ? 136.608 184.515 177.204 1.00 39.30  ? 2464 TYR A CA    1 
ATOM   8162  C  C     . TYR A 1 1247 ? 135.845 185.832 177.259 1.00 42.18  ? 2464 TYR A C     1 
ATOM   8163  O  O     . TYR A 1 1247 ? 134.704 185.874 177.731 1.00 51.53  ? 2464 TYR A O     1 
ATOM   8164  C  CB    . TYR A 1 1247 ? 135.970 183.570 176.187 1.00 40.26  ? 2464 TYR A CB    1 
ATOM   8165  C  CG    . TYR A 1 1247 ? 136.883 182.475 175.688 1.00 40.72  ? 2464 TYR A CG    1 
ATOM   8166  C  CD1   . TYR A 1 1247 ? 137.993 182.767 174.907 1.00 39.23  ? 2464 TYR A CD1   1 
ATOM   8167  C  CD2   . TYR A 1 1247 ? 136.630 181.145 175.993 1.00 36.75  ? 2464 TYR A CD2   1 
ATOM   8168  C  CE1   . TYR A 1 1247 ? 138.825 181.764 174.445 1.00 35.38  ? 2464 TYR A CE1   1 
ATOM   8169  C  CE2   . TYR A 1 1247 ? 137.457 180.137 175.538 1.00 32.20  ? 2464 TYR A CE2   1 
ATOM   8170  C  CZ    . TYR A 1 1247 ? 138.553 180.452 174.766 1.00 32.25  ? 2464 TYR A CZ    1 
ATOM   8171  O  OH    . TYR A 1 1247 ? 139.376 179.447 174.313 1.00 34.03  ? 2464 TYR A OH    1 
ATOM   8172  N  N     . VAL A 1 1248 ? 136.471 186.902 176.780 1.00 41.85  ? 2465 VAL A N     1 
ATOM   8173  C  CA    . VAL A 1 1248 ? 135.854 188.221 176.741 1.00 47.64  ? 2465 VAL A CA    1 
ATOM   8174  C  C     . VAL A 1 1248 ? 135.985 188.773 175.327 1.00 52.01  ? 2465 VAL A C     1 
ATOM   8175  O  O     . VAL A 1 1248 ? 137.013 188.584 174.667 1.00 52.73  ? 2465 VAL A O     1 
ATOM   8176  C  CB    . VAL A 1 1248 ? 136.480 189.171 177.791 1.00 47.14  ? 2465 VAL A CB    1 
ATOM   8177  C  CG1   . VAL A 1 1248 ? 137.978 189.327 177.577 1.00 44.04  ? 2465 VAL A CG1   1 
ATOM   8178  C  CG2   . VAL A 1 1248 ? 135.787 190.527 177.790 1.00 50.92  ? 2465 VAL A CG2   1 
ATOM   8179  N  N     . THR A 1 1249 ? 134.925 189.415 174.844 1.00 53.75  ? 2466 THR A N     1 
ATOM   8180  C  CA    . THR A 1 1249 ? 134.925 189.990 173.504 1.00 55.79  ? 2466 THR A CA    1 
ATOM   8181  C  C     . THR A 1 1249 ? 135.088 191.505 173.554 1.00 54.19  ? 2466 THR A C     1 
ATOM   8182  O  O     . THR A 1 1249 ? 136.184 192.029 173.355 1.00 51.52  ? 2466 THR A O     1 
ATOM   8183  C  CB    . THR A 1 1249 ? 133.632 189.648 172.744 1.00 55.59  ? 2466 THR A CB    1 
ATOM   8184  O  OG1   . THR A 1 1249 ? 132.572 190.502 173.191 1.00 61.97  ? 2466 THR A OG1   1 
ATOM   8185  C  CG2   . THR A 1 1249 ? 133.243 188.198 172.981 1.00 48.30  ? 2466 THR A CG2   1 
ATOM   8186  N  N     . GLY A 1 1253 ? 134.609 184.804 171.725 1.00 42.64  ? 2470 GLY A N     1 
ATOM   8187  C  CA    . GLY A 1 1253 ? 135.667 185.389 172.527 1.00 48.18  ? 2470 GLY A CA    1 
ATOM   8188  C  C     . GLY A 1 1253 ? 136.883 185.800 171.721 1.00 47.19  ? 2470 GLY A C     1 
ATOM   8189  O  O     . GLY A 1 1253 ? 137.603 184.956 171.190 1.00 44.37  ? 2470 GLY A O     1 
ATOM   8190  N  N     . LEU A 1 1254 ? 137.106 187.109 171.623 1.00 48.30  ? 2471 LEU A N     1 
ATOM   8191  C  CA    . LEU A 1 1254 ? 138.258 187.649 170.918 1.00 43.85  ? 2471 LEU A CA    1 
ATOM   8192  C  C     . LEU A 1 1254 ? 139.459 187.879 171.825 1.00 45.18  ? 2471 LEU A C     1 
ATOM   8193  O  O     . LEU A 1 1254 ? 140.535 188.221 171.323 1.00 48.60  ? 2471 LEU A O     1 
ATOM   8194  C  CB    . LEU A 1 1254 ? 137.886 188.968 170.232 1.00 44.81  ? 2471 LEU A CB    1 
ATOM   8195  C  CG    . LEU A 1 1254 ? 137.428 188.894 168.774 1.00 48.16  ? 2471 LEU A CG    1 
ATOM   8196  C  CD1   . LEU A 1 1254 ? 136.891 190.241 168.319 1.00 48.91  ? 2471 LEU A CD1   1 
ATOM   8197  C  CD2   . LEU A 1 1254 ? 138.562 188.435 167.872 1.00 40.26  ? 2471 LEU A CD2   1 
ATOM   8198  N  N     . THR A 1 1255 ? 139.306 187.703 173.135 1.00 44.92  ? 2472 THR A N     1 
ATOM   8199  C  CA    . THR A 1 1255 ? 140.379 187.969 174.081 1.00 40.57  ? 2472 THR A CA    1 
ATOM   8200  C  C     . THR A 1 1255 ? 140.292 186.960 175.217 1.00 41.04  ? 2472 THR A C     1 
ATOM   8201  O  O     . THR A 1 1255 ? 139.197 186.650 175.693 1.00 46.19  ? 2472 THR A O     1 
ATOM   8202  C  CB    . THR A 1 1255 ? 140.291 189.400 174.629 1.00 38.46  ? 2472 THR A CB    1 
ATOM   8203  O  OG1   . THR A 1 1255 ? 140.245 190.330 173.540 1.00 41.20  ? 2472 THR A OG1   1 
ATOM   8204  C  CG2   . THR A 1 1255 ? 141.490 189.724 175.496 1.00 33.77  ? 2472 THR A CG2   1 
ATOM   8205  N  N     . LEU A 1 1256 ? 141.445 186.449 175.644 1.00 37.81  ? 2473 LEU A N     1 
ATOM   8206  C  CA    . LEU A 1 1256 ? 141.527 185.526 176.768 1.00 34.73  ? 2473 LEU A CA    1 
ATOM   8207  C  C     . LEU A 1 1256 ? 142.099 186.262 177.972 1.00 36.32  ? 2473 LEU A C     1 
ATOM   8208  O  O     . LEU A 1 1256 ? 143.192 186.832 177.896 1.00 35.70  ? 2473 LEU A O     1 
ATOM   8209  C  CB    . LEU A 1 1256 ? 142.388 184.311 176.425 1.00 30.82  ? 2473 LEU A CB    1 
ATOM   8210  C  CG    . LEU A 1 1256 ? 142.267 183.116 177.369 1.00 34.29  ? 2473 LEU A CG    1 
ATOM   8211  C  CD1   . LEU A 1 1256 ? 140.880 182.514 177.280 1.00 37.41  ? 2473 LEU A CD1   1 
ATOM   8212  C  CD2   . LEU A 1 1256 ? 143.317 182.069 177.049 1.00 34.39  ? 2473 LEU A CD2   1 
ATOM   8213  N  N     . LEU A 1 1257 ? 141.362 186.244 179.076 1.00 38.91  ? 2474 LEU A N     1 
ATOM   8214  C  CA    . LEU A 1 1257 ? 141.758 186.894 180.312 1.00 40.31  ? 2474 LEU A CA    1 
ATOM   8215  C  C     . LEU A 1 1257 ? 141.655 185.905 181.462 1.00 45.63  ? 2474 LEU A C     1 
ATOM   8216  O  O     . LEU A 1 1257 ? 140.861 184.962 181.404 1.00 45.48  ? 2474 LEU A O     1 
ATOM   8217  C  CB    . LEU A 1 1257 ? 140.873 188.116 180.604 1.00 36.05  ? 2474 LEU A CB    1 
ATOM   8218  C  CG    . LEU A 1 1257 ? 141.278 189.447 179.971 1.00 35.64  ? 2474 LEU A CG    1 
ATOM   8219  C  CD1   . LEU A 1 1257 ? 140.244 190.515 180.277 1.00 37.29  ? 2474 LEU A CD1   1 
ATOM   8220  C  CD2   . LEU A 1 1257 ? 142.644 189.876 180.464 1.00 36.75  ? 2474 LEU A CD2   1 
ATOM   8221  N  N     . PRO A 1 1258 ? 142.457 186.083 182.511 1.00 42.65  ? 2475 PRO A N     1 
ATOM   8222  C  CA    . PRO A 1 1258 ? 142.298 185.245 183.702 1.00 38.70  ? 2475 PRO A CA    1 
ATOM   8223  C  C     . PRO A 1 1258 ? 140.976 185.527 184.395 1.00 44.24  ? 2475 PRO A C     1 
ATOM   8224  O  O     . PRO A 1 1258 ? 140.411 186.618 184.287 1.00 46.91  ? 2475 PRO A O     1 
ATOM   8225  C  CB    . PRO A 1 1258 ? 143.485 185.647 184.586 1.00 36.37  ? 2475 PRO A CB    1 
ATOM   8226  C  CG    . PRO A 1 1258 ? 144.442 186.331 183.675 1.00 33.79  ? 2475 PRO A CG    1 
ATOM   8227  C  CD    . PRO A 1 1258 ? 143.617 186.982 182.621 1.00 36.18  ? 2475 PRO A CD    1 
ATOM   8228  N  N     . LYS A 1 1259 ? 140.476 184.513 185.107 1.00 46.64  ? 2476 LYS A N     1 
ATOM   8229  C  CA    . LYS A 1 1259 ? 139.219 184.670 185.832 1.00 46.15  ? 2476 LYS A CA    1 
ATOM   8230  C  C     . LYS A 1 1259 ? 139.339 185.705 186.943 1.00 45.80  ? 2476 LYS A C     1 
ATOM   8231  O  O     . LYS A 1 1259 ? 138.353 186.370 187.280 1.00 45.19  ? 2476 LYS A O     1 
ATOM   8232  C  CB    . LYS A 1 1259 ? 138.767 183.327 186.402 1.00 48.75  ? 2476 LYS A CB    1 
ATOM   8233  C  CG    . LYS A 1 1259 ? 137.278 183.250 186.689 1.00 50.77  ? 2476 LYS A CG    1 
ATOM   8234  C  CD    . LYS A 1 1259 ? 136.489 182.933 185.430 1.00 49.72  ? 2476 LYS A CD    1 
ATOM   8235  C  CE    . LYS A 1 1259 ? 136.919 181.606 184.829 1.00 52.11  ? 2476 LYS A CE    1 
ATOM   8236  N  NZ    . LYS A 1 1259 ? 136.369 181.409 183.459 1.00 51.07  ? 2476 LYS A NZ    1 
ATOM   8237  N  N     . SER A 1 1260 ? 140.528 185.857 187.519 1.00 46.29  ? 2477 SER A N     1 
ATOM   8238  C  CA    . SER A 1 1260 ? 140.772 186.896 188.505 1.00 46.46  ? 2477 SER A CA    1 
ATOM   8239  C  C     . SER A 1 1260 ? 140.943 188.245 187.808 1.00 45.97  ? 2477 SER A C     1 
ATOM   8240  O  O     . SER A 1 1260 ? 140.876 188.357 186.581 1.00 45.58  ? 2477 SER A O     1 
ATOM   8241  C  CB    . SER A 1 1260 ? 141.993 186.548 189.354 1.00 43.17  ? 2477 SER A CB    1 
ATOM   8242  O  OG    . SER A 1 1260 ? 143.136 186.330 188.546 1.00 39.71  ? 2477 SER A OG    1 
ATOM   8243  N  N     . ASP A 1 1261 ? 141.173 189.291 188.601 1.00 43.71  ? 2478 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 1261 ? 141.273 190.641 188.068 1.00 48.00  ? 2478 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 1261 ? 142.519 191.396 188.502 1.00 49.35  ? 2478 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 1261 ? 142.772 192.480 187.963 1.00 48.51  ? 2478 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 1261 ? 140.039 191.467 188.465 1.00 53.98  ? 2478 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 1261 ? 138.776 190.997 187.772 1.00 62.62  ? 2478 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 1261 ? 138.877 190.471 186.644 1.00 63.29  ? 2478 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 1261 ? 137.683 191.152 188.355 1.00 66.39  ? 2478 ASP A OD2   1 
ATOM   8251  N  N     . ILE A 1 1262 ? 143.299 190.877 189.446 1.00 45.26  ? 2479 ILE A N     1 
ATOM   8252  C  CA    . ILE A 1 1262 ? 144.486 191.575 189.920 1.00 41.57  ? 2479 ILE A CA    1 
ATOM   8253  C  C     . ILE A 1 1262 ? 145.770 190.783 189.720 1.00 38.60  ? 2479 ILE A C     1 
ATOM   8254  O  O     . ILE A 1 1262 ? 146.856 191.385 189.742 1.00 40.76  ? 2479 ILE A O     1 
ATOM   8255  C  CB    . ILE A 1 1262 ? 144.340 191.976 191.404 1.00 43.88  ? 2479 ILE A CB    1 
ATOM   8256  C  CG1   . ILE A 1 1262 ? 144.185 190.735 192.282 1.00 40.94  ? 2479 ILE A CG1   1 
ATOM   8257  C  CG2   . ILE A 1 1262 ? 143.163 192.922 191.593 1.00 46.98  ? 2479 ILE A CG2   1 
ATOM   8258  C  CD1   . ILE A 1 1262 ? 144.271 191.021 193.764 1.00 41.78  ? 2479 ILE A CD1   1 
ATOM   8259  N  N     . LYS A 1 1263 ? 145.707 189.470 189.519 1.00 37.51  ? 2480 LYS A N     1 
ATOM   8260  C  CA    . LYS A 1 1263 ? 146.896 188.641 189.385 1.00 30.13  ? 2480 LYS A CA    1 
ATOM   8261  C  C     . LYS A 1 1263 ? 147.019 188.125 187.959 1.00 25.77  ? 2480 LYS A C     1 
ATOM   8262  O  O     . LYS A 1 1263 ? 146.072 187.542 187.421 1.00 26.95  ? 2480 LYS A O     1 
ATOM   8263  C  CB    . LYS A 1 1263 ? 146.863 187.461 190.360 1.00 26.03  ? 2480 LYS A CB    1 
ATOM   8264  C  CG    . LYS A 1 1263 ? 146.342 187.789 191.748 1.00 30.43  ? 2480 LYS A CG    1 
ATOM   8265  C  CD    . LYS A 1 1263 ? 146.514 186.602 192.684 1.00 27.16  ? 2480 LYS A CD    1 
ATOM   8266  C  CE    . LYS A 1 1263 ? 145.945 186.879 194.063 1.00 31.30  ? 2480 LYS A CE    1 
ATOM   8267  N  NZ    . LYS A 1 1263 ? 146.684 187.958 194.767 1.00 34.25  ? 2480 LYS A NZ    1 
ATOM   8268  N  N     . ASN A 1 1264 ? 148.185 188.341 187.354 1.00 24.39  ? 2481 ASN A N     1 
ATOM   8269  C  CA    . ASN A 1 1264 ? 148.499 187.720 186.076 1.00 21.75  ? 2481 ASN A CA    1 
ATOM   8270  C  C     . ASN A 1 1264 ? 148.606 186.210 186.246 1.00 19.59  ? 2481 ASN A C     1 
ATOM   8271  O  O     . ASN A 1 1264 ? 148.930 185.707 187.322 1.00 23.52  ? 2481 ASN A O     1 
ATOM   8272  C  CB    . ASN A 1 1264 ? 149.810 188.269 185.513 1.00 22.86  ? 2481 ASN A CB    1 
ATOM   8273  C  CG    . ASN A 1 1264 ? 149.772 189.766 185.290 1.00 29.83  ? 2481 ASN A CG    1 
ATOM   8274  O  OD1   . ASN A 1 1264 ? 149.600 190.230 184.164 1.00 32.19  ? 2481 ASN A OD1   1 
ATOM   8275  N  ND2   . ASN A 1 1264 ? 149.952 190.532 186.359 1.00 28.47  ? 2481 ASN A ND2   1 
ATOM   8276  N  N     . LEU A 1 1265 ? 148.329 185.483 185.174 1.00 17.64  ? 2482 LEU A N     1 
ATOM   8277  C  CA    . LEU A 1 1265 ? 148.312 184.030 185.226 1.00 19.00  ? 2482 LEU A CA    1 
ATOM   8278  C  C     . LEU A 1 1265 ? 149.608 183.476 184.652 1.00 21.13  ? 2482 LEU A C     1 
ATOM   8279  O  O     . LEU A 1 1265 ? 150.138 184.003 183.670 1.00 22.32  ? 2482 LEU A O     1 
ATOM   8280  C  CB    . LEU A 1 1265 ? 147.113 183.472 184.460 1.00 18.17  ? 2482 LEU A CB    1 
ATOM   8281  C  CG    . LEU A 1 1265 ? 146.809 181.999 184.717 1.00 16.68  ? 2482 LEU A CG    1 
ATOM   8282  C  CD1   . LEU A 1 1265 ? 146.361 181.829 186.154 1.00 20.70  ? 2482 LEU A CD1   1 
ATOM   8283  C  CD2   . LEU A 1 1265 ? 145.757 181.486 183.760 1.00 23.68  ? 2482 LEU A CD2   1 
ATOM   8284  N  N     . VAL A 1 1266 ? 150.120 182.415 185.272 1.00 17.90  ? 2483 VAL A N     1 
ATOM   8285  C  CA    . VAL A 1 1266 ? 151.360 181.773 184.857 1.00 15.06  ? 2483 VAL A CA    1 
ATOM   8286  C  C     . VAL A 1 1266 ? 151.054 180.328 184.498 1.00 15.90  ? 2483 VAL A C     1 
ATOM   8287  O  O     . VAL A 1 1266 ? 150.481 179.591 185.308 1.00 18.66  ? 2483 VAL A O     1 
ATOM   8288  C  CB    . VAL A 1 1266 ? 152.435 181.845 185.955 1.00 13.01  ? 2483 VAL A CB    1 
ATOM   8289  C  CG1   . VAL A 1 1266 ? 153.596 180.929 185.621 1.00 18.01  ? 2483 VAL A CG1   1 
ATOM   8290  C  CG2   . VAL A 1 1266 ? 152.905 183.270 186.133 1.00 14.16  ? 2483 VAL A CG2   1 
ATOM   8291  N  N     . LEU A 1 1267 ? 151.437 179.925 183.287 1.00 14.90  ? 2484 LEU A N     1 
ATOM   8292  C  CA    . LEU A 1 1267 ? 151.200 178.568 182.801 1.00 14.83  ? 2484 LEU A CA    1 
ATOM   8293  C  C     . LEU A 1 1267 ? 152.460 177.737 183.023 1.00 15.78  ? 2484 LEU A C     1 
ATOM   8294  O  O     . LEU A 1 1267 ? 153.289 177.558 182.132 1.00 18.17  ? 2484 LEU A O     1 
ATOM   8295  C  CB    . LEU A 1 1267 ? 150.793 178.590 181.332 1.00 16.08  ? 2484 LEU A CB    1 
ATOM   8296  C  CG    . LEU A 1 1267 ? 150.002 177.386 180.819 1.00 18.46  ? 2484 LEU A CG    1 
ATOM   8297  C  CD1   . LEU A 1 1267 ? 148.833 177.068 181.737 1.00 20.71  ? 2484 LEU A CD1   1 
ATOM   8298  C  CD2   . LEU A 1 1267 ? 149.526 177.636 179.400 1.00 23.64  ? 2484 LEU A CD2   1 
ATOM   8299  N  N     . PHE A 1 1268 ? 152.602 177.230 184.243 1.00 13.70  ? 2485 PHE A N     1 
ATOM   8300  C  CA    . PHE A 1 1268 ? 153.679 176.297 184.545 1.00 12.91  ? 2485 PHE A CA    1 
ATOM   8301  C  C     . PHE A 1 1268 ? 153.460 175.010 183.763 1.00 15.09  ? 2485 PHE A C     1 
ATOM   8302  O  O     . PHE A 1 1268 ? 152.438 174.338 183.934 1.00 19.12  ? 2485 PHE A O     1 
ATOM   8303  C  CB    . PHE A 1 1268 ? 153.729 176.009 186.042 1.00 14.54  ? 2485 PHE A CB    1 
ATOM   8304  C  CG    . PHE A 1 1268 ? 154.845 175.085 186.450 1.00 14.91  ? 2485 PHE A CG    1 
ATOM   8305  C  CD1   . PHE A 1 1268 ? 156.067 175.120 185.802 1.00 14.84  ? 2485 PHE A CD1   1 
ATOM   8306  C  CD2   . PHE A 1 1268 ? 154.668 174.179 187.480 1.00 14.67  ? 2485 PHE A CD2   1 
ATOM   8307  C  CE1   . PHE A 1 1268 ? 157.088 174.273 186.174 1.00 12.38  ? 2485 PHE A CE1   1 
ATOM   8308  C  CE2   . PHE A 1 1268 ? 155.689 173.330 187.854 1.00 15.09  ? 2485 PHE A CE2   1 
ATOM   8309  C  CZ    . PHE A 1 1268 ? 156.900 173.379 187.198 1.00 13.71  ? 2485 PHE A CZ    1 
ATOM   8310  N  N     . CYS A 1 1269 ? 154.417 174.664 182.910 1.00 13.21  ? 2486 CYS A N     1 
ATOM   8311  C  CA    . CYS A 1 1269 ? 154.354 173.451 182.102 1.00 14.08  ? 2486 CYS A CA    1 
ATOM   8312  C  C     . CYS A 1 1269 ? 155.571 172.609 182.463 1.00 16.24  ? 2486 CYS A C     1 
ATOM   8313  O  O     . CYS A 1 1269 ? 156.662 172.812 181.929 1.00 20.25  ? 2486 CYS A O     1 
ATOM   8314  C  CB    . CYS A 1 1269 ? 154.311 173.782 180.623 1.00 16.16  ? 2486 CYS A CB    1 
ATOM   8315  S  SG    . CYS A 1 1269 ? 152.892 174.786 180.142 1.00 29.90  ? 2486 CYS A SG    1 
ATOM   8316  N  N     . ASP A 1 1270 ? 155.383 171.670 183.383 1.00 17.10  ? 2487 ASP A N     1 
ATOM   8317  C  CA    . ASP A 1 1270 ? 156.488 170.832 183.821 1.00 18.99  ? 2487 ASP A CA    1 
ATOM   8318  C  C     . ASP A 1 1270 ? 156.792 169.764 182.780 1.00 22.76  ? 2487 ASP A C     1 
ATOM   8319  O  O     . ASP A 1 1270 ? 155.882 169.165 182.200 1.00 26.88  ? 2487 ASP A O     1 
ATOM   8320  C  CB    . ASP A 1 1270 ? 156.160 170.180 185.163 1.00 22.22  ? 2487 ASP A CB    1 
ATOM   8321  C  CG    . ASP A 1 1270 ? 157.401 169.796 185.944 1.00 24.13  ? 2487 ASP A CG    1 
ATOM   8322  O  OD1   . ASP A 1 1270 ? 158.419 170.506 185.824 1.00 22.99  ? 2487 ASP A OD1   1 
ATOM   8323  O  OD2   . ASP A 1 1270 ? 157.357 168.790 186.683 1.00 25.09  ? 2487 ASP A OD2   1 
ATOM   8324  N  N     . GLU A 1 1271 ? 158.087 169.545 182.541 1.00 23.16  ? 2488 GLU A N     1 
ATOM   8325  C  CA    . GLU A 1 1271 ? 158.590 168.484 181.667 1.00 25.64  ? 2488 GLU A CA    1 
ATOM   8326  C  C     . GLU A 1 1271 ? 158.055 168.630 180.239 1.00 29.30  ? 2488 GLU A C     1 
ATOM   8327  O  O     . GLU A 1 1271 ? 157.363 167.761 179.710 1.00 33.28  ? 2488 GLU A O     1 
ATOM   8328  C  CB    . GLU A 1 1271 ? 158.263 167.109 182.254 1.00 26.74  ? 2488 GLU A CB    1 
ATOM   8329  C  CG    . GLU A 1 1271 ? 158.958 166.831 183.570 1.00 31.87  ? 2488 GLU A CG    1 
ATOM   8330  C  CD    . GLU A 1 1271 ? 158.516 165.525 184.189 1.00 43.25  ? 2488 GLU A CD    1 
ATOM   8331  O  OE1   . GLU A 1 1271 ? 157.639 164.855 183.606 1.00 47.56  ? 2488 GLU A OE1   1 
ATOM   8332  O  OE2   . GLU A 1 1271 ? 159.032 165.174 185.268 1.00 44.13  ? 2488 GLU A OE2   1 
ATOM   8333  N  N     . ILE A 1 1272 ? 158.397 169.764 179.621 1.00 28.07  ? 2489 ILE A N     1 
ATOM   8334  C  CA    . ILE A 1 1272 ? 158.002 170.043 178.244 1.00 27.50  ? 2489 ILE A CA    1 
ATOM   8335  C  C     . ILE A 1 1272 ? 158.784 169.243 177.213 1.00 29.40  ? 2489 ILE A C     1 
ATOM   8336  O  O     . ILE A 1 1272 ? 158.530 169.392 176.014 1.00 28.81  ? 2489 ILE A O     1 
ATOM   8337  C  CB    . ILE A 1 1272 ? 158.122 171.557 177.970 1.00 24.28  ? 2489 ILE A CB    1 
ATOM   8338  C  CG1   . ILE A 1 1272 ? 159.533 172.055 178.282 1.00 24.16  ? 2489 ILE A CG1   1 
ATOM   8339  C  CG2   . ILE A 1 1272 ? 157.092 172.328 178.757 1.00 24.62  ? 2489 ILE A CG2   1 
ATOM   8340  C  CD1   . ILE A 1 1272 ? 159.758 173.496 177.903 1.00 21.81  ? 2489 ILE A CD1   1 
ATOM   8341  N  N     . ASN A 1 1273 ? 159.737 168.410 177.638 1.00 25.76  ? 2490 ASN A N     1 
ATOM   8342  C  CA    . ASN A 1 1273 ? 160.410 167.510 176.710 1.00 29.91  ? 2490 ASN A CA    1 
ATOM   8343  C  C     . ASN A 1 1273 ? 159.585 166.272 176.378 1.00 40.09  ? 2490 ASN A C     1 
ATOM   8344  O  O     . ASN A 1 1273 ? 159.907 165.575 175.410 1.00 47.08  ? 2490 ASN A O     1 
ATOM   8345  C  CB    . ASN A 1 1273 ? 161.759 167.070 177.276 1.00 35.08  ? 2490 ASN A CB    1 
ATOM   8346  C  CG    . ASN A 1 1273 ? 162.771 168.187 177.301 1.00 34.00  ? 2490 ASN A CG    1 
ATOM   8347  O  OD1   . ASN A 1 1273 ? 163.534 168.325 178.254 1.00 35.81  ? 2490 ASN A OD1   1 
ATOM   8348  N  ND2   . ASN A 1 1273 ? 162.768 169.010 176.262 1.00 30.63  ? 2490 ASN A ND2   1 
ATOM   8349  N  N     . LEU A 1 1274 ? 158.552 165.976 177.167 1.00 37.47  ? 2491 LEU A N     1 
ATOM   8350  C  CA    . LEU A 1 1274 ? 157.732 164.791 176.919 1.00 36.41  ? 2491 LEU A CA    1 
ATOM   8351  C  C     . LEU A 1 1274 ? 157.013 164.754 175.572 1.00 38.63  ? 2491 LEU A C     1 
ATOM   8352  O  O     . LEU A 1 1274 ? 156.961 163.658 174.986 1.00 42.10  ? 2491 LEU A O     1 
ATOM   8353  C  CB    . LEU A 1 1274 ? 156.729 164.590 178.065 1.00 34.43  ? 2491 LEU A CB    1 
ATOM   8354  C  CG    . LEU A 1 1274 ? 157.161 163.801 179.306 1.00 36.72  ? 2491 LEU A CG    1 
ATOM   8355  C  CD1   . LEU A 1 1274 ? 157.439 162.358 178.916 1.00 44.15  ? 2491 LEU A CD1   1 
ATOM   8356  C  CD2   . LEU A 1 1274 ? 158.377 164.378 179.971 1.00 37.44  ? 2491 LEU A CD2   1 
ATOM   8357  N  N     . PRO A 1 1275 ? 156.393 165.858 175.041 1.00 34.26  ? 2492 PRO A N     1 
ATOM   8358  C  CA    . PRO A 1 1275 ? 155.735 165.754 173.727 1.00 38.46  ? 2492 PRO A CA    1 
ATOM   8359  C  C     . PRO A 1 1275 ? 156.629 165.183 172.638 1.00 47.45  ? 2492 PRO A C     1 
ATOM   8360  O  O     . PRO A 1 1275 ? 157.608 165.806 172.221 1.00 51.39  ? 2492 PRO A O     1 
ATOM   8361  C  CB    . PRO A 1 1275 ? 155.345 167.203 173.419 1.00 36.57  ? 2492 PRO A CB    1 
ATOM   8362  C  CG    . PRO A 1 1275 ? 155.083 167.781 174.739 1.00 35.01  ? 2492 PRO A CG    1 
ATOM   8363  C  CD    . PRO A 1 1275 ? 156.093 167.160 175.670 1.00 34.20  ? 2492 PRO A CD    1 
ATOM   8364  N  N     . LYS A 1 1276 ? 156.298 163.974 172.197 1.00 51.27  ? 2493 LYS A N     1 
ATOM   8365  C  CA    . LYS A 1 1276 ? 157.116 163.246 171.245 1.00 53.23  ? 2493 LYS A CA    1 
ATOM   8366  C  C     . LYS A 1 1276 ? 156.929 163.801 169.839 1.00 55.89  ? 2493 LYS A C     1 
ATOM   8367  O  O     . LYS A 1 1276 ? 155.903 164.402 169.508 1.00 53.42  ? 2493 LYS A O     1 
ATOM   8368  C  CB    . LYS A 1 1276 ? 156.769 161.757 171.267 1.00 51.51  ? 2493 LYS A CB    1 
ATOM   8369  C  CG    . LYS A 1 1276 ? 155.336 161.455 170.860 1.00 54.32  ? 2493 LYS A CG    1 
ATOM   8370  C  CD    . LYS A 1 1276 ? 155.149 159.987 170.521 1.00 56.83  ? 2493 LYS A CD    1 
ATOM   8371  C  CE    . LYS A 1 1276 ? 153.747 159.721 170.001 1.00 57.85  ? 2493 LYS A CE    1 
ATOM   8372  N  NZ    . LYS A 1 1276 ? 152.702 160.201 170.948 1.00 48.67  ? 2493 LYS A NZ    1 
ATOM   8373  N  N     . LEU A 1 1277 ? 157.947 163.595 169.010 1.00 56.06  ? 2494 LEU A N     1 
ATOM   8374  C  CA    . LEU A 1 1277 ? 157.858 163.978 167.611 1.00 56.89  ? 2494 LEU A CA    1 
ATOM   8375  C  C     . LEU A 1 1277 ? 156.802 163.142 166.901 1.00 64.39  ? 2494 LEU A C     1 
ATOM   8376  O  O     . LEU A 1 1277 ? 156.552 161.985 167.249 1.00 68.63  ? 2494 LEU A O     1 
ATOM   8377  C  CB    . LEU A 1 1277 ? 159.207 163.800 166.916 1.00 59.92  ? 2494 LEU A CB    1 
ATOM   8378  C  CG    . LEU A 1 1277 ? 160.357 164.696 167.370 1.00 58.21  ? 2494 LEU A CG    1 
ATOM   8379  C  CD1   . LEU A 1 1277 ? 161.661 164.257 166.722 1.00 59.81  ? 2494 LEU A CD1   1 
ATOM   8380  C  CD2   . LEU A 1 1277 ? 160.063 166.151 167.051 1.00 54.45  ? 2494 LEU A CD2   1 
ATOM   8381  N  N     . ASP A 1 1278 ? 156.175 163.743 165.897 1.00 64.92  ? 2495 ASP A N     1 
ATOM   8382  C  CA    . ASP A 1 1278 ? 155.222 163.030 165.060 1.00 68.33  ? 2495 ASP A CA    1 
ATOM   8383  C  C     . ASP A 1 1278 ? 155.990 162.221 164.015 1.00 69.57  ? 2495 ASP A C     1 
ATOM   8384  O  O     . ASP A 1 1278 ? 157.213 162.070 164.083 1.00 70.23  ? 2495 ASP A O     1 
ATOM   8385  C  CB    . ASP A 1 1278 ? 154.234 164.011 164.434 1.00 69.10  ? 2495 ASP A CB    1 
ATOM   8386  C  CG    . ASP A 1 1278 ? 154.856 164.840 163.327 1.00 71.33  ? 2495 ASP A CG    1 
ATOM   8387  O  OD1   . ASP A 1 1278 ? 156.024 165.256 163.477 1.00 69.42  ? 2495 ASP A OD1   1 
ATOM   8388  O  OD2   . ASP A 1 1278 ? 154.176 165.075 162.307 1.00 76.07  ? 2495 ASP A OD2   1 
ATOM   8389  N  N     . LYS A 1 1279 ? 155.276 161.692 163.022 1.00 70.94  ? 2496 LYS A N     1 
ATOM   8390  C  CA    . LYS A 1 1279 ? 155.931 160.977 161.934 1.00 74.82  ? 2496 LYS A CA    1 
ATOM   8391  C  C     . LYS A 1 1279 ? 156.747 161.896 161.035 1.00 72.50  ? 2496 LYS A C     1 
ATOM   8392  O  O     . LYS A 1 1279 ? 157.518 161.399 160.207 1.00 70.40  ? 2496 LYS A O     1 
ATOM   8393  C  CB    . LYS A 1 1279 ? 154.891 160.227 161.099 1.00 77.99  ? 2496 LYS A CB    1 
ATOM   8394  N  N     . TYR A 1 1280 ? 156.600 163.215 161.178 1.00 72.86  ? 2497 TYR A N     1 
ATOM   8395  C  CA    . TYR A 1 1280 ? 157.291 164.184 160.337 1.00 75.03  ? 2497 TYR A CA    1 
ATOM   8396  C  C     . TYR A 1 1280 ? 158.172 165.133 161.145 1.00 73.17  ? 2497 TYR A C     1 
ATOM   8397  O  O     . TYR A 1 1280 ? 158.473 166.238 160.684 1.00 79.22  ? 2497 TYR A O     1 
ATOM   8398  C  CB    . TYR A 1 1280 ? 156.277 164.965 159.502 1.00 77.31  ? 2497 TYR A CB    1 
ATOM   8399  C  CG    . TYR A 1 1280 ? 155.309 164.071 158.761 1.00 80.92  ? 2497 TYR A CG    1 
ATOM   8400  C  CD1   . TYR A 1 1280 ? 155.770 163.069 157.917 1.00 81.86  ? 2497 TYR A CD1   1 
ATOM   8401  C  CD2   . TYR A 1 1280 ? 153.938 164.210 158.925 1.00 80.55  ? 2497 TYR A CD2   1 
ATOM   8402  C  CE1   . TYR A 1 1280 ? 154.891 162.244 157.242 1.00 81.74  ? 2497 TYR A CE1   1 
ATOM   8403  C  CE2   . TYR A 1 1280 ? 153.051 163.390 158.255 1.00 81.18  ? 2497 TYR A CE2   1 
ATOM   8404  C  CZ    . TYR A 1 1280 ? 153.533 162.408 157.415 1.00 81.00  ? 2497 TYR A CZ    1 
ATOM   8405  O  OH    . TYR A 1 1280 ? 152.652 161.589 156.748 1.00 78.99  ? 2497 TYR A OH    1 
ATOM   8406  N  N     . GLY A 1 1281 ? 158.595 164.720 162.339 1.00 65.79  ? 2498 GLY A N     1 
ATOM   8407  C  CA    . GLY A 1 1281 ? 159.550 165.475 163.130 1.00 60.58  ? 2498 GLY A CA    1 
ATOM   8408  C  C     . GLY A 1 1281 ? 159.087 166.813 163.672 1.00 61.60  ? 2498 GLY A C     1 
ATOM   8409  O  O     . GLY A 1 1281 ? 159.821 167.802 163.593 1.00 58.64  ? 2498 GLY A O     1 
ATOM   8410  N  N     . SER A 1 1282 ? 157.877 166.861 164.225 1.00 64.33  ? 2499 SER A N     1 
ATOM   8411  C  CA    . SER A 1 1282 ? 157.387 168.071 164.868 1.00 57.81  ? 2499 SER A CA    1 
ATOM   8412  C  C     . SER A 1 1282 ? 156.432 167.691 165.990 1.00 58.04  ? 2499 SER A C     1 
ATOM   8413  O  O     . SER A 1 1282 ? 155.868 166.595 166.010 1.00 59.59  ? 2499 SER A O     1 
ATOM   8414  C  CB    . SER A 1 1282 ? 156.700 169.006 163.868 1.00 53.60  ? 2499 SER A CB    1 
ATOM   8415  O  OG    . SER A 1 1282 ? 157.656 169.766 163.150 1.00 48.83  ? 2499 SER A OG    1 
ATOM   8416  N  N     . GLN A 1 1283 ? 156.260 168.619 166.929 1.00 50.37  ? 2500 GLN A N     1 
ATOM   8417  C  CA    . GLN A 1 1283 ? 155.437 168.416 168.112 1.00 40.87  ? 2500 GLN A CA    1 
ATOM   8418  C  C     . GLN A 1 1283 ? 154.323 169.450 168.132 1.00 35.12  ? 2500 GLN A C     1 
ATOM   8419  O  O     . GLN A 1 1283 ? 154.547 170.618 167.807 1.00 35.47  ? 2500 GLN A O     1 
ATOM   8420  C  CB    . GLN A 1 1283 ? 156.280 168.531 169.383 1.00 37.46  ? 2500 GLN A CB    1 
ATOM   8421  C  CG    . GLN A 1 1283 ? 157.710 168.044 169.207 1.00 43.97  ? 2500 GLN A CG    1 
ATOM   8422  C  CD    . GLN A 1 1283 ? 158.517 168.099 170.487 1.00 46.69  ? 2500 GLN A CD    1 
ATOM   8423  O  OE1   . GLN A 1 1283 ? 158.161 168.801 171.429 1.00 40.88  ? 2500 GLN A OE1   1 
ATOM   8424  N  NE2   . GLN A 1 1283 ? 159.615 167.355 170.527 1.00 48.89  ? 2500 GLN A NE2   1 
ATOM   8425  N  N     . ASN A 1 1284 ? 153.118 169.022 168.510 1.00 33.85  ? 2501 ASN A N     1 
ATOM   8426  C  CA    . ASN A 1 1284 ? 151.987 169.944 168.508 1.00 32.84  ? 2501 ASN A CA    1 
ATOM   8427  C  C     . ASN A 1 1284 ? 152.080 170.942 169.660 1.00 32.05  ? 2501 ASN A C     1 
ATOM   8428  O  O     . ASN A 1 1284 ? 151.861 172.148 169.472 1.00 32.85  ? 2501 ASN A O     1 
ATOM   8429  C  CB    . ASN A 1 1284 ? 150.678 169.156 168.582 1.00 35.83  ? 2501 ASN A CB    1 
ATOM   8430  C  CG    . ASN A 1 1284 ? 150.401 168.358 167.317 1.00 39.91  ? 2501 ASN A CG    1 
ATOM   8431  O  OD1   . ASN A 1 1284 ? 151.271 168.208 166.461 1.00 42.11  ? 2501 ASN A OD1   1 
ATOM   8432  N  ND2   . ASN A 1 1284 ? 149.183 167.836 167.199 1.00 42.94  ? 2501 ASN A ND2   1 
ATOM   8433  N  N     . VAL A 1 1285 ? 152.439 170.458 170.851 1.00 31.28  ? 2502 VAL A N     1 
ATOM   8434  C  CA    . VAL A 1 1285 ? 152.332 171.263 172.064 1.00 26.28  ? 2502 VAL A CA    1 
ATOM   8435  C  C     . VAL A 1 1285 ? 153.360 172.389 172.073 1.00 28.15  ? 2502 VAL A C     1 
ATOM   8436  O  O     . VAL A 1 1285 ? 153.041 173.529 172.429 1.00 30.91  ? 2502 VAL A O     1 
ATOM   8437  C  CB    . VAL A 1 1285 ? 152.462 170.359 173.302 1.00 27.97  ? 2502 VAL A CB    1 
ATOM   8438  C  CG1   . VAL A 1 1285 ? 152.451 171.182 174.570 1.00 28.00  ? 2502 VAL A CG1   1 
ATOM   8439  C  CG2   . VAL A 1 1285 ? 151.340 169.336 173.323 1.00 33.11  ? 2502 VAL A CG2   1 
ATOM   8440  N  N     . VAL A 1 1286 ? 154.606 172.099 171.689 1.00 28.44  ? 2503 VAL A N     1 
ATOM   8441  C  CA    . VAL A 1 1286 ? 155.635 173.134 171.758 1.00 25.68  ? 2503 VAL A CA    1 
ATOM   8442  C  C     . VAL A 1 1286 ? 155.445 174.185 170.667 1.00 24.40  ? 2503 VAL A C     1 
ATOM   8443  O  O     . VAL A 1 1286 ? 155.747 175.363 170.883 1.00 22.38  ? 2503 VAL A O     1 
ATOM   8444  C  CB    . VAL A 1 1286 ? 157.042 172.507 171.732 1.00 28.94  ? 2503 VAL A CB    1 
ATOM   8445  C  CG1   . VAL A 1 1286 ? 157.188 171.515 172.876 1.00 31.89  ? 2503 VAL A CG1   1 
ATOM   8446  C  CG2   . VAL A 1 1286 ? 157.338 171.845 170.397 1.00 30.23  ? 2503 VAL A CG2   1 
ATOM   8447  N  N     . LEU A 1 1287 ? 154.930 173.801 169.494 1.00 23.11  ? 2504 LEU A N     1 
ATOM   8448  C  CA    . LEU A 1 1287 ? 154.556 174.802 168.496 1.00 22.80  ? 2504 LEU A CA    1 
ATOM   8449  C  C     . LEU A 1 1287 ? 153.384 175.652 168.974 1.00 23.46  ? 2504 LEU A C     1 
ATOM   8450  O  O     . LEU A 1 1287 ? 153.337 176.860 168.705 1.00 25.01  ? 2504 LEU A O     1 
ATOM   8451  C  CB    . LEU A 1 1287 ? 154.239 174.139 167.154 1.00 24.01  ? 2504 LEU A CB    1 
ATOM   8452  C  CG    . LEU A 1 1287 ? 155.380 173.842 166.171 1.00 26.73  ? 2504 LEU A CG    1 
ATOM   8453  C  CD1   . LEU A 1 1287 ? 155.991 175.160 165.721 1.00 30.31  ? 2504 LEU A CD1   1 
ATOM   8454  C  CD2   . LEU A 1 1287 ? 156.459 172.925 166.726 1.00 33.37  ? 2504 LEU A CD2   1 
ATOM   8455  N  N     . PHE A 1 1288 ? 152.434 175.046 169.694 1.00 21.88  ? 2505 PHE A N     1 
ATOM   8456  C  CA    . PHE A 1 1288 ? 151.362 175.827 170.309 1.00 19.37  ? 2505 PHE A CA    1 
ATOM   8457  C  C     . PHE A 1 1288 ? 151.918 176.831 171.317 1.00 20.68  ? 2505 PHE A C     1 
ATOM   8458  O  O     . PHE A 1 1288 ? 151.501 177.999 171.347 1.00 22.97  ? 2505 PHE A O     1 
ATOM   8459  C  CB    . PHE A 1 1288 ? 150.365 174.881 170.977 1.00 18.85  ? 2505 PHE A CB    1 
ATOM   8460  C  CG    . PHE A 1 1288 ? 149.155 175.562 171.542 1.00 20.56  ? 2505 PHE A CG    1 
ATOM   8461  C  CD1   . PHE A 1 1288 ? 148.364 176.368 170.745 1.00 26.81  ? 2505 PHE A CD1   1 
ATOM   8462  C  CD2   . PHE A 1 1288 ? 148.792 175.373 172.864 1.00 23.77  ? 2505 PHE A CD2   1 
ATOM   8463  C  CE1   . PHE A 1 1288 ? 147.238 176.984 171.255 1.00 27.88  ? 2505 PHE A CE1   1 
ATOM   8464  C  CE2   . PHE A 1 1288 ? 147.668 175.991 173.383 1.00 27.25  ? 2505 PHE A CE2   1 
ATOM   8465  C  CZ    . PHE A 1 1288 ? 146.890 176.798 172.575 1.00 28.34  ? 2505 PHE A CZ    1 
ATOM   8466  N  N     . LEU A 1 1289 ? 152.876 176.392 172.138 1.00 18.97  ? 2506 LEU A N     1 
ATOM   8467  C  CA    . LEU A 1 1289 ? 153.511 177.287 173.100 1.00 16.65  ? 2506 LEU A CA    1 
ATOM   8468  C  C     . LEU A 1 1289 ? 154.249 178.415 172.395 1.00 17.11  ? 2506 LEU A C     1 
ATOM   8469  O  O     . LEU A 1 1289 ? 154.196 179.569 172.833 1.00 17.86  ? 2506 LEU A O     1 
ATOM   8470  C  CB    . LEU A 1 1289 ? 154.472 176.507 173.998 1.00 16.93  ? 2506 LEU A CB    1 
ATOM   8471  C  CG    . LEU A 1 1289 ? 153.870 175.479 174.954 1.00 19.39  ? 2506 LEU A CG    1 
ATOM   8472  C  CD1   . LEU A 1 1289 ? 154.942 174.878 175.855 1.00 20.25  ? 2506 LEU A CD1   1 
ATOM   8473  C  CD2   . LEU A 1 1289 ? 152.762 176.112 175.772 1.00 16.39  ? 2506 LEU A CD2   1 
ATOM   8474  N  N     . ARG A 1 1290 ? 154.944 178.098 171.301 1.00 16.46  ? 2507 ARG A N     1 
ATOM   8475  C  CA    . ARG A 1 1290 ? 155.626 179.127 170.525 1.00 15.57  ? 2507 ARG A CA    1 
ATOM   8476  C  C     . ARG A 1 1290 ? 154.631 180.135 169.974 1.00 14.75  ? 2507 ARG A C     1 
ATOM   8477  O  O     . ARG A 1 1290 ? 154.910 181.340 169.946 1.00 14.64  ? 2507 ARG A O     1 
ATOM   8478  C  CB    . ARG A 1 1290 ? 156.424 178.489 169.389 1.00 14.90  ? 2507 ARG A CB    1 
ATOM   8479  C  CG    . ARG A 1 1290 ? 157.218 179.482 168.556 1.00 13.07  ? 2507 ARG A CG    1 
ATOM   8480  C  CD    . ARG A 1 1290 ? 157.751 178.852 167.277 1.00 14.36  ? 2507 ARG A CD    1 
ATOM   8481  N  NE    . ARG A 1 1290 ? 157.028 179.308 166.096 1.00 14.08  ? 2507 ARG A NE    1 
ATOM   8482  C  CZ    . ARG A 1 1290 ? 157.310 180.418 165.428 1.00 14.30  ? 2507 ARG A CZ    1 
ATOM   8483  N  NH1   . ARG A 1 1290 ? 158.284 181.226 165.810 1.00 14.91  ? 2507 ARG A NH1   1 
ATOM   8484  N  NH2   . ARG A 1 1290 ? 156.592 180.729 164.354 1.00 15.22  ? 2507 ARG A NH2   1 
ATOM   8485  N  N     . GLN A 1 1291 ? 153.460 179.659 169.543 1.00 16.36  ? 2508 GLN A N     1 
ATOM   8486  C  CA    . GLN A 1 1291 ? 152.432 180.562 169.040 1.00 17.21  ? 2508 GLN A CA    1 
ATOM   8487  C  C     . GLN A 1 1291 ? 151.933 181.506 170.128 1.00 15.88  ? 2508 GLN A C     1 
ATOM   8488  O  O     . GLN A 1 1291 ? 151.733 182.699 169.874 1.00 16.88  ? 2508 GLN A O     1 
ATOM   8489  C  CB    . GLN A 1 1291 ? 151.272 179.766 168.445 1.00 17.82  ? 2508 GLN A CB    1 
ATOM   8490  C  CG    . GLN A 1 1291 ? 150.120 180.632 167.968 1.00 22.40  ? 2508 GLN A CG    1 
ATOM   8491  C  CD    . GLN A 1 1291 ? 149.241 179.942 166.949 1.00 29.83  ? 2508 GLN A CD    1 
ATOM   8492  O  OE1   . GLN A 1 1291 ? 149.166 180.361 165.795 1.00 34.40  ? 2508 GLN A OE1   1 
ATOM   8493  N  NE2   . GLN A 1 1291 ? 148.563 178.881 167.371 1.00 31.14  ? 2508 GLN A NE2   1 
ATOM   8494  N  N     . LEU A 1 1292 ? 151.722 180.997 171.347 1.00 14.27  ? 2509 LEU A N     1 
ATOM   8495  C  CA    . LEU A 1 1292 ? 151.306 181.900 172.425 1.00 15.69  ? 2509 LEU A CA    1 
ATOM   8496  C  C     . LEU A 1 1292 ? 152.398 182.893 172.812 1.00 16.74  ? 2509 LEU A C     1 
ATOM   8497  O  O     . LEU A 1 1292 ? 152.114 184.081 172.993 1.00 14.23  ? 2509 LEU A O     1 
ATOM   8498  C  CB    . LEU A 1 1292 ? 150.830 181.143 173.665 1.00 13.70  ? 2509 LEU A CB    1 
ATOM   8499  C  CG    . LEU A 1 1292 ? 149.395 180.613 173.695 1.00 16.52  ? 2509 LEU A CG    1 
ATOM   8500  C  CD1   . LEU A 1 1292 ? 149.168 179.453 172.791 1.00 18.51  ? 2509 LEU A CD1   1 
ATOM   8501  C  CD2   . LEU A 1 1292 ? 148.998 180.270 175.125 1.00 18.26  ? 2509 LEU A CD2   1 
ATOM   8502  N  N     . MET A 1 1293 ? 153.647 182.445 172.954 1.00 18.55  ? 2510 MET A N     1 
ATOM   8503  C  CA    . MET A 1 1293 ? 154.660 183.382 173.442 1.00 14.87  ? 2510 MET A CA    1 
ATOM   8504  C  C     . MET A 1 1293 ? 155.107 184.384 172.383 1.00 14.76  ? 2510 MET A C     1 
ATOM   8505  O  O     . MET A 1 1293 ? 155.409 185.532 172.727 1.00 12.53  ? 2510 MET A O     1 
ATOM   8506  C  CB    . MET A 1 1293 ? 155.876 182.649 174.018 1.00 11.40  ? 2510 MET A CB    1 
ATOM   8507  C  CG    . MET A 1 1293 ? 155.554 181.428 174.844 1.00 10.90  ? 2510 MET A CG    1 
ATOM   8508  S  SD    . MET A 1 1293 ? 156.995 180.401 175.146 1.00 11.71  ? 2510 MET A SD    1 
ATOM   8509  C  CE    . MET A 1 1293 ? 158.155 181.649 175.680 1.00 10.68  ? 2510 MET A CE    1 
ATOM   8510  N  N     . GLU A 1 1294 ? 155.160 183.998 171.108 1.00 14.41  ? 2511 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 1294 ? 155.596 184.958 170.098 1.00 14.06  ? 2511 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 1294 ? 154.461 185.883 169.674 1.00 16.68  ? 2511 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 1294 ? 154.554 187.105 169.825 1.00 16.89  ? 2511 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 1294 ? 156.174 184.240 168.878 1.00 15.43  ? 2511 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 1294 ? 156.658 185.218 167.815 1.00 17.90  ? 2511 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 1294 ? 157.384 184.552 166.667 1.00 18.75  ? 2511 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 1294 ? 157.460 183.307 166.647 1.00 16.82  ? 2511 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 1294 ? 157.887 185.280 165.786 1.00 18.25  ? 2511 GLU A OE2   1 
ATOM   8519  N  N     . LYS A 1 1295 ? 153.382 185.317 169.137 1.00 17.12  ? 2512 LYS A N     1 
ATOM   8520  C  CA    . LYS A 1 1295 ? 152.337 186.107 168.500 1.00 18.80  ? 2512 LYS A CA    1 
ATOM   8521  C  C     . LYS A 1 1295 ? 151.223 186.533 169.448 1.00 18.79  ? 2512 LYS A C     1 
ATOM   8522  O  O     . LYS A 1 1295 ? 150.366 187.324 169.038 1.00 21.70  ? 2512 LYS A O     1 
ATOM   8523  C  CB    . LYS A 1 1295 ? 151.743 185.327 167.325 1.00 18.31  ? 2512 LYS A CB    1 
ATOM   8524  C  CG    . LYS A 1 1295 ? 152.785 184.888 166.313 1.00 17.78  ? 2512 LYS A CG    1 
ATOM   8525  C  CD    . LYS A 1 1295 ? 152.336 183.668 165.537 1.00 20.69  ? 2512 LYS A CD    1 
ATOM   8526  C  CE    . LYS A 1 1295 ? 153.512 183.003 164.850 1.00 18.85  ? 2512 LYS A CE    1 
ATOM   8527  N  NZ    . LYS A 1 1295 ? 154.466 182.425 165.830 1.00 19.82  ? 2512 LYS A NZ    1 
ATOM   8528  N  N     . GLN A 1 1296 ? 151.220 186.039 170.689 1.00 17.29  ? 2513 GLN A N     1 
ATOM   8529  C  CA    . GLN A 1 1296 ? 150.250 186.418 171.723 1.00 16.63  ? 2513 GLN A CA    1 
ATOM   8530  C  C     . GLN A 1 1296 ? 148.812 186.144 171.275 1.00 19.05  ? 2513 GLN A C     1 
ATOM   8531  O  O     . GLN A 1 1296 ? 147.990 187.050 171.136 1.00 24.33  ? 2513 GLN A O     1 
ATOM   8532  C  CB    . GLN A 1 1296 ? 150.432 187.881 172.140 1.00 14.31  ? 2513 GLN A CB    1 
ATOM   8533  C  CG    . GLN A 1 1296 ? 151.800 188.192 172.711 1.00 14.59  ? 2513 GLN A CG    1 
ATOM   8534  C  CD    . GLN A 1 1296 ? 152.002 187.594 174.087 1.00 16.47  ? 2513 GLN A CD    1 
ATOM   8535  O  OE1   . GLN A 1 1296 ? 151.348 187.989 175.049 1.00 19.49  ? 2513 GLN A OE1   1 
ATOM   8536  N  NE2   . GLN A 1 1296 ? 152.909 186.630 174.185 1.00 18.08  ? 2513 GLN A NE2   1 
ATOM   8537  N  N     . GLY A 1 1297 ? 148.525 184.874 171.050 1.00 16.66  ? 2514 GLY A N     1 
ATOM   8538  C  CA    . GLY A 1 1297 ? 147.188 184.465 170.672 1.00 20.88  ? 2514 GLY A CA    1 
ATOM   8539  C  C     . GLY A 1 1297 ? 147.215 183.122 169.980 1.00 23.83  ? 2514 GLY A C     1 
ATOM   8540  O  O     . GLY A 1 1297 ? 148.268 182.524 169.774 1.00 27.91  ? 2514 GLY A O     1 
ATOM   8541  N  N     . PHE A 1 1298 ? 146.019 182.656 169.627 1.00 26.04  ? 2515 PHE A N     1 
ATOM   8542  C  CA    . PHE A 1 1298 ? 145.879 181.393 168.915 1.00 33.35  ? 2515 PHE A CA    1 
ATOM   8543  C  C     . PHE A 1 1298 ? 144.567 181.393 168.145 1.00 36.16  ? 2515 PHE A C     1 
ATOM   8544  O  O     . PHE A 1 1298 ? 143.647 182.156 168.447 1.00 34.70  ? 2515 PHE A O     1 
ATOM   8545  C  CB    . PHE A 1 1298 ? 145.952 180.191 169.868 1.00 32.80  ? 2515 PHE A CB    1 
ATOM   8546  C  CG    . PHE A 1 1298 ? 144.723 179.999 170.715 1.00 37.09  ? 2515 PHE A CG    1 
ATOM   8547  C  CD1   . PHE A 1 1298 ? 144.414 180.886 171.734 1.00 34.82  ? 2515 PHE A CD1   1 
ATOM   8548  C  CD2   . PHE A 1 1298 ? 143.880 178.921 170.498 1.00 39.24  ? 2515 PHE A CD2   1 
ATOM   8549  C  CE1   . PHE A 1 1298 ? 143.289 180.703 172.514 1.00 33.49  ? 2515 PHE A CE1   1 
ATOM   8550  C  CE2   . PHE A 1 1298 ? 142.751 178.735 171.275 1.00 37.50  ? 2515 PHE A CE2   1 
ATOM   8551  C  CZ    . PHE A 1 1298 ? 142.457 179.627 172.283 1.00 32.81  ? 2515 PHE A CZ    1 
ATOM   8552  N  N     . TRP A 1 1299 ? 144.500 180.523 167.139 1.00 39.68  ? 2516 TRP A N     1 
ATOM   8553  C  CA    . TRP A 1 1299 ? 143.302 180.354 166.327 1.00 40.15  ? 2516 TRP A CA    1 
ATOM   8554  C  C     . TRP A 1 1299 ? 142.378 179.333 166.978 1.00 45.69  ? 2516 TRP A C     1 
ATOM   8555  O  O     . TRP A 1 1299 ? 142.803 178.215 167.290 1.00 46.69  ? 2516 TRP A O     1 
ATOM   8556  C  CB    . TRP A 1 1299 ? 143.659 179.897 164.911 1.00 43.25  ? 2516 TRP A CB    1 
ATOM   8557  C  CG    . TRP A 1 1299 ? 144.353 180.924 164.070 1.00 38.36  ? 2516 TRP A CG    1 
ATOM   8558  C  CD1   . TRP A 1 1299 ? 145.632 180.869 163.603 1.00 34.34  ? 2516 TRP A CD1   1 
ATOM   8559  C  CD2   . TRP A 1 1299 ? 143.797 182.147 163.573 1.00 35.43  ? 2516 TRP A CD2   1 
ATOM   8560  N  NE1   . TRP A 1 1299 ? 145.913 181.987 162.859 1.00 30.96  ? 2516 TRP A NE1   1 
ATOM   8561  C  CE2   . TRP A 1 1299 ? 144.803 182.787 162.824 1.00 30.40  ? 2516 TRP A CE2   1 
ATOM   8562  C  CE3   . TRP A 1 1299 ? 142.551 182.766 163.693 1.00 39.54  ? 2516 TRP A CE3   1 
ATOM   8563  C  CZ2   . TRP A 1 1299 ? 144.601 184.015 162.200 1.00 29.22  ? 2516 TRP A CZ2   1 
ATOM   8564  C  CZ3   . TRP A 1 1299 ? 142.352 183.984 163.072 1.00 38.75  ? 2516 TRP A CZ3   1 
ATOM   8565  C  CH2   . TRP A 1 1299 ? 143.372 184.595 162.335 1.00 34.71  ? 2516 TRP A CH2   1 
ATOM   8566  N  N     . LYS A 1 1300 ? 141.121 179.720 167.185 1.00 46.73  ? 2517 LYS A N     1 
ATOM   8567  C  CA    . LYS A 1 1300 ? 140.120 178.780 167.670 1.00 46.16  ? 2517 LYS A CA    1 
ATOM   8568  C  C     . LYS A 1 1300 ? 139.870 177.702 166.625 1.00 53.31  ? 2517 LYS A C     1 
ATOM   8569  O  O     . LYS A 1 1300 ? 139.683 178.002 165.443 1.00 55.67  ? 2517 LYS A O     1 
ATOM   8570  C  CB    . LYS A 1 1300 ? 138.817 179.508 167.987 1.00 47.91  ? 2517 LYS A CB    1 
ATOM   8571  C  CG    . LYS A 1 1300 ? 138.581 179.787 169.456 1.00 44.78  ? 2517 LYS A CG    1 
ATOM   8572  C  CD    . LYS A 1 1300 ? 137.318 180.607 169.640 1.00 43.13  ? 2517 LYS A CD    1 
ATOM   8573  C  CE    . LYS A 1 1300 ? 137.210 181.158 171.046 1.00 41.72  ? 2517 LYS A CE    1 
ATOM   8574  N  NZ    . LYS A 1 1300 ? 136.612 182.519 171.041 1.00 42.26  ? 2517 LYS A NZ    1 
ATOM   8575  N  N     . THR A 1 1301 ? 139.875 176.447 167.054 1.00 57.67  ? 2518 THR A N     1 
ATOM   8576  C  CA    . THR A 1 1301 ? 139.585 175.365 166.119 1.00 62.34  ? 2518 THR A CA    1 
ATOM   8577  C  C     . THR A 1 1301 ? 138.121 175.238 165.666 1.00 65.49  ? 2518 THR A C     1 
ATOM   8578  O  O     . THR A 1 1301 ? 137.911 174.815 164.522 1.00 62.78  ? 2518 THR A O     1 
ATOM   8579  C  CB    . THR A 1 1301 ? 140.104 174.025 166.673 1.00 67.19  ? 2518 THR A CB    1 
ATOM   8580  O  OG1   . THR A 1 1301 ? 139.730 172.957 165.792 1.00 71.72  ? 2518 THR A OG1   1 
ATOM   8581  C  CG2   . THR A 1 1301 ? 139.637 173.733 168.096 1.00 64.87  ? 2518 THR A CG2   1 
ATOM   8582  N  N     . PRO A 1 1302 ? 137.080 175.560 166.453 1.00 68.62  ? 2519 PRO A N     1 
ATOM   8583  C  CA    . PRO A 1 1302 ? 135.726 175.470 165.893 1.00 71.69  ? 2519 PRO A CA    1 
ATOM   8584  C  C     . PRO A 1 1302 ? 135.176 176.756 165.294 1.00 65.96  ? 2519 PRO A C     1 
ATOM   8585  O  O     . PRO A 1 1302 ? 134.163 176.694 164.583 1.00 68.00  ? 2519 PRO A O     1 
ATOM   8586  C  CB    . PRO A 1 1302 ? 134.896 175.047 167.110 1.00 72.67  ? 2519 PRO A CB    1 
ATOM   8587  C  CG    . PRO A 1 1302 ? 135.521 175.780 168.219 1.00 63.40  ? 2519 PRO A CG    1 
ATOM   8588  C  CD    . PRO A 1 1302 ? 136.988 175.954 167.878 1.00 62.03  ? 2519 PRO A CD    1 
ATOM   8589  N  N     . GLU A 1 1303 ? 135.798 177.908 165.550 1.00 58.76  ? 2520 GLU A N     1 
ATOM   8590  C  CA    . GLU A 1 1303 ? 135.273 179.190 165.105 1.00 55.05  ? 2520 GLU A CA    1 
ATOM   8591  C  C     . GLU A 1 1303 ? 136.241 179.996 164.253 1.00 54.15  ? 2520 GLU A C     1 
ATOM   8592  O  O     . GLU A 1 1303 ? 135.793 180.916 163.559 1.00 52.62  ? 2520 GLU A O     1 
ATOM   8593  C  CB    . GLU A 1 1303 ? 134.856 180.045 166.312 1.00 52.32  ? 2520 GLU A CB    1 
ATOM   8594  C  CG    . GLU A 1 1303 ? 133.675 180.963 166.054 1.00 55.34  ? 2520 GLU A CG    1 
ATOM   8595  C  CD    . GLU A 1 1303 ? 133.399 181.889 167.220 1.00 56.90  ? 2520 GLU A CD    1 
ATOM   8596  O  OE1   . GLU A 1 1303 ? 134.108 181.784 168.242 1.00 61.30  ? 2520 GLU A OE1   1 
ATOM   8597  O  OE2   . GLU A 1 1303 ? 132.472 182.719 167.118 1.00 52.47  ? 2520 GLU A OE2   1 
ATOM   8598  N  N     . ASN A 1 1304 ? 137.540 179.684 164.292 1.00 54.12  ? 2521 ASN A N     1 
ATOM   8599  C  CA    . ASN A 1 1304 ? 138.574 180.374 163.518 1.00 51.32  ? 2521 ASN A CA    1 
ATOM   8600  C  C     . ASN A 1 1304 ? 138.600 181.872 163.835 1.00 52.12  ? 2521 ASN A C     1 
ATOM   8601  O  O     . ASN A 1 1304 ? 138.363 182.725 162.978 1.00 58.00  ? 2521 ASN A O     1 
ATOM   8602  C  CB    . ASN A 1 1304 ? 138.398 180.119 162.017 1.00 57.60  ? 2521 ASN A CB    1 
ATOM   8603  C  CG    . ASN A 1 1304 ? 138.245 178.646 161.695 1.00 64.24  ? 2521 ASN A CG    1 
ATOM   8604  O  OD1   . ASN A 1 1304 ? 138.847 177.793 162.344 1.00 67.38  ? 2521 ASN A OD1   1 
ATOM   8605  N  ND2   . ASN A 1 1304 ? 137.433 178.340 160.690 1.00 66.41  ? 2521 ASN A ND2   1 
ATOM   8606  N  N     . LYS A 1 1305 ? 138.896 182.174 165.097 1.00 49.33  ? 2522 LYS A N     1 
ATOM   8607  C  CA    . LYS A 1 1305 ? 138.996 183.543 165.578 1.00 48.19  ? 2522 LYS A CA    1 
ATOM   8608  C  C     . LYS A 1 1305 ? 140.292 183.712 166.356 1.00 45.54  ? 2522 LYS A C     1 
ATOM   8609  O  O     . LYS A 1 1305 ? 140.811 182.759 166.943 1.00 46.67  ? 2522 LYS A O     1 
ATOM   8610  C  CB    . LYS A 1 1305 ? 137.801 183.918 166.464 1.00 50.10  ? 2522 LYS A CB    1 
ATOM   8611  C  CG    . LYS A 1 1305 ? 136.470 183.965 165.729 1.00 51.98  ? 2522 LYS A CG    1 
ATOM   8612  C  CD    . LYS A 1 1305 ? 136.514 184.933 164.558 1.00 54.38  ? 2522 LYS A CD    1 
ATOM   8613  C  CE    . LYS A 1 1305 ? 135.193 184.954 163.807 1.00 53.40  ? 2522 LYS A CE    1 
ATOM   8614  N  NZ    . LYS A 1 1305 ? 135.139 186.055 162.807 1.00 53.45  ? 2522 LYS A NZ    1 
ATOM   8615  N  N     . TRP A 1 1306 ? 140.810 184.938 166.357 1.00 41.45  ? 2523 TRP A N     1 
ATOM   8616  C  CA    . TRP A 1 1306 ? 142.093 185.245 166.981 1.00 38.79  ? 2523 TRP A CA    1 
ATOM   8617  C  C     . TRP A 1 1306 ? 141.849 185.659 168.426 1.00 39.21  ? 2523 TRP A C     1 
ATOM   8618  O  O     . TRP A 1 1306 ? 141.350 186.758 168.690 1.00 41.75  ? 2523 TRP A O     1 
ATOM   8619  C  CB    . TRP A 1 1306 ? 142.816 186.344 166.208 1.00 35.95  ? 2523 TRP A CB    1 
ATOM   8620  C  CG    . TRP A 1 1306 ? 144.211 186.603 166.685 1.00 32.28  ? 2523 TRP A CG    1 
ATOM   8621  C  CD1   . TRP A 1 1306 ? 144.683 187.749 167.254 1.00 30.11  ? 2523 TRP A CD1   1 
ATOM   8622  C  CD2   . TRP A 1 1306 ? 145.320 185.699 166.622 1.00 30.39  ? 2523 TRP A CD2   1 
ATOM   8623  N  NE1   . TRP A 1 1306 ? 146.016 187.613 167.554 1.00 26.33  ? 2523 TRP A NE1   1 
ATOM   8624  C  CE2   . TRP A 1 1306 ? 146.431 186.363 167.175 1.00 27.47  ? 2523 TRP A CE2   1 
ATOM   8625  C  CE3   . TRP A 1 1306 ? 145.481 184.392 166.152 1.00 32.22  ? 2523 TRP A CE3   1 
ATOM   8626  C  CZ2   . TRP A 1 1306 ? 147.682 185.765 167.272 1.00 28.07  ? 2523 TRP A CZ2   1 
ATOM   8627  C  CZ3   . TRP A 1 1306 ? 146.725 183.802 166.249 1.00 30.57  ? 2523 TRP A CZ3   1 
ATOM   8628  C  CH2   . TRP A 1 1306 ? 147.808 184.486 166.804 1.00 28.03  ? 2523 TRP A CH2   1 
ATOM   8629  N  N     . VAL A 1 1307 ? 142.208 184.786 169.360 1.00 37.22  ? 2524 VAL A N     1 
ATOM   8630  C  CA    . VAL A 1 1307 ? 141.942 184.989 170.779 1.00 34.86  ? 2524 VAL A CA    1 
ATOM   8631  C  C     . VAL A 1 1307 ? 143.193 185.617 171.382 1.00 32.79  ? 2524 VAL A C     1 
ATOM   8632  O  O     . VAL A 1 1307 ? 144.164 184.923 171.693 1.00 34.92  ? 2524 VAL A O     1 
ATOM   8633  C  CB    . VAL A 1 1307 ? 141.570 183.677 171.473 1.00 34.46  ? 2524 VAL A CB    1 
ATOM   8634  C  CG1   . VAL A 1 1307 ? 141.380 183.896 172.959 1.00 37.63  ? 2524 VAL A CG1   1 
ATOM   8635  C  CG2   . VAL A 1 1307 ? 140.322 183.085 170.849 1.00 35.64  ? 2524 VAL A CG2   1 
ATOM   8636  N  N     . THR A 1 1308 ? 143.170 186.937 171.546 1.00 28.04  ? 2525 THR A N     1 
ATOM   8637  C  CA    . THR A 1 1308 ? 144.341 187.663 172.018 1.00 28.72  ? 2525 THR A CA    1 
ATOM   8638  C  C     . THR A 1 1308 ? 144.641 187.336 173.477 1.00 32.22  ? 2525 THR A C     1 
ATOM   8639  O  O     . THR A 1 1308 ? 143.737 187.253 174.311 1.00 38.85  ? 2525 THR A O     1 
ATOM   8640  C  CB    . THR A 1 1308 ? 144.126 189.167 171.853 1.00 32.68  ? 2525 THR A CB    1 
ATOM   8641  O  OG1   . THR A 1 1308 ? 143.653 189.437 170.529 1.00 38.93  ? 2525 THR A OG1   1 
ATOM   8642  C  CG2   . THR A 1 1308 ? 145.425 189.925 172.072 1.00 29.27  ? 2525 THR A CG2   1 
ATOM   8643  N  N     . ILE A 1 1309 ? 145.924 187.146 173.777 1.00 29.78  ? 2526 ILE A N     1 
ATOM   8644  C  CA    . ILE A 1 1309 ? 146.404 186.890 175.131 1.00 25.71  ? 2526 ILE A CA    1 
ATOM   8645  C  C     . ILE A 1 1309 ? 146.840 188.214 175.740 1.00 26.03  ? 2526 ILE A C     1 
ATOM   8646  O  O     . ILE A 1 1309 ? 147.571 188.985 175.106 1.00 26.68  ? 2526 ILE A O     1 
ATOM   8647  C  CB    . ILE A 1 1309 ? 147.561 185.878 175.125 1.00 22.00  ? 2526 ILE A CB    1 
ATOM   8648  C  CG1   . ILE A 1 1309 ? 147.116 184.565 174.484 1.00 25.05  ? 2526 ILE A CG1   1 
ATOM   8649  C  CG2   . ILE A 1 1309 ? 148.077 185.638 176.529 1.00 22.31  ? 2526 ILE A CG2   1 
ATOM   8650  C  CD1   . ILE A 1 1309 ? 145.962 183.911 175.189 1.00 29.04  ? 2526 ILE A CD1   1 
ATOM   8651  N  N     . GLU A 1 1310 ? 146.394 188.486 176.964 1.00 26.20  ? 2527 GLU A N     1 
ATOM   8652  C  CA    . GLU A 1 1310 ? 146.705 189.743 177.633 1.00 30.39  ? 2527 GLU A CA    1 
ATOM   8653  C  C     . GLU A 1 1310 ? 147.592 189.575 178.857 1.00 34.16  ? 2527 GLU A C     1 
ATOM   8654  O  O     . GLU A 1 1310 ? 148.631 190.234 178.958 1.00 36.70  ? 2527 GLU A O     1 
ATOM   8655  C  CB    . GLU A 1 1310 ? 145.409 190.462 178.031 1.00 30.33  ? 2527 GLU A CB    1 
ATOM   8656  C  CG    . GLU A 1 1310 ? 144.639 191.034 176.856 1.00 37.26  ? 2527 GLU A CG    1 
ATOM   8657  C  CD    . GLU A 1 1310 ? 143.648 192.102 177.271 1.00 38.21  ? 2527 GLU A CD    1 
ATOM   8658  O  OE1   . GLU A 1 1310 ? 143.600 192.433 178.474 1.00 37.84  ? 2527 GLU A OE1   1 
ATOM   8659  O  OE2   . GLU A 1 1310 ? 142.916 192.608 176.395 1.00 34.24  ? 2527 GLU A OE2   1 
ATOM   8660  N  N     . ARG A 1 1311 ? 147.214 188.714 179.798 1.00 31.86  ? 2528 ARG A N     1 
ATOM   8661  C  CA    . ARG A 1 1311 ? 147.909 188.603 181.077 1.00 28.35  ? 2528 ARG A CA    1 
ATOM   8662  C  C     . ARG A 1 1311 ? 148.163 187.144 181.434 1.00 25.68  ? 2528 ARG A C     1 
ATOM   8663  O  O     . ARG A 1 1311 ? 147.897 186.699 182.552 1.00 28.42  ? 2528 ARG A O     1 
ATOM   8664  C  CB    . ARG A 1 1311 ? 147.118 189.294 182.183 1.00 28.39  ? 2528 ARG A CB    1 
ATOM   8665  C  CG    . ARG A 1 1311 ? 147.085 190.809 182.075 1.00 29.54  ? 2528 ARG A CG    1 
ATOM   8666  C  CD    . ARG A 1 1311 ? 146.277 191.422 183.204 1.00 31.20  ? 2528 ARG A CD    1 
ATOM   8667  N  NE    . ARG A 1 1311 ? 145.028 190.706 183.429 1.00 29.81  ? 2528 ARG A NE    1 
ATOM   8668  C  CZ    . ARG A 1 1311 ? 144.625 190.263 184.611 1.00 28.89  ? 2528 ARG A CZ    1 
ATOM   8669  N  NH1   . ARG A 1 1311 ? 145.348 190.451 185.702 1.00 30.85  ? 2528 ARG A NH1   1 
ATOM   8670  N  NH2   . ARG A 1 1311 ? 143.466 189.616 184.701 1.00 29.88  ? 2528 ARG A NH2   1 
ATOM   8671  N  N     . ILE A 1 1312 ? 148.680 186.371 180.484 1.00 24.32  ? 2529 ILE A N     1 
ATOM   8672  C  CA    . ILE A 1 1312 ? 149.021 184.972 180.715 1.00 24.13  ? 2529 ILE A CA    1 
ATOM   8673  C  C     . ILE A 1 1312 ? 150.485 184.770 180.350 1.00 24.43  ? 2529 ILE A C     1 
ATOM   8674  O  O     . ILE A 1 1312 ? 150.894 185.064 179.220 1.00 27.01  ? 2529 ILE A O     1 
ATOM   8675  C  CB    . ILE A 1 1312 ? 148.119 184.021 179.914 1.00 22.83  ? 2529 ILE A CB    1 
ATOM   8676  C  CG1   . ILE A 1 1312 ? 146.700 184.037 180.481 1.00 23.53  ? 2529 ILE A CG1   1 
ATOM   8677  C  CG2   . ILE A 1 1312 ? 148.678 182.608 179.935 1.00 17.57  ? 2529 ILE A CG2   1 
ATOM   8678  C  CD1   . ILE A 1 1312 ? 145.748 183.126 179.752 1.00 27.17  ? 2529 ILE A CD1   1 
ATOM   8679  N  N     . HIS A 1 1313 ? 151.268 184.273 181.303 1.00 19.38  ? 2530 HIS A N     1 
ATOM   8680  C  CA    . HIS A 1 1313 ? 152.670 183.952 181.090 1.00 19.22  ? 2530 HIS A CA    1 
ATOM   8681  C  C     . HIS A 1 1313 ? 152.852 182.447 180.937 1.00 18.53  ? 2530 HIS A C     1 
ATOM   8682  O  O     . HIS A 1 1313 ? 152.008 181.649 181.350 1.00 19.67  ? 2530 HIS A O     1 
ATOM   8683  C  CB    . HIS A 1 1313 ? 153.533 184.460 182.246 1.00 14.83  ? 2530 HIS A CB    1 
ATOM   8684  C  CG    . HIS A 1 1313 ? 153.529 185.948 182.399 1.00 14.64  ? 2530 HIS A CG    1 
ATOM   8685  N  ND1   . HIS A 1 1313 ? 152.884 186.587 183.435 1.00 18.28  ? 2530 HIS A ND1   1 
ATOM   8686  C  CD2   . HIS A 1 1313 ? 154.095 186.923 181.650 1.00 17.19  ? 2530 HIS A CD2   1 
ATOM   8687  C  CE1   . HIS A 1 1313 ? 153.053 187.892 183.318 1.00 20.28  ? 2530 HIS A CE1   1 
ATOM   8688  N  NE2   . HIS A 1 1313 ? 153.783 188.122 182.242 1.00 17.68  ? 2530 HIS A NE2   1 
ATOM   8689  N  N     . ILE A 1 1314 ? 153.976 182.069 180.335 1.00 14.20  ? 2531 ILE A N     1 
ATOM   8690  C  CA    . ILE A 1 1314 ? 154.333 180.671 180.132 1.00 14.16  ? 2531 ILE A CA    1 
ATOM   8691  C  C     . ILE A 1 1314 ? 155.742 180.456 180.660 1.00 15.48  ? 2531 ILE A C     1 
ATOM   8692  O  O     . ILE A 1 1314 ? 156.673 181.162 180.260 1.00 19.45  ? 2531 ILE A O     1 
ATOM   8693  C  CB    . ILE A 1 1314 ? 154.244 180.264 178.648 1.00 14.16  ? 2531 ILE A CB    1 
ATOM   8694  C  CG1   . ILE A 1 1314 ? 152.789 180.050 178.238 1.00 14.88  ? 2531 ILE A CG1   1 
ATOM   8695  C  CG2   . ILE A 1 1314 ? 155.049 179.003 178.380 1.00 11.53  ? 2531 ILE A CG2   1 
ATOM   8696  C  CD1   . ILE A 1 1314 ? 152.605 179.838 176.755 1.00 16.38  ? 2531 ILE A CD1   1 
ATOM   8697  N  N     . VAL A 1 1315 ? 155.895 179.490 181.565 1.00 15.05  ? 2532 VAL A N     1 
ATOM   8698  C  CA    . VAL A 1 1315 ? 157.199 179.068 182.052 1.00 13.55  ? 2532 VAL A CA    1 
ATOM   8699  C  C     . VAL A 1 1315 ? 157.293 177.558 181.898 1.00 12.73  ? 2532 VAL A C     1 
ATOM   8700  O  O     . VAL A 1 1315 ? 156.286 176.855 181.797 1.00 17.12  ? 2532 VAL A O     1 
ATOM   8701  C  CB    . VAL A 1 1315 ? 157.453 179.474 183.517 1.00 13.95  ? 2532 VAL A CB    1 
ATOM   8702  C  CG1   . VAL A 1 1315 ? 157.351 180.976 183.682 1.00 14.35  ? 2532 VAL A CG1   1 
ATOM   8703  C  CG2   . VAL A 1 1315 ? 156.480 178.777 184.419 1.00 14.76  ? 2532 VAL A CG2   1 
ATOM   8704  N  N     . GLY A 1 1316 ? 158.525 177.059 181.873 1.00 9.60   ? 2533 GLY A N     1 
ATOM   8705  C  CA    . GLY A 1 1316 ? 158.753 175.646 181.669 1.00 10.98  ? 2533 GLY A CA    1 
ATOM   8706  C  C     . GLY A 1 1316 ? 159.786 175.111 182.638 1.00 14.12  ? 2533 GLY A C     1 
ATOM   8707  O  O     . GLY A 1 1316 ? 160.581 175.856 183.212 1.00 16.74  ? 2533 GLY A O     1 
ATOM   8708  N  N     . ALA A 1 1317 ? 159.756 173.793 182.808 1.00 15.27  ? 2534 ALA A N     1 
ATOM   8709  C  CA    . ALA A 1 1317 ? 160.711 173.109 183.677 1.00 13.59  ? 2534 ALA A CA    1 
ATOM   8710  C  C     . ALA A 1 1317 ? 160.842 171.676 183.197 1.00 16.72  ? 2534 ALA A C     1 
ATOM   8711  O  O     . ALA A 1 1317 ? 159.926 170.874 183.399 1.00 22.95  ? 2534 ALA A O     1 
ATOM   8712  C  CB    . ALA A 1 1317 ? 160.260 173.150 185.134 1.00 14.55  ? 2534 ALA A CB    1 
ATOM   8713  N  N     . CYS A 1 1318 ? 161.975 171.347 182.587 1.00 16.73  ? 2535 CYS A N     1 
ATOM   8714  C  CA    . CYS A 1 1318 ? 162.135 170.046 181.963 1.00 21.30  ? 2535 CYS A CA    1 
ATOM   8715  C  C     . CYS A 1 1318 ? 163.540 169.526 182.218 1.00 26.40  ? 2535 CYS A C     1 
ATOM   8716  O  O     . CYS A 1 1318 ? 164.486 170.300 182.375 1.00 30.36  ? 2535 CYS A O     1 
ATOM   8717  C  CB    . CYS A 1 1318 ? 161.860 170.122 180.460 1.00 25.93  ? 2535 CYS A CB    1 
ATOM   8718  S  SG    . CYS A 1 1318 ? 163.081 171.077 179.533 1.00 29.55  ? 2535 CYS A SG    1 
ATOM   8719  N  N     . ASN A 1 1319 ? 163.663 168.202 182.257 1.00 28.91  ? 2536 ASN A N     1 
ATOM   8720  C  CA    . ASN A 1 1319 ? 164.957 167.566 182.414 1.00 29.63  ? 2536 ASN A CA    1 
ATOM   8721  C  C     . ASN A 1 1319 ? 165.788 167.767 181.147 1.00 33.02  ? 2536 ASN A C     1 
ATOM   8722  O  O     . ASN A 1 1319 ? 165.239 168.057 180.081 1.00 33.85  ? 2536 ASN A O     1 
ATOM   8723  C  CB    . ASN A 1 1319 ? 164.771 166.081 182.719 1.00 33.31  ? 2536 ASN A CB    1 
ATOM   8724  C  CG    . ASN A 1 1319 ? 163.839 165.842 183.891 1.00 38.73  ? 2536 ASN A CG    1 
ATOM   8725  O  OD1   . ASN A 1 1319 ? 163.468 166.775 184.601 1.00 38.93  ? 2536 ASN A OD1   1 
ATOM   8726  N  ND2   . ASN A 1 1319 ? 163.461 164.588 184.103 1.00 45.95  ? 2536 ASN A ND2   1 
ATOM   8727  N  N     . PRO A 1 1320 ? 167.114 167.660 181.247 1.00 33.04  ? 2537 PRO A N     1 
ATOM   8728  C  CA    . PRO A 1 1320 ? 167.952 167.869 180.069 1.00 35.52  ? 2537 PRO A CA    1 
ATOM   8729  C  C     . PRO A 1 1320 ? 167.638 166.853 178.989 1.00 41.50  ? 2537 PRO A C     1 
ATOM   8730  O  O     . PRO A 1 1320 ? 167.219 165.718 179.282 1.00 46.13  ? 2537 PRO A O     1 
ATOM   8731  C  CB    . PRO A 1 1320 ? 169.376 167.689 180.614 1.00 41.69  ? 2537 PRO A CB    1 
ATOM   8732  C  CG    . PRO A 1 1320 ? 169.272 168.071 182.036 1.00 35.38  ? 2537 PRO A CG    1 
ATOM   8733  C  CD    . PRO A 1 1320 ? 167.922 167.590 182.479 1.00 34.19  ? 2537 PRO A CD    1 
ATOM   8734  N  N     . PRO A 1 1321 ? 167.814 167.225 177.716 1.00 42.48  ? 2538 PRO A N     1 
ATOM   8735  C  CA    . PRO A 1 1321 ? 167.410 166.329 176.619 1.00 45.67  ? 2538 PRO A CA    1 
ATOM   8736  C  C     . PRO A 1 1321 ? 168.262 165.077 176.485 1.00 48.36  ? 2538 PRO A C     1 
ATOM   8737  O  O     . PRO A 1 1321 ? 167.876 164.172 175.735 1.00 50.61  ? 2538 PRO A O     1 
ATOM   8738  C  CB    . PRO A 1 1321 ? 167.543 167.220 175.378 1.00 45.44  ? 2538 PRO A CB    1 
ATOM   8739  C  CG    . PRO A 1 1321 ? 168.592 168.214 175.751 1.00 46.65  ? 2538 PRO A CG    1 
ATOM   8740  C  CD    . PRO A 1 1321 ? 168.405 168.479 177.217 1.00 42.73  ? 2538 PRO A CD    1 
ATOM   8741  N  N     . THR A 1 1322 ? 169.403 164.995 177.172 1.00 44.97  ? 2539 THR A N     1 
ATOM   8742  C  CA    . THR A 1 1322 ? 170.253 163.815 177.066 1.00 46.62  ? 2539 THR A CA    1 
ATOM   8743  C  C     . THR A 1 1322 ? 169.683 162.614 177.809 1.00 49.96  ? 2539 THR A C     1 
ATOM   8744  O  O     . THR A 1 1322 ? 170.123 161.486 177.561 1.00 51.85  ? 2539 THR A O     1 
ATOM   8745  C  CB    . THR A 1 1322 ? 171.654 164.123 177.596 1.00 51.81  ? 2539 THR A CB    1 
ATOM   8746  O  OG1   . THR A 1 1322 ? 171.628 164.145 179.028 1.00 50.72  ? 2539 THR A OG1   1 
ATOM   8747  C  CG2   . THR A 1 1322 ? 172.130 165.473 177.083 1.00 51.92  ? 2539 THR A CG2   1 
ATOM   8748  N  N     . ASP A 1 1323 ? 168.726 162.825 178.709 1.00 48.36  ? 2540 ASP A N     1 
ATOM   8749  C  CA    . ASP A 1 1323 ? 168.162 161.729 179.475 1.00 49.12  ? 2540 ASP A CA    1 
ATOM   8750  C  C     . ASP A 1 1323 ? 167.266 160.861 178.594 1.00 52.02  ? 2540 ASP A C     1 
ATOM   8751  O  O     . ASP A 1 1323 ? 166.773 161.309 177.557 1.00 54.34  ? 2540 ASP A O     1 
ATOM   8752  C  CB    . ASP A 1 1323 ? 167.368 162.264 180.663 1.00 46.14  ? 2540 ASP A CB    1 
ATOM   8753  C  CG    . ASP A 1 1323 ? 168.248 162.946 181.691 1.00 50.09  ? 2540 ASP A CG    1 
ATOM   8754  O  OD1   . ASP A 1 1323 ? 167.873 162.958 182.882 1.00 49.89  ? 2540 ASP A OD1   1 
ATOM   8755  O  OD2   . ASP A 1 1323 ? 169.314 163.471 181.307 1.00 50.30  ? 2540 ASP A OD2   1 
ATOM   8756  N  N     . PRO A 1 1324 ? 167.057 159.604 178.981 1.00 55.05  ? 2541 PRO A N     1 
ATOM   8757  C  CA    . PRO A 1 1324 ? 166.193 158.726 178.186 1.00 59.86  ? 2541 PRO A CA    1 
ATOM   8758  C  C     . PRO A 1 1324 ? 164.733 159.142 178.265 1.00 55.23  ? 2541 PRO A C     1 
ATOM   8759  O  O     . PRO A 1 1324 ? 164.260 159.657 179.281 1.00 55.34  ? 2541 PRO A O     1 
ATOM   8760  C  CB    . PRO A 1 1324 ? 166.410 157.347 178.819 1.00 62.40  ? 2541 PRO A CB    1 
ATOM   8761  N  N     . GLY A 1 1325 ? 164.016 158.904 177.169 1.00 53.28  ? 2542 GLY A N     1 
ATOM   8762  C  CA    . GLY A 1 1325 ? 162.611 159.245 177.091 1.00 51.10  ? 2542 GLY A CA    1 
ATOM   8763  C  C     . GLY A 1 1325 ? 162.315 160.699 176.804 1.00 50.46  ? 2542 GLY A C     1 
ATOM   8764  O  O     . GLY A 1 1325 ? 161.155 161.112 176.918 1.00 51.53  ? 2542 GLY A O     1 
ATOM   8765  N  N     . ARG A 1 1326 ? 163.322 161.489 176.438 1.00 52.33  ? 2543 ARG A N     1 
ATOM   8766  C  CA    . ARG A 1 1326 ? 163.159 162.911 176.184 1.00 48.04  ? 2543 ARG A CA    1 
ATOM   8767  C  C     . ARG A 1 1326 ? 163.603 163.230 174.764 1.00 51.07  ? 2543 ARG A C     1 
ATOM   8768  O  O     . ARG A 1 1326 ? 164.517 162.598 174.226 1.00 55.30  ? 2543 ARG A O     1 
ATOM   8769  C  CB    . ARG A 1 1326 ? 163.967 163.749 177.178 1.00 41.46  ? 2543 ARG A CB    1 
ATOM   8770  C  CG    . ARG A 1 1326 ? 164.175 163.072 178.518 1.00 44.13  ? 2543 ARG A CG    1 
ATOM   8771  C  CD    . ARG A 1 1326 ? 164.383 164.077 179.625 1.00 44.04  ? 2543 ARG A CD    1 
ATOM   8772  N  NE    . ARG A 1 1326 ? 163.137 164.690 180.061 1.00 42.18  ? 2543 ARG A NE    1 
ATOM   8773  C  CZ    . ARG A 1 1326 ? 162.356 164.192 181.009 1.00 42.74  ? 2543 ARG A CZ    1 
ATOM   8774  N  NH1   . ARG A 1 1326 ? 162.642 163.049 181.609 1.00 44.24  ? 2543 ARG A NH1   1 
ATOM   8775  N  NH2   . ARG A 1 1326 ? 161.268 164.863 181.372 1.00 38.73  ? 2543 ARG A NH2   1 
ATOM   8776  N  N     . ILE A 1 1327 ? 162.949 164.217 174.161 1.00 47.04  ? 2544 ILE A N     1 
ATOM   8777  C  CA    . ILE A 1 1327 ? 163.201 164.618 172.784 1.00 48.47  ? 2544 ILE A CA    1 
ATOM   8778  C  C     . ILE A 1 1327 ? 163.482 166.115 172.776 1.00 47.49  ? 2544 ILE A C     1 
ATOM   8779  O  O     . ILE A 1 1327 ? 162.701 166.880 173.343 1.00 45.65  ? 2544 ILE A O     1 
ATOM   8780  C  CB    . ILE A 1 1327 ? 162.022 164.286 171.851 1.00 51.25  ? 2544 ILE A CB    1 
ATOM   8781  C  CG1   . ILE A 1 1327 ? 162.018 162.791 171.523 1.00 57.04  ? 2544 ILE A CG1   1 
ATOM   8782  C  CG2   . ILE A 1 1327 ? 162.100 165.098 170.574 1.00 55.28  ? 2544 ILE A CG2   1 
ATOM   8783  C  CD1   . ILE A 1 1327 ? 160.744 162.309 170.867 1.00 59.91  ? 2544 ILE A CD1   1 
ATOM   8784  N  N     . PRO A 1 1328 ? 164.583 166.568 172.170 1.00 45.75  ? 2545 PRO A N     1 
ATOM   8785  C  CA    . PRO A 1 1328 ? 164.896 168.003 172.174 1.00 41.71  ? 2545 PRO A CA    1 
ATOM   8786  C  C     . PRO A 1 1328 ? 163.859 168.815 171.414 1.00 37.30  ? 2545 PRO A C     1 
ATOM   8787  O  O     . PRO A 1 1328 ? 163.270 168.356 170.433 1.00 37.38  ? 2545 PRO A O     1 
ATOM   8788  C  CB    . PRO A 1 1328 ? 166.267 168.071 171.487 1.00 44.72  ? 2545 PRO A CB    1 
ATOM   8789  C  CG    . PRO A 1 1328 ? 166.803 166.674 171.533 1.00 41.99  ? 2545 PRO A CG    1 
ATOM   8790  C  CD    . PRO A 1 1328 ? 165.610 165.781 171.472 1.00 42.89  ? 2545 PRO A CD    1 
ATOM   8791  N  N     . MET A 1 1329 ? 163.645 170.040 171.881 1.00 33.35  ? 2546 MET A N     1 
ATOM   8792  C  CA    . MET A 1 1329 ? 162.638 170.923 171.318 1.00 30.80  ? 2546 MET A CA    1 
ATOM   8793  C  C     . MET A 1 1329 ? 163.232 171.806 170.227 1.00 26.88  ? 2546 MET A C     1 
ATOM   8794  O  O     . MET A 1 1329 ? 164.448 171.982 170.124 1.00 29.07  ? 2546 MET A O     1 
ATOM   8795  C  CB    . MET A 1 1329 ? 162.020 171.793 172.409 1.00 24.61  ? 2546 MET A CB    1 
ATOM   8796  C  CG    . MET A 1 1329 ? 161.149 171.028 173.377 1.00 29.07  ? 2546 MET A CG    1 
ATOM   8797  S  SD    . MET A 1 1329 ? 160.822 171.986 174.859 1.00 32.78  ? 2546 MET A SD    1 
ATOM   8798  C  CE    . MET A 1 1329 ? 162.487 172.432 175.344 1.00 23.93  ? 2546 MET A CE    1 
ATOM   8799  N  N     . SER A 1 1330 ? 162.345 172.359 169.405 1.00 22.95  ? 2547 SER A N     1 
ATOM   8800  C  CA    . SER A 1 1330 ? 162.763 173.260 168.342 1.00 21.42  ? 2547 SER A CA    1 
ATOM   8801  C  C     . SER A 1 1330 ? 163.282 174.564 168.928 1.00 15.06  ? 2547 SER A C     1 
ATOM   8802  O  O     . SER A 1 1330 ? 162.720 175.101 169.886 1.00 14.36  ? 2547 SER A O     1 
ATOM   8803  C  CB    . SER A 1 1330 ? 161.601 173.535 167.390 1.00 23.31  ? 2547 SER A CB    1 
ATOM   8804  O  OG    . SER A 1 1330 ? 160.479 174.036 168.094 1.00 23.19  ? 2547 SER A OG    1 
ATOM   8805  N  N     . GLU A 1 1331 ? 164.368 175.074 168.345 1.00 12.93  ? 2548 GLU A N     1 
ATOM   8806  C  CA    . GLU A 1 1331 ? 165.000 176.278 168.869 1.00 11.24  ? 2548 GLU A CA    1 
ATOM   8807  C  C     . GLU A 1 1331 ? 164.159 177.518 168.595 1.00 10.14  ? 2548 GLU A C     1 
ATOM   8808  O  O     . GLU A 1 1331 ? 164.315 178.524 169.296 1.00 10.26  ? 2548 GLU A O     1 
ATOM   8809  C  CB    . GLU A 1 1331 ? 166.409 176.402 168.276 1.00 10.02  ? 2548 GLU A CB    1 
ATOM   8810  C  CG    . GLU A 1 1331 ? 167.407 177.238 169.077 1.00 9.85   ? 2548 GLU A CG    1 
ATOM   8811  C  CD    . GLU A 1 1331 ? 167.283 178.728 168.860 1.00 12.61  ? 2548 GLU A CD    1 
ATOM   8812  O  OE1   . GLU A 1 1331 ? 166.658 179.139 167.866 1.00 11.37  ? 2548 GLU A OE1   1 
ATOM   8813  O  OE2   . GLU A 1 1331 ? 167.820 179.493 169.685 1.00 16.39  ? 2548 GLU A OE2   1 
ATOM   8814  N  N     . ARG A 1 1332 ? 163.240 177.446 167.623 1.00 10.40  ? 2549 ARG A N     1 
ATOM   8815  C  CA    . ARG A 1 1332 ? 162.325 178.552 167.354 1.00 10.02  ? 2549 ARG A CA    1 
ATOM   8816  C  C     . ARG A 1 1332 ? 161.458 178.874 168.562 1.00 10.16  ? 2549 ARG A C     1 
ATOM   8817  O  O     . ARG A 1 1332 ? 161.023 180.018 168.727 1.00 11.56  ? 2549 ARG A O     1 
ATOM   8818  C  CB    . ARG A 1 1332 ? 161.426 178.217 166.163 1.00 13.47  ? 2549 ARG A CB    1 
ATOM   8819  C  CG    . ARG A 1 1332 ? 162.148 177.740 164.921 1.00 16.72  ? 2549 ARG A CG    1 
ATOM   8820  C  CD    . ARG A 1 1332 ? 161.178 177.582 163.762 1.00 16.98  ? 2549 ARG A CD    1 
ATOM   8821  N  NE    . ARG A 1 1332 ? 161.041 178.810 162.991 1.00 13.92  ? 2549 ARG A NE    1 
ATOM   8822  C  CZ    . ARG A 1 1332 ? 159.931 179.183 162.368 1.00 15.54  ? 2549 ARG A CZ    1 
ATOM   8823  N  NH1   . ARG A 1 1332 ? 158.834 178.446 162.411 1.00 18.81  ? 2549 ARG A NH1   1 
ATOM   8824  N  NH2   . ARG A 1 1332 ? 159.921 180.325 161.690 1.00 17.09  ? 2549 ARG A NH2   1 
ATOM   8825  N  N     . PHE A 1 1333 ? 161.189 177.882 169.408 1.00 10.66  ? 2550 PHE A N     1 
ATOM   8826  C  CA    . PHE A 1 1333 ? 160.422 178.098 170.625 1.00 10.57  ? 2550 PHE A CA    1 
ATOM   8827  C  C     . PHE A 1 1333 ? 161.317 178.505 171.792 1.00 10.17  ? 2550 PHE A C     1 
ATOM   8828  O  O     . PHE A 1 1333 ? 161.009 179.467 172.502 1.00 10.54  ? 2550 PHE A O     1 
ATOM   8829  C  CB    . PHE A 1 1333 ? 159.625 176.836 170.965 1.00 10.83  ? 2550 PHE A CB    1 
ATOM   8830  C  CG    . PHE A 1 1333 ? 159.399 176.636 172.432 1.00 9.52   ? 2550 PHE A CG    1 
ATOM   8831  C  CD1   . PHE A 1 1333 ? 158.483 177.408 173.121 1.00 9.90   ? 2550 PHE A CD1   1 
ATOM   8832  C  CD2   . PHE A 1 1333 ? 160.102 175.666 173.122 1.00 12.28  ? 2550 PHE A CD2   1 
ATOM   8833  C  CE1   . PHE A 1 1333 ? 158.280 177.221 174.466 1.00 12.24  ? 2550 PHE A CE1   1 
ATOM   8834  C  CE2   . PHE A 1 1333 ? 159.902 175.477 174.468 1.00 12.94  ? 2550 PHE A CE2   1 
ATOM   8835  C  CZ    . PHE A 1 1333 ? 158.989 176.255 175.141 1.00 12.39  ? 2550 PHE A CZ    1 
ATOM   8836  N  N     . THR A 1 1334 ? 162.429 177.791 172.002 1.00 10.08  ? 2551 THR A N     1 
ATOM   8837  C  CA    . THR A 1 1334 ? 163.297 178.081 173.139 1.00 10.36  ? 2551 THR A CA    1 
ATOM   8838  C  C     . THR A 1 1334 ? 164.016 179.416 173.008 1.00 10.34  ? 2551 THR A C     1 
ATOM   8839  O  O     . THR A 1 1334 ? 164.544 179.915 174.006 1.00 12.11  ? 2551 THR A O     1 
ATOM   8840  C  CB    . THR A 1 1334 ? 164.332 176.970 173.338 1.00 7.94   ? 2551 THR A CB    1 
ATOM   8841  O  OG1   . THR A 1 1334 ? 165.031 176.734 172.112 1.00 10.42  ? 2551 THR A OG1   1 
ATOM   8842  C  CG2   . THR A 1 1334 ? 163.662 175.688 173.791 1.00 8.83   ? 2551 THR A CG2   1 
ATOM   8843  N  N     . ARG A 1 1335 ? 164.058 180.008 171.813 1.00 8.74   ? 2552 ARG A N     1 
ATOM   8844  C  CA    . ARG A 1 1335 ? 164.621 181.346 171.704 1.00 7.93   ? 2552 ARG A CA    1 
ATOM   8845  C  C     . ARG A 1 1335 ? 163.696 182.413 172.268 1.00 8.55   ? 2552 ARG A C     1 
ATOM   8846  O  O     . ARG A 1 1335 ? 164.135 183.553 172.450 1.00 9.44   ? 2552 ARG A O     1 
ATOM   8847  C  CB    . ARG A 1 1335 ? 164.958 181.671 170.249 1.00 8.44   ? 2552 ARG A CB    1 
ATOM   8848  C  CG    . ARG A 1 1335 ? 163.754 181.901 169.363 1.00 10.17  ? 2552 ARG A CG    1 
ATOM   8849  C  CD    . ARG A 1 1335 ? 164.162 182.518 168.039 1.00 8.40   ? 2552 ARG A CD    1 
ATOM   8850  N  NE    . ARG A 1 1335 ? 164.295 183.964 168.143 1.00 6.76   ? 2552 ARG A NE    1 
ATOM   8851  C  CZ    . ARG A 1 1335 ? 163.324 184.823 167.871 1.00 5.87   ? 2552 ARG A CZ    1 
ATOM   8852  N  NH1   . ARG A 1 1335 ? 162.139 184.415 167.452 1.00 7.62   ? 2552 ARG A NH1   1 
ATOM   8853  N  NH2   . ARG A 1 1335 ? 163.548 186.124 168.024 1.00 5.51   ? 2552 ARG A NH2   1 
ATOM   8854  N  N     . HIS A 1 1336 ? 162.439 182.074 172.550 1.00 9.17   ? 2553 HIS A N     1 
ATOM   8855  C  CA    . HIS A 1 1336 ? 161.480 183.005 173.126 1.00 10.71  ? 2553 HIS A CA    1 
ATOM   8856  C  C     . HIS A 1 1336 ? 161.407 182.925 174.644 1.00 10.51  ? 2553 HIS A C     1 
ATOM   8857  O  O     . HIS A 1 1336 ? 160.661 183.697 175.253 1.00 9.14   ? 2553 HIS A O     1 
ATOM   8858  C  CB    . HIS A 1 1336 ? 160.087 182.755 172.543 1.00 7.82   ? 2553 HIS A CB    1 
ATOM   8859  C  CG    . HIS A 1 1336 ? 159.911 183.285 171.157 1.00 7.68   ? 2553 HIS A CG    1 
ATOM   8860  N  ND1   . HIS A 1 1336 ? 159.661 182.470 170.075 1.00 10.22  ? 2553 HIS A ND1   1 
ATOM   8861  C  CD2   . HIS A 1 1336 ? 159.951 184.549 170.676 1.00 8.94   ? 2553 HIS A CD2   1 
ATOM   8862  C  CE1   . HIS A 1 1336 ? 159.555 183.209 168.986 1.00 10.65  ? 2553 HIS A CE1   1 
ATOM   8863  N  NE2   . HIS A 1 1336 ? 159.725 184.475 169.323 1.00 11.03  ? 2553 HIS A NE2   1 
ATOM   8864  N  N     . ALA A 1 1337 ? 162.163 182.024 175.267 1.00 9.21   ? 2554 ALA A N     1 
ATOM   8865  C  CA    . ALA A 1 1337 ? 162.100 181.813 176.706 1.00 8.58   ? 2554 ALA A CA    1 
ATOM   8866  C  C     . ALA A 1 1337 ? 163.499 181.876 177.292 1.00 8.68   ? 2554 ALA A C     1 
ATOM   8867  O  O     . ALA A 1 1337 ? 164.407 181.192 176.812 1.00 8.97   ? 2554 ALA A O     1 
ATOM   8868  C  CB    . ALA A 1 1337 ? 161.452 180.466 177.036 1.00 10.66  ? 2554 ALA A CB    1 
ATOM   8869  N  N     . ALA A 1 1338 ? 163.668 182.696 178.326 1.00 9.21   ? 2555 ALA A N     1 
ATOM   8870  C  CA    . ALA A 1 1338 ? 164.930 182.749 179.049 1.00 10.71  ? 2555 ALA A CA    1 
ATOM   8871  C  C     . ALA A 1 1338 ? 165.164 181.433 179.771 1.00 11.78  ? 2555 ALA A C     1 
ATOM   8872  O  O     . ALA A 1 1338 ? 164.259 180.901 180.416 1.00 12.99  ? 2555 ALA A O     1 
ATOM   8873  C  CB    . ALA A 1 1338 ? 164.921 183.900 180.048 1.00 10.20  ? 2555 ALA A CB    1 
ATOM   8874  N  N     . ILE A 1 1339 ? 166.375 180.901 179.669 1.00 12.06  ? 2556 ILE A N     1 
ATOM   8875  C  CA    . ILE A 1 1339 ? 166.680 179.575 180.187 1.00 12.67  ? 2556 ILE A CA    1 
ATOM   8876  C  C     . ILE A 1 1339 ? 167.523 179.725 181.443 1.00 16.01  ? 2556 ILE A C     1 
ATOM   8877  O  O     . ILE A 1 1339 ? 168.594 180.343 181.415 1.00 19.92  ? 2556 ILE A O     1 
ATOM   8878  C  CB    . ILE A 1 1339 ? 167.387 178.706 179.139 1.00 15.37  ? 2556 ILE A CB    1 
ATOM   8879  C  CG1   . ILE A 1 1339 ? 166.480 178.524 177.928 1.00 14.26  ? 2556 ILE A CG1   1 
ATOM   8880  C  CG2   . ILE A 1 1339 ? 167.729 177.352 179.720 1.00 16.18  ? 2556 ILE A CG2   1 
ATOM   8881  C  CD1   . ILE A 1 1339 ? 167.137 177.822 176.790 1.00 19.59  ? 2556 ILE A CD1   1 
ATOM   8882  N  N     . LEU A 1 1340 ? 167.033 179.163 182.543 1.00 14.63  ? 2557 LEU A N     1 
ATOM   8883  C  CA    . LEU A 1 1340 ? 167.769 179.076 183.792 1.00 15.25  ? 2557 LEU A CA    1 
ATOM   8884  C  C     . LEU A 1 1340 ? 168.150 177.625 184.049 1.00 13.55  ? 2557 LEU A C     1 
ATOM   8885  O  O     . LEU A 1 1340 ? 167.412 176.702 183.699 1.00 13.57  ? 2557 LEU A O     1 
ATOM   8886  C  CB    . LEU A 1 1340 ? 166.946 179.609 184.970 1.00 13.60  ? 2557 LEU A CB    1 
ATOM   8887  C  CG    . LEU A 1 1340 ? 166.289 180.984 184.858 1.00 10.76  ? 2557 LEU A CG    1 
ATOM   8888  C  CD1   . LEU A 1 1340 ? 165.374 181.219 186.044 1.00 9.16   ? 2557 LEU A CD1   1 
ATOM   8889  C  CD2   . LEU A 1 1340 ? 167.340 182.073 184.774 1.00 12.77  ? 2557 LEU A CD2   1 
ATOM   8890  N  N     . TYR A 1 1341 ? 169.312 177.432 184.660 1.00 14.93  ? 2558 TYR A N     1 
ATOM   8891  C  CA    . TYR A 1 1341 ? 169.802 176.108 185.013 1.00 18.49  ? 2558 TYR A CA    1 
ATOM   8892  C  C     . TYR A 1 1341 ? 169.751 175.928 186.523 1.00 22.02  ? 2558 TYR A C     1 
ATOM   8893  O  O     . TYR A 1 1341 ? 170.208 176.797 187.274 1.00 21.88  ? 2558 TYR A O     1 
ATOM   8894  C  CB    . TYR A 1 1341 ? 171.223 175.891 184.490 1.00 21.56  ? 2558 TYR A CB    1 
ATOM   8895  C  CG    . TYR A 1 1341 ? 171.845 174.594 184.945 1.00 20.77  ? 2558 TYR A CG    1 
ATOM   8896  C  CD1   . TYR A 1 1341 ? 171.550 173.401 184.308 1.00 21.39  ? 2558 TYR A CD1   1 
ATOM   8897  C  CD2   . TYR A 1 1341 ? 172.760 174.570 185.989 1.00 23.49  ? 2558 TYR A CD2   1 
ATOM   8898  C  CE1   . TYR A 1 1341 ? 172.116 172.215 184.723 1.00 23.89  ? 2558 TYR A CE1   1 
ATOM   8899  C  CE2   . TYR A 1 1341 ? 173.339 173.389 186.403 1.00 23.56  ? 2558 TYR A CE2   1 
ATOM   8900  C  CZ    . TYR A 1 1341 ? 173.014 172.215 185.763 1.00 24.64  ? 2558 TYR A CZ    1 
ATOM   8901  O  OH    . TYR A 1 1341 ? 173.587 171.032 186.168 1.00 28.51  ? 2558 TYR A OH    1 
ATOM   8902  N  N     . LEU A 1 1342 ? 169.194 174.801 186.961 1.00 21.77  ? 2559 LEU A N     1 
ATOM   8903  C  CA    . LEU A 1 1342 ? 169.028 174.480 188.377 1.00 19.67  ? 2559 LEU A CA    1 
ATOM   8904  C  C     . LEU A 1 1342 ? 169.803 173.202 188.673 1.00 22.87  ? 2559 LEU A C     1 
ATOM   8905  O  O     . LEU A 1 1342 ? 169.293 172.099 188.460 1.00 24.04  ? 2559 LEU A O     1 
ATOM   8906  C  CB    . LEU A 1 1342 ? 167.555 174.318 188.738 1.00 14.14  ? 2559 LEU A CB    1 
ATOM   8907  C  CG    . LEU A 1 1342 ? 166.683 175.568 188.798 1.00 13.46  ? 2559 LEU A CG    1 
ATOM   8908  C  CD1   . LEU A 1 1342 ? 166.133 175.897 187.430 1.00 16.76  ? 2559 LEU A CD1   1 
ATOM   8909  C  CD2   . LEU A 1 1342 ? 165.554 175.371 189.792 1.00 12.85  ? 2559 LEU A CD2   1 
ATOM   8910  N  N     . GLY A 1 1343 ? 171.027 173.345 189.168 1.00 25.53  ? 2560 GLY A N     1 
ATOM   8911  C  CA    . GLY A 1 1343 ? 171.804 172.201 189.586 1.00 24.33  ? 2560 GLY A CA    1 
ATOM   8912  C  C     . GLY A 1 1343 ? 171.426 171.750 190.981 1.00 23.08  ? 2560 GLY A C     1 
ATOM   8913  O  O     . GLY A 1 1343 ? 170.593 172.348 191.661 1.00 21.48  ? 2560 GLY A O     1 
ATOM   8914  N  N     . TYR A 1 1344 ? 172.049 170.657 191.406 1.00 24.36  ? 2561 TYR A N     1 
ATOM   8915  C  CA    . TYR A 1 1344 ? 171.829 170.171 192.758 1.00 24.84  ? 2561 TYR A CA    1 
ATOM   8916  C  C     . TYR A 1 1344 ? 172.444 171.143 193.763 1.00 25.55  ? 2561 TYR A C     1 
ATOM   8917  O  O     . TYR A 1 1344 ? 173.524 171.688 193.515 1.00 30.17  ? 2561 TYR A O     1 
ATOM   8918  C  CB    . TYR A 1 1344 ? 172.430 168.780 192.937 1.00 25.38  ? 2561 TYR A CB    1 
ATOM   8919  C  CG    . TYR A 1 1344 ? 171.582 167.667 192.365 1.00 25.47  ? 2561 TYR A CG    1 
ATOM   8920  C  CD1   . TYR A 1 1344 ? 170.338 167.367 192.903 1.00 24.61  ? 2561 TYR A CD1   1 
ATOM   8921  C  CD2   . TYR A 1 1344 ? 172.030 166.912 191.290 1.00 24.05  ? 2561 TYR A CD2   1 
ATOM   8922  C  CE1   . TYR A 1 1344 ? 169.563 166.351 192.384 1.00 25.77  ? 2561 TYR A CE1   1 
ATOM   8923  C  CE2   . TYR A 1 1344 ? 171.264 165.894 190.767 1.00 25.62  ? 2561 TYR A CE2   1 
ATOM   8924  C  CZ    . TYR A 1 1344 ? 170.032 165.619 191.316 1.00 28.49  ? 2561 TYR A CZ    1 
ATOM   8925  O  OH    . TYR A 1 1344 ? 169.268 164.604 190.793 1.00 35.31  ? 2561 TYR A OH    1 
ATOM   8926  N  N     . PRO A 1 1345 ? 171.776 171.395 194.887 1.00 26.10  ? 2562 PRO A N     1 
ATOM   8927  C  CA    . PRO A 1 1345 ? 172.321 172.332 195.876 1.00 31.26  ? 2562 PRO A CA    1 
ATOM   8928  C  C     . PRO A 1 1345 ? 173.614 171.822 196.490 1.00 37.19  ? 2562 PRO A C     1 
ATOM   8929  O  O     . PRO A 1 1345 ? 173.870 170.617 196.556 1.00 37.09  ? 2562 PRO A O     1 
ATOM   8930  C  CB    . PRO A 1 1345 ? 171.210 172.434 196.928 1.00 31.78  ? 2562 PRO A CB    1 
ATOM   8931  C  CG    . PRO A 1 1345 ? 170.328 171.259 196.693 1.00 28.77  ? 2562 PRO A CG    1 
ATOM   8932  C  CD    . PRO A 1 1345 ? 170.425 170.933 195.241 1.00 25.67  ? 2562 PRO A CD    1 
ATOM   8933  N  N     . SER A 1 1346 ? 174.441 172.767 196.933 1.00 43.80  ? 2563 SER A N     1 
ATOM   8934  C  CA    . SER A 1 1346 ? 175.751 172.442 197.474 1.00 48.56  ? 2563 SER A CA    1 
ATOM   8935  C  C     . SER A 1 1346 ? 175.620 171.765 198.839 1.00 47.74  ? 2563 SER A C     1 
ATOM   8936  O  O     . SER A 1 1346 ? 174.539 171.691 199.431 1.00 46.32  ? 2563 SER A O     1 
ATOM   8937  C  CB    . SER A 1 1346 ? 176.610 173.700 197.586 1.00 46.18  ? 2563 SER A CB    1 
ATOM   8938  O  OG    . SER A 1 1346 ? 177.223 174.010 196.347 1.00 45.05  ? 2563 SER A OG    1 
ATOM   8939  N  N     . GLY A 1 1347 ? 176.755 171.262 199.333 1.00 48.64  ? 2564 GLY A N     1 
ATOM   8940  C  CA    . GLY A 1 1347 ? 176.753 170.548 200.600 1.00 47.45  ? 2564 GLY A CA    1 
ATOM   8941  C  C     . GLY A 1 1347 ? 176.370 171.426 201.777 1.00 51.17  ? 2564 GLY A C     1 
ATOM   8942  O  O     . GLY A 1 1347 ? 175.715 170.967 202.715 1.00 48.84  ? 2564 GLY A O     1 
ATOM   8943  N  N     . LYS A 1 1348 ? 176.773 172.698 201.742 1.00 55.85  ? 2565 LYS A N     1 
ATOM   8944  C  CA    . LYS A 1 1348 ? 176.429 173.623 202.819 1.00 53.89  ? 2565 LYS A CA    1 
ATOM   8945  C  C     . LYS A 1 1348 ? 174.924 173.848 202.890 1.00 49.91  ? 2565 LYS A C     1 
ATOM   8946  O  O     . LYS A 1 1348 ? 174.316 173.756 203.965 1.00 51.09  ? 2565 LYS A O     1 
ATOM   8947  C  CB    . LYS A 1 1348 ? 177.159 174.950 202.613 1.00 55.03  ? 2565 LYS A CB    1 
ATOM   8948  C  CG    . LYS A 1 1348 ? 177.221 175.835 203.846 1.00 53.50  ? 2565 LYS A CG    1 
ATOM   8949  C  CD    . LYS A 1 1348 ? 177.852 177.182 203.523 1.00 62.41  ? 2565 LYS A CD    1 
ATOM   8950  C  CE    . LYS A 1 1348 ? 179.175 177.020 202.789 1.00 64.09  ? 2565 LYS A CE    1 
ATOM   8951  N  NZ    . LYS A 1 1348 ? 179.772 178.334 202.424 1.00 67.94  ? 2565 LYS A NZ    1 
ATOM   8952  N  N     . SER A 1 1349 ? 174.304 174.136 201.742 1.00 48.02  ? 2566 SER A N     1 
ATOM   8953  C  CA    . SER A 1 1349 ? 172.862 174.350 201.708 1.00 51.05  ? 2566 SER A CA    1 
ATOM   8954  C  C     . SER A 1 1349 ? 172.108 173.081 202.075 1.00 50.83  ? 2566 SER A C     1 
ATOM   8955  O  O     . SER A 1 1349 ? 171.104 173.137 202.794 1.00 51.64  ? 2566 SER A O     1 
ATOM   8956  C  CB    . SER A 1 1349 ? 172.437 174.846 200.326 1.00 47.17  ? 2566 SER A CB    1 
ATOM   8957  O  OG    . SER A 1 1349 ? 171.132 175.394 200.365 1.00 42.71  ? 2566 SER A OG    1 
ATOM   8958  N  N     . LEU A 1 1350 ? 172.580 171.928 201.594 1.00 46.40  ? 2567 LEU A N     1 
ATOM   8959  C  CA    . LEU A 1 1350 ? 171.945 170.657 201.932 1.00 44.80  ? 2567 LEU A CA    1 
ATOM   8960  C  C     . LEU A 1 1350 ? 171.991 170.408 203.435 1.00 47.34  ? 2567 LEU A C     1 
ATOM   8961  O  O     . LEU A 1 1350 ? 170.977 170.057 204.052 1.00 46.25  ? 2567 LEU A O     1 
ATOM   8962  C  CB    . LEU A 1 1350 ? 172.629 169.515 201.180 1.00 40.07  ? 2567 LEU A CB    1 
ATOM   8963  C  CG    . LEU A 1 1350 ? 172.128 169.184 199.774 1.00 32.16  ? 2567 LEU A CG    1 
ATOM   8964  C  CD1   . LEU A 1 1350 ? 172.788 167.919 199.258 1.00 28.94  ? 2567 LEU A CD1   1 
ATOM   8965  C  CD2   . LEU A 1 1350 ? 170.619 169.043 199.758 1.00 31.45  ? 2567 LEU A CD2   1 
ATOM   8966  N  N     . SER A 1 1351 ? 173.162 170.610 204.043 1.00 46.56  ? 2568 SER A N     1 
ATOM   8967  C  CA    . SER A 1 1351 ? 173.296 170.397 205.478 1.00 45.67  ? 2568 SER A CA    1 
ATOM   8968  C  C     . SER A 1 1351 ? 172.429 171.370 206.262 1.00 45.37  ? 2568 SER A C     1 
ATOM   8969  O  O     . SER A 1 1351 ? 171.848 170.997 207.284 1.00 48.25  ? 2568 SER A O     1 
ATOM   8970  C  CB    . SER A 1 1351 ? 174.761 170.519 205.893 1.00 49.52  ? 2568 SER A CB    1 
ATOM   8971  O  OG    . SER A 1 1351 ? 175.521 169.443 205.371 1.00 52.61  ? 2568 SER A OG    1 
ATOM   8972  N  N     . GLN A 1 1352 ? 172.303 172.612 205.784 1.00 44.88  ? 2569 GLN A N     1 
ATOM   8973  C  CA    . GLN A 1 1352 ? 171.446 173.586 206.459 1.00 47.53  ? 2569 GLN A CA    1 
ATOM   8974  C  C     . GLN A 1 1352 ? 169.974 173.178 206.397 1.00 48.90  ? 2569 GLN A C     1 
ATOM   8975  O  O     . GLN A 1 1352 ? 169.267 173.193 207.418 1.00 51.03  ? 2569 GLN A O     1 
ATOM   8976  C  CB    . GLN A 1 1352 ? 171.654 174.968 205.839 1.00 44.49  ? 2569 GLN A CB    1 
ATOM   8977  C  CG    . GLN A 1 1352 ? 170.521 175.945 206.080 1.00 50.56  ? 2569 GLN A CG    1 
ATOM   8978  C  CD    . GLN A 1 1352 ? 170.829 177.325 205.540 1.00 53.47  ? 2569 GLN A CD    1 
ATOM   8979  O  OE1   . GLN A 1 1352 ? 171.943 177.591 205.090 1.00 56.98  ? 2569 GLN A OE1   1 
ATOM   8980  N  NE2   . GLN A 1 1352 ? 169.841 178.211 205.579 1.00 47.85  ? 2569 GLN A NE2   1 
ATOM   8981  N  N     . ILE A 1 1353 ? 169.499 172.796 205.207 1.00 44.87  ? 2570 ILE A N     1 
ATOM   8982  C  CA    . ILE A 1 1353 ? 168.104 172.384 205.055 1.00 42.24  ? 2570 ILE A CA    1 
ATOM   8983  C  C     . ILE A 1 1353 ? 167.809 171.178 205.933 1.00 46.06  ? 2570 ILE A C     1 
ATOM   8984  O  O     . ILE A 1 1353 ? 166.784 171.126 206.627 1.00 47.43  ? 2570 ILE A O     1 
ATOM   8985  C  CB    . ILE A 1 1353 ? 167.780 172.088 203.579 1.00 41.02  ? 2570 ILE A CB    1 
ATOM   8986  C  CG1   . ILE A 1 1353 ? 167.953 173.332 202.718 1.00 41.63  ? 2570 ILE A CG1   1 
ATOM   8987  C  CG2   . ILE A 1 1353 ? 166.361 171.568 203.437 1.00 39.57  ? 2570 ILE A CG2   1 
ATOM   8988  C  CD1   . ILE A 1 1353 ? 168.268 173.011 201.279 1.00 37.17  ? 2570 ILE A CD1   1 
ATOM   8989  N  N     . TYR A 1 1354 ? 168.711 170.200 205.944 1.00 44.05  ? 2571 TYR A N     1 
ATOM   8990  C  CA    . TYR A 1 1354 ? 168.390 168.987 206.676 1.00 42.54  ? 2571 TYR A CA    1 
ATOM   8991  C  C     . TYR A 1 1354 ? 168.698 169.087 208.165 1.00 45.70  ? 2571 TYR A C     1 
ATOM   8992  O  O     . TYR A 1 1354 ? 168.130 168.317 208.940 1.00 48.48  ? 2571 TYR A O     1 
ATOM   8993  C  CB    . TYR A 1 1354 ? 169.076 167.797 206.009 1.00 36.24  ? 2571 TYR A CB    1 
ATOM   8994  C  CG    . TYR A 1 1354 ? 168.419 167.516 204.676 1.00 33.58  ? 2571 TYR A CG    1 
ATOM   8995  C  CD1   . TYR A 1 1354 ? 167.120 167.035 204.614 1.00 33.82  ? 2571 TYR A CD1   1 
ATOM   8996  C  CD2   . TYR A 1 1354 ? 169.069 167.788 203.483 1.00 35.59  ? 2571 TYR A CD2   1 
ATOM   8997  C  CE1   . TYR A 1 1354 ? 166.500 166.805 203.402 1.00 32.11  ? 2571 TYR A CE1   1 
ATOM   8998  C  CE2   . TYR A 1 1354 ? 168.458 167.563 202.267 1.00 33.01  ? 2571 TYR A CE2   1 
ATOM   8999  C  CZ    . TYR A 1 1354 ? 167.175 167.072 202.233 1.00 30.08  ? 2571 TYR A CZ    1 
ATOM   9000  O  OH    . TYR A 1 1354 ? 166.569 166.842 201.023 1.00 28.64  ? 2571 TYR A OH    1 
ATOM   9001  N  N     . GLU A 1 1355 ? 169.491 170.069 208.610 1.00 44.17  ? 2572 GLU A N     1 
ATOM   9002  C  CA    . GLU A 1 1355 ? 169.522 170.316 210.047 1.00 45.28  ? 2572 GLU A CA    1 
ATOM   9003  C  C     . GLU A 1 1355 ? 168.275 171.055 210.502 1.00 44.97  ? 2572 GLU A C     1 
ATOM   9004  O  O     . GLU A 1 1355 ? 167.834 170.862 211.637 1.00 48.91  ? 2572 GLU A O     1 
ATOM   9005  C  CB    . GLU A 1 1355 ? 170.791 171.072 210.470 1.00 47.19  ? 2572 GLU A CB    1 
ATOM   9006  C  CG    . GLU A 1 1355 ? 170.977 172.484 209.944 1.00 47.56  ? 2572 GLU A CG    1 
ATOM   9007  C  CD    . GLU A 1 1355 ? 170.343 173.539 210.829 1.00 51.37  ? 2572 GLU A CD    1 
ATOM   9008  O  OE1   . GLU A 1 1355 ? 170.091 173.244 212.016 1.00 51.33  ? 2572 GLU A OE1   1 
ATOM   9009  O  OE2   . GLU A 1 1355 ? 170.102 174.662 210.339 1.00 51.91  ? 2572 GLU A OE2   1 
ATOM   9010  N  N     . ILE A 1 1356 ? 167.673 171.874 209.634 1.00 43.25  ? 2573 ILE A N     1 
ATOM   9011  C  CA    . ILE A 1 1356 ? 166.360 172.422 209.971 1.00 45.74  ? 2573 ILE A CA    1 
ATOM   9012  C  C     . ILE A 1 1356 ? 165.314 171.309 210.037 1.00 44.53  ? 2573 ILE A C     1 
ATOM   9013  O  O     . ILE A 1 1356 ? 164.480 171.273 210.955 1.00 48.01  ? 2573 ILE A O     1 
ATOM   9014  C  CB    . ILE A 1 1356 ? 165.971 173.533 208.979 1.00 47.02  ? 2573 ILE A CB    1 
ATOM   9015  C  CG1   . ILE A 1 1356 ? 166.954 174.700 209.097 1.00 44.54  ? 2573 ILE A CG1   1 
ATOM   9016  C  CG2   . ILE A 1 1356 ? 164.551 174.009 209.233 1.00 49.31  ? 2573 ILE A CG2   1 
ATOM   9017  C  CD1   . ILE A 1 1356 ? 166.827 175.733 208.007 1.00 42.89  ? 2573 ILE A CD1   1 
ATOM   9018  N  N     . TYR A 1 1357 ? 165.362 170.366 209.088 1.00 42.48  ? 2574 TYR A N     1 
ATOM   9019  C  CA    . TYR A 1 1357 ? 164.478 169.200 209.152 1.00 45.01  ? 2574 TYR A CA    1 
ATOM   9020  C  C     . TYR A 1 1357 ? 164.708 168.377 210.416 1.00 49.15  ? 2574 TYR A C     1 
ATOM   9021  O  O     . TYR A 1 1357 ? 163.751 167.888 211.029 1.00 47.99  ? 2574 TYR A O     1 
ATOM   9022  C  CB    . TYR A 1 1357 ? 164.652 168.312 207.919 1.00 38.05  ? 2574 TYR A CB    1 
ATOM   9023  C  CG    . TYR A 1 1357 ? 163.822 168.708 206.721 1.00 38.49  ? 2574 TYR A CG    1 
ATOM   9024  C  CD1   . TYR A 1 1357 ? 162.828 169.666 206.824 1.00 41.97  ? 2574 TYR A CD1   1 
ATOM   9025  C  CD2   . TYR A 1 1357 ? 163.997 168.079 205.497 1.00 35.76  ? 2574 TYR A CD2   1 
ATOM   9026  C  CE1   . TYR A 1 1357 ? 162.056 170.013 205.733 1.00 40.47  ? 2574 TYR A CE1   1 
ATOM   9027  C  CE2   . TYR A 1 1357 ? 163.232 168.419 204.402 1.00 34.32  ? 2574 TYR A CE2   1 
ATOM   9028  C  CZ    . TYR A 1 1357 ? 162.262 169.386 204.526 1.00 34.39  ? 2574 TYR A CZ    1 
ATOM   9029  O  OH    . TYR A 1 1357 ? 161.493 169.730 203.438 1.00 31.48  ? 2574 TYR A OH    1 
ATOM   9030  N  N     . TYR A 1 1358 ? 165.967 168.206 210.822 1.00 48.07  ? 2575 TYR A N     1 
ATOM   9031  C  CA    . TYR A 1 1358 ? 166.236 167.401 212.006 1.00 45.53  ? 2575 TYR A CA    1 
ATOM   9032  C  C     . TYR A 1 1358 ? 165.873 168.136 213.291 1.00 48.25  ? 2575 TYR A C     1 
ATOM   9033  O  O     . TYR A 1 1358 ? 165.477 167.496 214.268 1.00 54.94  ? 2575 TYR A O     1 
ATOM   9034  C  CB    . TYR A 1 1358 ? 167.687 166.935 212.008 1.00 43.25  ? 2575 TYR A CB    1 
ATOM   9035  C  CG    . TYR A 1 1358 ? 167.861 165.653 211.228 1.00 43.81  ? 2575 TYR A CG    1 
ATOM   9036  C  CD1   . TYR A 1 1358 ? 166.962 164.609 211.370 1.00 44.46  ? 2575 TYR A CD1   1 
ATOM   9037  C  CD2   . TYR A 1 1358 ? 168.895 165.499 210.327 1.00 45.01  ? 2575 TYR A CD2   1 
ATOM   9038  C  CE1   . TYR A 1 1358 ? 167.102 163.439 210.656 1.00 40.76  ? 2575 TYR A CE1   1 
ATOM   9039  C  CE2   . TYR A 1 1358 ? 169.044 164.333 209.604 1.00 44.60  ? 2575 TYR A CE2   1 
ATOM   9040  C  CZ    . TYR A 1 1358 ? 168.147 163.307 209.774 1.00 42.52  ? 2575 TYR A CZ    1 
ATOM   9041  O  OH    . TYR A 1 1358 ? 168.299 162.148 209.053 1.00 43.90  ? 2575 TYR A OH    1 
ATOM   9042  N  N     . LYS A 1 1359 ? 165.965 169.467 213.307 1.00 45.31  ? 2576 LYS A N     1 
ATOM   9043  C  CA    . LYS A 1 1359 ? 165.396 170.225 214.417 1.00 45.73  ? 2576 LYS A CA    1 
ATOM   9044  C  C     . LYS A 1 1359 ? 163.891 170.015 214.502 1.00 49.82  ? 2576 LYS A C     1 
ATOM   9045  O  O     . LYS A 1 1359 ? 163.342 169.808 215.593 1.00 57.48  ? 2576 LYS A O     1 
ATOM   9046  C  CB    . LYS A 1 1359 ? 165.717 171.710 214.262 1.00 46.59  ? 2576 LYS A CB    1 
ATOM   9047  C  CG    . LYS A 1 1359 ? 167.107 172.104 214.720 1.00 48.39  ? 2576 LYS A CG    1 
ATOM   9048  C  CD    . LYS A 1 1359 ? 167.525 173.429 214.109 1.00 46.83  ? 2576 LYS A CD    1 
ATOM   9049  C  CE    . LYS A 1 1359 ? 166.558 174.539 214.480 1.00 47.02  ? 2576 LYS A CE    1 
ATOM   9050  N  NZ    . LYS A 1 1359 ? 166.722 174.963 215.896 1.00 50.79  ? 2576 LYS A NZ    1 
ATOM   9051  N  N     . ALA A 1 1360 ? 163.211 170.040 213.352 1.00 51.16  ? 2577 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 1360 ? 161.765 169.836 213.342 1.00 57.28  ? 2577 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 1360 ? 161.393 168.435 213.814 1.00 57.62  ? 2577 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 1360 ? 160.385 168.254 214.508 1.00 60.37  ? 2577 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 1360 ? 161.211 170.092 211.942 1.00 60.66  ? 2577 ALA A CB    1 
ATOM   9056  N  N     . ILE A 1 1361 ? 162.187 167.430 213.442 1.00 52.14  ? 2578 ILE A N     1 
ATOM   9057  C  CA    . ILE A 1 1361 ? 161.850 166.062 213.827 1.00 53.64  ? 2578 ILE A CA    1 
ATOM   9058  C  C     . ILE A 1 1361 ? 162.245 165.788 215.280 1.00 57.85  ? 2578 ILE A C     1 
ATOM   9059  O  O     . ILE A 1 1361 ? 161.618 164.959 215.949 1.00 62.34  ? 2578 ILE A O     1 
ATOM   9060  C  CB    . ILE A 1 1361 ? 162.499 165.056 212.858 1.00 52.35  ? 2578 ILE A CB    1 
ATOM   9061  C  CG1   . ILE A 1 1361 ? 161.949 163.651 213.043 1.00 45.95  ? 2578 ILE A CG1   1 
ATOM   9062  C  CG2   . ILE A 1 1361 ? 163.959 164.924 213.096 1.00 52.34  ? 2578 ILE A CG2   1 
ATOM   9063  C  CD1   . ILE A 1 1361 ? 162.373 162.754 211.920 1.00 42.37  ? 2578 ILE A CD1   1 
ATOM   9064  N  N     . PHE A 1 1362 ? 163.261 166.480 215.803 1.00 58.37  ? 2579 PHE A N     1 
ATOM   9065  C  CA    . PHE A 1 1362 ? 163.712 166.265 217.169 1.00 57.43  ? 2579 PHE A CA    1 
ATOM   9066  C  C     . PHE A 1 1362 ? 163.006 167.167 218.167 1.00 62.38  ? 2579 PHE A C     1 
ATOM   9067  O  O     . PHE A 1 1362 ? 163.246 167.038 219.372 1.00 67.24  ? 2579 PHE A O     1 
ATOM   9068  C  CB    . PHE A 1 1362 ? 165.228 166.467 217.265 1.00 51.68  ? 2579 PHE A CB    1 
ATOM   9069  C  CG    . PHE A 1 1362 ? 166.030 165.264 216.847 1.00 51.16  ? 2579 PHE A CG    1 
ATOM   9070  C  CD1   . PHE A 1 1362 ? 165.422 164.189 216.220 1.00 51.41  ? 2579 PHE A CD1   1 
ATOM   9071  C  CD2   . PHE A 1 1362 ? 167.394 165.214 217.071 1.00 59.61  ? 2579 PHE A CD2   1 
ATOM   9072  C  CE1   . PHE A 1 1362 ? 166.155 163.089 215.829 1.00 57.23  ? 2579 PHE A CE1   1 
ATOM   9073  C  CE2   . PHE A 1 1362 ? 168.133 164.115 216.682 1.00 62.63  ? 2579 PHE A CE2   1 
ATOM   9074  C  CZ    . PHE A 1 1362 ? 167.511 163.052 216.060 1.00 60.46  ? 2579 PHE A CZ    1 
ATOM   9075  N  N     . LYS A 1 1363 ? 162.161 168.087 217.697 1.00 64.55  ? 2580 LYS A N     1 
ATOM   9076  C  CA    . LYS A 1 1363 ? 161.176 168.682 218.594 1.00 67.41  ? 2580 LYS A CA    1 
ATOM   9077  C  C     . LYS A 1 1363 ? 160.212 167.638 219.148 1.00 67.88  ? 2580 LYS A C     1 
ATOM   9078  O  O     . LYS A 1 1363 ? 159.632 167.850 220.217 1.00 69.89  ? 2580 LYS A O     1 
ATOM   9079  C  CB    . LYS A 1 1363 ? 160.390 169.783 217.879 1.00 70.83  ? 2580 LYS A CB    1 
ATOM   9080  C  CG    . LYS A 1 1363 ? 161.184 171.050 217.601 1.00 75.52  ? 2580 LYS A CG    1 
ATOM   9081  C  CD    . LYS A 1 1363 ? 161.667 171.697 218.887 1.00 80.23  ? 2580 LYS A CD    1 
ATOM   9082  C  CE    . LYS A 1 1363 ? 160.523 172.373 219.625 1.00 86.09  ? 2580 LYS A CE    1 
ATOM   9083  N  NZ    . LYS A 1 1363 ? 159.975 173.526 218.858 1.00 90.14  ? 2580 LYS A NZ    1 
ATOM   9084  N  N     . LEU A 1 1364 ? 160.026 166.519 218.439 1.00 68.03  ? 2581 LEU A N     1 
ATOM   9085  C  CA    . LEU A 1 1364 ? 159.204 165.428 218.954 1.00 67.95  ? 2581 LEU A CA    1 
ATOM   9086  C  C     . LEU A 1 1364 ? 159.902 164.698 220.096 1.00 69.95  ? 2581 LEU A C     1 
ATOM   9087  O  O     . LEU A 1 1364 ? 159.251 164.277 221.060 1.00 72.68  ? 2581 LEU A O     1 
ATOM   9088  C  CB    . LEU A 1 1364 ? 158.861 164.456 217.824 1.00 61.06  ? 2581 LEU A CB    1 
ATOM   9089  C  CG    . LEU A 1 1364 ? 157.880 163.321 218.126 1.00 56.72  ? 2581 LEU A CG    1 
ATOM   9090  C  CD1   . LEU A 1 1364 ? 156.671 163.824 218.898 1.00 58.52  ? 2581 LEU A CD1   1 
ATOM   9091  C  CD2   . LEU A 1 1364 ? 157.448 162.639 216.839 1.00 53.08  ? 2581 LEU A CD2   1 
ATOM   9092  N  N     . VAL A 1 1365 ? 161.219 164.540 220.008 1.00 69.69  ? 2582 VAL A N     1 
ATOM   9093  C  CA    . VAL A 1 1365 ? 162.001 163.875 221.051 1.00 70.60  ? 2582 VAL A CA    1 
ATOM   9094  C  C     . VAL A 1 1365 ? 163.037 164.863 221.591 1.00 74.51  ? 2582 VAL A C     1 
ATOM   9095  O  O     . VAL A 1 1365 ? 164.189 164.912 221.134 1.00 77.38  ? 2582 VAL A O     1 
ATOM   9096  C  CB    . VAL A 1 1365 ? 162.578 162.539 220.533 1.00 63.98  ? 2582 VAL A CB    1 
ATOM   9097  C  CG1   . VAL A 1 1365 ? 163.397 162.694 219.242 1.00 59.87  ? 2582 VAL A CG1   1 
ATOM   9098  C  CG2   . VAL A 1 1365 ? 163.395 161.845 221.618 1.00 68.96  ? 2582 VAL A CG2   1 
ATOM   9099  N  N     . PRO A 1 1366 ? 162.657 165.686 222.574 1.00 74.13  ? 2583 PRO A N     1 
ATOM   9100  C  CA    . PRO A 1 1366 ? 163.507 166.817 222.969 1.00 76.37  ? 2583 PRO A CA    1 
ATOM   9101  C  C     . PRO A 1 1366 ? 164.717 166.445 223.807 1.00 78.85  ? 2583 PRO A C     1 
ATOM   9102  O  O     . PRO A 1 1366 ? 165.564 167.315 224.045 1.00 81.19  ? 2583 PRO A O     1 
ATOM   9103  C  CB    . PRO A 1 1366 ? 162.546 167.702 223.772 1.00 78.89  ? 2583 PRO A CB    1 
ATOM   9104  C  CG    . PRO A 1 1366 ? 161.571 166.739 224.355 1.00 80.32  ? 2583 PRO A CG    1 
ATOM   9105  C  CD    . PRO A 1 1366 ? 161.401 165.637 223.343 1.00 74.67  ? 2583 PRO A CD    1 
ATOM   9106  N  N     . GLU A 1 1367 ? 164.830 165.197 224.266 1.00 80.26  ? 2584 GLU A N     1 
ATOM   9107  C  CA    . GLU A 1 1367 ? 165.970 164.825 225.096 1.00 84.27  ? 2584 GLU A CA    1 
ATOM   9108  C  C     . GLU A 1 1367 ? 167.272 164.785 224.309 1.00 83.61  ? 2584 GLU A C     1 
ATOM   9109  O  O     . GLU A 1 1367 ? 168.348 164.850 224.912 1.00 86.63  ? 2584 GLU A O     1 
ATOM   9110  C  CB    . GLU A 1 1367 ? 165.721 163.468 225.755 1.00 82.92  ? 2584 GLU A CB    1 
ATOM   9111  C  CG    . GLU A 1 1367 ? 164.793 163.523 226.958 1.00 76.15  ? 2584 GLU A CG    1 
ATOM   9112  C  CD    . GLU A 1 1367 ? 163.332 163.361 226.580 1.00 79.35  ? 2584 GLU A CD    1 
ATOM   9113  O  OE1   . GLU A 1 1367 ? 163.011 163.440 225.375 1.00 79.68  ? 2584 GLU A OE1   1 
ATOM   9114  O  OE2   . GLU A 1 1367 ? 162.503 163.157 227.490 1.00 77.16  ? 2584 GLU A OE2   1 
ATOM   9115  N  N     . PHE A 1 1368 ? 167.199 164.691 222.985 1.00 78.29  ? 2585 PHE A N     1 
ATOM   9116  C  CA    . PHE A 1 1368 ? 168.359 164.635 222.103 1.00 78.25  ? 2585 PHE A CA    1 
ATOM   9117  C  C     . PHE A 1 1368 ? 168.340 165.802 221.123 1.00 78.09  ? 2585 PHE A C     1 
ATOM   9118  O  O     . PHE A 1 1368 ? 168.752 165.678 219.967 1.00 75.05  ? 2585 PHE A O     1 
ATOM   9119  C  CB    . PHE A 1 1368 ? 168.409 163.304 221.355 1.00 77.98  ? 2585 PHE A CB    1 
ATOM   9120  C  CG    . PHE A 1 1368 ? 168.440 162.095 222.251 1.00 85.07  ? 2585 PHE A CG    1 
ATOM   9121  C  CD1   . PHE A 1 1368 ? 169.054 162.138 223.493 1.00 85.38  ? 2585 PHE A CD1   1 
ATOM   9122  C  CD2   . PHE A 1 1368 ? 167.816 160.923 221.862 1.00 85.10  ? 2585 PHE A CD2   1 
ATOM   9123  C  CE1   . PHE A 1 1368 ? 169.068 161.029 224.316 1.00 83.38  ? 2585 PHE A CE1   1 
ATOM   9124  C  CE2   . PHE A 1 1368 ? 167.823 159.812 222.682 1.00 81.11  ? 2585 PHE A CE2   1 
ATOM   9125  C  CZ    . PHE A 1 1368 ? 168.452 159.864 223.910 1.00 80.24  ? 2585 PHE A CZ    1 
ATOM   9126  N  N     . ARG A 1 1369 ? 167.855 166.957 221.585 1.00 81.50  ? 2586 ARG A N     1 
ATOM   9127  C  CA    . ARG A 1 1369 ? 167.697 168.118 220.717 1.00 82.29  ? 2586 ARG A CA    1 
ATOM   9128  C  C     . ARG A 1 1369 ? 169.028 168.716 220.280 1.00 78.41  ? 2586 ARG A C     1 
ATOM   9129  O  O     . ARG A 1 1369 ? 169.063 169.455 219.292 1.00 73.79  ? 2586 ARG A O     1 
ATOM   9130  C  CB    . ARG A 1 1369 ? 166.859 169.185 221.422 1.00 87.53  ? 2586 ARG A CB    1 
ATOM   9131  C  CG    . ARG A 1 1369 ? 167.507 169.760 222.673 1.00 86.49  ? 2586 ARG A CG    1 
ATOM   9132  C  CD    . ARG A 1 1369 ? 166.548 170.673 223.417 1.00 85.89  ? 2586 ARG A CD    1 
ATOM   9133  N  NE    . ARG A 1 1369 ? 165.928 171.647 222.528 1.00 89.19  ? 2586 ARG A NE    1 
ATOM   9134  C  CZ    . ARG A 1 1369 ? 164.619 171.783 222.362 1.00 89.04  ? 2586 ARG A CZ    1 
ATOM   9135  N  NH1   . ARG A 1 1369 ? 163.757 171.019 223.012 1.00 90.63  ? 2586 ARG A NH1   1 
ATOM   9136  N  NH2   . ARG A 1 1369 ? 164.165 172.707 221.520 1.00 85.50  ? 2586 ARG A NH2   1 
ATOM   9137  N  N     . SER A 1 1370 ? 170.116 168.417 220.983 1.00 79.33  ? 2587 SER A N     1 
ATOM   9138  C  CA    . SER A 1 1370 ? 171.422 168.958 220.632 1.00 81.34  ? 2587 SER A CA    1 
ATOM   9139  C  C     . SER A 1 1370 ? 172.138 168.139 219.567 1.00 79.85  ? 2587 SER A C     1 
ATOM   9140  O  O     . SER A 1 1370 ? 173.251 168.503 219.174 1.00 79.15  ? 2587 SER A O     1 
ATOM   9141  C  CB    . SER A 1 1370 ? 172.301 169.059 221.880 1.00 83.45  ? 2587 SER A CB    1 
ATOM   9142  O  OG    . SER A 1 1370 ? 172.486 167.787 222.477 1.00 84.83  ? 2587 SER A OG    1 
ATOM   9143  N  N     . TYR A 1 1371 ? 171.532 167.050 219.094 1.00 75.72  ? 2588 TYR A N     1 
ATOM   9144  C  CA    . TYR A 1 1371 ? 172.158 166.158 218.126 1.00 73.31  ? 2588 TYR A CA    1 
ATOM   9145  C  C     . TYR A 1 1371 ? 171.548 166.291 216.735 1.00 70.64  ? 2588 TYR A C     1 
ATOM   9146  O  O     . TYR A 1 1371 ? 171.688 165.380 215.914 1.00 67.03  ? 2588 TYR A O     1 
ATOM   9147  C  CB    . TYR A 1 1371 ? 172.070 164.707 218.604 1.00 75.38  ? 2588 TYR A CB    1 
ATOM   9148  C  CG    . TYR A 1 1371 ? 173.102 164.319 219.643 1.00 83.68  ? 2588 TYR A CG    1 
ATOM   9149  C  CD1   . TYR A 1 1371 ? 173.293 165.083 220.788 1.00 85.09  ? 2588 TYR A CD1   1 
ATOM   9150  C  CD2   . TYR A 1 1371 ? 173.879 163.180 219.480 1.00 86.73  ? 2588 TYR A CD2   1 
ATOM   9151  C  CE1   . TYR A 1 1371 ? 174.232 164.728 221.735 1.00 86.49  ? 2588 TYR A CE1   1 
ATOM   9152  C  CE2   . TYR A 1 1371 ? 174.820 162.817 220.423 1.00 90.53  ? 2588 TYR A CE2   1 
ATOM   9153  C  CZ    . TYR A 1 1371 ? 174.992 163.595 221.548 1.00 92.04  ? 2588 TYR A CZ    1 
ATOM   9154  O  OH    . TYR A 1 1371 ? 175.928 163.238 222.491 1.00 97.96  ? 2588 TYR A OH    1 
ATOM   9155  N  N     . THR A 1 1372 ? 170.873 167.406 216.454 1.00 68.97  ? 2589 THR A N     1 
ATOM   9156  C  CA    . THR A 1 1372 ? 170.247 167.590 215.149 1.00 59.04  ? 2589 THR A CA    1 
ATOM   9157  C  C     . THR A 1 1372 ? 171.293 167.745 214.051 1.00 62.11  ? 2589 THR A C     1 
ATOM   9158  O  O     . THR A 1 1372 ? 171.205 167.097 213.002 1.00 65.06  ? 2589 THR A O     1 
ATOM   9159  C  CB    . THR A 1 1372 ? 169.323 168.806 215.180 1.00 53.93  ? 2589 THR A CB    1 
ATOM   9160  O  OG1   . THR A 1 1372 ? 170.066 169.959 215.594 1.00 55.45  ? 2589 THR A OG1   1 
ATOM   9161  C  CG2   . THR A 1 1372 ? 168.189 168.576 216.157 1.00 60.07  ? 2589 THR A CG2   1 
ATOM   9162  N  N     . GLU A 1 1373 ? 172.284 168.606 214.277 1.00 65.37  ? 2590 GLU A N     1 
ATOM   9163  C  CA    . GLU A 1 1373 ? 173.319 168.845 213.272 1.00 65.39  ? 2590 GLU A CA    1 
ATOM   9164  C  C     . GLU A 1 1373 ? 174.157 167.616 212.907 1.00 63.79  ? 2590 GLU A C     1 
ATOM   9165  O  O     . GLU A 1 1373 ? 174.403 167.420 211.702 1.00 62.71  ? 2590 GLU A O     1 
ATOM   9166  C  CB    . GLU A 1 1373 ? 174.222 169.997 213.732 1.00 67.18  ? 2590 GLU A CB    1 
ATOM   9167  C  CG    . GLU A 1 1373 ? 174.965 170.688 212.602 1.00 70.53  ? 2590 GLU A CG    1 
ATOM   9168  C  CD    . GLU A 1 1373 ? 176.369 170.155 212.414 1.00 76.06  ? 2590 GLU A CD    1 
ATOM   9169  O  OE1   . GLU A 1 1373 ? 176.869 169.456 213.321 1.00 77.74  ? 2590 GLU A OE1   1 
ATOM   9170  O  OE2   . GLU A 1 1373 ? 176.974 170.438 211.360 1.00 75.19  ? 2590 GLU A OE2   1 
ATOM   9171  N  N     . PRO A 1 1374 ? 174.660 166.791 213.845 1.00 65.16  ? 2591 PRO A N     1 
ATOM   9172  C  CA    . PRO A 1 1374 ? 175.357 165.572 213.402 1.00 66.83  ? 2591 PRO A CA    1 
ATOM   9173  C  C     . PRO A 1 1374 ? 174.478 164.600 212.632 1.00 63.88  ? 2591 PRO A C     1 
ATOM   9174  O  O     . PRO A 1 1374 ? 174.978 163.943 211.713 1.00 67.07  ? 2591 PRO A O     1 
ATOM   9175  C  CB    . PRO A 1 1374 ? 175.888 164.976 214.708 1.00 74.12  ? 2591 PRO A CB    1 
ATOM   9176  C  CG    . PRO A 1 1374 ? 175.005 165.480 215.753 1.00 71.91  ? 2591 PRO A CG    1 
ATOM   9177  C  CD    . PRO A 1 1374 ? 174.610 166.861 215.318 1.00 70.83  ? 2591 PRO A CD    1 
ATOM   9178  N  N     . PHE A 1 1375 ? 173.186 164.493 212.957 1.00 59.14  ? 2592 PHE A N     1 
ATOM   9179  C  CA    . PHE A 1 1375 ? 172.287 163.710 212.110 1.00 59.65  ? 2592 PHE A CA    1 
ATOM   9180  C  C     . PHE A 1 1375 ? 172.193 164.297 210.708 1.00 59.11  ? 2592 PHE A C     1 
ATOM   9181  O  O     . PHE A 1 1375 ? 172.113 163.555 209.721 1.00 58.88  ? 2592 PHE A O     1 
ATOM   9182  C  CB    . PHE A 1 1375 ? 170.894 163.616 212.735 1.00 58.51  ? 2592 PHE A CB    1 
ATOM   9183  C  CG    . PHE A 1 1375 ? 170.703 162.424 213.629 1.00 57.61  ? 2592 PHE A CG    1 
ATOM   9184  C  CD1   . PHE A 1 1375 ? 170.385 161.190 213.087 1.00 55.23  ? 2592 PHE A CD1   1 
ATOM   9185  C  CD2   . PHE A 1 1375 ? 170.821 162.535 215.001 1.00 62.34  ? 2592 PHE A CD2   1 
ATOM   9186  C  CE1   . PHE A 1 1375 ? 170.198 160.090 213.895 1.00 57.94  ? 2592 PHE A CE1   1 
ATOM   9187  C  CE2   . PHE A 1 1375 ? 170.635 161.436 215.816 1.00 64.68  ? 2592 PHE A CE2   1 
ATOM   9188  C  CZ    . PHE A 1 1375 ? 170.322 160.213 215.261 1.00 62.28  ? 2592 PHE A CZ    1 
ATOM   9189  N  N     . ALA A 1 1376 ? 172.186 165.628 210.601 1.00 58.31  ? 2593 ALA A N     1 
ATOM   9190  C  CA    . ALA A 1 1376 ? 172.119 166.272 209.293 1.00 51.75  ? 2593 ALA A CA    1 
ATOM   9191  C  C     . ALA A 1 1376 ? 173.356 165.968 208.469 1.00 54.26  ? 2593 ALA A C     1 
ATOM   9192  O  O     . ALA A 1 1376 ? 173.257 165.600 207.293 1.00 55.07  ? 2593 ALA A O     1 
ATOM   9193  C  CB    . ALA A 1 1376 ? 171.954 167.776 209.459 1.00 49.37  ? 2593 ALA A CB    1 
ATOM   9194  N  N     . ARG A 1 1377 ? 174.536 166.127 209.073 1.00 57.77  ? 2594 ARG A N     1 
ATOM   9195  C  CA    . ARG A 1 1377 ? 175.765 165.789 208.369 1.00 62.93  ? 2594 ARG A CA    1 
ATOM   9196  C  C     . ARG A 1 1377 ? 175.824 164.304 208.047 1.00 62.29  ? 2594 ARG A C     1 
ATOM   9197  O  O     . ARG A 1 1377 ? 176.345 163.924 206.997 1.00 60.20  ? 2594 ARG A O     1 
ATOM   9198  C  CB    . ARG A 1 1377 ? 176.983 166.211 209.190 1.00 69.36  ? 2594 ARG A CB    1 
ATOM   9199  C  CG    . ARG A 1 1377 ? 176.965 167.670 209.612 1.00 69.30  ? 2594 ARG A CG    1 
ATOM   9200  C  CD    . ARG A 1 1377 ? 177.233 168.602 208.439 1.00 67.31  ? 2594 ARG A CD    1 
ATOM   9201  N  NE    . ARG A 1 1377 ? 178.113 168.005 207.441 1.00 69.47  ? 2594 ARG A NE    1 
ATOM   9202  C  CZ    . ARG A 1 1377 ? 179.425 168.185 207.394 1.00 70.92  ? 2594 ARG A CZ    1 
ATOM   9203  N  NH1   . ARG A 1 1377 ? 180.050 168.948 208.277 1.00 70.16  ? 2594 ARG A NH1   1 
ATOM   9204  N  NH2   . ARG A 1 1377 ? 180.128 167.588 206.436 1.00 71.25  ? 2594 ARG A NH2   1 
ATOM   9205  N  N     . ALA A 1 1378 ? 175.256 163.460 208.911 1.00 61.32  ? 2595 ALA A N     1 
ATOM   9206  C  CA    . ALA A 1 1378 ? 175.203 162.028 208.643 1.00 55.38  ? 2595 ALA A CA    1 
ATOM   9207  C  C     . ALA A 1 1378 ? 174.386 161.729 207.395 1.00 52.91  ? 2595 ALA A C     1 
ATOM   9208  O  O     . ALA A 1 1378 ? 174.853 161.032 206.487 1.00 55.99  ? 2595 ALA A O     1 
ATOM   9209  C  CB    . ALA A 1 1378 ? 174.624 161.295 209.853 1.00 54.41  ? 2595 ALA A CB    1 
ATOM   9210  N  N     . SER A 1 1379 ? 173.163 162.261 207.329 1.00 52.56  ? 2596 SER A N     1 
ATOM   9211  C  CA    . SER A 1 1379 ? 172.304 162.009 206.175 1.00 50.79  ? 2596 SER A CA    1 
ATOM   9212  C  C     . SER A 1 1379 ? 172.897 162.599 204.901 1.00 49.57  ? 2596 SER A C     1 
ATOM   9213  O  O     . SER A 1 1379 ? 172.904 161.945 203.849 1.00 51.35  ? 2596 SER A O     1 
ATOM   9214  C  CB    . SER A 1 1379 ? 170.905 162.571 206.426 1.00 44.83  ? 2596 SER A CB    1 
ATOM   9215  O  OG    . SER A 1 1379 ? 170.233 161.844 207.439 1.00 39.67  ? 2596 SER A OG    1 
ATOM   9216  N  N     . VAL A 1 1380 ? 173.419 163.827 204.981 1.00 49.54  ? 2597 VAL A N     1 
ATOM   9217  C  CA    . VAL A 1 1380 ? 173.965 164.487 203.800 1.00 50.37  ? 2597 VAL A CA    1 
ATOM   9218  C  C     . VAL A 1 1380 ? 175.207 163.758 203.299 1.00 55.64  ? 2597 VAL A C     1 
ATOM   9219  O  O     . VAL A 1 1380 ? 175.357 163.527 202.094 1.00 56.37  ? 2597 VAL A O     1 
ATOM   9220  C  CB    . VAL A 1 1380 ? 174.251 165.968 204.111 1.00 48.21  ? 2597 VAL A CB    1 
ATOM   9221  C  CG1   . VAL A 1 1380 ? 175.155 166.582 203.056 1.00 47.05  ? 2597 VAL A CG1   1 
ATOM   9222  C  CG2   . VAL A 1 1380 ? 172.948 166.742 204.207 1.00 45.78  ? 2597 VAL A CG2   1 
ATOM   9223  N  N     . HIS A 1 1381 ? 176.104 163.367 204.209 1.00 57.06  ? 2598 HIS A N     1 
ATOM   9224  C  CA    . HIS A 1 1381 ? 177.305 162.634 203.827 1.00 55.91  ? 2598 HIS A CA    1 
ATOM   9225  C  C     . HIS A 1 1381 ? 176.962 161.261 203.264 1.00 54.06  ? 2598 HIS A C     1 
ATOM   9226  O  O     . HIS A 1 1381 ? 177.583 160.811 202.294 1.00 54.68  ? 2598 HIS A O     1 
ATOM   9227  C  CB    . HIS A 1 1381 ? 178.230 162.512 205.037 1.00 58.72  ? 2598 HIS A CB    1 
ATOM   9228  C  CG    . HIS A 1 1381 ? 179.375 161.571 204.838 1.00 62.91  ? 2598 HIS A CG    1 
ATOM   9229  N  ND1   . HIS A 1 1381 ? 179.727 160.623 205.775 1.00 67.12  ? 2598 HIS A ND1   1 
ATOM   9230  C  CD2   . HIS A 1 1381 ? 180.257 161.439 203.820 1.00 65.88  ? 2598 HIS A CD2   1 
ATOM   9231  C  CE1   . HIS A 1 1381 ? 180.772 159.943 205.338 1.00 71.20  ? 2598 HIS A CE1   1 
ATOM   9232  N  NE2   . HIS A 1 1381 ? 181.113 160.418 204.155 1.00 70.79  ? 2598 HIS A NE2   1 
ATOM   9233  N  N     . LEU A 1 1382 ? 175.972 160.585 203.855 1.00 54.43  ? 2599 LEU A N     1 
ATOM   9234  C  CA    . LEU A 1 1382 ? 175.562 159.278 203.357 1.00 55.65  ? 2599 LEU A CA    1 
ATOM   9235  C  C     . LEU A 1 1382 ? 175.009 159.383 201.942 1.00 55.14  ? 2599 LEU A C     1 
ATOM   9236  O  O     . LEU A 1 1382 ? 175.371 158.587 201.067 1.00 58.38  ? 2599 LEU A O     1 
ATOM   9237  C  CB    . LEU A 1 1382 ? 174.534 158.668 204.317 1.00 52.45  ? 2599 LEU A CB    1 
ATOM   9238  C  CG    . LEU A 1 1382 ? 174.044 157.222 204.188 1.00 49.59  ? 2599 LEU A CG    1 
ATOM   9239  C  CD1   . LEU A 1 1382 ? 173.616 156.714 205.553 1.00 43.46  ? 2599 LEU A CD1   1 
ATOM   9240  C  CD2   . LEU A 1 1382 ? 172.889 157.091 203.216 1.00 54.44  ? 2599 LEU A CD2   1 
ATOM   9241  N  N     . TYR A 1 1383 ? 174.151 160.376 201.691 1.00 49.43  ? 2600 TYR A N     1 
ATOM   9242  C  CA    . TYR A 1 1383 ? 173.617 160.557 200.344 1.00 48.06  ? 2600 TYR A CA    1 
ATOM   9243  C  C     . TYR A 1 1383 ? 174.706 160.972 199.364 1.00 52.07  ? 2600 TYR A C     1 
ATOM   9244  O  O     . TYR A 1 1383 ? 174.712 160.526 198.211 1.00 54.89  ? 2600 TYR A O     1 
ATOM   9245  C  CB    . TYR A 1 1383 ? 172.498 161.594 200.348 1.00 43.17  ? 2600 TYR A CB    1 
ATOM   9246  C  CG    . TYR A 1 1383 ? 172.327 162.305 199.021 1.00 40.50  ? 2600 TYR A CG    1 
ATOM   9247  C  CD1   . TYR A 1 1383 ? 171.719 161.670 197.946 1.00 41.19  ? 2600 TYR A CD1   1 
ATOM   9248  C  CD2   . TYR A 1 1383 ? 172.763 163.614 198.848 1.00 43.16  ? 2600 TYR A CD2   1 
ATOM   9249  C  CE1   . TYR A 1 1383 ? 171.560 162.314 196.736 1.00 41.08  ? 2600 TYR A CE1   1 
ATOM   9250  C  CE2   . TYR A 1 1383 ? 172.608 164.264 197.639 1.00 42.23  ? 2600 TYR A CE2   1 
ATOM   9251  C  CZ    . TYR A 1 1383 ? 172.005 163.608 196.588 1.00 42.13  ? 2600 TYR A CZ    1 
ATOM   9252  O  OH    . TYR A 1 1383 ? 171.845 164.250 195.384 1.00 40.75  ? 2600 TYR A OH    1 
ATOM   9253  N  N     . ASN A 1 1384 ? 175.623 161.840 199.798 1.00 52.20  ? 2601 ASN A N     1 
ATOM   9254  C  CA    . ASN A 1 1384 ? 176.682 162.308 198.912 1.00 55.25  ? 2601 ASN A CA    1 
ATOM   9255  C  C     . ASN A 1 1384 ? 177.597 161.162 198.507 1.00 59.50  ? 2601 ASN A C     1 
ATOM   9256  O  O     . ASN A 1 1384 ? 178.001 161.063 197.343 1.00 59.98  ? 2601 ASN A O     1 
ATOM   9257  C  CB    . ASN A 1 1384 ? 177.472 163.424 199.596 1.00 54.40  ? 2601 ASN A CB    1 
ATOM   9258  C  CG    . ASN A 1 1384 ? 178.335 164.209 198.630 1.00 55.23  ? 2601 ASN A CG    1 
ATOM   9259  O  OD1   . ASN A 1 1384 ? 178.356 163.937 197.430 1.00 53.69  ? 2601 ASN A OD1   1 
ATOM   9260  N  ND2   . ASN A 1 1384 ? 179.052 165.197 199.151 1.00 58.67  ? 2601 ASN A ND2   1 
ATOM   9261  N  N     . GLU A 1 1385 ? 177.924 160.277 199.451 1.00 57.89  ? 2602 GLU A N     1 
ATOM   9262  C  CA    . GLU A 1 1385 ? 178.703 159.092 199.109 1.00 56.25  ? 2602 GLU A CA    1 
ATOM   9263  C  C     . GLU A 1 1385 ? 177.910 158.145 198.218 1.00 58.43  ? 2602 GLU A C     1 
ATOM   9264  O  O     . GLU A 1 1385 ? 178.453 157.605 197.247 1.00 65.99  ? 2602 GLU A O     1 
ATOM   9265  C  CB    . GLU A 1 1385 ? 179.163 158.383 200.381 1.00 59.12  ? 2602 GLU A CB    1 
ATOM   9266  C  CG    . GLU A 1 1385 ? 180.239 159.133 201.150 1.00 64.31  ? 2602 GLU A CG    1 
ATOM   9267  C  CD    . GLU A 1 1385 ? 181.231 159.834 200.243 1.00 67.16  ? 2602 GLU A CD    1 
ATOM   9268  O  OE1   . GLU A 1 1385 ? 181.989 159.137 199.536 1.00 70.36  ? 2602 GLU A OE1   1 
ATOM   9269  O  OE2   . GLU A 1 1385 ? 181.256 161.082 200.241 1.00 66.91  ? 2602 GLU A OE2   1 
ATOM   9270  N  N     . CYS A 1 1386 ? 176.619 157.950 198.514 1.00 53.67  ? 2603 CYS A N     1 
ATOM   9271  C  CA    . CYS A 1 1386 ? 175.788 157.067 197.700 1.00 55.46  ? 2603 CYS A CA    1 
ATOM   9272  C  C     . CYS A 1 1386 ? 175.629 157.588 196.277 1.00 59.12  ? 2603 CYS A C     1 
ATOM   9273  O  O     . CYS A 1 1386 ? 175.355 156.809 195.359 1.00 61.32  ? 2603 CYS A O     1 
ATOM   9274  C  CB    . CYS A 1 1386 ? 174.417 156.892 198.353 1.00 49.68  ? 2603 CYS A CB    1 
ATOM   9275  S  SG    . CYS A 1 1386 ? 174.376 155.732 199.738 1.00 38.87  ? 2603 CYS A SG    1 
ATOM   9276  N  N     . LYS A 1 1387 ? 175.780 158.897 196.078 1.00 58.17  ? 2604 LYS A N     1 
ATOM   9277  C  CA    . LYS A 1 1387 ? 175.736 159.454 194.730 1.00 60.07  ? 2604 LYS A CA    1 
ATOM   9278  C  C     . LYS A 1 1387 ? 177.099 159.397 194.050 1.00 66.74  ? 2604 LYS A C     1 
ATOM   9279  O  O     . LYS A 1 1387 ? 177.196 158.999 192.884 1.00 70.42  ? 2604 LYS A O     1 
ATOM   9280  C  CB    . LYS A 1 1387 ? 175.224 160.895 194.769 1.00 57.03  ? 2604 LYS A CB    1 
ATOM   9281  C  CG    . LYS A 1 1387 ? 175.612 161.724 193.550 1.00 59.89  ? 2604 LYS A CG    1 
ATOM   9282  C  CD    . LYS A 1 1387 ? 174.737 162.955 193.393 1.00 50.68  ? 2604 LYS A CD    1 
ATOM   9283  C  CE    . LYS A 1 1387 ? 173.335 162.575 192.957 1.00 48.18  ? 2604 LYS A CE    1 
ATOM   9284  N  NZ    . LYS A 1 1387 ? 173.347 161.602 191.830 1.00 53.88  ? 2604 LYS A NZ    1 
ATOM   9285  N  N     . ALA A 1 1388 ? 178.161 159.788 194.759 1.00 65.83  ? 2605 ALA A N     1 
ATOM   9286  C  CA    . ALA A 1 1388 ? 179.477 159.892 194.137 1.00 68.01  ? 2605 ALA A CA    1 
ATOM   9287  C  C     . ALA A 1 1388 ? 180.056 158.520 193.815 1.00 71.56  ? 2605 ALA A C     1 
ATOM   9288  O  O     . ALA A 1 1388 ? 180.553 158.292 192.706 1.00 78.93  ? 2605 ALA A O     1 
ATOM   9289  C  CB    . ALA A 1 1388 ? 180.424 160.677 195.044 1.00 66.99  ? 2605 ALA A CB    1 
ATOM   9290  N  N     . ARG A 1 1389 ? 180.005 157.589 194.769 1.00 67.95  ? 2606 ARG A N     1 
ATOM   9291  C  CA    . ARG A 1 1389 ? 180.620 156.286 194.551 1.00 72.59  ? 2606 ARG A CA    1 
ATOM   9292  C  C     . ARG A 1 1389 ? 179.756 155.357 193.709 1.00 70.88  ? 2606 ARG A C     1 
ATOM   9293  O  O     . ARG A 1 1389 ? 180.271 154.363 193.186 1.00 75.69  ? 2606 ARG A O     1 
ATOM   9294  C  CB    . ARG A 1 1389 ? 180.939 155.621 195.891 1.00 73.61  ? 2606 ARG A CB    1 
ATOM   9295  C  CG    . ARG A 1 1389 ? 179.793 154.814 196.460 1.00 73.41  ? 2606 ARG A CG    1 
ATOM   9296  C  CD    . ARG A 1 1389 ? 180.200 154.038 197.693 1.00 79.18  ? 2606 ARG A CD    1 
ATOM   9297  N  NE    . ARG A 1 1389 ? 179.118 153.163 198.119 1.00 78.97  ? 2606 ARG A NE    1 
ATOM   9298  C  CZ    . ARG A 1 1389 ? 178.824 152.884 199.380 1.00 78.46  ? 2606 ARG A CZ    1 
ATOM   9299  N  NH1   . ARG A 1 1389 ? 179.539 153.368 200.381 1.00 78.61  ? 2606 ARG A NH1   1 
ATOM   9300  N  NH2   . ARG A 1 1389 ? 177.785 152.098 199.642 1.00 76.51  ? 2606 ARG A NH2   1 
ATOM   9301  N  N     . TYR A 1 1390 ? 178.470 155.658 193.554 1.00 68.50  ? 2607 TYR A N     1 
ATOM   9302  C  CA    . TYR A 1 1390 ? 177.540 154.808 192.822 1.00 75.45  ? 2607 TYR A CA    1 
ATOM   9303  C  C     . TYR A 1 1390 ? 176.902 155.623 191.708 1.00 80.31  ? 2607 TYR A C     1 
ATOM   9304  O  O     . TYR A 1 1390 ? 176.090 156.515 191.975 1.00 79.29  ? 2607 TYR A O     1 
ATOM   9305  C  CB    . TYR A 1 1390 ? 176.470 154.242 193.756 1.00 75.42  ? 2607 TYR A CB    1 
ATOM   9306  C  CG    . TYR A 1 1390 ? 176.951 153.106 194.625 1.00 77.84  ? 2607 TYR A CG    1 
ATOM   9307  C  CD1   . TYR A 1 1390 ? 178.091 152.390 194.293 1.00 82.17  ? 2607 TYR A CD1   1 
ATOM   9308  C  CD2   . TYR A 1 1390 ? 176.267 152.752 195.779 1.00 76.07  ? 2607 TYR A CD2   1 
ATOM   9309  C  CE1   . TYR A 1 1390 ? 178.539 151.355 195.084 1.00 84.95  ? 2607 TYR A CE1   1 
ATOM   9310  C  CE2   . TYR A 1 1390 ? 176.706 151.715 196.576 1.00 77.07  ? 2607 TYR A CE2   1 
ATOM   9311  C  CZ    . TYR A 1 1390 ? 177.842 151.019 196.223 1.00 83.97  ? 2607 TYR A CZ    1 
ATOM   9312  O  OH    . TYR A 1 1390 ? 178.290 149.986 197.013 1.00 87.82  ? 2607 TYR A OH    1 
ATOM   9313  N  N     . SER A 1 1391 ? 177.256 155.309 190.467 1.00 81.89  ? 2608 SER A N     1 
ATOM   9314  C  CA    . SER A 1 1391 ? 176.785 156.044 189.304 1.00 82.57  ? 2608 SER A CA    1 
ATOM   9315  C  C     . SER A 1 1391 ? 175.742 155.231 188.547 1.00 83.57  ? 2608 SER A C     1 
ATOM   9316  O  O     . SER A 1 1391 ? 175.489 154.061 188.843 1.00 82.09  ? 2608 SER A O     1 
ATOM   9317  C  CB    . SER A 1 1391 ? 177.955 156.406 188.381 1.00 78.81  ? 2608 SER A CB    1 
ATOM   9318  O  OG    . SER A 1 1391 ? 178.866 157.273 189.033 1.00 75.83  ? 2608 SER A OG    1 
ATOM   9319  N  N     . THR A 1 1392 ? 175.139 155.877 187.547 1.00 84.47  ? 2609 THR A N     1 
ATOM   9320  C  CA    . THR A 1 1392 ? 174.102 155.246 186.739 1.00 83.07  ? 2609 THR A CA    1 
ATOM   9321  C  C     . THR A 1 1392 ? 174.650 154.194 185.785 1.00 84.56  ? 2609 THR A C     1 
ATOM   9322  O  O     . THR A 1 1392 ? 173.857 153.474 185.169 1.00 86.45  ? 2609 THR A O     1 
ATOM   9323  C  CB    . THR A 1 1392 ? 173.336 156.305 185.945 1.00 85.80  ? 2609 THR A CB    1 
ATOM   9324  O  OG1   . THR A 1 1392 ? 172.333 155.670 185.141 1.00 85.47  ? 2609 THR A OG1   1 
ATOM   9325  C  CG2   . THR A 1 1392 ? 174.282 157.084 185.046 1.00 86.81  ? 2609 THR A CG2   1 
ATOM   9326  N  N     . GLY A 1 1393 ? 175.971 154.088 185.644 1.00 85.29  ? 2610 GLY A N     1 
ATOM   9327  C  CA    . GLY A 1 1393 ? 176.555 153.067 184.795 1.00 87.41  ? 2610 GLY A CA    1 
ATOM   9328  C  C     . GLY A 1 1393 ? 176.445 151.659 185.340 1.00 87.14  ? 2610 GLY A C     1 
ATOM   9329  O  O     . GLY A 1 1393 ? 176.700 150.705 184.597 1.00 87.37  ? 2610 GLY A O     1 
ATOM   9330  N  N     . LEU A 1 1394 ? 176.075 151.507 186.613 1.00 83.66  ? 2611 LEU A N     1 
ATOM   9331  C  CA    . LEU A 1 1394 ? 175.893 150.179 187.190 1.00 80.98  ? 2611 LEU A CA    1 
ATOM   9332  C  C     . LEU A 1 1394 ? 174.499 149.640 186.889 1.00 81.18  ? 2611 LEU A C     1 
ATOM   9333  O  O     . LEU A 1 1394 ? 174.348 148.521 186.387 1.00 81.86  ? 2611 LEU A O     1 
ATOM   9334  C  CB    . LEU A 1 1394 ? 176.145 150.224 188.701 1.00 78.78  ? 2611 LEU A CB    1 
ATOM   9335  C  CG    . LEU A 1 1394 ? 177.594 150.099 189.184 1.00 80.44  ? 2611 LEU A CG    1 
ATOM   9336  C  CD1   . LEU A 1 1394 ? 178.347 151.415 189.042 1.00 82.04  ? 2611 LEU A CD1   1 
ATOM   9337  C  CD2   . LEU A 1 1394 ? 177.637 149.610 190.624 1.00 80.60  ? 2611 LEU A CD2   1 
ATOM   9338  N  N     . GLN A 1 1395 ? 173.467 150.430 187.184 1.00 80.42  ? 2612 GLN A N     1 
ATOM   9339  C  CA    . GLN A 1 1395 ? 172.085 150.059 186.914 1.00 79.01  ? 2612 GLN A CA    1 
ATOM   9340  C  C     . GLN A 1 1395 ? 171.289 151.312 186.573 1.00 75.37  ? 2612 GLN A C     1 
ATOM   9341  O  O     . GLN A 1 1395 ? 171.708 152.439 186.852 1.00 74.96  ? 2612 GLN A O     1 
ATOM   9342  C  CB    . GLN A 1 1395 ? 171.445 149.330 188.104 1.00 77.47  ? 2612 GLN A CB    1 
ATOM   9343  C  CG    . GLN A 1 1395 ? 171.716 147.836 188.153 1.00 77.86  ? 2612 GLN A CG    1 
ATOM   9344  C  CD    . GLN A 1 1395 ? 170.592 147.018 187.549 1.00 75.25  ? 2612 GLN A CD    1 
ATOM   9345  O  OE1   . GLN A 1 1395 ? 169.887 147.477 186.650 1.00 72.80  ? 2612 GLN A OE1   1 
ATOM   9346  N  NE2   . GLN A 1 1395 ? 170.420 145.796 188.039 1.00 71.74  ? 2612 GLN A NE2   1 
ATOM   9347  N  N     . SER A 1 1396 ? 170.123 151.101 185.961 1.00 73.90  ? 2613 SER A N     1 
ATOM   9348  C  CA    . SER A 1 1396 ? 169.239 152.198 185.586 1.00 74.70  ? 2613 SER A CA    1 
ATOM   9349  C  C     . SER A 1 1396 ? 168.535 152.834 186.778 1.00 72.19  ? 2613 SER A C     1 
ATOM   9350  O  O     . SER A 1 1396 ? 167.974 153.925 186.633 1.00 72.75  ? 2613 SER A O     1 
ATOM   9351  C  CB    . SER A 1 1396 ? 168.195 151.707 184.580 1.00 78.17  ? 2613 SER A CB    1 
ATOM   9352  O  OG    . SER A 1 1396 ? 167.491 150.587 185.087 1.00 79.02  ? 2613 SER A OG    1 
ATOM   9353  N  N     . HIS A 1 1397 ? 168.549 152.185 187.942 1.00 70.38  ? 2614 HIS A N     1 
ATOM   9354  C  CA    . HIS A 1 1397 ? 167.938 152.715 189.154 1.00 69.77  ? 2614 HIS A CA    1 
ATOM   9355  C  C     . HIS A 1 1397 ? 168.971 153.191 190.167 1.00 70.79  ? 2614 HIS A C     1 
ATOM   9356  O  O     . HIS A 1 1397 ? 168.669 153.281 191.361 1.00 71.25  ? 2614 HIS A O     1 
ATOM   9357  C  CB    . HIS A 1 1397 ? 167.006 151.673 189.775 1.00 69.33  ? 2614 HIS A CB    1 
ATOM   9358  C  CG    . HIS A 1 1397 ? 167.674 150.372 190.085 1.00 68.43  ? 2614 HIS A CG    1 
ATOM   9359  N  ND1   . HIS A 1 1397 ? 168.357 150.144 191.259 1.00 69.52  ? 2614 HIS A ND1   1 
ATOM   9360  C  CD2   . HIS A 1 1397 ? 167.750 149.221 189.376 1.00 72.48  ? 2614 HIS A CD2   1 
ATOM   9361  C  CE1   . HIS A 1 1397 ? 168.833 148.912 191.256 1.00 72.84  ? 2614 HIS A CE1   1 
ATOM   9362  N  NE2   . HIS A 1 1397 ? 168.478 148.331 190.125 1.00 75.61  ? 2614 HIS A NE2   1 
ATOM   9363  N  N     . TYR A 1 1398 ? 170.180 153.500 189.714 1.00 72.04  ? 2615 TYR A N     1 
ATOM   9364  C  CA    . TYR A 1 1398 ? 171.211 154.074 190.576 1.00 70.84  ? 2615 TYR A CA    1 
ATOM   9365  C  C     . TYR A 1 1398 ? 171.206 155.598 190.515 1.00 68.89  ? 2615 TYR A C     1 
ATOM   9366  O  O     . TYR A 1 1398 ? 172.224 156.240 190.261 1.00 69.50  ? 2615 TYR A O     1 
ATOM   9367  C  CB    . TYR A 1 1398 ? 172.573 153.511 190.198 1.00 74.28  ? 2615 TYR A CB    1 
ATOM   9368  C  CG    . TYR A 1 1398 ? 173.006 152.354 191.065 1.00 76.81  ? 2615 TYR A CG    1 
ATOM   9369  C  CD1   . TYR A 1 1398 ? 174.050 152.496 191.965 1.00 77.28  ? 2615 TYR A CD1   1 
ATOM   9370  C  CD2   . TYR A 1 1398 ? 172.360 151.127 190.998 1.00 73.29  ? 2615 TYR A CD2   1 
ATOM   9371  C  CE1   . TYR A 1 1398 ? 174.451 151.448 192.763 1.00 80.12  ? 2615 TYR A CE1   1 
ATOM   9372  C  CE2   . TYR A 1 1398 ? 172.754 150.070 191.795 1.00 74.16  ? 2615 TYR A CE2   1 
ATOM   9373  C  CZ    . TYR A 1 1398 ? 173.800 150.239 192.676 1.00 80.16  ? 2615 TYR A CZ    1 
ATOM   9374  O  OH    . TYR A 1 1398 ? 174.204 149.198 193.477 1.00 80.77  ? 2615 TYR A OH    1 
ATOM   9375  N  N     . LEU A 1 1399 ? 170.037 156.185 190.753 1.00 64.90  ? 2616 LEU A N     1 
ATOM   9376  C  CA    . LEU A 1 1399 ? 169.865 157.629 190.809 1.00 56.53  ? 2616 LEU A CA    1 
ATOM   9377  C  C     . LEU A 1 1399 ? 169.462 158.026 192.221 1.00 50.61  ? 2616 LEU A C     1 
ATOM   9378  O  O     . LEU A 1 1399 ? 168.617 157.368 192.835 1.00 53.65  ? 2616 LEU A O     1 
ATOM   9379  C  CB    . LEU A 1 1399 ? 168.809 158.102 189.808 1.00 61.23  ? 2616 LEU A CB    1 
ATOM   9380  C  CG    . LEU A 1 1399 ? 169.270 158.304 188.364 1.00 67.56  ? 2616 LEU A CG    1 
ATOM   9381  C  CD1   . LEU A 1 1399 ? 168.124 158.063 187.397 1.00 71.96  ? 2616 LEU A CD1   1 
ATOM   9382  C  CD2   . LEU A 1 1399 ? 169.843 159.699 188.182 1.00 70.54  ? 2616 LEU A CD2   1 
ATOM   9383  N  N     . PHE A 1 1400 ? 170.076 159.088 192.733 1.00 49.29  ? 2617 PHE A N     1 
ATOM   9384  C  CA    . PHE A 1 1400 ? 169.771 159.615 194.053 1.00 50.24  ? 2617 PHE A CA    1 
ATOM   9385  C  C     . PHE A 1 1400 ? 169.628 161.127 193.971 1.00 44.18  ? 2617 PHE A C     1 
ATOM   9386  O  O     . PHE A 1 1400 ? 170.190 161.773 193.083 1.00 43.45  ? 2617 PHE A O     1 
ATOM   9387  C  CB    . PHE A 1 1400 ? 170.853 159.234 195.074 1.00 48.37  ? 2617 PHE A CB    1 
ATOM   9388  C  CG    . PHE A 1 1400 ? 170.973 157.755 195.305 1.00 45.46  ? 2617 PHE A CG    1 
ATOM   9389  C  CD1   . PHE A 1 1400 ? 169.870 157.008 195.683 1.00 43.44  ? 2617 PHE A CD1   1 
ATOM   9390  C  CD2   . PHE A 1 1400 ? 172.184 157.109 195.131 1.00 54.43  ? 2617 PHE A CD2   1 
ATOM   9391  C  CE1   . PHE A 1 1400 ? 169.976 155.646 195.891 1.00 48.04  ? 2617 PHE A CE1   1 
ATOM   9392  C  CE2   . PHE A 1 1400 ? 172.297 155.748 195.337 1.00 54.01  ? 2617 PHE A CE2   1 
ATOM   9393  C  CZ    . PHE A 1 1400 ? 171.190 155.016 195.716 1.00 50.17  ? 2617 PHE A CZ    1 
ATOM   9394  N  N     . SER A 1 1401 ? 168.863 161.684 194.903 1.00 38.49  ? 2618 SER A N     1 
ATOM   9395  C  CA    . SER A 1 1401 ? 168.533 163.103 194.897 1.00 35.30  ? 2618 SER A CA    1 
ATOM   9396  C  C     . SER A 1 1401 ? 168.237 163.540 196.329 1.00 34.72  ? 2618 SER A C     1 
ATOM   9397  O  O     . SER A 1 1401 ? 168.272 162.702 197.238 1.00 41.22  ? 2618 SER A O     1 
ATOM   9398  C  CB    . SER A 1 1401 ? 167.335 163.354 193.981 1.00 33.67  ? 2618 SER A CB    1 
ATOM   9399  O  OG    . SER A 1 1401 ? 166.175 162.746 194.509 1.00 36.69  ? 2618 SER A OG    1 
ATOM   9400  N  N     . PRO A 1 1402 ? 167.960 164.824 196.586 1.00 27.98  ? 2619 PRO A N     1 
ATOM   9401  C  CA    . PRO A 1 1402 ? 167.440 165.200 197.912 1.00 26.44  ? 2619 PRO A CA    1 
ATOM   9402  C  C     . PRO A 1 1402 ? 166.118 164.539 198.276 1.00 30.09  ? 2619 PRO A C     1 
ATOM   9403  O  O     . PRO A 1 1402 ? 165.740 164.552 199.458 1.00 35.84  ? 2619 PRO A O     1 
ATOM   9404  C  CB    . PRO A 1 1402 ? 167.297 166.720 197.806 1.00 25.45  ? 2619 PRO A CB    1 
ATOM   9405  C  CG    . PRO A 1 1402 ? 168.393 167.107 196.897 1.00 27.27  ? 2619 PRO A CG    1 
ATOM   9406  C  CD    . PRO A 1 1402 ? 168.505 166.000 195.880 1.00 29.43  ? 2619 PRO A CD    1 
ATOM   9407  N  N     . ARG A 1 1403 ? 165.405 163.962 197.304 1.00 26.80  ? 2620 ARG A N     1 
ATOM   9408  C  CA    . ARG A 1 1403 ? 164.161 163.264 197.607 1.00 26.56  ? 2620 ARG A CA    1 
ATOM   9409  C  C     . ARG A 1 1403 ? 164.397 162.065 198.512 1.00 31.37  ? 2620 ARG A C     1 
ATOM   9410  O  O     . ARG A 1 1403 ? 163.557 161.748 199.359 1.00 35.05  ? 2620 ARG A O     1 
ATOM   9411  C  CB    . ARG A 1 1403 ? 163.475 162.828 196.318 1.00 28.43  ? 2620 ARG A CB    1 
ATOM   9412  C  CG    . ARG A 1 1403 ? 162.355 163.741 195.903 1.00 31.10  ? 2620 ARG A CG    1 
ATOM   9413  C  CD    . ARG A 1 1403 ? 161.699 163.231 194.655 1.00 32.23  ? 2620 ARG A CD    1 
ATOM   9414  N  NE    . ARG A 1 1403 ? 162.548 163.436 193.493 1.00 31.86  ? 2620 ARG A NE    1 
ATOM   9415  C  CZ    . ARG A 1 1403 ? 162.089 163.651 192.271 1.00 37.19  ? 2620 ARG A CZ    1 
ATOM   9416  N  NH1   . ARG A 1 1403 ? 160.791 163.698 192.020 1.00 40.62  ? 2620 ARG A NH1   1 
ATOM   9417  N  NH2   . ARG A 1 1403 ? 162.951 163.810 191.273 1.00 37.88  ? 2620 ARG A NH2   1 
ATOM   9418  N  N     . GLU A 1 1404 ? 165.532 161.381 198.348 1.00 32.79  ? 2621 GLU A N     1 
ATOM   9419  C  CA    . GLU A 1 1404 ? 165.859 160.282 199.252 1.00 31.58  ? 2621 GLU A CA    1 
ATOM   9420  C  C     . GLU A 1 1404 ? 166.105 160.769 200.673 1.00 31.92  ? 2621 GLU A C     1 
ATOM   9421  O  O     . GLU A 1 1404 ? 165.696 160.105 201.630 1.00 33.61  ? 2621 GLU A O     1 
ATOM   9422  C  CB    . GLU A 1 1404 ? 167.056 159.494 198.729 1.00 29.61  ? 2621 GLU A CB    1 
ATOM   9423  C  CG    . GLU A 1 1404 ? 166.908 159.052 197.293 1.00 34.25  ? 2621 GLU A CG    1 
ATOM   9424  C  CD    . GLU A 1 1404 ? 165.998 157.841 197.178 1.00 39.31  ? 2621 GLU A CD    1 
ATOM   9425  O  OE1   . GLU A 1 1404 ? 165.613 157.473 196.054 1.00 40.59  ? 2621 GLU A OE1   1 
ATOM   9426  O  OE2   . GLU A 1 1404 ? 165.673 157.240 198.220 1.00 43.22  ? 2621 GLU A OE2   1 
ATOM   9427  N  N     . LEU A 1 1405 ? 166.766 161.917 200.841 1.00 29.95  ? 2622 LEU A N     1 
ATOM   9428  C  CA    . LEU A 1 1405 ? 166.942 162.453 202.189 1.00 29.55  ? 2622 LEU A CA    1 
ATOM   9429  C  C     . LEU A 1 1405 ? 165.605 162.835 202.805 1.00 30.56  ? 2622 LEU A C     1 
ATOM   9430  O  O     . LEU A 1 1405 ? 165.375 162.598 203.998 1.00 32.21  ? 2622 LEU A O     1 
ATOM   9431  C  CB    . LEU A 1 1405 ? 167.874 163.663 202.188 1.00 27.66  ? 2622 LEU A CB    1 
ATOM   9432  C  CG    . LEU A 1 1405 ? 169.348 163.474 201.850 1.00 26.36  ? 2622 LEU A CG    1 
ATOM   9433  C  CD1   . LEU A 1 1405 ? 169.530 163.623 200.372 1.00 28.32  ? 2622 LEU A CD1   1 
ATOM   9434  C  CD2   . LEU A 1 1405 ? 170.214 164.465 202.600 1.00 31.59  ? 2622 LEU A CD2   1 
ATOM   9435  N  N     . THR A 1 1406 ? 164.711 163.428 202.012 1.00 29.16  ? 2623 THR A N     1 
ATOM   9436  C  CA    . THR A 1 1406 ? 163.402 163.787 202.549 1.00 31.57  ? 2623 THR A CA    1 
ATOM   9437  C  C     . THR A 1 1406 ? 162.584 162.547 202.893 1.00 35.77  ? 2623 THR A C     1 
ATOM   9438  O  O     . THR A 1 1406 ? 161.875 162.529 203.905 1.00 38.30  ? 2623 THR A O     1 
ATOM   9439  C  CB    . THR A 1 1406 ? 162.647 164.671 201.563 1.00 32.54  ? 2623 THR A CB    1 
ATOM   9440  O  OG1   . THR A 1 1406 ? 162.540 163.999 200.305 1.00 36.49  ? 2623 THR A OG1   1 
ATOM   9441  C  CG2   . THR A 1 1406 ? 163.386 165.978 201.373 1.00 27.83  ? 2623 THR A CG2   1 
ATOM   9442  N  N     . ARG A 1 1407 ? 162.681 161.495 202.074 1.00 34.96  ? 2624 ARG A N     1 
ATOM   9443  C  CA    . ARG A 1 1407 ? 161.987 160.251 202.389 1.00 34.31  ? 2624 ARG A CA    1 
ATOM   9444  C  C     . ARG A 1 1407 ? 162.569 159.605 203.636 1.00 33.88  ? 2624 ARG A C     1 
ATOM   9445  O  O     . ARG A 1 1407 ? 161.838 159.008 204.431 1.00 33.88  ? 2624 ARG A O     1 
ATOM   9446  C  CB    . ARG A 1 1407 ? 162.069 159.275 201.219 1.00 32.54  ? 2624 ARG A CB    1 
ATOM   9447  C  CG    . ARG A 1 1407 ? 161.036 158.164 201.303 1.00 36.54  ? 2624 ARG A CG    1 
ATOM   9448  C  CD    . ARG A 1 1407 ? 161.353 156.983 200.396 1.00 42.61  ? 2624 ARG A CD    1 
ATOM   9449  N  NE    . ARG A 1 1407 ? 162.175 157.325 199.243 1.00 42.76  ? 2624 ARG A NE    1 
ATOM   9450  C  CZ    . ARG A 1 1407 ? 161.712 157.888 198.138 1.00 44.22  ? 2624 ARG A CZ    1 
ATOM   9451  N  NH1   . ARG A 1 1407 ? 160.440 158.201 198.011 1.00 46.80  ? 2624 ARG A NH1   1 
ATOM   9452  N  NH2   . ARG A 1 1407 ? 162.550 158.143 197.138 1.00 46.74  ? 2624 ARG A NH2   1 
ATOM   9453  N  N     . LEU A 1 1408 ? 163.889 159.700 203.812 1.00 33.94  ? 2625 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 1408 ? 164.525 159.198 205.024 1.00 34.37  ? 2625 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 1408 ? 164.028 159.947 206.251 1.00 33.78  ? 2625 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 1408 ? 163.755 159.337 207.291 1.00 33.70  ? 2625 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 1408 ? 166.042 159.321 204.900 1.00 30.26  ? 2625 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 1408 ? 166.923 158.711 205.988 1.00 31.40  ? 2625 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 1408 ? 168.126 158.064 205.352 1.00 35.86  ? 2625 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 1408 ? 167.370 159.758 206.988 1.00 35.96  ? 2625 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 1409 ? 163.907 161.273 206.146 1.00 34.52  ? 2626 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 1409 ? 163.407 162.071 207.263 1.00 34.06  ? 2626 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 1409 ? 161.960 161.707 207.576 1.00 35.76  ? 2626 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 1409 ? 161.585 161.552 208.743 1.00 37.13  ? 2626 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 1409 ? 163.568 163.571 206.958 1.00 33.44  ? 2626 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 1409 ? 162.754 164.408 207.928 1.00 39.76  ? 2626 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 1409 ? 165.034 163.961 207.020 1.00 34.67  ? 2626 VAL A CG2   1 
ATOM   9468  N  N     . ARG A 1 1410 ? 161.133 161.539 206.540 1.00 36.15  ? 2627 ARG A N     1 
ATOM   9469  C  CA    . ARG A 1 1410 ? 159.741 161.147 206.752 1.00 37.69  ? 2627 ARG A CA    1 
ATOM   9470  C  C     . ARG A 1 1410 ? 159.633 159.751 207.361 1.00 39.35  ? 2627 ARG A C     1 
ATOM   9471  O  O     . ARG A 1 1410 ? 158.775 159.508 208.218 1.00 41.94  ? 2627 ARG A O     1 
ATOM   9472  C  CB    . ARG A 1 1410 ? 158.969 161.220 205.436 1.00 40.54  ? 2627 ARG A CB    1 
ATOM   9473  C  CG    . ARG A 1 1410 ? 158.858 162.623 204.872 1.00 48.28  ? 2627 ARG A CG    1 
ATOM   9474  C  CD    . ARG A 1 1410 ? 157.979 162.671 203.640 1.00 52.84  ? 2627 ARG A CD    1 
ATOM   9475  N  NE    . ARG A 1 1410 ? 157.750 164.044 203.209 1.00 56.22  ? 2627 ARG A NE    1 
ATOM   9476  C  CZ    . ARG A 1 1410 ? 158.229 164.564 202.088 1.00 58.46  ? 2627 ARG A CZ    1 
ATOM   9477  N  NH1   . ARG A 1 1410 ? 158.965 163.848 201.254 1.00 55.32  ? 2627 ARG A NH1   1 
ATOM   9478  N  NH2   . ARG A 1 1410 ? 157.966 165.834 201.798 1.00 59.61  ? 2627 ARG A NH2   1 
ATOM   9479  N  N     . GLY A 1 1411 ? 160.485 158.821 206.927 1.00 37.04  ? 2628 GLY A N     1 
ATOM   9480  C  CA    . GLY A 1 1411 ? 160.468 157.485 207.500 1.00 36.12  ? 2628 GLY A CA    1 
ATOM   9481  C  C     . GLY A 1 1411 ? 160.906 157.467 208.951 1.00 37.18  ? 2628 GLY A C     1 
ATOM   9482  O  O     . GLY A 1 1411 ? 160.291 156.796 209.786 1.00 40.13  ? 2628 GLY A O     1 
ATOM   9483  N  N     . VAL A 1 1412 ? 161.964 158.214 209.275 1.00 33.86  ? 2629 VAL A N     1 
ATOM   9484  C  CA    . VAL A 1 1412 ? 162.398 158.321 210.663 1.00 30.86  ? 2629 VAL A CA    1 
ATOM   9485  C  C     . VAL A 1 1412 ? 161.311 158.981 211.501 1.00 36.51  ? 2629 VAL A C     1 
ATOM   9486  O  O     . VAL A 1 1412 ? 161.064 158.584 212.645 1.00 38.33  ? 2629 VAL A O     1 
ATOM   9487  C  CB    . VAL A 1 1412 ? 163.737 159.078 210.746 1.00 29.49  ? 2629 VAL A CB    1 
ATOM   9488  C  CG1   . VAL A 1 1412 ? 164.074 159.440 212.179 1.00 32.45  ? 2629 VAL A CG1   1 
ATOM   9489  C  CG2   . VAL A 1 1412 ? 164.850 158.236 210.154 1.00 28.94  ? 2629 VAL A CG2   1 
ATOM   9490  N  N     . TYR A 1 1413 ? 160.599 159.953 210.924 1.00 39.01  ? 2630 TYR A N     1 
ATOM   9491  C  CA    . TYR A 1 1413 ? 159.534 160.623 211.661 1.00 39.02  ? 2630 TYR A CA    1 
ATOM   9492  C  C     . TYR A 1 1413 ? 158.365 159.690 211.938 1.00 41.64  ? 2630 TYR A C     1 
ATOM   9493  O  O     . TYR A 1 1413 ? 157.843 159.665 213.057 1.00 43.17  ? 2630 TYR A O     1 
ATOM   9494  C  CB    . TYR A 1 1413 ? 159.045 161.852 210.899 1.00 41.61  ? 2630 TYR A CB    1 
ATOM   9495  C  CG    . TYR A 1 1413 ? 157.984 162.603 211.656 1.00 49.25  ? 2630 TYR A CG    1 
ATOM   9496  C  CD1   . TYR A 1 1413 ? 158.318 163.404 212.735 1.00 52.06  ? 2630 TYR A CD1   1 
ATOM   9497  C  CD2   . TYR A 1 1413 ? 156.648 162.487 211.315 1.00 55.23  ? 2630 TYR A CD2   1 
ATOM   9498  C  CE1   . TYR A 1 1413 ? 157.351 164.084 213.441 1.00 56.71  ? 2630 TYR A CE1   1 
ATOM   9499  C  CE2   . TYR A 1 1413 ? 155.673 163.160 212.017 1.00 60.12  ? 2630 TYR A CE2   1 
ATOM   9500  C  CZ    . TYR A 1 1413 ? 156.028 163.959 213.077 1.00 63.35  ? 2630 TYR A CZ    1 
ATOM   9501  O  OH    . TYR A 1 1413 ? 155.051 164.631 213.772 1.00 77.09  ? 2630 TYR A OH    1 
ATOM   9502  N  N     . THR A 1 1414 ? 157.924 158.933 210.933 1.00 43.22  ? 2631 THR A N     1 
ATOM   9503  C  CA    . THR A 1 1414 ? 156.796 158.040 211.164 1.00 46.40  ? 2631 THR A CA    1 
ATOM   9504  C  C     . THR A 1 1414 ? 157.186 156.879 212.071 1.00 48.42  ? 2631 THR A C     1 
ATOM   9505  O  O     . THR A 1 1414 ? 156.343 156.376 212.823 1.00 54.40  ? 2631 THR A O     1 
ATOM   9506  C  CB    . THR A 1 1414 ? 156.211 157.545 209.834 1.00 42.97  ? 2631 THR A CB    1 
ATOM   9507  O  OG1   . THR A 1 1414 ? 154.996 156.827 210.083 1.00 51.00  ? 2631 THR A OG1   1 
ATOM   9508  C  CG2   . THR A 1 1414 ? 157.179 156.651 209.084 1.00 41.54  ? 2631 THR A CG2   1 
ATOM   9509  N  N     . ALA A 1 1415 ? 158.461 156.480 212.064 1.00 43.35  ? 2632 ALA A N     1 
ATOM   9510  C  CA    . ALA A 1 1415 ? 158.898 155.428 212.973 1.00 44.37  ? 2632 ALA A CA    1 
ATOM   9511  C  C     . ALA A 1 1415 ? 159.004 155.937 214.407 1.00 47.85  ? 2632 ALA A C     1 
ATOM   9512  O  O     . ALA A 1 1415 ? 158.703 155.202 215.354 1.00 49.70  ? 2632 ALA A O     1 
ATOM   9513  C  CB    . ALA A 1 1415 ? 160.229 154.855 212.499 1.00 41.75  ? 2632 ALA A CB    1 
ATOM   9514  N  N     . ILE A 1 1416 ? 159.436 157.189 214.587 1.00 48.14  ? 2633 ILE A N     1 
ATOM   9515  C  CA    . ILE A 1 1416 ? 159.501 157.773 215.925 1.00 47.40  ? 2633 ILE A CA    1 
ATOM   9516  C  C     . ILE A 1 1416 ? 158.098 158.023 216.466 1.00 47.86  ? 2633 ILE A C     1 
ATOM   9517  O  O     . ILE A 1 1416 ? 157.811 157.748 217.638 1.00 50.46  ? 2633 ILE A O     1 
ATOM   9518  C  CB    . ILE A 1 1416 ? 160.345 159.062 215.897 1.00 42.52  ? 2633 ILE A CB    1 
ATOM   9519  C  CG1   . ILE A 1 1416 ? 161.831 158.732 215.731 1.00 37.94  ? 2633 ILE A CG1   1 
ATOM   9520  C  CG2   . ILE A 1 1416 ? 160.113 159.902 217.145 1.00 45.45  ? 2633 ILE A CG2   1 
ATOM   9521  C  CD1   . ILE A 1 1416 ? 162.511 158.284 216.994 1.00 45.25  ? 2633 ILE A CD1   1 
ATOM   9522  N  N     . ASN A 1 1417 ? 157.203 158.538 215.620 1.00 46.50  ? 2634 ASN A N     1 
ATOM   9523  C  CA    . ASN A 1 1417 ? 155.832 158.812 216.039 1.00 51.88  ? 2634 ASN A CA    1 
ATOM   9524  C  C     . ASN A 1 1417 ? 155.083 157.525 216.363 1.00 57.36  ? 2634 ASN A C     1 
ATOM   9525  O  O     . ASN A 1 1417 ? 154.374 157.451 217.373 1.00 58.06  ? 2634 ASN A O     1 
ATOM   9526  C  CB    . ASN A 1 1417 ? 155.114 159.600 214.943 1.00 54.26  ? 2634 ASN A CB    1 
ATOM   9527  C  CG    . ASN A 1 1417 ? 153.794 160.190 215.404 1.00 63.85  ? 2634 ASN A CG    1 
ATOM   9528  O  OD1   . ASN A 1 1417 ? 153.382 160.019 216.551 1.00 66.18  ? 2634 ASN A OD1   1 
ATOM   9529  N  ND2   . ASN A 1 1417 ? 153.124 160.898 214.503 1.00 67.99  ? 2634 ASN A ND2   1 
ATOM   9530  N  N     . THR A 1 1418 ? 155.230 156.498 215.524 1.00 57.38  ? 2635 THR A N     1 
ATOM   9531  C  CA    . THR A 1 1418 ? 154.583 155.213 215.745 1.00 54.11  ? 2635 THR A CA    1 
ATOM   9532  C  C     . THR A 1 1418 ? 155.440 154.257 216.569 1.00 55.97  ? 2635 THR A C     1 
ATOM   9533  O  O     . THR A 1 1418 ? 155.235 153.040 216.500 1.00 61.30  ? 2635 THR A O     1 
ATOM   9534  C  CB    . THR A 1 1418 ? 154.222 154.569 214.405 1.00 54.92  ? 2635 THR A CB    1 
ATOM   9535  O  OG1   . THR A 1 1418 ? 155.415 154.354 213.640 1.00 51.01  ? 2635 THR A OG1   1 
ATOM   9536  C  CG2   . THR A 1 1418 ? 153.278 155.469 213.622 1.00 57.43  ? 2635 THR A CG2   1 
ATOM   9537  N  N     . GLY A 1 1419 ? 156.388 154.777 217.343 1.00 58.83  ? 2636 GLY A N     1 
ATOM   9538  C  CA    . GLY A 1 1419 ? 157.273 153.948 218.125 1.00 62.79  ? 2636 GLY A CA    1 
ATOM   9539  C  C     . GLY A 1 1419 ? 157.245 154.291 219.600 1.00 64.38  ? 2636 GLY A C     1 
ATOM   9540  O  O     . GLY A 1 1419 ? 156.612 155.261 220.027 1.00 64.42  ? 2636 GLY A O     1 
ATOM   9541  N  N     . PRO A 1 1420 ? 157.938 153.491 220.412 1.00 66.51  ? 2637 PRO A N     1 
ATOM   9542  C  CA    . PRO A 1 1420 ? 157.945 153.729 221.860 1.00 72.56  ? 2637 PRO A CA    1 
ATOM   9543  C  C     . PRO A 1 1420 ? 158.932 154.812 222.263 1.00 76.72  ? 2637 PRO A C     1 
ATOM   9544  O  O     . PRO A 1 1420 ? 159.496 155.491 221.401 1.00 79.17  ? 2637 PRO A O     1 
ATOM   9545  C  CB    . PRO A 1 1420 ? 158.344 152.365 222.428 1.00 73.81  ? 2637 PRO A CB    1 
ATOM   9546  C  CG    . PRO A 1 1420 ? 159.246 151.797 221.378 1.00 70.92  ? 2637 PRO A CG    1 
ATOM   9547  C  CD    . PRO A 1 1420 ? 158.754 152.320 220.043 1.00 68.32  ? 2637 PRO A CD    1 
ATOM   9548  N  N     . ARG A 1 1421 ? 159.125 154.995 223.569 1.00 77.16  ? 2638 ARG A N     1 
ATOM   9549  C  CA    . ARG A 1 1421 ? 160.131 155.927 224.062 1.00 76.52  ? 2638 ARG A CA    1 
ATOM   9550  C  C     . ARG A 1 1421 ? 161.521 155.463 223.639 1.00 73.38  ? 2638 ARG A C     1 
ATOM   9551  O  O     . ARG A 1 1421 ? 161.842 154.273 223.713 1.00 70.67  ? 2638 ARG A O     1 
ATOM   9552  C  CB    . ARG A 1 1421 ? 160.004 156.057 225.585 1.00 78.60  ? 2638 ARG A CB    1 
ATOM   9553  C  CG    . ARG A 1 1421 ? 161.071 156.877 226.300 1.00 81.42  ? 2638 ARG A CG    1 
ATOM   9554  C  CD    . ARG A 1 1421 ? 161.630 156.136 227.528 1.00 82.03  ? 2638 ARG A CD    1 
ATOM   9555  N  NE    . ARG A 1 1421 ? 162.074 154.764 227.295 1.00 81.48  ? 2638 ARG A NE    1 
ATOM   9556  C  CZ    . ARG A 1 1421 ? 163.064 154.406 226.488 1.00 82.07  ? 2638 ARG A CZ    1 
ATOM   9557  N  NH1   . ARG A 1 1421 ? 163.814 155.302 225.871 1.00 81.82  ? 2638 ARG A NH1   1 
ATOM   9558  N  NH2   . ARG A 1 1421 ? 163.327 153.113 226.319 1.00 82.20  ? 2638 ARG A NH2   1 
ATOM   9559  N  N     . GLN A 1 1422 ? 162.335 156.403 223.162 1.00 74.23  ? 2639 GLN A N     1 
ATOM   9560  C  CA    . GLN A 1 1422 ? 163.549 156.093 222.416 1.00 73.99  ? 2639 GLN A CA    1 
ATOM   9561  C  C     . GLN A 1 1422 ? 164.792 156.493 223.196 1.00 75.55  ? 2639 GLN A C     1 
ATOM   9562  O  O     . GLN A 1 1422 ? 164.866 157.603 223.734 1.00 76.67  ? 2639 GLN A O     1 
ATOM   9563  C  CB    . GLN A 1 1422 ? 163.551 156.804 221.061 1.00 70.07  ? 2639 GLN A CB    1 
ATOM   9564  C  CG    . GLN A 1 1422 ? 162.253 156.694 220.295 1.00 67.36  ? 2639 GLN A CG    1 
ATOM   9565  C  CD    . GLN A 1 1422 ? 162.111 155.360 219.592 1.00 72.51  ? 2639 GLN A CD    1 
ATOM   9566  O  OE1   . GLN A 1 1422 ? 163.101 154.757 219.178 1.00 73.30  ? 2639 GLN A OE1   1 
ATOM   9567  N  NE2   . GLN A 1 1422 ? 160.877 154.893 219.451 1.00 72.37  ? 2639 GLN A NE2   1 
ATOM   9568  N  N     . THR A 1 1423 ? 165.765 155.585 223.252 1.00 72.85  ? 2640 THR A N     1 
ATOM   9569  C  CA    . THR A 1 1423 ? 167.090 155.892 223.761 1.00 74.53  ? 2640 THR A CA    1 
ATOM   9570  C  C     . THR A 1 1423 ? 167.949 156.447 222.628 1.00 73.60  ? 2640 THR A C     1 
ATOM   9571  O  O     . THR A 1 1423 ? 167.506 156.572 221.484 1.00 74.19  ? 2640 THR A O     1 
ATOM   9572  C  CB    . THR A 1 1423 ? 167.740 154.651 224.370 1.00 73.19  ? 2640 THR A CB    1 
ATOM   9573  O  OG1   . THR A 1 1423 ? 168.014 153.698 223.336 1.00 72.36  ? 2640 THR A OG1   1 
ATOM   9574  C  CG2   . THR A 1 1423 ? 166.826 154.016 225.402 1.00 75.14  ? 2640 THR A CG2   1 
ATOM   9575  N  N     . LEU A 1 1424 ? 169.196 156.799 222.948 1.00 72.01  ? 2641 LEU A N     1 
ATOM   9576  C  CA    . LEU A 1 1424 ? 170.125 157.214 221.902 1.00 72.56  ? 2641 LEU A CA    1 
ATOM   9577  C  C     . LEU A 1 1424 ? 170.470 156.050 220.982 1.00 71.53  ? 2641 LEU A C     1 
ATOM   9578  O  O     . LEU A 1 1424 ? 170.492 156.207 219.756 1.00 70.88  ? 2641 LEU A O     1 
ATOM   9579  C  CB    . LEU A 1 1424 ? 171.391 157.803 222.524 1.00 75.66  ? 2641 LEU A CB    1 
ATOM   9580  C  CG    . LEU A 1 1424 ? 172.391 158.416 221.541 1.00 77.98  ? 2641 LEU A CG    1 
ATOM   9581  C  CD1   . LEU A 1 1424 ? 171.768 159.590 220.803 1.00 79.22  ? 2641 LEU A CD1   1 
ATOM   9582  C  CD2   . LEU A 1 1424 ? 173.660 158.845 222.260 1.00 80.49  ? 2641 LEU A CD2   1 
ATOM   9583  N  N     . ARG A 1 1425 ? 170.727 154.873 221.558 1.00 70.93  ? 2642 ARG A N     1 
ATOM   9584  C  CA    . ARG A 1 1425 ? 171.046 153.696 220.757 1.00 68.30  ? 2642 ARG A CA    1 
ATOM   9585  C  C     . ARG A 1 1425 ? 169.868 153.287 219.883 1.00 68.56  ? 2642 ARG A C     1 
ATOM   9586  O  O     . ARG A 1 1425 ? 170.050 152.915 218.717 1.00 68.74  ? 2642 ARG A O     1 
ATOM   9587  C  CB    . ARG A 1 1425 ? 171.462 152.547 221.674 1.00 73.20  ? 2642 ARG A CB    1 
ATOM   9588  C  CG    . ARG A 1 1425 ? 171.766 151.241 220.964 1.00 77.17  ? 2642 ARG A CG    1 
ATOM   9589  C  CD    . ARG A 1 1425 ? 172.101 150.155 221.970 1.00 79.27  ? 2642 ARG A CD    1 
ATOM   9590  N  NE    . ARG A 1 1425 ? 172.836 149.051 221.366 1.00 81.75  ? 2642 ARG A NE    1 
ATOM   9591  C  CZ    . ARG A 1 1425 ? 174.157 148.994 221.275 1.00 84.36  ? 2642 ARG A CZ    1 
ATOM   9592  N  NH1   . ARG A 1 1425 ? 174.924 149.975 221.724 1.00 82.28  ? 2642 ARG A NH1   1 
ATOM   9593  N  NH2   . ARG A 1 1425 ? 174.724 147.927 220.720 1.00 84.24  ? 2642 ARG A NH2   1 
ATOM   9594  N  N     . SER A 1 1426 ? 168.652 153.351 220.432 1.00 71.31  ? 2643 SER A N     1 
ATOM   9595  C  CA    . SER A 1 1426 ? 167.463 153.043 219.645 1.00 67.94  ? 2643 SER A CA    1 
ATOM   9596  C  C     . SER A 1 1426 ? 167.289 154.036 218.505 1.00 64.09  ? 2643 SER A C     1 
ATOM   9597  O  O     . SER A 1 1426 ? 166.909 153.655 217.394 1.00 61.48  ? 2643 SER A O     1 
ATOM   9598  C  CB    . SER A 1 1426 ? 166.225 153.031 220.540 1.00 70.93  ? 2643 SER A CB    1 
ATOM   9599  O  OG    . SER A 1 1426 ? 165.944 154.330 221.026 1.00 70.62  ? 2643 SER A OG    1 
ATOM   9600  N  N     . LEU A 1 1427 ? 167.578 155.315 218.760 1.00 64.64  ? 2644 LEU A N     1 
ATOM   9601  C  CA    . LEU A 1 1427 ? 167.493 156.325 217.710 1.00 62.75  ? 2644 LEU A CA    1 
ATOM   9602  C  C     . LEU A 1 1427 ? 168.509 156.066 216.603 1.00 61.19  ? 2644 LEU A C     1 
ATOM   9603  O  O     . LEU A 1 1427 ? 168.179 156.161 215.413 1.00 58.45  ? 2644 LEU A O     1 
ATOM   9604  C  CB    . LEU A 1 1427 ? 167.699 157.713 218.314 1.00 65.54  ? 2644 LEU A CB    1 
ATOM   9605  C  CG    . LEU A 1 1427 ? 167.484 158.928 217.416 1.00 64.23  ? 2644 LEU A CG    1 
ATOM   9606  C  CD1   . LEU A 1 1427 ? 166.178 158.807 216.656 1.00 61.34  ? 2644 LEU A CD1   1 
ATOM   9607  C  CD2   . LEU A 1 1427 ? 167.507 160.195 218.251 1.00 65.10  ? 2644 LEU A CD2   1 
ATOM   9608  N  N     . ILE A 1 1428 ? 169.748 155.728 216.975 1.00 62.05  ? 2645 ILE A N     1 
ATOM   9609  C  CA    . ILE A 1 1428 ? 170.784 155.463 215.977 1.00 57.34  ? 2645 ILE A CA    1 
ATOM   9610  C  C     . ILE A 1 1428 ? 170.435 154.233 215.149 1.00 54.43  ? 2645 ILE A C     1 
ATOM   9611  O  O     . ILE A 1 1428 ? 170.570 154.238 213.919 1.00 52.98  ? 2645 ILE A O     1 
ATOM   9612  C  CB    . ILE A 1 1428 ? 172.161 155.314 216.650 1.00 60.95  ? 2645 ILE A CB    1 
ATOM   9613  C  CG1   . ILE A 1 1428 ? 172.540 156.595 217.389 1.00 67.27  ? 2645 ILE A CG1   1 
ATOM   9614  C  CG2   . ILE A 1 1428 ? 173.224 154.969 215.623 1.00 65.98  ? 2645 ILE A CG2   1 
ATOM   9615  C  CD1   . ILE A 1 1428 ? 172.654 157.792 216.495 1.00 68.64  ? 2645 ILE A CD1   1 
ATOM   9616  N  N     . ARG A 1 1429 ? 169.976 153.161 215.802 1.00 56.70  ? 2646 ARG A N     1 
ATOM   9617  C  CA    . ARG A 1 1429 ? 169.640 151.957 215.051 1.00 55.37  ? 2646 ARG A CA    1 
ATOM   9618  C  C     . ARG A 1 1429 ? 168.392 152.157 214.199 1.00 53.55  ? 2646 ARG A C     1 
ATOM   9619  O  O     . ARG A 1 1429 ? 168.292 151.577 213.113 1.00 54.05  ? 2646 ARG A O     1 
ATOM   9620  C  CB    . ARG A 1 1429 ? 169.482 150.761 215.993 1.00 60.81  ? 2646 ARG A CB    1 
ATOM   9621  C  CG    . ARG A 1 1429 ? 168.270 150.796 216.898 1.00 60.76  ? 2646 ARG A CG    1 
ATOM   9622  C  CD    . ARG A 1 1429 ? 168.040 149.456 217.564 1.00 62.54  ? 2646 ARG A CD    1 
ATOM   9623  N  NE    . ARG A 1 1429 ? 169.201 149.018 218.327 1.00 62.69  ? 2646 ARG A NE    1 
ATOM   9624  C  CZ    . ARG A 1 1429 ? 169.825 147.863 218.142 1.00 62.88  ? 2646 ARG A CZ    1 
ATOM   9625  N  NH1   . ARG A 1 1429 ? 169.424 147.001 217.223 1.00 57.70  ? 2646 ARG A NH1   1 
ATOM   9626  N  NH2   . ARG A 1 1429 ? 170.876 147.565 218.900 1.00 69.71  ? 2646 ARG A NH2   1 
ATOM   9627  N  N     . LEU A 1 1430 ? 167.450 152.993 214.648 1.00 54.60  ? 2647 LEU A N     1 
ATOM   9628  C  CA    . LEU A 1 1430 ? 166.292 153.315 213.824 1.00 51.87  ? 2647 LEU A CA    1 
ATOM   9629  C  C     . LEU A 1 1430 ? 166.697 154.106 212.589 1.00 47.44  ? 2647 LEU A C     1 
ATOM   9630  O  O     . LEU A 1 1430 ? 166.203 153.841 211.487 1.00 45.41  ? 2647 LEU A O     1 
ATOM   9631  C  CB    . LEU A 1 1430 ? 165.268 154.094 214.645 1.00 48.87  ? 2647 LEU A CB    1 
ATOM   9632  C  CG    . LEU A 1 1430 ? 163.998 154.486 213.900 1.00 37.94  ? 2647 LEU A CG    1 
ATOM   9633  C  CD1   . LEU A 1 1430 ? 163.345 153.239 213.340 1.00 41.60  ? 2647 LEU A CD1   1 
ATOM   9634  C  CD2   . LEU A 1 1430 ? 163.056 155.222 214.830 1.00 41.89  ? 2647 LEU A CD2   1 
ATOM   9635  N  N     . TRP A 1 1431 ? 167.599 155.077 212.755 1.00 49.36  ? 2648 TRP A N     1 
ATOM   9636  C  CA    . TRP A 1 1431 ? 168.085 155.835 211.608 1.00 49.20  ? 2648 TRP A CA    1 
ATOM   9637  C  C     . TRP A 1 1431 ? 168.848 154.941 210.640 1.00 49.76  ? 2648 TRP A C     1 
ATOM   9638  O  O     . TRP A 1 1431 ? 168.710 155.077 209.420 1.00 50.01  ? 2648 TRP A O     1 
ATOM   9639  C  CB    . TRP A 1 1431 ? 168.967 156.994 212.072 1.00 49.96  ? 2648 TRP A CB    1 
ATOM   9640  C  CG    . TRP A 1 1431 ? 169.749 157.616 210.962 1.00 48.60  ? 2648 TRP A CG    1 
ATOM   9641  C  CD1   . TRP A 1 1431 ? 169.303 158.543 210.069 1.00 47.22  ? 2648 TRP A CD1   1 
ATOM   9642  C  CD2   . TRP A 1 1431 ? 171.114 157.354 210.620 1.00 51.56  ? 2648 TRP A CD2   1 
ATOM   9643  N  NE1   . TRP A 1 1431 ? 170.305 158.877 209.193 1.00 48.82  ? 2648 TRP A NE1   1 
ATOM   9644  C  CE2   . TRP A 1 1431 ? 171.428 158.159 209.510 1.00 53.49  ? 2648 TRP A CE2   1 
ATOM   9645  C  CE3   . TRP A 1 1431 ? 172.100 156.515 211.145 1.00 54.76  ? 2648 TRP A CE3   1 
ATOM   9646  C  CZ2   . TRP A 1 1431 ? 172.687 158.153 208.916 1.00 59.45  ? 2648 TRP A CZ2   1 
ATOM   9647  C  CZ3   . TRP A 1 1431 ? 173.349 156.510 210.555 1.00 55.88  ? 2648 TRP A CZ3   1 
ATOM   9648  C  CH2   . TRP A 1 1431 ? 173.632 157.323 209.451 1.00 60.90  ? 2648 TRP A CH2   1 
ATOM   9649  N  N     . ALA A 1 1432 ? 169.655 154.015 211.166 1.00 50.51  ? 2649 ALA A N     1 
ATOM   9650  C  CA    . ALA A 1 1432 ? 170.390 153.094 210.304 1.00 50.48  ? 2649 ALA A CA    1 
ATOM   9651  C  C     . ALA A 1 1432 ? 169.448 152.164 209.549 1.00 48.68  ? 2649 ALA A C     1 
ATOM   9652  O  O     . ALA A 1 1432 ? 169.637 151.916 208.352 1.00 50.58  ? 2649 ALA A O     1 
ATOM   9653  C  CB    . ALA A 1 1432 ? 171.389 152.290 211.132 1.00 55.86  ? 2649 ALA A CB    1 
ATOM   9654  N  N     . TYR A 1 1433 ? 168.426 151.645 210.233 1.00 47.59  ? 2650 TYR A N     1 
ATOM   9655  C  CA    . TYR A 1 1433 ? 167.451 150.776 209.584 1.00 49.07  ? 2650 TYR A CA    1 
ATOM   9656  C  C     . TYR A 1 1433 ? 166.684 151.520 208.501 1.00 49.33  ? 2650 TYR A C     1 
ATOM   9657  O  O     . TYR A 1 1433 ? 166.448 150.981 207.413 1.00 52.62  ? 2650 TYR A O     1 
ATOM   9658  C  CB    . TYR A 1 1433 ? 166.493 150.215 210.631 1.00 52.68  ? 2650 TYR A CB    1 
ATOM   9659  C  CG    . TYR A 1 1433 ? 165.219 149.639 210.069 1.00 52.87  ? 2650 TYR A CG    1 
ATOM   9660  C  CD1   . TYR A 1 1433 ? 165.238 148.481 209.307 1.00 56.21  ? 2650 TYR A CD1   1 
ATOM   9661  C  CD2   . TYR A 1 1433 ? 163.997 150.248 210.305 1.00 52.80  ? 2650 TYR A CD2   1 
ATOM   9662  C  CE1   . TYR A 1 1433 ? 164.076 147.945 208.798 1.00 56.54  ? 2650 TYR A CE1   1 
ATOM   9663  C  CE2   . TYR A 1 1433 ? 162.829 149.722 209.799 1.00 53.24  ? 2650 TYR A CE2   1 
ATOM   9664  C  CZ    . TYR A 1 1433 ? 162.875 148.571 209.045 1.00 55.28  ? 2650 TYR A CZ    1 
ATOM   9665  O  OH    . TYR A 1 1433 ? 161.714 148.040 208.537 1.00 55.12  ? 2650 TYR A OH    1 
ATOM   9666  N  N     . GLU A 1 1434 ? 166.296 152.767 208.779 1.00 47.12  ? 2651 GLU A N     1 
ATOM   9667  C  CA    . GLU A 1 1434 ? 165.584 153.557 207.782 1.00 43.43  ? 2651 GLU A CA    1 
ATOM   9668  C  C     . GLU A 1 1434 ? 166.477 153.878 206.591 1.00 45.32  ? 2651 GLU A C     1 
ATOM   9669  O  O     . GLU A 1 1434 ? 166.025 153.829 205.442 1.00 47.69  ? 2651 GLU A O     1 
ATOM   9670  C  CB    . GLU A 1 1434 ? 165.047 154.836 208.417 1.00 41.16  ? 2651 GLU A CB    1 
ATOM   9671  C  CG    . GLU A 1 1434 ? 163.937 155.479 207.627 1.00 41.00  ? 2651 GLU A CG    1 
ATOM   9672  C  CD    . GLU A 1 1434 ? 162.825 154.504 207.319 1.00 45.97  ? 2651 GLU A CD    1 
ATOM   9673  O  OE1   . GLU A 1 1434 ? 162.344 153.836 208.257 1.00 51.71  ? 2651 GLU A OE1   1 
ATOM   9674  O  OE2   . GLU A 1 1434 ? 162.433 154.402 206.140 1.00 43.62  ? 2651 GLU A OE2   1 
ATOM   9675  N  N     . ALA A 1 1435 ? 167.748 154.206 206.842 1.00 43.52  ? 2652 ALA A N     1 
ATOM   9676  C  CA    . ALA A 1 1435 ? 168.678 154.466 205.749 1.00 42.10  ? 2652 ALA A CA    1 
ATOM   9677  C  C     . ALA A 1 1435 ? 168.869 153.229 204.887 1.00 44.39  ? 2652 ALA A C     1 
ATOM   9678  O  O     . ALA A 1 1435 ? 168.943 153.325 203.657 1.00 47.13  ? 2652 ALA A O     1 
ATOM   9679  C  CB    . ALA A 1 1435 ? 170.018 154.949 206.300 1.00 43.94  ? 2652 ALA A CB    1 
ATOM   9680  N  N     . TRP A 1 1436 ? 168.943 152.056 205.516 1.00 49.18  ? 2653 TRP A N     1 
ATOM   9681  C  CA    . TRP A 1 1436 ? 169.048 150.815 204.757 1.00 53.40  ? 2653 TRP A CA    1 
ATOM   9682  C  C     . TRP A 1 1436 ? 167.793 150.561 203.932 1.00 46.86  ? 2653 TRP A C     1 
ATOM   9683  O  O     . TRP A 1 1436 ? 167.877 150.109 202.784 1.00 48.55  ? 2653 TRP A O     1 
ATOM   9684  C  CB    . TRP A 1 1436 ? 169.319 149.647 205.705 1.00 55.88  ? 2653 TRP A CB    1 
ATOM   9685  C  CG    . TRP A 1 1436 ? 170.774 149.353 205.869 1.00 57.84  ? 2653 TRP A CG    1 
ATOM   9686  C  CD1   . TRP A 1 1436 ? 171.632 149.922 206.764 1.00 57.90  ? 2653 TRP A CD1   1 
ATOM   9687  C  CD2   . TRP A 1 1436 ? 171.547 148.423 205.107 1.00 59.31  ? 2653 TRP A CD2   1 
ATOM   9688  N  NE1   . TRP A 1 1436 ? 172.892 149.400 206.608 1.00 58.99  ? 2653 TRP A NE1   1 
ATOM   9689  C  CE2   . TRP A 1 1436 ? 172.866 148.477 205.596 1.00 61.10  ? 2653 TRP A CE2   1 
ATOM   9690  C  CE3   . TRP A 1 1436 ? 171.251 147.547 204.058 1.00 58.82  ? 2653 TRP A CE3   1 
ATOM   9691  C  CZ2   . TRP A 1 1436 ? 173.887 147.689 205.074 1.00 65.74  ? 2653 TRP A CZ2   1 
ATOM   9692  C  CZ3   . TRP A 1 1436 ? 172.264 146.767 203.542 1.00 62.74  ? 2653 TRP A CZ3   1 
ATOM   9693  C  CH2   . TRP A 1 1436 ? 173.566 146.842 204.051 1.00 66.20  ? 2653 TRP A CH2   1 
ATOM   9694  N  N     . ARG A 1 1437 ? 166.619 150.847 204.496 1.00 42.47  ? 2654 ARG A N     1 
ATOM   9695  C  CA    . ARG A 1 1437 ? 165.380 150.543 203.787 1.00 44.87  ? 2654 ARG A CA    1 
ATOM   9696  C  C     . ARG A 1 1437 ? 165.122 151.503 202.631 1.00 48.48  ? 2654 ARG A C     1 
ATOM   9697  O  O     . ARG A 1 1437 ? 164.525 151.105 201.625 1.00 50.67  ? 2654 ARG A O     1 
ATOM   9698  C  CB    . ARG A 1 1437 ? 164.203 150.550 204.759 1.00 50.13  ? 2654 ARG A CB    1 
ATOM   9699  C  CG    . ARG A 1 1437 ? 164.039 149.245 205.509 1.00 50.35  ? 2654 ARG A CG    1 
ATOM   9700  C  CD    . ARG A 1 1437 ? 163.149 148.281 204.747 1.00 49.27  ? 2654 ARG A CD    1 
ATOM   9701  N  NE    . ARG A 1 1437 ? 163.464 146.891 205.054 1.00 51.37  ? 2654 ARG A NE    1 
ATOM   9702  C  CZ    . ARG A 1 1437 ? 162.834 146.161 205.964 1.00 52.23  ? 2654 ARG A CZ    1 
ATOM   9703  N  NH1   . ARG A 1 1437 ? 161.829 146.651 206.669 1.00 53.90  ? 2654 ARG A NH1   1 
ATOM   9704  N  NH2   . ARG A 1 1437 ? 163.220 144.905 206.170 1.00 52.55  ? 2654 ARG A NH2   1 
ATOM   9705  N  N     . ILE A 1 1438 ? 165.551 152.757 202.747 1.00 48.87  ? 2655 ILE A N     1 
ATOM   9706  C  CA    . ILE A 1 1438 ? 165.343 153.722 201.665 1.00 46.24  ? 2655 ILE A CA    1 
ATOM   9707  C  C     . ILE A 1 1438 ? 166.472 153.682 200.645 1.00 49.13  ? 2655 ILE A C     1 
ATOM   9708  O  O     . ILE A 1 1438 ? 166.231 153.514 199.447 1.00 50.48  ? 2655 ILE A O     1 
ATOM   9709  C  CB    . ILE A 1 1438 ? 165.149 155.145 202.232 1.00 39.19  ? 2655 ILE A CB    1 
ATOM   9710  C  CG1   . ILE A 1 1438 ? 164.134 155.134 203.374 1.00 41.64  ? 2655 ILE A CG1   1 
ATOM   9711  C  CG2   . ILE A 1 1438 ? 164.754 156.104 201.138 1.00 37.79  ? 2655 ILE A CG2   1 
ATOM   9712  C  CD1   . ILE A 1 1438 ? 162.744 154.756 202.941 1.00 44.43  ? 2655 ILE A CD1   1 
ATOM   9713  N  N     . PHE A 1 1439 ? 167.719 153.846 201.086 1.00 48.95  ? 2656 PHE A N     1 
ATOM   9714  C  CA    . PHE A 1 1439 ? 168.832 153.906 200.146 1.00 44.72  ? 2656 PHE A CA    1 
ATOM   9715  C  C     . PHE A 1 1439 ? 169.189 152.524 199.609 1.00 51.01  ? 2656 PHE A C     1 
ATOM   9716  O  O     . PHE A 1 1439 ? 169.156 152.293 198.396 1.00 53.83  ? 2656 PHE A O     1 
ATOM   9717  C  CB    . PHE A 1 1439 ? 170.045 154.556 200.813 1.00 45.84  ? 2656 PHE A CB    1 
ATOM   9718  C  CG    . PHE A 1 1439 ? 169.974 156.053 200.873 1.00 38.69  ? 2656 PHE A CG    1 
ATOM   9719  C  CD1   . PHE A 1 1439 ? 170.313 156.817 199.772 1.00 44.03  ? 2656 PHE A CD1   1 
ATOM   9720  C  CD2   . PHE A 1 1439 ? 169.565 156.696 202.026 1.00 34.13  ? 2656 PHE A CD2   1 
ATOM   9721  C  CE1   . PHE A 1 1439 ? 170.252 158.194 199.822 1.00 45.82  ? 2656 PHE A CE1   1 
ATOM   9722  C  CE2   . PHE A 1 1439 ? 169.504 158.074 202.082 1.00 30.38  ? 2656 PHE A CE2   1 
ATOM   9723  C  CZ    . PHE A 1 1439 ? 169.846 158.822 200.979 1.00 38.84  ? 2656 PHE A CZ    1 
ATOM   9724  N  N     . ALA A 1 1440 ? 169.528 151.591 200.498 1.00 54.78  ? 2657 ALA A N     1 
ATOM   9725  C  CA    . ALA A 1 1440 ? 170.020 150.275 200.085 1.00 54.98  ? 2657 ALA A CA    1 
ATOM   9726  C  C     . ALA A 1 1440 ? 168.876 149.269 199.954 1.00 54.43  ? 2657 ALA A C     1 
ATOM   9727  O  O     . ALA A 1 1440 ? 168.908 148.162 200.488 1.00 56.50  ? 2657 ALA A O     1 
ATOM   9728  C  CB    . ALA A 1 1440 ? 171.074 149.774 201.060 1.00 54.62  ? 2657 ALA A CB    1 
ATOM   9729  N  N     . ASP A 1 1441 ? 167.849 149.680 199.221 1.00 56.43  ? 2658 ASP A N     1 
ATOM   9730  C  CA    . ASP A 1 1441 ? 166.828 148.765 198.738 1.00 60.07  ? 2658 ASP A CA    1 
ATOM   9731  C  C     . ASP A 1 1441 ? 167.106 148.345 197.304 1.00 65.20  ? 2658 ASP A C     1 
ATOM   9732  O  O     . ASP A 1 1441 ? 166.311 147.609 196.711 1.00 62.54  ? 2658 ASP A O     1 
ATOM   9733  C  CB    . ASP A 1 1441 ? 165.445 149.408 198.847 1.00 61.58  ? 2658 ASP A CB    1 
ATOM   9734  C  CG    . ASP A 1 1441 ? 164.373 148.419 199.242 1.00 63.59  ? 2658 ASP A CG    1 
ATOM   9735  O  OD1   . ASP A 1 1441 ? 164.561 147.208 199.006 1.00 61.63  ? 2658 ASP A OD1   1 
ATOM   9736  O  OD2   . ASP A 1 1441 ? 163.340 148.855 199.793 1.00 61.95  ? 2658 ASP A OD2   1 
ATOM   9737  N  N     . ARG A 1 1442 ? 168.220 148.810 196.734 1.00 67.04  ? 2659 ARG A N     1 
ATOM   9738  C  CA    . ARG A 1 1442 ? 168.512 148.602 195.325 1.00 68.46  ? 2659 ARG A CA    1 
ATOM   9739  C  C     . ARG A 1 1442 ? 169.967 148.266 195.029 1.00 67.23  ? 2659 ARG A C     1 
ATOM   9740  O  O     . ARG A 1 1442 ? 170.317 148.150 193.851 1.00 69.76  ? 2659 ARG A O     1 
ATOM   9741  C  CB    . ARG A 1 1442 ? 168.127 149.854 194.519 1.00 69.16  ? 2659 ARG A CB    1 
ATOM   9742  C  CG    . ARG A 1 1442 ? 166.640 150.152 194.443 1.00 65.96  ? 2659 ARG A CG    1 
ATOM   9743  C  CD    . ARG A 1 1442 ? 166.401 151.467 193.722 1.00 64.46  ? 2659 ARG A CD    1 
ATOM   9744  N  NE    . ARG A 1 1442 ? 166.724 152.613 194.563 1.00 62.67  ? 2659 ARG A NE    1 
ATOM   9745  C  CZ    . ARG A 1 1442 ? 166.550 153.878 194.205 1.00 57.61  ? 2659 ARG A CZ    1 
ATOM   9746  N  NH1   . ARG A 1 1442 ? 166.070 154.199 193.016 1.00 54.34  ? 2659 ARG A NH1   1 
ATOM   9747  N  NH2   . ARG A 1 1442 ? 166.865 154.843 195.063 1.00 53.59  ? 2659 ARG A NH2   1 
ATOM   9748  N  N     . LEU A 1 1443 ? 170.826 148.121 196.036 1.00 65.97  ? 2660 LEU A N     1 
ATOM   9749  C  CA    . LEU A 1 1443 ? 172.237 147.882 195.767 1.00 73.24  ? 2660 LEU A CA    1 
ATOM   9750  C  C     . LEU A 1 1443 ? 172.453 146.470 195.232 1.00 80.20  ? 2660 LEU A C     1 
ATOM   9751  O  O     . LEU A 1 1443 ? 171.703 145.542 195.546 1.00 80.21  ? 2660 LEU A O     1 
ATOM   9752  C  CB    . LEU A 1 1443 ? 173.075 148.117 197.024 1.00 74.60  ? 2660 LEU A CB    1 
ATOM   9753  C  CG    . LEU A 1 1443 ? 173.043 149.558 197.540 1.00 69.45  ? 2660 LEU A CG    1 
ATOM   9754  C  CD1   . LEU A 1 1443 ? 173.977 149.745 198.726 1.00 69.45  ? 2660 LEU A CD1   1 
ATOM   9755  C  CD2   . LEU A 1 1443 ? 173.370 150.538 196.426 1.00 69.33  ? 2660 LEU A CD2   1 
ATOM   9756  N  N     . VAL A 1 1444 ? 173.510 146.315 194.429 1.00 81.11  ? 2661 VAL A N     1 
ATOM   9757  C  CA    . VAL A 1 1444 ? 173.621 145.160 193.538 1.00 79.43  ? 2661 VAL A CA    1 
ATOM   9758  C  C     . VAL A 1 1444 ? 173.879 143.882 194.328 1.00 77.18  ? 2661 VAL A C     1 
ATOM   9759  O  O     . VAL A 1 1444 ? 173.063 142.954 194.323 1.00 72.54  ? 2661 VAL A O     1 
ATOM   9760  C  CB    . VAL A 1 1444 ? 174.714 145.395 192.482 1.00 78.29  ? 2661 VAL A CB    1 
ATOM   9761  C  CG1   . VAL A 1 1444 ? 174.923 144.140 191.651 1.00 79.25  ? 2661 VAL A CG1   1 
ATOM   9762  C  CG2   . VAL A 1 1444 ? 174.342 146.561 191.586 1.00 77.06  ? 2661 VAL A CG2   1 
ATOM   9763  N  N     . GLY A 1 1445 ? 175.016 143.813 195.018 1.00 76.45  ? 2662 GLY A N     1 
ATOM   9764  C  CA    . GLY A 1 1445 ? 175.456 142.593 195.653 1.00 78.91  ? 2662 GLY A CA    1 
ATOM   9765  C  C     . GLY A 1 1445 ? 175.635 142.736 197.154 1.00 83.28  ? 2662 GLY A C     1 
ATOM   9766  O  O     . GLY A 1 1445 ? 175.393 143.792 197.745 1.00 81.96  ? 2662 GLY A O     1 
ATOM   9767  N  N     . VAL A 1 1446 ? 176.060 141.627 197.762 1.00 87.01  ? 2663 VAL A N     1 
ATOM   9768  C  CA    . VAL A 1 1446 ? 176.392 141.634 199.181 1.00 85.37  ? 2663 VAL A CA    1 
ATOM   9769  C  C     . VAL A 1 1446 ? 177.629 142.489 199.430 1.00 86.81  ? 2663 VAL A C     1 
ATOM   9770  O  O     . VAL A 1 1446 ? 177.758 143.112 200.490 1.00 85.74  ? 2663 VAL A O     1 
ATOM   9771  C  CB    . VAL A 1 1446 ? 176.576 140.190 199.685 1.00 81.51  ? 2663 VAL A CB    1 
ATOM   9772  C  CG1   . VAL A 1 1446 ? 176.800 140.158 201.192 1.00 79.41  ? 2663 VAL A CG1   1 
ATOM   9773  C  CG2   . VAL A 1 1446 ? 175.373 139.341 199.302 1.00 82.51  ? 2663 VAL A CG2   1 
ATOM   9774  N  N     . LYS A 1 1447 ? 178.551 142.538 198.463 1.00 88.66  ? 2664 LYS A N     1 
ATOM   9775  C  CA    . LYS A 1 1447 ? 179.730 143.391 198.595 1.00 89.46  ? 2664 LYS A CA    1 
ATOM   9776  C  C     . LYS A 1 1447 ? 179.346 144.866 198.645 1.00 87.36  ? 2664 LYS A C     1 
ATOM   9777  O  O     . LYS A 1 1447 ? 179.879 145.626 199.463 1.00 86.86  ? 2664 LYS A O     1 
ATOM   9778  C  CB    . LYS A 1 1447 ? 180.699 143.120 197.442 1.00 91.12  ? 2664 LYS A CB    1 
ATOM   9779  C  CG    . LYS A 1 1447 ? 182.070 143.780 197.578 1.00 89.29  ? 2664 LYS A CG    1 
ATOM   9780  C  CD    . LYS A 1 1447 ? 182.166 145.078 196.783 1.00 89.19  ? 2664 LYS A CD    1 
ATOM   9781  C  CE    . LYS A 1 1447 ? 183.553 145.691 196.883 1.00 92.18  ? 2664 LYS A CE    1 
ATOM   9782  N  NZ    . LYS A 1 1447 ? 183.644 146.982 196.146 1.00 97.89  ? 2664 LYS A NZ    1 
ATOM   9783  N  N     . GLU A 1 1448 ? 178.426 145.292 197.777 1.00 86.53  ? 2665 GLU A N     1 
ATOM   9784  C  CA    . GLU A 1 1448 ? 178.007 146.690 197.771 1.00 85.06  ? 2665 GLU A CA    1 
ATOM   9785  C  C     . GLU A 1 1448 ? 177.248 147.045 199.044 1.00 81.38  ? 2665 GLU A C     1 
ATOM   9786  O  O     . GLU A 1 1448 ? 177.418 148.141 199.593 1.00 81.86  ? 2665 GLU A O     1 
ATOM   9787  C  CB    . GLU A 1 1448 ? 177.157 146.978 196.533 1.00 86.03  ? 2665 GLU A CB    1 
ATOM   9788  C  CG    . GLU A 1 1448 ? 177.809 146.589 195.202 1.00 88.44  ? 2665 GLU A CG    1 
ATOM   9789  C  CD    . GLU A 1 1448 ? 178.816 147.611 194.683 1.00 89.97  ? 2665 GLU A CD    1 
ATOM   9790  O  OE1   . GLU A 1 1448 ? 179.419 148.352 195.488 1.00 89.59  ? 2665 GLU A OE1   1 
ATOM   9791  O  OE2   . GLU A 1 1448 ? 179.006 147.672 193.450 1.00 88.63  ? 2665 GLU A OE2   1 
ATOM   9792  N  N     . LYS A 1 1449 ? 176.411 146.130 199.533 1.00 79.61  ? 2666 LYS A N     1 
ATOM   9793  C  CA    . LYS A 1 1449 ? 175.706 146.380 200.784 1.00 76.79  ? 2666 LYS A CA    1 
ATOM   9794  C  C     . LYS A 1 1449 ? 176.660 146.401 201.972 1.00 80.22  ? 2666 LYS A C     1 
ATOM   9795  O  O     . LYS A 1 1449 ? 176.455 147.171 202.913 1.00 78.20  ? 2666 LYS A O     1 
ATOM   9796  C  CB    . LYS A 1 1449 ? 174.604 145.340 200.975 1.00 73.56  ? 2666 LYS A CB    1 
ATOM   9797  C  CG    . LYS A 1 1449 ? 173.470 145.499 199.976 1.00 68.69  ? 2666 LYS A CG    1 
ATOM   9798  C  CD    . LYS A 1 1449 ? 172.568 144.285 199.927 1.00 64.97  ? 2666 LYS A CD    1 
ATOM   9799  C  CE    . LYS A 1 1449 ? 171.570 144.411 198.788 1.00 66.84  ? 2666 LYS A CE    1 
ATOM   9800  N  NZ    . LYS A 1 1449 ? 170.243 143.834 199.135 1.00 68.59  ? 2666 LYS A NZ    1 
ATOM   9801  N  N     . ASN A 1 1450 ? 177.720 145.590 201.940 1.00 83.81  ? 2667 ASN A N     1 
ATOM   9802  C  CA    . ASN A 1 1450 ? 178.733 145.667 202.988 1.00 84.58  ? 2667 ASN A CA    1 
ATOM   9803  C  C     . ASN A 1 1450 ? 179.524 146.966 202.905 1.00 84.36  ? 2667 ASN A C     1 
ATOM   9804  O  O     . ASN A 1 1450 ? 179.938 147.509 203.937 1.00 83.40  ? 2667 ASN A O     1 
ATOM   9805  C  CB    . ASN A 1 1450 ? 179.670 144.462 202.904 1.00 84.89  ? 2667 ASN A CB    1 
ATOM   9806  C  CG    . ASN A 1 1450 ? 180.048 143.923 204.269 1.00 86.87  ? 2667 ASN A CG    1 
ATOM   9807  O  OD1   . ASN A 1 1450 ? 180.028 144.649 205.263 1.00 84.84  ? 2667 ASN A OD1   1 
ATOM   9808  N  ND2   . ASN A 1 1450 ? 180.394 142.643 204.324 1.00 89.83  ? 2667 ASN A ND2   1 
ATOM   9809  N  N     . SER A 1 1451 ? 179.748 147.474 201.690 1.00 83.76  ? 2668 SER A N     1 
ATOM   9810  C  CA    . SER A 1 1451 ? 180.353 148.794 201.540 1.00 82.66  ? 2668 SER A CA    1 
ATOM   9811  C  C     . SER A 1 1451 ? 179.452 149.875 202.124 1.00 79.40  ? 2668 SER A C     1 
ATOM   9812  O  O     . SER A 1 1451 ? 179.931 150.813 202.772 1.00 79.46  ? 2668 SER A O     1 
ATOM   9813  C  CB    . SER A 1 1451 ? 180.648 149.075 200.067 1.00 84.60  ? 2668 SER A CB    1 
ATOM   9814  O  OG    . SER A 1 1451 ? 180.910 150.451 199.854 1.00 85.56  ? 2668 SER A OG    1 
ATOM   9815  N  N     . PHE A 1 1452 ? 178.140 149.756 201.912 1.00 77.54  ? 2669 PHE A N     1 
ATOM   9816  C  CA    . PHE A 1 1452 ? 177.210 150.684 202.549 1.00 72.54  ? 2669 PHE A CA    1 
ATOM   9817  C  C     . PHE A 1 1452 ? 177.249 150.550 204.064 1.00 72.04  ? 2669 PHE A C     1 
ATOM   9818  O  O     . PHE A 1 1452 ? 177.132 151.545 204.785 1.00 70.53  ? 2669 PHE A O     1 
ATOM   9819  C  CB    . PHE A 1 1452 ? 175.786 150.457 202.055 1.00 70.93  ? 2669 PHE A CB    1 
ATOM   9820  C  CG    . PHE A 1 1452 ? 174.801 151.451 202.602 1.00 69.30  ? 2669 PHE A CG    1 
ATOM   9821  C  CD1   . PHE A 1 1452 ? 173.562 151.042 203.057 1.00 67.56  ? 2669 PHE A CD1   1 
ATOM   9822  C  CD2   . PHE A 1 1452 ? 175.110 152.801 202.642 1.00 68.11  ? 2669 PHE A CD2   1 
ATOM   9823  C  CE1   . PHE A 1 1452 ? 172.651 151.955 203.557 1.00 62.12  ? 2669 PHE A CE1   1 
ATOM   9824  C  CE2   . PHE A 1 1452 ? 174.204 153.719 203.139 1.00 63.81  ? 2669 PHE A CE2   1 
ATOM   9825  C  CZ    . PHE A 1 1452 ? 172.973 153.295 203.598 1.00 59.91  ? 2669 PHE A CZ    1 
ATOM   9826  N  N     . GLU A 1 1453 ? 177.384 149.320 204.562 1.00 74.92  ? 2670 GLU A N     1 
ATOM   9827  C  CA    . GLU A 1 1453 ? 177.425 149.102 206.003 1.00 76.81  ? 2670 GLU A CA    1 
ATOM   9828  C  C     . GLU A 1 1453 ? 178.666 149.732 206.623 1.00 75.39  ? 2670 GLU A C     1 
ATOM   9829  O  O     . GLU A 1 1453 ? 178.579 150.370 207.678 1.00 75.81  ? 2670 GLU A O     1 
ATOM   9830  C  CB    . GLU A 1 1453 ? 177.366 147.606 206.309 1.00 78.45  ? 2670 GLU A CB    1 
ATOM   9831  C  CG    . GLU A 1 1453 ? 177.495 147.264 207.783 1.00 80.63  ? 2670 GLU A CG    1 
ATOM   9832  C  CD    . GLU A 1 1453 ? 177.073 145.842 208.088 1.00 81.25  ? 2670 GLU A CD    1 
ATOM   9833  O  OE1   . GLU A 1 1453 ? 176.308 145.265 207.287 1.00 74.80  ? 2670 GLU A OE1   1 
ATOM   9834  O  OE2   . GLU A 1 1453 ? 177.508 145.300 209.125 1.00 85.31  ? 2670 GLU A OE2   1 
ATOM   9835  N  N     . GLN A 1 1454 ? 179.827 149.580 205.980 1.00 76.95  ? 2671 GLN A N     1 
ATOM   9836  C  CA    . GLN A 1 1454 ? 181.025 150.225 206.511 1.00 79.15  ? 2671 GLN A CA    1 
ATOM   9837  C  C     . GLN A 1 1454 ? 180.958 151.740 206.353 1.00 78.10  ? 2671 GLN A C     1 
ATOM   9838  O  O     . GLN A 1 1454 ? 181.475 152.468 207.207 1.00 77.85  ? 2671 GLN A O     1 
ATOM   9839  C  CB    . GLN A 1 1454 ? 182.294 149.656 205.862 1.00 81.19  ? 2671 GLN A CB    1 
ATOM   9840  C  CG    . GLN A 1 1454 ? 182.468 149.905 204.373 1.00 81.81  ? 2671 GLN A CG    1 
ATOM   9841  C  CD    . GLN A 1 1454 ? 183.190 151.205 204.066 1.00 81.00  ? 2671 GLN A CD    1 
ATOM   9842  O  OE1   . GLN A 1 1454 ? 183.733 151.854 204.961 1.00 81.52  ? 2671 GLN A OE1   1 
ATOM   9843  N  NE2   . GLN A 1 1454 ? 183.193 151.595 202.797 1.00 80.06  ? 2671 GLN A NE2   1 
ATOM   9844  N  N     . LEU A 1 1455 ? 180.312 152.233 205.290 1.00 80.91  ? 2672 LEU A N     1 
ATOM   9845  C  CA    . LEU A 1 1455 ? 180.096 153.672 205.160 1.00 78.73  ? 2672 LEU A CA    1 
ATOM   9846  C  C     . LEU A 1 1455 ? 179.219 154.202 206.286 1.00 73.57  ? 2672 LEU A C     1 
ATOM   9847  O  O     . LEU A 1 1455 ? 179.505 155.257 206.860 1.00 74.33  ? 2672 LEU A O     1 
ATOM   9848  C  CB    . LEU A 1 1455 ? 179.469 153.990 203.802 1.00 78.01  ? 2672 LEU A CB    1 
ATOM   9849  C  CG    . LEU A 1 1455 ? 178.875 155.394 203.662 1.00 70.57  ? 2672 LEU A CG    1 
ATOM   9850  C  CD1   . LEU A 1 1455 ? 179.978 156.436 203.612 1.00 71.76  ? 2672 LEU A CD1   1 
ATOM   9851  C  CD2   . LEU A 1 1455 ? 177.973 155.496 202.443 1.00 66.19  ? 2672 LEU A CD2   1 
ATOM   9852  N  N     . LEU A 1 1456 ? 178.152 153.476 206.622 1.00 70.43  ? 2673 LEU A N     1 
ATOM   9853  C  CA    . LEU A 1 1456 ? 177.261 153.908 207.693 1.00 70.62  ? 2673 LEU A CA    1 
ATOM   9854  C  C     . LEU A 1 1456 ? 177.960 153.823 209.045 1.00 78.39  ? 2673 LEU A C     1 
ATOM   9855  O  O     . LEU A 1 1456 ? 177.760 154.684 209.910 1.00 79.49  ? 2673 LEU A O     1 
ATOM   9856  C  CB    . LEU A 1 1456 ? 175.984 153.064 207.673 1.00 65.05  ? 2673 LEU A CB    1 
ATOM   9857  C  CG    . LEU A 1 1456 ? 174.718 153.542 208.397 1.00 62.11  ? 2673 LEU A CG    1 
ATOM   9858  C  CD1   . LEU A 1 1456 ? 173.491 152.923 207.746 1.00 54.81  ? 2673 LEU A CD1   1 
ATOM   9859  C  CD2   . LEU A 1 1456 ? 174.726 153.233 209.881 1.00 68.62  ? 2673 LEU A CD2   1 
ATOM   9860  N  N     . TYR A 1 1457 ? 178.787 152.791 209.242 1.00 79.81  ? 2674 TYR A N     1 
ATOM   9861  C  CA    . TYR A 1 1457 ? 179.573 152.683 210.468 1.00 81.37  ? 2674 TYR A CA    1 
ATOM   9862  C  C     . TYR A 1 1457 ? 180.547 153.846 210.604 1.00 83.84  ? 2674 TYR A C     1 
ATOM   9863  O  O     . TYR A 1 1457 ? 180.677 154.432 211.685 1.00 86.66  ? 2674 TYR A O     1 
ATOM   9864  C  CB    . TYR A 1 1457 ? 180.330 151.355 210.488 1.00 83.56  ? 2674 TYR A CB    1 
ATOM   9865  C  CG    . TYR A 1 1457 ? 179.624 150.234 211.216 1.00 83.35  ? 2674 TYR A CG    1 
ATOM   9866  C  CD1   . TYR A 1 1457 ? 179.424 150.287 212.589 1.00 85.30  ? 2674 TYR A CD1   1 
ATOM   9867  C  CD2   . TYR A 1 1457 ? 179.171 149.115 210.530 1.00 83.73  ? 2674 TYR A CD2   1 
ATOM   9868  C  CE1   . TYR A 1 1457 ? 178.784 149.260 213.256 1.00 92.42  ? 2674 TYR A CE1   1 
ATOM   9869  C  CE2   . TYR A 1 1457 ? 178.530 148.084 211.188 1.00 87.42  ? 2674 TYR A CE2   1 
ATOM   9870  C  CZ    . TYR A 1 1457 ? 178.340 148.161 212.550 1.00 91.56  ? 2674 TYR A CZ    1 
ATOM   9871  O  OH    . TYR A 1 1457 ? 177.701 147.135 213.208 1.00 90.13  ? 2674 TYR A OH    1 
ATOM   9872  N  N     . GLU A 1 1458 ? 181.238 154.195 209.515 1.00 82.02  ? 2675 GLU A N     1 
ATOM   9873  C  CA    . GLU A 1 1458 ? 182.158 155.328 209.545 1.00 83.56  ? 2675 GLU A CA    1 
ATOM   9874  C  C     . GLU A 1 1458 ? 181.410 156.634 209.775 1.00 86.74  ? 2675 GLU A C     1 
ATOM   9875  O  O     . GLU A 1 1458 ? 181.900 157.521 210.480 1.00 88.97  ? 2675 GLU A O     1 
ATOM   9876  C  CB    . GLU A 1 1458 ? 182.960 155.386 208.244 1.00 83.56  ? 2675 GLU A CB    1 
ATOM   9877  C  CG    . GLU A 1 1458 ? 184.161 156.325 208.278 1.00 84.14  ? 2675 GLU A CG    1 
ATOM   9878  C  CD    . GLU A 1 1458 ? 183.802 157.762 207.950 1.00 85.29  ? 2675 GLU A CD    1 
ATOM   9879  O  OE1   . GLU A 1 1458 ? 182.777 157.980 207.270 1.00 80.42  ? 2675 GLU A OE1   1 
ATOM   9880  O  OE2   . GLU A 1 1458 ? 184.542 158.672 208.376 1.00 88.55  ? 2675 GLU A OE2   1 
ATOM   9881  N  N     . THR A 1 1459 ? 180.226 156.771 209.176 1.00 86.78  ? 2676 THR A N     1 
ATOM   9882  C  CA    . THR A 1 1459 ? 179.410 157.963 209.373 1.00 85.57  ? 2676 THR A CA    1 
ATOM   9883  C  C     . THR A 1 1459 ? 178.986 158.108 210.829 1.00 87.94  ? 2676 THR A C     1 
ATOM   9884  O  O     . THR A 1 1459 ? 179.044 159.206 211.397 1.00 88.07  ? 2676 THR A O     1 
ATOM   9885  C  CB    . THR A 1 1459 ? 178.190 157.899 208.455 1.00 78.07  ? 2676 THR A CB    1 
ATOM   9886  O  OG1   . THR A 1 1459 ? 178.619 157.874 207.087 1.00 75.95  ? 2676 THR A OG1   1 
ATOM   9887  C  CG2   . THR A 1 1459 ? 177.298 159.088 208.669 1.00 72.36  ? 2676 THR A CG2   1 
ATOM   9888  N  N     . VAL A 1 1460 ? 178.569 157.003 211.451 1.00 86.47  ? 2677 VAL A N     1 
ATOM   9889  C  CA    . VAL A 1 1460 ? 178.214 157.025 212.867 1.00 89.14  ? 2677 VAL A CA    1 
ATOM   9890  C  C     . VAL A 1 1460 ? 179.432 157.369 213.717 1.00 89.23  ? 2677 VAL A C     1 
ATOM   9891  O  O     . VAL A 1 1460 ? 179.358 158.209 214.621 1.00 91.50  ? 2677 VAL A O     1 
ATOM   9892  C  CB    . VAL A 1 1460 ? 177.588 155.678 213.278 1.00 90.48  ? 2677 VAL A CB    1 
ATOM   9893  C  CG1   . VAL A 1 1460 ? 177.536 155.541 214.790 1.00 92.02  ? 2677 VAL A CG1   1 
ATOM   9894  C  CG2   . VAL A 1 1460 ? 176.194 155.542 212.689 1.00 85.09  ? 2677 VAL A CG2   1 
ATOM   9895  N  N     . ASP A 1 1461 ? 180.578 156.751 213.420 1.00 88.40  ? 2678 ASP A N     1 
ATOM   9896  C  CA    . ASP A 1 1461 ? 181.781 156.997 214.211 1.00 94.88  ? 2678 ASP A CA    1 
ATOM   9897  C  C     . ASP A 1 1461 ? 182.298 158.421 214.039 1.00 96.53  ? 2678 ASP A C     1 
ATOM   9898  O  O     . ASP A 1 1461 ? 182.955 158.952 214.942 1.00 99.29  ? 2678 ASP A O     1 
ATOM   9899  C  CB    . ASP A 1 1461 ? 182.868 155.990 213.836 1.00 98.63  ? 2678 ASP A CB    1 
ATOM   9900  C  CG    . ASP A 1 1461 ? 182.492 154.565 214.194 1.00 99.81  ? 2678 ASP A CG    1 
ATOM   9901  O  OD1   . ASP A 1 1461 ? 181.358 154.349 214.672 1.00 99.53  ? 2678 ASP A OD1   1 
ATOM   9902  O  OD2   . ASP A 1 1461 ? 183.328 153.659 213.995 1.00 99.43  ? 2678 ASP A OD2   1 
ATOM   9903  N  N     . LYS A 1 1462 ? 182.017 159.052 212.900 1.00 94.66  ? 2679 LYS A N     1 
ATOM   9904  C  CA    . LYS A 1 1462 ? 182.474 160.411 212.644 1.00 92.84  ? 2679 LYS A CA    1 
ATOM   9905  C  C     . LYS A 1 1462 ? 181.510 161.470 213.158 1.00 91.67  ? 2679 LYS A C     1 
ATOM   9906  O  O     . LYS A 1 1462 ? 181.948 162.570 213.516 1.00 93.11  ? 2679 LYS A O     1 
ATOM   9907  C  CB    . LYS A 1 1462 ? 182.697 160.615 211.142 1.00 88.61  ? 2679 LYS A CB    1 
ATOM   9908  C  CG    . LYS A 1 1462 ? 183.530 161.838 210.787 1.00 91.10  ? 2679 LYS A CG    1 
ATOM   9909  C  CD    . LYS A 1 1462 ? 184.030 161.772 209.352 1.00 92.35  ? 2679 LYS A CD    1 
ATOM   9910  C  CE    . LYS A 1 1462 ? 185.043 162.869 209.064 1.00 96.35  ? 2679 LYS A CE    1 
ATOM   9911  N  NZ    . LYS A 1 1462 ? 184.406 164.213 208.999 1.00 95.64  ? 2679 LYS A NZ    1 
ATOM   9912  N  N     . TYR A 1 1463 ? 180.213 161.172 213.215 1.00 89.57  ? 2680 TYR A N     1 
ATOM   9913  C  CA    . TYR A 1 1463 ? 179.229 162.184 213.572 1.00 88.67  ? 2680 TYR A CA    1 
ATOM   9914  C  C     . TYR A 1 1463 ? 178.409 161.862 214.811 1.00 89.89  ? 2680 TYR A C     1 
ATOM   9915  O  O     . TYR A 1 1463 ? 178.069 162.783 215.555 1.00 89.44  ? 2680 TYR A O     1 
ATOM   9916  C  CB    . TYR A 1 1463 ? 178.273 162.430 212.394 1.00 85.23  ? 2680 TYR A CB    1 
ATOM   9917  C  CG    . TYR A 1 1463 ? 178.923 163.147 211.232 1.00 83.84  ? 2680 TYR A CG    1 
ATOM   9918  C  CD1   . TYR A 1 1463 ? 179.572 164.362 211.417 1.00 83.96  ? 2680 TYR A CD1   1 
ATOM   9919  C  CD2   . TYR A 1 1463 ? 178.895 162.607 209.953 1.00 80.79  ? 2680 TYR A CD2   1 
ATOM   9920  C  CE1   . TYR A 1 1463 ? 180.172 165.019 210.360 1.00 83.02  ? 2680 TYR A CE1   1 
ATOM   9921  C  CE2   . TYR A 1 1463 ? 179.491 163.258 208.890 1.00 79.75  ? 2680 TYR A CE2   1 
ATOM   9922  C  CZ    . TYR A 1 1463 ? 180.127 164.463 209.099 1.00 82.24  ? 2680 TYR A CZ    1 
ATOM   9923  O  OH    . TYR A 1 1463 ? 180.722 165.114 208.044 1.00 81.15  ? 2680 TYR A OH    1 
ATOM   9924  N  N     . LEU A 1 1464 ? 178.092 160.591 215.070 1.00 91.95  ? 2681 LEU A N     1 
ATOM   9925  C  CA    . LEU A 1 1464 ? 177.189 160.203 216.154 1.00 94.78  ? 2681 LEU A CA    1 
ATOM   9926  C  C     . LEU A 1 1464 ? 177.902 159.213 217.069 1.00 101.78 ? 2681 LEU A C     1 
ATOM   9927  O  O     . LEU A 1 1464 ? 177.696 157.995 216.962 1.00 101.81 ? 2681 LEU A O     1 
ATOM   9928  C  CB    . LEU A 1 1464 ? 175.892 159.598 215.615 1.00 87.45  ? 2681 LEU A CB    1 
ATOM   9929  C  CG    . LEU A 1 1464 ? 174.738 160.509 215.179 1.00 80.07  ? 2681 LEU A CG    1 
ATOM   9930  C  CD1   . LEU A 1 1464 ? 174.224 161.324 216.361 1.00 80.12  ? 2681 LEU A CD1   1 
ATOM   9931  C  CD2   . LEU A 1 1464 ? 175.081 161.401 213.995 1.00 77.24  ? 2681 LEU A CD2   1 
ATOM   9932  N  N     . PRO A 1 1465 ? 178.744 159.700 217.994 1.00 107.56 ? 2682 PRO A N     1 
ATOM   9933  C  CA    . PRO A 1 1465 ? 179.503 158.817 218.887 1.00 108.94 ? 2682 PRO A CA    1 
ATOM   9934  C  C     . PRO A 1 1465 ? 178.618 158.113 219.913 1.00 109.07 ? 2682 PRO A C     1 
ATOM   9935  O  O     . PRO A 1 1465 ? 178.248 156.960 219.689 1.00 107.79 ? 2682 PRO A O     1 
ATOM   9936  C  CB    . PRO A 1 1465 ? 180.487 159.771 219.584 1.00 108.22 ? 2682 PRO A CB    1 
ATOM   9937  C  CG    . PRO A 1 1465 ? 180.357 161.094 218.880 1.00 104.67 ? 2682 PRO A CG    1 
ATOM   9938  C  CD    . PRO A 1 1465 ? 178.997 161.120 218.279 1.00 105.09 ? 2682 PRO A CD    1 
ATOM   9939  N  N     . LEU A 1 1469 ? 178.464 150.272 219.267 1.00 99.45  ? 2686 LEU A N     1 
ATOM   9940  C  CA    . LEU A 1 1469 ? 177.392 150.158 218.285 1.00 104.30 ? 2686 LEU A CA    1 
ATOM   9941  C  C     . LEU A 1 1469 ? 177.163 148.701 217.895 1.00 102.74 ? 2686 LEU A C     1 
ATOM   9942  O  O     . LEU A 1 1469 ? 178.105 147.983 217.559 1.00 104.12 ? 2686 LEU A O     1 
ATOM   9943  C  CB    . LEU A 1 1469 ? 177.706 150.992 217.039 1.00 105.85 ? 2686 LEU A CB    1 
ATOM   9944  C  CG    . LEU A 1 1469 ? 177.228 152.449 216.997 1.00 106.02 ? 2686 LEU A CG    1 
ATOM   9945  C  CD1   . LEU A 1 1469 ? 175.710 152.517 217.104 1.00 101.07 ? 2686 LEU A CD1   1 
ATOM   9946  C  CD2   . LEU A 1 1469 ? 177.890 153.307 218.069 1.00 107.48 ? 2686 LEU A CD2   1 
ATOM   9947  N  N     . GLY A 1 1470 ? 175.903 148.271 217.937 1.00 97.52  ? 2687 GLY A N     1 
ATOM   9948  C  CA    . GLY A 1 1470 ? 175.553 146.908 217.607 1.00 93.30  ? 2687 GLY A CA    1 
ATOM   9949  C  C     . GLY A 1 1470 ? 175.514 146.667 216.112 1.00 86.49  ? 2687 GLY A C     1 
ATOM   9950  O  O     . GLY A 1 1470 ? 175.763 147.554 215.296 1.00 84.10  ? 2687 GLY A O     1 
ATOM   9951  N  N     . ASN A 1 1471 ? 175.200 145.425 215.753 1.00 87.87  ? 2688 ASN A N     1 
ATOM   9952  C  CA    . ASN A 1 1471 ? 175.115 145.057 214.347 1.00 84.99  ? 2688 ASN A CA    1 
ATOM   9953  C  C     . ASN A 1 1471 ? 173.903 145.726 213.712 1.00 84.44  ? 2688 ASN A C     1 
ATOM   9954  O  O     . ASN A 1 1471 ? 172.793 145.667 214.250 1.00 82.74  ? 2688 ASN A O     1 
ATOM   9955  C  CB    . ASN A 1 1471 ? 175.031 143.541 214.192 1.00 85.67  ? 2688 ASN A CB    1 
ATOM   9956  C  CG    . ASN A 1 1471 ? 175.395 143.079 212.794 1.00 84.09  ? 2688 ASN A CG    1 
ATOM   9957  O  OD1   . ASN A 1 1471 ? 174.562 143.082 211.888 1.00 81.39  ? 2688 ASN A OD1   1 
ATOM   9958  N  ND2   . ASN A 1 1471 ? 176.648 142.678 212.612 1.00 84.74  ? 2688 ASN A ND2   1 
ATOM   9959  N  N     . ILE A 1 1472 ? 174.121 146.361 212.563 1.00 84.93  ? 2689 ILE A N     1 
ATOM   9960  C  CA    . ILE A 1 1472 ? 173.117 147.220 211.946 1.00 79.88  ? 2689 ILE A CA    1 
ATOM   9961  C  C     . ILE A 1 1472 ? 172.862 146.794 210.507 1.00 76.04  ? 2689 ILE A C     1 
ATOM   9962  O  O     . ILE A 1 1472 ? 172.517 147.621 209.656 1.00 71.48  ? 2689 ILE A O     1 
ATOM   9963  C  CB    . ILE A 1 1472 ? 173.550 148.694 212.024 1.00 77.70  ? 2689 ILE A CB    1 
ATOM   9964  C  CG1   . ILE A 1 1472 ? 175.024 148.821 211.639 1.00 79.82  ? 2689 ILE A CG1   1 
ATOM   9965  C  CG2   . ILE A 1 1472 ? 173.298 149.253 213.416 1.00 78.72  ? 2689 ILE A CG2   1 
ATOM   9966  C  CD1   . ILE A 1 1472 ? 175.560 150.222 211.720 1.00 77.83  ? 2689 ILE A CD1   1 
ATOM   9967  N  N     . SER A 1 1473 ? 173.026 145.504 210.227 1.00 76.76  ? 2690 SER A N     1 
ATOM   9968  C  CA    . SER A 1 1473 ? 172.757 144.980 208.897 1.00 72.82  ? 2690 SER A CA    1 
ATOM   9969  C  C     . SER A 1 1473 ? 171.250 144.902 208.656 1.00 71.58  ? 2690 SER A C     1 
ATOM   9970  O  O     . SER A 1 1473 ? 170.430 145.208 209.526 1.00 73.23  ? 2690 SER A O     1 
ATOM   9971  C  CB    . SER A 1 1473 ? 173.413 143.613 208.723 1.00 73.56  ? 2690 SER A CB    1 
ATOM   9972  O  OG    . SER A 1 1473 ? 173.201 142.797 209.861 1.00 74.03  ? 2690 SER A OG    1 
ATOM   9973  N  N     . SER A 1 1474 ? 170.880 144.482 207.444 1.00 71.97  ? 2691 SER A N     1 
ATOM   9974  C  CA    . SER A 1 1474 ? 169.467 144.394 207.093 1.00 74.14  ? 2691 SER A CA    1 
ATOM   9975  C  C     . SER A 1 1474 ? 168.770 143.252 207.822 1.00 74.46  ? 2691 SER A C     1 
ATOM   9976  O  O     . SER A 1 1474 ? 167.567 143.337 208.094 1.00 71.57  ? 2691 SER A O     1 
ATOM   9977  C  CB    . SER A 1 1474 ? 169.312 144.230 205.581 1.00 71.52  ? 2691 SER A CB    1 
ATOM   9978  O  OG    . SER A 1 1474 ? 170.036 143.106 205.112 1.00 70.32  ? 2691 SER A OG    1 
ATOM   9979  N  N     . THR A 1 1475 ? 169.498 142.184 208.145 1.00 75.28  ? 2692 THR A N     1 
ATOM   9980  C  CA    . THR A 1 1475 ? 168.920 141.034 208.826 1.00 71.94  ? 2692 THR A CA    1 
ATOM   9981  C  C     . THR A 1 1475 ? 169.092 141.080 210.338 1.00 72.38  ? 2692 THR A C     1 
ATOM   9982  O  O     . THR A 1 1475 ? 168.531 140.227 211.034 1.00 71.83  ? 2692 THR A O     1 
ATOM   9983  C  CB    . THR A 1 1475 ? 169.534 139.738 208.289 1.00 75.99  ? 2692 THR A CB    1 
ATOM   9984  O  OG1   . THR A 1 1475 ? 170.952 139.897 208.159 1.00 77.98  ? 2692 THR A OG1   1 
ATOM   9985  C  CG2   . THR A 1 1475 ? 168.940 139.391 206.933 1.00 79.43  ? 2692 THR A CG2   1 
ATOM   9986  N  N     . SER A 1 1476 ? 169.850 142.042 210.862 1.00 73.16  ? 2693 SER A N     1 
ATOM   9987  C  CA    . SER A 1 1476 ? 169.989 142.192 212.305 1.00 70.20  ? 2693 SER A CA    1 
ATOM   9988  C  C     . SER A 1 1476 ? 168.991 143.181 212.887 1.00 70.99  ? 2693 SER A C     1 
ATOM   9989  O  O     . SER A 1 1476 ? 168.509 142.976 214.007 1.00 75.76  ? 2693 SER A O     1 
ATOM   9990  C  CB    . SER A 1 1476 ? 171.411 142.635 212.658 1.00 72.99  ? 2693 SER A CB    1 
ATOM   9991  O  OG    . SER A 1 1476 ? 171.582 144.024 212.440 1.00 73.52  ? 2693 SER A OG    1 
ATOM   9992  N  N     . LEU A 1 1477 ? 168.669 144.247 212.152 1.00 69.81  ? 2694 LEU A N     1 
ATOM   9993  C  CA    . LEU A 1 1477 ? 167.667 145.219 212.586 1.00 63.41  ? 2694 LEU A CA    1 
ATOM   9994  C  C     . LEU A 1 1477 ? 166.299 144.731 212.122 1.00 58.82  ? 2694 LEU A C     1 
ATOM   9995  O  O     . LEU A 1 1477 ? 165.740 145.188 211.123 1.00 57.34  ? 2694 LEU A O     1 
ATOM   9996  C  CB    . LEU A 1 1477 ? 167.983 146.604 212.039 1.00 63.78  ? 2694 LEU A CB    1 
ATOM   9997  C  CG    . LEU A 1 1477 ? 169.304 147.238 212.469 1.00 67.65  ? 2694 LEU A CG    1 
ATOM   9998  C  CD1   . LEU A 1 1477 ? 169.669 148.372 211.529 1.00 66.61  ? 2694 LEU A CD1   1 
ATOM   9999  C  CD2   . LEU A 1 1477 ? 169.215 147.728 213.899 1.00 66.14  ? 2694 LEU A CD2   1 
ATOM   10000 N  N     . LEU A 1 1478 ? 165.754 143.776 212.869 1.00 61.02  ? 2695 LEU A N     1 
ATOM   10001 C  CA    . LEU A 1 1478 ? 164.443 143.211 212.563 1.00 68.24  ? 2695 LEU A CA    1 
ATOM   10002 C  C     . LEU A 1 1478 ? 163.389 144.096 213.215 1.00 69.46  ? 2695 LEU A C     1 
ATOM   10003 O  O     . LEU A 1 1478 ? 163.160 144.024 214.424 1.00 72.09  ? 2695 LEU A O     1 
ATOM   10004 C  CB    . LEU A 1 1478 ? 164.351 141.766 213.042 1.00 70.15  ? 2695 LEU A CB    1 
ATOM   10005 C  CG    . LEU A 1 1478 ? 163.121 140.980 212.587 1.00 75.41  ? 2695 LEU A CG    1 
ATOM   10006 C  CD1   . LEU A 1 1478 ? 163.518 139.583 212.147 1.00 83.92  ? 2695 LEU A CD1   1 
ATOM   10007 C  CD2   . LEU A 1 1478 ? 162.091 140.909 213.700 1.00 75.39  ? 2695 LEU A CD2   1 
ATOM   10008 N  N     . PHE A 1 1479 ? 162.742 144.930 212.407 1.00 61.23  ? 2696 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 1479 ? 161.741 145.875 212.877 1.00 54.59  ? 2696 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 1479 ? 160.370 145.488 212.345 1.00 53.24  ? 2696 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 1479 ? 160.229 145.126 211.173 1.00 54.65  ? 2696 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 1479 ? 162.079 147.298 212.431 1.00 58.76  ? 2696 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 1479 ? 163.037 148.012 213.338 1.00 60.09  ? 2696 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 1479 ? 162.580 148.661 214.472 1.00 60.17  ? 2696 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 1479 ? 164.390 148.051 213.049 1.00 58.07  ? 2696 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 1479 ? 163.455 149.326 215.306 1.00 58.54  ? 2696 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 1479 ? 165.271 148.715 213.879 1.00 55.61  ? 2696 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 1479 ? 164.802 149.352 215.009 1.00 56.62  ? 2696 PHE A CZ    1 
ATOM   10019 N  N     . SER A 1 1480 ? 159.361 145.575 213.207 1.00 55.58  ? 2697 SER A N     1 
ATOM   10020 C  CA    . SER A 1 1480 ? 157.991 145.278 212.812 1.00 59.98  ? 2697 SER A CA    1 
ATOM   10021 C  C     . SER A 1 1480 ? 157.039 145.936 213.798 1.00 61.50  ? 2697 SER A C     1 
ATOM   10022 O  O     . SER A 1 1480 ? 157.444 146.434 214.850 1.00 63.41  ? 2697 SER A O     1 
ATOM   10023 C  CB    . SER A 1 1480 ? 157.736 143.771 212.748 1.00 70.13  ? 2697 SER A CB    1 
ATOM   10024 O  OG    . SER A 1 1480 ? 156.349 143.498 212.640 1.00 68.70  ? 2697 SER A OG    1 
ATOM   10025 N  N     . GLY A 1 1481 ? 155.760 145.932 213.436 1.00 65.35  ? 2698 GLY A N     1 
ATOM   10026 C  CA    . GLY A 1 1481 ? 154.716 146.416 214.314 1.00 73.37  ? 2698 GLY A CA    1 
ATOM   10027 C  C     . GLY A 1 1481 ? 153.528 145.478 214.353 1.00 79.27  ? 2698 GLY A C     1 
ATOM   10028 O  O     . GLY A 1 1481 ? 152.471 145.818 214.894 1.00 80.26  ? 2698 GLY A O     1 
ATOM   10029 N  N     . LEU A 1 1482 ? 153.691 144.289 213.771 1.00 80.01  ? 2699 LEU A N     1 
ATOM   10030 C  CA    . LEU A 1 1482 ? 152.607 143.314 213.737 1.00 76.53  ? 2699 LEU A CA    1 
ATOM   10031 C  C     . LEU A 1 1482 ? 152.422 142.626 215.084 1.00 79.12  ? 2699 LEU A C     1 
ATOM   10032 O  O     . LEU A 1 1482 ? 151.290 142.333 215.483 1.00 82.76  ? 2699 LEU A O     1 
ATOM   10033 C  CB    . LEU A 1 1482 ? 152.868 142.275 212.647 1.00 78.47  ? 2699 LEU A CB    1 
ATOM   10034 C  CG    . LEU A 1 1482 ? 152.707 142.746 211.202 1.00 77.58  ? 2699 LEU A CG    1 
ATOM   10035 C  CD1   . LEU A 1 1482 ? 153.105 141.646 210.232 1.00 80.70  ? 2699 LEU A CD1   1 
ATOM   10036 C  CD2   . LEU A 1 1482 ? 151.278 143.198 210.950 1.00 74.01  ? 2699 LEU A CD2   1 
ATOM   10037 N  N     . LEU A 1 1483 ? 153.516 142.363 215.793 1.00 80.67  ? 2700 LEU A N     1 
ATOM   10038 C  CA    . LEU A 1 1483 ? 153.468 141.631 217.051 1.00 83.26  ? 2700 LEU A CA    1 
ATOM   10039 C  C     . LEU A 1 1483 ? 153.267 142.534 218.259 1.00 84.69  ? 2700 LEU A C     1 
ATOM   10040 O  O     . LEU A 1 1483 ? 153.272 142.038 219.390 1.00 85.40  ? 2700 LEU A O     1 
ATOM   10041 C  CB    . LEU A 1 1483 ? 154.750 140.812 217.231 1.00 85.15  ? 2700 LEU A CB    1 
ATOM   10042 N  N     . SER A 1 1484 ? 153.089 143.835 218.055 1.00 85.41  ? 2701 SER A N     1 
ATOM   10043 C  CA    . SER A 1 1484 ? 152.904 144.769 219.157 1.00 82.88  ? 2701 SER A CA    1 
ATOM   10044 C  C     . SER A 1 1484 ? 152.053 145.935 218.668 1.00 78.53  ? 2701 SER A C     1 
ATOM   10045 O  O     . SER A 1 1484 ? 151.452 145.879 217.591 1.00 80.25  ? 2701 SER A O     1 
ATOM   10046 C  CB    . SER A 1 1484 ? 154.259 145.230 219.706 1.00 81.25  ? 2701 SER A CB    1 
ATOM   10047 O  OG    . SER A 1 1484 ? 154.991 145.942 218.724 1.00 80.36  ? 2701 SER A OG    1 
ATOM   10048 N  N     . LEU A 1 1485 ? 151.994 146.994 219.472 1.00 75.64  ? 2702 LEU A N     1 
ATOM   10049 C  CA    . LEU A 1 1485 ? 151.225 148.185 219.144 1.00 77.94  ? 2702 LEU A CA    1 
ATOM   10050 C  C     . LEU A 1 1485 ? 152.098 149.341 218.672 1.00 79.80  ? 2702 LEU A C     1 
ATOM   10051 O  O     . LEU A 1 1485 ? 151.587 150.448 218.477 1.00 76.64  ? 2702 LEU A O     1 
ATOM   10052 C  CB    . LEU A 1 1485 ? 150.393 148.622 220.351 1.00 74.11  ? 2702 LEU A CB    1 
ATOM   10053 N  N     . ASP A 1 1486 ? 153.397 149.114 218.483 1.00 77.33  ? 2703 ASP A N     1 
ATOM   10054 C  CA    . ASP A 1 1486 ? 154.289 150.177 218.044 1.00 69.21  ? 2703 ASP A CA    1 
ATOM   10055 C  C     . ASP A 1 1486 ? 155.446 149.584 217.253 1.00 65.55  ? 2703 ASP A C     1 
ATOM   10056 O  O     . ASP A 1 1486 ? 155.754 148.394 217.353 1.00 66.48  ? 2703 ASP A O     1 
ATOM   10057 C  CB    . ASP A 1 1486 ? 154.819 150.997 219.226 1.00 69.51  ? 2703 ASP A CB    1 
ATOM   10058 C  CG    . ASP A 1 1486 ? 155.250 150.132 220.394 1.00 74.32  ? 2703 ASP A CG    1 
ATOM   10059 O  OD1   . ASP A 1 1486 ? 155.271 148.892 220.247 1.00 73.39  ? 2703 ASP A OD1   1 
ATOM   10060 O  OD2   . ASP A 1 1486 ? 155.573 150.696 221.461 1.00 77.19  ? 2703 ASP A OD2   1 
ATOM   10061 N  N     . PHE A 1 1487 ? 156.085 150.444 216.465 1.00 65.54  ? 2704 PHE A N     1 
ATOM   10062 C  CA    . PHE A 1 1487 ? 157.227 150.060 215.641 1.00 59.43  ? 2704 PHE A CA    1 
ATOM   10063 C  C     . PHE A 1 1487 ? 158.445 149.843 216.530 1.00 59.83  ? 2704 PHE A C     1 
ATOM   10064 O  O     . PHE A 1 1487 ? 159.066 150.806 216.990 1.00 63.69  ? 2704 PHE A O     1 
ATOM   10065 C  CB    . PHE A 1 1487 ? 157.494 151.145 214.603 1.00 55.15  ? 2704 PHE A CB    1 
ATOM   10066 C  CG    . PHE A 1 1487 ? 158.146 150.646 213.351 1.00 48.48  ? 2704 PHE A CG    1 
ATOM   10067 C  CD1   . PHE A 1 1487 ? 157.383 150.192 212.291 1.00 47.70  ? 2704 PHE A CD1   1 
ATOM   10068 C  CD2   . PHE A 1 1487 ? 159.523 150.648 213.227 1.00 48.32  ? 2704 PHE A CD2   1 
ATOM   10069 C  CE1   . PHE A 1 1487 ? 157.983 149.741 211.134 1.00 49.84  ? 2704 PHE A CE1   1 
ATOM   10070 C  CE2   . PHE A 1 1487 ? 160.127 150.201 212.073 1.00 48.35  ? 2704 PHE A CE2   1 
ATOM   10071 C  CZ    . PHE A 1 1487 ? 159.357 149.744 211.026 1.00 49.98  ? 2704 PHE A CZ    1 
ATOM   10072 N  N     . LYS A 1 1488 ? 158.796 148.582 216.770 1.00 61.86  ? 2705 LYS A N     1 
ATOM   10073 C  CA    . LYS A 1 1488 ? 159.941 148.250 217.604 1.00 65.67  ? 2705 LYS A CA    1 
ATOM   10074 C  C     . LYS A 1 1488 ? 160.541 146.940 217.113 1.00 67.76  ? 2705 LYS A C     1 
ATOM   10075 O  O     . LYS A 1 1488 ? 160.014 146.292 216.205 1.00 68.88  ? 2705 LYS A O     1 
ATOM   10076 C  CB    . LYS A 1 1488 ? 159.543 148.160 219.081 1.00 67.15  ? 2705 LYS A CB    1 
ATOM   10077 C  CG    . LYS A 1 1488 ? 158.758 146.909 219.440 1.00 69.01  ? 2705 LYS A CG    1 
ATOM   10078 C  CD    . LYS A 1 1488 ? 158.270 146.959 220.879 1.00 69.82  ? 2705 LYS A CD    1 
ATOM   10079 C  CE    . LYS A 1 1488 ? 157.522 145.693 221.253 1.00 73.95  ? 2705 LYS A CE    1 
ATOM   10080 N  NZ    . LYS A 1 1488 ? 158.439 144.531 221.407 1.00 74.00  ? 2705 LYS A NZ    1 
ATOM   10081 N  N     . GLU A 1 1489 ? 161.660 146.554 217.721 1.00 67.03  ? 2706 GLU A N     1 
ATOM   10082 C  CA    . GLU A 1 1489 ? 162.321 145.297 217.392 1.00 72.38  ? 2706 GLU A CA    1 
ATOM   10083 C  C     . GLU A 1 1489 ? 161.589 144.160 218.093 1.00 77.46  ? 2706 GLU A C     1 
ATOM   10084 O  O     . GLU A 1 1489 ? 161.585 144.080 219.326 1.00 80.24  ? 2706 GLU A O     1 
ATOM   10085 C  CB    . GLU A 1 1489 ? 163.791 145.341 217.799 1.00 71.80  ? 2706 GLU A CB    1 
ATOM   10086 C  CG    . GLU A 1 1489 ? 164.686 146.108 216.837 1.00 66.07  ? 2706 GLU A CG    1 
ATOM   10087 C  CD    . GLU A 1 1489 ? 166.161 145.942 217.153 1.00 67.41  ? 2706 GLU A CD    1 
ATOM   10088 O  OE1   . GLU A 1 1489 ? 166.489 145.177 218.083 1.00 75.21  ? 2706 GLU A OE1   1 
ATOM   10089 O  OE2   . GLU A 1 1489 ? 166.994 146.572 216.468 1.00 63.54  ? 2706 GLU A OE2   1 
ATOM   10090 N  N     . VAL A 1 1490 ? 160.970 143.281 217.315 1.00 75.99  ? 2707 VAL A N     1 
ATOM   10091 C  CA    . VAL A 1 1490 ? 160.223 142.166 217.854 1.00 77.51  ? 2707 VAL A CA    1 
ATOM   10092 C  C     . VAL A 1 1490 ? 161.054 140.897 217.711 1.00 83.88  ? 2707 VAL A C     1 
ATOM   10093 O  O     . VAL A 1 1490 ? 162.076 140.870 217.030 1.00 83.37  ? 2707 VAL A O     1 
ATOM   10094 C  CB    . VAL A 1 1490 ? 158.842 142.016 217.175 1.00 75.44  ? 2707 VAL A CB    1 
ATOM   10095 C  CG1   . VAL A 1 1490 ? 158.090 143.333 217.219 1.00 75.15  ? 2707 VAL A CG1   1 
ATOM   10096 C  CG2   . VAL A 1 1490 ? 159.006 141.539 215.746 1.00 74.38  ? 2707 VAL A CG2   1 
ATOM   10097 N  N     . ASN A 1 1491 ? 160.616 139.830 218.371 1.00 90.40  ? 2708 ASN A N     1 
ATOM   10098 C  CA    . ASN A 1 1491 ? 161.359 138.578 218.380 1.00 92.20  ? 2708 ASN A CA    1 
ATOM   10099 C  C     . ASN A 1 1491 ? 160.939 137.633 217.254 1.00 91.86  ? 2708 ASN A C     1 
ATOM   10100 O  O     . ASN A 1 1491 ? 159.764 137.562 216.866 1.00 93.35  ? 2708 ASN A O     1 
ATOM   10101 C  CB    . ASN A 1 1491 ? 161.258 137.907 219.757 1.00 95.35  ? 2708 ASN A CB    1 
ATOM   10102 C  CG    . ASN A 1 1491 ? 159.832 137.590 220.173 1.00 100.78 ? 2708 ASN A CG    1 
ATOM   10103 O  OD1   . ASN A 1 1491 ? 158.887 137.776 219.418 1.00 98.95  ? 2708 ASN A OD1   1 
ATOM   10104 N  ND2   . ASN A 1 1491 ? 159.677 137.107 221.400 1.00 104.04 ? 2708 ASN A ND2   1 
ATOM   10105 N  N     . LYS A 1 1492 ? 161.937 136.920 216.723 1.00 91.67  ? 2709 LYS A N     1 
ATOM   10106 C  CA    . LYS A 1 1492 ? 161.763 136.147 215.498 1.00 90.95  ? 2709 LYS A CA    1 
ATOM   10107 C  C     . LYS A 1 1492 ? 160.782 134.999 215.687 1.00 92.14  ? 2709 LYS A C     1 
ATOM   10108 O  O     . LYS A 1 1492 ? 159.987 134.713 214.788 1.00 92.91  ? 2709 LYS A O     1 
ATOM   10109 C  CB    . LYS A 1 1492 ? 163.114 135.615 215.019 1.00 89.28  ? 2709 LYS A CB    1 
ATOM   10110 C  CG    . LYS A 1 1492 ? 164.037 136.669 214.428 1.00 81.60  ? 2709 LYS A CG    1 
ATOM   10111 C  CD    . LYS A 1 1492 ? 165.022 137.183 215.464 1.00 80.70  ? 2709 LYS A CD    1 
ATOM   10112 C  CE    . LYS A 1 1492 ? 166.006 138.165 214.857 1.00 84.50  ? 2709 LYS A CE    1 
ATOM   10113 N  NZ    . LYS A 1 1492 ? 166.700 138.955 215.909 1.00 89.78  ? 2709 LYS A NZ    1 
ATOM   10114 N  N     . THR A 1 1493 ? 160.830 134.327 216.840 1.00 94.83  ? 2710 THR A N     1 
ATOM   10115 C  CA    . THR A 1 1493 ? 159.993 133.149 217.053 1.00 97.77  ? 2710 THR A CA    1 
ATOM   10116 C  C     . THR A 1 1493 ? 158.511 133.510 217.040 1.00 99.87  ? 2710 THR A C     1 
ATOM   10117 O  O     . THR A 1 1493 ? 157.718 132.904 216.307 1.00 98.97  ? 2710 THR A O     1 
ATOM   10118 C  CB    . THR A 1 1493 ? 160.369 132.473 218.371 1.00 97.52  ? 2710 THR A CB    1 
ATOM   10119 O  OG1   . THR A 1 1493 ? 160.048 133.345 219.462 1.00 101.03 ? 2710 THR A OG1   1 
ATOM   10120 C  CG2   . THR A 1 1493 ? 161.857 132.160 218.401 1.00 93.76  ? 2710 THR A CG2   1 
ATOM   10121 N  N     . ASP A 1 1494 ? 158.122 134.512 217.831 1.00 102.47 ? 2711 ASP A N     1 
ATOM   10122 C  CA    . ASP A 1 1494 ? 156.724 134.924 217.841 1.00 103.98 ? 2711 ASP A CA    1 
ATOM   10123 C  C     . ASP A 1 1494 ? 156.322 135.573 216.525 1.00 100.18 ? 2711 ASP A C     1 
ATOM   10124 O  O     . ASP A 1 1494 ? 155.177 135.406 216.088 1.00 99.48  ? 2711 ASP A O     1 
ATOM   10125 C  CB    . ASP A 1 1494 ? 156.448 135.872 219.007 1.00 103.30 ? 2711 ASP A CB    1 
ATOM   10126 C  CG    . ASP A 1 1494 ? 154.980 136.223 219.140 1.00 103.08 ? 2711 ASP A CG    1 
ATOM   10127 O  OD1   . ASP A 1 1494 ? 154.199 135.363 219.597 1.00 105.01 ? 2711 ASP A OD1   1 
ATOM   10128 O  OD2   . ASP A 1 1494 ? 154.606 137.361 218.785 1.00 97.65  ? 2711 ASP A OD2   1 
ATOM   10129 N  N     . LEU A 1 1495 ? 157.240 136.295 215.870 1.00 97.68  ? 2712 LEU A N     1 
ATOM   10130 C  CA    . LEU A 1 1495 ? 156.910 136.884 214.575 1.00 95.92  ? 2712 LEU A CA    1 
ATOM   10131 C  C     . LEU A 1 1495 ? 156.590 135.809 213.540 1.00 94.98  ? 2712 LEU A C     1 
ATOM   10132 O  O     . LEU A 1 1495 ? 155.571 135.891 212.839 1.00 92.44  ? 2712 LEU A O     1 
ATOM   10133 C  CB    . LEU A 1 1495 ? 158.054 137.772 214.088 1.00 95.25  ? 2712 LEU A CB    1 
ATOM   10134 C  CG    . LEU A 1 1495 ? 157.655 138.779 213.007 1.00 90.91  ? 2712 LEU A CG    1 
ATOM   10135 C  CD1   . LEU A 1 1495 ? 156.580 139.725 213.521 1.00 83.32  ? 2712 LEU A CD1   1 
ATOM   10136 C  CD2   . LEU A 1 1495 ? 158.864 139.549 212.507 1.00 85.54  ? 2712 LEU A CD2   1 
ATOM   10137 N  N     . VAL A 1 1496 ? 157.442 134.783 213.440 1.00 95.20  ? 2713 VAL A N     1 
ATOM   10138 C  CA    . VAL A 1 1496 ? 157.202 133.741 212.449 1.00 91.29  ? 2713 VAL A CA    1 
ATOM   10139 C  C     . VAL A 1 1496 ? 155.987 132.905 212.828 1.00 92.88  ? 2713 VAL A C     1 
ATOM   10140 O  O     . VAL A 1 1496 ? 155.235 132.480 211.947 1.00 94.25  ? 2713 VAL A O     1 
ATOM   10141 C  CB    . VAL A 1 1496 ? 158.454 132.868 212.207 1.00 89.21  ? 2713 VAL A CB    1 
ATOM   10142 C  CG1   . VAL A 1 1496 ? 159.618 133.723 211.718 1.00 86.22  ? 2713 VAL A CG1   1 
ATOM   10143 C  CG2   . VAL A 1 1496 ? 158.840 132.053 213.433 1.00 92.38  ? 2713 VAL A CG2   1 
ATOM   10144 N  N     . ASN A 1 1497 ? 155.745 132.682 214.127 1.00 93.82  ? 2714 ASN A N     1 
ATOM   10145 C  CA    . ASN A 1 1497 ? 154.544 131.954 214.529 1.00 97.01  ? 2714 ASN A CA    1 
ATOM   10146 C  C     . ASN A 1 1497 ? 153.279 132.718 214.151 1.00 98.56  ? 2714 ASN A C     1 
ATOM   10147 O  O     . ASN A 1 1497 ? 152.323 132.130 213.629 1.00 99.37  ? 2714 ASN A O     1 
ATOM   10148 C  CB    . ASN A 1 1497 ? 154.574 131.676 216.031 1.00 96.30  ? 2714 ASN A CB    1 
ATOM   10149 C  CG    . ASN A 1 1497 ? 155.608 130.636 216.409 1.00 98.25  ? 2714 ASN A CG    1 
ATOM   10150 O  OD1   . ASN A 1 1497 ? 156.437 130.243 215.589 1.00 96.29  ? 2714 ASN A OD1   1 
ATOM   10151 N  ND2   . ASN A 1 1497 ? 155.566 130.185 217.657 1.00 103.07 ? 2714 ASN A ND2   1 
ATOM   10152 N  N     . PHE A 1 1498 ? 153.268 134.034 214.383 1.00 97.78  ? 2715 PHE A N     1 
ATOM   10153 C  CA    . PHE A 1 1498 ? 152.102 134.843 214.046 1.00 97.60  ? 2715 PHE A CA    1 
ATOM   10154 C  C     . PHE A 1 1498 ? 151.864 134.872 212.541 1.00 98.42  ? 2715 PHE A C     1 
ATOM   10155 O  O     . PHE A 1 1498 ? 150.728 134.697 212.077 1.00 101.19 ? 2715 PHE A O     1 
ATOM   10156 C  CB    . PHE A 1 1498 ? 152.279 136.260 214.594 1.00 96.67  ? 2715 PHE A CB    1 
ATOM   10157 C  CG    . PHE A 1 1498 ? 151.189 137.212 214.189 1.00 93.16  ? 2715 PHE A CG    1 
ATOM   10158 C  CD1   . PHE A 1 1498 ? 149.968 137.203 214.840 1.00 94.57  ? 2715 PHE A CD1   1 
ATOM   10159 C  CD2   . PHE A 1 1498 ? 151.392 138.126 213.168 1.00 89.39  ? 2715 PHE A CD2   1 
ATOM   10160 C  CE1   . PHE A 1 1498 ? 148.965 138.080 214.473 1.00 95.24  ? 2715 PHE A CE1   1 
ATOM   10161 C  CE2   . PHE A 1 1498 ? 150.394 139.004 212.796 1.00 88.76  ? 2715 PHE A CE2   1 
ATOM   10162 C  CZ    . PHE A 1 1498 ? 149.179 138.982 213.450 1.00 93.72  ? 2715 PHE A CZ    1 
ATOM   10163 N  N     . ILE A 1 1499 ? 152.925 135.085 211.756 1.00 97.82  ? 2716 ILE A N     1 
ATOM   10164 C  CA    . ILE A 1 1499 ? 152.718 135.177 210.314 1.00 96.21  ? 2716 ILE A CA    1 
ATOM   10165 C  C     . ILE A 1 1499 ? 152.379 133.812 209.727 1.00 93.63  ? 2716 ILE A C     1 
ATOM   10166 O  O     . ILE A 1 1499 ? 151.633 133.728 208.749 1.00 91.82  ? 2716 ILE A O     1 
ATOM   10167 C  CB    . ILE A 1 1499 ? 153.926 135.819 209.605 1.00 96.65  ? 2716 ILE A CB    1 
ATOM   10168 C  CG1   . ILE A 1 1499 ? 155.184 134.973 209.768 1.00 92.08  ? 2716 ILE A CG1   1 
ATOM   10169 C  CG2   . ILE A 1 1499 ? 154.162 137.227 210.129 1.00 94.67  ? 2716 ILE A CG2   1 
ATOM   10170 C  CD1   . ILE A 1 1499 ? 156.332 135.434 208.911 1.00 82.23  ? 2716 ILE A CD1   1 
ATOM   10171 N  N     . GLU A 1 1500 ? 152.871 132.721 210.325 1.00 92.25  ? 2717 GLU A N     1 
ATOM   10172 C  CA    . GLU A 1 1500 ? 152.512 131.393 209.839 1.00 93.53  ? 2717 GLU A CA    1 
ATOM   10173 C  C     . GLU A 1 1500 ? 151.064 131.053 210.170 1.00 98.21  ? 2717 GLU A C     1 
ATOM   10174 O  O     . GLU A 1 1500 ? 150.360 130.456 209.347 1.00 104.17 ? 2717 GLU A O     1 
ATOM   10175 C  CB    . GLU A 1 1500 ? 153.458 130.347 210.426 1.00 91.06  ? 2717 GLU A CB    1 
ATOM   10176 C  CG    . GLU A 1 1500 ? 154.780 130.212 209.683 1.00 91.32  ? 2717 GLU A CG    1 
ATOM   10177 C  CD    . GLU A 1 1500 ? 154.733 129.164 208.589 1.00 95.16  ? 2717 GLU A CD    1 
ATOM   10178 O  OE1   . GLU A 1 1500 ? 153.719 128.442 208.496 1.00 99.57  ? 2717 GLU A OE1   1 
ATOM   10179 O  OE2   . GLU A 1 1500 ? 155.715 129.059 207.826 1.00 93.44  ? 2717 GLU A OE2   1 
ATOM   10180 N  N     . GLU A 1 1501 ? 150.598 131.428 211.365 1.00 95.99  ? 2718 GLU A N     1 
ATOM   10181 C  CA    . GLU A 1 1501 ? 149.194 131.212 211.704 1.00 97.61  ? 2718 GLU A CA    1 
ATOM   10182 C  C     . GLU A 1 1501 ? 148.276 132.029 210.801 1.00 99.32  ? 2718 GLU A C     1 
ATOM   10183 O  O     . GLU A 1 1501 ? 147.250 131.526 210.321 1.00 98.52  ? 2718 GLU A O     1 
ATOM   10184 C  CB    . GLU A 1 1501 ? 148.950 131.554 213.173 1.00 100.94 ? 2718 GLU A CB    1 
ATOM   10185 N  N     . ARG A 1 1502 ? 148.638 133.288 210.539 1.00 101.14 ? 2719 ARG A N     1 
ATOM   10186 C  CA    . ARG A 1 1502 ? 147.818 134.104 209.650 1.00 100.65 ? 2719 ARG A CA    1 
ATOM   10187 C  C     . ARG A 1 1502 ? 147.903 133.625 208.205 1.00 101.57 ? 2719 ARG A C     1 
ATOM   10188 O  O     . ARG A 1 1502 ? 146.929 133.751 207.457 1.00 102.62 ? 2719 ARG A O     1 
ATOM   10189 C  CB    . ARG A 1 1502 ? 148.220 135.573 209.768 1.00 98.92  ? 2719 ARG A CB    1 
ATOM   10190 C  CG    . ARG A 1 1502 ? 147.681 136.260 211.020 1.00 98.26  ? 2719 ARG A CG    1 
ATOM   10191 C  CD    . ARG A 1 1502 ? 146.188 136.001 211.221 1.00 98.60  ? 2719 ARG A CD    1 
ATOM   10192 N  NE    . ARG A 1 1502 ? 145.923 134.948 212.197 1.00 99.24  ? 2719 ARG A NE    1 
ATOM   10193 C  CZ    . ARG A 1 1502 ? 145.973 135.109 213.512 1.00 102.68 ? 2719 ARG A CZ    1 
ATOM   10194 N  NH1   . ARG A 1 1502 ? 146.257 136.280 214.056 1.00 103.36 ? 2719 ARG A NH1   1 
ATOM   10195 N  NH2   . ARG A 1 1502 ? 145.729 134.067 214.302 1.00 104.07 ? 2719 ARG A NH2   1 
ATOM   10196 N  N     . PHE A 1 1503 ? 149.042 133.063 207.798 1.00 99.93  ? 2720 PHE A N     1 
ATOM   10197 C  CA    . PHE A 1 1503 ? 149.147 132.452 206.477 1.00 98.74  ? 2720 PHE A CA    1 
ATOM   10198 C  C     . PHE A 1 1503 ? 148.249 131.228 206.358 1.00 102.40 ? 2720 PHE A C     1 
ATOM   10199 O  O     . PHE A 1 1503 ? 147.624 131.010 205.313 1.00 104.04 ? 2720 PHE A O     1 
ATOM   10200 C  CB    . PHE A 1 1503 ? 150.600 132.080 206.193 1.00 96.37  ? 2720 PHE A CB    1 
ATOM   10201 C  CG    . PHE A 1 1503 ? 150.809 131.465 204.846 1.00 100.22 ? 2720 PHE A CG    1 
ATOM   10202 C  CD1   . PHE A 1 1503 ? 150.802 132.246 203.703 1.00 96.45  ? 2720 PHE A CD1   1 
ATOM   10203 C  CD2   . PHE A 1 1503 ? 151.002 130.100 204.722 1.00 103.42 ? 2720 PHE A CD2   1 
ATOM   10204 C  CE1   . PHE A 1 1503 ? 150.988 131.676 202.462 1.00 92.72  ? 2720 PHE A CE1   1 
ATOM   10205 C  CE2   . PHE A 1 1503 ? 151.188 129.525 203.485 1.00 103.42 ? 2720 PHE A CE2   1 
ATOM   10206 C  CZ    . PHE A 1 1503 ? 151.180 130.313 202.355 1.00 97.91  ? 2720 PHE A CZ    1 
ATOM   10207 N  N     . LYS A 1 1504 ? 148.194 130.405 207.409 1.00 104.52 ? 2721 LYS A N     1 
ATOM   10208 C  CA    . LYS A 1 1504 ? 147.270 129.275 207.420 1.00 106.20 ? 2721 LYS A CA    1 
ATOM   10209 C  C     . LYS A 1 1504 ? 145.827 129.750 207.333 1.00 107.85 ? 2721 LYS A C     1 
ATOM   10210 O  O     . LYS A 1 1504 ? 145.011 129.155 206.618 1.00 110.20 ? 2721 LYS A O     1 
ATOM   10211 C  CB    . LYS A 1 1504 ? 147.482 128.430 208.676 1.00 105.43 ? 2721 LYS A CB    1 
ATOM   10212 C  CG    . LYS A 1 1504 ? 148.617 127.424 208.573 1.00 106.95 ? 2721 LYS A CG    1 
ATOM   10213 C  CD    . LYS A 1 1504 ? 148.476 126.557 207.333 1.00 110.77 ? 2721 LYS A CD    1 
ATOM   10214 C  CE    . LYS A 1 1504 ? 148.828 125.109 207.632 1.00 114.23 ? 2721 LYS A CE    1 
ATOM   10215 N  NZ    . LYS A 1 1504 ? 148.715 124.246 206.424 1.00 107.80 ? 2721 LYS A NZ    1 
ATOM   10216 N  N     . THR A 1 1505 ? 145.499 130.828 208.052 1.00 106.04 ? 2722 THR A N     1 
ATOM   10217 C  CA    . THR A 1 1505 ? 144.160 131.406 207.957 1.00 107.13 ? 2722 THR A CA    1 
ATOM   10218 C  C     . THR A 1 1505 ? 143.864 131.892 206.541 1.00 106.93 ? 2722 THR A C     1 
ATOM   10219 O  O     . THR A 1 1505 ? 142.771 131.658 206.013 1.00 108.85 ? 2722 THR A O     1 
ATOM   10220 C  CB    . THR A 1 1505 ? 144.011 132.551 208.958 1.00 105.59 ? 2722 THR A CB    1 
ATOM   10221 O  OG1   . THR A 1 1505 ? 144.465 132.122 210.248 1.00 105.03 ? 2722 THR A OG1   1 
ATOM   10222 C  CG2   . THR A 1 1505 ? 142.557 132.989 209.058 1.00 102.02 ? 2722 THR A CG2   1 
ATOM   10223 N  N     . PHE A 1 1506 ? 144.838 132.553 205.908 1.00 103.55 ? 2723 PHE A N     1 
ATOM   10224 C  CA    . PHE A 1 1506 ? 144.677 133.033 204.537 1.00 102.32 ? 2723 PHE A CA    1 
ATOM   10225 C  C     . PHE A 1 1506 ? 144.418 131.877 203.578 1.00 107.09 ? 2723 PHE A C     1 
ATOM   10226 O  O     . PHE A 1 1506 ? 143.483 131.920 202.767 1.00 109.29 ? 2723 PHE A O     1 
ATOM   10227 C  CB    . PHE A 1 1506 ? 145.933 133.801 204.117 1.00 98.41  ? 2723 PHE A CB    1 
ATOM   10228 C  CG    . PHE A 1 1506 ? 145.768 134.634 202.870 1.00 98.80  ? 2723 PHE A CG    1 
ATOM   10229 C  CD1   . PHE A 1 1506 ? 146.880 135.164 202.237 1.00 95.95  ? 2723 PHE A CD1   1 
ATOM   10230 C  CD2   . PHE A 1 1506 ? 144.514 134.921 202.354 1.00 98.11  ? 2723 PHE A CD2   1 
ATOM   10231 C  CE1   . PHE A 1 1506 ? 146.747 135.932 201.096 1.00 88.73  ? 2723 PHE A CE1   1 
ATOM   10232 C  CE2   . PHE A 1 1506 ? 144.378 135.693 201.215 1.00 96.47  ? 2723 PHE A CE2   1 
ATOM   10233 C  CZ    . PHE A 1 1506 ? 145.496 136.200 200.588 1.00 88.31  ? 2723 PHE A CZ    1 
ATOM   10234 N  N     . CYS A 1 1507 ? 145.234 130.826 203.670 1.00 106.73 ? 2724 CYS A N     1 
ATOM   10235 C  CA    . CYS A 1 1507 ? 145.118 129.708 202.740 1.00 110.72 ? 2724 CYS A CA    1 
ATOM   10236 C  C     . CYS A 1 1507 ? 143.851 128.898 202.983 1.00 114.36 ? 2724 CYS A C     1 
ATOM   10237 O  O     . CYS A 1 1507 ? 143.293 128.331 202.037 1.00 117.28 ? 2724 CYS A O     1 
ATOM   10238 C  CB    . CYS A 1 1507 ? 146.352 128.814 202.837 1.00 113.33 ? 2724 CYS A CB    1 
ATOM   10239 S  SG    . CYS A 1 1507 ? 147.756 129.395 201.858 1.00 110.42 ? 2724 CYS A SG    1 
ATOM   10240 N  N     . ASP A 1 1508 ? 143.382 128.826 204.229 1.00 112.94 ? 2725 ASP A N     1 
ATOM   10241 C  CA    . ASP A 1 1508 ? 142.147 128.107 204.508 1.00 113.00 ? 2725 ASP A CA    1 
ATOM   10242 C  C     . ASP A 1 1508 ? 140.903 128.953 204.273 1.00 113.97 ? 2725 ASP A C     1 
ATOM   10243 O  O     . ASP A 1 1508 ? 139.800 128.399 204.214 1.00 115.74 ? 2725 ASP A O     1 
ATOM   10244 C  CB    . ASP A 1 1508 ? 142.151 127.593 205.949 1.00 111.77 ? 2725 ASP A CB    1 
ATOM   10245 N  N     . GLU A 1 1509 ? 141.045 130.272 204.139 1.00 112.15 ? 2726 GLU A N     1 
ATOM   10246 C  CA    . GLU A 1 1509 ? 139.881 131.138 204.013 1.00 110.62 ? 2726 GLU A CA    1 
ATOM   10247 C  C     . GLU A 1 1509 ? 139.642 131.640 202.594 1.00 111.89 ? 2726 GLU A C     1 
ATOM   10248 O  O     . GLU A 1 1509 ? 138.498 131.641 202.131 1.00 112.39 ? 2726 GLU A O     1 
ATOM   10249 C  CB    . GLU A 1 1509 ? 140.015 132.331 204.966 1.00 109.44 ? 2726 GLU A CB    1 
ATOM   10250 C  CG    . GLU A 1 1509 ? 138.735 133.133 205.134 1.00 109.53 ? 2726 GLU A CG    1 
ATOM   10251 C  CD    . GLU A 1 1509 ? 138.970 134.473 205.800 1.00 107.79 ? 2726 GLU A CD    1 
ATOM   10252 O  OE1   . GLU A 1 1509 ? 139.836 134.548 206.697 1.00 104.71 ? 2726 GLU A OE1   1 
ATOM   10253 O  OE2   . GLU A 1 1509 ? 138.288 135.451 205.428 1.00 107.47 ? 2726 GLU A OE2   1 
ATOM   10254 N  N     . GLU A 1 1510 ? 140.686 132.070 201.884 1.00 112.79 ? 2727 GLU A N     1 
ATOM   10255 C  CA    . GLU A 1 1510 ? 140.483 132.799 200.637 1.00 115.73 ? 2727 GLU A CA    1 
ATOM   10256 C  C     . GLU A 1 1510 ? 140.882 131.999 199.403 1.00 117.37 ? 2727 GLU A C     1 
ATOM   10257 O  O     . GLU A 1 1510 ? 140.046 131.770 198.524 1.00 116.84 ? 2727 GLU A O     1 
ATOM   10258 C  CB    . GLU A 1 1510 ? 141.251 134.126 200.687 1.00 113.79 ? 2727 GLU A CB    1 
ATOM   10259 C  CG    . GLU A 1 1510 ? 140.644 135.225 199.830 1.00 115.23 ? 2727 GLU A CG    1 
ATOM   10260 C  CD    . GLU A 1 1510 ? 139.308 135.707 200.359 1.00 116.29 ? 2727 GLU A CD    1 
ATOM   10261 O  OE1   . GLU A 1 1510 ? 139.085 135.625 201.585 1.00 115.45 ? 2727 GLU A OE1   1 
ATOM   10262 O  OE2   . GLU A 1 1510 ? 138.478 136.166 199.547 1.00 115.32 ? 2727 GLU A OE2   1 
ATOM   10263 N  N     . LEU A 1 1511 ? 142.136 131.564 199.303 1.00 118.09 ? 2728 LEU A N     1 
ATOM   10264 C  CA    . LEU A 1 1511 ? 142.586 130.804 198.145 1.00 122.70 ? 2728 LEU A CA    1 
ATOM   10265 C  C     . LEU A 1 1511 ? 143.436 129.628 198.598 1.00 119.67 ? 2728 LEU A C     1 
ATOM   10266 O  O     . LEU A 1 1511 ? 144.097 129.681 199.638 1.00 114.87 ? 2728 LEU A O     1 
ATOM   10267 C  CB    . LEU A 1 1511 ? 143.389 131.653 197.143 1.00 122.58 ? 2728 LEU A CB    1 
ATOM   10268 C  CG    . LEU A 1 1511 ? 142.707 132.606 196.152 1.00 121.56 ? 2728 LEU A CG    1 
ATOM   10269 C  CD1   . LEU A 1 1511 ? 142.142 133.860 196.804 1.00 116.93 ? 2728 LEU A CD1   1 
ATOM   10270 C  CD2   . LEU A 1 1511 ? 143.669 132.964 195.023 1.00 119.45 ? 2728 LEU A CD2   1 
ATOM   10271 N  N     . GLU A 1 1512 ? 143.412 128.567 197.798 1.00 120.95 ? 2729 GLU A N     1 
ATOM   10272 C  CA    . GLU A 1 1512 ? 144.155 127.337 198.076 1.00 123.46 ? 2729 GLU A CA    1 
ATOM   10273 C  C     . GLU A 1 1512 ? 145.529 127.348 197.410 1.00 120.02 ? 2729 GLU A C     1 
ATOM   10274 O  O     . GLU A 1 1512 ? 145.945 126.386 196.764 1.00 117.53 ? 2729 GLU A O     1 
ATOM   10275 C  CB    . GLU A 1 1512 ? 143.332 126.135 197.623 1.00 125.36 ? 2729 GLU A CB    1 
ATOM   10276 C  CG    . GLU A 1 1512 ? 142.847 126.208 196.171 1.00 127.52 ? 2729 GLU A CG    1 
ATOM   10277 C  CD    . GLU A 1 1512 ? 141.508 126.904 196.024 1.00 130.51 ? 2729 GLU A CD    1 
ATOM   10278 O  OE1   . GLU A 1 1512 ? 141.000 127.441 197.031 1.00 131.56 ? 2729 GLU A OE1   1 
ATOM   10279 O  OE2   . GLU A 1 1512 ? 140.967 126.920 194.899 1.00 132.80 ? 2729 GLU A OE2   1 
ATOM   10280 N  N     . VAL A 1 1513 ? 146.264 128.440 197.590 1.00 117.41 ? 2730 VAL A N     1 
ATOM   10281 C  CA    . VAL A 1 1513 ? 147.556 128.607 196.929 1.00 115.49 ? 2730 VAL A CA    1 
ATOM   10282 C  C     . VAL A 1 1513 ? 148.628 127.859 197.714 1.00 108.46 ? 2730 VAL A C     1 
ATOM   10283 O  O     . VAL A 1 1513 ? 148.837 128.141 198.903 1.00 109.12 ? 2730 VAL A O     1 
ATOM   10284 C  CB    . VAL A 1 1513 ? 147.916 130.092 196.774 1.00 116.66 ? 2730 VAL A CB    1 
ATOM   10285 C  CG1   . VAL A 1 1513 ? 149.210 130.233 195.999 1.00 103.99 ? 2730 VAL A CG1   1 
ATOM   10286 C  CG2   . VAL A 1 1513 ? 146.791 130.841 196.079 1.00 113.42 ? 2730 VAL A CG2   1 
ATOM   10287 N  N     . PRO A 1 1514 ? 149.327 126.908 197.098 1.00 102.78 ? 2731 PRO A N     1 
ATOM   10288 C  CA    . PRO A 1 1514 ? 150.383 126.144 197.799 1.00 101.40 ? 2731 PRO A CA    1 
ATOM   10289 C  C     . PRO A 1 1514 ? 151.715 126.885 197.847 1.00 94.03  ? 2731 PRO A C     1 
ATOM   10290 O  O     . PRO A 1 1514 ? 152.720 126.486 197.247 1.00 89.52  ? 2731 PRO A O     1 
ATOM   10291 C  CB    . PRO A 1 1514 ? 150.453 124.856 196.974 1.00 103.56 ? 2731 PRO A CB    1 
ATOM   10292 C  CG    . PRO A 1 1514 ? 150.091 125.288 195.594 1.00 98.77  ? 2731 PRO A CG    1 
ATOM   10293 C  CD    . PRO A 1 1514 ? 149.074 126.388 195.742 1.00 100.93 ? 2731 PRO A CD    1 
ATOM   10294 N  N     . MET A 1 1515 ? 151.739 127.997 198.577 1.00 92.67  ? 2732 MET A N     1 
ATOM   10295 C  CA    . MET A 1 1515 ? 152.970 128.759 198.725 1.00 87.94  ? 2732 MET A CA    1 
ATOM   10296 C  C     . MET A 1 1515 ? 153.938 128.061 199.676 1.00 83.72  ? 2732 MET A C     1 
ATOM   10297 O  O     . MET A 1 1515 ? 153.552 127.256 200.528 1.00 85.44  ? 2732 MET A O     1 
ATOM   10298 C  CB    . MET A 1 1515 ? 152.684 130.172 199.232 1.00 93.42  ? 2732 MET A CB    1 
ATOM   10299 C  CG    . MET A 1 1515 ? 151.923 131.052 198.265 1.00 92.68  ? 2732 MET A CG    1 
ATOM   10300 S  SD    . MET A 1 1515 ? 152.829 131.297 196.726 1.00 81.08  ? 2732 MET A SD    1 
ATOM   10301 C  CE    . MET A 1 1515 ? 154.197 132.307 197.289 1.00 73.66  ? 2732 MET A CE    1 
ATOM   10302 N  N     . VAL A 1 1516 ? 155.217 128.387 199.517 1.00 79.48  ? 2733 VAL A N     1 
ATOM   10303 C  CA    . VAL A 1 1516 ? 156.288 127.854 200.348 1.00 79.56  ? 2733 VAL A CA    1 
ATOM   10304 C  C     . VAL A 1 1516 ? 156.885 129.004 201.144 1.00 79.57  ? 2733 VAL A C     1 
ATOM   10305 O  O     . VAL A 1 1516 ? 157.276 130.026 200.568 1.00 83.34  ? 2733 VAL A O     1 
ATOM   10306 C  CB    . VAL A 1 1516 ? 157.366 127.153 199.503 1.00 76.30  ? 2733 VAL A CB    1 
ATOM   10307 C  CG1   . VAL A 1 1516 ? 158.463 126.619 200.396 1.00 76.47  ? 2733 VAL A CG1   1 
ATOM   10308 C  CG2   . VAL A 1 1516 ? 156.751 126.033 198.682 1.00 81.11  ? 2733 VAL A CG2   1 
ATOM   10309 N  N     . ILE A 1 1517 ? 156.951 128.841 202.461 1.00 75.03  ? 2734 ILE A N     1 
ATOM   10310 C  CA    . ILE A 1 1517 ? 157.429 129.888 203.356 1.00 73.97  ? 2734 ILE A CA    1 
ATOM   10311 C  C     . ILE A 1 1517 ? 158.931 129.730 203.541 1.00 66.78  ? 2734 ILE A C     1 
ATOM   10312 O  O     . ILE A 1 1517 ? 159.427 128.617 203.752 1.00 70.44  ? 2734 ILE A O     1 
ATOM   10313 C  CB    . ILE A 1 1517 ? 156.697 129.835 204.708 1.00 81.90  ? 2734 ILE A CB    1 
ATOM   10314 C  CG1   . ILE A 1 1517 ? 155.181 129.784 204.500 1.00 86.82  ? 2734 ILE A CG1   1 
ATOM   10315 C  CG2   . ILE A 1 1517 ? 157.071 131.035 205.566 1.00 77.98  ? 2734 ILE A CG2   1 
ATOM   10316 C  CD1   . ILE A 1 1517 ? 154.567 128.414 204.736 1.00 84.41  ? 2734 ILE A CD1   1 
ATOM   10317 N  N     . HIS A 1 1518 ? 159.658 130.842 203.459 1.00 61.39  ? 2735 HIS A N     1 
ATOM   10318 C  CA    . HIS A 1 1518 ? 161.105 130.826 203.615 1.00 60.38  ? 2735 HIS A CA    1 
ATOM   10319 C  C     . HIS A 1 1518 ? 161.566 132.172 204.162 1.00 63.24  ? 2735 HIS A C     1 
ATOM   10320 O  O     . HIS A 1 1518 ? 160.794 133.133 204.242 1.00 66.26  ? 2735 HIS A O     1 
ATOM   10321 C  CB    . HIS A 1 1518 ? 161.802 130.462 202.296 1.00 61.81  ? 2735 HIS A CB    1 
ATOM   10322 C  CG    . HIS A 1 1518 ? 161.308 131.225 201.107 1.00 60.15  ? 2735 HIS A CG    1 
ATOM   10323 N  ND1   . HIS A 1 1518 ? 162.015 132.262 200.539 1.00 62.05  ? 2735 HIS A ND1   1 
ATOM   10324 C  CD2   . HIS A 1 1518 ? 160.183 131.088 200.365 1.00 60.64  ? 2735 HIS A CD2   1 
ATOM   10325 C  CE1   . HIS A 1 1518 ? 161.344 132.737 199.505 1.00 61.25  ? 2735 HIS A CE1   1 
ATOM   10326 N  NE2   . HIS A 1 1518 ? 160.228 132.043 199.379 1.00 57.15  ? 2735 HIS A NE2   1 
ATOM   10327 N  N     . GLU A 1 1519 ? 162.840 132.215 204.566 1.00 62.90  ? 2736 GLU A N     1 
ATOM   10328 C  CA    . GLU A 1 1519 ? 163.373 133.372 205.285 1.00 63.18  ? 2736 GLU A CA    1 
ATOM   10329 C  C     . GLU A 1 1519 ? 163.367 134.629 204.425 1.00 62.42  ? 2736 GLU A C     1 
ATOM   10330 O  O     . GLU A 1 1519 ? 163.076 135.726 204.920 1.00 65.37  ? 2736 GLU A O     1 
ATOM   10331 C  CB    . GLU A 1 1519 ? 164.789 133.075 205.777 1.00 65.94  ? 2736 GLU A CB    1 
ATOM   10332 C  CG    . GLU A 1 1519 ? 164.848 132.271 207.064 1.00 70.57  ? 2736 GLU A CG    1 
ATOM   10333 C  CD    . GLU A 1 1519 ? 166.268 131.925 207.468 1.00 74.67  ? 2736 GLU A CD    1 
ATOM   10334 O  OE1   . GLU A 1 1519 ? 167.208 132.344 206.761 1.00 76.16  ? 2736 GLU A OE1   1 
ATOM   10335 O  OE2   . GLU A 1 1519 ? 166.444 131.235 208.494 1.00 71.39  ? 2736 GLU A OE2   1 
ATOM   10336 N  N     . SER A 1 1520 ? 163.713 134.496 203.142 1.00 59.29  ? 2737 SER A N     1 
ATOM   10337 C  CA    . SER A 1 1520 ? 163.671 135.645 202.244 1.00 58.52  ? 2737 SER A CA    1 
ATOM   10338 C  C     . SER A 1 1520 ? 162.249 136.168 202.097 1.00 55.78  ? 2737 SER A C     1 
ATOM   10339 O  O     . SER A 1 1520 ? 162.024 137.384 202.079 1.00 58.70  ? 2737 SER A O     1 
ATOM   10340 C  CB    . SER A 1 1520 ? 164.252 135.267 200.882 1.00 60.79  ? 2737 SER A CB    1 
ATOM   10341 O  OG    . SER A 1 1520 ? 164.648 136.418 200.158 1.00 59.13  ? 2737 SER A OG    1 
ATOM   10342 N  N     . MET A 1 1521 ? 161.274 135.260 202.014 1.00 53.22  ? 2738 MET A N     1 
ATOM   10343 C  CA    . MET A 1 1521 ? 159.876 135.669 201.952 1.00 53.05  ? 2738 MET A CA    1 
ATOM   10344 C  C     . MET A 1 1521 ? 159.457 136.394 203.225 1.00 57.13  ? 2738 MET A C     1 
ATOM   10345 O  O     . MET A 1 1521 ? 158.732 137.391 203.164 1.00 57.23  ? 2738 MET A O     1 
ATOM   10346 C  CB    . MET A 1 1521 ? 158.986 134.451 201.703 1.00 58.38  ? 2738 MET A CB    1 
ATOM   10347 C  CG    . MET A 1 1521 ? 157.495 134.726 201.803 1.00 62.67  ? 2738 MET A CG    1 
ATOM   10348 S  SD    . MET A 1 1521 ? 156.498 133.238 201.600 1.00 73.26  ? 2738 MET A SD    1 
ATOM   10349 C  CE    . MET A 1 1521 ? 155.459 133.315 203.057 1.00 68.12  ? 2738 MET A CE    1 
ATOM   10350 N  N     . VAL A 1 1522 ? 159.909 135.914 204.387 1.00 59.13  ? 2739 VAL A N     1 
ATOM   10351 C  CA    . VAL A 1 1522 ? 159.552 136.559 205.651 1.00 58.96  ? 2739 VAL A CA    1 
ATOM   10352 C  C     . VAL A 1 1522 ? 160.141 137.964 205.722 1.00 58.14  ? 2739 VAL A C     1 
ATOM   10353 O  O     . VAL A 1 1522 ? 159.451 138.934 206.067 1.00 66.20  ? 2739 VAL A O     1 
ATOM   10354 C  CB    . VAL A 1 1522 ? 160.011 135.697 206.840 1.00 60.21  ? 2739 VAL A CB    1 
ATOM   10355 C  CG1   . VAL A 1 1522 ? 159.865 136.465 208.143 1.00 56.96  ? 2739 VAL A CG1   1 
ATOM   10356 C  CG2   . VAL A 1 1522 ? 159.222 134.401 206.888 1.00 66.04  ? 2739 VAL A CG2   1 
ATOM   10357 N  N     . ASP A 1 1523 ? 161.423 138.096 205.371 1.00 54.99  ? 2740 ASP A N     1 
ATOM   10358 C  CA    . ASP A 1 1523 ? 162.073 139.405 205.387 1.00 55.60  ? 2740 ASP A CA    1 
ATOM   10359 C  C     . ASP A 1 1523 ? 161.408 140.369 204.411 1.00 55.16  ? 2740 ASP A C     1 
ATOM   10360 O  O     . ASP A 1 1523 ? 161.200 141.548 204.727 1.00 56.13  ? 2740 ASP A O     1 
ATOM   10361 C  CB    . ASP A 1 1523 ? 163.558 139.252 205.062 1.00 54.10  ? 2740 ASP A CB    1 
ATOM   10362 C  CG    . ASP A 1 1523 ? 164.242 140.582 204.829 1.00 54.49  ? 2740 ASP A CG    1 
ATOM   10363 O  OD1   . ASP A 1 1523 ? 164.568 141.269 205.820 1.00 61.33  ? 2740 ASP A OD1   1 
ATOM   10364 O  OD2   . ASP A 1 1523 ? 164.452 140.943 203.653 1.00 48.54  ? 2740 ASP A OD2   1 
ATOM   10365 N  N     . HIS A 1 1524 ? 161.038 139.880 203.230 1.00 53.10  ? 2741 HIS A N     1 
ATOM   10366 C  CA    . HIS A 1 1524 ? 160.453 140.766 202.236 1.00 51.17  ? 2741 HIS A CA    1 
ATOM   10367 C  C     . HIS A 1 1524 ? 159.001 141.122 202.538 1.00 50.93  ? 2741 HIS A C     1 
ATOM   10368 O  O     . HIS A 1 1524 ? 158.575 142.238 202.221 1.00 57.67  ? 2741 HIS A O     1 
ATOM   10369 C  CB    . HIS A 1 1524 ? 160.591 140.139 200.856 1.00 56.50  ? 2741 HIS A CB    1 
ATOM   10370 C  CG    . HIS A 1 1524 ? 161.989 140.175 200.322 1.00 59.31  ? 2741 HIS A CG    1 
ATOM   10371 N  ND1   . HIS A 1 1524 ? 163.006 140.873 200.935 1.00 56.17  ? 2741 HIS A ND1   1 
ATOM   10372 C  CD2   . HIS A 1 1524 ? 162.536 139.600 199.225 1.00 60.48  ? 2741 HIS A CD2   1 
ATOM   10373 C  CE1   . HIS A 1 1524 ? 164.119 140.728 200.238 1.00 55.96  ? 2741 HIS A CE1   1 
ATOM   10374 N  NE2   . HIS A 1 1524 ? 163.860 139.959 199.196 1.00 58.55  ? 2741 HIS A NE2   1 
ATOM   10375 N  N     . ILE A 1 1525 ? 158.224 140.221 203.147 1.00 48.47  ? 2742 ILE A N     1 
ATOM   10376 C  CA    . ILE A 1 1525 ? 156.889 140.634 203.568 1.00 54.47  ? 2742 ILE A CA    1 
ATOM   10377 C  C     . ILE A 1 1525 ? 156.991 141.624 204.718 1.00 52.34  ? 2742 ILE A C     1 
ATOM   10378 O  O     . ILE A 1 1525 ? 156.171 142.543 204.821 1.00 58.85  ? 2742 ILE A O     1 
ATOM   10379 C  CB    . ILE A 1 1525 ? 155.975 139.438 203.921 1.00 58.71  ? 2742 ILE A CB    1 
ATOM   10380 C  CG1   . ILE A 1 1525 ? 156.462 138.673 205.152 1.00 55.97  ? 2742 ILE A CG1   1 
ATOM   10381 C  CG2   . ILE A 1 1525 ? 155.790 138.519 202.722 1.00 68.17  ? 2742 ILE A CG2   1 
ATOM   10382 C  CD1   . ILE A 1 1525 ? 155.449 137.696 205.693 1.00 59.19  ? 2742 ILE A CD1   1 
ATOM   10383 N  N     . LEU A 1 1526 ? 158.012 141.488 205.570 1.00 49.34  ? 2743 LEU A N     1 
ATOM   10384 C  CA    . LEU A 1 1526 ? 158.261 142.500 206.593 1.00 49.73  ? 2743 LEU A CA    1 
ATOM   10385 C  C     . LEU A 1 1526 ? 158.553 143.856 205.960 1.00 52.85  ? 2743 LEU A C     1 
ATOM   10386 O  O     . LEU A 1 1526 ? 158.003 144.884 206.376 1.00 54.14  ? 2743 LEU A O     1 
ATOM   10387 C  CB    . LEU A 1 1526 ? 159.425 142.058 207.477 1.00 53.07  ? 2743 LEU A CB    1 
ATOM   10388 C  CG    . LEU A 1 1526 ? 159.402 142.514 208.929 1.00 59.67  ? 2743 LEU A CG    1 
ATOM   10389 C  CD1   . LEU A 1 1526 ? 158.210 141.899 209.634 1.00 62.52  ? 2743 LEU A CD1   1 
ATOM   10390 C  CD2   . LEU A 1 1526 ? 160.702 142.130 209.617 1.00 60.83  ? 2743 LEU A CD2   1 
ATOM   10391 N  N     . ARG A 1 1527 ? 159.405 143.869 204.931 1.00 52.69  ? 2744 ARG A N     1 
ATOM   10392 C  CA    . ARG A 1 1527 ? 159.769 145.126 204.280 1.00 50.40  ? 2744 ARG A CA    1 
ATOM   10393 C  C     . ARG A 1 1527 ? 158.579 145.758 203.562 1.00 48.70  ? 2744 ARG A C     1 
ATOM   10394 O  O     . ARG A 1 1527 ? 158.379 146.978 203.635 1.00 49.70  ? 2744 ARG A O     1 
ATOM   10395 C  CB    . ARG A 1 1527 ? 160.924 144.893 203.308 1.00 47.09  ? 2744 ARG A CB    1 
ATOM   10396 C  CG    . ARG A 1 1527 ? 161.277 146.103 202.469 1.00 47.22  ? 2744 ARG A CG    1 
ATOM   10397 C  CD    . ARG A 1 1527 ? 162.478 145.831 201.586 1.00 48.11  ? 2744 ARG A CD    1 
ATOM   10398 N  NE    . ARG A 1 1527 ? 163.625 145.352 202.346 1.00 48.50  ? 2744 ARG A NE    1 
ATOM   10399 C  CZ    . ARG A 1 1527 ? 164.733 144.868 201.802 1.00 49.72  ? 2744 ARG A CZ    1 
ATOM   10400 N  NH1   . ARG A 1 1527 ? 164.876 144.780 200.490 1.00 50.16  ? 2744 ARG A NH1   1 
ATOM   10401 N  NH2   . ARG A 1 1527 ? 165.721 144.463 202.593 1.00 50.23  ? 2744 ARG A NH2   1 
ATOM   10402 N  N     . ILE A 1 1528 ? 157.773 144.953 202.867 1.00 48.33  ? 2745 ILE A N     1 
ATOM   10403 C  CA    . ILE A 1 1528 ? 156.632 145.525 202.159 1.00 47.86  ? 2745 ILE A CA    1 
ATOM   10404 C  C     . ILE A 1 1528 ? 155.548 145.968 203.139 1.00 53.79  ? 2745 ILE A C     1 
ATOM   10405 O  O     . ILE A 1 1528 ? 154.835 146.943 202.876 1.00 59.06  ? 2745 ILE A O     1 
ATOM   10406 C  CB    . ILE A 1 1528 ? 156.096 144.553 201.088 1.00 50.03  ? 2745 ILE A CB    1 
ATOM   10407 C  CG1   . ILE A 1 1528 ? 155.178 145.294 200.115 1.00 54.93  ? 2745 ILE A CG1   1 
ATOM   10408 C  CG2   . ILE A 1 1528 ? 155.371 143.377 201.704 1.00 49.15  ? 2745 ILE A CG2   1 
ATOM   10409 C  CD1   . ILE A 1 1528 ? 154.554 144.407 199.072 1.00 60.45  ? 2745 ILE A CD1   1 
ATOM   10410 N  N     . ASP A 1 1529 ? 155.420 145.303 204.293 1.00 52.13  ? 2746 ASP A N     1 
ATOM   10411 C  CA    . ASP A 1 1529 ? 154.493 145.791 205.309 1.00 50.03  ? 2746 ASP A CA    1 
ATOM   10412 C  C     . ASP A 1 1529 ? 154.976 147.107 205.901 1.00 54.10  ? 2746 ASP A C     1 
ATOM   10413 O  O     . ASP A 1 1529 ? 154.166 147.990 206.207 1.00 58.68  ? 2746 ASP A O     1 
ATOM   10414 C  CB    . ASP A 1 1529 ? 154.308 144.747 206.406 1.00 51.94  ? 2746 ASP A CB    1 
ATOM   10415 C  CG    . ASP A 1 1529 ? 153.091 145.019 207.265 1.00 56.97  ? 2746 ASP A CG    1 
ATOM   10416 O  OD1   . ASP A 1 1529 ? 152.292 145.909 206.907 1.00 55.99  ? 2746 ASP A OD1   1 
ATOM   10417 O  OD2   . ASP A 1 1529 ? 152.933 144.340 208.299 1.00 63.98  ? 2746 ASP A OD2   1 
ATOM   10418 N  N     . ARG A 1 1530 ? 156.294 147.255 206.067 1.00 51.14  ? 2747 ARG A N     1 
ATOM   10419 C  CA    . ARG A 1 1530 ? 156.850 148.539 206.487 1.00 47.27  ? 2747 ARG A CA    1 
ATOM   10420 C  C     . ARG A 1 1530 ? 156.513 149.627 205.476 1.00 50.51  ? 2747 ARG A C     1 
ATOM   10421 O  O     . ARG A 1 1530 ? 156.047 150.711 205.843 1.00 53.86  ? 2747 ARG A O     1 
ATOM   10422 C  CB    . ARG A 1 1530 ? 158.366 148.420 206.663 1.00 43.71  ? 2747 ARG A CB    1 
ATOM   10423 C  CG    . ARG A 1 1530 ? 159.042 149.550 207.448 1.00 46.32  ? 2747 ARG A CG    1 
ATOM   10424 C  CD    . ARG A 1 1530 ? 159.424 150.740 206.574 1.00 46.24  ? 2747 ARG A CD    1 
ATOM   10425 N  NE    . ARG A 1 1530 ? 160.250 150.351 205.438 1.00 46.13  ? 2747 ARG A NE    1 
ATOM   10426 C  CZ    . ARG A 1 1530 ? 160.442 151.107 204.366 1.00 48.66  ? 2747 ARG A CZ    1 
ATOM   10427 N  NH1   . ARG A 1 1530 ? 159.888 152.303 204.257 1.00 48.45  ? 2747 ARG A NH1   1 
ATOM   10428 N  NH2   . ARG A 1 1530 ? 161.200 150.649 203.375 1.00 52.14  ? 2747 ARG A NH2   1 
ATOM   10429 N  N     . ALA A 1 1531 ? 156.743 149.349 204.191 1.00 50.98  ? 2748 ALA A N     1 
ATOM   10430 C  CA    . ALA A 1 1531 ? 156.521 150.361 203.163 1.00 48.81  ? 2748 ALA A CA    1 
ATOM   10431 C  C     . ALA A 1 1531 ? 155.041 150.676 202.979 1.00 46.97  ? 2748 ALA A C     1 
ATOM   10432 O  O     . ALA A 1 1531 ? 154.696 151.783 202.553 1.00 50.74  ? 2748 ALA A O     1 
ATOM   10433 C  CB    . ALA A 1 1531 ? 157.140 149.913 201.842 1.00 52.61  ? 2748 ALA A CB    1 
ATOM   10434 N  N     . LEU A 1 1532 ? 154.156 149.728 203.285 1.00 48.98  ? 2749 LEU A N     1 
ATOM   10435 C  CA    . LEU A 1 1532 ? 152.725 149.999 203.285 1.00 54.90  ? 2749 LEU A CA    1 
ATOM   10436 C  C     . LEU A 1 1532 ? 152.228 150.568 204.607 1.00 58.80  ? 2749 LEU A C     1 
ATOM   10437 O  O     . LEU A 1 1532 ? 151.054 150.945 204.698 1.00 60.44  ? 2749 LEU A O     1 
ATOM   10438 C  CB    . LEU A 1 1532 ? 151.936 148.729 202.949 1.00 53.84  ? 2749 LEU A CB    1 
ATOM   10439 C  CG    . LEU A 1 1532 ? 151.543 148.548 201.480 1.00 59.74  ? 2749 LEU A CG    1 
ATOM   10440 C  CD1   . LEU A 1 1532 ? 152.742 148.177 200.626 1.00 57.15  ? 2749 LEU A CD1   1 
ATOM   10441 C  CD2   . LEU A 1 1532 ? 150.437 147.514 201.339 1.00 61.38  ? 2749 LEU A CD2   1 
ATOM   10442 N  N     . LYS A 1 1533 ? 153.081 150.636 205.626 1.00 54.13  ? 2750 LYS A N     1 
ATOM   10443 C  CA    . LYS A 1 1533 ? 152.726 151.261 206.893 1.00 50.96  ? 2750 LYS A CA    1 
ATOM   10444 C  C     . LYS A 1 1533 ? 153.092 152.737 206.950 1.00 54.68  ? 2750 LYS A C     1 
ATOM   10445 O  O     . LYS A 1 1533 ? 152.934 153.358 208.006 1.00 57.86  ? 2750 LYS A O     1 
ATOM   10446 C  CB    . LYS A 1 1533 ? 153.403 150.526 208.053 1.00 50.44  ? 2750 LYS A CB    1 
ATOM   10447 C  CG    . LYS A 1 1533 ? 152.548 149.441 208.685 1.00 55.69  ? 2750 LYS A CG    1 
ATOM   10448 C  CD    . LYS A 1 1533 ? 152.988 149.162 210.109 1.00 58.41  ? 2750 LYS A CD    1 
ATOM   10449 C  CE    . LYS A 1 1533 ? 152.153 148.065 210.736 1.00 58.77  ? 2750 LYS A CE    1 
ATOM   10450 N  NZ    . LYS A 1 1533 ? 152.584 147.781 212.129 1.00 62.38  ? 2750 LYS A NZ    1 
ATOM   10451 N  N     . GLN A 1 1534 ? 153.574 153.312 205.853 1.00 56.87  ? 2751 GLN A N     1 
ATOM   10452 C  CA    . GLN A 1 1534 ? 153.965 154.710 205.811 1.00 57.42  ? 2751 GLN A CA    1 
ATOM   10453 C  C     . GLN A 1 1534 ? 152.876 155.551 205.150 1.00 62.39  ? 2751 GLN A C     1 
ATOM   10454 O  O     . GLN A 1 1534 ? 151.788 155.073 204.818 1.00 57.53  ? 2751 GLN A O     1 
ATOM   10455 C  CB    . GLN A 1 1534 ? 155.295 154.875 205.074 1.00 46.47  ? 2751 GLN A CB    1 
ATOM   10456 C  CG    . GLN A 1 1534 ? 156.517 154.567 205.913 1.00 44.26  ? 2751 GLN A CG    1 
ATOM   10457 C  CD    . GLN A 1 1534 ? 157.807 154.909 205.200 1.00 45.99  ? 2751 GLN A CD    1 
ATOM   10458 O  OE1   . GLN A 1 1534 ? 157.796 155.370 204.059 1.00 40.72  ? 2751 GLN A OE1   1 
ATOM   10459 N  NE2   . GLN A 1 1534 ? 158.930 154.687 205.871 1.00 47.73  ? 2751 GLN A NE2   1 
ATOM   10460 N  N     . VAL A 1 1535 ? 153.182 156.831 204.965 1.00 68.22  ? 2752 VAL A N     1 
ATOM   10461 C  CA    . VAL A 1 1535 ? 152.326 157.747 204.223 1.00 71.33  ? 2752 VAL A CA    1 
ATOM   10462 C  C     . VAL A 1 1535 ? 152.765 157.725 202.766 1.00 75.08  ? 2752 VAL A C     1 
ATOM   10463 O  O     . VAL A 1 1535 ? 153.957 157.873 202.470 1.00 76.61  ? 2752 VAL A O     1 
ATOM   10464 C  CB    . VAL A 1 1535 ? 152.406 159.168 204.805 1.00 65.39  ? 2752 VAL A CB    1 
ATOM   10465 C  CG1   . VAL A 1 1535 ? 151.658 160.154 203.920 1.00 68.47  ? 2752 VAL A CG1   1 
ATOM   10466 C  CG2   . VAL A 1 1535 ? 151.859 159.192 206.222 1.00 64.17  ? 2752 VAL A CG2   1 
ATOM   10467 N  N     . GLN A 1 1536 ? 151.802 157.526 201.861 1.00 76.98  ? 2753 GLN A N     1 
ATOM   10468 C  CA    . GLN A 1 1536 ? 152.048 157.414 200.421 1.00 76.71  ? 2753 GLN A CA    1 
ATOM   10469 C  C     . GLN A 1 1536 ? 153.008 156.260 200.120 1.00 74.09  ? 2753 GLN A C     1 
ATOM   10470 O  O     . GLN A 1 1536 ? 154.133 156.449 199.650 1.00 76.49  ? 2753 GLN A O     1 
ATOM   10471 C  CB    . GLN A 1 1536 ? 152.558 158.741 199.842 1.00 77.77  ? 2753 GLN A CB    1 
ATOM   10472 C  CG    . GLN A 1 1536 ? 152.392 158.871 198.342 1.00 81.34  ? 2753 GLN A CG    1 
ATOM   10473 C  CD    . GLN A 1 1536 ? 150.967 159.186 197.946 1.00 88.69  ? 2753 GLN A CD    1 
ATOM   10474 O  OE1   . GLN A 1 1536 ? 150.199 158.293 197.587 1.00 87.58  ? 2753 GLN A OE1   1 
ATOM   10475 N  NE2   . GLN A 1 1536 ? 150.606 160.461 198.005 1.00 87.07  ? 2753 GLN A NE2   1 
ATOM   10476 N  N     . GLY A 1 1537 ? 152.545 155.049 200.424 1.00 70.33  ? 2754 GLY A N     1 
ATOM   10477 C  CA    . GLY A 1 1537 ? 153.317 153.849 200.203 1.00 67.46  ? 2754 GLY A CA    1 
ATOM   10478 C  C     . GLY A 1 1537 ? 152.934 153.165 198.907 1.00 66.21  ? 2754 GLY A C     1 
ATOM   10479 O  O     . GLY A 1 1537 ? 151.793 152.735 198.732 1.00 67.00  ? 2754 GLY A O     1 
ATOM   10480 N  N     . HIS A 1 1538 ? 153.900 153.072 197.994 1.00 62.47  ? 2755 HIS A N     1 
ATOM   10481 C  CA    . HIS A 1 1538 ? 153.723 152.396 196.716 1.00 62.57  ? 2755 HIS A CA    1 
ATOM   10482 C  C     . HIS A 1 1538 ? 154.983 151.599 196.407 1.00 64.49  ? 2755 HIS A C     1 
ATOM   10483 O  O     . HIS A 1 1538 ? 156.067 151.895 196.917 1.00 63.55  ? 2755 HIS A O     1 
ATOM   10484 C  CB    . HIS A 1 1538 ? 153.411 153.388 195.588 1.00 62.52  ? 2755 HIS A CB    1 
ATOM   10485 C  CG    . HIS A 1 1538 ? 152.423 154.444 195.971 1.00 64.10  ? 2755 HIS A CG    1 
ATOM   10486 N  ND1   . HIS A 1 1538 ? 151.062 154.227 195.953 1.00 70.37  ? 2755 HIS A ND1   1 
ATOM   10487 C  CD2   . HIS A 1 1538 ? 152.595 155.719 196.389 1.00 67.18  ? 2755 HIS A CD2   1 
ATOM   10488 C  CE1   . HIS A 1 1538 ? 150.439 155.326 196.339 1.00 75.12  ? 2755 HIS A CE1   1 
ATOM   10489 N  NE2   . HIS A 1 1538 ? 151.346 156.246 196.610 1.00 67.87  ? 2755 HIS A NE2   1 
ATOM   10490 N  N     . MET A 1 1539 ? 154.835 150.576 195.565 1.00 63.45  ? 2756 MET A N     1 
ATOM   10491 C  CA    . MET A 1 1539 ? 155.866 149.563 195.391 1.00 60.20  ? 2756 MET A CA    1 
ATOM   10492 C  C     . MET A 1 1539 ? 156.284 149.412 193.934 1.00 62.03  ? 2756 MET A C     1 
ATOM   10493 O  O     . MET A 1 1539 ? 155.442 149.285 193.040 1.00 61.21  ? 2756 MET A O     1 
ATOM   10494 C  CB    . MET A 1 1539 ? 155.390 148.202 195.924 1.00 55.88  ? 2756 MET A CB    1 
ATOM   10495 C  CG    . MET A 1 1539 ? 154.786 148.229 197.327 1.00 52.02  ? 2756 MET A CG    1 
ATOM   10496 S  SD    . MET A 1 1539 ? 155.811 148.839 198.685 1.00 52.13  ? 2756 MET A SD    1 
ATOM   10497 C  CE    . MET A 1 1539 ? 157.453 148.244 198.268 1.00 58.59  ? 2756 MET A CE    1 
ATOM   10498 N  N     . MET A 1 1540 ? 157.598 149.425 193.716 1.00 62.75  ? 2757 MET A N     1 
ATOM   10499 C  CA    . MET A 1 1540 ? 158.256 148.974 192.489 1.00 65.86  ? 2757 MET A CA    1 
ATOM   10500 C  C     . MET A 1 1540 ? 159.029 147.711 192.860 1.00 71.41  ? 2757 MET A C     1 
ATOM   10501 O  O     . MET A 1 1540 ? 160.211 147.776 193.206 1.00 70.57  ? 2757 MET A O     1 
ATOM   10502 C  CB    . MET A 1 1540 ? 159.188 150.042 191.914 1.00 68.77  ? 2757 MET A CB    1 
ATOM   10503 C  CG    . MET A 1 1540 ? 159.184 150.179 190.395 1.00 66.99  ? 2757 MET A CG    1 
ATOM   10504 S  SD    . MET A 1 1540 ? 157.584 150.490 189.638 1.00 68.33  ? 2757 MET A SD    1 
ATOM   10505 C  CE    . MET A 1 1540 ? 157.512 152.277 189.697 1.00 64.99  ? 2757 MET A CE    1 
ATOM   10506 N  N     . LEU A 1 1541 ? 158.361 146.563 192.791 1.00 70.59  ? 2758 LEU A N     1 
ATOM   10507 C  CA    . LEU A 1 1541 ? 158.954 145.303 193.227 1.00 62.12  ? 2758 LEU A CA    1 
ATOM   10508 C  C     . LEU A 1 1541 ? 159.748 144.698 192.075 1.00 66.06  ? 2758 LEU A C     1 
ATOM   10509 O  O     . LEU A 1 1541 ? 159.165 144.198 191.108 1.00 73.82  ? 2758 LEU A O     1 
ATOM   10510 C  CB    . LEU A 1 1541 ? 157.865 144.347 193.704 1.00 57.51  ? 2758 LEU A CB    1 
ATOM   10511 C  CG    . LEU A 1 1541 ? 157.169 144.696 195.021 1.00 50.98  ? 2758 LEU A CG    1 
ATOM   10512 C  CD1   . LEU A 1 1541 ? 155.724 144.225 195.007 1.00 47.92  ? 2758 LEU A CD1   1 
ATOM   10513 C  CD2   . LEU A 1 1541 ? 157.913 144.097 196.194 1.00 51.12  ? 2758 LEU A CD2   1 
ATOM   10514 N  N     . ILE A 1 1542 ? 161.075 144.730 192.173 1.00 61.06  ? 2759 ILE A N     1 
ATOM   10515 C  CA    . ILE A 1 1542 ? 161.940 144.132 191.160 1.00 69.24  ? 2759 ILE A CA    1 
ATOM   10516 C  C     . ILE A 1 1542 ? 162.179 142.678 191.543 1.00 72.10  ? 2759 ILE A C     1 
ATOM   10517 O  O     . ILE A 1 1542 ? 162.954 142.389 192.458 1.00 73.29  ? 2759 ILE A O     1 
ATOM   10518 C  CB    . ILE A 1 1542 ? 163.268 144.884 191.017 1.00 63.44  ? 2759 ILE A CB    1 
ATOM   10519 C  CG1   . ILE A 1 1542 ? 163.039 146.360 190.716 1.00 66.02  ? 2759 ILE A CG1   1 
ATOM   10520 C  CG2   . ILE A 1 1542 ? 164.112 144.264 189.915 1.00 66.71  ? 2759 ILE A CG2   1 
ATOM   10521 C  CD1   . ILE A 1 1542 ? 164.328 147.141 190.610 1.00 67.62  ? 2759 ILE A CD1   1 
ATOM   10522 N  N     . GLY A 1 1543 ? 161.529 141.760 190.834 1.00 69.37  ? 2760 GLY A N     1 
ATOM   10523 C  CA    . GLY A 1 1543 ? 161.724 140.345 191.080 1.00 71.07  ? 2760 GLY A CA    1 
ATOM   10524 C  C     . GLY A 1 1543 ? 161.280 139.523 189.896 1.00 76.88  ? 2760 GLY A C     1 
ATOM   10525 O  O     . GLY A 1 1543 ? 160.387 139.923 189.143 1.00 78.40  ? 2760 GLY A O     1 
ATOM   10526 N  N     . ALA A 1 1544 ? 161.897 138.353 189.742 1.00 75.78  ? 2761 ALA A N     1 
ATOM   10527 C  CA    . ALA A 1 1544 ? 161.588 137.468 188.630 1.00 72.88  ? 2761 ALA A CA    1 
ATOM   10528 C  C     . ALA A 1 1544 ? 160.182 136.887 188.778 1.00 73.38  ? 2761 ALA A C     1 
ATOM   10529 O  O     . ALA A 1 1544 ? 159.541 136.984 189.828 1.00 74.25  ? 2761 ALA A O     1 
ATOM   10530 C  CB    . ALA A 1 1544 ? 162.618 136.345 188.536 1.00 71.26  ? 2761 ALA A CB    1 
ATOM   10531 N  N     . SER A 1 1545 ? 159.701 136.281 187.696 1.00 67.66  ? 2762 SER A N     1 
ATOM   10532 C  CA    . SER A 1 1545 ? 158.351 135.740 187.673 1.00 66.00  ? 2762 SER A CA    1 
ATOM   10533 C  C     . SER A 1 1545 ? 158.218 134.561 188.631 1.00 63.33  ? 2762 SER A C     1 
ATOM   10534 O  O     . SER A 1 1545 ? 159.149 133.774 188.816 1.00 60.07  ? 2762 SER A O     1 
ATOM   10535 C  CB    . SER A 1 1545 ? 157.972 135.307 186.258 1.00 70.97  ? 2762 SER A CB    1 
ATOM   10536 O  OG    . SER A 1 1545 ? 156.587 135.021 186.170 1.00 74.12  ? 2762 SER A OG    1 
ATOM   10537 N  N     . ARG A 1 1546 ? 157.033 134.456 189.239 1.00 67.97  ? 2763 ARG A N     1 
ATOM   10538 C  CA    . ARG A 1 1546 ? 156.701 133.412 190.215 1.00 65.80  ? 2763 ARG A CA    1 
ATOM   10539 C  C     . ARG A 1 1546 ? 157.677 133.395 191.391 1.00 64.95  ? 2763 ARG A C     1 
ATOM   10540 O  O     . ARG A 1 1546 ? 158.097 132.335 191.857 1.00 61.75  ? 2763 ARG A O     1 
ATOM   10541 C  CB    . ARG A 1 1546 ? 156.618 132.035 189.553 1.00 61.57  ? 2763 ARG A CB    1 
ATOM   10542 C  CG    . ARG A 1 1546 ? 155.316 131.793 188.822 1.00 60.72  ? 2763 ARG A CG    1 
ATOM   10543 C  CD    . ARG A 1 1546 ? 155.261 130.393 188.252 1.00 63.31  ? 2763 ARG A CD    1 
ATOM   10544 N  NE    . ARG A 1 1546 ? 154.581 129.474 189.155 1.00 63.14  ? 2763 ARG A NE    1 
ATOM   10545 C  CZ    . ARG A 1 1546 ? 153.988 128.351 188.772 1.00 65.65  ? 2763 ARG A CZ    1 
ATOM   10546 N  NH1   . ARG A 1 1546 ? 153.961 127.983 187.502 1.00 66.67  ? 2763 ARG A NH1   1 
ATOM   10547 N  NH2   . ARG A 1 1546 ? 153.406 127.581 189.687 1.00 65.97  ? 2763 ARG A NH2   1 
ATOM   10548 N  N     . THR A 1 1547 ? 158.040 134.582 191.874 1.00 66.80  ? 2764 THR A N     1 
ATOM   10549 C  CA    . THR A 1 1547 ? 158.817 134.724 193.097 1.00 64.29  ? 2764 THR A CA    1 
ATOM   10550 C  C     . THR A 1 1547 ? 157.950 135.088 194.297 1.00 63.78  ? 2764 THR A C     1 
ATOM   10551 O  O     . THR A 1 1547 ? 158.486 135.362 195.375 1.00 58.40  ? 2764 THR A O     1 
ATOM   10552 C  CB    . THR A 1 1547 ? 159.919 135.769 192.911 1.00 63.22  ? 2764 THR A CB    1 
ATOM   10553 O  OG1   . THR A 1 1547 ? 159.395 136.899 192.205 1.00 71.02  ? 2764 THR A OG1   1 
ATOM   10554 C  CG2   . THR A 1 1547 ? 161.080 135.183 192.123 1.00 59.12  ? 2764 THR A CG2   1 
ATOM   10555 N  N     . GLY A 1 1548 ? 156.629 135.099 194.133 1.00 65.53  ? 2765 GLY A N     1 
ATOM   10556 C  CA    . GLY A 1 1548 ? 155.720 135.317 195.241 1.00 59.74  ? 2765 GLY A CA    1 
ATOM   10557 C  C     . GLY A 1 1548 ? 155.359 136.756 195.522 1.00 63.62  ? 2765 GLY A C     1 
ATOM   10558 O  O     . GLY A 1 1548 ? 154.833 137.043 196.602 1.00 64.41  ? 2765 GLY A O     1 
ATOM   10559 N  N     . LYS A 1 1549 ? 155.615 137.671 194.585 1.00 67.44  ? 2766 LYS A N     1 
ATOM   10560 C  CA    . LYS A 1 1549 ? 155.456 139.096 194.862 1.00 62.50  ? 2766 LYS A CA    1 
ATOM   10561 C  C     . LYS A 1 1549 ? 153.990 139.477 195.036 1.00 55.84  ? 2766 LYS A C     1 
ATOM   10562 O  O     . LYS A 1 1549 ? 153.618 140.115 196.030 1.00 61.37  ? 2766 LYS A O     1 
ATOM   10563 C  CB    . LYS A 1 1549 ? 156.100 139.904 193.737 1.00 61.87  ? 2766 LYS A CB    1 
ATOM   10564 C  CG    . LYS A 1 1549 ? 157.548 139.517 193.498 1.00 59.70  ? 2766 LYS A CG    1 
ATOM   10565 C  CD    . LYS A 1 1549 ? 158.190 140.298 192.366 1.00 62.62  ? 2766 LYS A CD    1 
ATOM   10566 C  CE    . LYS A 1 1549 ? 157.497 140.028 191.050 1.00 70.38  ? 2766 LYS A CE    1 
ATOM   10567 N  NZ    . LYS A 1 1549 ? 158.194 139.004 190.232 1.00 63.82  ? 2766 LYS A NZ    1 
ATOM   10568 N  N     . THR A 1 1550 ? 153.141 139.078 194.087 1.00 56.73  ? 2767 THR A N     1 
ATOM   10569 C  CA    . THR A 1 1550 ? 151.723 139.414 194.162 1.00 60.51  ? 2767 THR A CA    1 
ATOM   10570 C  C     . THR A 1 1550 ? 151.050 138.724 195.343 1.00 63.81  ? 2767 THR A C     1 
ATOM   10571 O  O     . THR A 1 1550 ? 150.215 139.328 196.027 1.00 64.60  ? 2767 THR A O     1 
ATOM   10572 C  CB    . THR A 1 1550 ? 151.031 139.043 192.849 1.00 63.20  ? 2767 THR A CB    1 
ATOM   10573 O  OG1   . THR A 1 1550 ? 151.665 139.734 191.766 1.00 69.10  ? 2767 THR A OG1   1 
ATOM   10574 C  CG2   . THR A 1 1550 ? 149.560 139.424 192.884 1.00 62.48  ? 2767 THR A CG2   1 
ATOM   10575 N  N     . ILE A 1 1551 ? 151.414 137.468 195.609 1.00 64.04  ? 2768 ILE A N     1 
ATOM   10576 C  CA    . ILE A 1 1551 ? 150.814 136.740 196.723 1.00 63.40  ? 2768 ILE A CA    1 
ATOM   10577 C  C     . ILE A 1 1551 ? 151.246 137.345 198.055 1.00 66.39  ? 2768 ILE A C     1 
ATOM   10578 O  O     . ILE A 1 1551 ? 150.447 137.446 198.993 1.00 69.66  ? 2768 ILE A O     1 
ATOM   10579 C  CB    . ILE A 1 1551 ? 151.167 135.244 196.633 1.00 61.04  ? 2768 ILE A CB    1 
ATOM   10580 C  CG1   . ILE A 1 1551 ? 150.714 134.669 195.290 1.00 66.93  ? 2768 ILE A CG1   1 
ATOM   10581 C  CG2   . ILE A 1 1551 ? 150.519 134.472 197.770 1.00 61.68  ? 2768 ILE A CG2   1 
ATOM   10582 C  CD1   . ILE A 1 1551 ? 149.274 134.984 194.935 1.00 71.35  ? 2768 ILE A CD1   1 
ATOM   10583 N  N     . LEU A 1 1552 ? 152.510 137.768 198.156 1.00 65.21  ? 2769 LEU A N     1 
ATOM   10584 C  CA    . LEU A 1 1552 ? 152.976 138.439 199.367 1.00 65.47  ? 2769 LEU A CA    1 
ATOM   10585 C  C     . LEU A 1 1552 ? 152.260 139.768 199.572 1.00 69.87  ? 2769 LEU A C     1 
ATOM   10586 O  O     . LEU A 1 1552 ? 151.889 140.115 200.701 1.00 71.80  ? 2769 LEU A O     1 
ATOM   10587 C  CB    . LEU A 1 1552 ? 154.488 138.649 199.296 1.00 60.01  ? 2769 LEU A CB    1 
ATOM   10588 N  N     . THR A 1 1553 ? 152.059 140.524 198.487 1.00 66.25  ? 2770 THR A N     1 
ATOM   10589 C  CA    . THR A 1 1553 ? 151.322 141.780 198.579 1.00 57.79  ? 2770 THR A CA    1 
ATOM   10590 C  C     . THR A 1 1553 ? 149.889 141.542 199.036 1.00 63.68  ? 2770 THR A C     1 
ATOM   10591 O  O     . THR A 1 1553 ? 149.371 142.268 199.893 1.00 71.38  ? 2770 THR A O     1 
ATOM   10592 C  CB    . THR A 1 1553 ? 151.346 142.496 197.228 1.00 54.80  ? 2770 THR A CB    1 
ATOM   10593 O  OG1   . THR A 1 1553 ? 152.691 142.869 196.908 1.00 57.10  ? 2770 THR A OG1   1 
ATOM   10594 C  CG2   . THR A 1 1553 ? 150.482 143.745 197.257 1.00 57.38  ? 2770 THR A CG2   1 
ATOM   10595 N  N     . ARG A 1 1554 ? 149.241 140.511 198.489 1.00 64.86  ? 2771 ARG A N     1 
ATOM   10596 C  CA    . ARG A 1 1554 ? 147.876 140.189 198.891 1.00 74.62  ? 2771 ARG A CA    1 
ATOM   10597 C  C     . ARG A 1 1554 ? 147.815 139.747 200.349 1.00 76.59  ? 2771 ARG A C     1 
ATOM   10598 O  O     . ARG A 1 1554 ? 146.874 140.101 201.068 1.00 79.76  ? 2771 ARG A O     1 
ATOM   10599 C  CB    . ARG A 1 1554 ? 147.301 139.111 197.973 1.00 77.53  ? 2771 ARG A CB    1 
ATOM   10600 C  CG    . ARG A 1 1554 ? 147.050 139.589 196.553 1.00 75.53  ? 2771 ARG A CG    1 
ATOM   10601 C  CD    . ARG A 1 1554 ? 145.572 139.596 196.220 1.00 83.05  ? 2771 ARG A CD    1 
ATOM   10602 N  NE    . ARG A 1 1554 ? 144.977 138.272 196.344 1.00 87.89  ? 2771 ARG A NE    1 
ATOM   10603 C  CZ    . ARG A 1 1554 ? 144.777 137.446 195.327 1.00 90.72  ? 2771 ARG A CZ    1 
ATOM   10604 N  NH1   . ARG A 1 1554 ? 145.110 137.778 194.091 1.00 89.24  ? 2771 ARG A NH1   1 
ATOM   10605 N  NH2   . ARG A 1 1554 ? 144.226 136.258 195.556 1.00 92.98  ? 2771 ARG A NH2   1 
ATOM   10606 N  N     . PHE A 1 1555 ? 148.814 138.987 200.808 1.00 75.63  ? 2772 PHE A N     1 
ATOM   10607 C  CA    . PHE A 1 1555 ? 148.845 138.559 202.204 1.00 79.73  ? 2772 PHE A CA    1 
ATOM   10608 C  C     . PHE A 1 1555 ? 149.018 139.742 203.147 1.00 80.85  ? 2772 PHE A C     1 
ATOM   10609 O  O     . PHE A 1 1555 ? 148.341 139.824 204.180 1.00 81.28  ? 2772 PHE A O     1 
ATOM   10610 C  CB    . PHE A 1 1555 ? 149.966 137.543 202.418 1.00 80.06  ? 2772 PHE A CB    1 
ATOM   10611 C  CG    . PHE A 1 1555 ? 150.167 137.153 203.856 1.00 83.29  ? 2772 PHE A CG    1 
ATOM   10612 C  CD1   . PHE A 1 1555 ? 149.097 136.742 204.634 1.00 84.01  ? 2772 PHE A CD1   1 
ATOM   10613 C  CD2   . PHE A 1 1555 ? 151.426 137.207 204.430 1.00 85.22  ? 2772 PHE A CD2   1 
ATOM   10614 C  CE1   . PHE A 1 1555 ? 149.281 136.386 205.955 1.00 91.10  ? 2772 PHE A CE1   1 
ATOM   10615 C  CE2   . PHE A 1 1555 ? 151.616 136.852 205.752 1.00 89.37  ? 2772 PHE A CE2   1 
ATOM   10616 C  CZ    . PHE A 1 1555 ? 150.541 136.442 206.515 1.00 94.92  ? 2772 PHE A CZ    1 
ATOM   10617 N  N     . VAL A 1 1556 ? 149.921 140.666 202.811 1.00 80.06  ? 2773 VAL A N     1 
ATOM   10618 C  CA    . VAL A 1 1556 ? 150.131 141.842 203.652 1.00 75.77  ? 2773 VAL A CA    1 
ATOM   10619 C  C     . VAL A 1 1556 ? 148.885 142.719 203.668 1.00 69.90  ? 2773 VAL A C     1 
ATOM   10620 O  O     . VAL A 1 1556 ? 148.479 143.225 204.723 1.00 69.78  ? 2773 VAL A O     1 
ATOM   10621 C  CB    . VAL A 1 1556 ? 151.376 142.613 203.178 1.00 67.48  ? 2773 VAL A CB    1 
ATOM   10622 C  CG1   . VAL A 1 1556 ? 151.468 143.964 203.862 1.00 67.55  ? 2773 VAL A CG1   1 
ATOM   10623 C  CG2   . VAL A 1 1556 ? 152.620 141.796 203.462 1.00 58.52  ? 2773 VAL A CG2   1 
ATOM   10624 N  N     . ALA A 1 1557 ? 148.246 142.896 202.509 1.00 68.50  ? 2774 ALA A N     1 
ATOM   10625 C  CA    . ALA A 1 1557 ? 147.021 143.683 202.449 1.00 77.22  ? 2774 ALA A CA    1 
ATOM   10626 C  C     . ALA A 1 1557 ? 145.882 143.026 203.219 1.00 80.56  ? 2774 ALA A C     1 
ATOM   10627 O  O     . ALA A 1 1557 ? 145.047 143.726 203.803 1.00 83.38  ? 2774 ALA A O     1 
ATOM   10628 C  CB    . ALA A 1 1557 ? 146.620 143.908 200.994 1.00 79.90  ? 2774 ALA A CB    1 
ATOM   10629 N  N     . TRP A 1 1558 ? 145.823 141.693 203.227 1.00 77.56  ? 2775 TRP A N     1 
ATOM   10630 C  CA    . TRP A 1 1558 ? 144.816 141.002 204.023 1.00 83.15  ? 2775 TRP A CA    1 
ATOM   10631 C  C     . TRP A 1 1558 ? 145.097 141.145 205.513 1.00 83.85  ? 2775 TRP A C     1 
ATOM   10632 O  O     . TRP A 1 1558 ? 144.169 141.303 206.314 1.00 87.11  ? 2775 TRP A O     1 
ATOM   10633 C  CB    . TRP A 1 1558 ? 144.761 139.527 203.630 1.00 84.53  ? 2775 TRP A CB    1 
ATOM   10634 C  CG    . TRP A 1 1558 ? 143.778 138.731 204.428 1.00 86.25  ? 2775 TRP A CG    1 
ATOM   10635 C  CD1   . TRP A 1 1558 ? 142.431 138.661 204.234 1.00 87.03  ? 2775 TRP A CD1   1 
ATOM   10636 C  CD2   . TRP A 1 1558 ? 144.066 137.896 205.555 1.00 87.20  ? 2775 TRP A CD2   1 
ATOM   10637 N  NE1   . TRP A 1 1558 ? 141.861 137.829 205.167 1.00 90.74  ? 2775 TRP A NE1   1 
ATOM   10638 C  CE2   . TRP A 1 1558 ? 142.844 137.347 205.990 1.00 89.41  ? 2775 TRP A CE2   1 
ATOM   10639 C  CE3   . TRP A 1 1558 ? 145.238 137.558 206.237 1.00 88.02  ? 2775 TRP A CE3   1 
ATOM   10640 C  CZ2   . TRP A 1 1558 ? 142.761 136.479 207.075 1.00 91.26  ? 2775 TRP A CZ2   1 
ATOM   10641 C  CZ3   . TRP A 1 1558 ? 145.154 136.697 207.314 1.00 92.07  ? 2775 TRP A CZ3   1 
ATOM   10642 C  CH2   . TRP A 1 1558 ? 143.924 136.167 207.723 1.00 94.01  ? 2775 TRP A CH2   1 
ATOM   10643 N  N     . LEU A 1 1559 ? 146.373 141.087 205.902 1.00 81.40  ? 2776 LEU A N     1 
ATOM   10644 C  CA    . LEU A 1 1559 ? 146.719 141.178 207.316 1.00 81.28  ? 2776 LEU A CA    1 
ATOM   10645 C  C     . LEU A 1 1559 ? 146.513 142.586 207.858 1.00 77.81  ? 2776 LEU A C     1 
ATOM   10646 O  O     . LEU A 1 1559 ? 146.125 142.750 209.020 1.00 76.56  ? 2776 LEU A O     1 
ATOM   10647 C  CB    . LEU A 1 1559 ? 148.164 140.729 207.530 1.00 80.70  ? 2776 LEU A CB    1 
ATOM   10648 C  CG    . LEU A 1 1559 ? 148.618 140.496 208.973 1.00 83.48  ? 2776 LEU A CG    1 
ATOM   10649 C  CD1   . LEU A 1 1559 ? 147.541 139.790 209.785 1.00 84.23  ? 2776 LEU A CD1   1 
ATOM   10650 C  CD2   . LEU A 1 1559 ? 149.916 139.706 208.998 1.00 88.77  ? 2776 LEU A CD2   1 
ATOM   10651 N  N     . ASN A 1 1560 ? 146.760 143.608 207.043 1.00 78.50  ? 2777 ASN A N     1 
ATOM   10652 C  CA    . ASN A 1 1560 ? 146.568 144.989 207.461 1.00 76.41  ? 2777 ASN A CA    1 
ATOM   10653 C  C     . ASN A 1 1560 ? 145.150 145.490 207.221 1.00 78.76  ? 2777 ASN A C     1 
ATOM   10654 O  O     . ASN A 1 1560 ? 144.875 146.668 207.469 1.00 79.08  ? 2777 ASN A O     1 
ATOM   10655 C  CB    . ASN A 1 1560 ? 147.566 145.902 206.744 1.00 68.13  ? 2777 ASN A CB    1 
ATOM   10656 C  CG    . ASN A 1 1560 ? 148.978 145.740 207.263 1.00 59.11  ? 2777 ASN A CG    1 
ATOM   10657 O  OD1   . ASN A 1 1560 ? 149.208 145.067 208.267 1.00 60.22  ? 2777 ASN A OD1   1 
ATOM   10658 N  ND2   . ASN A 1 1560 ? 149.934 146.357 206.581 1.00 57.79  ? 2777 ASN A ND2   1 
ATOM   10659 N  N     . GLY A 1 1561 ? 144.250 144.633 206.746 1.00 77.05  ? 2778 GLY A N     1 
ATOM   10660 C  CA    . GLY A 1 1561 ? 142.866 145.014 206.558 1.00 82.13  ? 2778 GLY A CA    1 
ATOM   10661 C  C     . GLY A 1 1561 ? 142.559 145.736 205.267 1.00 86.54  ? 2778 GLY A C     1 
ATOM   10662 O  O     . GLY A 1 1561 ? 141.437 146.231 205.108 1.00 94.33  ? 2778 GLY A O     1 
ATOM   10663 N  N     . LEU A 1 1562 ? 143.512 145.819 204.344 1.00 80.86  ? 2779 LEU A N     1 
ATOM   10664 C  CA    . LEU A 1 1562 ? 143.264 146.468 203.067 1.00 84.25  ? 2779 LEU A CA    1 
ATOM   10665 C  C     . LEU A 1 1562 ? 142.322 145.627 202.210 1.00 89.81  ? 2779 LEU A C     1 
ATOM   10666 O  O     . LEU A 1 1562 ? 142.227 144.405 202.356 1.00 85.03  ? 2779 LEU A O     1 
ATOM   10667 C  CB    . LEU A 1 1562 ? 144.576 146.702 202.315 1.00 81.79  ? 2779 LEU A CB    1 
ATOM   10668 C  CG    . LEU A 1 1562 ? 145.411 147.946 202.626 1.00 80.13  ? 2779 LEU A CG    1 
ATOM   10669 C  CD1   . LEU A 1 1562 ? 146.092 147.852 203.981 1.00 77.20  ? 2779 LEU A CD1   1 
ATOM   10670 C  CD2   . LEU A 1 1562 ? 146.438 148.167 201.529 1.00 80.54  ? 2779 LEU A CD2   1 
ATOM   10671 N  N     . LYS A 1 1563 ? 141.615 146.300 201.308 1.00 95.76  ? 2780 LYS A N     1 
ATOM   10672 C  CA    . LYS A 1 1563 ? 140.758 145.636 200.338 1.00 95.81  ? 2780 LYS A CA    1 
ATOM   10673 C  C     . LYS A 1 1563 ? 141.467 145.563 198.991 1.00 97.34  ? 2780 LYS A C     1 
ATOM   10674 O  O     . LYS A 1 1563 ? 142.330 146.386 198.676 1.00 96.74  ? 2780 LYS A O     1 
ATOM   10675 C  CB    . LYS A 1 1563 ? 139.411 146.354 200.207 1.00 94.00  ? 2780 LYS A CB    1 
ATOM   10676 C  CG    . LYS A 1 1563 ? 139.401 147.570 199.296 1.00 96.36  ? 2780 LYS A CG    1 
ATOM   10677 C  CD    . LYS A 1 1563 ? 137.971 147.993 198.995 1.00 101.00 ? 2780 LYS A CD    1 
ATOM   10678 C  CE    . LYS A 1 1563 ? 137.917 149.326 198.270 1.00 106.65 ? 2780 LYS A CE    1 
ATOM   10679 N  NZ    . LYS A 1 1563 ? 138.564 149.258 196.934 1.00 109.18 ? 2780 LYS A NZ    1 
ATOM   10680 N  N     . ILE A 1 1564 ? 141.106 144.553 198.203 1.00 98.24  ? 2781 ILE A N     1 
ATOM   10681 C  CA    . ILE A 1 1564 ? 141.827 144.202 196.985 1.00 97.99  ? 2781 ILE A CA    1 
ATOM   10682 C  C     . ILE A 1 1564 ? 140.977 144.562 195.777 1.00 98.66  ? 2781 ILE A C     1 
ATOM   10683 O  O     . ILE A 1 1564 ? 139.824 144.128 195.668 1.00 102.98 ? 2781 ILE A O     1 
ATOM   10684 C  CB    . ILE A 1 1564 ? 142.189 142.707 196.956 1.00 96.03  ? 2781 ILE A CB    1 
ATOM   10685 C  CG1   . ILE A 1 1564 ? 142.623 142.227 198.341 1.00 91.78  ? 2781 ILE A CG1   1 
ATOM   10686 C  CG2   . ILE A 1 1564 ? 143.277 142.451 195.927 1.00 93.25  ? 2781 ILE A CG2   1 
ATOM   10687 C  CD1   . ILE A 1 1564 ? 143.937 142.800 198.797 1.00 90.66  ? 2781 ILE A CD1   1 
ATOM   10688 N  N     . VAL A 1 1565 ? 141.547 145.354 194.871 1.00 94.93  ? 2782 VAL A N     1 
ATOM   10689 C  CA    . VAL A 1 1565 ? 140.976 145.589 193.551 1.00 98.18  ? 2782 VAL A CA    1 
ATOM   10690 C  C     . VAL A 1 1565 ? 142.056 145.327 192.507 1.00 97.56  ? 2782 VAL A C     1 
ATOM   10691 O  O     . VAL A 1 1565 ? 143.201 145.769 192.659 1.00 96.90  ? 2782 VAL A O     1 
ATOM   10692 C  CB    . VAL A 1 1565 ? 140.377 147.006 193.409 1.00 100.42 ? 2782 VAL A CB    1 
ATOM   10693 C  CG1   . VAL A 1 1565 ? 139.213 147.184 194.367 1.00 103.61 ? 2782 VAL A CG1   1 
ATOM   10694 C  CG2   . VAL A 1 1565 ? 141.414 148.086 193.687 1.00 94.39  ? 2782 VAL A CG2   1 
ATOM   10695 N  N     . GLN A 1 1566 ? 141.709 144.556 191.483 1.00 100.89 ? 2783 GLN A N     1 
ATOM   10696 C  CA    . GLN A 1 1566 ? 142.619 144.249 190.381 1.00 99.03  ? 2783 GLN A CA    1 
ATOM   10697 C  C     . GLN A 1 1566 ? 141.915 144.586 189.074 1.00 99.51  ? 2783 GLN A C     1 
ATOM   10698 O  O     . GLN A 1 1566 ? 140.971 143.868 188.684 1.00 100.81 ? 2783 GLN A O     1 
ATOM   10699 C  CB    . GLN A 1 1566 ? 143.055 142.786 190.409 1.00 96.97  ? 2783 GLN A CB    1 
ATOM   10700 C  CG    . GLN A 1 1566 ? 143.533 142.299 191.773 1.00 94.58  ? 2783 GLN A CG    1 
ATOM   10701 C  CD    . GLN A 1 1566 ? 143.972 140.848 191.759 1.00 94.41  ? 2783 GLN A CD    1 
ATOM   10702 O  OE1   . GLN A 1 1566 ? 144.956 140.492 191.111 1.00 88.64  ? 2783 GLN A OE1   1 
ATOM   10703 N  NE2   . GLN A 1 1566 ? 143.246 140.002 192.481 1.00 95.45  ? 2783 GLN A NE2   1 
ATOM   10704 N  N     . PRO A 1 1567 ? 142.316 145.657 188.389 1.00 102.53 ? 2784 PRO A N     1 
ATOM   10705 C  CA    . PRO A 1 1567 ? 141.611 146.068 187.168 1.00 110.65 ? 2784 PRO A CA    1 
ATOM   10706 C  C     . PRO A 1 1567 ? 141.711 145.030 186.059 1.00 110.04 ? 2784 PRO A C     1 
ATOM   10707 O  O     . PRO A 1 1567 ? 142.732 144.359 185.896 1.00 108.05 ? 2784 PRO A O     1 
ATOM   10708 C  CB    . PRO A 1 1567 ? 142.316 147.371 186.773 1.00 113.95 ? 2784 PRO A CB    1 
ATOM   10709 C  CG    . PRO A 1 1567 ? 142.959 147.857 188.027 1.00 109.34 ? 2784 PRO A CG    1 
ATOM   10710 C  CD    . PRO A 1 1567 ? 143.348 146.628 188.785 1.00 103.05 ? 2784 PRO A CD    1 
ATOM   10711 N  N     . LYS A 1 1568 ? 140.627 144.908 185.292 1.00 112.25 ? 2785 LYS A N     1 
ATOM   10712 C  CA    . LYS A 1 1568 ? 140.589 144.034 184.120 1.00 114.99 ? 2785 LYS A CA    1 
ATOM   10713 C  C     . LYS A 1 1568 ? 141.054 144.826 182.897 1.00 116.12 ? 2785 LYS A C     1 
ATOM   10714 O  O     . LYS A 1 1568 ? 140.276 145.237 182.033 1.00 118.47 ? 2785 LYS A O     1 
ATOM   10715 C  CB    . LYS A 1 1568 ? 139.190 143.459 183.931 1.00 112.52 ? 2785 LYS A CB    1 
ATOM   10716 C  CG    . LYS A 1 1568 ? 139.090 142.359 182.881 1.00 113.17 ? 2785 LYS A CG    1 
ATOM   10717 C  CD    . LYS A 1 1568 ? 140.093 141.247 183.131 1.00 113.89 ? 2785 LYS A CD    1 
ATOM   10718 C  CE    . LYS A 1 1568 ? 139.546 140.215 184.100 1.00 116.27 ? 2785 LYS A CE    1 
ATOM   10719 N  NZ    . LYS A 1 1568 ? 140.430 139.021 184.193 1.00 111.78 ? 2785 LYS A NZ    1 
ATOM   10720 N  N     . ILE A 1 1569 ? 142.363 145.049 182.847 1.00 113.28 ? 2786 ILE A N     1 
ATOM   10721 C  CA    . ILE A 1 1569 ? 142.964 145.818 181.766 1.00 116.39 ? 2786 ILE A CA    1 
ATOM   10722 C  C     . ILE A 1 1569 ? 143.219 144.926 180.557 1.00 119.42 ? 2786 ILE A C     1 
ATOM   10723 O  O     . ILE A 1 1569 ? 142.334 144.194 180.113 1.00 119.96 ? 2786 ILE A O     1 
ATOM   10724 C  CB    . ILE A 1 1569 ? 144.264 146.497 182.226 1.00 110.80 ? 2786 ILE A CB    1 
ATOM   10725 C  CG1   . ILE A 1 1569 ? 143.965 147.551 183.293 1.00 109.82 ? 2786 ILE A CG1   1 
ATOM   10726 C  CG2   . ILE A 1 1569 ? 144.978 147.129 181.044 1.00 108.87 ? 2786 ILE A CG2   1 
ATOM   10727 C  CD1   . ILE A 1 1569 ? 143.033 148.645 182.826 1.00 115.57 ? 2786 ILE A CD1   1 
ATOM   10728 N  N     . ARG A 1 1571 ? 142.221 143.917 177.440 1.00 126.45 ? 2788 ARG A N     1 
ATOM   10729 C  CA    . ARG A 1 1571 ? 142.012 144.144 176.016 1.00 134.89 ? 2788 ARG A CA    1 
ATOM   10730 C  C     . ARG A 1 1571 ? 140.738 144.947 175.771 1.00 136.61 ? 2788 ARG A C     1 
ATOM   10731 O  O     . ARG A 1 1571 ? 139.744 144.771 176.479 1.00 138.12 ? 2788 ARG A O     1 
ATOM   10732 C  CB    . ARG A 1 1571 ? 141.949 142.814 175.263 1.00 132.32 ? 2788 ARG A CB    1 
ATOM   10733 N  N     . HIS A 1 1572 ? 140.794 145.825 174.764 1.00 132.59 ? 2789 HIS A N     1 
ATOM   10734 C  CA    . HIS A 1 1572 ? 139.677 146.693 174.376 1.00 133.63 ? 2789 HIS A CA    1 
ATOM   10735 C  C     . HIS A 1 1572 ? 139.205 147.561 175.542 1.00 137.00 ? 2789 HIS A C     1 
ATOM   10736 O  O     . HIS A 1 1572 ? 138.011 147.814 175.710 1.00 137.84 ? 2789 HIS A O     1 
ATOM   10737 C  CB    . HIS A 1 1572 ? 138.515 145.881 173.794 1.00 131.66 ? 2789 HIS A CB    1 
ATOM   10738 N  N     . SER A 1 1573 ? 140.154 148.022 176.352 1.00 136.10 ? 2790 SER A N     1 
ATOM   10739 C  CA    . SER A 1 1573 ? 139.880 148.913 177.469 1.00 133.57 ? 2790 SER A CA    1 
ATOM   10740 C  C     . SER A 1 1573 ? 140.745 150.159 177.339 1.00 132.62 ? 2790 SER A C     1 
ATOM   10741 O  O     . SER A 1 1573 ? 141.874 150.099 176.842 1.00 131.82 ? 2790 SER A O     1 
ATOM   10742 C  CB    . SER A 1 1573 ? 140.144 148.222 178.812 1.00 128.97 ? 2790 SER A CB    1 
ATOM   10743 O  OG    . SER A 1 1573 ? 139.151 147.250 179.086 1.00 126.18 ? 2790 SER A OG    1 
ATOM   10744 N  N     . ASN A 1 1574 ? 140.211 151.293 177.786 1.00 131.30 ? 2791 ASN A N     1 
ATOM   10745 C  CA    . ASN A 1 1574 ? 140.868 152.573 177.559 1.00 128.86 ? 2791 ASN A CA    1 
ATOM   10746 C  C     . ASN A 1 1574 ? 140.753 153.434 178.814 1.00 124.10 ? 2791 ASN A C     1 
ATOM   10747 O  O     . ASN A 1 1574 ? 140.327 152.977 179.883 1.00 123.72 ? 2791 ASN A O     1 
ATOM   10748 C  CB    . ASN A 1 1574 ? 140.276 153.270 176.326 1.00 129.62 ? 2791 ASN A CB    1 
ATOM   10749 C  CG    . ASN A 1 1574 ? 141.304 154.089 175.568 1.00 130.91 ? 2791 ASN A CG    1 
ATOM   10750 O  OD1   . ASN A 1 1574 ? 142.398 154.348 176.068 1.00 126.60 ? 2791 ASN A OD1   1 
ATOM   10751 N  ND2   . ASN A 1 1574 ? 140.955 154.502 174.356 1.00 136.39 ? 2791 ASN A ND2   1 
ATOM   10752 N  N     . LEU A 1 1575 ? 141.145 154.704 178.658 1.00 122.85 ? 2792 LEU A N     1 
ATOM   10753 C  CA    . LEU A 1 1575 ? 141.197 155.633 179.780 1.00 122.81 ? 2792 LEU A CA    1 
ATOM   10754 C  C     . LEU A 1 1575 ? 139.816 155.916 180.351 1.00 122.19 ? 2792 LEU A C     1 
ATOM   10755 O  O     . LEU A 1 1575 ? 139.704 156.221 181.539 1.00 122.66 ? 2792 LEU A O     1 
ATOM   10756 C  CB    . LEU A 1 1575 ? 141.867 156.943 179.357 1.00 122.53 ? 2792 LEU A CB    1 
ATOM   10757 C  CG    . LEU A 1 1575 ? 143.396 157.068 179.424 1.00 115.42 ? 2792 LEU A CG    1 
ATOM   10758 C  CD1   . LEU A 1 1575 ? 143.889 156.889 180.855 1.00 116.18 ? 2792 LEU A CD1   1 
ATOM   10759 C  CD2   . LEU A 1 1575 ? 144.111 156.110 178.477 1.00 110.56 ? 2792 LEU A CD2   1 
ATOM   10760 N  N     . SER A 1 1576 ? 138.761 155.808 179.540 1.00 122.75 ? 2793 SER A N     1 
ATOM   10761 C  CA    . SER A 1 1576 ? 137.410 156.024 180.051 1.00 122.19 ? 2793 SER A CA    1 
ATOM   10762 C  C     . SER A 1 1576 ? 137.045 154.978 181.100 1.00 122.73 ? 2793 SER A C     1 
ATOM   10763 O  O     . SER A 1 1576 ? 136.632 155.316 182.216 1.00 122.01 ? 2793 SER A O     1 
ATOM   10764 C  CB    . SER A 1 1576 ? 136.405 156.006 178.899 1.00 117.35 ? 2793 SER A CB    1 
ATOM   10765 O  OG    . SER A 1 1576 ? 136.734 156.974 177.918 1.00 115.73 ? 2793 SER A OG    1 
ATOM   10766 N  N     . ASP A 1 1577 ? 137.216 153.696 180.764 1.00 123.27 ? 2794 ASP A N     1 
ATOM   10767 C  CA    . ASP A 1 1577 ? 136.930 152.631 181.720 1.00 119.96 ? 2794 ASP A CA    1 
ATOM   10768 C  C     . ASP A 1 1577 ? 137.902 152.664 182.894 1.00 121.37 ? 2794 ASP A C     1 
ATOM   10769 O  O     . ASP A 1 1577 ? 137.506 152.416 184.041 1.00 121.63 ? 2794 ASP A O     1 
ATOM   10770 C  CB    . ASP A 1 1577 ? 136.977 151.272 181.022 1.00 116.46 ? 2794 ASP A CB    1 
ATOM   10771 N  N     . PHE A 1 1578 ? 139.177 152.969 182.627 1.00 122.73 ? 2795 PHE A N     1 
ATOM   10772 C  CA    . PHE A 1 1578 ? 140.160 153.037 183.706 1.00 123.61 ? 2795 PHE A CA    1 
ATOM   10773 C  C     . PHE A 1 1578 ? 139.811 154.137 184.703 1.00 123.52 ? 2795 PHE A C     1 
ATOM   10774 O  O     . PHE A 1 1578 ? 139.865 153.928 185.921 1.00 122.45 ? 2795 PHE A O     1 
ATOM   10775 C  CB    . PHE A 1 1578 ? 141.559 153.255 183.130 1.00 118.67 ? 2795 PHE A CB    1 
ATOM   10776 C  CG    . PHE A 1 1578 ? 142.666 152.930 184.091 1.00 117.94 ? 2795 PHE A CG    1 
ATOM   10777 C  CD1   . PHE A 1 1578 ? 142.673 151.725 184.776 1.00 120.23 ? 2795 PHE A CD1   1 
ATOM   10778 C  CD2   . PHE A 1 1578 ? 143.695 153.828 184.314 1.00 114.32 ? 2795 PHE A CD2   1 
ATOM   10779 C  CE1   . PHE A 1 1578 ? 143.691 151.422 185.662 1.00 116.37 ? 2795 PHE A CE1   1 
ATOM   10780 C  CE2   . PHE A 1 1578 ? 144.718 153.529 185.196 1.00 112.52 ? 2795 PHE A CE2   1 
ATOM   10781 C  CZ    . PHE A 1 1578 ? 144.714 152.326 185.873 1.00 111.76 ? 2795 PHE A CZ    1 
ATOM   10782 N  N     . ASP A 1 1579 ? 139.424 155.312 184.203 1.00 123.66 ? 2796 ASP A N     1 
ATOM   10783 C  CA    . ASP A 1 1579 ? 139.049 156.407 185.083 1.00 122.50 ? 2796 ASP A CA    1 
ATOM   10784 C  C     . ASP A 1 1579 ? 137.719 156.146 185.769 1.00 124.22 ? 2796 ASP A C     1 
ATOM   10785 O  O     . ASP A 1 1579 ? 137.514 156.611 186.889 1.00 125.58 ? 2796 ASP A O     1 
ATOM   10786 C  CB    . ASP A 1 1579 ? 139.001 157.719 184.302 1.00 122.70 ? 2796 ASP A CB    1 
ATOM   10787 C  CG    . ASP A 1 1579 ? 140.379 158.211 183.906 1.00 119.81 ? 2796 ASP A CG    1 
ATOM   10788 O  OD1   . ASP A 1 1579 ? 141.349 157.919 184.638 1.00 113.66 ? 2796 ASP A OD1   1 
ATOM   10789 O  OD2   . ASP A 1 1579 ? 140.493 158.889 182.863 1.00 120.89 ? 2796 ASP A OD2   1 
ATOM   10790 N  N     . MET A 1 1580 ? 136.810 155.404 185.131 1.00 123.76 ? 2797 MET A N     1 
ATOM   10791 C  CA    . MET A 1 1580 ? 135.579 155.011 185.814 1.00 123.43 ? 2797 MET A CA    1 
ATOM   10792 C  C     . MET A 1 1580 ? 135.880 154.108 187.006 1.00 125.49 ? 2797 MET A C     1 
ATOM   10793 O  O     . MET A 1 1580 ? 135.342 154.303 188.104 1.00 126.69 ? 2797 MET A O     1 
ATOM   10794 C  CB    . MET A 1 1580 ? 134.635 154.317 184.832 1.00 121.74 ? 2797 MET A CB    1 
ATOM   10795 N  N     . ILE A 1 1581 ? 136.762 153.122 186.807 1.00 124.84 ? 2798 ILE A N     1 
ATOM   10796 C  CA    . ILE A 1 1581 ? 137.146 152.226 187.898 1.00 124.58 ? 2798 ILE A CA    1 
ATOM   10797 C  C     . ILE A 1 1581 ? 137.857 153.000 189.003 1.00 125.81 ? 2798 ILE A C     1 
ATOM   10798 O  O     . ILE A 1 1581 ? 137.586 152.801 190.196 1.00 124.44 ? 2798 ILE A O     1 
ATOM   10799 C  CB    . ILE A 1 1581 ? 138.014 151.073 187.359 1.00 122.72 ? 2798 ILE A CB    1 
ATOM   10800 C  CG1   . ILE A 1 1581 ? 137.202 150.192 186.409 1.00 122.89 ? 2798 ILE A CG1   1 
ATOM   10801 C  CG2   . ILE A 1 1581 ? 138.579 150.239 188.500 1.00 120.63 ? 2798 ILE A CG2   1 
ATOM   10802 C  CD1   . ILE A 1 1581 ? 138.049 149.298 185.533 1.00 120.48 ? 2798 ILE A CD1   1 
ATOM   10803 N  N     . LEU A 1 1582 ? 138.765 153.904 188.625 1.00 126.64 ? 2799 LEU A N     1 
ATOM   10804 C  CA    . LEU A 1 1582 ? 139.491 154.689 189.620 1.00 126.47 ? 2799 LEU A CA    1 
ATOM   10805 C  C     . LEU A 1 1582 ? 138.568 155.645 190.366 1.00 128.40 ? 2799 LEU A C     1 
ATOM   10806 O  O     . LEU A 1 1582 ? 138.749 155.874 191.566 1.00 127.12 ? 2799 LEU A O     1 
ATOM   10807 C  CB    . LEU A 1 1582 ? 140.630 155.454 188.951 1.00 121.83 ? 2799 LEU A CB    1 
ATOM   10808 C  CG    . LEU A 1 1582 ? 141.792 154.585 188.475 1.00 116.31 ? 2799 LEU A CG    1 
ATOM   10809 C  CD1   . LEU A 1 1582 ? 142.624 155.344 187.471 1.00 115.27 ? 2799 LEU A CD1   1 
ATOM   10810 C  CD2   . LEU A 1 1582 ? 142.641 154.142 189.652 1.00 112.65 ? 2799 LEU A CD2   1 
ATOM   10811 N  N     . LYS A 1 1583 ? 137.580 156.218 189.675 1.00 130.31 ? 2800 LYS A N     1 
ATOM   10812 C  CA    . LYS A 1 1583 ? 136.615 157.092 190.330 1.00 131.48 ? 2800 LYS A CA    1 
ATOM   10813 C  C     . LYS A 1 1583 ? 135.758 156.318 191.320 1.00 131.91 ? 2800 LYS A C     1 
ATOM   10814 O  O     . LYS A 1 1583 ? 135.490 156.804 192.424 1.00 131.28 ? 2800 LYS A O     1 
ATOM   10815 C  CB    . LYS A 1 1583 ? 135.741 157.784 189.284 1.00 130.80 ? 2800 LYS A CB    1 
ATOM   10816 C  CG    . LYS A 1 1583 ? 136.342 159.065 188.724 1.00 128.27 ? 2800 LYS A CG    1 
ATOM   10817 C  CD    . LYS A 1 1583 ? 135.756 159.412 187.363 1.00 126.11 ? 2800 LYS A CD    1 
ATOM   10818 C  CE    . LYS A 1 1583 ? 134.240 159.485 187.409 1.00 125.99 ? 2800 LYS A CE    1 
ATOM   10819 N  NZ    . LYS A 1 1583 ? 133.640 159.420 186.048 1.00 132.20 ? 2800 LYS A NZ    1 
ATOM   10820 N  N     . LYS A 1 1584 ? 135.333 155.105 190.950 1.00 131.72 ? 2801 LYS A N     1 
ATOM   10821 C  CA    . LYS A 1 1584 ? 134.591 154.270 191.891 1.00 132.73 ? 2801 LYS A CA    1 
ATOM   10822 C  C     . LYS A 1 1584 ? 135.442 153.913 193.105 1.00 133.01 ? 2801 LYS A C     1 
ATOM   10823 O  O     . LYS A 1 1584 ? 134.967 153.974 194.248 1.00 133.54 ? 2801 LYS A O     1 
ATOM   10824 C  CB    . LYS A 1 1584 ? 134.096 153.004 191.191 1.00 130.38 ? 2801 LYS A CB    1 
ATOM   10825 N  N     . ALA A 1 1585 ? 136.711 153.561 192.876 1.00 130.79 ? 2802 ALA A N     1 
ATOM   10826 C  CA    . ALA A 1 1585 ? 137.597 153.199 193.979 1.00 131.79 ? 2802 ALA A CA    1 
ATOM   10827 C  C     . ALA A 1 1585 ? 137.859 154.384 194.904 1.00 132.09 ? 2802 ALA A C     1 
ATOM   10828 O  O     . ALA A 1 1585 ? 137.822 154.238 196.131 1.00 129.41 ? 2802 ALA A O     1 
ATOM   10829 C  CB    . ALA A 1 1585 ? 138.912 152.645 193.433 1.00 130.10 ? 2802 ALA A CB    1 
ATOM   10830 N  N     . ILE A 1 1586 ? 138.118 155.565 194.337 1.00 132.85 ? 2803 ILE A N     1 
ATOM   10831 C  CA    . ILE A 1 1586 ? 138.395 156.737 195.161 1.00 131.70 ? 2803 ILE A CA    1 
ATOM   10832 C  C     . ILE A 1 1586 ? 137.130 157.219 195.866 1.00 131.46 ? 2803 ILE A C     1 
ATOM   10833 O  O     . ILE A 1 1586 ? 137.203 157.745 196.982 1.00 129.22 ? 2803 ILE A O     1 
ATOM   10834 C  CB    . ILE A 1 1586 ? 139.065 157.843 194.317 1.00 127.92 ? 2803 ILE A CB    1 
ATOM   10835 C  CG1   . ILE A 1 1586 ? 139.852 158.804 195.212 1.00 120.38 ? 2803 ILE A CG1   1 
ATOM   10836 C  CG2   . ILE A 1 1586 ? 138.061 158.595 193.454 1.00 126.57 ? 2803 ILE A CG2   1 
ATOM   10837 C  CD1   . ILE A 1 1586 ? 141.192 158.265 195.652 1.00 114.06 ? 2803 ILE A CD1   1 
ATOM   10838 N  N     . SER A 1 1587 ? 135.953 157.021 195.260 1.00 133.58 ? 2804 SER A N     1 
ATOM   10839 C  CA    . SER A 1 1587 ? 134.709 157.357 195.942 1.00 134.23 ? 2804 SER A CA    1 
ATOM   10840 C  C     . SER A 1 1587 ? 134.468 156.429 197.123 1.00 131.77 ? 2804 SER A C     1 
ATOM   10841 O  O     . SER A 1 1587 ? 134.045 156.878 198.195 1.00 128.52 ? 2804 SER A O     1 
ATOM   10842 C  CB    . SER A 1 1587 ? 133.541 157.295 194.959 1.00 136.93 ? 2804 SER A CB    1 
ATOM   10843 O  OG    . SER A 1 1587 ? 133.693 158.255 193.928 1.00 136.45 ? 2804 SER A OG    1 
ATOM   10844 N  N     . ASP A 1 1588 ? 134.741 155.132 196.946 1.00 133.71 ? 2805 ASP A N     1 
ATOM   10845 C  CA    . ASP A 1 1588 ? 134.638 154.196 198.061 1.00 135.05 ? 2805 ASP A CA    1 
ATOM   10846 C  C     . ASP A 1 1588 ? 135.639 154.535 199.159 1.00 132.42 ? 2805 ASP A C     1 
ATOM   10847 O  O     . ASP A 1 1588 ? 135.316 154.458 200.350 1.00 129.68 ? 2805 ASP A O     1 
ATOM   10848 C  CB    . ASP A 1 1588 ? 134.847 152.765 197.566 1.00 134.02 ? 2805 ASP A CB    1 
ATOM   10849 N  N     . CYS A 1 1589 ? 136.858 154.924 198.773 1.00 131.88 ? 2806 CYS A N     1 
ATOM   10850 C  CA    . CYS A 1 1589 ? 137.874 155.298 199.754 1.00 130.95 ? 2806 CYS A CA    1 
ATOM   10851 C  C     . CYS A 1 1589 ? 137.472 156.549 200.528 1.00 129.60 ? 2806 CYS A C     1 
ATOM   10852 O  O     . CYS A 1 1589 ? 137.690 156.632 201.743 1.00 124.53 ? 2806 CYS A O     1 
ATOM   10853 C  CB    . CYS A 1 1589 ? 139.218 155.509 199.055 1.00 125.48 ? 2806 CYS A CB    1 
ATOM   10854 S  SG    . CYS A 1 1589 ? 140.535 156.131 200.125 1.00 112.30 ? 2806 CYS A SG    1 
ATOM   10855 N  N     . SER A 1 1590 ? 136.889 157.535 199.842 1.00 131.47 ? 2807 SER A N     1 
ATOM   10856 C  CA    . SER A 1 1590 ? 136.516 158.778 200.508 1.00 126.98 ? 2807 SER A CA    1 
ATOM   10857 C  C     . SER A 1 1590 ? 135.289 158.596 201.394 1.00 129.03 ? 2807 SER A C     1 
ATOM   10858 O  O     . SER A 1 1590 ? 135.236 159.136 202.505 1.00 125.33 ? 2807 SER A O     1 
ATOM   10859 C  CB    . SER A 1 1590 ? 136.270 159.875 199.472 1.00 123.84 ? 2807 SER A CB    1 
ATOM   10860 O  OG    . SER A 1 1590 ? 135.014 159.708 198.839 1.00 124.65 ? 2807 SER A OG    1 
ATOM   10861 N  N     . LEU A 1 1591 ? 134.294 157.842 200.928 1.00 132.42 ? 2808 LEU A N     1 
ATOM   10862 C  CA    . LEU A 1 1591 ? 133.038 157.700 201.649 1.00 133.62 ? 2808 LEU A CA    1 
ATOM   10863 C  C     . LEU A 1 1591 ? 133.014 156.509 202.599 1.00 133.26 ? 2808 LEU A C     1 
ATOM   10864 O  O     . LEU A 1 1591 ? 132.010 156.311 203.290 1.00 133.12 ? 2808 LEU A O     1 
ATOM   10865 C  CB    . LEU A 1 1591 ? 131.875 157.585 200.658 1.00 134.29 ? 2808 LEU A CB    1 
ATOM   10866 N  N     . LYS A 1 1592 ? 134.082 155.712 202.654 1.00 131.90 ? 2809 LYS A N     1 
ATOM   10867 C  CA    . LYS A 1 1592 ? 134.102 154.561 203.548 1.00 129.25 ? 2809 LYS A CA    1 
ATOM   10868 C  C     . LYS A 1 1592 ? 135.392 154.400 204.336 1.00 125.23 ? 2809 LYS A C     1 
ATOM   10869 O  O     . LYS A 1 1592 ? 135.429 153.542 205.223 1.00 123.24 ? 2809 LYS A O     1 
ATOM   10870 C  CB    . LYS A 1 1592 ? 133.844 153.270 202.757 1.00 130.28 ? 2809 LYS A CB    1 
ATOM   10871 N  N     . GLU A 1 1593 ? 136.438 155.183 204.049 1.00 126.41 ? 2810 GLU A N     1 
ATOM   10872 C  CA    . GLU A 1 1593 ? 137.758 155.046 204.676 1.00 123.23 ? 2810 GLU A CA    1 
ATOM   10873 C  C     . GLU A 1 1593 ? 138.313 153.633 204.503 1.00 121.20 ? 2810 GLU A C     1 
ATOM   10874 O  O     . GLU A 1 1593 ? 138.951 153.079 205.401 1.00 115.47 ? 2810 GLU A O     1 
ATOM   10875 C  CB    . GLU A 1 1593 ? 137.725 155.445 206.154 1.00 121.29 ? 2810 GLU A CB    1 
ATOM   10876 N  N     . SER A 1 1594 ? 138.066 153.045 203.334 1.00 123.32 ? 2811 SER A N     1 
ATOM   10877 C  CA    . SER A 1 1594 ? 138.528 151.698 203.019 1.00 118.55 ? 2811 SER A CA    1 
ATOM   10878 C  C     . SER A 1 1594 ? 139.875 151.803 202.316 1.00 110.22 ? 2811 SER A C     1 
ATOM   10879 O  O     . SER A 1 1594 ? 139.955 152.279 201.179 1.00 107.73 ? 2811 SER A O     1 
ATOM   10880 C  CB    . SER A 1 1594 ? 137.509 150.966 202.151 1.00 117.98 ? 2811 SER A CB    1 
ATOM   10881 O  OG    . SER A 1 1594 ? 136.303 150.738 202.860 1.00 119.09 ? 2811 SER A OG    1 
ATOM   10882 N  N     . ARG A 1 1595 ? 140.931 151.361 202.993 1.00 106.87 ? 2812 ARG A N     1 
ATOM   10883 C  CA    . ARG A 1 1595 ? 142.268 151.416 202.419 1.00 106.68 ? 2812 ARG A CA    1 
ATOM   10884 C  C     . ARG A 1 1595 ? 142.391 150.402 201.289 1.00 105.10 ? 2812 ARG A C     1 
ATOM   10885 O  O     . ARG A 1 1595 ? 142.041 149.228 201.449 1.00 101.24 ? 2812 ARG A O     1 
ATOM   10886 C  CB    . ARG A 1 1595 ? 143.312 151.155 203.503 1.00 100.21 ? 2812 ARG A CB    1 
ATOM   10887 C  CG    . ARG A 1 1595 ? 143.637 152.386 204.335 1.00 93.64  ? 2812 ARG A CG    1 
ATOM   10888 C  CD    . ARG A 1 1595 ? 144.513 152.042 205.525 1.00 91.78  ? 2812 ARG A CD    1 
ATOM   10889 N  NE    . ARG A 1 1595 ? 143.830 151.152 206.456 1.00 90.73  ? 2812 ARG A NE    1 
ATOM   10890 C  CZ    . ARG A 1 1595 ? 144.444 150.315 207.280 1.00 89.84  ? 2812 ARG A CZ    1 
ATOM   10891 N  NH1   . ARG A 1 1595 ? 145.763 150.228 207.321 1.00 86.40  ? 2812 ARG A NH1   1 
ATOM   10892 N  NH2   . ARG A 1 1595 ? 143.716 149.547 208.086 1.00 91.76  ? 2812 ARG A NH2   1 
ATOM   10893 N  N     . THR A 1 1596 ? 142.890 150.858 200.144 1.00 104.15 ? 2813 THR A N     1 
ATOM   10894 C  CA    . THR A 1 1596 ? 142.869 150.079 198.916 1.00 100.54 ? 2813 THR A CA    1 
ATOM   10895 C  C     . THR A 1 1596 ? 144.240 149.485 198.623 1.00 96.82  ? 2813 THR A C     1 
ATOM   10896 O  O     . THR A 1 1596 ? 145.271 150.120 198.863 1.00 95.12  ? 2813 THR A O     1 
ATOM   10897 C  CB    . THR A 1 1596 ? 142.427 150.943 197.733 1.00 97.33  ? 2813 THR A CB    1 
ATOM   10898 O  OG1   . THR A 1 1596 ? 143.271 152.097 197.643 1.00 93.33  ? 2813 THR A OG1   1 
ATOM   10899 C  CG2   . THR A 1 1596 ? 140.992 151.397 197.919 1.00 100.74 ? 2813 THR A CG2   1 
ATOM   10900 N  N     . CYS A 1 1597 ? 144.240 148.259 198.106 1.00 94.90  ? 2814 CYS A N     1 
ATOM   10901 C  CA    . CYS A 1 1597 ? 145.429 147.602 197.569 1.00 87.45  ? 2814 CYS A CA    1 
ATOM   10902 C  C     . CYS A 1 1597 ? 145.158 147.359 196.088 1.00 90.02  ? 2814 CYS A C     1 
ATOM   10903 O  O     . CYS A 1 1597 ? 144.685 146.288 195.700 1.00 94.16  ? 2814 CYS A O     1 
ATOM   10904 C  CB    . CYS A 1 1597 ? 145.732 146.307 198.306 1.00 83.74  ? 2814 CYS A CB    1 
ATOM   10905 S  SG    . CYS A 1 1597 ? 147.225 145.467 197.736 1.00 95.17  ? 2814 CYS A SG    1 
ATOM   10906 N  N     . LEU A 1 1598 ? 145.463 148.355 195.262 1.00 87.28  ? 2815 LEU A N     1 
ATOM   10907 C  CA    . LEU A 1 1598 ? 145.150 148.310 193.839 1.00 86.23  ? 2815 LEU A CA    1 
ATOM   10908 C  C     . LEU A 1 1598 ? 146.336 147.679 193.116 1.00 85.60  ? 2815 LEU A C     1 
ATOM   10909 O  O     . LEU A 1 1598 ? 147.427 148.257 193.074 1.00 86.45  ? 2815 LEU A O     1 
ATOM   10910 C  CB    . LEU A 1 1598 ? 144.835 149.715 193.325 1.00 82.40  ? 2815 LEU A CB    1 
ATOM   10911 C  CG    . LEU A 1 1598 ? 144.241 149.940 191.931 1.00 86.84  ? 2815 LEU A CG    1 
ATOM   10912 C  CD1   . LEU A 1 1598 ? 143.417 151.213 191.934 1.00 86.40  ? 2815 LEU A CD1   1 
ATOM   10913 C  CD2   . LEU A 1 1598 ? 145.304 150.034 190.865 1.00 86.65  ? 2815 LEU A CD2   1 
ATOM   10914 N  N     . ILE A 1 1599 ? 146.120 146.497 192.547 1.00 89.87  ? 2816 ILE A N     1 
ATOM   10915 C  CA    . ILE A 1 1599 ? 147.193 145.695 191.969 1.00 91.73  ? 2816 ILE A CA    1 
ATOM   10916 C  C     . ILE A 1 1599 ? 147.318 146.032 190.489 1.00 93.74  ? 2816 ILE A C     1 
ATOM   10917 O  O     . ILE A 1 1599 ? 146.340 145.942 189.740 1.00 95.90  ? 2816 ILE A O     1 
ATOM   10918 C  CB    . ILE A 1 1599 ? 146.927 144.195 192.163 1.00 90.66  ? 2816 ILE A CB    1 
ATOM   10919 C  CG1   . ILE A 1 1599 ? 146.700 143.867 193.642 1.00 88.67  ? 2816 ILE A CG1   1 
ATOM   10920 C  CG2   . ILE A 1 1599 ? 148.068 143.370 191.584 1.00 89.53  ? 2816 ILE A CG2   1 
ATOM   10921 C  CD1   . ILE A 1 1599 ? 147.958 143.824 194.472 1.00 81.75  ? 2816 ILE A CD1   1 
ATOM   10922 N  N     . ILE A 1 1600 ? 148.520 146.412 190.063 1.00 94.45  ? 2817 ILE A N     1 
ATOM   10923 C  CA    . ILE A 1 1600 ? 148.818 146.647 188.654 1.00 97.69  ? 2817 ILE A CA    1 
ATOM   10924 C  C     . ILE A 1 1600 ? 150.077 145.870 188.303 1.00 97.30  ? 2817 ILE A C     1 
ATOM   10925 O  O     . ILE A 1 1600 ? 151.129 146.074 188.921 1.00 94.32  ? 2817 ILE A O     1 
ATOM   10926 C  CB    . ILE A 1 1600 ? 148.996 148.140 188.334 1.00 96.98  ? 2817 ILE A CB    1 
ATOM   10927 C  CG1   . ILE A 1 1600 ? 147.654 148.863 188.414 1.00 98.16  ? 2817 ILE A CG1   1 
ATOM   10928 C  CG2   . ILE A 1 1600 ? 149.612 148.324 186.955 1.00 95.19  ? 2817 ILE A CG2   1 
ATOM   10929 C  CD1   . ILE A 1 1600 ? 146.657 148.427 187.362 1.00 99.56  ? 2817 ILE A CD1   1 
ATOM   10930 N  N     . ASP A 1 1601 ? 149.970 144.987 187.318 1.00 97.90  ? 2818 ASP A N     1 
ATOM   10931 C  CA    . ASP A 1 1601 ? 151.088 144.188 186.843 1.00 98.15  ? 2818 ASP A CA    1 
ATOM   10932 C  C     . ASP A 1 1601 ? 151.734 144.851 185.633 1.00 98.89  ? 2818 ASP A C     1 
ATOM   10933 O  O     . ASP A 1 1601 ? 151.167 145.753 185.012 1.00 100.16 ? 2818 ASP A O     1 
ATOM   10934 C  CB    . ASP A 1 1601 ? 150.626 142.774 186.479 1.00 103.31 ? 2818 ASP A CB    1 
ATOM   10935 C  CG    . ASP A 1 1601 ? 150.317 141.928 187.698 1.00 100.29 ? 2818 ASP A CG    1 
ATOM   10936 O  OD1   . ASP A 1 1601 ? 150.002 142.505 188.760 1.00 96.82  ? 2818 ASP A OD1   1 
ATOM   10937 O  OD2   . ASP A 1 1601 ? 150.384 140.685 187.593 1.00 97.31  ? 2818 ASP A OD2   1 
ATOM   10938 N  N     . GLU A 1 1602 ? 152.942 144.387 185.303 1.00 98.33  ? 2819 GLU A N     1 
ATOM   10939 C  CA    . GLU A 1 1602 ? 153.612 144.854 184.095 1.00 98.78  ? 2819 GLU A CA    1 
ATOM   10940 C  C     . GLU A 1 1602 ? 152.889 144.409 182.830 1.00 98.78  ? 2819 GLU A C     1 
ATOM   10941 O  O     . GLU A 1 1602 ? 153.113 144.991 181.763 1.00 95.40  ? 2819 GLU A O     1 
ATOM   10942 C  CB    . GLU A 1 1602 ? 155.062 144.365 184.072 1.00 92.88  ? 2819 GLU A CB    1 
ATOM   10943 C  CG    . GLU A 1 1602 ? 155.999 145.227 183.237 1.00 87.38  ? 2819 GLU A CG    1 
ATOM   10944 C  CD    . GLU A 1 1602 ? 157.448 144.801 183.360 1.00 83.09  ? 2819 GLU A CD    1 
ATOM   10945 O  OE1   . GLU A 1 1602 ? 157.710 143.581 183.398 1.00 82.18  ? 2819 GLU A OE1   1 
ATOM   10946 O  OE2   . GLU A 1 1602 ? 158.326 145.687 183.421 1.00 82.20  ? 2819 GLU A OE2   1 
ATOM   10947 N  N     . SER A 1 1603 ? 152.032 143.392 182.923 1.00 100.04 ? 2820 SER A N     1 
ATOM   10948 C  CA    . SER A 1 1603 ? 151.208 142.974 181.798 1.00 102.35 ? 2820 SER A CA    1 
ATOM   10949 C  C     . SER A 1 1603 ? 150.018 143.894 181.562 1.00 103.19 ? 2820 SER A C     1 
ATOM   10950 O  O     . SER A 1 1603 ? 149.347 143.758 180.534 1.00 103.26 ? 2820 SER A O     1 
ATOM   10951 C  CB    . SER A 1 1603 ? 150.713 141.541 182.014 1.00 101.84 ? 2820 SER A CB    1 
ATOM   10952 O  OG    . SER A 1 1603 ? 149.825 141.470 183.116 1.00 98.45  ? 2820 SER A OG    1 
ATOM   10953 N  N     . ASN A 1 1604 ? 149.739 144.818 182.483 1.00 101.83 ? 2821 ASN A N     1 
ATOM   10954 C  CA    . ASN A 1 1604 ? 148.603 145.719 182.356 1.00 105.02 ? 2821 ASN A CA    1 
ATOM   10955 C  C     . ASN A 1 1604 ? 148.993 147.155 182.036 1.00 104.33 ? 2821 ASN A C     1 
ATOM   10956 O  O     . ASN A 1 1604 ? 148.101 147.980 181.807 1.00 107.12 ? 2821 ASN A O     1 
ATOM   10957 C  CB    . ASN A 1 1604 ? 147.763 145.695 183.642 1.00 104.43 ? 2821 ASN A CB    1 
ATOM   10958 C  CG    . ASN A 1 1604 ? 147.113 144.347 183.887 1.00 103.67 ? 2821 ASN A CG    1 
ATOM   10959 O  OD1   . ASN A 1 1604 ? 146.904 143.568 182.957 1.00 105.66 ? 2821 ASN A OD1   1 
ATOM   10960 N  ND2   . ASN A 1 1604 ? 146.788 144.065 185.143 1.00 99.10  ? 2821 ASN A ND2   1 
ATOM   10961 N  N     . ILE A 1 1605 ? 150.284 147.480 182.012 1.00 100.78 ? 2822 ILE A N     1 
ATOM   10962 C  CA    . ILE A 1 1605 ? 150.741 148.815 181.618 1.00 99.68  ? 2822 ILE A CA    1 
ATOM   10963 C  C     . ILE A 1 1605 ? 150.976 148.768 180.108 1.00 100.51 ? 2822 ILE A C     1 
ATOM   10964 O  O     . ILE A 1 1605 ? 152.063 148.456 179.618 1.00 102.32 ? 2822 ILE A O     1 
ATOM   10965 C  CB    . ILE A 1 1605 ? 151.967 149.267 182.419 1.00 99.82  ? 2822 ILE A CB    1 
ATOM   10966 C  CG1   . ILE A 1 1605 ? 152.503 150.611 181.913 1.00 98.08  ? 2822 ILE A CG1   1 
ATOM   10967 C  CG2   . ILE A 1 1605 ? 153.039 148.172 182.527 1.00 99.90  ? 2822 ILE A CG2   1 
ATOM   10968 C  CD1   . ILE A 1 1605 ? 153.515 151.242 182.836 1.00 92.62  ? 2822 ILE A CD1   1 
ATOM   10969 N  N     . LEU A 1 1606 ? 149.916 149.060 179.354 1.00 102.29 ? 2823 LEU A N     1 
ATOM   10970 C  CA    . LEU A 1 1606 ? 149.973 148.996 177.899 1.00 104.04 ? 2823 LEU A CA    1 
ATOM   10971 C  C     . LEU A 1 1606 ? 150.431 150.308 177.276 1.00 105.67 ? 2823 LEU A C     1 
ATOM   10972 O  O     . LEU A 1 1606 ? 151.178 150.297 176.292 1.00 108.42 ? 2823 LEU A O     1 
ATOM   10973 C  CB    . LEU A 1 1606 ? 148.606 148.604 177.326 1.00 102.38 ? 2823 LEU A CB    1 
ATOM   10974 C  CG    . LEU A 1 1606 ? 148.178 147.131 177.311 1.00 94.33  ? 2823 LEU A CG    1 
ATOM   10975 C  CD1   . LEU A 1 1606 ? 147.895 146.582 178.704 1.00 95.67  ? 2823 LEU A CD1   1 
ATOM   10976 C  CD2   . LEU A 1 1606 ? 146.968 146.948 176.406 1.00 82.25  ? 2823 LEU A CD2   1 
ATOM   10977 N  N     . GLU A 1 1607 ? 149.999 151.438 177.827 1.00 101.84 ? 2824 GLU A N     1 
ATOM   10978 C  CA    . GLU A 1 1607 ? 150.315 152.745 177.276 1.00 94.94  ? 2824 GLU A CA    1 
ATOM   10979 C  C     . GLU A 1 1607 ? 151.109 153.564 178.285 1.00 95.00  ? 2824 GLU A C     1 
ATOM   10980 O  O     . GLU A 1 1607 ? 150.930 153.432 179.500 1.00 94.17  ? 2824 GLU A O     1 
ATOM   10981 C  CB    . GLU A 1 1607 ? 149.042 153.503 176.877 1.00 93.90  ? 2824 GLU A CB    1 
ATOM   10982 N  N     . THR A 1 1608 ? 151.992 154.417 177.762 1.00 94.84  ? 2825 THR A N     1 
ATOM   10983 C  CA    . THR A 1 1608 ? 152.784 155.306 178.605 1.00 88.31  ? 2825 THR A CA    1 
ATOM   10984 C  C     . THR A 1 1608 ? 151.922 156.405 179.226 1.00 87.20  ? 2825 THR A C     1 
ATOM   10985 O  O     . THR A 1 1608 ? 152.355 157.060 180.180 1.00 86.23  ? 2825 THR A O     1 
ATOM   10986 C  CB    . THR A 1 1608 ? 153.934 155.892 177.772 1.00 84.51  ? 2825 THR A CB    1 
ATOM   10987 O  OG1   . THR A 1 1608 ? 154.571 154.834 177.046 1.00 86.58  ? 2825 THR A OG1   1 
ATOM   10988 C  CG2   . THR A 1 1608 ? 154.996 156.542 178.655 1.00 85.90  ? 2825 THR A CG2   1 
ATOM   10989 N  N     . ALA A 1 1609 ? 150.703 156.607 178.717 1.00 90.87  ? 2826 ALA A N     1 
ATOM   10990 C  CA    . ALA A 1 1609 ? 149.780 157.550 179.342 1.00 92.97  ? 2826 ALA A CA    1 
ATOM   10991 C  C     . ALA A 1 1609 ? 149.396 157.112 180.750 1.00 93.17  ? 2826 ALA A C     1 
ATOM   10992 O  O     . ALA A 1 1609 ? 149.237 157.958 181.637 1.00 89.26  ? 2826 ALA A O     1 
ATOM   10993 C  CB    . ALA A 1 1609 ? 148.531 157.716 178.477 1.00 93.23  ? 2826 ALA A CB    1 
ATOM   10994 N  N     . PHE A 1 1610 ? 149.247 155.803 180.975 1.00 93.35  ? 2827 PHE A N     1 
ATOM   10995 C  CA    . PHE A 1 1610 ? 148.984 155.293 182.319 1.00 91.61  ? 2827 PHE A CA    1 
ATOM   10996 C  C     . PHE A 1 1610 ? 150.151 155.609 183.248 1.00 92.97  ? 2827 PHE A C     1 
ATOM   10997 O  O     . PHE A 1 1610 ? 149.964 156.054 184.393 1.00 93.58  ? 2827 PHE A O     1 
ATOM   10998 C  CB    . PHE A 1 1610 ? 148.767 153.782 182.257 1.00 91.84  ? 2827 PHE A CB    1 
ATOM   10999 C  CG    . PHE A 1 1610 ? 147.553 153.370 181.480 1.00 94.73  ? 2827 PHE A CG    1 
ATOM   11000 C  CD1   . PHE A 1 1610 ? 146.293 153.412 182.047 1.00 103.18 ? 2827 PHE A CD1   1 
ATOM   11001 C  CD2   . PHE A 1 1610 ? 147.681 152.926 180.175 1.00 93.34  ? 2827 PHE A CD2   1 
ATOM   11002 C  CE1   . PHE A 1 1610 ? 145.181 153.024 181.321 1.00 106.55 ? 2827 PHE A CE1   1 
ATOM   11003 C  CE2   . PHE A 1 1610 ? 146.576 152.538 179.447 1.00 97.61  ? 2827 PHE A CE2   1 
ATOM   11004 C  CZ    . PHE A 1 1610 ? 145.324 152.587 180.020 1.00 106.62 ? 2827 PHE A CZ    1 
ATOM   11005 N  N     . LEU A 1 1611 ? 151.369 155.382 182.751 1.00 90.48  ? 2828 LEU A N     1 
ATOM   11006 C  CA    . LEU A 1 1611 ? 152.578 155.663 183.513 1.00 87.20  ? 2828 LEU A CA    1 
ATOM   11007 C  C     . LEU A 1 1611 ? 152.678 157.139 183.860 1.00 87.36  ? 2828 LEU A C     1 
ATOM   11008 O  O     . LEU A 1 1611 ? 153.028 157.494 184.987 1.00 86.81  ? 2828 LEU A O     1 
ATOM   11009 C  CB    . LEU A 1 1611 ? 153.799 155.222 182.712 1.00 88.31  ? 2828 LEU A CB    1 
ATOM   11010 C  CG    . LEU A 1 1611 ? 155.133 155.166 183.446 1.00 90.50  ? 2828 LEU A CG    1 
ATOM   11011 C  CD1   . LEU A 1 1611 ? 155.073 154.117 184.539 1.00 96.44  ? 2828 LEU A CD1   1 
ATOM   11012 C  CD2   . LEU A 1 1611 ? 156.250 154.880 182.457 1.00 91.78  ? 2828 LEU A CD2   1 
ATOM   11013 N  N     . GLU A 1 1612 ? 152.362 158.015 182.905 1.00 89.57  ? 2829 GLU A N     1 
ATOM   11014 C  CA    . GLU A 1 1612 ? 152.413 159.449 183.166 1.00 86.79  ? 2829 GLU A CA    1 
ATOM   11015 C  C     . GLU A 1 1612 ? 151.296 159.896 184.102 1.00 83.91  ? 2829 GLU A C     1 
ATOM   11016 O  O     . GLU A 1 1612 ? 151.479 160.849 184.869 1.00 79.46  ? 2829 GLU A O     1 
ATOM   11017 C  CB    . GLU A 1 1612 ? 152.345 160.221 181.854 1.00 81.93  ? 2829 GLU A CB    1 
ATOM   11018 N  N     . ARG A 1 1613 ? 150.140 159.230 184.049 1.00 84.47  ? 2830 ARG A N     1 
ATOM   11019 C  CA    . ARG A 1 1613 ? 149.081 159.498 185.016 1.00 86.01  ? 2830 ARG A CA    1 
ATOM   11020 C  C     . ARG A 1 1613 ? 149.556 159.219 186.435 1.00 86.79  ? 2830 ARG A C     1 
ATOM   11021 O  O     . ARG A 1 1613 ? 149.442 160.077 187.320 1.00 85.83  ? 2830 ARG A O     1 
ATOM   11022 C  CB    . ARG A 1 1613 ? 147.848 158.654 184.697 1.00 88.51  ? 2830 ARG A CB    1 
ATOM   11023 C  CG    . ARG A 1 1613 ? 146.802 158.712 185.791 1.00 93.61  ? 2830 ARG A CG    1 
ATOM   11024 C  CD    . ARG A 1 1613 ? 146.057 157.393 185.932 1.00 97.66  ? 2830 ARG A CD    1 
ATOM   11025 N  NE    . ARG A 1 1613 ? 145.266 157.315 187.156 1.00 97.13  ? 2830 ARG A NE    1 
ATOM   11026 C  CZ    . ARG A 1 1613 ? 145.758 157.289 188.390 1.00 88.07  ? 2830 ARG A CZ    1 
ATOM   11027 N  NH1   . ARG A 1 1613 ? 147.061 157.260 188.619 1.00 86.66  ? 2830 ARG A NH1   1 
ATOM   11028 N  NH2   . ARG A 1 1613 ? 144.919 157.264 189.421 1.00 85.09  ? 2830 ARG A NH2   1 
ATOM   11029 N  N     . MET A 1 1614 ? 150.109 158.023 186.666 1.00 87.36  ? 2831 MET A N     1 
ATOM   11030 C  CA    . MET A 1 1614 ? 150.675 157.732 187.984 1.00 86.32  ? 2831 MET A CA    1 
ATOM   11031 C  C     . MET A 1 1614 ? 151.865 158.632 188.297 1.00 84.80  ? 2831 MET A C     1 
ATOM   11032 O  O     . MET A 1 1614 ? 152.122 158.941 189.467 1.00 85.62  ? 2831 MET A O     1 
ATOM   11033 C  CB    . MET A 1 1614 ? 151.079 156.260 188.091 1.00 83.10  ? 2831 MET A CB    1 
ATOM   11034 C  CG    . MET A 1 1614 ? 149.948 155.332 188.517 1.00 82.10  ? 2831 MET A CG    1 
ATOM   11035 S  SD    . MET A 1 1614 ? 148.794 154.875 187.209 1.00 98.17  ? 2831 MET A SD    1 
ATOM   11036 C  CE    . MET A 1 1614 ? 149.691 153.546 186.411 1.00 85.92  ? 2831 MET A CE    1 
ATOM   11037 N  N     . ASN A 1 1615 ? 152.577 159.087 187.265 1.00 83.66  ? 2832 ASN A N     1 
ATOM   11038 C  CA    . ASN A 1 1615 ? 153.738 159.945 187.461 1.00 77.79  ? 2832 ASN A CA    1 
ATOM   11039 C  C     . ASN A 1 1615 ? 153.318 161.293 188.032 1.00 80.97  ? 2832 ASN A C     1 
ATOM   11040 O  O     . ASN A 1 1615 ? 153.921 161.795 188.983 1.00 78.84  ? 2832 ASN A O     1 
ATOM   11041 C  CB    . ASN A 1 1615 ? 154.462 160.117 186.125 1.00 76.21  ? 2832 ASN A CB    1 
ATOM   11042 C  CG    . ASN A 1 1615 ? 155.931 160.405 186.287 1.00 71.74  ? 2832 ASN A CG    1 
ATOM   11043 O  OD1   . ASN A 1 1615 ? 156.449 160.408 187.394 1.00 71.17  ? 2832 ASN A OD1   1 
ATOM   11044 N  ND2   . ASN A 1 1615 ? 156.615 160.646 185.175 1.00 71.29  ? 2832 ASN A ND2   1 
ATOM   11045 N  N     . THR A 1 1616 ? 152.258 161.883 187.473 1.00 88.07  ? 2833 THR A N     1 
ATOM   11046 C  CA    . THR A 1 1616 ? 151.698 163.111 188.035 1.00 90.14  ? 2833 THR A CA    1 
ATOM   11047 C  C     . THR A 1 1616 ? 151.073 162.856 189.404 1.00 87.32  ? 2833 THR A C     1 
ATOM   11048 O  O     . THR A 1 1616 ? 151.218 163.676 190.328 1.00 80.70  ? 2833 THR A O     1 
ATOM   11049 C  CB    . THR A 1 1616 ? 150.663 163.703 187.075 1.00 84.49  ? 2833 THR A CB    1 
ATOM   11050 O  OG1   . THR A 1 1616 ? 151.230 163.806 185.762 1.00 70.05  ? 2833 THR A OG1   1 
ATOM   11051 C  CG2   . THR A 1 1616 ? 150.226 165.085 187.538 1.00 81.86  ? 2833 THR A CG2   1 
ATOM   11052 N  N     . LEU A 1 1617 ? 150.384 161.712 189.546 1.00 86.83  ? 2834 LEU A N     1 
ATOM   11053 C  CA    . LEU A 1 1617 ? 149.792 161.310 190.819 1.00 87.09  ? 2834 LEU A CA    1 
ATOM   11054 C  C     . LEU A 1 1617 ? 150.819 161.274 191.930 1.00 83.79  ? 2834 LEU A C     1 
ATOM   11055 O  O     . LEU A 1 1617 ? 150.505 161.590 193.082 1.00 90.80  ? 2834 LEU A O     1 
ATOM   11056 C  CB    . LEU A 1 1617 ? 149.140 159.932 190.679 1.00 86.63  ? 2834 LEU A CB    1 
ATOM   11057 C  CG    . LEU A 1 1617 ? 148.799 159.151 191.954 1.00 82.56  ? 2834 LEU A CG    1 
ATOM   11058 C  CD1   . LEU A 1 1617 ? 147.671 159.822 192.722 1.00 85.74  ? 2834 LEU A CD1   1 
ATOM   11059 C  CD2   . LEU A 1 1617 ? 148.466 157.701 191.646 1.00 83.79  ? 2834 LEU A CD2   1 
ATOM   11060 N  N     . LEU A 1 1618 ? 152.047 160.901 191.608 1.00 77.31  ? 2835 LEU A N     1 
ATOM   11061 C  CA    . LEU A 1 1618 ? 153.055 160.782 192.637 1.00 78.14  ? 2835 LEU A CA    1 
ATOM   11062 C  C     . LEU A 1 1618 ? 153.962 162.010 192.678 1.00 80.36  ? 2835 LEU A C     1 
ATOM   11063 O  O     . LEU A 1 1618 ? 154.674 162.210 193.668 1.00 74.42  ? 2835 LEU A O     1 
ATOM   11064 C  CB    . LEU A 1 1618 ? 153.844 159.488 192.404 1.00 76.23  ? 2835 LEU A CB    1 
ATOM   11065 C  CG    . LEU A 1 1618 ? 154.821 159.058 193.474 1.00 70.07  ? 2835 LEU A CG    1 
ATOM   11066 C  CD1   . LEU A 1 1618 ? 153.927 158.830 194.659 1.00 70.87  ? 2835 LEU A CD1   1 
ATOM   11067 C  CD2   . LEU A 1 1618 ? 155.485 157.770 193.078 1.00 68.09  ? 2835 LEU A CD2   1 
ATOM   11068 N  N     . ALA A 1 1619 ? 153.917 162.851 191.637 1.00 83.32  ? 2836 ALA A N     1 
ATOM   11069 C  CA    . ALA A 1 1619 ? 154.480 164.196 191.721 1.00 82.72  ? 2836 ALA A CA    1 
ATOM   11070 C  C     . ALA A 1 1619 ? 153.771 165.006 192.790 1.00 81.98  ? 2836 ALA A C     1 
ATOM   11071 O  O     . ALA A 1 1619 ? 154.405 165.569 193.690 1.00 79.68  ? 2836 ALA A O     1 
ATOM   11072 C  CB    . ALA A 1 1619 ? 154.357 164.905 190.371 1.00 76.55  ? 2836 ALA A CB    1 
ATOM   11073 N  N     . ASN A 1 1620 ? 152.450 165.070 192.708 1.00 82.83  ? 2837 ASN A N     1 
ATOM   11074 C  CA    . ASN A 1 1620 ? 151.653 165.583 193.811 1.00 85.82  ? 2837 ASN A CA    1 
ATOM   11075 C  C     . ASN A 1 1620 ? 151.285 164.401 194.706 1.00 85.99  ? 2837 ASN A C     1 
ATOM   11076 O  O     . ASN A 1 1620 ? 151.920 163.346 194.647 1.00 90.53  ? 2837 ASN A O     1 
ATOM   11077 C  CB    . ASN A 1 1620 ? 150.435 166.347 193.281 1.00 90.87  ? 2837 ASN A CB    1 
ATOM   11078 C  CG    . ASN A 1 1620 ? 150.816 167.594 192.508 1.00 93.14  ? 2837 ASN A CG    1 
ATOM   11079 O  OD1   . ASN A 1 1620 ? 151.961 168.044 192.554 1.00 90.87  ? 2837 ASN A OD1   1 
ATOM   11080 N  ND2   . ASN A 1 1620 ? 149.850 168.165 191.798 1.00 92.31  ? 2837 ASN A ND2   1 
ATOM   11081 N  N     . ALA A 1 1621 ? 150.314 164.577 195.591 1.00 86.10  ? 2838 ALA A N     1 
ATOM   11082 C  CA    . ALA A 1 1621 ? 149.628 163.446 196.193 1.00 88.06  ? 2838 ALA A CA    1 
ATOM   11083 C  C     . ALA A 1 1621 ? 148.257 163.225 195.569 1.00 92.24  ? 2838 ALA A C     1 
ATOM   11084 O  O     . ALA A 1 1621 ? 147.465 162.436 196.092 1.00 92.50  ? 2838 ALA A O     1 
ATOM   11085 C  CB    . ALA A 1 1621 ? 149.508 163.637 197.703 1.00 92.73  ? 2838 ALA A CB    1 
ATOM   11086 N  N     . ASP A 1 1622 ? 147.970 163.905 194.462 1.00 91.00  ? 2839 ASP A N     1 
ATOM   11087 C  CA    . ASP A 1 1622 ? 146.695 163.807 193.763 1.00 90.59  ? 2839 ASP A CA    1 
ATOM   11088 C  C     . ASP A 1 1622 ? 146.914 164.276 192.328 1.00 91.14  ? 2839 ASP A C     1 
ATOM   11089 O  O     . ASP A 1 1622 ? 148.006 164.715 191.959 1.00 86.88  ? 2839 ASP A O     1 
ATOM   11090 C  CB    . ASP A 1 1622 ? 145.617 164.631 194.475 1.00 90.67  ? 2839 ASP A CB    1 
ATOM   11091 C  CG    . ASP A 1 1622 ? 144.213 164.160 194.155 1.00 92.86  ? 2839 ASP A CG    1 
ATOM   11092 O  OD1   . ASP A 1 1622 ? 144.067 163.258 193.305 1.00 96.78  ? 2839 ASP A OD1   1 
ATOM   11093 O  OD2   . ASP A 1 1622 ? 143.256 164.694 194.753 1.00 90.05  ? 2839 ASP A OD2   1 
ATOM   11094 N  N     . ILE A 1 1623 ? 145.870 164.169 191.512 1.00 95.07  ? 2840 ILE A N     1 
ATOM   11095 C  CA    . ILE A 1 1623 ? 145.913 164.691 190.148 1.00 96.44  ? 2840 ILE A CA    1 
ATOM   11096 C  C     . ILE A 1 1623 ? 144.797 165.719 190.004 1.00 98.58  ? 2840 ILE A C     1 
ATOM   11097 O  O     . ILE A 1 1623 ? 143.655 165.448 190.404 1.00 97.23  ? 2840 ILE A O     1 
ATOM   11098 C  CB    . ILE A 1 1623 ? 145.770 163.573 189.105 1.00 97.95  ? 2840 ILE A CB    1 
ATOM   11099 C  CG1   . ILE A 1 1623 ? 146.809 162.485 189.322 1.00 93.45  ? 2840 ILE A CG1   1 
ATOM   11100 C  CG2   . ILE A 1 1623 ? 145.982 164.115 187.717 1.00 96.77  ? 2840 ILE A CG2   1 
ATOM   11101 C  CD1   . ILE A 1 1623 ? 146.581 161.261 188.469 1.00 91.62  ? 2840 ILE A CD1   1 
ATOM   11102 N  N     . PRO A 1 1624 ? 145.074 166.906 189.455 1.00 101.73 ? 2841 PRO A N     1 
ATOM   11103 C  CA    . PRO A 1 1624 ? 144.024 167.929 189.343 1.00 100.74 ? 2841 PRO A CA    1 
ATOM   11104 C  C     . PRO A 1 1624 ? 142.918 167.590 188.352 1.00 103.91 ? 2841 PRO A C     1 
ATOM   11105 O  O     . PRO A 1 1624 ? 141.737 167.757 188.671 1.00 105.42 ? 2841 PRO A O     1 
ATOM   11106 C  CB    . PRO A 1 1624 ? 144.799 169.179 188.900 1.00 103.05 ? 2841 PRO A CB    1 
ATOM   11107 C  CG    . PRO A 1 1624 ? 146.222 168.907 189.269 1.00 102.63 ? 2841 PRO A CG    1 
ATOM   11108 C  CD    . PRO A 1 1624 ? 146.400 167.437 189.101 1.00 101.19 ? 2841 PRO A CD    1 
ATOM   11109 N  N     . ASP A 1 1625 ? 143.271 167.111 187.159 1.00 105.05 ? 2842 ASP A N     1 
ATOM   11110 C  CA    . ASP A 1 1625 ? 142.281 167.000 186.093 1.00 106.61 ? 2842 ASP A CA    1 
ATOM   11111 C  C     . ASP A 1 1625 ? 141.459 165.717 186.150 1.00 109.57 ? 2842 ASP A C     1 
ATOM   11112 O  O     . ASP A 1 1625 ? 140.629 165.500 185.260 1.00 109.85 ? 2842 ASP A O     1 
ATOM   11113 C  CB    . ASP A 1 1625 ? 142.952 167.132 184.718 1.00 101.40 ? 2842 ASP A CB    1 
ATOM   11114 C  CG    . ASP A 1 1625 ? 143.889 165.984 184.401 1.00 101.96 ? 2842 ASP A CG    1 
ATOM   11115 O  OD1   . ASP A 1 1625 ? 144.276 165.244 185.323 1.00 99.36  ? 2842 ASP A OD1   1 
ATOM   11116 O  OD2   . ASP A 1 1625 ? 144.239 165.820 183.214 1.00 108.20 ? 2842 ASP A OD2   1 
ATOM   11117 N  N     . LEU A 1 1626 ? 141.670 164.856 187.149 1.00 109.68 ? 2843 LEU A N     1 
ATOM   11118 C  CA    . LEU A 1 1626 ? 140.772 163.718 187.327 1.00 111.75 ? 2843 LEU A CA    1 
ATOM   11119 C  C     . LEU A 1 1626 ? 139.381 164.176 187.744 1.00 111.61 ? 2843 LEU A C     1 
ATOM   11120 O  O     . LEU A 1 1626 ? 138.378 163.569 187.352 1.00 113.07 ? 2843 LEU A O     1 
ATOM   11121 C  CB    . LEU A 1 1626 ? 141.336 162.739 188.355 1.00 108.52 ? 2843 LEU A CB    1 
ATOM   11122 C  CG    . LEU A 1 1626 ? 142.656 162.037 188.045 1.00 100.52 ? 2843 LEU A CG    1 
ATOM   11123 C  CD1   . LEU A 1 1626 ? 142.944 160.987 189.105 1.00 98.82  ? 2843 LEU A CD1   1 
ATOM   11124 C  CD2   . LEU A 1 1626 ? 142.631 161.415 186.659 1.00 100.77 ? 2843 LEU A CD2   1 
ATOM   11125 N  N     . PHE A 1 1627 ? 139.301 165.237 188.540 1.00 109.96 ? 2844 PHE A N     1 
ATOM   11126 C  CA    . PHE A 1 1627 ? 138.034 165.780 189.015 1.00 117.40 ? 2844 PHE A CA    1 
ATOM   11127 C  C     . PHE A 1 1627 ? 137.843 167.167 188.417 1.00 118.35 ? 2844 PHE A C     1 
ATOM   11128 O  O     . PHE A 1 1627 ? 138.546 168.113 188.790 1.00 115.25 ? 2844 PHE A O     1 
ATOM   11129 C  CB    . PHE A 1 1627 ? 137.999 165.826 190.541 1.00 120.63 ? 2844 PHE A CB    1 
ATOM   11130 C  CG    . PHE A 1 1627 ? 138.060 164.475 191.185 1.00 115.11 ? 2844 PHE A CG    1 
ATOM   11131 C  CD1   . PHE A 1 1627 ? 137.028 163.568 191.013 1.00 113.16 ? 2844 PHE A CD1   1 
ATOM   11132 C  CD2   . PHE A 1 1627 ? 139.148 164.108 191.957 1.00 109.97 ? 2844 PHE A CD2   1 
ATOM   11133 C  CE1   . PHE A 1 1627 ? 137.079 162.322 191.601 1.00 111.81 ? 2844 PHE A CE1   1 
ATOM   11134 C  CE2   . PHE A 1 1627 ? 139.205 162.863 192.545 1.00 106.64 ? 2844 PHE A CE2   1 
ATOM   11135 C  CZ    . PHE A 1 1627 ? 138.168 161.971 192.368 1.00 111.22 ? 2844 PHE A CZ    1 
ATOM   11136 N  N     . GLN A 1 1628 ? 136.896 167.283 187.490 1.00 120.46 ? 2845 GLN A N     1 
ATOM   11137 C  CA    . GLN A 1 1628 ? 136.557 168.563 186.891 1.00 118.63 ? 2845 GLN A CA    1 
ATOM   11138 C  C     . GLN A 1 1628 ? 135.095 168.536 186.464 1.00 122.24 ? 2845 GLN A C     1 
ATOM   11139 O  O     . GLN A 1 1628 ? 134.610 167.533 185.932 1.00 125.91 ? 2845 GLN A O     1 
ATOM   11140 C  CB    . GLN A 1 1628 ? 137.483 168.891 185.710 1.00 112.31 ? 2845 GLN A CB    1 
ATOM   11141 C  CG    . GLN A 1 1628 ? 137.384 167.949 184.521 1.00 105.25 ? 2845 GLN A CG    1 
ATOM   11142 C  CD    . GLN A 1 1628 ? 138.368 168.292 183.423 1.00 100.73 ? 2845 GLN A CD    1 
ATOM   11143 O  OE1   . GLN A 1 1628 ? 139.105 169.274 183.518 1.00 97.25  ? 2845 GLN A OE1   1 
ATOM   11144 N  NE2   . GLN A 1 1628 ? 138.383 167.484 182.370 1.00 101.27 ? 2845 GLN A NE2   1 
ATOM   11145 N  N     . GLY A 1 1629 ? 134.391 169.626 186.740 1.00 120.87 ? 2846 GLY A N     1 
ATOM   11146 C  CA    . GLY A 1 1629 ? 133.003 169.752 186.327 1.00 123.71 ? 2846 GLY A CA    1 
ATOM   11147 C  C     . GLY A 1 1629 ? 132.061 169.070 187.301 1.00 129.18 ? 2846 GLY A C     1 
ATOM   11148 O  O     . GLY A 1 1629 ? 132.134 169.300 188.513 1.00 130.16 ? 2846 GLY A O     1 
ATOM   11149 N  N     . GLU A 1 1630 ? 131.167 168.235 186.761 1.00 131.03 ? 2847 GLU A N     1 
ATOM   11150 C  CA    . GLU A 1 1630 ? 130.140 167.595 187.578 1.00 131.08 ? 2847 GLU A CA    1 
ATOM   11151 C  C     . GLU A 1 1630 ? 130.746 166.632 188.592 1.00 131.38 ? 2847 GLU A C     1 
ATOM   11152 O  O     . GLU A 1 1630 ? 130.281 166.556 189.735 1.00 128.94 ? 2847 GLU A O     1 
ATOM   11153 C  CB    . GLU A 1 1630 ? 129.138 166.869 186.681 1.00 132.90 ? 2847 GLU A CB    1 
ATOM   11154 C  CG    . GLU A 1 1630 ? 127.894 166.385 187.405 1.00 135.47 ? 2847 GLU A CG    1 
ATOM   11155 C  CD    . GLU A 1 1630 ? 127.962 164.912 187.754 1.00 141.83 ? 2847 GLU A CD    1 
ATOM   11156 O  OE1   . GLU A 1 1630 ? 128.971 164.264 187.406 1.00 143.42 ? 2847 GLU A OE1   1 
ATOM   11157 O  OE2   . GLU A 1 1630 ? 127.007 164.403 188.377 1.00 143.65 ? 2847 GLU A OE2   1 
ATOM   11158 N  N     . GLU A 1 1631 ? 131.777 165.882 188.190 1.00 131.53 ? 2848 GLU A N     1 
ATOM   11159 C  CA    . GLU A 1 1631 ? 132.438 164.971 189.121 1.00 131.83 ? 2848 GLU A CA    1 
ATOM   11160 C  C     . GLU A 1 1631 ? 133.119 165.734 190.250 1.00 130.01 ? 2848 GLU A C     1 
ATOM   11161 O  O     . GLU A 1 1631 ? 133.074 165.310 191.411 1.00 129.60 ? 2848 GLU A O     1 
ATOM   11162 C  CB    . GLU A 1 1631 ? 133.447 164.101 188.373 1.00 129.62 ? 2848 GLU A CB    1 
ATOM   11163 N  N     . TYR A 1 1632 ? 133.755 166.863 189.928 1.00 126.72 ? 2849 TYR A N     1 
ATOM   11164 C  CA    . TYR A 1 1632 ? 134.389 167.692 190.949 1.00 122.87 ? 2849 TYR A CA    1 
ATOM   11165 C  C     . TYR A 1 1632 ? 133.357 168.274 191.909 1.00 125.74 ? 2849 TYR A C     1 
ATOM   11166 O  O     . TYR A 1 1632 ? 133.584 168.315 193.126 1.00 124.98 ? 2849 TYR A O     1 
ATOM   11167 C  CB    . TYR A 1 1632 ? 135.197 168.799 190.273 1.00 120.55 ? 2849 TYR A CB    1 
ATOM   11168 C  CG    . TYR A 1 1632 ? 135.950 169.716 191.207 1.00 119.38 ? 2849 TYR A CG    1 
ATOM   11169 C  CD1   . TYR A 1 1632 ? 137.115 169.297 191.834 1.00 119.49 ? 2849 TYR A CD1   1 
ATOM   11170 C  CD2   . TYR A 1 1632 ? 135.516 171.016 191.430 1.00 117.18 ? 2849 TYR A CD2   1 
ATOM   11171 C  CE1   . TYR A 1 1632 ? 137.814 170.139 192.679 1.00 117.78 ? 2849 TYR A CE1   1 
ATOM   11172 C  CE2   . TYR A 1 1632 ? 136.210 171.866 192.268 1.00 113.68 ? 2849 TYR A CE2   1 
ATOM   11173 C  CZ    . TYR A 1 1632 ? 137.356 171.423 192.893 1.00 112.15 ? 2849 TYR A CZ    1 
ATOM   11174 O  OH    . TYR A 1 1632 ? 138.048 172.266 193.731 1.00 104.04 ? 2849 TYR A OH    1 
ATOM   11175 N  N     . ASP A 1 1633 ? 132.214 168.721 191.380 1.00 128.89 ? 2850 ASP A N     1 
ATOM   11176 C  CA    . ASP A 1 1633 ? 131.147 169.232 192.235 1.00 127.38 ? 2850 ASP A CA    1 
ATOM   11177 C  C     . ASP A 1 1633 ? 130.586 168.138 193.138 1.00 127.20 ? 2850 ASP A C     1 
ATOM   11178 O  O     . ASP A 1 1633 ? 130.317 168.377 194.322 1.00 125.60 ? 2850 ASP A O     1 
ATOM   11179 C  CB    . ASP A 1 1633 ? 130.037 169.843 191.379 1.00 125.64 ? 2850 ASP A CB    1 
ATOM   11180 N  N     . LYS A 1 1634 ? 130.405 166.931 192.594 1.00 126.77 ? 2851 LYS A N     1 
ATOM   11181 C  CA    . LYS A 1 1634 ? 129.928 165.808 193.397 1.00 127.60 ? 2851 LYS A CA    1 
ATOM   11182 C  C     . LYS A 1 1634 ? 130.926 165.446 194.490 1.00 128.00 ? 2851 LYS A C     1 
ATOM   11183 O  O     . LYS A 1 1634 ? 130.534 165.144 195.624 1.00 128.24 ? 2851 LYS A O     1 
ATOM   11184 C  CB    . LYS A 1 1634 ? 129.659 164.602 192.497 1.00 127.36 ? 2851 LYS A CB    1 
ATOM   11185 C  CG    . LYS A 1 1634 ? 129.040 163.412 193.210 1.00 128.12 ? 2851 LYS A CG    1 
ATOM   11186 C  CD    . LYS A 1 1634 ? 127.560 163.628 193.461 1.00 128.48 ? 2851 LYS A CD    1 
ATOM   11187 C  CE    . LYS A 1 1634 ? 126.783 163.646 192.155 1.00 130.50 ? 2851 LYS A CE    1 
ATOM   11188 N  NZ    . LYS A 1 1634 ? 126.869 162.343 191.440 1.00 127.88 ? 2851 LYS A NZ    1 
ATOM   11189 N  N     . LEU A 1 1635 ? 132.221 165.468 194.163 1.00 127.07 ? 2852 LEU A N     1 
ATOM   11190 C  CA    . LEU A 1 1635 ? 133.248 165.182 195.160 1.00 126.22 ? 2852 LEU A CA    1 
ATOM   11191 C  C     . LEU A 1 1635 ? 133.247 166.224 196.271 1.00 125.84 ? 2852 LEU A C     1 
ATOM   11192 O  O     . LEU A 1 1635 ? 133.358 165.878 197.453 1.00 125.82 ? 2852 LEU A O     1 
ATOM   11193 C  CB    . LEU A 1 1635 ? 134.621 165.110 194.492 1.00 127.83 ? 2852 LEU A CB    1 
ATOM   11194 N  N     . LEU A 1 1636 ? 133.119 167.505 195.913 1.00 126.81 ? 2853 LEU A N     1 
ATOM   11195 C  CA    . LEU A 1 1636 ? 133.057 168.549 196.933 1.00 126.45 ? 2853 LEU A CA    1 
ATOM   11196 C  C     . LEU A 1 1636 ? 131.811 168.407 197.798 1.00 127.28 ? 2853 LEU A C     1 
ATOM   11197 O  O     . LEU A 1 1636 ? 131.865 168.618 199.016 1.00 125.95 ? 2853 LEU A O     1 
ATOM   11198 C  CB    . LEU A 1 1636 ? 133.102 169.933 196.288 1.00 125.44 ? 2853 LEU A CB    1 
ATOM   11199 C  CG    . LEU A 1 1636 ? 134.450 170.411 195.749 1.00 120.00 ? 2853 LEU A CG    1 
ATOM   11200 C  CD1   . LEU A 1 1636 ? 134.323 171.840 195.256 1.00 115.34 ? 2853 LEU A CD1   1 
ATOM   11201 C  CD2   . LEU A 1 1636 ? 135.532 170.299 196.809 1.00 115.92 ? 2853 LEU A CD2   1 
ATOM   11202 N  N     . ASN A 1 1637 ? 130.677 168.051 197.187 1.00 127.97 ? 2854 ASN A N     1 
ATOM   11203 C  CA    . ASN A 1 1637 ? 129.454 167.840 197.955 1.00 126.04 ? 2854 ASN A CA    1 
ATOM   11204 C  C     . ASN A 1 1637 ? 129.602 166.673 198.925 1.00 126.81 ? 2854 ASN A C     1 
ATOM   11205 O  O     . ASN A 1 1637 ? 129.147 166.749 200.072 1.00 128.24 ? 2854 ASN A O     1 
ATOM   11206 C  CB    . ASN A 1 1637 ? 128.274 167.607 197.011 1.00 122.20 ? 2854 ASN A CB    1 
ATOM   11207 N  N     . ASN A 1 1638 ? 130.242 165.587 198.484 1.00 127.33 ? 2855 ASN A N     1 
ATOM   11208 C  CA    . ASN A 1 1638 ? 130.443 164.440 199.366 1.00 127.37 ? 2855 ASN A CA    1 
ATOM   11209 C  C     . ASN A 1 1638 ? 131.421 164.765 200.491 1.00 125.25 ? 2855 ASN A C     1 
ATOM   11210 O  O     . ASN A 1 1638 ? 131.241 164.306 201.626 1.00 123.75 ? 2855 ASN A O     1 
ATOM   11211 C  CB    . ASN A 1 1638 ? 130.923 163.235 198.559 1.00 127.53 ? 2855 ASN A CB    1 
ATOM   11212 C  CG    . ASN A 1 1638 ? 129.784 162.509 197.866 1.00 127.80 ? 2855 ASN A CG    1 
ATOM   11213 O  OD1   . ASN A 1 1638 ? 129.626 162.594 196.649 1.00 127.46 ? 2855 ASN A OD1   1 
ATOM   11214 N  ND2   . ASN A 1 1638 ? 128.983 161.789 198.643 1.00 126.04 ? 2855 ASN A ND2   1 
ATOM   11215 N  N     . LEU A 1 1639 ? 132.464 165.548 200.197 1.00 125.28 ? 2856 LEU A N     1 
ATOM   11216 C  CA    . LEU A 1 1639 ? 133.374 165.995 201.249 1.00 122.80 ? 2856 LEU A CA    1 
ATOM   11217 C  C     . LEU A 1 1639 ? 132.660 166.883 202.262 1.00 122.29 ? 2856 LEU A C     1 
ATOM   11218 O  O     . LEU A 1 1639 ? 132.911 166.786 203.468 1.00 122.21 ? 2856 LEU A O     1 
ATOM   11219 C  CB    . LEU A 1 1639 ? 134.571 166.731 200.643 1.00 119.34 ? 2856 LEU A CB    1 
ATOM   11220 C  CG    . LEU A 1 1639 ? 135.882 165.962 200.440 1.00 108.91 ? 2856 LEU A CG    1 
ATOM   11221 C  CD1   . LEU A 1 1639 ? 135.772 164.910 199.352 1.00 107.98 ? 2856 LEU A CD1   1 
ATOM   11222 C  CD2   . LEU A 1 1639 ? 137.014 166.930 200.132 1.00 101.59 ? 2856 LEU A CD2   1 
ATOM   11223 N  N     . ARG A 1 1640 ? 131.772 167.761 201.788 1.00 125.05 ? 2857 ARG A N     1 
ATOM   11224 C  CA    . ARG A 1 1640 ? 131.014 168.613 202.700 1.00 129.03 ? 2857 ARG A CA    1 
ATOM   11225 C  C     . ARG A 1 1640 ? 130.045 167.797 203.549 1.00 126.67 ? 2857 ARG A C     1 
ATOM   11226 O  O     . ARG A 1 1640 ? 129.860 168.084 204.737 1.00 125.77 ? 2857 ARG A O     1 
ATOM   11227 C  CB    . ARG A 1 1640 ? 130.264 169.686 201.910 1.00 129.42 ? 2857 ARG A CB    1 
ATOM   11228 C  CG    . ARG A 1 1640 ? 131.148 170.810 201.398 1.00 127.87 ? 2857 ARG A CG    1 
ATOM   11229 C  CD    . ARG A 1 1640 ? 130.396 171.712 200.432 1.00 124.86 ? 2857 ARG A CD    1 
ATOM   11230 N  NE    . ARG A 1 1640 ? 131.297 172.429 199.538 1.00 125.86 ? 2857 ARG A NE    1 
ATOM   11231 C  CZ    . ARG A 1 1640 ? 131.973 173.521 199.870 1.00 124.16 ? 2857 ARG A CZ    1 
ATOM   11232 N  NH1   . ARG A 1 1640 ? 131.868 174.062 201.073 1.00 120.10 ? 2857 ARG A NH1   1 
ATOM   11233 N  NH2   . ARG A 1 1640 ? 132.774 174.086 198.971 1.00 121.30 ? 2857 ARG A NH2   1 
ATOM   11234 N  N     . ASN A 1 1641 ? 129.411 166.784 202.953 1.00 124.62 ? 2858 ASN A N     1 
ATOM   11235 C  CA    . ASN A 1 1641 ? 128.474 165.951 203.701 1.00 124.64 ? 2858 ASN A CA    1 
ATOM   11236 C  C     . ASN A 1 1641 ? 129.191 165.099 204.742 1.00 125.08 ? 2858 ASN A C     1 
ATOM   11237 O  O     . ASN A 1 1641 ? 128.702 164.945 205.867 1.00 124.30 ? 2858 ASN A O     1 
ATOM   11238 C  CB    . ASN A 1 1641 ? 127.679 165.063 202.743 1.00 125.18 ? 2858 ASN A CB    1 
ATOM   11239 C  CG    . ASN A 1 1641 ? 126.761 165.859 201.837 1.00 126.51 ? 2858 ASN A CG    1 
ATOM   11240 O  OD1   . ASN A 1 1641 ? 126.177 166.861 202.249 1.00 125.60 ? 2858 ASN A OD1   1 
ATOM   11241 N  ND2   . ASN A 1 1641 ? 126.629 165.414 200.592 1.00 127.01 ? 2858 ASN A ND2   1 
ATOM   11242 N  N     . LYS A 1 1642 ? 130.347 164.533 204.385 1.00 125.75 ? 2859 LYS A N     1 
ATOM   11243 C  CA    . LYS A 1 1642 ? 131.069 163.681 205.325 1.00 125.62 ? 2859 LYS A CA    1 
ATOM   11244 C  C     . LYS A 1 1642 ? 131.717 164.498 206.436 1.00 125.55 ? 2859 LYS A C     1 
ATOM   11245 O  O     . LYS A 1 1642 ? 131.635 164.128 207.614 1.00 125.67 ? 2859 LYS A O     1 
ATOM   11246 C  CB    . LYS A 1 1642 ? 132.119 162.856 204.583 1.00 123.85 ? 2859 LYS A CB    1 
ATOM   11247 N  N     . THR A 1 1643 ? 132.359 165.607 206.087 1.00 125.75 ? 2860 THR A N     1 
ATOM   11248 C  CA    . THR A 1 1643 ? 133.047 166.435 207.072 1.00 125.02 ? 2860 THR A CA    1 
ATOM   11249 C  C     . THR A 1 1643 ? 132.104 167.472 207.674 1.00 125.04 ? 2860 THR A C     1 
ATOM   11250 O  O     . THR A 1 1643 ? 132.081 167.674 208.888 1.00 123.78 ? 2860 THR A O     1 
ATOM   11251 C  CB    . THR A 1 1643 ? 134.264 167.153 206.454 1.00 120.70 ? 2860 THR A CB    1 
ATOM   11252 O  OG1   . THR A 1 1643 ? 135.026 166.224 205.674 1.00 111.64 ? 2860 THR A OG1   1 
ATOM   11253 C  CG2   . THR A 1 1643 ? 135.151 167.739 207.542 1.00 115.58 ? 2860 THR A CG2   1 
ATOM   11254 N  N     . THR A 1 1652 ? 135.731 176.372 202.558 1.00 93.85  ? 2869 THR A N     1 
ATOM   11255 C  CA    . THR A 1 1652 ? 137.010 176.690 201.936 1.00 93.53  ? 2869 THR A CA    1 
ATOM   11256 C  C     . THR A 1 1652 ? 137.421 175.605 200.946 1.00 98.91  ? 2869 THR A C     1 
ATOM   11257 O  O     . THR A 1 1652 ? 137.702 174.468 201.337 1.00 101.50 ? 2869 THR A O     1 
ATOM   11258 C  CB    . THR A 1 1652 ? 138.122 176.865 202.986 1.00 88.68  ? 2869 THR A CB    1 
ATOM   11259 N  N     . GLU A 1 1653 ? 137.448 175.968 199.660 1.00 98.57  ? 2870 GLU A N     1 
ATOM   11260 C  CA    . GLU A 1 1653 ? 137.819 175.011 198.622 1.00 97.85  ? 2870 GLU A CA    1 
ATOM   11261 C  C     . GLU A 1 1653 ? 139.268 174.566 198.769 1.00 95.61  ? 2870 GLU A C     1 
ATOM   11262 O  O     . GLU A 1 1653 ? 139.584 173.387 198.571 1.00 95.71  ? 2870 GLU A O     1 
ATOM   11263 C  CB    . GLU A 1 1653 ? 137.584 175.616 197.238 1.00 96.58  ? 2870 GLU A CB    1 
ATOM   11264 C  CG    . GLU A 1 1653 ? 137.603 174.598 196.110 1.00 95.68  ? 2870 GLU A CG    1 
ATOM   11265 C  CD    . GLU A 1 1653 ? 137.653 175.246 194.741 1.00 97.98  ? 2870 GLU A CD    1 
ATOM   11266 O  OE1   . GLU A 1 1653 ? 137.980 176.448 194.661 1.00 97.02  ? 2870 GLU A OE1   1 
ATOM   11267 O  OE2   . GLU A 1 1653 ? 137.366 174.552 193.744 1.00 102.30 ? 2870 GLU A OE2   1 
ATOM   11268 N  N     . GLN A 1 1654 ? 140.162 175.498 199.112 1.00 93.83  ? 2871 GLN A N     1 
ATOM   11269 C  CA    . GLN A 1 1654 ? 141.567 175.146 199.300 1.00 91.02  ? 2871 GLN A CA    1 
ATOM   11270 C  C     . GLN A 1 1654 ? 141.746 174.171 200.457 1.00 92.43  ? 2871 GLN A C     1 
ATOM   11271 O  O     . GLN A 1 1654 ? 142.486 173.189 200.337 1.00 95.13  ? 2871 GLN A O     1 
ATOM   11272 C  CB    . GLN A 1 1654 ? 142.398 176.408 199.532 1.00 95.69  ? 2871 GLN A CB    1 
ATOM   11273 C  CG    . GLN A 1 1654 ? 143.879 176.233 199.247 1.00 99.15  ? 2871 GLN A CG    1 
ATOM   11274 C  CD    . GLN A 1 1654 ? 144.740 177.203 200.031 1.00 104.29 ? 2871 GLN A CD    1 
ATOM   11275 O  OE1   . GLN A 1 1654 ? 144.871 177.090 201.250 1.00 101.99 ? 2871 GLN A OE1   1 
ATOM   11276 N  NE2   . GLN A 1 1654 ? 145.333 178.165 199.333 1.00 105.20 ? 2871 GLN A NE2   1 
ATOM   11277 N  N     . GLU A 1 1655 ? 141.067 174.417 201.580 1.00 93.93  ? 2872 GLU A N     1 
ATOM   11278 C  CA    . GLU A 1 1655 ? 141.171 173.514 202.724 1.00 93.94  ? 2872 GLU A CA    1 
ATOM   11279 C  C     . GLU A 1 1655 ? 140.554 172.155 202.418 1.00 94.89  ? 2872 GLU A C     1 
ATOM   11280 O  O     . GLU A 1 1655 ? 141.093 171.117 202.825 1.00 97.17  ? 2872 GLU A O     1 
ATOM   11281 C  CB    . GLU A 1 1655 ? 140.509 174.140 203.950 1.00 92.87  ? 2872 GLU A CB    1 
ATOM   11282 N  N     . LEU A 1 1656 ? 139.421 172.140 201.709 1.00 93.88  ? 2873 LEU A N     1 
ATOM   11283 C  CA    . LEU A 1 1656 ? 138.793 170.873 201.344 1.00 93.02  ? 2873 LEU A CA    1 
ATOM   11284 C  C     . LEU A 1 1656 ? 139.687 170.058 200.417 1.00 91.58  ? 2873 LEU A C     1 
ATOM   11285 O  O     . LEU A 1 1656 ? 139.841 168.844 200.598 1.00 93.16  ? 2873 LEU A O     1 
ATOM   11286 C  CB    . LEU A 1 1656 ? 137.435 171.130 200.693 1.00 96.42  ? 2873 LEU A CB    1 
ATOM   11287 C  CG    . LEU A 1 1656 ? 136.268 171.360 201.655 1.00 98.85  ? 2873 LEU A CG    1 
ATOM   11288 C  CD1   . LEU A 1 1656 ? 135.172 172.176 200.988 1.00 104.22 ? 2873 LEU A CD1   1 
ATOM   11289 C  CD2   . LEU A 1 1656 ? 135.724 170.033 202.157 1.00 102.67 ? 2873 LEU A CD2   1 
ATOM   11290 N  N     . TYR A 1 1657 ? 140.305 170.712 199.430 1.00 90.13  ? 2874 TYR A N     1 
ATOM   11291 C  CA    . TYR A 1 1657 ? 141.211 169.999 198.537 1.00 87.53  ? 2874 TYR A CA    1 
ATOM   11292 C  C     . TYR A 1 1657 ? 142.480 169.564 199.257 1.00 88.73  ? 2874 TYR A C     1 
ATOM   11293 O  O     . TYR A 1 1657 ? 143.036 168.510 198.935 1.00 90.19  ? 2874 TYR A O     1 
ATOM   11294 C  CB    . TYR A 1 1657 ? 141.554 170.866 197.327 1.00 86.76  ? 2874 TYR A CB    1 
ATOM   11295 C  CG    . TYR A 1 1657 ? 142.149 170.084 196.180 1.00 86.25  ? 2874 TYR A CG    1 
ATOM   11296 C  CD1   . TYR A 1 1657 ? 141.336 169.371 195.309 1.00 86.01  ? 2874 TYR A CD1   1 
ATOM   11297 C  CD2   . TYR A 1 1657 ? 143.521 170.053 195.972 1.00 89.00  ? 2874 TYR A CD2   1 
ATOM   11298 C  CE1   . TYR A 1 1657 ? 141.873 168.652 194.259 1.00 85.21  ? 2874 TYR A CE1   1 
ATOM   11299 C  CE2   . TYR A 1 1657 ? 144.067 169.335 194.924 1.00 89.18  ? 2874 TYR A CE2   1 
ATOM   11300 C  CZ    . TYR A 1 1657 ? 143.238 168.638 194.072 1.00 88.87  ? 2874 TYR A CZ    1 
ATOM   11301 O  OH    . TYR A 1 1657 ? 143.776 167.923 193.028 1.00 94.36  ? 2874 TYR A OH    1 
ATOM   11302 N  N     . ASP A 1 1658 ? 142.950 170.352 200.229 1.00 88.77  ? 2875 ASP A N     1 
ATOM   11303 C  CA    . ASP A 1 1658 ? 144.107 169.948 201.020 1.00 82.62  ? 2875 ASP A CA    1 
ATOM   11304 C  C     . ASP A 1 1658 ? 143.805 168.702 201.843 1.00 82.15  ? 2875 ASP A C     1 
ATOM   11305 O  O     . ASP A 1 1658 ? 144.632 167.786 201.923 1.00 80.95  ? 2875 ASP A O     1 
ATOM   11306 C  CB    . ASP A 1 1658 ? 144.545 171.098 201.927 1.00 86.74  ? 2875 ASP A CB    1 
ATOM   11307 C  CG    . ASP A 1 1658 ? 146.023 171.055 202.255 1.00 83.78  ? 2875 ASP A CG    1 
ATOM   11308 O  OD1   . ASP A 1 1658 ? 146.603 169.949 202.266 1.00 83.42  ? 2875 ASP A OD1   1 
ATOM   11309 O  OD2   . ASP A 1 1658 ? 146.607 172.130 202.506 1.00 83.55  ? 2875 ASP A OD2   1 
ATOM   11310 N  N     . TRP A 1 1659 ? 142.619 168.643 202.456 1.00 84.71  ? 2876 TRP A N     1 
ATOM   11311 C  CA    . TRP A 1 1659 ? 142.239 167.441 203.192 1.00 83.78  ? 2876 TRP A CA    1 
ATOM   11312 C  C     . TRP A 1 1659 ? 142.033 166.254 202.259 1.00 88.74  ? 2876 TRP A C     1 
ATOM   11313 O  O     . TRP A 1 1659 ? 142.335 165.116 202.635 1.00 91.59  ? 2876 TRP A O     1 
ATOM   11314 C  CB    . TRP A 1 1659 ? 140.975 167.688 204.013 1.00 87.97  ? 2876 TRP A CB    1 
ATOM   11315 C  CG    . TRP A 1 1659 ? 140.504 166.466 204.743 1.00 90.44  ? 2876 TRP A CG    1 
ATOM   11316 C  CD1   . TRP A 1 1659 ? 140.900 166.050 205.980 1.00 88.70  ? 2876 TRP A CD1   1 
ATOM   11317 C  CD2   . TRP A 1 1659 ? 139.557 165.497 204.278 1.00 90.78  ? 2876 TRP A CD2   1 
ATOM   11318 N  NE1   . TRP A 1 1659 ? 140.256 164.884 206.316 1.00 88.21  ? 2876 TRP A NE1   1 
ATOM   11319 C  CE2   . TRP A 1 1659 ? 139.426 164.523 205.287 1.00 90.31  ? 2876 TRP A CE2   1 
ATOM   11320 C  CE3   . TRP A 1 1659 ? 138.806 165.358 203.106 1.00 90.38  ? 2876 TRP A CE3   1 
ATOM   11321 C  CZ2   . TRP A 1 1659 ? 138.575 163.428 205.162 1.00 90.17  ? 2876 TRP A CZ2   1 
ATOM   11322 C  CZ3   . TRP A 1 1659 ? 137.962 164.270 202.984 1.00 91.43  ? 2876 TRP A CZ3   1 
ATOM   11323 C  CH2   . TRP A 1 1659 ? 137.853 163.320 204.005 1.00 88.87  ? 2876 TRP A CH2   1 
ATOM   11324 N  N     . PHE A 1 1660 ? 141.513 166.495 201.052 1.00 90.20  ? 2877 PHE A N     1 
ATOM   11325 C  CA    . PHE A 1 1660 ? 141.379 165.424 200.067 1.00 88.88  ? 2877 PHE A CA    1 
ATOM   11326 C  C     . PHE A 1 1660 ? 142.743 164.869 199.668 1.00 86.50  ? 2877 PHE A C     1 
ATOM   11327 O  O     . PHE A 1 1660 ? 142.933 163.648 199.588 1.00 89.76  ? 2877 PHE A O     1 
ATOM   11328 C  CB    . PHE A 1 1660 ? 140.627 165.953 198.845 1.00 92.88  ? 2877 PHE A CB    1 
ATOM   11329 C  CG    . PHE A 1 1660 ? 140.213 164.891 197.874 1.00 97.85  ? 2877 PHE A CG    1 
ATOM   11330 C  CD1   . PHE A 1 1660 ? 139.384 163.855 198.269 1.00 101.43 ? 2877 PHE A CD1   1 
ATOM   11331 C  CD2   . PHE A 1 1660 ? 140.635 164.941 196.557 1.00 98.75  ? 2877 PHE A CD2   1 
ATOM   11332 C  CE1   . PHE A 1 1660 ? 138.995 162.880 197.371 1.00 102.99 ? 2877 PHE A CE1   1 
ATOM   11333 C  CE2   . PHE A 1 1660 ? 140.249 163.973 195.654 1.00 100.09 ? 2877 PHE A CE2   1 
ATOM   11334 C  CZ    . PHE A 1 1660 ? 139.428 162.939 196.062 1.00 102.47 ? 2877 PHE A CZ    1 
ATOM   11335 N  N     . VAL A 1 1661 ? 143.708 165.761 199.436 1.00 84.84  ? 2878 VAL A N     1 
ATOM   11336 C  CA    . VAL A 1 1661 ? 145.077 165.357 199.130 1.00 86.27  ? 2878 VAL A CA    1 
ATOM   11337 C  C     . VAL A 1 1661 ? 145.675 164.570 200.290 1.00 89.25  ? 2878 VAL A C     1 
ATOM   11338 O  O     . VAL A 1 1661 ? 146.326 163.537 200.087 1.00 93.48  ? 2878 VAL A O     1 
ATOM   11339 C  CB    . VAL A 1 1661 ? 145.919 166.600 198.781 1.00 85.89  ? 2878 VAL A CB    1 
ATOM   11340 C  CG1   . VAL A 1 1661 ? 147.402 166.313 198.890 1.00 77.75  ? 2878 VAL A CG1   1 
ATOM   11341 C  CG2   . VAL A 1 1661 ? 145.580 167.086 197.382 1.00 88.41  ? 2878 VAL A CG2   1 
ATOM   11342 N  N     . GLY A 1 1662 ? 145.450 165.033 201.521 1.00 89.09  ? 2879 GLY A N     1 
ATOM   11343 C  CA    . GLY A 1 1662 ? 145.984 164.332 202.679 1.00 82.75  ? 2879 GLY A CA    1 
ATOM   11344 C  C     . GLY A 1 1662 ? 145.395 162.945 202.861 1.00 81.23  ? 2879 GLY A C     1 
ATOM   11345 O  O     . GLY A 1 1662 ? 146.117 161.986 203.146 1.00 82.59  ? 2879 GLY A O     1 
ATOM   11346 N  N     . GLU A 1 1663 ? 144.077 162.813 202.683 1.00 83.80  ? 2880 GLU A N     1 
ATOM   11347 C  CA    . GLU A 1 1663 ? 143.458 161.506 202.871 1.00 86.79  ? 2880 GLU A CA    1 
ATOM   11348 C  C     . GLU A 1 1663 ? 143.813 160.555 201.736 1.00 90.45  ? 2880 GLU A C     1 
ATOM   11349 O  O     . GLU A 1 1663 ? 143.880 159.341 201.953 1.00 91.82  ? 2880 GLU A O     1 
ATOM   11350 C  CB    . GLU A 1 1663 ? 141.938 161.637 203.023 1.00 90.72  ? 2880 GLU A CB    1 
ATOM   11351 C  CG    . GLU A 1 1663 ? 141.173 162.128 201.801 1.00 92.13  ? 2880 GLU A CG    1 
ATOM   11352 C  CD    . GLU A 1 1663 ? 140.720 160.994 200.895 1.00 90.31  ? 2880 GLU A CD    1 
ATOM   11353 O  OE1   . GLU A 1 1663 ? 140.648 159.843 201.373 1.00 92.49  ? 2880 GLU A OE1   1 
ATOM   11354 O  OE2   . GLU A 1 1663 ? 140.437 161.252 199.708 1.00 88.79  ? 2880 GLU A OE2   1 
ATOM   11355 N  N     . ILE A 1 1664 ? 144.059 161.074 200.529 1.00 91.57  ? 2881 ILE A N     1 
ATOM   11356 C  CA    . ILE A 1 1664 ? 144.570 160.210 199.468 1.00 88.24  ? 2881 ILE A CA    1 
ATOM   11357 C  C     . ILE A 1 1664 ? 145.995 159.766 199.781 1.00 88.68  ? 2881 ILE A C     1 
ATOM   11358 O  O     . ILE A 1 1664 ? 146.327 158.581 199.659 1.00 91.29  ? 2881 ILE A O     1 
ATOM   11359 C  CB    . ILE A 1 1664 ? 144.478 160.911 198.101 1.00 90.10  ? 2881 ILE A CB    1 
ATOM   11360 C  CG1   . ILE A 1 1664 ? 143.029 160.945 197.620 1.00 99.98  ? 2881 ILE A CG1   1 
ATOM   11361 C  CG2   . ILE A 1 1664 ? 145.334 160.198 197.070 1.00 84.84  ? 2881 ILE A CG2   1 
ATOM   11362 C  CD1   . ILE A 1 1664 ? 142.849 161.666 196.310 1.00 102.31 ? 2881 ILE A CD1   1 
ATOM   11363 N  N     . ALA A 1 1665 ? 146.852 160.699 200.212 1.00 88.35  ? 2882 ALA A N     1 
ATOM   11364 C  CA    . ALA A 1 1665 ? 148.240 160.358 200.515 1.00 88.44  ? 2882 ALA A CA    1 
ATOM   11365 C  C     . ALA A 1 1665 ? 148.349 159.407 201.701 1.00 89.98  ? 2882 ALA A C     1 
ATOM   11366 O  O     . ALA A 1 1665 ? 149.345 158.687 201.828 1.00 85.73  ? 2882 ALA A O     1 
ATOM   11367 C  CB    . ALA A 1 1665 ? 149.047 161.627 200.785 1.00 83.47  ? 2882 ALA A CB    1 
ATOM   11368 N  N     . LYS A 1 1666 ? 147.349 159.394 202.578 1.00 91.17  ? 2883 LYS A N     1 
ATOM   11369 C  CA    . LYS A 1 1666 ? 147.355 158.451 203.688 1.00 86.91  ? 2883 LYS A CA    1 
ATOM   11370 C  C     . LYS A 1 1666 ? 146.622 157.154 203.375 1.00 87.40  ? 2883 LYS A C     1 
ATOM   11371 O  O     . LYS A 1 1666 ? 146.894 156.134 204.017 1.00 92.62  ? 2883 LYS A O     1 
ATOM   11372 C  CB    . LYS A 1 1666 ? 146.735 159.094 204.932 1.00 89.22  ? 2883 LYS A CB    1 
ATOM   11373 C  CG    . LYS A 1 1666 ? 147.707 159.930 205.750 1.00 84.67  ? 2883 LYS A CG    1 
ATOM   11374 C  CD    . LYS A 1 1666 ? 147.065 160.442 207.032 1.00 86.60  ? 2883 LYS A CD    1 
ATOM   11375 C  CE    . LYS A 1 1666 ? 146.397 159.317 207.810 1.00 92.73  ? 2883 LYS A CE    1 
ATOM   11376 N  NZ    . LYS A 1 1666 ? 145.471 159.833 208.856 1.00 89.96  ? 2883 LYS A NZ    1 
ATOM   11377 N  N     . ASN A 1 1667 ? 145.708 157.158 202.405 1.00 87.88  ? 2884 ASN A N     1 
ATOM   11378 C  CA    . ASN A 1 1667 ? 144.807 156.034 202.157 1.00 92.89  ? 2884 ASN A CA    1 
ATOM   11379 C  C     . ASN A 1 1667 ? 144.803 155.642 200.682 1.00 95.71  ? 2884 ASN A C     1 
ATOM   11380 O  O     . ASN A 1 1667 ? 143.748 155.469 200.067 1.00 99.45  ? 2884 ASN A O     1 
ATOM   11381 C  CB    . ASN A 1 1667 ? 143.383 156.360 202.609 1.00 92.01  ? 2884 ASN A CB    1 
ATOM   11382 C  CG    . ASN A 1 1667 ? 143.260 156.517 204.114 1.00 89.69  ? 2884 ASN A CG    1 
ATOM   11383 O  OD1   . ASN A 1 1667 ? 144.167 156.169 204.868 1.00 90.43  ? 2884 ASN A OD1   1 
ATOM   11384 N  ND2   . ASN A 1 1667 ? 142.125 157.044 204.559 1.00 89.01  ? 2884 ASN A ND2   1 
ATOM   11385 N  N     . LEU A 1 1668 ? 145.984 155.500 200.084 1.00 91.64  ? 2885 LEU A N     1 
ATOM   11386 C  CA    . LEU A 1 1668 ? 146.075 154.956 198.733 1.00 87.49  ? 2885 LEU A CA    1 
ATOM   11387 C  C     . LEU A 1 1668 ? 147.399 154.227 198.580 1.00 80.89  ? 2885 LEU A C     1 
ATOM   11388 O  O     . LEU A 1 1668 ? 148.458 154.800 198.852 1.00 80.62  ? 2885 LEU A O     1 
ATOM   11389 C  CB    . LEU A 1 1668 ? 145.943 156.054 197.669 1.00 85.76  ? 2885 LEU A CB    1 
ATOM   11390 C  CG    . LEU A 1 1668 ? 145.731 155.593 196.223 1.00 80.93  ? 2885 LEU A CG    1 
ATOM   11391 C  CD1   . LEU A 1 1668 ? 144.698 156.469 195.534 1.00 83.07  ? 2885 LEU A CD1   1 
ATOM   11392 C  CD2   . LEU A 1 1668 ? 147.033 155.603 195.436 1.00 75.99  ? 2885 LEU A CD2   1 
ATOM   11393 N  N     . HIS A 1 1669 ? 147.334 152.971 198.136 1.00 75.10  ? 2886 HIS A N     1 
ATOM   11394 C  CA    . HIS A 1 1669 ? 148.524 152.142 197.942 1.00 69.27  ? 2886 HIS A CA    1 
ATOM   11395 C  C     . HIS A 1 1669 ? 148.353 151.339 196.656 1.00 73.23  ? 2886 HIS A C     1 
ATOM   11396 O  O     . HIS A 1 1669 ? 147.721 150.280 196.659 1.00 83.28  ? 2886 HIS A O     1 
ATOM   11397 C  CB    . HIS A 1 1669 ? 148.758 151.222 199.134 1.00 68.73  ? 2886 HIS A CB    1 
ATOM   11398 C  CG    . HIS A 1 1669 ? 149.047 151.944 200.413 1.00 67.42  ? 2886 HIS A CG    1 
ATOM   11399 N  ND1   . HIS A 1 1669 ? 150.316 152.345 200.771 1.00 59.48  ? 2886 HIS A ND1   1 
ATOM   11400 C  CD2   . HIS A 1 1669 ? 148.234 152.320 201.428 1.00 72.32  ? 2886 HIS A CD2   1 
ATOM   11401 C  CE1   . HIS A 1 1669 ? 150.272 152.946 201.946 1.00 59.38  ? 2886 HIS A CE1   1 
ATOM   11402 N  NE2   . HIS A 1 1669 ? 149.020 152.943 202.367 1.00 68.89  ? 2886 HIS A NE2   1 
ATOM   11403 N  N     . VAL A 1 1670 ? 148.923 151.842 195.563 1.00 71.21  ? 2887 VAL A N     1 
ATOM   11404 C  CA    . VAL A 1 1670 ? 148.971 151.129 194.291 1.00 75.86  ? 2887 VAL A CA    1 
ATOM   11405 C  C     . VAL A 1 1670 ? 150.358 150.519 194.138 1.00 77.96  ? 2887 VAL A C     1 
ATOM   11406 O  O     . VAL A 1 1670 ? 151.369 151.151 194.472 1.00 79.12  ? 2887 VAL A O     1 
ATOM   11407 C  CB    . VAL A 1 1670 ? 148.614 152.061 193.112 1.00 73.42  ? 2887 VAL A CB    1 
ATOM   11408 C  CG1   . VAL A 1 1670 ? 149.540 153.269 193.049 1.00 73.53  ? 2887 VAL A CG1   1 
ATOM   11409 C  CG2   . VAL A 1 1670 ? 148.643 151.306 191.793 1.00 73.29  ? 2887 VAL A CG2   1 
ATOM   11410 N  N     . VAL A 1 1671 ? 150.413 149.272 193.674 1.00 77.85  ? 2888 VAL A N     1 
ATOM   11411 C  CA    . VAL A 1 1671 ? 151.671 148.541 193.597 1.00 73.86  ? 2888 VAL A CA    1 
ATOM   11412 C  C     . VAL A 1 1671 ? 151.965 148.192 192.145 1.00 77.08  ? 2888 VAL A C     1 
ATOM   11413 O  O     . VAL A 1 1671 ? 151.058 148.048 191.318 1.00 78.18  ? 2888 VAL A O     1 
ATOM   11414 C  CB    . VAL A 1 1671 ? 151.650 147.267 194.469 1.00 72.18  ? 2888 VAL A CB    1 
ATOM   11415 C  CG1   . VAL A 1 1671 ? 151.441 147.628 195.932 1.00 68.63  ? 2888 VAL A CG1   1 
ATOM   11416 C  CG2   . VAL A 1 1671 ? 150.580 146.310 193.992 1.00 77.60  ? 2888 VAL A CG2   1 
ATOM   11417 N  N     . PHE A 1 1672 ? 153.253 148.072 191.836 1.00 73.69  ? 2889 PHE A N     1 
ATOM   11418 C  CA    . PHE A 1 1672 ? 153.715 147.657 190.519 1.00 76.80  ? 2889 PHE A CA    1 
ATOM   11419 C  C     . PHE A 1 1672 ? 154.535 146.383 190.647 1.00 82.37  ? 2889 PHE A C     1 
ATOM   11420 O  O     . PHE A 1 1672 ? 155.454 146.307 191.470 1.00 78.91  ? 2889 PHE A O     1 
ATOM   11421 C  CB    . PHE A 1 1672 ? 154.554 148.742 189.846 1.00 79.21  ? 2889 PHE A CB    1 
ATOM   11422 C  CG    . PHE A 1 1672 ? 153.760 149.918 189.362 1.00 82.76  ? 2889 PHE A CG    1 
ATOM   11423 C  CD1   . PHE A 1 1672 ? 152.766 149.753 188.413 1.00 83.80  ? 2889 PHE A CD1   1 
ATOM   11424 C  CD2   . PHE A 1 1672 ? 154.025 151.193 189.837 1.00 80.77  ? 2889 PHE A CD2   1 
ATOM   11425 C  CE1   . PHE A 1 1672 ? 152.039 150.834 187.959 1.00 86.22  ? 2889 PHE A CE1   1 
ATOM   11426 C  CE2   . PHE A 1 1672 ? 153.302 152.278 189.385 1.00 82.19  ? 2889 PHE A CE2   1 
ATOM   11427 C  CZ    . PHE A 1 1672 ? 152.308 152.098 188.445 1.00 87.69  ? 2889 PHE A CZ    1 
ATOM   11428 N  N     . THR A 1 1673 ? 154.203 145.395 189.826 1.00 88.43  ? 2890 THR A N     1 
ATOM   11429 C  CA    . THR A 1 1673 ? 154.901 144.116 189.779 1.00 82.59  ? 2890 THR A CA    1 
ATOM   11430 C  C     . THR A 1 1673 ? 155.656 144.046 188.457 1.00 86.51  ? 2890 THR A C     1 
ATOM   11431 O  O     . THR A 1 1673 ? 155.042 143.924 187.392 1.00 87.94  ? 2890 THR A O     1 
ATOM   11432 C  CB    . THR A 1 1673 ? 153.908 142.964 189.922 1.00 79.72  ? 2890 THR A CB    1 
ATOM   11433 O  OG1   . THR A 1 1673 ? 153.318 143.001 191.227 1.00 72.23  ? 2890 THR A OG1   1 
ATOM   11434 C  CG2   . THR A 1 1673 ? 154.591 141.631 189.711 1.00 75.59  ? 2890 THR A CG2   1 
ATOM   11435 N  N     . ILE A 1 1674 ? 156.983 144.136 188.522 1.00 81.40  ? 2891 ILE A N     1 
ATOM   11436 C  CA    . ILE A 1 1674 ? 157.825 144.147 187.332 1.00 83.18  ? 2891 ILE A CA    1 
ATOM   11437 C  C     . ILE A 1 1674 ? 158.868 143.045 187.443 1.00 80.73  ? 2891 ILE A C     1 
ATOM   11438 O  O     . ILE A 1 1674 ? 159.442 142.820 188.514 1.00 75.09  ? 2891 ILE A O     1 
ATOM   11439 C  CB    . ILE A 1 1674 ? 158.504 145.518 187.116 1.00 82.29  ? 2891 ILE A CB    1 
ATOM   11440 C  CG1   . ILE A 1 1674 ? 159.177 146.006 188.400 1.00 72.37  ? 2891 ILE A CG1   1 
ATOM   11441 C  CG2   . ILE A 1 1674 ? 157.496 146.539 186.614 1.00 83.98  ? 2891 ILE A CG2   1 
ATOM   11442 C  CD1   . ILE A 1 1674 ? 160.097 147.183 188.190 1.00 64.76  ? 2891 ILE A CD1   1 
ATOM   11443 N  N     . CYS A 1 1675 ? 159.100 142.347 186.331 1.00 86.97  ? 2892 CYS A N     1 
ATOM   11444 C  CA    . CYS A 1 1675 ? 160.137 141.328 186.233 1.00 83.84  ? 2892 CYS A CA    1 
ATOM   11445 C  C     . CYS A 1 1675 ? 161.386 141.842 185.528 1.00 86.32  ? 2892 CYS A C     1 
ATOM   11446 O  O     . CYS A 1 1675 ? 162.486 141.774 186.084 1.00 85.17  ? 2892 CYS A O     1 
ATOM   11447 C  CB    . CYS A 1 1675 ? 159.594 140.093 185.506 1.00 76.40  ? 2892 CYS A CB    1 
ATOM   11448 S  SG    . CYS A 1 1675 ? 158.200 139.298 186.333 1.00 62.48  ? 2892 CYS A SG    1 
ATOM   11449 N  N     . ASP A 1 1676 ? 161.234 142.359 184.310 1.00 90.38  ? 2893 ASP A N     1 
ATOM   11450 C  CA    . ASP A 1 1676 ? 162.351 142.909 183.559 1.00 93.24  ? 2893 ASP A CA    1 
ATOM   11451 C  C     . ASP A 1 1676 ? 162.441 144.401 183.833 1.00 97.51  ? 2893 ASP A C     1 
ATOM   11452 O  O     . ASP A 1 1676 ? 161.517 145.144 183.467 1.00 97.51  ? 2893 ASP A O     1 
ATOM   11453 C  CB    . ASP A 1 1676 ? 162.168 142.651 182.064 1.00 94.94  ? 2893 ASP A CB    1 
ATOM   11454 C  CG    . ASP A 1 1676 ? 163.434 142.897 181.266 1.00 102.23 ? 2893 ASP A CG    1 
ATOM   11455 O  OD1   . ASP A 1 1676 ? 164.486 143.177 181.877 1.00 104.22 ? 2893 ASP A OD1   1 
ATOM   11456 O  OD2   . ASP A 1 1676 ? 163.377 142.810 180.021 1.00 106.25 ? 2893 ASP A OD2   1 
ATOM   11457 N  N     . PRO A 1 1677 ? 163.515 144.892 184.471 1.00 98.48  ? 2894 PRO A N     1 
ATOM   11458 C  CA    . PRO A 1 1677 ? 163.686 146.324 184.744 1.00 99.99  ? 2894 PRO A CA    1 
ATOM   11459 C  C     . PRO A 1 1677 ? 163.918 147.139 183.474 1.00 100.02 ? 2894 PRO A C     1 
ATOM   11460 O  O     . PRO A 1 1677 ? 164.883 146.869 182.759 1.00 95.71  ? 2894 PRO A O     1 
ATOM   11461 C  CB    . PRO A 1 1677 ? 164.925 146.367 185.649 1.00 92.05  ? 2894 PRO A CB    1 
ATOM   11462 C  CG    . PRO A 1 1677 ? 165.085 144.971 186.164 1.00 89.78  ? 2894 PRO A CG    1 
ATOM   11463 C  CD    . PRO A 1 1677 ? 164.599 144.092 185.062 1.00 92.51  ? 2894 PRO A CD    1 
ATOM   11464 N  N     . LYS A 1 1681 ? 159.855 150.458 177.340 1.00 120.26 ? 2898 LYS A N     1 
ATOM   11465 C  CA    . LYS A 1 1681 ? 158.741 151.302 177.753 1.00 119.16 ? 2898 LYS A CA    1 
ATOM   11466 C  C     . LYS A 1 1681 ? 158.703 151.480 179.270 1.00 110.90 ? 2898 LYS A C     1 
ATOM   11467 O  O     . LYS A 1 1681 ? 158.320 152.538 179.769 1.00 108.69 ? 2898 LYS A O     1 
ATOM   11468 C  CB    . LYS A 1 1681 ? 157.416 150.719 177.246 1.00 120.40 ? 2898 LYS A CB    1 
ATOM   11469 C  CG    . LYS A 1 1681 ? 157.162 149.272 177.652 1.00 116.95 ? 2898 LYS A CG    1 
ATOM   11470 C  CD    . LYS A 1 1681 ? 155.853 148.751 177.082 1.00 113.29 ? 2898 LYS A CD    1 
ATOM   11471 C  CE    . LYS A 1 1681 ? 154.661 149.379 177.783 1.00 108.87 ? 2898 LYS A CE    1 
ATOM   11472 N  NZ    . LYS A 1 1681 ? 154.589 148.974 179.215 1.00 105.49 ? 2898 LYS A NZ    1 
ATOM   11473 N  N     . SER A 1 1682 ? 159.104 150.441 180.001 1.00 109.63 ? 2899 SER A N     1 
ATOM   11474 C  CA    . SER A 1 1682 ? 159.133 150.486 181.455 1.00 110.75 ? 2899 SER A CA    1 
ATOM   11475 C  C     . SER A 1 1682 ? 160.476 150.939 182.011 1.00 114.75 ? 2899 SER A C     1 
ATOM   11476 O  O     . SER A 1 1682 ? 160.592 151.131 183.227 1.00 112.38 ? 2899 SER A O     1 
ATOM   11477 C  CB    . SER A 1 1682 ? 158.779 149.111 182.032 1.00 104.48 ? 2899 SER A CB    1 
ATOM   11478 O  OG    . SER A 1 1682 ? 159.751 148.144 181.675 1.00 99.25  ? 2899 SER A OG    1 
ATOM   11479 N  N     . SER A 1 1683 ? 161.488 151.109 181.157 1.00 114.50 ? 2900 SER A N     1 
ATOM   11480 C  CA    . SER A 1 1683 ? 162.791 151.564 181.633 1.00 110.40 ? 2900 SER A CA    1 
ATOM   11481 C  C     . SER A 1 1683 ? 162.755 153.037 182.019 1.00 110.95 ? 2900 SER A C     1 
ATOM   11482 O  O     . SER A 1 1683 ? 163.379 153.441 183.007 1.00 104.42 ? 2900 SER A O     1 
ATOM   11483 C  CB    . SER A 1 1683 ? 163.856 151.312 180.567 1.00 102.89 ? 2900 SER A CB    1 
ATOM   11484 N  N     . ALA A 1 1684 ? 162.029 153.855 181.251 1.00 114.12 ? 2901 ALA A N     1 
ATOM   11485 C  CA    . ALA A 1 1684 ? 161.906 155.273 181.569 1.00 112.01 ? 2901 ALA A CA    1 
ATOM   11486 C  C     . ALA A 1 1684 ? 161.085 155.516 182.828 1.00 103.32 ? 2901 ALA A C     1 
ATOM   11487 O  O     . ALA A 1 1684 ? 161.170 156.604 183.406 1.00 94.07  ? 2901 ALA A O     1 
ATOM   11488 C  CB    . ALA A 1 1684 ? 161.289 156.026 180.390 1.00 107.34 ? 2901 ALA A CB    1 
ATOM   11489 N  N     . MET A 1 1685 ? 160.283 154.535 183.250 1.00 108.76 ? 2902 MET A N     1 
ATOM   11490 C  CA    . MET A 1 1685 ? 159.571 154.643 184.519 1.00 106.00 ? 2902 MET A CA    1 
ATOM   11491 C  C     . MET A 1 1685 ? 160.543 154.738 185.685 1.00 99.93  ? 2902 MET A C     1 
ATOM   11492 O  O     . MET A 1 1685 ? 160.323 155.507 186.629 1.00 93.11  ? 2902 MET A O     1 
ATOM   11493 C  CB    . MET A 1 1685 ? 158.651 153.437 184.706 1.00 104.55 ? 2902 MET A CB    1 
ATOM   11494 N  N     . ILE A 1 1686 ? 161.617 153.951 185.635 1.00 100.58 ? 2903 ILE A N     1 
ATOM   11495 C  CA    . ILE A 1 1686 ? 162.585 153.915 186.725 1.00 101.73 ? 2903 ILE A CA    1 
ATOM   11496 C  C     . ILE A 1 1686 ? 163.294 155.258 186.858 1.00 99.01  ? 2903 ILE A C     1 
ATOM   11497 O  O     . ILE A 1 1686 ? 163.429 155.802 187.961 1.00 90.90  ? 2903 ILE A O     1 
ATOM   11498 C  CB    . ILE A 1 1686 ? 163.578 152.760 186.499 1.00 92.23  ? 2903 ILE A CB    1 
ATOM   11499 C  CG1   . ILE A 1 1686 ? 162.940 151.422 186.888 1.00 81.87  ? 2903 ILE A CG1   1 
ATOM   11500 C  CG2   . ILE A 1 1686 ? 164.860 153.000 187.248 1.00 86.27  ? 2903 ILE A CG2   1 
ATOM   11501 C  CD1   . ILE A 1 1686 ? 162.796 151.218 188.380 1.00 70.77  ? 2903 ILE A CD1   1 
ATOM   11502 N  N     . SER A 1 1687 ? 163.733 155.825 185.736 1.00 99.03  ? 2904 SER A N     1 
ATOM   11503 C  CA    . SER A 1 1687 ? 164.437 157.101 185.747 1.00 91.79  ? 2904 SER A CA    1 
ATOM   11504 C  C     . SER A 1 1687 ? 163.498 158.297 185.814 1.00 84.31  ? 2904 SER A C     1 
ATOM   11505 O  O     . SER A 1 1687 ? 163.981 159.431 185.911 1.00 75.82  ? 2904 SER A O     1 
ATOM   11506 C  CB    . SER A 1 1687 ? 165.334 157.223 184.513 1.00 86.66  ? 2904 SER A CB    1 
ATOM   11507 O  OG    . SER A 1 1687 ? 166.228 158.314 184.642 1.00 72.40  ? 2904 SER A OG    1 
ATOM   11508 N  N     . SER A 1 1688 ? 162.186 158.077 185.748 1.00 87.77  ? 2905 SER A N     1 
ATOM   11509 C  CA    . SER A 1 1688 ? 161.243 159.182 185.814 1.00 84.83  ? 2905 SER A CA    1 
ATOM   11510 C  C     . SER A 1 1688 ? 161.314 159.846 187.187 1.00 73.26  ? 2905 SER A C     1 
ATOM   11511 O  O     . SER A 1 1688 ? 161.331 159.155 188.210 1.00 69.83  ? 2905 SER A O     1 
ATOM   11512 C  CB    . SER A 1 1688 ? 159.819 158.698 185.540 1.00 85.77  ? 2905 SER A CB    1 
ATOM   11513 O  OG    . SER A 1 1688 ? 158.900 159.777 185.579 1.00 74.91  ? 2905 SER A OG    1 
ATOM   11514 N  N     . PRO A 1 1689 ? 161.363 161.179 187.241 1.00 71.80  ? 2906 PRO A N     1 
ATOM   11515 C  CA    . PRO A 1 1689 ? 161.600 161.842 188.534 1.00 63.34  ? 2906 PRO A CA    1 
ATOM   11516 C  C     . PRO A 1 1689 ? 160.431 161.753 189.495 1.00 59.59  ? 2906 PRO A C     1 
ATOM   11517 O  O     . PRO A 1 1689 ? 160.642 161.592 190.700 1.00 60.36  ? 2906 PRO A O     1 
ATOM   11518 C  CB    . PRO A 1 1689 ? 161.894 163.294 188.132 1.00 60.97  ? 2906 PRO A CB    1 
ATOM   11519 C  CG    . PRO A 1 1689 ? 161.255 163.464 186.807 1.00 63.53  ? 2906 PRO A CG    1 
ATOM   11520 C  CD    . PRO A 1 1689 ? 161.315 162.133 186.120 1.00 70.35  ? 2906 PRO A CD    1 
ATOM   11521 N  N     . ALA A 1 1690 ? 159.199 161.859 189.011 1.00 60.40  ? 2907 ALA A N     1 
ATOM   11522 C  CA    . ALA A 1 1690 ? 158.084 161.930 189.942 1.00 64.66  ? 2907 ALA A CA    1 
ATOM   11523 C  C     . ALA A 1 1690 ? 157.570 160.557 190.363 1.00 64.74  ? 2907 ALA A C     1 
ATOM   11524 O  O     . ALA A 1 1690 ? 156.882 160.458 191.383 1.00 60.97  ? 2907 ALA A O     1 
ATOM   11525 C  CB    . ALA A 1 1690 ? 156.966 162.770 189.335 1.00 69.14  ? 2907 ALA A CB    1 
ATOM   11526 N  N     . LEU A 1 1691 ? 157.879 159.501 189.606 1.00 68.28  ? 2908 LEU A N     1 
ATOM   11527 C  CA    . LEU A 1 1691 ? 157.748 158.151 190.149 1.00 67.96  ? 2908 LEU A CA    1 
ATOM   11528 C  C     . LEU A 1 1691 ? 158.780 157.915 191.238 1.00 63.45  ? 2908 LEU A C     1 
ATOM   11529 O  O     . LEU A 1 1691 ? 158.511 157.242 192.237 1.00 67.02  ? 2908 LEU A O     1 
ATOM   11530 C  CB    . LEU A 1 1691 ? 157.897 157.110 189.040 1.00 67.53  ? 2908 LEU A CB    1 
ATOM   11531 C  CG    . LEU A 1 1691 ? 156.814 157.090 187.968 1.00 70.87  ? 2908 LEU A CG    1 
ATOM   11532 C  CD1   . LEU A 1 1691 ? 157.070 155.947 187.018 1.00 77.94  ? 2908 LEU A CD1   1 
ATOM   11533 C  CD2   . LEU A 1 1691 ? 155.454 156.938 188.620 1.00 71.29  ? 2908 LEU A CD2   1 
ATOM   11534 N  N     . PHE A 1 1692 ? 159.961 158.499 191.075 1.00 59.97  ? 2909 PHE A N     1 
ATOM   11535 C  CA    . PHE A 1 1692 ? 161.083 158.402 192.000 1.00 55.42  ? 2909 PHE A CA    1 
ATOM   11536 C  C     . PHE A 1 1692 ? 160.777 159.104 193.325 1.00 51.38  ? 2909 PHE A C     1 
ATOM   11537 O  O     . PHE A 1 1692 ? 161.602 159.104 194.244 1.00 45.89  ? 2909 PHE A O     1 
ATOM   11538 C  CB    . PHE A 1 1692 ? 162.303 158.986 191.277 1.00 56.15  ? 2909 PHE A CB    1 
ATOM   11539 C  CG    . PHE A 1 1692 ? 163.577 158.952 192.045 1.00 44.72  ? 2909 PHE A CG    1 
ATOM   11540 C  CD1   . PHE A 1 1692 ? 164.278 157.773 192.196 1.00 50.16  ? 2909 PHE A CD1   1 
ATOM   11541 C  CD2   . PHE A 1 1692 ? 164.110 160.118 192.556 1.00 41.84  ? 2909 PHE A CD2   1 
ATOM   11542 C  CE1   . PHE A 1 1692 ? 165.469 157.756 192.883 1.00 55.44  ? 2909 PHE A CE1   1 
ATOM   11543 C  CE2   . PHE A 1 1692 ? 165.295 160.105 193.240 1.00 43.54  ? 2909 PHE A CE2   1 
ATOM   11544 C  CZ    . PHE A 1 1692 ? 165.979 158.929 193.402 1.00 50.24  ? 2909 PHE A CZ    1 
ATOM   11545 N  N     . ASN A 1 1693 ? 159.572 159.672 193.448 1.00 56.58  ? 2910 ASN A N     1 
ATOM   11546 C  CA    . ASN A 1 1693 ? 159.249 160.541 194.575 1.00 62.48  ? 2910 ASN A CA    1 
ATOM   11547 C  C     . ASN A 1 1693 ? 158.877 159.744 195.820 1.00 62.81  ? 2910 ASN A C     1 
ATOM   11548 O  O     . ASN A 1 1693 ? 159.482 159.924 196.883 1.00 56.94  ? 2910 ASN A O     1 
ATOM   11549 C  CB    . ASN A 1 1693 ? 158.118 161.497 194.185 1.00 64.65  ? 2910 ASN A CB    1 
ATOM   11550 C  CG    . ASN A 1 1693 ? 157.774 162.478 195.288 1.00 62.28  ? 2910 ASN A CG    1 
ATOM   11551 O  OD1   . ASN A 1 1693 ? 158.659 163.027 195.944 1.00 58.94  ? 2910 ASN A OD1   1 
ATOM   11552 N  ND2   . ASN A 1 1693 ? 156.483 162.710 195.493 1.00 63.30  ? 2910 ASN A ND2   1 
ATOM   11553 N  N     . ARG A 1 1694 ? 157.876 158.864 195.725 1.00 63.47  ? 2911 ARG A N     1 
ATOM   11554 C  CA    . ARG A 1 1694 ? 157.401 158.166 196.916 1.00 62.56  ? 2911 ARG A CA    1 
ATOM   11555 C  C     . ARG A 1 1694 ? 157.258 156.658 196.771 1.00 64.67  ? 2911 ARG A C     1 
ATOM   11556 O  O     . ARG A 1 1694 ? 157.182 155.976 197.795 1.00 68.33  ? 2911 ARG A O     1 
ATOM   11557 C  CB    . ARG A 1 1694 ? 156.049 158.725 197.381 1.00 66.85  ? 2911 ARG A CB    1 
ATOM   11558 C  CG    . ARG A 1 1694 ? 156.048 160.177 197.808 1.00 70.90  ? 2911 ARG A CG    1 
ATOM   11559 C  CD    . ARG A 1 1694 ? 156.357 160.311 199.285 1.00 69.16  ? 2911 ARG A CD    1 
ATOM   11560 N  NE    . ARG A 1 1694 ? 156.389 161.708 199.697 1.00 71.12  ? 2911 ARG A NE    1 
ATOM   11561 C  CZ    . ARG A 1 1694 ? 155.313 162.410 200.027 1.00 75.30  ? 2911 ARG A CZ    1 
ATOM   11562 N  NH1   . ARG A 1 1694 ? 154.102 161.878 199.989 1.00 77.98  ? 2911 ARG A NH1   1 
ATOM   11563 N  NH2   . ARG A 1 1694 ? 155.456 163.676 200.404 1.00 76.76  ? 2911 ARG A NH2   1 
ATOM   11564 N  N     . CYS A 1 1695 ? 157.206 156.110 195.558 1.00 60.07  ? 2912 CYS A N     1 
ATOM   11565 C  CA    . CYS A 1 1695 ? 157.112 154.660 195.445 1.00 59.77  ? 2912 CYS A CA    1 
ATOM   11566 C  C     . CYS A 1 1695 ? 158.463 154.045 195.790 1.00 57.57  ? 2912 CYS A C     1 
ATOM   11567 O  O     . CYS A 1 1695 ? 159.506 154.491 195.303 1.00 56.67  ? 2912 CYS A O     1 
ATOM   11568 C  CB    . CYS A 1 1695 ? 156.650 154.229 194.050 1.00 62.69  ? 2912 CYS A CB    1 
ATOM   11569 S  SG    . CYS A 1 1695 ? 157.857 154.266 192.709 1.00 51.13  ? 2912 CYS A SG    1 
ATOM   11570 N  N     . ILE A 1 1696 ? 158.448 153.048 196.666 1.00 58.55  ? 2913 ILE A N     1 
ATOM   11571 C  CA    . ILE A 1 1696 ? 159.676 152.454 197.177 1.00 65.79  ? 2913 ILE A CA    1 
ATOM   11572 C  C     . ILE A 1 1696 ? 160.041 151.267 196.296 1.00 64.65  ? 2913 ILE A C     1 
ATOM   11573 O  O     . ILE A 1 1696 ? 159.241 150.342 196.118 1.00 60.29  ? 2913 ILE A O     1 
ATOM   11574 C  CB    . ILE A 1 1696 ? 159.525 152.035 198.646 1.00 63.91  ? 2913 ILE A CB    1 
ATOM   11575 C  CG1   . ILE A 1 1696 ? 159.299 153.271 199.520 1.00 55.42  ? 2913 ILE A CG1   1 
ATOM   11576 C  CG2   . ILE A 1 1696 ? 160.755 151.275 199.114 1.00 61.58  ? 2913 ILE A CG2   1 
ATOM   11577 C  CD1   . ILE A 1 1696 ? 159.130 152.964 200.988 1.00 51.94  ? 2913 ILE A CD1   1 
ATOM   11578 N  N     . ILE A 1 1697 ? 161.251 151.297 195.745 1.00 65.85  ? 2914 ILE A N     1 
ATOM   11579 C  CA    . ILE A 1 1697 ? 161.706 150.264 194.822 1.00 63.62  ? 2914 ILE A CA    1 
ATOM   11580 C  C     . ILE A 1 1697 ? 162.288 149.122 195.648 1.00 67.84  ? 2914 ILE A C     1 
ATOM   11581 O  O     . ILE A 1 1697 ? 163.370 149.250 196.226 1.00 66.55  ? 2914 ILE A O     1 
ATOM   11582 C  CB    . ILE A 1 1697 ? 162.737 150.813 193.832 1.00 65.51  ? 2914 ILE A CB    1 
ATOM   11583 C  CG1   . ILE A 1 1697 ? 162.107 151.888 192.948 1.00 68.19  ? 2914 ILE A CG1   1 
ATOM   11584 C  CG2   . ILE A 1 1697 ? 163.267 149.698 192.966 1.00 65.87  ? 2914 ILE A CG2   1 
ATOM   11585 C  CD1   . ILE A 1 1697 ? 163.039 152.441 191.896 1.00 68.30  ? 2914 ILE A CD1   1 
ATOM   11586 N  N     . ASN A 1 1698 ? 161.570 148.005 195.705 1.00 65.77  ? 2915 ASN A N     1 
ATOM   11587 C  CA    . ASN A 1 1698 ? 162.000 146.836 196.458 1.00 63.53  ? 2915 ASN A CA    1 
ATOM   11588 C  C     . ASN A 1 1698 ? 162.597 145.811 195.505 1.00 67.24  ? 2915 ASN A C     1 
ATOM   11589 O  O     . ASN A 1 1698 ? 161.961 145.432 194.515 1.00 65.33  ? 2915 ASN A O     1 
ATOM   11590 C  CB    . ASN A 1 1698 ? 160.830 146.228 197.233 1.00 55.32  ? 2915 ASN A CB    1 
ATOM   11591 C  CG    . ASN A 1 1698 ? 161.263 145.115 198.168 1.00 56.36  ? 2915 ASN A CG    1 
ATOM   11592 O  OD1   . ASN A 1 1698 ? 162.450 144.941 198.442 1.00 55.67  ? 2915 ASN A OD1   1 
ATOM   11593 N  ND2   . ASN A 1 1698 ? 160.297 144.357 198.667 1.00 54.18  ? 2915 ASN A ND2   1 
ATOM   11594 N  N     . TRP A 1 1699 ? 163.817 145.372 195.802 1.00 66.41  ? 2916 TRP A N     1 
ATOM   11595 C  CA    . TRP A 1 1699 ? 164.514 144.366 195.004 1.00 67.77  ? 2916 TRP A CA    1 
ATOM   11596 C  C     . TRP A 1 1699 ? 164.252 142.991 195.605 1.00 62.58  ? 2916 TRP A C     1 
ATOM   11597 O  O     . TRP A 1 1699 ? 164.899 142.590 196.576 1.00 63.25  ? 2916 TRP A O     1 
ATOM   11598 C  CB    . TRP A 1 1699 ? 166.004 144.679 194.910 1.00 71.74  ? 2916 TRP A CB    1 
ATOM   11599 C  CG    . TRP A 1 1699 ? 166.612 144.152 193.647 1.00 74.29  ? 2916 TRP A CG    1 
ATOM   11600 C  CD1   . TRP A 1 1699 ? 165.988 143.394 192.703 1.00 74.50  ? 2916 TRP A CD1   1 
ATOM   11601 C  CD2   . TRP A 1 1699 ? 167.934 144.397 193.152 1.00 73.97  ? 2916 TRP A CD2   1 
ATOM   11602 N  NE1   . TRP A 1 1699 ? 166.848 143.116 191.671 1.00 76.37  ? 2916 TRP A NE1   1 
ATOM   11603 C  CE2   . TRP A 1 1699 ? 168.048 143.725 191.918 1.00 74.59  ? 2916 TRP A CE2   1 
ATOM   11604 C  CE3   . TRP A 1 1699 ? 169.035 145.106 193.635 1.00 68.77  ? 2916 TRP A CE3   1 
ATOM   11605 C  CZ2   . TRP A 1 1699 ? 169.217 143.742 191.164 1.00 69.91  ? 2916 TRP A CZ2   1 
ATOM   11606 C  CZ3   . TRP A 1 1699 ? 170.190 145.122 192.882 1.00 70.16  ? 2916 TRP A CZ3   1 
ATOM   11607 C  CH2   . TRP A 1 1699 ? 170.275 144.443 191.663 1.00 69.29  ? 2916 TRP A CH2   1 
ATOM   11608 N  N     . MET A 1 1700 ? 163.280 142.281 195.026 1.00 58.47  ? 2917 MET A N     1 
ATOM   11609 C  CA    . MET A 1 1700 ? 162.998 140.913 195.441 1.00 57.22  ? 2917 MET A CA    1 
ATOM   11610 C  C     . MET A 1 1700 ? 164.208 140.025 195.196 1.00 62.35  ? 2917 MET A C     1 
ATOM   11611 O  O     . MET A 1 1700 ? 164.575 139.206 196.044 1.00 64.55  ? 2917 MET A O     1 
ATOM   11612 C  CB    . MET A 1 1700 ? 161.810 140.367 194.655 1.00 60.94  ? 2917 MET A CB    1 
ATOM   11613 C  CG    . MET A 1 1700 ? 160.433 140.670 195.196 1.00 60.50  ? 2917 MET A CG    1 
ATOM   11614 S  SD    . MET A 1 1700 ? 159.871 139.793 196.650 1.00 61.53  ? 2917 MET A SD    1 
ATOM   11615 C  CE    . MET A 1 1700 ? 159.632 141.206 197.701 1.00 57.80  ? 2917 MET A CE    1 
ATOM   11616 N  N     . GLY A 1 1701 ? 164.835 140.176 194.031 1.00 63.98  ? 2918 GLY A N     1 
ATOM   11617 C  CA    . GLY A 1 1701 ? 165.984 139.382 193.653 1.00 68.89  ? 2918 GLY A CA    1 
ATOM   11618 C  C     . GLY A 1 1701 ? 165.611 138.023 193.103 1.00 67.11  ? 2918 GLY A C     1 
ATOM   11619 O  O     . GLY A 1 1701 ? 164.612 137.428 193.521 1.00 61.40  ? 2918 GLY A O     1 
ATOM   11620 N  N     . ASP A 1 1702 ? 166.400 137.524 192.155 1.00 70.46  ? 2919 ASP A N     1 
ATOM   11621 C  CA    . ASP A 1 1702 ? 166.239 136.148 191.715 1.00 68.56  ? 2919 ASP A CA    1 
ATOM   11622 C  C     . ASP A 1 1702 ? 166.717 135.202 192.809 1.00 67.11  ? 2919 ASP A C     1 
ATOM   11623 O  O     . ASP A 1 1702 ? 167.561 135.553 193.638 1.00 71.27  ? 2919 ASP A O     1 
ATOM   11624 C  CB    . ASP A 1 1702 ? 167.004 135.895 190.413 1.00 71.94  ? 2919 ASP A CB    1 
ATOM   11625 C  CG    . ASP A 1 1702 ? 168.456 136.337 190.483 1.00 75.28  ? 2919 ASP A CG    1 
ATOM   11626 O  OD1   . ASP A 1 1702 ? 168.851 136.976 191.481 1.00 73.52  ? 2919 ASP A OD1   1 
ATOM   11627 O  OD2   . ASP A 1 1702 ? 169.208 136.039 189.531 1.00 77.42  ? 2919 ASP A OD2   1 
ATOM   11628 N  N     . TRP A 1 1703 ? 166.156 133.997 192.814 1.00 63.79  ? 2920 TRP A N     1 
ATOM   11629 C  CA    . TRP A 1 1703 ? 166.449 133.040 193.870 1.00 60.48  ? 2920 TRP A CA    1 
ATOM   11630 C  C     . TRP A 1 1703 ? 167.901 132.586 193.811 1.00 60.40  ? 2920 TRP A C     1 
ATOM   11631 O  O     . TRP A 1 1703 ? 168.473 132.410 192.732 1.00 61.18  ? 2920 TRP A O     1 
ATOM   11632 C  CB    . TRP A 1 1703 ? 165.522 131.832 193.762 1.00 58.93  ? 2920 TRP A CB    1 
ATOM   11633 C  CG    . TRP A 1 1703 ? 164.174 132.067 194.345 1.00 50.68  ? 2920 TRP A CG    1 
ATOM   11634 C  CD1   . TRP A 1 1703 ? 163.675 133.249 194.800 1.00 52.43  ? 2920 TRP A CD1   1 
ATOM   11635 C  CD2   . TRP A 1 1703 ? 163.147 131.093 194.548 1.00 51.46  ? 2920 TRP A CD2   1 
ATOM   11636 N  NE1   . TRP A 1 1703 ? 162.398 133.074 195.271 1.00 51.37  ? 2920 TRP A NE1   1 
ATOM   11637 C  CE2   . TRP A 1 1703 ? 162.050 131.758 195.127 1.00 53.49  ? 2920 TRP A CE2   1 
ATOM   11638 C  CE3   . TRP A 1 1703 ? 163.047 129.722 194.295 1.00 60.95  ? 2920 TRP A CE3   1 
ATOM   11639 C  CZ2   . TRP A 1 1703 ? 160.869 131.100 195.458 1.00 61.93  ? 2920 TRP A CZ2   1 
ATOM   11640 C  CZ3   . TRP A 1 1703 ? 161.873 129.071 194.624 1.00 63.26  ? 2920 TRP A CZ3   1 
ATOM   11641 C  CH2   . TRP A 1 1703 ? 160.800 129.760 195.198 1.00 63.41  ? 2920 TRP A CH2   1 
ATOM   11642 N  N     . ASP A 1 1704 ? 168.499 132.408 194.983 1.00 60.50  ? 2921 ASP A N     1 
ATOM   11643 C  CA    . ASP A 1 1704 ? 169.838 131.860 195.097 1.00 66.43  ? 2921 ASP A CA    1 
ATOM   11644 C  C     . ASP A 1 1704 ? 169.757 130.410 195.568 1.00 71.25  ? 2921 ASP A C     1 
ATOM   11645 O  O     . ASP A 1 1704 ? 168.674 129.841 195.735 1.00 70.93  ? 2921 ASP A O     1 
ATOM   11646 C  CB    . ASP A 1 1704 ? 170.694 132.713 196.037 1.00 71.13  ? 2921 ASP A CB    1 
ATOM   11647 C  CG    . ASP A 1 1704 ? 169.963 133.095 197.306 1.00 72.42  ? 2921 ASP A CG    1 
ATOM   11648 O  OD1   . ASP A 1 1704 ? 168.743 132.848 197.387 1.00 71.09  ? 2921 ASP A OD1   1 
ATOM   11649 O  OD2   . ASP A 1 1704 ? 170.608 133.647 198.223 1.00 71.64  ? 2921 ASP A OD2   1 
ATOM   11650 N  N     . THR A 1 1705 ? 170.932 129.808 195.776 1.00 74.42  ? 2922 THR A N     1 
ATOM   11651 C  CA    . THR A 1 1705 ? 171.002 128.391 196.119 1.00 74.69  ? 2922 THR A CA    1 
ATOM   11652 C  C     . THR A 1 1705 ? 170.326 128.105 197.454 1.00 75.14  ? 2922 THR A C     1 
ATOM   11653 O  O     . THR A 1 1705 ? 169.611 127.105 197.592 1.00 76.56  ? 2922 THR A O     1 
ATOM   11654 C  CB    . THR A 1 1705 ? 172.459 127.935 196.152 1.00 77.61  ? 2922 THR A CB    1 
ATOM   11655 O  OG1   . THR A 1 1705 ? 173.154 128.636 197.191 1.00 77.40  ? 2922 THR A OG1   1 
ATOM   11656 C  CG2   . THR A 1 1705 ? 173.134 128.224 194.820 1.00 76.02  ? 2922 THR A CG2   1 
ATOM   11657 N  N     . LYS A 1 1706 ? 170.541 128.973 198.446 1.00 73.87  ? 2923 LYS A N     1 
ATOM   11658 C  CA    . LYS A 1 1706 ? 169.941 128.770 199.761 1.00 74.52  ? 2923 LYS A CA    1 
ATOM   11659 C  C     . LYS A 1 1706 ? 168.420 128.818 199.694 1.00 74.84  ? 2923 LYS A C     1 
ATOM   11660 O  O     . LYS A 1 1706 ? 167.739 127.964 200.274 1.00 74.51  ? 2923 LYS A O     1 
ATOM   11661 C  CB    . LYS A 1 1706 ? 170.467 129.817 200.742 1.00 75.52  ? 2923 LYS A CB    1 
ATOM   11662 C  CG    . LYS A 1 1706 ? 169.902 129.694 202.147 1.00 77.60  ? 2923 LYS A CG    1 
ATOM   11663 C  CD    . LYS A 1 1706 ? 170.384 128.425 202.828 1.00 79.44  ? 2923 LYS A CD    1 
ATOM   11664 C  CE    . LYS A 1 1706 ? 169.946 128.379 204.283 1.00 81.55  ? 2923 LYS A CE    1 
ATOM   11665 N  NZ    . LYS A 1 1706 ? 168.467 128.267 204.411 1.00 81.21  ? 2923 LYS A NZ    1 
ATOM   11666 N  N     . THR A 1 1707 ? 167.869 129.800 198.974 1.00 72.04  ? 2924 THR A N     1 
ATOM   11667 C  CA    . THR A 1 1707 ? 166.417 129.914 198.869 1.00 71.08  ? 2924 THR A CA    1 
ATOM   11668 C  C     . THR A 1 1707 ? 165.827 128.753 198.078 1.00 71.97  ? 2924 THR A C     1 
ATOM   11669 O  O     . THR A 1 1707 ? 164.776 128.216 198.451 1.00 72.33  ? 2924 THR A O     1 
ATOM   11670 C  CB    . THR A 1 1707 ? 166.036 131.249 198.231 1.00 65.15  ? 2924 THR A CB    1 
ATOM   11671 O  OG1   . THR A 1 1707 ? 166.656 132.318 198.956 1.00 69.13  ? 2924 THR A OG1   1 
ATOM   11672 C  CG2   . THR A 1 1707 ? 164.529 131.448 198.267 1.00 60.45  ? 2924 THR A CG2   1 
ATOM   11673 N  N     . MET A 1 1708 ? 166.492 128.346 196.991 1.00 70.07  ? 2925 MET A N     1 
ATOM   11674 C  CA    . MET A 1 1708 ? 166.014 127.206 196.211 1.00 70.43  ? 2925 MET A CA    1 
ATOM   11675 C  C     . MET A 1 1708 ? 165.989 125.938 197.054 1.00 71.50  ? 2925 MET A C     1 
ATOM   11676 O  O     . MET A 1 1708 ? 164.996 125.197 197.057 1.00 71.91  ? 2925 MET A O     1 
ATOM   11677 C  CB    . MET A 1 1708 ? 166.895 127.004 194.977 1.00 69.99  ? 2925 MET A CB    1 
ATOM   11678 C  CG    . MET A 1 1708 ? 166.695 128.020 193.870 1.00 66.43  ? 2925 MET A CG    1 
ATOM   11679 S  SD    . MET A 1 1708 ? 168.107 128.053 192.750 1.00 63.77  ? 2925 MET A SD    1 
ATOM   11680 C  CE    . MET A 1 1708 ? 167.424 128.950 191.361 1.00 55.89  ? 2925 MET A CE    1 
ATOM   11681 N  N     . SER A 1 1709 ? 167.075 125.683 197.791 1.00 69.08  ? 2926 SER A N     1 
ATOM   11682 C  CA    . SER A 1 1709 ? 167.146 124.493 198.630 1.00 70.25  ? 2926 SER A CA    1 
ATOM   11683 C  C     . SER A 1 1709 ? 166.102 124.531 199.736 1.00 73.16  ? 2926 SER A C     1 
ATOM   11684 O  O     . SER A 1 1709 ? 165.454 123.517 200.016 1.00 77.16  ? 2926 SER A O     1 
ATOM   11685 C  CB    . SER A 1 1709 ? 168.547 124.358 199.223 1.00 69.12  ? 2926 SER A CB    1 
ATOM   11686 O  OG    . SER A 1 1709 ? 168.871 125.487 200.014 1.00 68.80  ? 2926 SER A OG    1 
ATOM   11687 N  N     . GLN A 1 1710 ? 165.917 125.693 200.370 1.00 70.76  ? 2927 GLN A N     1 
ATOM   11688 C  CA    . GLN A 1 1710 ? 164.949 125.803 201.455 1.00 69.16  ? 2927 GLN A CA    1 
ATOM   11689 C  C     . GLN A 1 1710 ? 163.526 125.587 200.949 1.00 70.76  ? 2927 GLN A C     1 
ATOM   11690 O  O     . GLN A 1 1710 ? 162.737 124.873 201.583 1.00 74.77  ? 2927 GLN A O     1 
ATOM   11691 C  CB    . GLN A 1 1710 ? 165.090 127.170 202.128 1.00 67.54  ? 2927 GLN A CB    1 
ATOM   11692 C  CG    . GLN A 1 1710 ? 163.938 127.619 203.032 1.00 69.75  ? 2927 GLN A CG    1 
ATOM   11693 C  CD    . GLN A 1 1710 ? 163.759 126.774 204.293 1.00 75.56  ? 2927 GLN A CD    1 
ATOM   11694 O  OE1   . GLN A 1 1710 ? 163.512 125.572 204.236 1.00 80.01  ? 2927 GLN A OE1   1 
ATOM   11695 N  NE2   . GLN A 1 1710 ? 163.888 127.419 205.446 1.00 75.06  ? 2927 GLN A NE2   1 
ATOM   11696 N  N     . VAL A 1 1711 ? 163.193 126.167 199.791 1.00 69.98  ? 2928 VAL A N     1 
ATOM   11697 C  CA    . VAL A 1 1711 ? 161.860 125.993 199.219 1.00 72.90  ? 2928 VAL A CA    1 
ATOM   11698 C  C     . VAL A 1 1711 ? 161.619 124.536 198.843 1.00 75.51  ? 2928 VAL A C     1 
ATOM   11699 O  O     . VAL A 1 1711 ? 160.557 123.970 199.145 1.00 75.27  ? 2928 VAL A O     1 
ATOM   11700 C  CB    . VAL A 1 1711 ? 161.672 126.929 198.010 1.00 70.59  ? 2928 VAL A CB    1 
ATOM   11701 C  CG1   . VAL A 1 1711 ? 160.465 126.510 197.185 1.00 70.05  ? 2928 VAL A CG1   1 
ATOM   11702 C  CG2   . VAL A 1 1711 ? 161.509 128.358 198.477 1.00 71.82  ? 2928 VAL A CG2   1 
ATOM   11703 N  N     . ALA A 1 1712 ? 162.598 123.905 198.187 1.00 73.30  ? 2929 ALA A N     1 
ATOM   11704 C  CA    . ALA A 1 1712 ? 162.442 122.511 197.784 1.00 68.68  ? 2929 ALA A CA    1 
ATOM   11705 C  C     . ALA A 1 1712 ? 162.288 121.602 198.997 1.00 72.49  ? 2929 ALA A C     1 
ATOM   11706 O  O     . ALA A 1 1712 ? 161.426 120.714 199.015 1.00 77.39  ? 2929 ALA A O     1 
ATOM   11707 C  CB    . ALA A 1 1712 ? 163.632 122.079 196.928 1.00 68.48  ? 2929 ALA A CB    1 
ATOM   11708 N  N     . ASN A 1 1713 ? 163.100 121.830 200.035 1.00 71.47  ? 2930 ASN A N     1 
ATOM   11709 C  CA    . ASN A 1 1713 ? 163.019 121.022 201.248 1.00 73.45  ? 2930 ASN A CA    1 
ATOM   11710 C  C     . ASN A 1 1713 ? 161.677 121.192 201.945 1.00 75.46  ? 2930 ASN A C     1 
ATOM   11711 O  O     . ASN A 1 1713 ? 161.106 120.217 202.448 1.00 79.93  ? 2930 ASN A O     1 
ATOM   11712 C  CB    . ASN A 1 1713 ? 164.160 121.386 202.199 1.00 70.26  ? 2930 ASN A CB    1 
ATOM   11713 C  CG    . ASN A 1 1713 ? 165.509 120.929 201.691 1.00 68.19  ? 2930 ASN A CG    1 
ATOM   11714 O  OD1   . ASN A 1 1713 ? 165.682 120.672 200.501 1.00 65.26  ? 2930 ASN A OD1   1 
ATOM   11715 N  ND2   . ASN A 1 1713 ? 166.478 120.831 202.592 1.00 66.59  ? 2930 ASN A ND2   1 
ATOM   11716 N  N     . ASN A 1 1714 ? 161.159 122.421 201.997 1.00 75.03  ? 2931 ASN A N     1 
ATOM   11717 C  CA    . ASN A 1 1714 ? 159.872 122.635 202.648 1.00 76.90  ? 2931 ASN A CA    1 
ATOM   11718 C  C     . ASN A 1 1714 ? 158.718 122.047 201.846 1.00 80.66  ? 2931 ASN A C     1 
ATOM   11719 O  O     . ASN A 1 1714 ? 157.730 121.593 202.435 1.00 83.80  ? 2931 ASN A O     1 
ATOM   11720 C  CB    . ASN A 1 1714 ? 159.647 124.125 202.895 1.00 79.34  ? 2931 ASN A CB    1 
ATOM   11721 C  CG    . ASN A 1 1714 ? 160.271 124.600 204.192 1.00 81.60  ? 2931 ASN A CG    1 
ATOM   11722 O  OD1   . ASN A 1 1714 ? 161.207 123.987 204.704 1.00 82.39  ? 2931 ASN A OD1   1 
ATOM   11723 N  ND2   . ASN A 1 1714 ? 159.758 125.701 204.729 1.00 78.67  ? 2931 ASN A ND2   1 
ATOM   11724 N  N     . MET A 1 1715 ? 158.813 122.034 200.515 1.00 80.28  ? 2932 MET A N     1 
ATOM   11725 C  CA    . MET A 1 1715 ? 157.660 121.583 199.742 1.00 81.67  ? 2932 MET A CA    1 
ATOM   11726 C  C     . MET A 1 1715 ? 157.640 120.065 199.564 1.00 83.13  ? 2932 MET A C     1 
ATOM   11727 O  O     . MET A 1 1715 ? 156.568 119.453 199.627 1.00 80.97  ? 2932 MET A O     1 
ATOM   11728 C  CB    . MET A 1 1715 ? 157.614 122.301 198.391 1.00 77.57  ? 2932 MET A CB    1 
ATOM   11729 C  CG    . MET A 1 1715 ? 156.505 121.821 197.463 1.00 77.27  ? 2932 MET A CG    1 
ATOM   11730 S  SD    . MET A 1 1715 ? 156.411 122.742 195.917 1.00 76.42  ? 2932 MET A SD    1 
ATOM   11731 C  CE    . MET A 1 1715 ? 158.141 123.053 195.606 1.00 69.65  ? 2932 MET A CE    1 
ATOM   11732 N  N     . VAL A 1 1716 ? 158.800 119.428 199.363 1.00 87.25  ? 2933 VAL A N     1 
ATOM   11733 C  CA    . VAL A 1 1716 ? 158.808 117.977 199.162 1.00 88.91  ? 2933 VAL A CA    1 
ATOM   11734 C  C     . VAL A 1 1716 ? 158.758 117.191 200.463 1.00 93.46  ? 2933 VAL A C     1 
ATOM   11735 O  O     . VAL A 1 1716 ? 158.725 115.954 200.423 1.00 93.07  ? 2933 VAL A O     1 
ATOM   11736 C  CB    . VAL A 1 1716 ? 160.041 117.500 198.365 1.00 84.77  ? 2933 VAL A CB    1 
ATOM   11737 C  CG1   . VAL A 1 1716 ? 160.216 118.328 197.100 1.00 81.06  ? 2933 VAL A CG1   1 
ATOM   11738 C  CG2   . VAL A 1 1716 ? 161.296 117.525 199.230 1.00 85.43  ? 2933 VAL A CG2   1 
ATOM   11739 N  N     . ASP A 1 1717 ? 158.735 117.864 201.616 1.00 95.39  ? 2934 ASP A N     1 
ATOM   11740 C  CA    . ASP A 1 1717 ? 158.795 117.177 202.902 1.00 99.07  ? 2934 ASP A CA    1 
ATOM   11741 C  C     . ASP A 1 1717 ? 157.518 116.421 203.246 1.00 101.97 ? 2934 ASP A C     1 
ATOM   11742 O  O     . ASP A 1 1717 ? 157.537 115.612 204.180 1.00 103.17 ? 2934 ASP A O     1 
ATOM   11743 C  CB    . ASP A 1 1717 ? 159.106 118.177 204.017 1.00 101.86 ? 2934 ASP A CB    1 
ATOM   11744 C  CG    . ASP A 1 1717 ? 160.008 117.596 205.086 1.00 106.09 ? 2934 ASP A CG    1 
ATOM   11745 O  OD1   . ASP A 1 1717 ? 160.433 116.431 204.937 1.00 103.61 ? 2934 ASP A OD1   1 
ATOM   11746 O  OD2   . ASP A 1 1717 ? 160.294 118.303 206.076 1.00 107.13 ? 2934 ASP A OD2   1 
ATOM   11747 N  N     . VAL A 1 1718 ? 156.423 116.658 202.532 1.00 101.64 ? 2935 VAL A N     1 
ATOM   11748 C  CA    . VAL A 1 1718 ? 155.153 116.007 202.826 1.00 102.32 ? 2935 VAL A CA    1 
ATOM   11749 C  C     . VAL A 1 1718 ? 154.880 114.849 201.864 1.00 104.68 ? 2935 VAL A C     1 
ATOM   11750 O  O     . VAL A 1 1718 ? 153.732 114.440 201.700 1.00 105.05 ? 2935 VAL A O     1 
ATOM   11751 C  CB    . VAL A 1 1718 ? 153.993 117.014 202.824 1.00 100.68 ? 2935 VAL A CB    1 
ATOM   11752 N  N     . VAL A 1 1719 ? 155.916 114.315 201.228 1.00 105.18 ? 2936 VAL A N     1 
ATOM   11753 C  CA    . VAL A 1 1719 ? 155.791 113.216 200.281 1.00 106.44 ? 2936 VAL A CA    1 
ATOM   11754 C  C     . VAL A 1 1719 ? 156.699 112.084 200.748 1.00 109.44 ? 2936 VAL A C     1 
ATOM   11755 O  O     . VAL A 1 1719 ? 157.898 112.298 200.947 1.00 108.30 ? 2936 VAL A O     1 
ATOM   11756 C  CB    . VAL A 1 1719 ? 156.150 113.645 198.848 1.00 103.12 ? 2936 VAL A CB    1 
ATOM   11757 C  CG1   . VAL A 1 1719 ? 156.223 112.434 197.935 1.00 103.54 ? 2936 VAL A CG1   1 
ATOM   11758 C  CG2   . VAL A 1 1719 ? 155.133 114.648 198.325 1.00 101.30 ? 2936 VAL A CG2   1 
ATOM   11759 N  N     . PRO A 1 1720 ? 156.180 110.870 200.944 1.00 110.52 ? 2937 PRO A N     1 
ATOM   11760 C  CA    . PRO A 1 1720 ? 157.033 109.750 201.376 1.00 110.39 ? 2937 PRO A CA    1 
ATOM   11761 C  C     . PRO A 1 1720 ? 157.964 109.306 200.257 1.00 110.74 ? 2937 PRO A C     1 
ATOM   11762 O  O     . PRO A 1 1720 ? 157.522 108.785 199.230 1.00 110.95 ? 2937 PRO A O     1 
ATOM   11763 C  CB    . PRO A 1 1720 ? 156.023 108.657 201.745 1.00 110.29 ? 2937 PRO A CB    1 
ATOM   11764 C  CG    . PRO A 1 1720 ? 154.798 108.993 200.956 1.00 110.02 ? 2937 PRO A CG    1 
ATOM   11765 C  CD    . PRO A 1 1720 ? 154.758 110.492 200.879 1.00 108.78 ? 2937 PRO A CD    1 
ATOM   11766 N  N     . MET A 1 1721 ? 159.264 109.516 200.463 1.00 111.12 ? 2938 MET A N     1 
ATOM   11767 C  CA    . MET A 1 1721 ? 160.275 109.174 199.471 1.00 110.71 ? 2938 MET A CA    1 
ATOM   11768 C  C     . MET A 1 1721 ? 161.404 108.309 200.014 1.00 116.13 ? 2938 MET A C     1 
ATOM   11769 O  O     . MET A 1 1721 ? 161.989 107.541 199.241 1.00 118.29 ? 2938 MET A O     1 
ATOM   11770 C  CB    . MET A 1 1721 ? 160.871 110.454 198.860 1.00 110.91 ? 2938 MET A CB    1 
ATOM   11771 C  CG    . MET A 1 1721 ? 161.731 110.246 197.620 1.00 105.93 ? 2938 MET A CG    1 
ATOM   11772 S  SD    . MET A 1 1721 ? 161.797 111.710 196.570 1.00 98.75  ? 2938 MET A SD    1 
ATOM   11773 C  CE    . MET A 1 1721 ? 163.173 112.589 197.302 1.00 91.59  ? 2938 MET A CE    1 
ATOM   11774 N  N     . GLU A 1 1722 ? 161.712 108.380 201.311 1.00 120.62 ? 2939 GLU A N     1 
ATOM   11775 C  CA    . GLU A 1 1722 ? 162.813 107.614 201.898 1.00 120.15 ? 2939 GLU A CA    1 
ATOM   11776 C  C     . GLU A 1 1722 ? 162.397 106.150 202.053 1.00 119.99 ? 2939 GLU A C     1 
ATOM   11777 O  O     . GLU A 1 1722 ? 162.094 105.657 203.142 1.00 120.81 ? 2939 GLU A O     1 
ATOM   11778 C  CB    . GLU A 1 1722 ? 163.233 108.222 203.230 1.00 119.50 ? 2939 GLU A CB    1 
ATOM   11779 N  N     . PHE A 1 1723 ? 162.388 105.448 200.919 1.00 118.98 ? 2940 PHE A N     1 
ATOM   11780 C  CA    . PHE A 1 1723 ? 162.064 104.031 200.886 1.00 119.06 ? 2940 PHE A CA    1 
ATOM   11781 C  C     . PHE A 1 1723 ? 162.977 103.226 199.973 1.00 119.93 ? 2940 PHE A C     1 
ATOM   11782 O  O     . PHE A 1 1723 ? 162.804 102.007 199.873 1.00 123.72 ? 2940 PHE A O     1 
ATOM   11783 C  CB    . PHE A 1 1723 ? 160.604 103.823 200.452 1.00 118.30 ? 2940 PHE A CB    1 
ATOM   11784 N  N     . THR A 1 1724 ? 163.934 103.863 199.306 1.00 120.69 ? 2941 THR A N     1 
ATOM   11785 C  CA    . THR A 1 1724 ? 164.832 103.163 198.397 1.00 124.00 ? 2941 THR A CA    1 
ATOM   11786 C  C     . THR A 1 1724 ? 166.226 103.034 199.001 1.00 118.40 ? 2941 THR A C     1 
ATOM   11787 O  O     . THR A 1 1724 ? 166.472 103.483 200.120 1.00 112.39 ? 2941 THR A O     1 
ATOM   11788 C  CB    . THR A 1 1724 ? 164.934 103.881 197.038 1.00 125.75 ? 2941 THR A CB    1 
ATOM   11789 O  OG1   . THR A 1 1724 ? 165.233 105.267 197.247 1.00 121.99 ? 2941 THR A OG1   1 
ATOM   11790 C  CG2   . THR A 1 1724 ? 163.624 103.764 196.274 1.00 126.15 ? 2941 THR A CG2   1 
ATOM   11791 N  N     . THR A 1 1743 ? 171.008 111.601 202.792 1.00 88.01  ? 2960 THR A N     1 
ATOM   11792 C  CA    . THR A 1 1743 ? 169.827 110.840 202.402 1.00 92.93  ? 2960 THR A CA    1 
ATOM   11793 C  C     . THR A 1 1743 ? 169.447 111.110 200.947 1.00 94.04  ? 2960 THR A C     1 
ATOM   11794 O  O     . THR A 1 1743 ? 170.260 111.597 200.163 1.00 92.19  ? 2960 THR A O     1 
ATOM   11795 C  CB    . THR A 1 1743 ? 168.627 111.159 203.318 1.00 92.17  ? 2960 THR A CB    1 
ATOM   11796 O  OG1   . THR A 1 1743 ? 167.478 110.419 202.885 1.00 92.80  ? 2960 THR A OG1   1 
ATOM   11797 C  CG2   . THR A 1 1743 ? 168.314 112.651 203.307 1.00 89.72  ? 2960 THR A CG2   1 
ATOM   11798 N  N     . ILE A 1 1744 ? 168.211 110.760 200.586 1.00 96.12  ? 2961 ILE A N     1 
ATOM   11799 C  CA    . ILE A 1 1744 ? 167.738 110.991 199.224 1.00 93.54  ? 2961 ILE A CA    1 
ATOM   11800 C  C     . ILE A 1 1744 ? 167.417 112.465 199.005 1.00 89.59  ? 2961 ILE A C     1 
ATOM   11801 O  O     . ILE A 1 1744 ? 167.663 113.012 197.923 1.00 88.97  ? 2961 ILE A O     1 
ATOM   11802 C  CB    . ILE A 1 1744 ? 166.518 110.101 198.928 1.00 96.86  ? 2961 ILE A CB    1 
ATOM   11803 C  CG1   . ILE A 1 1744 ? 166.772 108.671 199.399 1.00 102.64 ? 2961 ILE A CG1   1 
ATOM   11804 C  CG2   . ILE A 1 1744 ? 166.194 110.111 197.443 1.00 96.30  ? 2961 ILE A CG2   1 
ATOM   11805 C  CD1   . ILE A 1 1744 ? 165.536 107.808 199.388 1.00 108.63 ? 2961 ILE A CD1   1 
ATOM   11806 N  N     . ARG A 1 1745 ? 166.847 113.122 200.021 1.00 88.63  ? 2962 ARG A N     1 
ATOM   11807 C  CA    . ARG A 1 1745 ? 166.243 114.438 199.829 1.00 87.94  ? 2962 ARG A CA    1 
ATOM   11808 C  C     . ARG A 1 1745 ? 167.288 115.505 199.521 1.00 84.44  ? 2962 ARG A C     1 
ATOM   11809 O  O     . ARG A 1 1745 ? 167.144 116.263 198.553 1.00 86.72  ? 2962 ARG A O     1 
ATOM   11810 C  CB    . ARG A 1 1745 ? 165.433 114.818 201.068 1.00 91.09  ? 2962 ARG A CB    1 
ATOM   11811 C  CG    . ARG A 1 1745 ? 164.542 116.034 200.887 1.00 91.75  ? 2962 ARG A CG    1 
ATOM   11812 C  CD    . ARG A 1 1745 ? 163.523 116.131 202.011 1.00 95.97  ? 2962 ARG A CD    1 
ATOM   11813 N  NE    . ARG A 1 1745 ? 162.605 114.998 202.007 1.00 104.26 ? 2962 ARG A NE    1 
ATOM   11814 C  CZ    . ARG A 1 1745 ? 162.483 114.127 203.000 1.00 107.49 ? 2962 ARG A CZ    1 
ATOM   11815 N  NH1   . ARG A 1 1745 ? 163.205 114.232 204.104 1.00 108.19 ? 2962 ARG A NH1   1 
ATOM   11816 N  NH2   . ARG A 1 1745 ? 161.616 113.126 202.883 1.00 107.32 ? 2962 ARG A NH2   1 
ATOM   11817 N  N     . ASP A 1 1746 ? 168.347 115.582 200.331 1.00 83.30  ? 2963 ASP A N     1 
ATOM   11818 C  CA    . ASP A 1 1746 ? 169.371 116.597 200.099 1.00 83.39  ? 2963 ASP A CA    1 
ATOM   11819 C  C     . ASP A 1 1746 ? 170.102 116.350 198.786 1.00 80.33  ? 2963 ASP A C     1 
ATOM   11820 O  O     . ASP A 1 1746 ? 170.423 117.298 198.059 1.00 79.68  ? 2963 ASP A O     1 
ATOM   11821 C  CB    . ASP A 1 1746 ? 170.356 116.639 201.269 1.00 88.03  ? 2963 ASP A CB    1 
ATOM   11822 C  CG    . ASP A 1 1746 ? 170.830 115.263 201.686 1.00 94.78  ? 2963 ASP A CG    1 
ATOM   11823 O  OD1   . ASP A 1 1746 ? 171.627 115.172 202.645 1.00 96.26  ? 2963 ASP A OD1   1 
ATOM   11824 O  OD2   . ASP A 1 1746 ? 170.406 114.271 201.060 1.00 95.46  ? 2963 ASP A OD2   1 
ATOM   11825 N  N     . ALA A 1 1747 ? 170.352 115.079 198.459 1.00 80.32  ? 2964 ALA A N     1 
ATOM   11826 C  CA    . ALA A 1 1747 ? 171.024 114.752 197.207 1.00 81.37  ? 2964 ALA A CA    1 
ATOM   11827 C  C     . ALA A 1 1747 ? 170.182 115.147 196.001 1.00 82.86  ? 2964 ALA A C     1 
ATOM   11828 O  O     . ALA A 1 1747 ? 170.698 115.737 195.045 1.00 83.68  ? 2964 ALA A O     1 
ATOM   11829 C  CB    . ALA A 1 1747 ? 171.358 113.261 197.163 1.00 84.54  ? 2964 ALA A CB    1 
ATOM   11830 N  N     . VAL A 1 1748 ? 168.878 114.850 196.028 1.00 82.60  ? 2965 VAL A N     1 
ATOM   11831 C  CA    . VAL A 1 1748 ? 168.047 115.183 194.874 1.00 78.98  ? 2965 VAL A CA    1 
ATOM   11832 C  C     . VAL A 1 1748 ? 167.826 116.690 194.781 1.00 81.79  ? 2965 VAL A C     1 
ATOM   11833 O  O     . VAL A 1 1748 ? 167.728 117.236 193.675 1.00 81.13  ? 2965 VAL A O     1 
ATOM   11834 C  CB    . VAL A 1 1748 ? 166.720 114.393 194.899 1.00 75.04  ? 2965 VAL A CB    1 
ATOM   11835 C  CG1   . VAL A 1 1748 ? 165.779 114.888 195.984 1.00 76.47  ? 2965 VAL A CG1   1 
ATOM   11836 C  CG2   . VAL A 1 1748 ? 166.044 114.462 193.543 1.00 75.48  ? 2965 VAL A CG2   1 
ATOM   11837 N  N     . VAL A 1 1749 ? 167.785 117.394 195.917 1.00 85.29  ? 2966 VAL A N     1 
ATOM   11838 C  CA    . VAL A 1 1749 ? 167.672 118.849 195.877 1.00 79.59  ? 2966 VAL A CA    1 
ATOM   11839 C  C     . VAL A 1 1749 ? 168.936 119.466 195.285 1.00 82.10  ? 2966 VAL A C     1 
ATOM   11840 O  O     . VAL A 1 1749 ? 168.866 120.394 194.467 1.00 81.56  ? 2966 VAL A O     1 
ATOM   11841 C  CB    . VAL A 1 1749 ? 167.360 119.394 197.282 1.00 71.98  ? 2966 VAL A CB    1 
ATOM   11842 C  CG1   . VAL A 1 1749 ? 167.663 120.878 197.374 1.00 70.23  ? 2966 VAL A CG1   1 
ATOM   11843 C  CG2   . VAL A 1 1749 ? 165.906 119.136 197.622 1.00 70.23  ? 2966 VAL A CG2   1 
ATOM   11844 N  N     . ASN A 1 1750 ? 170.107 118.944 195.667 1.00 80.85  ? 2967 ASN A N     1 
ATOM   11845 C  CA    . ASN A 1 1750 ? 171.356 119.410 195.072 1.00 78.23  ? 2967 ASN A CA    1 
ATOM   11846 C  C     . ASN A 1 1750 ? 171.395 119.119 193.577 1.00 79.21  ? 2967 ASN A C     1 
ATOM   11847 O  O     . ASN A 1 1750 ? 171.851 119.956 192.789 1.00 82.77  ? 2967 ASN A O     1 
ATOM   11848 C  CB    . ASN A 1 1750 ? 172.549 118.765 195.775 1.00 76.97  ? 2967 ASN A CB    1 
ATOM   11849 C  CG    . ASN A 1 1750 ? 173.816 119.587 195.644 1.00 75.73  ? 2967 ASN A CG    1 
ATOM   11850 O  OD1   . ASN A 1 1750 ? 174.229 119.940 194.540 1.00 76.21  ? 2967 ASN A OD1   1 
ATOM   11851 N  ND2   . ASN A 1 1750 ? 174.440 119.896 196.774 1.00 74.91  ? 2967 ASN A ND2   1 
ATOM   11852 N  N     . ILE A 1 1751 ? 170.903 117.944 193.172 1.00 77.94  ? 2968 ILE A N     1 
ATOM   11853 C  CA    . ILE A 1 1751 ? 170.845 117.594 191.753 1.00 83.12  ? 2968 ILE A CA    1 
ATOM   11854 C  C     . ILE A 1 1751 ? 169.982 118.594 190.995 1.00 80.40  ? 2968 ILE A C     1 
ATOM   11855 O  O     . ILE A 1 1751 ? 170.375 119.110 189.942 1.00 83.33  ? 2968 ILE A O     1 
ATOM   11856 C  CB    . ILE A 1 1751 ? 170.312 116.161 191.575 1.00 86.35  ? 2968 ILE A CB    1 
ATOM   11857 C  CG1   . ILE A 1 1751 ? 171.366 115.126 191.958 1.00 88.98  ? 2968 ILE A CG1   1 
ATOM   11858 C  CG2   . ILE A 1 1751 ? 169.858 115.925 190.142 1.00 89.60  ? 2968 ILE A CG2   1 
ATOM   11859 C  CD1   . ILE A 1 1751 ? 170.807 113.724 192.039 1.00 91.51  ? 2968 ILE A CD1   1 
ATOM   11860 N  N     . LEU A 1 1752 ? 168.799 118.893 191.535 1.00 76.04  ? 2969 LEU A N     1 
ATOM   11861 C  CA    . LEU A 1 1752 ? 167.869 119.782 190.850 1.00 76.26  ? 2969 LEU A CA    1 
ATOM   11862 C  C     . LEU A 1 1752 ? 168.424 121.199 190.747 1.00 79.07  ? 2969 LEU A C     1 
ATOM   11863 O  O     . LEU A 1 1752 ? 168.364 121.820 189.678 1.00 78.77  ? 2969 LEU A O     1 
ATOM   11864 C  CB    . LEU A 1 1752 ? 166.520 119.772 191.567 1.00 74.33  ? 2969 LEU A CB    1 
ATOM   11865 C  CG    . LEU A 1 1752 ? 165.697 118.510 191.309 1.00 71.39  ? 2969 LEU A CG    1 
ATOM   11866 C  CD1   . LEU A 1 1752 ? 164.852 118.159 192.514 1.00 69.83  ? 2969 LEU A CD1   1 
ATOM   11867 C  CD2   . LEU A 1 1752 ? 164.828 118.685 190.076 1.00 67.23  ? 2969 LEU A CD2   1 
ATOM   11868 N  N     . ILE A 1 1753 ? 168.993 121.721 191.839 1.00 77.83  ? 2970 ILE A N     1 
ATOM   11869 C  CA    . ILE A 1 1753 ? 169.499 123.091 191.798 1.00 75.02  ? 2970 ILE A CA    1 
ATOM   11870 C  C     . ILE A 1 1753 ? 170.723 123.191 190.890 1.00 78.90  ? 2970 ILE A C     1 
ATOM   11871 O  O     . ILE A 1 1753 ? 170.882 124.174 190.153 1.00 79.73  ? 2970 ILE A O     1 
ATOM   11872 C  CB    . ILE A 1 1753 ? 169.782 123.629 193.217 1.00 72.68  ? 2970 ILE A CB    1 
ATOM   11873 C  CG1   . ILE A 1 1753 ? 170.898 122.856 193.920 1.00 77.33  ? 2970 ILE A CG1   1 
ATOM   11874 C  CG2   . ILE A 1 1753 ? 168.520 123.607 194.060 1.00 70.95  ? 2970 ILE A CG2   1 
ATOM   11875 C  CD1   . ILE A 1 1753 ? 171.282 123.431 195.265 1.00 76.77  ? 2970 ILE A CD1   1 
ATOM   11876 N  N     . HIS A 1 1754 ? 171.584 122.167 190.886 1.00 82.36  ? 2971 HIS A N     1 
ATOM   11877 C  CA    . HIS A 1 1754 ? 172.784 122.245 190.063 1.00 84.12  ? 2971 HIS A CA    1 
ATOM   11878 C  C     . HIS A 1 1754 ? 172.437 122.078 188.587 1.00 85.38  ? 2971 HIS A C     1 
ATOM   11879 O  O     . HIS A 1 1754 ? 173.044 122.725 187.725 1.00 87.75  ? 2971 HIS A O     1 
ATOM   11880 C  CB    . HIS A 1 1754 ? 173.800 121.199 190.526 1.00 84.75  ? 2971 HIS A CB    1 
ATOM   11881 C  CG    . HIS A 1 1754 ? 175.148 121.334 189.888 1.00 93.15  ? 2971 HIS A CG    1 
ATOM   11882 N  ND1   . HIS A 1 1754 ? 176.112 120.353 189.973 1.00 98.81  ? 2971 HIS A ND1   1 
ATOM   11883 C  CD2   . HIS A 1 1754 ? 175.705 122.346 189.181 1.00 94.46  ? 2971 HIS A CD2   1 
ATOM   11884 C  CE1   . HIS A 1 1754 ? 177.197 120.747 189.330 1.00 98.09  ? 2971 HIS A CE1   1 
ATOM   11885 N  NE2   . HIS A 1 1754 ? 176.976 121.953 188.840 1.00 96.30  ? 2971 HIS A NE2   1 
ATOM   11886 N  N     . PHE A 1 1755 ? 171.436 121.246 188.275 1.00 83.65  ? 2972 PHE A N     1 
ATOM   11887 C  CA    . PHE A 1 1755 ? 170.988 121.154 186.891 1.00 83.06  ? 2972 PHE A CA    1 
ATOM   11888 C  C     . PHE A 1 1755 ? 170.288 122.429 186.445 1.00 84.03  ? 2972 PHE A C     1 
ATOM   11889 O  O     . PHE A 1 1755 ? 170.391 122.805 185.276 1.00 85.02  ? 2972 PHE A O     1 
ATOM   11890 C  CB    . PHE A 1 1755 ? 170.061 119.957 186.689 1.00 79.75  ? 2972 PHE A CB    1 
ATOM   11891 C  CG    . PHE A 1 1755 ? 169.481 119.881 185.305 1.00 76.33  ? 2972 PHE A CG    1 
ATOM   11892 C  CD1   . PHE A 1 1755 ? 170.316 119.762 184.205 1.00 79.52  ? 2972 PHE A CD1   1 
ATOM   11893 C  CD2   . PHE A 1 1755 ? 168.116 119.942 185.098 1.00 74.05  ? 2972 PHE A CD2   1 
ATOM   11894 C  CE1   . PHE A 1 1755 ? 169.801 119.698 182.926 1.00 77.69  ? 2972 PHE A CE1   1 
ATOM   11895 C  CE2   . PHE A 1 1755 ? 167.597 119.878 183.819 1.00 77.86  ? 2972 PHE A CE2   1 
ATOM   11896 C  CZ    . PHE A 1 1755 ? 168.441 119.755 182.734 1.00 78.07  ? 2972 PHE A CZ    1 
ATOM   11897 N  N     . ASP A 1 1756 ? 169.567 123.100 187.350 1.00 81.04  ? 2973 ASP A N     1 
ATOM   11898 C  CA    . ASP A 1 1756 ? 168.989 124.396 187.008 1.00 76.82  ? 2973 ASP A CA    1 
ATOM   11899 C  C     . ASP A 1 1756 ? 170.076 125.415 186.693 1.00 79.34  ? 2973 ASP A C     1 
ATOM   11900 O  O     . ASP A 1 1756 ? 169.959 126.182 185.726 1.00 80.51  ? 2973 ASP A O     1 
ATOM   11901 C  CB    . ASP A 1 1756 ? 168.104 124.894 188.149 1.00 77.79  ? 2973 ASP A CB    1 
ATOM   11902 C  CG    . ASP A 1 1756 ? 167.381 126.179 187.805 1.00 78.35  ? 2973 ASP A CG    1 
ATOM   11903 O  OD1   . ASP A 1 1756 ? 166.270 126.104 187.241 1.00 76.86  ? 2973 ASP A OD1   1 
ATOM   11904 O  OD2   . ASP A 1 1756 ? 167.926 127.264 188.098 1.00 79.79  ? 2973 ASP A OD2   1 
ATOM   11905 N  N     . ARG A 1 1757 ? 171.146 125.431 187.496 1.00 82.68  ? 2974 ARG A N     1 
ATOM   11906 C  CA    . ARG A 1 1757 ? 172.274 126.317 187.212 1.00 85.48  ? 2974 ARG A CA    1 
ATOM   11907 C  C     . ARG A 1 1757 ? 172.909 125.992 185.866 1.00 85.25  ? 2974 ARG A C     1 
ATOM   11908 O  O     . ARG A 1 1757 ? 173.213 126.899 185.081 1.00 85.81  ? 2974 ARG A O     1 
ATOM   11909 C  CB    . ARG A 1 1757 ? 173.322 126.223 188.322 1.00 87.31  ? 2974 ARG A CB    1 
ATOM   11910 C  CG    . ARG A 1 1757 ? 172.848 126.653 189.699 1.00 87.04  ? 2974 ARG A CG    1 
ATOM   11911 C  CD    . ARG A 1 1757 ? 174.033 126.956 190.604 1.00 87.47  ? 2974 ARG A CD    1 
ATOM   11912 N  NE    . ARG A 1 1757 ? 173.859 126.413 191.946 1.00 88.96  ? 2974 ARG A NE    1 
ATOM   11913 C  CZ    . ARG A 1 1757 ? 174.750 125.652 192.566 1.00 89.88  ? 2974 ARG A CZ    1 
ATOM   11914 N  NH1   . ARG A 1 1757 ? 175.894 125.320 191.991 1.00 92.51  ? 2974 ARG A NH1   1 
ATOM   11915 N  NH2   . ARG A 1 1757 ? 174.487 125.213 193.793 1.00 85.69  ? 2974 ARG A NH2   1 
ATOM   11916 N  N     . ASN A 1 1758 ? 173.105 124.701 185.576 1.00 84.54  ? 2975 ASN A N     1 
ATOM   11917 C  CA    . ASN A 1 1758 ? 173.700 124.305 184.302 1.00 84.92  ? 2975 ASN A CA    1 
ATOM   11918 C  C     . ASN A 1 1758 ? 172.806 124.682 183.125 1.00 86.24  ? 2975 ASN A C     1 
ATOM   11919 O  O     . ASN A 1 1758 ? 173.294 125.159 182.094 1.00 85.50  ? 2975 ASN A O     1 
ATOM   11920 C  CB    . ASN A 1 1758 ? 173.983 122.802 184.301 1.00 80.42  ? 2975 ASN A CB    1 
ATOM   11921 C  CG    . ASN A 1 1758 ? 175.341 122.464 184.882 1.00 84.09  ? 2975 ASN A CG    1 
ATOM   11922 O  OD1   . ASN A 1 1758 ? 175.449 122.033 186.029 1.00 84.71  ? 2975 ASN A OD1   1 
ATOM   11923 N  ND2   . ASN A 1 1758 ? 176.388 122.660 184.089 1.00 89.37  ? 2975 ASN A ND2   1 
ATOM   11924 N  N     . PHE A 1 1759 ? 171.494 124.481 183.269 1.00 85.21  ? 2976 PHE A N     1 
ATOM   11925 C  CA    . PHE A 1 1759 ? 170.550 124.817 182.209 1.00 82.15  ? 2976 PHE A CA    1 
ATOM   11926 C  C     . PHE A 1 1759 ? 170.549 126.314 181.930 1.00 82.89  ? 2976 PHE A C     1 
ATOM   11927 O  O     . PHE A 1 1759 ? 170.610 126.742 180.771 1.00 84.39  ? 2976 PHE A O     1 
ATOM   11928 C  CB    . PHE A 1 1759 ? 169.152 124.331 182.605 1.00 81.41  ? 2976 PHE A CB    1 
ATOM   11929 C  CG    . PHE A 1 1759 ? 168.078 124.639 181.595 1.00 82.12  ? 2976 PHE A CG    1 
ATOM   11930 C  CD1   . PHE A 1 1759 ? 168.323 124.536 180.235 1.00 82.52  ? 2976 PHE A CD1   1 
ATOM   11931 C  CD2   . PHE A 1 1759 ? 166.813 125.021 182.015 1.00 79.52  ? 2976 PHE A CD2   1 
ATOM   11932 C  CE1   . PHE A 1 1759 ? 167.329 124.818 179.315 1.00 84.57  ? 2976 PHE A CE1   1 
ATOM   11933 C  CE2   . PHE A 1 1759 ? 165.818 125.303 181.100 1.00 77.51  ? 2976 PHE A CE2   1 
ATOM   11934 C  CZ    . PHE A 1 1759 ? 166.076 125.201 179.749 1.00 82.13  ? 2976 PHE A CZ    1 
ATOM   11935 N  N     . TYR A 1 1760 ? 170.505 127.131 182.985 1.00 82.71  ? 2977 TYR A N     1 
ATOM   11936 C  CA    . TYR A 1 1760 ? 170.464 128.573 182.784 1.00 80.99  ? 2977 TYR A CA    1 
ATOM   11937 C  C     . TYR A 1 1760 ? 171.815 129.159 182.398 1.00 83.76  ? 2977 TYR A C     1 
ATOM   11938 O  O     . TYR A 1 1760 ? 171.858 130.277 181.874 1.00 86.06  ? 2977 TYR A O     1 
ATOM   11939 C  CB    . TYR A 1 1760 ? 169.930 129.268 184.037 1.00 78.91  ? 2977 TYR A CB    1 
ATOM   11940 C  CG    . TYR A 1 1760 ? 168.423 129.237 184.135 1.00 75.79  ? 2977 TYR A CG    1 
ATOM   11941 C  CD1   . TYR A 1 1760 ? 167.632 129.719 183.101 1.00 74.65  ? 2977 TYR A CD1   1 
ATOM   11942 C  CD2   . TYR A 1 1760 ? 167.791 128.723 185.259 1.00 77.07  ? 2977 TYR A CD2   1 
ATOM   11943 C  CE1   . TYR A 1 1760 ? 166.254 129.693 183.184 1.00 73.94  ? 2977 TYR A CE1   1 
ATOM   11944 C  CE2   . TYR A 1 1760 ? 166.412 128.691 185.351 1.00 76.03  ? 2977 TYR A CE2   1 
ATOM   11945 C  CZ    . TYR A 1 1760 ? 165.650 129.177 184.311 1.00 72.62  ? 2977 TYR A CZ    1 
ATOM   11946 O  OH    . TYR A 1 1760 ? 164.278 129.148 184.399 1.00 67.81  ? 2977 TYR A OH    1 
ATOM   11947 N  N     . GLN A 1 1761 ? 172.915 128.443 182.637 1.00 84.25  ? 2978 GLN A N     1 
ATOM   11948 C  CA    . GLN A 1 1761 ? 174.217 128.925 182.196 1.00 85.00  ? 2978 GLN A CA    1 
ATOM   11949 C  C     . GLN A 1 1761 ? 174.616 128.399 180.825 1.00 86.14  ? 2978 GLN A C     1 
ATOM   11950 O  O     . GLN A 1 1761 ? 175.547 128.941 180.218 1.00 84.94  ? 2978 GLN A O     1 
ATOM   11951 C  CB    . GLN A 1 1761 ? 175.297 128.553 183.219 1.00 81.84  ? 2978 GLN A CB    1 
ATOM   11952 C  CG    . GLN A 1 1761 ? 175.842 127.142 183.078 1.00 81.12  ? 2978 GLN A CG    1 
ATOM   11953 C  CD    . GLN A 1 1761 ? 176.427 126.614 184.372 1.00 83.53  ? 2978 GLN A CD    1 
ATOM   11954 O  OE1   . GLN A 1 1761 ? 176.106 127.100 185.457 1.00 82.03  ? 2978 GLN A OE1   1 
ATOM   11955 N  NE2   . GLN A 1 1761 ? 177.296 125.615 184.265 1.00 85.63  ? 2978 GLN A NE2   1 
ATOM   11956 N  N     . LYS A 1 1762 ? 173.942 127.364 180.321 1.00 87.63  ? 2979 LYS A N     1 
ATOM   11957 C  CA    . LYS A 1 1762 ? 174.232 126.832 178.999 1.00 85.73  ? 2979 LYS A CA    1 
ATOM   11958 C  C     . LYS A 1 1762 ? 173.154 127.134 177.968 1.00 87.27  ? 2979 LYS A C     1 
ATOM   11959 O  O     . LYS A 1 1762 ? 173.375 126.879 176.779 1.00 85.98  ? 2979 LYS A O     1 
ATOM   11960 C  CB    . LYS A 1 1762 ? 174.445 125.313 179.073 1.00 84.13  ? 2979 LYS A CB    1 
ATOM   11961 N  N     . MET A 1 1763 ? 172.003 127.660 178.380 1.00 90.66  ? 2980 MET A N     1 
ATOM   11962 C  CA    . MET A 1 1763 ? 170.945 127.997 177.434 1.00 91.53  ? 2980 MET A CA    1 
ATOM   11963 C  C     . MET A 1 1763 ? 171.333 129.208 176.590 1.00 88.77  ? 2980 MET A C     1 
ATOM   11964 O  O     . MET A 1 1763 ? 171.848 129.065 175.481 1.00 83.08  ? 2980 MET A O     1 
ATOM   11965 C  CB    . MET A 1 1763 ? 169.630 128.268 178.168 1.00 88.96  ? 2980 MET A CB    1 
ATOM   11966 C  CG    . MET A 1 1763 ? 168.678 129.185 177.416 1.00 93.63  ? 2980 MET A CG    1 
ATOM   11967 S  SD    . MET A 1 1763 ? 167.379 129.865 178.463 1.00 106.45 ? 2980 MET A SD    1 
ATOM   11968 C  CE    . MET A 1 1763 ? 168.357 130.723 179.693 1.00 86.32  ? 2980 MET A CE    1 
ATOM   11969 N  N     . ASN A 1 1768 ? 169.539 139.352 183.109 1.00 92.71  ? 2985 ASN A N     1 
ATOM   11970 C  CA    . ASN A 1 1768 ? 168.138 138.970 183.240 1.00 93.92  ? 2985 ASN A CA    1 
ATOM   11971 C  C     . ASN A 1 1768 ? 167.962 138.002 184.407 1.00 92.54  ? 2985 ASN A C     1 
ATOM   11972 O  O     . ASN A 1 1768 ? 168.752 137.073 184.569 1.00 91.00  ? 2985 ASN A O     1 
ATOM   11973 C  CB    . ASN A 1 1768 ? 167.630 138.341 181.940 1.00 98.33  ? 2985 ASN A CB    1 
ATOM   11974 C  CG    . ASN A 1 1768 ? 166.117 138.195 181.907 1.00 100.81 ? 2985 ASN A CG    1 
ATOM   11975 O  OD1   . ASN A 1 1768 ? 165.410 138.689 182.786 1.00 94.02  ? 2985 ASN A OD1   1 
ATOM   11976 N  ND2   . ASN A 1 1768 ? 165.614 137.512 180.885 1.00 107.05 ? 2985 ASN A ND2   1 
ATOM   11977 N  N     . PRO A 1 1769 ? 166.936 138.229 185.222 1.00 90.53  ? 2986 PRO A N     1 
ATOM   11978 C  CA    . PRO A 1 1769 ? 166.671 137.315 186.338 1.00 87.85  ? 2986 PRO A CA    1 
ATOM   11979 C  C     . PRO A 1 1769 ? 166.205 135.953 185.847 1.00 91.10  ? 2986 PRO A C     1 
ATOM   11980 O  O     . PRO A 1 1769 ? 165.650 135.814 184.754 1.00 93.99  ? 2986 PRO A O     1 
ATOM   11981 C  CB    . PRO A 1 1769 ? 165.569 138.030 187.128 1.00 85.40  ? 2986 PRO A CB    1 
ATOM   11982 N  N     . ARG A 1 1770 ? 166.440 134.939 186.675 1.00 84.88  ? 2987 ARG A N     1 
ATOM   11983 C  CA    . ARG A 1 1770 ? 166.124 133.556 186.344 1.00 76.46  ? 2987 ARG A CA    1 
ATOM   11984 C  C     . ARG A 1 1770 ? 164.907 133.116 187.148 1.00 68.35  ? 2987 ARG A C     1 
ATOM   11985 O  O     . ARG A 1 1770 ? 164.941 133.112 188.383 1.00 62.38  ? 2987 ARG A O     1 
ATOM   11986 C  CB    . ARG A 1 1770 ? 167.322 132.650 186.620 1.00 74.27  ? 2987 ARG A CB    1 
ATOM   11987 C  CG    . ARG A 1 1770 ? 168.568 133.060 185.854 1.00 79.64  ? 2987 ARG A CG    1 
ATOM   11988 C  CD    . ARG A 1 1770 ? 168.336 132.964 184.355 1.00 85.50  ? 2987 ARG A CD    1 
ATOM   11989 N  NE    . ARG A 1 1770 ? 169.552 133.202 183.588 1.00 91.20  ? 2987 ARG A NE    1 
ATOM   11990 C  CZ    . ARG A 1 1770 ? 169.822 134.327 182.940 1.00 92.77  ? 2987 ARG A CZ    1 
ATOM   11991 N  NH1   . ARG A 1 1770 ? 168.970 135.338 182.927 1.00 90.52  ? 2987 ARG A NH1   1 
ATOM   11992 N  NH2   . ARG A 1 1770 ? 170.973 134.438 182.283 1.00 94.48  ? 2987 ARG A NH2   1 
ATOM   11993 N  N     . SER A 1 1771 ? 163.842 132.744 186.445 1.00 64.70  ? 2988 SER A N     1 
ATOM   11994 C  CA    . SER A 1 1771 ? 162.567 132.437 187.078 1.00 62.94  ? 2988 SER A CA    1 
ATOM   11995 C  C     . SER A 1 1771 ? 162.589 131.043 187.702 1.00 60.08  ? 2988 SER A C     1 
ATOM   11996 O  O     . SER A 1 1771 ? 163.181 130.118 187.141 1.00 62.74  ? 2988 SER A O     1 
ATOM   11997 C  CB    . SER A 1 1771 ? 161.434 132.524 186.060 1.00 64.73  ? 2988 SER A CB    1 
ATOM   11998 O  OG    . SER A 1 1771 ? 161.511 131.465 185.122 1.00 62.00  ? 2988 SER A OG    1 
ATOM   11999 N  N     . PRO A 1 1772 ? 161.958 130.871 188.862 1.00 56.81  ? 2989 PRO A N     1 
ATOM   12000 C  CA    . PRO A 1 1772 ? 161.723 129.529 189.415 1.00 57.00  ? 2989 PRO A CA    1 
ATOM   12001 C  C     . PRO A 1 1772 ? 160.426 128.870 188.967 1.00 57.59  ? 2989 PRO A C     1 
ATOM   12002 O  O     . PRO A 1 1772 ? 160.016 127.889 189.595 1.00 55.18  ? 2989 PRO A O     1 
ATOM   12003 C  CB    . PRO A 1 1772 ? 161.681 129.807 190.922 1.00 52.80  ? 2989 PRO A CB    1 
ATOM   12004 C  CG    . PRO A 1 1772 ? 161.076 131.154 191.010 1.00 56.99  ? 2989 PRO A CG    1 
ATOM   12005 C  CD    . PRO A 1 1772 ? 161.604 131.926 189.826 1.00 60.81  ? 2989 PRO A CD    1 
ATOM   12006 N  N     . GLY A 1 1773 ? 159.765 129.389 187.928 1.00 58.97  ? 2990 GLY A N     1 
ATOM   12007 C  CA    . GLY A 1 1773 ? 158.523 128.782 187.473 1.00 58.04  ? 2990 GLY A CA    1 
ATOM   12008 C  C     . GLY A 1 1773 ? 158.723 127.373 186.950 1.00 62.96  ? 2990 GLY A C     1 
ATOM   12009 O  O     . GLY A 1 1773 ? 157.974 126.455 187.298 1.00 68.00  ? 2990 GLY A O     1 
ATOM   12010 N  N     . TYR A 1 1774 ? 159.750 127.183 186.115 1.00 63.75  ? 2991 TYR A N     1 
ATOM   12011 C  CA    . TYR A 1 1774 ? 160.142 125.837 185.709 1.00 61.80  ? 2991 TYR A CA    1 
ATOM   12012 C  C     . TYR A 1 1774 ? 160.518 124.995 186.919 1.00 65.67  ? 2991 TYR A C     1 
ATOM   12013 O  O     . TYR A 1 1774 ? 160.109 123.835 187.027 1.00 69.42  ? 2991 TYR A O     1 
ATOM   12014 C  CB    . TYR A 1 1774 ? 161.318 125.896 184.734 1.00 56.06  ? 2991 TYR A CB    1 
ATOM   12015 C  CG    . TYR A 1 1774 ? 161.005 126.448 183.364 1.00 58.42  ? 2991 TYR A CG    1 
ATOM   12016 C  CD1   . TYR A 1 1774 ? 159.722 126.384 182.842 1.00 62.38  ? 2991 TYR A CD1   1 
ATOM   12017 C  CD2   . TYR A 1 1774 ? 162.004 127.017 182.584 1.00 60.23  ? 2991 TYR A CD2   1 
ATOM   12018 C  CE1   . TYR A 1 1774 ? 159.438 126.885 181.584 1.00 67.49  ? 2991 TYR A CE1   1 
ATOM   12019 C  CE2   . TYR A 1 1774 ? 161.732 127.520 181.328 1.00 62.89  ? 2991 TYR A CE2   1 
ATOM   12020 C  CZ    . TYR A 1 1774 ? 160.447 127.451 180.833 1.00 68.52  ? 2991 TYR A CZ    1 
ATOM   12021 O  OH    . TYR A 1 1774 ? 160.167 127.950 179.582 1.00 72.74  ? 2991 TYR A OH    1 
ATOM   12022 N  N     . PHE A 1 1775 ? 161.275 125.580 187.849 1.00 64.28  ? 2992 PHE A N     1 
ATOM   12023 C  CA    . PHE A 1 1775 ? 161.721 124.868 189.044 1.00 61.29  ? 2992 PHE A CA    1 
ATOM   12024 C  C     . PHE A 1 1775 ? 160.541 124.427 189.905 1.00 61.09  ? 2992 PHE A C     1 
ATOM   12025 O  O     . PHE A 1 1775 ? 160.442 123.256 190.297 1.00 65.02  ? 2992 PHE A O     1 
ATOM   12026 C  CB    . PHE A 1 1775 ? 162.663 125.777 189.834 1.00 60.98  ? 2992 PHE A CB    1 
ATOM   12027 C  CG    . PHE A 1 1775 ? 163.610 125.049 190.732 1.00 59.24  ? 2992 PHE A CG    1 
ATOM   12028 C  CD1   . PHE A 1 1775 ? 164.830 124.607 190.256 1.00 59.54  ? 2992 PHE A CD1   1 
ATOM   12029 C  CD2   . PHE A 1 1775 ? 163.297 124.837 192.063 1.00 60.79  ? 2992 PHE A CD2   1 
ATOM   12030 C  CE1   . PHE A 1 1775 ? 165.710 123.946 191.084 1.00 65.82  ? 2992 PHE A CE1   1 
ATOM   12031 C  CE2   . PHE A 1 1775 ? 164.174 124.179 192.896 1.00 63.60  ? 2992 PHE A CE2   1 
ATOM   12032 C  CZ    . PHE A 1 1775 ? 165.380 123.731 192.405 1.00 67.69  ? 2992 PHE A CZ    1 
ATOM   12033 N  N     . ILE A 1 1776 ? 159.624 125.355 190.193 1.00 58.45  ? 2993 ILE A N     1 
ATOM   12034 C  CA    . ILE A 1 1776 ? 158.493 125.046 191.063 1.00 61.64  ? 2993 ILE A CA    1 
ATOM   12035 C  C     . ILE A 1 1776 ? 157.549 124.057 190.390 1.00 66.23  ? 2993 ILE A C     1 
ATOM   12036 O  O     . ILE A 1 1776 ? 157.069 123.111 191.027 1.00 69.45  ? 2993 ILE A O     1 
ATOM   12037 C  CB    . ILE A 1 1776 ? 157.771 126.341 191.478 1.00 59.49  ? 2993 ILE A CB    1 
ATOM   12038 C  CG1   . ILE A 1 1776 ? 158.643 127.144 192.442 1.00 62.71  ? 2993 ILE A CG1   1 
ATOM   12039 C  CG2   . ILE A 1 1776 ? 156.430 126.034 192.130 1.00 64.29  ? 2993 ILE A CG2   1 
ATOM   12040 C  CD1   . ILE A 1 1776 ? 158.932 126.427 193.740 1.00 67.00  ? 2993 ILE A CD1   1 
ATOM   12041 N  N     . ASP A 1 1777 ? 157.275 124.246 189.095 1.00 65.21  ? 2994 ASP A N     1 
ATOM   12042 C  CA    . ASP A 1 1777 ? 156.406 123.310 188.388 1.00 64.80  ? 2994 ASP A CA    1 
ATOM   12043 C  C     . ASP A 1 1777 ? 157.031 121.923 188.306 1.00 69.02  ? 2994 ASP A C     1 
ATOM   12044 O  O     . ASP A 1 1777 ? 156.327 120.914 188.425 1.00 72.49  ? 2994 ASP A O     1 
ATOM   12045 C  CB    . ASP A 1 1777 ? 156.074 123.836 186.992 1.00 66.45  ? 2994 ASP A CB    1 
ATOM   12046 C  CG    . ASP A 1 1777 ? 155.160 125.046 187.027 1.00 67.82  ? 2994 ASP A CG    1 
ATOM   12047 O  OD1   . ASP A 1 1777 ? 154.358 125.162 187.977 1.00 67.13  ? 2994 ASP A OD1   1 
ATOM   12048 O  OD2   . ASP A 1 1777 ? 155.240 125.880 186.101 1.00 67.83  ? 2994 ASP A OD2   1 
ATOM   12049 N  N     . GLY A 1 1778 ? 158.351 121.850 188.120 1.00 72.29  ? 2995 GLY A N     1 
ATOM   12050 C  CA    . GLY A 1 1778 ? 159.015 120.558 188.111 1.00 76.61  ? 2995 GLY A CA    1 
ATOM   12051 C  C     . GLY A 1 1778 ? 158.939 119.848 189.447 1.00 74.39  ? 2995 GLY A C     1 
ATOM   12052 O  O     . GLY A 1 1778 ? 158.659 118.647 189.503 1.00 76.84  ? 2995 GLY A O     1 
ATOM   12053 N  N     . LEU A 1 1779 ? 159.177 120.578 190.542 1.00 69.58  ? 2996 LEU A N     1 
ATOM   12054 C  CA    . LEU A 1 1779 ? 159.058 119.969 191.864 1.00 66.89  ? 2996 LEU A CA    1 
ATOM   12055 C  C     . LEU A 1 1779 ? 157.630 119.518 192.147 1.00 72.21  ? 2996 LEU A C     1 
ATOM   12056 O  O     . LEU A 1 1779 ? 157.416 118.436 192.707 1.00 75.16  ? 2996 LEU A O     1 
ATOM   12057 C  CB    . LEU A 1 1779 ? 159.536 120.936 192.943 1.00 62.10  ? 2996 LEU A CB    1 
ATOM   12058 C  CG    . LEU A 1 1779 ? 161.004 121.336 192.878 1.00 59.40  ? 2996 LEU A CG    1 
ATOM   12059 C  CD1   . LEU A 1 1779 ? 161.311 122.390 193.918 1.00 63.17  ? 2996 LEU A CD1   1 
ATOM   12060 C  CD2   . LEU A 1 1779 ? 161.863 120.116 193.089 1.00 59.71  ? 2996 LEU A CD2   1 
ATOM   12061 N  N     . ARG A 1 1780 ? 156.641 120.330 191.763 1.00 72.79  ? 2997 ARG A N     1 
ATOM   12062 C  CA    . ARG A 1 1780 ? 155.248 119.954 191.982 1.00 75.45  ? 2997 ARG A CA    1 
ATOM   12063 C  C     . ARG A 1 1780 ? 154.884 118.706 191.185 1.00 80.53  ? 2997 ARG A C     1 
ATOM   12064 O  O     . ARG A 1 1780 ? 154.261 117.778 191.717 1.00 86.05  ? 2997 ARG A O     1 
ATOM   12065 C  CB    . ARG A 1 1780 ? 154.327 121.116 191.613 1.00 73.04  ? 2997 ARG A CB    1 
ATOM   12066 C  CG    . ARG A 1 1780 ? 154.374 122.280 192.588 1.00 73.23  ? 2997 ARG A CG    1 
ATOM   12067 C  CD    . ARG A 1 1780 ? 153.248 123.268 192.331 1.00 81.51  ? 2997 ARG A CD    1 
ATOM   12068 N  NE    . ARG A 1 1780 ? 153.241 124.352 193.306 1.00 87.51  ? 2997 ARG A NE    1 
ATOM   12069 C  CZ    . ARG A 1 1780 ? 152.756 125.564 193.074 1.00 82.42  ? 2997 ARG A CZ    1 
ATOM   12070 N  NH1   . ARG A 1 1780 ? 152.210 125.878 191.911 1.00 77.69  ? 2997 ARG A NH1   1 
ATOM   12071 N  NH2   . ARG A 1 1780 ? 152.822 126.484 194.032 1.00 81.40  ? 2997 ARG A NH2   1 
ATOM   12072 N  N     . ALA A 1 1781 ? 155.280 118.664 189.909 1.00 79.06  ? 2998 ALA A N     1 
ATOM   12073 C  CA    . ALA A 1 1781 ? 154.989 117.504 189.074 1.00 82.21  ? 2998 ALA A CA    1 
ATOM   12074 C  C     . ALA A 1 1781 ? 155.669 116.256 189.614 1.00 84.60  ? 2998 ALA A C     1 
ATOM   12075 O  O     . ALA A 1 1781 ? 155.073 115.173 189.624 1.00 86.85  ? 2998 ALA A O     1 
ATOM   12076 C  CB    . ALA A 1 1781 ? 155.421 117.770 187.632 1.00 78.25  ? 2998 ALA A CB    1 
ATOM   12077 N  N     . LEU A 1 1782 ? 156.912 116.395 190.087 1.00 81.98  ? 2999 LEU A N     1 
ATOM   12078 C  CA    . LEU A 1 1782 ? 157.608 115.268 190.698 1.00 81.35  ? 2999 LEU A CA    1 
ATOM   12079 C  C     . LEU A 1 1782 ? 156.877 114.781 191.942 1.00 85.91  ? 2999 LEU A C     1 
ATOM   12080 O  O     . LEU A 1 1782 ? 156.754 113.572 192.156 1.00 92.15  ? 2999 LEU A O     1 
ATOM   12081 C  CB    . LEU A 1 1782 ? 159.048 115.663 191.033 1.00 75.46  ? 2999 LEU A CB    1 
ATOM   12082 C  CG    . LEU A 1 1782 ? 159.867 114.741 191.938 1.00 71.02  ? 2999 LEU A CG    1 
ATOM   12083 C  CD1   . LEU A 1 1782 ? 160.147 113.424 191.248 1.00 84.43  ? 2999 LEU A CD1   1 
ATOM   12084 C  CD2   . LEU A 1 1782 ? 161.168 115.410 192.346 1.00 62.57  ? 2999 LEU A CD2   1 
ATOM   12085 N  N     . VAL A 1 1783 ? 156.359 115.705 192.756 1.00 83.40  ? 3000 VAL A N     1 
ATOM   12086 C  CA    . VAL A 1 1783 ? 155.663 115.315 193.983 1.00 83.41  ? 3000 VAL A CA    1 
ATOM   12087 C  C     . VAL A 1 1783 ? 154.392 114.534 193.661 1.00 90.97  ? 3000 VAL A C     1 
ATOM   12088 O  O     . VAL A 1 1783 ? 154.154 113.448 194.211 1.00 95.40  ? 3000 VAL A O     1 
ATOM   12089 C  CB    . VAL A 1 1783 ? 155.360 116.554 194.843 1.00 80.31  ? 3000 VAL A CB    1 
ATOM   12090 N  N     . LYS A 1 1784 ? 153.556 115.070 192.761 1.00 91.32  ? 3001 LYS A N     1 
ATOM   12091 C  CA    . LYS A 1 1784 ? 152.312 114.369 192.429 1.00 94.19  ? 3001 LYS A CA    1 
ATOM   12092 C  C     . LYS A 1 1784 ? 152.588 113.040 191.737 1.00 97.97  ? 3001 LYS A C     1 
ATOM   12093 O  O     . LYS A 1 1784 ? 151.900 112.044 192.000 1.00 105.35 ? 3001 LYS A O     1 
ATOM   12094 C  CB    . LYS A 1 1784 ? 151.381 115.226 191.565 1.00 92.93  ? 3001 LYS A CB    1 
ATOM   12095 C  CG    . LYS A 1 1784 ? 151.414 116.718 191.803 1.00 92.64  ? 3001 LYS A CG    1 
ATOM   12096 C  CD    . LYS A 1 1784 ? 150.866 117.104 193.165 1.00 89.68  ? 3001 LYS A CD    1 
ATOM   12097 C  CE    . LYS A 1 1784 ? 150.924 118.612 193.357 1.00 86.47  ? 3001 LYS A CE    1 
ATOM   12098 N  NZ    . LYS A 1 1784 ? 149.884 119.105 194.301 1.00 86.94  ? 3001 LYS A NZ    1 
ATOM   12099 N  N     . LEU A 1 1785 ? 153.588 113.000 190.850 1.00 96.36  ? 3002 LEU A N     1 
ATOM   12100 C  CA    . LEU A 1 1785 ? 153.916 111.757 190.164 1.00 102.31 ? 3002 LEU A CA    1 
ATOM   12101 C  C     . LEU A 1 1785 ? 154.434 110.704 191.136 1.00 103.63 ? 3002 LEU A C     1 
ATOM   12102 O  O     . LEU A 1 1785 ? 154.065 109.531 191.029 1.00 107.52 ? 3002 LEU A O     1 
ATOM   12103 C  CB    . LEU A 1 1785 ? 154.933 112.023 189.056 1.00 99.49  ? 3002 LEU A CB    1 
ATOM   12104 N  N     . VAL A 1 1786 ? 155.274 111.101 192.099 1.00 101.74 ? 3003 VAL A N     1 
ATOM   12105 C  CA    . VAL A 1 1786 ? 155.757 110.158 193.106 1.00 103.44 ? 3003 VAL A CA    1 
ATOM   12106 C  C     . VAL A 1 1786 ? 154.601 109.624 193.940 1.00 107.73 ? 3003 VAL A C     1 
ATOM   12107 O  O     . VAL A 1 1786 ? 154.515 108.418 194.191 1.00 113.32 ? 3003 VAL A O     1 
ATOM   12108 C  CB    . VAL A 1 1786 ? 156.842 110.806 193.989 1.00 102.32 ? 3003 VAL A CB    1 
ATOM   12109 C  CG1   . VAL A 1 1786 ? 157.068 109.988 195.250 1.00 96.85  ? 3003 VAL A CG1   1 
ATOM   12110 C  CG2   . VAL A 1 1786 ? 158.149 110.898 193.233 1.00 98.36  ? 3003 VAL A CG2   1 
ATOM   12111 N  N     . THR A 1 1787 ? 153.682 110.501 194.360 1.00 105.93 ? 3004 THR A N     1 
ATOM   12112 C  CA    . THR A 1 1787 ? 152.561 110.042 195.182 1.00 108.82 ? 3004 THR A CA    1 
ATOM   12113 C  C     . THR A 1 1787 ? 151.672 109.063 194.417 1.00 112.03 ? 3004 THR A C     1 
ATOM   12114 O  O     . THR A 1 1787 ? 151.348 107.977 194.920 1.00 116.42 ? 3004 THR A O     1 
ATOM   12115 C  CB    . THR A 1 1787 ? 151.739 111.233 195.677 1.00 106.42 ? 3004 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 1787 ? 151.432 112.096 194.578 1.00 104.85 ? 3004 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 1787 ? 152.511 112.011 196.732 1.00 105.80 ? 3004 THR A CG2   1 
ATOM   12118 N  N     . ALA A 1 1788 ? 151.288 109.420 193.186 1.00 109.52 ? 3005 ALA A N     1 
ATOM   12119 C  CA    . ALA A 1 1788 ? 150.413 108.552 192.400 1.00 112.97 ? 3005 ALA A CA    1 
ATOM   12120 C  C     . ALA A 1 1788 ? 151.098 107.237 192.041 1.00 120.51 ? 3005 ALA A C     1 
ATOM   12121 O  O     . ALA A 1 1788 ? 150.479 106.167 192.113 1.00 123.57 ? 3005 ALA A O     1 
ATOM   12122 C  CB    . ALA A 1 1788 ? 149.951 109.279 191.138 1.00 110.33 ? 3005 ALA A CB    1 
ATOM   12123 N  N     . LYS A 1 1789 ? 152.379 107.293 191.665 1.00 119.81 ? 3006 LYS A N     1 
ATOM   12124 C  CA    . LYS A 1 1789 ? 153.098 106.088 191.277 1.00 119.15 ? 3006 LYS A CA    1 
ATOM   12125 C  C     . LYS A 1 1789 ? 153.362 105.185 192.475 1.00 121.51 ? 3006 LYS A C     1 
ATOM   12126 O  O     . LYS A 1 1789 ? 153.330 103.959 192.339 1.00 125.89 ? 3006 LYS A O     1 
ATOM   12127 C  CB    . LYS A 1 1789 ? 154.403 106.480 190.586 1.00 115.83 ? 3006 LYS A CB    1 
ATOM   12128 C  CG    . LYS A 1 1789 ? 155.075 105.368 189.815 1.00 118.27 ? 3006 LYS A CG    1 
ATOM   12129 C  CD    . LYS A 1 1789 ? 155.990 105.945 188.748 1.00 113.88 ? 3006 LYS A CD    1 
ATOM   12130 C  CE    . LYS A 1 1789 ? 155.219 106.286 187.485 1.00 110.80 ? 3006 LYS A CE    1 
ATOM   12131 N  NZ    . LYS A 1 1789 ? 156.130 106.677 186.374 1.00 108.10 ? 3006 LYS A NZ    1 
ATOM   12132 N  N     . TYR A 1 1790 ? 153.601 105.765 193.654 1.00 120.67 ? 3007 TYR A N     1 
ATOM   12133 C  CA    . TYR A 1 1790 ? 153.759 104.960 194.858 1.00 124.98 ? 3007 TYR A CA    1 
ATOM   12134 C  C     . TYR A 1 1790 ? 152.441 104.314 195.260 1.00 128.27 ? 3007 TYR A C     1 
ATOM   12135 O  O     . TYR A 1 1790 ? 152.428 103.174 195.734 1.00 132.63 ? 3007 TYR A O     1 
ATOM   12136 C  CB    . TYR A 1 1790 ? 154.309 105.821 195.995 1.00 126.46 ? 3007 TYR A CB    1 
ATOM   12137 C  CG    . TYR A 1 1790 ? 154.734 105.035 197.215 1.00 128.53 ? 3007 TYR A CG    1 
ATOM   12138 C  CD1   . TYR A 1 1790 ? 155.971 104.405 197.260 1.00 126.85 ? 3007 TYR A CD1   1 
ATOM   12139 C  CD2   . TYR A 1 1790 ? 153.901 104.927 198.321 1.00 128.88 ? 3007 TYR A CD2   1 
ATOM   12140 C  CE1   . TYR A 1 1790 ? 156.367 103.688 198.373 1.00 128.88 ? 3007 TYR A CE1   1 
ATOM   12141 C  CE2   . TYR A 1 1790 ? 154.288 104.211 199.438 1.00 130.28 ? 3007 TYR A CE2   1 
ATOM   12142 C  CZ    . TYR A 1 1790 ? 155.521 103.594 199.459 1.00 132.79 ? 3007 TYR A CZ    1 
ATOM   12143 O  OH    . TYR A 1 1790 ? 155.910 102.881 200.569 1.00 134.19 ? 3007 TYR A OH    1 
ATOM   12144 N  N     . GLN A 1 1791 ? 151.321 105.022 195.079 1.00 126.40 ? 3008 GLN A N     1 
ATOM   12145 C  CA    . GLN A 1 1791 ? 150.019 104.406 195.327 1.00 129.17 ? 3008 GLN A CA    1 
ATOM   12146 C  C     . GLN A 1 1791 ? 149.766 103.245 194.371 1.00 134.45 ? 3008 GLN A C     1 
ATOM   12147 O  O     . GLN A 1 1791 ? 149.278 102.182 194.783 1.00 137.08 ? 3008 GLN A O     1 
ATOM   12148 C  CB    . GLN A 1 1791 ? 148.912 105.453 195.206 1.00 124.24 ? 3008 GLN A CB    1 
ATOM   12149 N  N     . ASP A 1 1792 ? 150.103 103.427 193.090 1.00 134.29 ? 3009 ASP A N     1 
ATOM   12150 C  CA    . ASP A 1 1792 ? 149.935 102.352 192.114 1.00 135.80 ? 3009 ASP A CA    1 
ATOM   12151 C  C     . ASP A 1 1792 ? 150.833 101.161 192.434 1.00 139.76 ? 3009 ASP A C     1 
ATOM   12152 O  O     . ASP A 1 1792 ? 150.407 100.005 192.324 1.00 141.46 ? 3009 ASP A O     1 
ATOM   12153 C  CB    . ASP A 1 1792 ? 150.219 102.874 190.705 1.00 132.07 ? 3009 ASP A CB    1 
ATOM   12154 N  N     . LEU A 1 1793 ? 152.078 101.423 192.841 1.00 139.57 ? 3010 LEU A N     1 
ATOM   12155 C  CA    . LEU A 1 1793 ? 152.985 100.340 193.203 1.00 139.80 ? 3010 LEU A CA    1 
ATOM   12156 C  C     . LEU A 1 1793 ? 152.541 99.638  194.480 1.00 142.55 ? 3010 LEU A C     1 
ATOM   12157 O  O     . LEU A 1 1793 ? 152.725 98.424  194.607 1.00 143.03 ? 3010 LEU A O     1 
ATOM   12158 C  CB    . LEU A 1 1793 ? 154.412 100.877 193.344 1.00 137.63 ? 3010 LEU A CB    1 
ATOM   12159 C  CG    . LEU A 1 1793 ? 155.541 99.880  193.626 1.00 137.30 ? 3010 LEU A CG    1 
ATOM   12160 C  CD1   . LEU A 1 1793 ? 156.758 100.201 192.776 1.00 132.86 ? 3010 LEU A CD1   1 
ATOM   12161 C  CD2   . LEU A 1 1793 ? 155.918 99.892  195.102 1.00 138.09 ? 3010 LEU A CD2   1 
ATOM   12162 N  N     . GLN A 1 1794 ? 151.958 100.373 195.430 1.00 143.13 ? 3011 GLN A N     1 
ATOM   12163 C  CA    . GLN A 1 1794 ? 151.408 99.742  196.626 1.00 143.93 ? 3011 GLN A CA    1 
ATOM   12164 C  C     . GLN A 1 1794 ? 150.230 98.841  196.280 1.00 147.21 ? 3011 GLN A C     1 
ATOM   12165 O  O     . GLN A 1 1794 ? 150.101 97.741  196.830 1.00 149.64 ? 3011 GLN A O     1 
ATOM   12166 C  CB    . GLN A 1 1794 ? 150.990 100.808 197.638 1.00 137.81 ? 3011 GLN A CB    1 
ATOM   12167 N  N     . GLU A 1 1795 ? 149.364 99.291  195.367 1.00 146.78 ? 3012 GLU A N     1 
ATOM   12168 C  CA    . GLU A 1 1795 ? 148.265 98.443  194.910 1.00 148.73 ? 3012 GLU A CA    1 
ATOM   12169 C  C     . GLU A 1 1795 ? 148.786 97.194  194.206 1.00 147.54 ? 3012 GLU A C     1 
ATOM   12170 O  O     . GLU A 1 1795 ? 148.272 96.088  194.422 1.00 147.08 ? 3012 GLU A O     1 
ATOM   12171 C  CB    . GLU A 1 1795 ? 147.340 99.235  193.986 1.00 147.38 ? 3012 GLU A CB    1 
ATOM   12172 N  N     . ASN A 1 1796 ? 149.813 97.353  193.365 1.00 147.56 ? 3013 ASN A N     1 
ATOM   12173 C  CA    . ASN A 1 1796 ? 150.397 96.209  192.671 1.00 150.26 ? 3013 ASN A CA    1 
ATOM   12174 C  C     . ASN A 1 1796 ? 151.041 95.233  193.649 1.00 150.86 ? 3013 ASN A C     1 
ATOM   12175 O  O     . ASN A 1 1796 ? 150.921 94.013  193.489 1.00 153.02 ? 3013 ASN A O     1 
ATOM   12176 C  CB    . ASN A 1 1796 ? 151.420 96.687  191.640 1.00 148.38 ? 3013 ASN A CB    1 
ATOM   12177 N  N     . GLN A 1 1797 ? 151.731 95.752  194.669 1.00 148.92 ? 3014 GLN A N     1 
ATOM   12178 C  CA    . GLN A 1 1797 ? 152.344 94.891  195.676 1.00 148.54 ? 3014 GLN A CA    1 
ATOM   12179 C  C     . GLN A 1 1797 ? 151.291 94.160  196.498 1.00 148.88 ? 3014 GLN A C     1 
ATOM   12180 O  O     . GLN A 1 1797 ? 151.469 92.983  196.831 1.00 148.86 ? 3014 GLN A O     1 
ATOM   12181 C  CB    . GLN A 1 1797 ? 153.258 95.713  196.584 1.00 146.36 ? 3014 GLN A CB    1 
ATOM   12182 C  CG    . GLN A 1 1797 ? 154.694 95.802  196.099 1.00 145.07 ? 3014 GLN A CG    1 
ATOM   12183 C  CD    . GLN A 1 1797 ? 155.297 94.440  195.819 1.00 143.65 ? 3014 GLN A CD    1 
ATOM   12184 O  OE1   . GLN A 1 1797 ? 155.548 94.083  194.668 1.00 141.84 ? 3014 GLN A OE1   1 
ATOM   12185 N  NE2   . GLN A 1 1797 ? 155.533 93.670  196.875 1.00 141.73 ? 3014 GLN A NE2   1 
ATOM   12186 N  N     . ARG A 1 1798 ? 150.191 94.839  196.838 1.00 149.06 ? 3015 ARG A N     1 
ATOM   12187 C  CA    . ARG A 1 1798 ? 149.106 94.177  197.556 1.00 149.28 ? 3015 ARG A CA    1 
ATOM   12188 C  C     . ARG A 1 1798 ? 148.484 93.069  196.715 1.00 150.41 ? 3015 ARG A C     1 
ATOM   12189 O  O     . ARG A 1 1798 ? 148.207 91.974  197.223 1.00 149.55 ? 3015 ARG A O     1 
ATOM   12190 C  CB    . ARG A 1 1798 ? 148.048 95.200  197.967 1.00 148.10 ? 3015 ARG A CB    1 
ATOM   12191 N  N     . PHE A 1 1799 ? 148.269 93.330  195.422 1.00 151.13 ? 3016 PHE A N     1 
ATOM   12192 C  CA    . PHE A 1 1799 ? 147.718 92.306  194.538 1.00 149.93 ? 3016 PHE A CA    1 
ATOM   12193 C  C     . PHE A 1 1799 ? 148.673 91.126  194.389 1.00 150.56 ? 3016 PHE A C     1 
ATOM   12194 O  O     . PHE A 1 1799 ? 148.242 89.966  194.384 1.00 150.21 ? 3016 PHE A O     1 
ATOM   12195 C  CB    . PHE A 1 1799 ? 147.394 92.911  193.173 1.00 146.60 ? 3016 PHE A CB    1 
ATOM   12196 N  N     . VAL A 1 1800 ? 149.975 91.402  194.274 1.00 150.50 ? 3017 VAL A N     1 
ATOM   12197 C  CA    . VAL A 1 1800 ? 150.960 90.334  194.134 1.00 147.52 ? 3017 VAL A CA    1 
ATOM   12198 C  C     . VAL A 1 1800 ? 151.043 89.506  195.410 1.00 151.45 ? 3017 VAL A C     1 
ATOM   12199 O  O     . VAL A 1 1800 ? 151.171 88.278  195.358 1.00 151.83 ? 3017 VAL A O     1 
ATOM   12200 C  CB    . VAL A 1 1800 ? 152.331 90.920  193.750 1.00 144.85 ? 3017 VAL A CB    1 
ATOM   12201 N  N     . ASN A 1 1801 ? 150.977 90.161  196.573 1.00 154.16 ? 3018 ASN A N     1 
ATOM   12202 C  CA    . ASN A 1 1801 ? 150.984 89.436  197.839 1.00 155.02 ? 3018 ASN A CA    1 
ATOM   12203 C  C     . ASN A 1 1801 ? 149.733 88.580  197.994 1.00 155.21 ? 3018 ASN A C     1 
ATOM   12204 O  O     . ASN A 1 1801 ? 149.809 87.447  198.485 1.00 153.72 ? 3018 ASN A O     1 
ATOM   12205 C  CB    . ASN A 1 1801 ? 151.112 90.417  199.004 1.00 152.34 ? 3018 ASN A CB    1 
ATOM   12206 N  N     . VAL A 1 1802 ? 148.576 89.102  197.576 1.00 156.12 ? 3019 VAL A N     1 
ATOM   12207 C  CA    . VAL A 1 1802 ? 147.340 88.324  197.629 1.00 155.82 ? 3019 VAL A CA    1 
ATOM   12208 C  C     . VAL A 1 1802 ? 147.432 87.109  196.714 1.00 156.57 ? 3019 VAL A C     1 
ATOM   12209 O  O     . VAL A 1 1802 ? 147.021 86.002  197.084 1.00 157.95 ? 3019 VAL A O     1 
ATOM   12210 C  CB    . VAL A 1 1802 ? 146.133 89.211  197.273 1.00 153.45 ? 3019 VAL A CB    1 
ATOM   12211 N  N     . GLY A 1 1803 ? 147.976 87.295  195.508 1.00 155.76 ? 3020 GLY A N     1 
ATOM   12212 C  CA    . GLY A 1 1803 ? 148.139 86.173  194.596 1.00 152.96 ? 3020 GLY A CA    1 
ATOM   12213 C  C     . GLY A 1 1803 ? 149.114 85.130  195.110 1.00 150.81 ? 3020 GLY A C     1 
ATOM   12214 O  O     . GLY A 1 1803 ? 148.879 83.926  194.973 1.00 149.77 ? 3020 GLY A O     1 
ATOM   12215 N  N     . LEU A 1 1804 ? 150.221 85.577  195.710 1.00 151.24 ? 3021 LEU A N     1 
ATOM   12216 C  CA    . LEU A 1 1804 ? 151.190 84.646  196.282 1.00 152.34 ? 3021 LEU A CA    1 
ATOM   12217 C  C     . LEU A 1 1804 ? 150.596 83.878  197.457 1.00 155.44 ? 3021 LEU A C     1 
ATOM   12218 O  O     . LEU A 1 1804 ? 150.852 82.679  197.613 1.00 155.32 ? 3021 LEU A O     1 
ATOM   12219 C  CB    . LEU A 1 1804 ? 152.449 85.397  196.712 1.00 150.88 ? 3021 LEU A CB    1 
ATOM   12220 N  N     . GLU A 1 1805 ? 149.804 84.553  198.296 1.00 156.20 ? 3022 GLU A N     1 
ATOM   12221 C  CA    . GLU A 1 1805 ? 149.147 83.871  199.407 1.00 153.92 ? 3022 GLU A CA    1 
ATOM   12222 C  C     . GLU A 1 1805 ? 148.109 82.872  198.911 1.00 154.62 ? 3022 GLU A C     1 
ATOM   12223 O  O     . GLU A 1 1805 ? 147.957 81.789  199.489 1.00 154.43 ? 3022 GLU A O     1 
ATOM   12224 C  CB    . GLU A 1 1805 ? 148.504 84.894  200.343 1.00 149.72 ? 3022 GLU A CB    1 
ATOM   12225 N  N     . LYS A 1 1806 ? 147.377 83.223  197.849 1.00 154.40 ? 3023 LYS A N     1 
ATOM   12226 C  CA    . LYS A 1 1806 ? 146.402 82.298  197.278 1.00 150.73 ? 3023 LYS A CA    1 
ATOM   12227 C  C     . LYS A 1 1806 ? 147.084 81.081  196.664 1.00 150.82 ? 3023 LYS A C     1 
ATOM   12228 O  O     . LYS A 1 1806 ? 146.593 79.954  196.801 1.00 148.66 ? 3023 LYS A O     1 
ATOM   12229 C  CB    . LYS A 1 1806 ? 145.546 83.017  196.235 1.00 147.79 ? 3023 LYS A CB    1 
ATOM   12230 N  N     . LEU A 1 1807 ? 148.213 81.287  195.982 1.00 151.41 ? 3024 LEU A N     1 
ATOM   12231 C  CA    . LEU A 1 1807 ? 148.929 80.165  195.383 1.00 150.24 ? 3024 LEU A CA    1 
ATOM   12232 C  C     . LEU A 1 1807 ? 149.635 79.318  196.434 1.00 151.40 ? 3024 LEU A C     1 
ATOM   12233 O  O     . LEU A 1 1807 ? 149.851 78.120  196.219 1.00 152.24 ? 3024 LEU A O     1 
ATOM   12234 C  CB    . LEU A 1 1807 ? 149.934 80.674  194.350 1.00 147.25 ? 3024 LEU A CB    1 
ATOM   12235 N  N     . ASN A 1 1808 ? 150.000 79.913  197.566 1.00 151.03 ? 3025 ASN A N     1 
ATOM   12236 C  CA    . ASN A 1 1808 ? 150.670 79.180  198.633 1.00 149.72 ? 3025 ASN A CA    1 
ATOM   12237 C  C     . ASN A 1 1808 ? 149.661 78.617  199.628 1.00 147.79 ? 3025 ASN A C     1 
ATOM   12238 O  O     . ASN A 1 1808 ? 149.671 77.423  199.928 1.00 144.10 ? 3025 ASN A O     1 
ATOM   12239 C  CB    . ASN A 1 1808 ? 151.673 80.082  199.355 1.00 148.70 ? 3025 ASN A CB    1 
ATOM   12240 N  N     . SER A 1 2081 ? 154.278 72.346  188.891 1.00 167.62 ? 3298 SER A N     1 
ATOM   12241 C  CA    . SER A 1 2081 ? 153.348 73.395  188.489 1.00 171.81 ? 3298 SER A CA    1 
ATOM   12242 C  C     . SER A 1 2081 ? 153.550 74.657  189.320 1.00 175.44 ? 3298 SER A C     1 
ATOM   12243 O  O     . SER A 1 2081 ? 153.735 75.746  188.778 1.00 175.30 ? 3298 SER A O     1 
ATOM   12244 C  CB    . SER A 1 2081 ? 151.903 72.907  188.616 1.00 171.34 ? 3298 SER A CB    1 
ATOM   12245 N  N     . LEU A 1 2082 ? 153.512 74.502  190.645 1.00 178.31 ? 3299 LEU A N     1 
ATOM   12246 C  CA    . LEU A 1 2082 ? 153.690 75.635  191.544 1.00 177.34 ? 3299 LEU A CA    1 
ATOM   12247 C  C     . LEU A 1 2082 ? 155.142 76.082  191.651 1.00 176.76 ? 3299 LEU A C     1 
ATOM   12248 O  O     . LEU A 1 2082 ? 155.397 77.194  192.129 1.00 176.78 ? 3299 LEU A O     1 
ATOM   12249 C  CB    . LEU A 1 2082 ? 153.157 75.290  192.937 1.00 175.91 ? 3299 LEU A CB    1 
ATOM   12250 N  N     . THR A 1 2083 ? 156.092 75.242  191.229 1.00 176.51 ? 3300 THR A N     1 
ATOM   12251 C  CA    . THR A 1 2083 ? 157.505 75.599  191.330 1.00 174.40 ? 3300 THR A CA    1 
ATOM   12252 C  C     . THR A 1 2083 ? 157.847 76.790  190.442 1.00 173.25 ? 3300 THR A C     1 
ATOM   12253 O  O     . THR A 1 2083 ? 158.598 77.682  190.856 1.00 171.23 ? 3300 THR A O     1 
ATOM   12254 C  CB    . THR A 1 2083 ? 158.378 74.396  190.968 1.00 172.72 ? 3300 THR A CB    1 
ATOM   12255 N  N     . PHE A 1 2084 ? 157.305 76.822  189.221 1.00 174.62 ? 3301 PHE A N     1 
ATOM   12256 C  CA    . PHE A 1 2084 ? 157.555 77.947  188.325 1.00 173.77 ? 3301 PHE A CA    1 
ATOM   12257 C  C     . PHE A 1 2084 ? 156.961 79.238  188.876 1.00 171.74 ? 3301 PHE A C     1 
ATOM   12258 O  O     . PHE A 1 2084 ? 157.588 80.302  188.791 1.00 171.36 ? 3301 PHE A O     1 
ATOM   12259 C  CB    . PHE A 1 2084 ? 156.991 77.646  186.936 1.00 173.23 ? 3301 PHE A CB    1 
ATOM   12260 N  N     . GLU A 1 2085 ? 155.754 79.164  189.444 1.00 170.76 ? 3302 GLU A N     1 
ATOM   12261 C  CA    . GLU A 1 2085 ? 155.138 80.345  190.042 1.00 170.46 ? 3302 GLU A CA    1 
ATOM   12262 C  C     . GLU A 1 2085 ? 155.936 80.838  191.243 1.00 169.94 ? 3302 GLU A C     1 
ATOM   12263 O  O     . GLU A 1 2085 ? 156.114 82.049  191.424 1.00 168.81 ? 3302 GLU A O     1 
ATOM   12264 C  CB    . GLU A 1 2085 ? 153.696 80.036  190.445 1.00 170.35 ? 3302 GLU A CB    1 
ATOM   12265 N  N     . LYS A 1 2086 ? 156.428 79.912  192.073 1.00 169.40 ? 3303 LYS A N     1 
ATOM   12266 C  CA    . LYS A 1 2086 ? 157.248 80.300  193.217 1.00 167.94 ? 3303 LYS A CA    1 
ATOM   12267 C  C     . LYS A 1 2086 ? 158.558 80.937  192.770 1.00 168.29 ? 3303 LYS A C     1 
ATOM   12268 O  O     . LYS A 1 2086 ? 159.014 81.920  193.366 1.00 168.46 ? 3303 LYS A O     1 
ATOM   12269 C  CB    . LYS A 1 2086 ? 157.515 79.086  194.106 1.00 168.00 ? 3303 LYS A CB    1 
ATOM   12270 N  N     . GLU A 1 2087 ? 159.176 80.393  191.717 1.00 169.58 ? 3304 GLU A N     1 
ATOM   12271 C  CA    . GLU A 1 2087 ? 160.406 80.977  191.190 1.00 168.48 ? 3304 GLU A CA    1 
ATOM   12272 C  C     . GLU A 1 2087 ? 160.162 82.371  190.623 1.00 167.49 ? 3304 GLU A C     1 
ATOM   12273 O  O     . GLU A 1 2087 ? 160.978 83.279  190.822 1.00 165.73 ? 3304 GLU A O     1 
ATOM   12274 C  CB    . GLU A 1 2087 ? 161.007 80.061  190.125 1.00 168.25 ? 3304 GLU A CB    1 
ATOM   12275 N  N     . ARG A 1 2088 ? 159.045 82.558  189.913 1.00 169.06 ? 3305 ARG A N     1 
ATOM   12276 C  CA    . ARG A 1 2088 ? 158.713 83.877  189.384 1.00 166.01 ? 3305 ARG A CA    1 
ATOM   12277 C  C     . ARG A 1 2088 ? 158.459 84.877  190.506 1.00 165.51 ? 3305 ARG A C     1 
ATOM   12278 O  O     . ARG A 1 2088 ? 158.892 86.034  190.427 1.00 164.07 ? 3305 ARG A O     1 
ATOM   12279 C  CB    . ARG A 1 2088 ? 157.496 83.781  188.463 1.00 163.73 ? 3305 ARG A CB    1 
ATOM   12280 N  N     . TRP A 1 2089 ? 157.760 84.447  191.561 1.00 167.87 ? 3306 TRP A N     1 
ATOM   12281 C  CA    . TRP A 1 2089 ? 157.518 85.325  192.702 1.00 167.91 ? 3306 TRP A CA    1 
ATOM   12282 C  C     . TRP A 1 2089 ? 158.819 85.695  193.403 1.00 166.20 ? 3306 TRP A C     1 
ATOM   12283 O  O     . TRP A 1 2089 ? 159.009 86.849  193.808 1.00 165.57 ? 3306 TRP A O     1 
ATOM   12284 C  CB    . TRP A 1 2089 ? 156.550 84.658  193.680 1.00 167.39 ? 3306 TRP A CB    1 
ATOM   12285 N  N     . LEU A 1 2090 ? 159.729 84.727  193.554 1.00 165.76 ? 3307 LEU A N     1 
ATOM   12286 C  CA    . LEU A 1 2090 ? 161.022 85.009  194.170 1.00 163.85 ? 3307 LEU A CA    1 
ATOM   12287 C  C     . LEU A 1 2090 ? 161.842 85.976  193.324 1.00 164.33 ? 3307 LEU A C     1 
ATOM   12288 O  O     . LEU A 1 2090 ? 162.494 86.880  193.860 1.00 164.41 ? 3307 LEU A O     1 
ATOM   12289 C  CB    . LEU A 1 2090 ? 161.791 83.706  194.395 1.00 163.25 ? 3307 LEU A CB    1 
ATOM   12290 N  N     . ASN A 1 2091 ? 161.817 85.805  191.999 1.00 164.86 ? 3308 ASN A N     1 
ATOM   12291 C  CA    . ASN A 1 2091 ? 162.537 86.721  191.118 1.00 163.22 ? 3308 ASN A CA    1 
ATOM   12292 C  C     . ASN A 1 2091 ? 161.958 88.130  191.188 1.00 161.61 ? 3308 ASN A C     1 
ATOM   12293 O  O     . ASN A 1 2091 ? 162.706 89.117  191.205 1.00 159.51 ? 3308 ASN A O     1 
ATOM   12294 C  CB    . ASN A 1 2091 ? 162.507 86.199  189.681 1.00 161.94 ? 3308 ASN A CB    1 
ATOM   12295 N  N     . THR A 1 2092 ? 160.626 88.243  191.229 1.00 161.56 ? 3309 THR A N     1 
ATOM   12296 C  CA    . THR A 1 2092 ? 159.995 89.553  191.356 1.00 159.76 ? 3309 THR A CA    1 
ATOM   12297 C  C     . THR A 1 2092 ? 160.349 90.214  192.684 1.00 159.94 ? 3309 THR A C     1 
ATOM   12298 O  O     . THR A 1 2092 ? 160.641 91.416  192.731 1.00 158.81 ? 3309 THR A O     1 
ATOM   12299 C  CB    . THR A 1 2092 ? 158.478 89.424  191.212 1.00 157.91 ? 3309 THR A CB    1 
ATOM   12300 N  N     . THR A 1 2093 ? 160.337 89.441  193.775 1.00 159.86 ? 3310 THR A N     1 
ATOM   12301 C  CA    . THR A 1 2093 ? 160.704 89.992  195.076 1.00 157.59 ? 3310 THR A CA    1 
ATOM   12302 C  C     . THR A 1 2093 ? 162.172 90.399  195.121 1.00 158.22 ? 3310 THR A C     1 
ATOM   12303 O  O     . THR A 1 2093 ? 162.523 91.368  195.804 1.00 159.84 ? 3310 THR A O     1 
ATOM   12304 C  CB    . THR A 1 2093 ? 160.402 88.982  196.183 1.00 154.04 ? 3310 THR A CB    1 
ATOM   12305 N  N     . LYS A 1 2094 ? 163.038 89.675  194.409 1.00 158.36 ? 3311 LYS A N     1 
ATOM   12306 C  CA    . LYS A 1 2094 ? 164.447 90.053  194.354 1.00 157.87 ? 3311 LYS A CA    1 
ATOM   12307 C  C     . LYS A 1 2094 ? 164.649 91.328  193.542 1.00 156.72 ? 3311 LYS A C     1 
ATOM   12308 O  O     . LYS A 1 2094 ? 165.473 92.176  193.905 1.00 156.59 ? 3311 LYS A O     1 
ATOM   12309 C  CB    . LYS A 1 2094 ? 165.274 88.908  193.771 1.00 157.31 ? 3311 LYS A CB    1 
ATOM   12310 N  N     . GLN A 1 2095 ? 163.911 91.481  192.441 1.00 155.49 ? 3312 GLN A N     1 
ATOM   12311 C  CA    . GLN A 1 2095 ? 164.078 92.644  191.577 1.00 152.82 ? 3312 GLN A CA    1 
ATOM   12312 C  C     . GLN A 1 2095 ? 163.261 93.853  192.020 1.00 148.64 ? 3312 GLN A C     1 
ATOM   12313 O  O     . GLN A 1 2095 ? 163.391 94.919  191.407 1.00 146.70 ? 3312 GLN A O     1 
ATOM   12314 C  CB    . GLN A 1 2095 ? 163.708 92.282  190.136 1.00 149.73 ? 3312 GLN A CB    1 
ATOM   12315 N  N     . PHE A 1 2096 ? 162.424 93.708  193.053 1.00 148.45 ? 3313 PHE A N     1 
ATOM   12316 C  CA    . PHE A 1 2096 ? 161.562 94.808  193.482 1.00 148.49 ? 3313 PHE A CA    1 
ATOM   12317 C  C     . PHE A 1 2096 ? 162.358 96.016  193.972 1.00 148.16 ? 3313 PHE A C     1 
ATOM   12318 O  O     . PHE A 1 2096 ? 161.949 97.161  193.750 1.00 148.44 ? 3313 PHE A O     1 
ATOM   12319 C  CB    . PHE A 1 2096 ? 160.606 94.325  194.573 1.00 149.43 ? 3313 PHE A CB    1 
ATOM   12320 C  CG    . PHE A 1 2096 ? 159.913 95.437  195.302 1.00 148.99 ? 3313 PHE A CG    1 
ATOM   12321 C  CD1   . PHE A 1 2096 ? 158.952 96.205  194.666 1.00 146.29 ? 3313 PHE A CD1   1 
ATOM   12322 C  CD2   . PHE A 1 2096 ? 160.226 95.721  196.622 1.00 149.08 ? 3313 PHE A CD2   1 
ATOM   12323 C  CE1   . PHE A 1 2096 ? 158.314 97.233  195.332 1.00 144.43 ? 3313 PHE A CE1   1 
ATOM   12324 C  CE2   . PHE A 1 2096 ? 159.592 96.749  197.294 1.00 146.98 ? 3313 PHE A CE2   1 
ATOM   12325 C  CZ    . PHE A 1 2096 ? 158.634 97.506  196.647 1.00 145.71 ? 3313 PHE A CZ    1 
ATOM   12326 N  N     . SER A 1 2097 ? 163.481 95.788  194.658 1.00 146.56 ? 3314 SER A N     1 
ATOM   12327 C  CA    . SER A 1 2097 ? 164.266 96.908  195.178 1.00 146.21 ? 3314 SER A CA    1 
ATOM   12328 C  C     . SER A 1 2097 ? 164.876 97.732  194.047 1.00 144.31 ? 3314 SER A C     1 
ATOM   12329 O  O     . SER A 1 2097 ? 164.818 98.972  194.059 1.00 140.98 ? 3314 SER A O     1 
ATOM   12330 C  CB    . SER A 1 2097 ? 165.355 96.390  196.117 1.00 143.28 ? 3314 SER A CB    1 
ATOM   12331 O  OG    . SER A 1 2097 ? 166.183 95.446  195.461 1.00 138.79 ? 3314 SER A OG    1 
ATOM   12332 N  N     . LYS A 1 2098 ? 165.464 97.053  193.057 1.00 143.97 ? 3315 LYS A N     1 
ATOM   12333 C  CA    . LYS A 1 2098 ? 165.978 97.749  191.883 1.00 141.33 ? 3315 LYS A CA    1 
ATOM   12334 C  C     . LYS A 1 2098 ? 164.851 98.428  191.120 1.00 140.93 ? 3315 LYS A C     1 
ATOM   12335 O  O     . LYS A 1 2098 ? 165.036 99.520  190.572 1.00 139.17 ? 3315 LYS A O     1 
ATOM   12336 C  CB    . LYS A 1 2098 ? 166.731 96.772  190.980 1.00 139.19 ? 3315 LYS A CB    1 
ATOM   12337 N  N     . THR A 1 2099 ? 163.669 97.803  191.094 1.00 141.64 ? 3316 THR A N     1 
ATOM   12338 C  CA    . THR A 1 2099 ? 162.511 98.421  190.457 1.00 139.06 ? 3316 THR A CA    1 
ATOM   12339 C  C     . THR A 1 2099 ? 162.118 99.717  191.157 1.00 138.90 ? 3316 THR A C     1 
ATOM   12340 O  O     . THR A 1 2099 ? 161.786 100.705 190.500 1.00 138.39 ? 3316 THR A O     1 
ATOM   12341 C  CB    . THR A 1 2099 ? 161.338 97.439  190.443 1.00 139.21 ? 3316 THR A CB    1 
ATOM   12342 O  OG1   . THR A 1 2099 ? 161.739 96.224  189.798 1.00 137.99 ? 3316 THR A OG1   1 
ATOM   12343 C  CG2   . THR A 1 2099 ? 160.148 98.028  189.697 1.00 137.92 ? 3316 THR A CG2   1 
ATOM   12344 N  N     . SER A 1 2100 ? 162.166 99.737  192.491 1.00 138.55 ? 3317 SER A N     1 
ATOM   12345 C  CA    . SER A 1 2100 ? 161.801 100.942 193.235 1.00 137.06 ? 3317 SER A CA    1 
ATOM   12346 C  C     . SER A 1 2100 ? 162.823 102.059 193.037 1.00 138.24 ? 3317 SER A C     1 
ATOM   12347 O  O     . SER A 1 2100 ? 162.450 103.231 192.861 1.00 135.63 ? 3317 SER A O     1 
ATOM   12348 C  CB    . SER A 1 2100 ? 161.648 100.614 194.719 1.00 135.70 ? 3317 SER A CB    1 
ATOM   12349 O  OG    . SER A 1 2100 ? 162.912 100.427 195.329 1.00 136.83 ? 3317 SER A OG    1 
ATOM   12350 N  N     . GLN A 1 2101 ? 164.118 101.719 193.076 1.00 139.68 ? 3318 GLN A N     1 
ATOM   12351 C  CA    . GLN A 1 2101 ? 165.147 102.726 192.813 1.00 137.90 ? 3318 GLN A CA    1 
ATOM   12352 C  C     . GLN A 1 2101 ? 165.020 103.280 191.399 1.00 132.87 ? 3318 GLN A C     1 
ATOM   12353 O  O     . GLN A 1 2101 ? 165.120 104.499 191.181 1.00 126.77 ? 3318 GLN A O     1 
ATOM   12354 C  CB    . GLN A 1 2101 ? 166.541 102.135 193.030 1.00 136.23 ? 3318 GLN A CB    1 
ATOM   12355 C  CG    . GLN A 1 2101 ? 166.760 101.520 194.400 1.00 134.36 ? 3318 GLN A CG    1 
ATOM   12356 C  CD    . GLN A 1 2101 ? 168.220 101.220 194.675 1.00 133.02 ? 3318 GLN A CD    1 
ATOM   12357 O  OE1   . GLN A 1 2101 ? 169.048 101.218 193.764 1.00 129.50 ? 3318 GLN A OE1   1 
ATOM   12358 N  NE2   . GLN A 1 2101 ? 168.544 100.963 195.937 1.00 132.83 ? 3318 GLN A NE2   1 
ATOM   12359 N  N     . GLU A 1 2102 ? 164.775 102.397 190.428 1.00 133.14 ? 3319 GLU A N     1 
ATOM   12360 C  CA    . GLU A 1 2102 ? 164.564 102.828 189.055 1.00 130.56 ? 3319 GLU A CA    1 
ATOM   12361 C  C     . GLU A 1 2102 ? 163.306 103.675 188.934 1.00 129.58 ? 3319 GLU A C     1 
ATOM   12362 O  O     . GLU A 1 2102 ? 163.259 104.611 188.134 1.00 126.92 ? 3319 GLU A O     1 
ATOM   12363 C  CB    . GLU A 1 2102 ? 164.482 101.609 188.138 1.00 133.07 ? 3319 GLU A CB    1 
ATOM   12364 C  CG    . GLU A 1 2102 ? 164.474 101.980 186.683 1.00 132.48 ? 3319 GLU A CG    1 
ATOM   12365 C  CD    . GLU A 1 2102 ? 165.698 102.782 186.321 1.00 128.49 ? 3319 GLU A CD    1 
ATOM   12366 O  OE1   . GLU A 1 2102 ? 166.822 102.299 186.573 1.00 126.60 ? 3319 GLU A OE1   1 
ATOM   12367 O  OE2   . GLU A 1 2102 ? 165.539 103.914 185.821 1.00 125.65 ? 3319 GLU A OE2   1 
ATOM   12368 N  N     . LEU A 1 2103 ? 162.278 103.361 189.726 1.00 132.21 ? 3320 LEU A N     1 
ATOM   12369 C  CA    . LEU A 1 2103 ? 161.046 104.140 189.715 1.00 129.88 ? 3320 LEU A CA    1 
ATOM   12370 C  C     . LEU A 1 2103 ? 161.295 105.570 190.167 1.00 124.01 ? 3320 LEU A C     1 
ATOM   12371 O  O     . LEU A 1 2103 ? 160.836 106.521 189.524 1.00 122.30 ? 3320 LEU A O     1 
ATOM   12372 C  CB    . LEU A 1 2103 ? 160.009 103.476 190.620 1.00 131.57 ? 3320 LEU A CB    1 
ATOM   12373 C  CG    . LEU A 1 2103 ? 158.536 103.801 190.385 1.00 128.90 ? 3320 LEU A CG    1 
ATOM   12374 C  CD1   . LEU A 1 2103 ? 157.981 102.934 189.264 1.00 125.45 ? 3320 LEU A CD1   1 
ATOM   12375 C  CD2   . LEU A 1 2103 ? 157.741 103.619 191.667 1.00 129.76 ? 3320 LEU A CD2   1 
ATOM   12376 N  N     . ILE A 1 2104 ? 162.037 105.740 191.265 1.00 123.94 ? 3321 ILE A N     1 
ATOM   12377 C  CA    . ILE A 1 2104 ? 162.325 107.086 191.763 1.00 122.83 ? 3321 ILE A CA    1 
ATOM   12378 C  C     . ILE A 1 2104 ? 163.181 107.858 190.761 1.00 117.20 ? 3321 ILE A C     1 
ATOM   12379 O  O     . ILE A 1 2104 ? 162.898 109.024 190.439 1.00 111.65 ? 3321 ILE A O     1 
ATOM   12380 C  CB    . ILE A 1 2104 ? 162.994 107.016 193.147 1.00 125.83 ? 3321 ILE A CB    1 
ATOM   12381 C  CG1   . ILE A 1 2104 ? 162.031 106.405 194.168 1.00 125.64 ? 3321 ILE A CG1   1 
ATOM   12382 C  CG2   . ILE A 1 2104 ? 163.443 108.400 193.597 1.00 118.36 ? 3321 ILE A CG2   1 
ATOM   12383 C  CD1   . ILE A 1 2104 ? 160.808 107.256 194.438 1.00 122.72 ? 3321 ILE A CD1   1 
ATOM   12384 N  N     . GLY A 1 2105 ? 164.228 107.212 190.236 1.00 119.44 ? 3322 GLY A N     1 
ATOM   12385 C  CA    . GLY A 1 2105 ? 165.084 107.885 189.267 1.00 114.44 ? 3322 GLY A CA    1 
ATOM   12386 C  C     . GLY A 1 2105 ? 164.353 108.256 187.989 1.00 108.87 ? 3322 GLY A C     1 
ATOM   12387 O  O     . GLY A 1 2105 ? 164.509 109.366 187.470 1.00 104.55 ? 3322 GLY A O     1 
ATOM   12388 N  N     . ASN A 1 2106 ? 163.533 107.337 187.474 1.00 111.40 ? 3323 ASN A N     1 
ATOM   12389 C  CA    . ASN A 1 2106 ? 162.752 107.601 186.276 1.00 111.38 ? 3323 ASN A CA    1 
ATOM   12390 C  C     . ASN A 1 2106 ? 161.710 108.678 186.515 1.00 109.52 ? 3323 ASN A C     1 
ATOM   12391 O  O     . ASN A 1 2106 ? 161.392 109.432 185.595 1.00 108.64 ? 3323 ASN A O     1 
ATOM   12392 C  CB    . ASN A 1 2106 ? 162.077 106.318 185.794 1.00 116.71 ? 3323 ASN A CB    1 
ATOM   12393 C  CG    . ASN A 1 2106 ? 163.001 105.451 184.971 1.00 121.07 ? 3323 ASN A CG    1 
ATOM   12394 O  OD1   . ASN A 1 2106 ? 164.000 105.927 184.433 1.00 124.47 ? 3323 ASN A OD1   1 
ATOM   12395 N  ND2   . ASN A 1 2106 ? 162.669 104.171 184.859 1.00 122.40 ? 3323 ASN A ND2   1 
ATOM   12396 N  N     . CYS A 1 2107 ? 161.168 108.772 187.731 1.00 108.27 ? 3324 CYS A N     1 
ATOM   12397 C  CA    . CYS A 1 2107 ? 160.222 109.844 188.015 1.00 100.90 ? 3324 CYS A CA    1 
ATOM   12398 C  C     . CYS A 1 2107 ? 160.918 111.198 188.034 1.00 96.25  ? 3324 CYS A C     1 
ATOM   12399 O  O     . CYS A 1 2107 ? 160.355 112.194 187.564 1.00 94.17  ? 3324 CYS A O     1 
ATOM   12400 C  CB    . CYS A 1 2107 ? 159.510 109.583 189.338 1.00 101.28 ? 3324 CYS A CB    1 
ATOM   12401 S  SG    . CYS A 1 2107 ? 158.207 110.770 189.680 1.00 88.31  ? 3324 CYS A SG    1 
ATOM   12402 N  N     . ILE A 1 2108 ? 162.144 111.253 188.562 1.00 97.11  ? 3325 ILE A N     1 
ATOM   12403 C  CA    . ILE A 1 2108 ? 162.918 112.497 188.509 1.00 93.12  ? 3325 ILE A CA    1 
ATOM   12404 C  C     . ILE A 1 2108 ? 163.198 112.887 187.060 1.00 91.14  ? 3325 ILE A C     1 
ATOM   12405 O  O     . ILE A 1 2108 ? 163.019 114.049 186.658 1.00 89.23  ? 3325 ILE A O     1 
ATOM   12406 C  CB    . ILE A 1 2108 ? 164.222 112.353 189.314 1.00 93.08  ? 3325 ILE A CB    1 
ATOM   12407 C  CG1   . ILE A 1 2108 ? 163.914 112.092 190.788 1.00 95.79  ? 3325 ILE A CG1   1 
ATOM   12408 C  CG2   . ILE A 1 2108 ? 165.086 113.596 189.164 1.00 81.40  ? 3325 ILE A CG2   1 
ATOM   12409 C  CD1   . ILE A 1 2108 ? 165.084 111.532 191.562 1.00 98.75  ? 3325 ILE A CD1   1 
ATOM   12410 N  N     . ILE A 1 2109 ? 163.624 111.909 186.252 1.00 95.50  ? 3326 ILE A N     1 
ATOM   12411 C  CA    . ILE A 1 2109 ? 163.906 112.160 184.839 1.00 91.62  ? 3326 ILE A CA    1 
ATOM   12412 C  C     . ILE A 1 2109 ? 162.644 112.608 184.112 1.00 92.36  ? 3326 ILE A C     1 
ATOM   12413 O  O     . ILE A 1 2109 ? 162.684 113.515 183.275 1.00 86.91  ? 3326 ILE A O     1 
ATOM   12414 C  CB    . ILE A 1 2109 ? 164.521 110.908 184.183 1.00 93.66  ? 3326 ILE A CB    1 
ATOM   12415 C  CG1   . ILE A 1 2109 ? 165.872 110.570 184.815 1.00 90.65  ? 3326 ILE A CG1   1 
ATOM   12416 C  CG2   . ILE A 1 2109 ? 164.679 111.102 182.680 1.00 93.50  ? 3326 ILE A CG2   1 
ATOM   12417 C  CD1   . ILE A 1 2109 ? 166.990 111.477 184.384 1.00 80.88  ? 3326 ILE A CD1   1 
ATOM   12418 N  N     . SER A 1 2110 ? 161.502 111.998 184.439 1.00 97.55  ? 3327 SER A N     1 
ATOM   12419 C  CA    . SER A 1 2110 ? 160.244 112.342 183.787 1.00 98.11  ? 3327 SER A CA    1 
ATOM   12420 C  C     . SER A 1 2110 ? 159.778 113.741 184.167 1.00 90.49  ? 3327 SER A C     1 
ATOM   12421 O  O     . SER A 1 2110 ? 159.266 114.475 183.317 1.00 89.47  ? 3327 SER A O     1 
ATOM   12422 C  CB    . SER A 1 2110 ? 159.174 111.310 184.141 1.00 103.71 ? 3327 SER A CB    1 
ATOM   12423 O  OG    . SER A 1 2110 ? 157.876 111.832 183.923 1.00 107.16 ? 3327 SER A OG    1 
ATOM   12424 N  N     . SER A 1 2111 ? 159.936 114.124 185.436 1.00 86.44  ? 3328 SER A N     1 
ATOM   12425 C  CA    . SER A 1 2111 ? 159.566 115.472 185.854 1.00 80.44  ? 3328 SER A CA    1 
ATOM   12426 C  C     . SER A 1 2111 ? 160.417 116.518 185.143 1.00 80.06  ? 3328 SER A C     1 
ATOM   12427 O  O     . SER A 1 2111 ? 159.895 117.522 184.635 1.00 80.46  ? 3328 SER A O     1 
ATOM   12428 C  CB    . SER A 1 2111 ? 159.703 115.605 187.370 1.00 79.31  ? 3328 SER A CB    1 
ATOM   12429 O  OG    . SER A 1 2111 ? 159.463 116.935 187.788 1.00 77.54  ? 3328 SER A OG    1 
ATOM   12430 N  N     . ILE A 1 2112 ? 161.734 116.290 185.085 1.00 80.08  ? 3329 ILE A N     1 
ATOM   12431 C  CA    . ILE A 1 2112 ? 162.612 117.236 184.400 1.00 75.45  ? 3329 ILE A CA    1 
ATOM   12432 C  C     . ILE A 1 2112 ? 162.303 117.274 182.905 1.00 81.17  ? 3329 ILE A C     1 
ATOM   12433 O  O     . ILE A 1 2112 ? 162.258 118.350 182.296 1.00 83.20  ? 3329 ILE A O     1 
ATOM   12434 C  CB    . ILE A 1 2112 ? 164.087 116.893 184.683 1.00 69.39  ? 3329 ILE A CB    1 
ATOM   12435 C  CG1   . ILE A 1 2112 ? 164.508 117.495 186.023 1.00 69.80  ? 3329 ILE A CG1   1 
ATOM   12436 C  CG2   . ILE A 1 2112 ? 164.994 117.392 183.572 1.00 71.11  ? 3329 ILE A CG2   1 
ATOM   12437 C  CD1   . ILE A 1 2112 ? 165.934 117.208 186.406 1.00 71.15  ? 3329 ILE A CD1   1 
ATOM   12438 N  N     . TYR A 1 2113 ? 162.047 116.110 182.304 1.00 84.27  ? 3330 TYR A N     1 
ATOM   12439 C  CA    . TYR A 1 2113 ? 161.713 116.032 180.885 1.00 84.24  ? 3330 TYR A CA    1 
ATOM   12440 C  C     . TYR A 1 2113 ? 160.415 116.767 180.577 1.00 83.46  ? 3330 TYR A C     1 
ATOM   12441 O  O     . TYR A 1 2113 ? 160.308 117.455 179.556 1.00 84.76  ? 3330 TYR A O     1 
ATOM   12442 C  CB    . TYR A 1 2113 ? 161.611 114.561 180.478 1.00 86.94  ? 3330 TYR A CB    1 
ATOM   12443 C  CG    . TYR A 1 2113 ? 161.641 114.284 178.992 1.00 91.24  ? 3330 TYR A CG    1 
ATOM   12444 C  CD1   . TYR A 1 2113 ? 162.846 114.106 178.325 1.00 93.51  ? 3330 TYR A CD1   1 
ATOM   12445 C  CD2   . TYR A 1 2113 ? 160.464 114.165 178.263 1.00 92.70  ? 3330 TYR A CD2   1 
ATOM   12446 C  CE1   . TYR A 1 2113 ? 162.880 113.840 176.972 1.00 96.34  ? 3330 TYR A CE1   1 
ATOM   12447 C  CE2   . TYR A 1 2113 ? 160.488 113.898 176.909 1.00 94.68  ? 3330 TYR A CE2   1 
ATOM   12448 C  CZ    . TYR A 1 2113 ? 161.700 113.736 176.268 1.00 100.30 ? 3330 TYR A CZ    1 
ATOM   12449 O  OH    . TYR A 1 2113 ? 161.734 113.470 174.920 1.00 106.42 ? 3330 TYR A OH    1 
ATOM   12450 N  N     . GLU A 1 2114 ? 159.420 116.633 181.453 1.00 80.56  ? 3331 GLU A N     1 
ATOM   12451 C  CA    . GLU A 1 2114 ? 158.124 117.256 181.222 1.00 79.91  ? 3331 GLU A CA    1 
ATOM   12452 C  C     . GLU A 1 2114 ? 158.198 118.769 181.375 1.00 78.47  ? 3331 GLU A C     1 
ATOM   12453 O  O     . GLU A 1 2114 ? 157.709 119.513 180.517 1.00 77.43  ? 3331 GLU A O     1 
ATOM   12454 C  CB    . GLU A 1 2114 ? 157.093 116.667 182.184 1.00 83.20  ? 3331 GLU A CB    1 
ATOM   12455 C  CG    . GLU A 1 2114 ? 155.670 116.667 181.665 1.00 89.43  ? 3331 GLU A CG    1 
ATOM   12456 C  CD    . GLU A 1 2114 ? 154.734 115.883 182.562 1.00 95.55  ? 3331 GLU A CD    1 
ATOM   12457 O  OE1   . GLU A 1 2114 ? 154.423 116.369 183.669 1.00 91.32  ? 3331 GLU A OE1   1 
ATOM   12458 O  OE2   . GLU A 1 2114 ? 154.314 114.777 182.163 1.00 101.44 ? 3331 GLU A OE2   1 
ATOM   12459 N  N     . THR A 1 2115 ? 158.811 119.250 182.457 1.00 79.42  ? 3332 THR A N     1 
ATOM   12460 C  CA    . THR A 1 2115 ? 158.731 120.667 182.788 1.00 77.26  ? 3332 THR A CA    1 
ATOM   12461 C  C     . THR A 1 2115 ? 159.914 121.488 182.289 1.00 76.09  ? 3332 THR A C     1 
ATOM   12462 O  O     . THR A 1 2115 ? 159.875 122.718 182.392 1.00 76.52  ? 3332 THR A O     1 
ATOM   12463 C  CB    . THR A 1 2115 ? 158.589 120.845 184.303 1.00 73.55  ? 3332 THR A CB    1 
ATOM   12464 O  OG1   . THR A 1 2115 ? 159.824 120.505 184.943 1.00 74.03  ? 3332 THR A OG1   1 
ATOM   12465 C  CG2   . THR A 1 2115 ? 157.480 119.953 184.836 1.00 72.22  ? 3332 THR A CG2   1 
ATOM   12466 N  N     . TYR A 1 2116 ? 160.950 120.860 181.738 1.00 73.99  ? 3333 TYR A N     1 
ATOM   12467 C  CA    . TYR A 1 2116 ? 162.128 121.584 181.279 1.00 70.19  ? 3333 TYR A CA    1 
ATOM   12468 C  C     . TYR A 1 2116 ? 162.416 121.410 179.798 1.00 72.65  ? 3333 TYR A C     1 
ATOM   12469 O  O     . TYR A 1 2116 ? 162.866 122.361 179.158 1.00 74.79  ? 3333 TYR A O     1 
ATOM   12470 C  CB    . TYR A 1 2116 ? 163.383 121.134 182.048 1.00 75.49  ? 3333 TYR A CB    1 
ATOM   12471 C  CG    . TYR A 1 2116 ? 163.434 121.490 183.519 1.00 78.34  ? 3333 TYR A CG    1 
ATOM   12472 C  CD1   . TYR A 1 2116 ? 162.569 122.421 184.071 1.00 77.53  ? 3333 TYR A CD1   1 
ATOM   12473 C  CD2   . TYR A 1 2116 ? 164.364 120.891 184.355 1.00 79.93  ? 3333 TYR A CD2   1 
ATOM   12474 C  CE1   . TYR A 1 2116 ? 162.622 122.734 185.416 1.00 74.06  ? 3333 TYR A CE1   1 
ATOM   12475 C  CE2   . TYR A 1 2116 ? 164.427 121.202 185.697 1.00 77.88  ? 3333 TYR A CE2   1 
ATOM   12476 C  CZ    . TYR A 1 2116 ? 163.554 122.123 186.222 1.00 73.30  ? 3333 TYR A CZ    1 
ATOM   12477 O  OH    . TYR A 1 2116 ? 163.612 122.437 187.560 1.00 72.96  ? 3333 TYR A OH    1 
ATOM   12478 N  N     . PHE A 1 2117 ? 162.168 120.226 179.240 1.00 77.00  ? 3334 PHE A N     1 
ATOM   12479 C  CA    . PHE A 1 2117 ? 162.643 119.858 177.914 1.00 78.52  ? 3334 PHE A CA    1 
ATOM   12480 C  C     . PHE A 1 2117 ? 161.579 120.008 176.835 1.00 80.53  ? 3334 PHE A C     1 
ATOM   12481 O  O     . PHE A 1 2117 ? 161.759 119.491 175.729 1.00 84.98  ? 3334 PHE A O     1 
ATOM   12482 C  CB    . PHE A 1 2117 ? 163.163 118.418 177.927 1.00 79.36  ? 3334 PHE A CB    1 
ATOM   12483 C  CG    . PHE A 1 2117 ? 164.391 118.222 178.770 1.00 82.02  ? 3334 PHE A CG    1 
ATOM   12484 C  CD1   . PHE A 1 2117 ? 165.221 119.288 179.072 1.00 84.36  ? 3334 PHE A CD1   1 
ATOM   12485 C  CD2   . PHE A 1 2117 ? 164.716 116.969 179.260 1.00 79.87  ? 3334 PHE A CD2   1 
ATOM   12486 C  CE1   . PHE A 1 2117 ? 166.347 119.108 179.849 1.00 86.33  ? 3334 PHE A CE1   1 
ATOM   12487 C  CE2   . PHE A 1 2117 ? 165.841 116.783 180.039 1.00 80.67  ? 3334 PHE A CE2   1 
ATOM   12488 C  CZ    . PHE A 1 2117 ? 166.659 117.853 180.331 1.00 84.84  ? 3334 PHE A CZ    1 
ATOM   12489 N  N     . GLY A 1 2118 ? 160.478 120.697 177.127 1.00 78.35  ? 3335 GLY A N     1 
ATOM   12490 C  CA    . GLY A 1 2118 ? 159.420 120.842 176.147 1.00 71.05  ? 3335 GLY A CA    1 
ATOM   12491 C  C     . GLY A 1 2118 ? 159.679 121.854 175.053 1.00 70.79  ? 3335 GLY A C     1 
ATOM   12492 O  O     . GLY A 1 2118 ? 158.900 121.918 174.099 1.00 74.19  ? 3335 GLY A O     1 
ATOM   12493 N  N     . HIS A 1 2119 ? 160.750 122.637 175.154 1.00 72.88  ? 3336 HIS A N     1 
ATOM   12494 C  CA    . HIS A 1 2119 ? 161.032 123.695 174.191 1.00 77.47  ? 3336 HIS A CA    1 
ATOM   12495 C  C     . HIS A 1 2119 ? 162.499 123.694 173.784 1.00 77.88  ? 3336 HIS A C     1 
ATOM   12496 O  O     . HIS A 1 2119 ? 163.130 124.747 173.662 1.00 77.32  ? 3336 HIS A O     1 
ATOM   12497 C  CB    . HIS A 1 2119 ? 160.625 125.059 174.744 1.00 78.15  ? 3336 HIS A CB    1 
ATOM   12498 C  CG    . HIS A 1 2119 ? 161.189 125.357 176.098 1.00 74.83  ? 3336 HIS A CG    1 
ATOM   12499 N  ND1   . HIS A 1 2119 ? 162.323 126.119 176.280 1.00 74.13  ? 3336 HIS A ND1   1 
ATOM   12500 C  CD2   . HIS A 1 2119 ? 160.774 125.000 177.336 1.00 74.11  ? 3336 HIS A CD2   1 
ATOM   12501 C  CE1   . HIS A 1 2119 ? 162.584 126.215 177.571 1.00 73.94  ? 3336 HIS A CE1   1 
ATOM   12502 N  NE2   . HIS A 1 2119 ? 161.659 125.545 178.234 1.00 74.13  ? 3336 HIS A NE2   1 
ATOM   12503 N  N     . LEU A 1 2120 ? 163.066 122.511 173.561 1.00 80.44  ? 3337 LEU A N     1 
ATOM   12504 C  CA    . LEU A 1 2120 ? 164.438 122.376 173.096 1.00 89.60  ? 3337 LEU A CA    1 
ATOM   12505 C  C     . LEU A 1 2120 ? 164.472 121.511 171.844 1.00 98.66  ? 3337 LEU A C     1 
ATOM   12506 O  O     . LEU A 1 2120 ? 163.643 120.614 171.668 1.00 99.04  ? 3337 LEU A O     1 
ATOM   12507 C  CB    . LEU A 1 2120 ? 165.345 121.762 174.172 1.00 91.29  ? 3337 LEU A CB    1 
ATOM   12508 C  CG    . LEU A 1 2120 ? 165.342 122.414 175.554 1.00 87.06  ? 3337 LEU A CG    1 
ATOM   12509 C  CD1   . LEU A 1 2120 ? 166.236 121.640 176.507 1.00 84.37  ? 3337 LEU A CD1   1 
ATOM   12510 C  CD2   . LEU A 1 2120 ? 165.792 123.860 175.458 1.00 90.34  ? 3337 LEU A CD2   1 
ATOM   12511 N  N     . ASN A 1 2121 ? 165.443 121.783 170.974 1.00 100.33 ? 3338 ASN A N     1 
ATOM   12512 C  CA    . ASN A 1 2121 ? 165.622 120.985 169.768 1.00 100.45 ? 3338 ASN A CA    1 
ATOM   12513 C  C     . ASN A 1 2121 ? 166.344 119.681 170.120 1.00 104.27 ? 3338 ASN A C     1 
ATOM   12514 O  O     . ASN A 1 2121 ? 166.559 119.361 171.292 1.00 103.36 ? 3338 ASN A O     1 
ATOM   12515 C  CB    . ASN A 1 2121 ? 166.329 121.803 168.684 1.00 103.94 ? 3338 ASN A CB    1 
ATOM   12516 C  CG    . ASN A 1 2121 ? 167.736 122.242 169.074 1.00 108.52 ? 3338 ASN A CG    1 
ATOM   12517 O  OD1   . ASN A 1 2121 ? 168.268 121.860 170.112 1.00 105.35 ? 3338 ASN A OD1   1 
ATOM   12518 N  ND2   . ASN A 1 2121 ? 168.348 123.054 168.220 1.00 114.20 ? 3338 ASN A ND2   1 
ATOM   12519 N  N     . GLU A 1 2122 ? 166.735 118.913 169.101 1.00 108.31 ? 3339 GLU A N     1 
ATOM   12520 C  CA    . GLU A 1 2122 ? 167.250 117.568 169.346 1.00 109.10 ? 3339 GLU A CA    1 
ATOM   12521 C  C     . GLU A 1 2122 ? 168.654 117.597 169.946 1.00 107.05 ? 3339 GLU A C     1 
ATOM   12522 O  O     . GLU A 1 2122 ? 168.943 116.857 170.895 1.00 105.30 ? 3339 GLU A O     1 
ATOM   12523 C  CB    . GLU A 1 2122 ? 167.238 116.764 168.047 1.00 111.02 ? 3339 GLU A CB    1 
ATOM   12524 C  CG    . GLU A 1 2122 ? 165.856 116.606 167.428 1.00 109.00 ? 3339 GLU A CG    1 
ATOM   12525 C  CD    . GLU A 1 2122 ? 164.897 115.824 168.304 1.00 108.90 ? 3339 GLU A CD    1 
ATOM   12526 O  OE1   . GLU A 1 2122 ? 165.350 114.919 169.036 1.00 114.59 ? 3339 GLU A OE1   1 
ATOM   12527 O  OE2   . GLU A 1 2122 ? 163.685 116.119 168.260 1.00 104.57 ? 3339 GLU A OE2   1 
ATOM   12528 N  N     . ARG A 1 2123 ? 169.538 118.443 169.409 1.00 107.64 ? 3340 ARG A N     1 
ATOM   12529 C  CA    . ARG A 1 2123 ? 170.923 118.467 169.876 1.00 107.11 ? 3340 ARG A CA    1 
ATOM   12530 C  C     . ARG A 1 2123 ? 171.028 119.013 171.296 1.00 106.22 ? 3340 ARG A C     1 
ATOM   12531 O  O     . ARG A 1 2123 ? 171.759 118.459 172.128 1.00 103.31 ? 3340 ARG A O     1 
ATOM   12532 C  CB    . ARG A 1 2123 ? 171.783 119.293 168.919 1.00 98.24  ? 3340 ARG A CB    1 
ATOM   12533 N  N     . GLU A 1 2124 ? 170.312 120.101 171.591 1.00 104.16 ? 3341 GLU A N     1 
ATOM   12534 C  CA    . GLU A 1 2124 ? 170.345 120.650 172.940 1.00 100.49 ? 3341 GLU A CA    1 
ATOM   12535 C  C     . GLU A 1 2124 ? 169.688 119.711 173.941 1.00 98.60  ? 3341 GLU A C     1 
ATOM   12536 O  O     . GLU A 1 2124 ? 170.136 119.627 175.088 1.00 102.80 ? 3341 GLU A O     1 
ATOM   12537 C  CB    . GLU A 1 2124 ? 169.675 122.023 172.978 1.00 102.42 ? 3341 GLU A CB    1 
ATOM   12538 C  CG    . GLU A 1 2124 ? 170.459 123.110 172.260 1.00 105.32 ? 3341 GLU A CG    1 
ATOM   12539 C  CD    . GLU A 1 2124 ? 171.774 123.435 172.942 1.00 107.64 ? 3341 GLU A CD    1 
ATOM   12540 O  OE1   . GLU A 1 2124 ? 171.850 123.319 174.184 1.00 106.67 ? 3341 GLU A OE1   1 
ATOM   12541 O  OE2   . GLU A 1 2124 ? 172.734 123.807 172.234 1.00 108.51 ? 3341 GLU A OE2   1 
ATOM   12542 N  N     . ARG A 1 2125 ? 168.637 118.994 173.532 1.00 96.64  ? 3342 ARG A N     1 
ATOM   12543 C  CA    . ARG A 1 2125 ? 168.051 117.992 174.416 1.00 98.06  ? 3342 ARG A CA    1 
ATOM   12544 C  C     . ARG A 1 2125 ? 169.023 116.848 174.676 1.00 98.06  ? 3342 ARG A C     1 
ATOM   12545 O  O     . ARG A 1 2125 ? 169.092 116.333 175.796 1.00 94.57  ? 3342 ARG A O     1 
ATOM   12546 C  CB    . ARG A 1 2125 ? 166.744 117.459 173.833 1.00 98.20  ? 3342 ARG A CB    1 
ATOM   12547 C  CG    . ARG A 1 2125 ? 165.841 116.800 174.858 1.00 95.56  ? 3342 ARG A CG    1 
ATOM   12548 C  CD    . ARG A 1 2125 ? 164.642 116.149 174.196 1.00 96.66  ? 3342 ARG A CD    1 
ATOM   12549 N  NE    . ARG A 1 2125 ? 163.547 117.094 174.016 1.00 95.98  ? 3342 ARG A NE    1 
ATOM   12550 C  CZ    . ARG A 1 2125 ? 163.299 117.750 172.891 1.00 93.20  ? 3342 ARG A CZ    1 
ATOM   12551 N  NH1   . ARG A 1 2125 ? 164.049 117.584 171.814 1.00 95.70  ? 3342 ARG A NH1   1 
ATOM   12552 N  NH2   . ARG A 1 2125 ? 162.273 118.594 172.845 1.00 89.91  ? 3342 ARG A NH2   1 
ATOM   12553 N  N     . GLY A 1 2126 ? 169.782 116.438 173.656 1.00 98.67  ? 3343 GLY A N     1 
ATOM   12554 C  CA    . GLY A 1 2126 ? 170.800 115.421 173.874 1.00 96.52  ? 3343 GLY A CA    1 
ATOM   12555 C  C     . GLY A 1 2126 ? 171.881 115.877 174.835 1.00 95.98  ? 3343 GLY A C     1 
ATOM   12556 O  O     . GLY A 1 2126 ? 172.292 115.127 175.726 1.00 97.04  ? 3343 GLY A O     1 
ATOM   12557 N  N     . ASP A 1 2127 ? 172.340 117.122 174.680 1.00 96.44  ? 3344 ASP A N     1 
ATOM   12558 C  CA    . ASP A 1 2127 ? 173.333 117.668 175.603 1.00 97.22  ? 3344 ASP A CA    1 
ATOM   12559 C  C     . ASP A 1 2127 ? 172.775 117.779 177.019 1.00 94.70  ? 3344 ASP A C     1 
ATOM   12560 O  O     . ASP A 1 2127 ? 173.485 117.517 177.999 1.00 93.43  ? 3344 ASP A O     1 
ATOM   12561 C  CB    . ASP A 1 2127 ? 173.814 119.031 175.105 1.00 99.09  ? 3344 ASP A CB    1 
ATOM   12562 N  N     . MET A 1 2128 ? 171.504 118.169 177.145 1.00 95.36  ? 3345 MET A N     1 
ATOM   12563 C  CA    . MET A 1 2128 ? 170.878 118.272 178.459 1.00 93.41  ? 3345 MET A CA    1 
ATOM   12564 C  C     . MET A 1 2128 ? 170.735 116.906 179.118 1.00 93.39  ? 3345 MET A C     1 
ATOM   12565 O  O     . MET A 1 2128 ? 170.948 116.775 180.328 1.00 95.29  ? 3345 MET A O     1 
ATOM   12566 C  CB    . MET A 1 2128 ? 169.518 118.956 178.336 1.00 90.65  ? 3345 MET A CB    1 
ATOM   12567 N  N     . LEU A 1 2129 ? 170.369 115.879 178.344 1.00 89.65  ? 3346 LEU A N     1 
ATOM   12568 C  CA    . LEU A 1 2129 ? 170.327 114.524 178.888 1.00 89.13  ? 3346 LEU A CA    1 
ATOM   12569 C  C     . LEU A 1 2129 ? 171.714 114.052 179.305 1.00 91.91  ? 3346 LEU A C     1 
ATOM   12570 O  O     . LEU A 1 2129 ? 171.859 113.369 180.325 1.00 94.09  ? 3346 LEU A O     1 
ATOM   12571 C  CB    . LEU A 1 2129 ? 169.714 113.551 177.878 1.00 87.69  ? 3346 LEU A CB    1 
ATOM   12572 C  CG    . LEU A 1 2129 ? 168.209 113.257 177.939 1.00 88.80  ? 3346 LEU A CG    1 
ATOM   12573 C  CD1   . LEU A 1 2129 ? 167.858 112.569 179.253 1.00 80.33  ? 3346 LEU A CD1   1 
ATOM   12574 C  CD2   . LEU A 1 2129 ? 167.351 114.494 177.744 1.00 94.35  ? 3346 LEU A CD2   1 
ATOM   12575 N  N     . VAL A 1 2130 ? 172.744 114.413 178.534 1.00 93.28  ? 3347 VAL A N     1 
ATOM   12576 C  CA    . VAL A 1 2130 ? 174.115 114.056 178.900 1.00 91.67  ? 3347 VAL A CA    1 
ATOM   12577 C  C     . VAL A 1 2130 ? 174.493 114.691 180.235 1.00 92.87  ? 3347 VAL A C     1 
ATOM   12578 O  O     . VAL A 1 2130 ? 175.016 114.023 181.137 1.00 93.13  ? 3347 VAL A O     1 
ATOM   12579 C  CB    . VAL A 1 2130 ? 175.090 114.464 177.781 1.00 89.73  ? 3347 VAL A CB    1 
ATOM   12580 C  CG1   . VAL A 1 2130 ? 176.516 114.560 178.309 1.00 85.28  ? 3347 VAL A CG1   1 
ATOM   12581 C  CG2   . VAL A 1 2130 ? 175.014 113.477 176.627 1.00 91.24  ? 3347 VAL A CG2   1 
ATOM   12582 N  N     . ILE A 1 2131 ? 174.202 115.985 180.391 1.00 93.91  ? 3348 ILE A N     1 
ATOM   12583 C  CA    . ILE A 1 2131 ? 174.549 116.691 181.624 1.00 92.84  ? 3348 ILE A CA    1 
ATOM   12584 C  C     . ILE A 1 2131 ? 173.748 116.152 182.806 1.00 94.10  ? 3348 ILE A C     1 
ATOM   12585 O  O     . ILE A 1 2131 ? 174.276 116.002 183.916 1.00 98.02  ? 3348 ILE A O     1 
ATOM   12586 C  CB    . ILE A 1 2131 ? 174.344 118.206 181.447 1.00 88.53  ? 3348 ILE A CB    1 
ATOM   12587 N  N     . LEU A 1 2132 ? 172.467 115.848 182.591 1.00 89.64  ? 3349 LEU A N     1 
ATOM   12588 C  CA    . LEU A 1 2132 ? 171.630 115.348 183.675 1.00 86.22  ? 3349 LEU A CA    1 
ATOM   12589 C  C     . LEU A 1 2132 ? 172.050 113.948 184.109 1.00 91.63  ? 3349 LEU A C     1 
ATOM   12590 O  O     . LEU A 1 2132 ? 172.060 113.642 185.308 1.00 92.48  ? 3349 LEU A O     1 
ATOM   12591 C  CB    . LEU A 1 2132 ? 170.166 115.373 183.248 1.00 82.68  ? 3349 LEU A CB    1 
ATOM   12592 C  CG    . LEU A 1 2132 ? 169.159 114.932 184.301 1.00 83.50  ? 3349 LEU A CG    1 
ATOM   12593 C  CD1   . LEU A 1 2132 ? 169.228 115.854 185.498 1.00 83.71  ? 3349 LEU A CD1   1 
ATOM   12594 C  CD2   . LEU A 1 2132 ? 167.775 114.961 183.692 1.00 85.28  ? 3349 LEU A CD2   1 
ATOM   12595 N  N     . LYS A 1 2133 ? 172.403 113.084 183.153 1.00 94.35  ? 3350 LYS A N     1 
ATOM   12596 C  CA    . LYS A 1 2133 ? 172.929 111.773 183.510 1.00 95.42  ? 3350 LYS A CA    1 
ATOM   12597 C  C     . LYS A 1 2133 ? 174.278 111.885 184.208 1.00 96.04  ? 3350 LYS A C     1 
ATOM   12598 O  O     . LYS A 1 2133 ? 174.571 111.091 185.108 1.00 96.44  ? 3350 LYS A O     1 
ATOM   12599 C  CB    . LYS A 1 2133 ? 173.037 110.889 182.268 1.00 93.93  ? 3350 LYS A CB    1 
ATOM   12600 C  CG    . LYS A 1 2133 ? 171.784 110.076 181.972 1.00 87.88  ? 3350 LYS A CG    1 
ATOM   12601 C  CD    . LYS A 1 2133 ? 171.254 109.395 183.226 1.00 94.13  ? 3350 LYS A CD    1 
ATOM   12602 C  CE    . LYS A 1 2133 ? 172.040 108.133 183.548 1.00 95.77  ? 3350 LYS A CE    1 
ATOM   12603 N  NZ    . LYS A 1 2133 ? 171.425 107.363 184.665 1.00 96.54  ? 3350 LYS A NZ    1 
ATOM   12604 N  N     . ARG A 1 2134 ? 175.102 112.863 183.816 1.00 95.16  ? 3351 ARG A N     1 
ATOM   12605 C  CA    . ARG A 1 2134 ? 176.349 113.114 184.532 1.00 95.33  ? 3351 ARG A CA    1 
ATOM   12606 C  C     . ARG A 1 2134 ? 176.081 113.505 185.980 1.00 97.79  ? 3351 ARG A C     1 
ATOM   12607 O  O     . ARG A 1 2134 ? 176.767 113.036 186.896 1.00 100.61 ? 3351 ARG A O     1 
ATOM   12608 C  CB    . ARG A 1 2134 ? 177.150 114.206 183.824 1.00 92.74  ? 3351 ARG A CB    1 
ATOM   12609 C  CG    . ARG A 1 2134 ? 178.584 114.349 184.309 1.00 96.95  ? 3351 ARG A CG    1 
ATOM   12610 C  CD    . ARG A 1 2134 ? 178.757 115.560 185.215 1.00 97.58  ? 3351 ARG A CD    1 
ATOM   12611 N  NE    . ARG A 1 2134 ? 178.207 116.777 184.631 1.00 97.58  ? 3351 ARG A NE    1 
ATOM   12612 C  CZ    . ARG A 1 2134 ? 177.766 117.811 185.334 1.00 95.65  ? 3351 ARG A CZ    1 
ATOM   12613 N  NH1   . ARG A 1 2134 ? 177.791 117.809 186.657 1.00 92.44  ? 3351 ARG A NH1   1 
ATOM   12614 N  NH2   . ARG A 1 2134 ? 177.288 118.875 184.695 1.00 95.92  ? 3351 ARG A NH2   1 
ATOM   12615 N  N     . LEU A 1 2135 ? 175.084 114.365 186.203 1.00 98.82  ? 3352 LEU A N     1 
ATOM   12616 C  CA    . LEU A 1 2135 ? 174.723 114.748 187.567 1.00 100.39 ? 3352 LEU A CA    1 
ATOM   12617 C  C     . LEU A 1 2135 ? 174.211 113.556 188.367 1.00 102.24 ? 3352 LEU A C     1 
ATOM   12618 O  O     . LEU A 1 2135 ? 174.558 113.393 189.545 1.00 104.32 ? 3352 LEU A O     1 
ATOM   12619 C  CB    . LEU A 1 2135 ? 173.675 115.859 187.544 1.00 96.82  ? 3352 LEU A CB    1 
ATOM   12620 C  CG    . LEU A 1 2135 ? 174.222 117.273 187.710 1.00 93.28  ? 3352 LEU A CG    1 
ATOM   12621 C  CD1   . LEU A 1 2135 ? 173.085 118.258 187.820 1.00 87.18  ? 3352 LEU A CD1   1 
ATOM   12622 C  CD2   . LEU A 1 2135 ? 175.104 117.339 188.936 1.00 93.69  ? 3352 LEU A CD2   1 
ATOM   12623 N  N     . LEU A 1 2136 ? 173.375 112.719 187.746 1.00 100.62 ? 3353 LEU A N     1 
ATOM   12624 C  CA    . LEU A 1 2136 ? 172.850 111.548 188.441 1.00 100.99 ? 3353 LEU A CA    1 
ATOM   12625 C  C     . LEU A 1 2136 ? 173.963 110.569 188.791 1.00 103.15 ? 3353 LEU A C     1 
ATOM   12626 O  O     . LEU A 1 2136 ? 173.942 109.949 189.861 1.00 102.14 ? 3353 LEU A O     1 
ATOM   12627 C  CB    . LEU A 1 2136 ? 171.782 110.861 187.592 1.00 100.14 ? 3353 LEU A CB    1 
ATOM   12628 C  CG    . LEU A 1 2136 ? 170.359 111.411 187.692 1.00 100.12 ? 3353 LEU A CG    1 
ATOM   12629 C  CD1   . LEU A 1 2136 ? 169.400 110.505 186.946 1.00 96.15  ? 3353 LEU A CD1   1 
ATOM   12630 C  CD2   . LEU A 1 2136 ? 169.929 111.573 189.137 1.00 102.69 ? 3353 LEU A CD2   1 
ATOM   12631 N  N     . GLY A 1 2137 ? 174.938 110.408 187.894 1.00 104.95 ? 3354 GLY A N     1 
ATOM   12632 C  CA    . GLY A 1 2137 ? 176.086 109.572 188.205 1.00 106.50 ? 3354 GLY A CA    1 
ATOM   12633 C  C     . GLY A 1 2137 ? 176.958 110.157 189.299 1.00 108.13 ? 3354 GLY A C     1 
ATOM   12634 O  O     . GLY A 1 2137 ? 177.510 109.423 190.124 1.00 112.28 ? 3354 GLY A O     1 
ATOM   12635 N  N     . LYS A 1 2138 ? 177.108 111.485 189.313 1.00 106.59 ? 3355 LYS A N     1 
ATOM   12636 C  CA    . LYS A 1 2138 ? 177.908 112.132 190.348 1.00 105.65 ? 3355 LYS A CA    1 
ATOM   12637 C  C     . LYS A 1 2138 ? 177.268 111.977 191.723 1.00 107.40 ? 3355 LYS A C     1 
ATOM   12638 O  O     . LYS A 1 2138 ? 177.963 111.701 192.708 1.00 107.93 ? 3355 LYS A O     1 
ATOM   12639 C  CB    . LYS A 1 2138 ? 178.105 113.612 190.016 1.00 100.48 ? 3355 LYS A CB    1 
ATOM   12640 C  CG    . LYS A 1 2138 ? 178.876 114.384 191.076 1.00 98.09  ? 3355 LYS A CG    1 
ATOM   12641 C  CD    . LYS A 1 2138 ? 178.745 115.886 190.886 1.00 101.25 ? 3355 LYS A CD    1 
ATOM   12642 C  CE    . LYS A 1 2138 ? 177.495 116.421 191.565 1.00 100.89 ? 3355 LYS A CE    1 
ATOM   12643 N  NZ    . LYS A 1 2138 ? 177.631 116.446 193.047 1.00 100.97 ? 3355 LYS A NZ    1 
ATOM   12644 N  N     . PHE A 1 2139 ? 175.951 112.145 191.813 1.00 108.18 ? 3356 PHE A N     1 
ATOM   12645 C  CA    . PHE A 1 2139 ? 175.267 112.062 193.097 1.00 108.03 ? 3356 PHE A CA    1 
ATOM   12646 C  C     . PHE A 1 2139 ? 174.670 110.687 193.377 1.00 105.34 ? 3356 PHE A C     1 
ATOM   12647 O  O     . PHE A 1 2139 ? 174.016 110.519 194.412 1.00 105.08 ? 3356 PHE A O     1 
ATOM   12648 C  CB    . PHE A 1 2139 ? 174.173 113.128 193.183 1.00 105.54 ? 3356 PHE A CB    1 
ATOM   12649 N  N     . ALA A 1 2140 ? 174.876 109.717 192.482 1.00 105.44 ? 3357 ALA A N     1 
ATOM   12650 C  CA    . ALA A 1 2140 ? 174.556 108.305 192.709 1.00 111.18 ? 3357 ALA A CA    1 
ATOM   12651 C  C     . ALA A 1 2140 ? 173.070 108.086 193.010 1.00 109.41 ? 3357 ALA A C     1 
ATOM   12652 O  O     . ALA A 1 2140 ? 172.681 107.668 194.102 1.00 104.96 ? 3357 ALA A O     1 
ATOM   12653 C  CB    . ALA A 1 2140 ? 175.434 107.720 193.822 1.00 116.33 ? 3357 ALA A CB    1 
ATOM   12654 N  N     . VAL A 1 2141 ? 172.239 108.383 192.014 1.00 111.22 ? 3358 VAL A N     1 
ATOM   12655 C  CA    . VAL A 1 2141 ? 170.819 108.047 192.038 1.00 111.84 ? 3358 VAL A CA    1 
ATOM   12656 C  C     . VAL A 1 2141 ? 170.532 107.155 190.837 1.00 112.91 ? 3358 VAL A C     1 
ATOM   12657 O  O     . VAL A 1 2141 ? 170.869 107.509 189.701 1.00 113.48 ? 3358 VAL A O     1 
ATOM   12658 C  CB    . VAL A 1 2141 ? 169.929 109.302 192.023 1.00 104.80 ? 3358 VAL A CB    1 
ATOM   12659 C  CG1   . VAL A 1 2141 ? 168.460 108.911 192.020 1.00 103.66 ? 3358 VAL A CG1   1 
ATOM   12660 C  CG2   . VAL A 1 2141 ? 170.242 110.191 193.216 1.00 101.69 ? 3358 VAL A CG2   1 
ATOM   12661 N  N     . LYS A 1 2142 ? 169.914 106.003 191.091 1.00 112.19 ? 3359 LYS A N     1 
ATOM   12662 C  CA    . LYS A 1 2142 ? 169.758 104.973 190.072 1.00 113.10 ? 3359 LYS A CA    1 
ATOM   12663 C  C     . LYS A 1 2142 ? 168.756 105.398 189.004 1.00 115.85 ? 3359 LYS A C     1 
ATOM   12664 O  O     . LYS A 1 2142 ? 167.644 105.831 189.319 1.00 118.74 ? 3359 LYS A O     1 
ATOM   12665 C  CB    . LYS A 1 2142 ? 169.313 103.660 190.714 1.00 117.98 ? 3359 LYS A CB    1 
ATOM   12666 N  N     . TYR A 1 2143 ? 169.156 105.265 187.740 1.00 116.35 ? 3360 TYR A N     1 
ATOM   12667 C  CA    . TYR A 1 2143 ? 168.293 105.540 186.600 1.00 116.75 ? 3360 TYR A CA    1 
ATOM   12668 C  C     . TYR A 1 2143 ? 168.644 104.570 185.479 1.00 120.60 ? 3360 TYR A C     1 
ATOM   12669 O  O     . TYR A 1 2143 ? 169.729 103.983 185.455 1.00 124.77 ? 3360 TYR A O     1 
ATOM   12670 C  CB    . TYR A 1 2143 ? 168.427 106.991 186.126 1.00 112.59 ? 3360 TYR A CB    1 
ATOM   12671 N  N     . ASP A 1 2144 ? 167.714 104.401 184.542 1.00 122.86 ? 3361 ASP A N     1 
ATOM   12672 C  CA    . ASP A 1 2144 ? 167.891 103.451 183.452 1.00 127.21 ? 3361 ASP A CA    1 
ATOM   12673 C  C     . ASP A 1 2144 ? 168.583 104.107 182.266 1.00 129.92 ? 3361 ASP A C     1 
ATOM   12674 O  O     . ASP A 1 2144 ? 168.277 105.245 181.899 1.00 131.17 ? 3361 ASP A O     1 
ATOM   12675 C  CB    . ASP A 1 2144 ? 166.550 102.872 182.998 1.00 128.22 ? 3361 ASP A CB    1 
ATOM   12676 N  N     . VAL A 1 2145 ? 169.525 103.373 181.672 1.00 130.01 ? 3362 VAL A N     1 
ATOM   12677 C  CA    . VAL A 1 2145 ? 170.122 103.805 180.415 1.00 132.08 ? 3362 VAL A CA    1 
ATOM   12678 C  C     . VAL A 1 2145 ? 169.095 103.728 179.291 1.00 134.76 ? 3362 VAL A C     1 
ATOM   12679 O  O     . VAL A 1 2145 ? 169.112 104.547 178.362 1.00 133.87 ? 3362 VAL A O     1 
ATOM   12680 C  CB    . VAL A 1 2145 ? 171.376 102.958 180.120 1.00 129.62 ? 3362 VAL A CB    1 
ATOM   12681 C  CG1   . VAL A 1 2145 ? 172.027 103.370 178.805 1.00 130.00 ? 3362 VAL A CG1   1 
ATOM   12682 C  CG2   . VAL A 1 2145 ? 172.367 103.061 181.271 1.00 124.64 ? 3362 VAL A CG2   1 
ATOM   12683 N  N     . ASN A 1 2146 ? 168.165 102.778 179.372 1.00 135.30 ? 3363 ASN A N     1 
ATOM   12684 C  CA    . ASN A 1 2146 ? 167.171 102.535 178.332 1.00 137.07 ? 3363 ASN A CA    1 
ATOM   12685 C  C     . ASN A 1 2146 ? 165.758 102.858 178.813 1.00 140.51 ? 3363 ASN A C     1 
ATOM   12686 O  O     . ASN A 1 2146 ? 164.813 102.105 178.566 1.00 142.38 ? 3363 ASN A O     1 
ATOM   12687 C  CB    . ASN A 1 2146 ? 167.249 101.092 177.843 1.00 131.51 ? 3363 ASN A CB    1 
ATOM   12688 N  N     . TYR A 1 2147 ? 165.599 103.980 179.509 1.00 138.71 ? 3364 TYR A N     1 
ATOM   12689 C  CA    . TYR A 1 2147 ? 164.289 104.440 179.950 1.00 133.69 ? 3364 TYR A CA    1 
ATOM   12690 C  C     . TYR A 1 2147 ? 163.618 105.252 178.851 1.00 133.07 ? 3364 TYR A C     1 
ATOM   12691 O  O     . TYR A 1 2147 ? 164.265 106.050 178.168 1.00 133.69 ? 3364 TYR A O     1 
ATOM   12692 C  CB    . TYR A 1 2147 ? 164.411 105.284 181.221 1.00 129.52 ? 3364 TYR A CB    1 
ATOM   12693 C  CG    . TYR A 1 2147 ? 163.277 106.269 181.423 1.00 128.52 ? 3364 TYR A CG    1 
ATOM   12694 C  CD1   . TYR A 1 2147 ? 162.006 105.833 181.783 1.00 127.66 ? 3364 TYR A CD1   1 
ATOM   12695 C  CD2   . TYR A 1 2147 ? 163.478 107.634 181.254 1.00 123.15 ? 3364 TYR A CD2   1 
ATOM   12696 C  CE1   . TYR A 1 2147 ? 160.969 106.729 181.967 1.00 124.27 ? 3364 TYR A CE1   1 
ATOM   12697 C  CE2   . TYR A 1 2147 ? 162.447 108.536 181.434 1.00 118.51 ? 3364 TYR A CE2   1 
ATOM   12698 C  CZ    . TYR A 1 2147 ? 161.195 108.079 181.792 1.00 118.68 ? 3364 TYR A CZ    1 
ATOM   12699 O  OH    . TYR A 1 2147 ? 160.166 108.973 181.974 1.00 114.45 ? 3364 TYR A OH    1 
ATOM   12700 N  N     . ARG A 1 2148 ? 162.313 105.041 178.684 1.00 132.01 ? 3365 ARG A N     1 
ATOM   12701 C  CA    . ARG A 1 2148 ? 161.510 105.813 177.746 1.00 131.25 ? 3365 ARG A CA    1 
ATOM   12702 C  C     . ARG A 1 2148 ? 160.284 106.363 178.457 1.00 128.77 ? 3365 ARG A C     1 
ATOM   12703 O  O     . ARG A 1 2148 ? 159.545 105.613 179.102 1.00 126.77 ? 3365 ARG A O     1 
ATOM   12704 C  CB    . ARG A 1 2148 ? 161.093 104.966 176.539 1.00 130.02 ? 3365 ARG A CB    1 
ATOM   12705 C  CG    . ARG A 1 2148 ? 162.159 104.877 175.458 1.00 131.64 ? 3365 ARG A CG    1 
ATOM   12706 C  CD    . ARG A 1 2148 ? 162.570 106.264 174.985 1.00 134.49 ? 3365 ARG A CD    1 
ATOM   12707 N  NE    . ARG A 1 2148 ? 163.860 106.673 175.530 1.00 135.08 ? 3365 ARG A NE    1 
ATOM   12708 C  CZ    . ARG A 1 2148 ? 164.261 107.932 175.643 1.00 133.76 ? 3365 ARG A CZ    1 
ATOM   12709 N  NH1   . ARG A 1 2148 ? 163.489 108.940 175.268 1.00 130.49 ? 3365 ARG A NH1   1 
ATOM   12710 N  NH2   . ARG A 1 2148 ? 165.463 108.187 176.150 1.00 133.22 ? 3365 ARG A NH2   1 
ATOM   12711 N  N     . PHE A 1 2149 ? 160.077 107.678 178.337 1.00 128.55 ? 3366 PHE A N     1 
ATOM   12712 C  CA    . PHE A 1 2149 ? 158.879 108.304 178.887 1.00 128.95 ? 3366 PHE A CA    1 
ATOM   12713 C  C     . PHE A 1 2149 ? 157.627 107.854 178.147 1.00 128.58 ? 3366 PHE A C     1 
ATOM   12714 O  O     . PHE A 1 2149 ? 156.535 107.841 178.728 1.00 129.71 ? 3366 PHE A O     1 
ATOM   12715 C  CB    . PHE A 1 2149 ? 159.018 109.826 178.831 1.00 125.00 ? 3366 PHE A CB    1 
ATOM   12716 C  CG    . PHE A 1 2149 ? 157.881 110.569 179.475 1.00 120.56 ? 3366 PHE A CG    1 
ATOM   12717 C  CD1   . PHE A 1 2149 ? 157.399 110.191 180.717 1.00 119.40 ? 3366 PHE A CD1   1 
ATOM   12718 C  CD2   . PHE A 1 2149 ? 157.296 111.651 178.836 1.00 116.88 ? 3366 PHE A CD2   1 
ATOM   12719 C  CE1   . PHE A 1 2149 ? 156.352 110.875 181.309 1.00 115.23 ? 3366 PHE A CE1   1 
ATOM   12720 C  CE2   . PHE A 1 2149 ? 156.250 112.339 179.423 1.00 113.13 ? 3366 PHE A CE2   1 
ATOM   12721 C  CZ    . PHE A 1 2149 ? 155.778 111.951 180.661 1.00 110.87 ? 3366 PHE A CZ    1 
ATOM   12722 N  N     . ILE A 1 2150 ? 157.766 107.489 176.870 1.00 127.03 ? 3367 ILE A N     1 
ATOM   12723 C  CA    . ILE A 1 2150 ? 156.625 107.020 176.088 1.00 129.93 ? 3367 ILE A CA    1 
ATOM   12724 C  C     . ILE A 1 2150 ? 156.087 105.714 176.660 1.00 132.04 ? 3367 ILE A C     1 
ATOM   12725 O  O     . ILE A 1 2150 ? 154.872 105.540 176.817 1.00 130.02 ? 3367 ILE A O     1 
ATOM   12726 C  CB    . ILE A 1 2150 ? 157.019 106.870 174.606 1.00 129.25 ? 3367 ILE A CB    1 
ATOM   12727 C  CG1   . ILE A 1 2150 ? 157.407 108.224 174.006 1.00 124.91 ? 3367 ILE A CG1   1 
ATOM   12728 C  CG2   . ILE A 1 2150 ? 155.890 106.237 173.809 1.00 128.65 ? 3367 ILE A CG2   1 
ATOM   12729 C  CD1   . ILE A 1 2150 ? 158.903 108.456 173.914 1.00 127.09 ? 3367 ILE A CD1   1 
ATOM   12730 N  N     . ASP A 1 2151 ? 156.981 104.781 176.995 1.00 135.77 ? 3368 ASP A N     1 
ATOM   12731 C  CA    . ASP A 1 2151 ? 156.552 103.503 177.552 1.00 136.97 ? 3368 ASP A CA    1 
ATOM   12732 C  C     . ASP A 1 2151 ? 155.979 103.642 178.957 1.00 135.46 ? 3368 ASP A C     1 
ATOM   12733 O  O     . ASP A 1 2151 ? 155.235 102.760 179.398 1.00 134.68 ? 3368 ASP A O     1 
ATOM   12734 C  CB    . ASP A 1 2151 ? 157.720 102.516 177.564 1.00 135.52 ? 3368 ASP A CB    1 
ATOM   12735 N  N     . TYR A 1 2152 ? 156.305 104.722 179.667 1.00 134.73 ? 3369 TYR A N     1 
ATOM   12736 C  CA    . TYR A 1 2152 ? 155.812 104.937 181.019 1.00 134.49 ? 3369 TYR A CA    1 
ATOM   12737 C  C     . TYR A 1 2152 ? 154.571 105.819 181.078 1.00 135.12 ? 3369 TYR A C     1 
ATOM   12738 O  O     . TYR A 1 2152 ? 153.886 105.822 182.106 1.00 131.41 ? 3369 TYR A O     1 
ATOM   12739 C  CB    . TYR A 1 2152 ? 156.913 105.556 181.891 1.00 129.28 ? 3369 TYR A CB    1 
ATOM   12740 N  N     . LEU A 1 2153 ? 154.267 106.559 180.019 1.00 135.53 ? 3370 LEU A N     1 
ATOM   12741 C  CA    . LEU A 1 2153 ? 153.111 107.450 180.051 1.00 133.84 ? 3370 LEU A CA    1 
ATOM   12742 C  C     . LEU A 1 2153 ? 152.150 107.243 178.890 1.00 134.67 ? 3370 LEU A C     1 
ATOM   12743 O  O     . LEU A 1 2153 ? 150.936 107.357 179.080 1.00 133.34 ? 3370 LEU A O     1 
ATOM   12744 C  CB    . LEU A 1 2153 ? 153.583 108.913 180.075 1.00 126.78 ? 3370 LEU A CB    1 
ATOM   12745 N  N     . VAL A 1 2154 ? 152.654 106.940 177.696 1.00 136.79 ? 3371 VAL A N     1 
ATOM   12746 C  CA    . VAL A 1 2154 ? 151.835 106.841 176.493 1.00 139.55 ? 3371 VAL A CA    1 
ATOM   12747 C  C     . VAL A 1 2154 ? 151.396 105.395 176.312 1.00 141.82 ? 3371 VAL A C     1 
ATOM   12748 O  O     . VAL A 1 2154 ? 152.230 104.481 176.290 1.00 138.34 ? 3371 VAL A O     1 
ATOM   12749 C  CB    . VAL A 1 2154 ? 152.599 107.343 175.256 1.00 137.87 ? 3371 VAL A CB    1 
ATOM   12750 C  CG1   . VAL A 1 2154 ? 151.703 107.313 174.027 1.00 135.99 ? 3371 VAL A CG1   1 
ATOM   12751 C  CG2   . VAL A 1 2154 ? 153.137 108.745 175.497 1.00 132.78 ? 3371 VAL A CG2   1 
ATOM   12752 N  N     . THR A 1 2155 ? 150.089 105.188 176.181 1.00 141.12 ? 3372 THR A N     1 
ATOM   12753 C  CA    . THR A 1 2155 ? 149.532 103.862 175.969 1.00 139.72 ? 3372 THR A CA    1 
ATOM   12754 C  C     . THR A 1 2155 ? 149.353 103.590 174.477 1.00 138.59 ? 3372 THR A C     1 
ATOM   12755 O  O     . THR A 1 2155 ? 149.405 104.494 173.641 1.00 137.79 ? 3372 THR A O     1 
ATOM   12756 C  CB    . THR A 1 2155 ? 148.197 103.717 176.701 1.00 138.17 ? 3372 THR A CB    1 
ATOM   12757 N  N     . LEU A 1 2156 ? 149.151 102.310 174.149 1.00 138.60 ? 3373 LEU A N     1 
ATOM   12758 C  CA    . LEU A 1 2156 ? 148.979 101.914 172.754 1.00 138.46 ? 3373 LEU A CA    1 
ATOM   12759 C  C     . LEU A 1 2156 ? 147.698 102.491 172.163 1.00 139.48 ? 3373 LEU A C     1 
ATOM   12760 O  O     . LEU A 1 2156 ? 147.690 102.945 171.012 1.00 141.13 ? 3373 LEU A O     1 
ATOM   12761 C  CB    . LEU A 1 2156 ? 148.984 100.390 172.638 1.00 137.44 ? 3373 LEU A CB    1 
ATOM   12762 N  N     . ASP A 1 2157 ? 146.604 102.473 172.930 1.00 139.34 ? 3374 ASP A N     1 
ATOM   12763 C  CA    . ASP A 1 2157 ? 145.352 103.053 172.453 1.00 140.15 ? 3374 ASP A CA    1 
ATOM   12764 C  C     . ASP A 1 2157 ? 145.483 104.557 172.255 1.00 139.19 ? 3374 ASP A C     1 
ATOM   12765 O  O     . ASP A 1 2157 ? 145.005 105.104 171.254 1.00 139.27 ? 3374 ASP A O     1 
ATOM   12766 C  CB    . ASP A 1 2157 ? 144.221 102.735 173.431 1.00 140.14 ? 3374 ASP A CB    1 
ATOM   12767 N  N     . GLU A 1 2158 ? 146.138 105.239 173.198 1.00 139.97 ? 3375 GLU A N     1 
ATOM   12768 C  CA    . GLU A 1 2158 ? 146.376 106.672 173.057 1.00 140.78 ? 3375 GLU A CA    1 
ATOM   12769 C  C     . GLU A 1 2158 ? 147.281 106.965 171.865 1.00 139.73 ? 3375 GLU A C     1 
ATOM   12770 O  O     . GLU A 1 2158 ? 147.046 107.923 171.117 1.00 136.90 ? 3375 GLU A O     1 
ATOM   12771 C  CB    . GLU A 1 2158 ? 146.981 107.223 174.350 1.00 139.46 ? 3375 GLU A CB    1 
ATOM   12772 C  CG    . GLU A 1 2158 ? 147.533 108.633 174.244 1.00 137.61 ? 3375 GLU A CG    1 
ATOM   12773 C  CD    . GLU A 1 2158 ? 147.783 109.265 175.598 1.00 135.89 ? 3375 GLU A CD    1 
ATOM   12774 O  OE1   . GLU A 1 2158 ? 147.043 108.944 176.552 1.00 134.20 ? 3375 GLU A OE1   1 
ATOM   12775 O  OE2   . GLU A 1 2158 ? 148.719 110.085 175.709 1.00 138.08 ? 3375 GLU A OE2   1 
ATOM   12776 N  N     . LYS A 1 2159 ? 148.315 106.141 171.668 1.00 140.18 ? 3376 LYS A N     1 
ATOM   12777 C  CA    . LYS A 1 2159 ? 149.212 106.328 170.532 1.00 138.45 ? 3376 LYS A CA    1 
ATOM   12778 C  C     . LYS A 1 2159 ? 148.475 106.159 169.211 1.00 140.70 ? 3376 LYS A C     1 
ATOM   12779 O  O     . LYS A 1 2159 ? 148.678 106.942 168.277 1.00 140.46 ? 3376 LYS A O     1 
ATOM   12780 C  CB    . LYS A 1 2159 ? 150.384 105.350 170.620 1.00 135.77 ? 3376 LYS A CB    1 
ATOM   12781 N  N     . MET A 1 2160 ? 147.605 105.149 169.117 1.00 141.81 ? 3377 MET A N     1 
ATOM   12782 C  CA    . MET A 1 2160 ? 146.824 104.952 167.899 1.00 141.12 ? 3377 MET A CA    1 
ATOM   12783 C  C     . MET A 1 2160 ? 145.834 106.091 167.680 1.00 140.11 ? 3377 MET A C     1 
ATOM   12784 O  O     . MET A 1 2160 ? 145.633 106.535 166.542 1.00 138.69 ? 3377 MET A O     1 
ATOM   12785 C  CB    . MET A 1 2160 ? 146.094 103.611 167.956 1.00 139.22 ? 3377 MET A CB    1 
ATOM   12786 N  N     . LYS A 1 2161 ? 145.208 106.575 168.759 1.00 140.02 ? 3378 LYS A N     1 
ATOM   12787 C  CA    . LYS A 1 2161 ? 144.253 107.673 168.641 1.00 139.81 ? 3378 LYS A CA    1 
ATOM   12788 C  C     . LYS A 1 2161 ? 144.933 108.952 168.171 1.00 137.95 ? 3378 LYS A C     1 
ATOM   12789 O  O     . LYS A 1 2161 ? 144.357 109.722 167.395 1.00 137.37 ? 3378 LYS A O     1 
ATOM   12790 C  CB    . LYS A 1 2161 ? 143.549 107.901 169.979 1.00 139.12 ? 3378 LYS A CB    1 
ATOM   12791 N  N     . TRP A 1 2162 ? 146.156 109.205 168.641 1.00 137.21 ? 3379 TRP A N     1 
ATOM   12792 C  CA    . TRP A 1 2162 ? 146.880 110.379 168.166 1.00 136.85 ? 3379 TRP A CA    1 
ATOM   12793 C  C     . TRP A 1 2162 ? 147.413 110.183 166.753 1.00 135.54 ? 3379 TRP A C     1 
ATOM   12794 O  O     . TRP A 1 2162 ? 147.437 111.138 165.968 1.00 131.61 ? 3379 TRP A O     1 
ATOM   12795 C  CB    . TRP A 1 2162 ? 148.013 110.730 169.127 1.00 136.68 ? 3379 TRP A CB    1 
ATOM   12796 C  CG    . TRP A 1 2162 ? 147.522 111.398 170.369 1.00 131.37 ? 3379 TRP A CG    1 
ATOM   12797 C  CD1   . TRP A 1 2162 ? 147.505 110.879 171.626 1.00 127.88 ? 3379 TRP A CD1   1 
ATOM   12798 C  CD2   . TRP A 1 2162 ? 146.950 112.707 170.467 1.00 128.34 ? 3379 TRP A CD2   1 
ATOM   12799 N  NE1   . TRP A 1 2162 ? 146.970 111.786 172.507 1.00 125.82 ? 3379 TRP A NE1   1 
ATOM   12800 C  CE2   . TRP A 1 2162 ? 146.620 112.917 171.818 1.00 126.17 ? 3379 TRP A CE2   1 
ATOM   12801 C  CE3   . TRP A 1 2162 ? 146.691 113.724 169.542 1.00 128.12 ? 3379 TRP A CE3   1 
ATOM   12802 C  CZ2   . TRP A 1 2162 ? 146.044 114.100 172.269 1.00 125.11 ? 3379 TRP A CZ2   1 
ATOM   12803 C  CZ3   . TRP A 1 2162 ? 146.119 114.898 169.992 1.00 126.16 ? 3379 TRP A CZ3   1 
ATOM   12804 C  CH2   . TRP A 1 2162 ? 145.802 115.077 171.343 1.00 125.86 ? 3379 TRP A CH2   1 
ATOM   12805 N  N     . LEU A 1 2163 ? 147.841 108.964 166.409 1.00 137.08 ? 3380 LEU A N     1 
ATOM   12806 C  CA    . LEU A 1 2163 ? 148.346 108.704 165.065 1.00 137.54 ? 3380 LEU A CA    1 
ATOM   12807 C  C     . LEU A 1 2163 ? 147.250 108.859 164.018 1.00 140.29 ? 3380 LEU A C     1 
ATOM   12808 O  O     . LEU A 1 2163 ? 147.497 109.399 162.933 1.00 137.99 ? 3380 LEU A O     1 
ATOM   12809 C  CB    . LEU A 1 2163 ? 148.961 107.307 164.998 1.00 137.46 ? 3380 LEU A CB    1 
ATOM   12810 N  N     . GLU A 1 2164 ? 146.033 108.396 164.319 1.00 141.60 ? 3381 GLU A N     1 
ATOM   12811 C  CA    . GLU A 1 2164 ? 144.941 108.567 163.368 1.00 140.40 ? 3381 GLU A CA    1 
ATOM   12812 C  C     . GLU A 1 2164 ? 144.455 110.010 163.303 1.00 138.92 ? 3381 GLU A C     1 
ATOM   12813 O  O     . GLU A 1 2164 ? 143.857 110.404 162.297 1.00 137.16 ? 3381 GLU A O     1 
ATOM   12814 C  CB    . GLU A 1 2164 ? 143.776 107.632 163.711 1.00 139.95 ? 3381 GLU A CB    1 
ATOM   12815 C  CG    . GLU A 1 2164 ? 143.066 107.931 165.024 1.00 138.88 ? 3381 GLU A CG    1 
ATOM   12816 C  CD    . GLU A 1 2164 ? 141.850 108.825 164.848 1.00 138.44 ? 3381 GLU A CD    1 
ATOM   12817 O  OE1   . GLU A 1 2164 ? 141.340 108.920 163.712 1.00 138.47 ? 3381 GLU A OE1   1 
ATOM   12818 O  OE2   . GLU A 1 2164 ? 141.406 109.432 165.845 1.00 137.54 ? 3381 GLU A OE2   1 
ATOM   12819 N  N     . CYS A 1 2165 ? 144.703 110.805 164.346 1.00 139.29 ? 3382 CYS A N     1 
ATOM   12820 C  CA    . CYS A 1 2165 ? 144.293 112.203 164.353 1.00 138.52 ? 3382 CYS A CA    1 
ATOM   12821 C  C     . CYS A 1 2165 ? 145.209 113.093 163.524 1.00 135.41 ? 3382 CYS A C     1 
ATOM   12822 O  O     . CYS A 1 2165 ? 144.859 114.253 163.279 1.00 131.40 ? 3382 CYS A O     1 
ATOM   12823 C  CB    . CYS A 1 2165 ? 144.232 112.728 165.789 1.00 138.26 ? 3382 CYS A CB    1 
ATOM   12824 S  SG    . CYS A 1 2165 ? 142.659 112.430 166.629 1.00 136.69 ? 3382 CYS A SG    1 
ATOM   12825 N  N     . GLY A 1 2166 ? 146.355 112.584 163.083 1.00 134.62 ? 3383 GLY A N     1 
ATOM   12826 C  CA    . GLY A 1 2166 ? 147.277 113.345 162.268 1.00 133.21 ? 3383 GLY A CA    1 
ATOM   12827 C  C     . GLY A 1 2166 ? 148.649 113.573 162.862 1.00 128.99 ? 3383 GLY A C     1 
ATOM   12828 O  O     . GLY A 1 2166 ? 149.459 114.273 162.245 1.00 125.48 ? 3383 GLY A O     1 
ATOM   12829 N  N     . LEU A 1 2167 ? 148.943 113.007 164.030 1.00 126.37 ? 3384 LEU A N     1 
ATOM   12830 C  CA    . LEU A 1 2167 ? 150.256 113.182 164.632 1.00 122.28 ? 3384 LEU A CA    1 
ATOM   12831 C  C     . LEU A 1 2167 ? 151.307 112.410 163.845 1.00 122.68 ? 3384 LEU A C     1 
ATOM   12832 O  O     . LEU A 1 2167 ? 151.048 111.315 163.338 1.00 123.90 ? 3384 LEU A O     1 
ATOM   12833 C  CB    . LEU A 1 2167 ? 150.241 112.716 166.087 1.00 121.15 ? 3384 LEU A CB    1 
ATOM   12834 C  CG    . LEU A 1 2167 ? 151.441 113.089 166.959 1.00 115.55 ? 3384 LEU A CG    1 
ATOM   12835 C  CD1   . LEU A 1 2167 ? 151.838 114.542 166.741 1.00 110.91 ? 3384 LEU A CD1   1 
ATOM   12836 C  CD2   . LEU A 1 2167 ? 151.141 112.821 168.421 1.00 114.99 ? 3384 LEU A CD2   1 
ATOM   12837 N  N     . ASP A 1 2168 ? 152.500 112.990 163.740 1.00 120.76 ? 3385 ASP A N     1 
ATOM   12838 C  CA    . ASP A 1 2168 ? 153.576 112.356 162.997 1.00 118.75 ? 3385 ASP A CA    1 
ATOM   12839 C  C     . ASP A 1 2168 ? 154.167 111.193 163.795 1.00 115.02 ? 3385 ASP A C     1 
ATOM   12840 O  O     . ASP A 1 2168 ? 153.846 110.971 164.966 1.00 113.29 ? 3385 ASP A O     1 
ATOM   12841 C  CB    . ASP A 1 2168 ? 154.661 113.375 162.651 1.00 116.39 ? 3385 ASP A CB    1 
ATOM   12842 C  CG    . ASP A 1 2168 ? 154.204 114.380 161.614 1.00 116.23 ? 3385 ASP A CG    1 
ATOM   12843 O  OD1   . ASP A 1 2168 ? 153.283 114.055 160.835 1.00 117.80 ? 3385 ASP A OD1   1 
ATOM   12844 O  OD2   . ASP A 1 2168 ? 154.768 115.494 161.571 1.00 111.80 ? 3385 ASP A OD2   1 
ATOM   12845 N  N     . LYS A 1 2169 ? 155.048 110.444 163.136 1.00 113.75 ? 3386 LYS A N     1 
ATOM   12846 C  CA    . LYS A 1 2169 ? 155.674 109.270 163.727 1.00 115.58 ? 3386 LYS A CA    1 
ATOM   12847 C  C     . LYS A 1 2169 ? 156.991 109.583 164.424 1.00 116.54 ? 3386 LYS A C     1 
ATOM   12848 O  O     . LYS A 1 2169 ? 157.626 108.664 164.952 1.00 119.73 ? 3386 LYS A O     1 
ATOM   12849 C  CB    . LYS A 1 2169 ? 155.905 108.202 162.653 1.00 116.36 ? 3386 LYS A CB    1 
ATOM   12850 N  N     . ASN A 1 2170 ? 157.417 110.844 164.432 1.00 114.76 ? 3387 ASN A N     1 
ATOM   12851 C  CA    . ASN A 1 2170 ? 158.660 111.214 165.092 1.00 113.38 ? 3387 ASN A CA    1 
ATOM   12852 C  C     . ASN A 1 2170 ? 158.528 111.093 166.606 1.00 110.98 ? 3387 ASN A C     1 
ATOM   12853 O  O     . ASN A 1 2170 ? 157.442 111.235 167.174 1.00 112.59 ? 3387 ASN A O     1 
ATOM   12854 C  CB    . ASN A 1 2170 ? 159.061 112.643 164.724 1.00 110.62 ? 3387 ASN A CB    1 
ATOM   12855 C  CG    . ASN A 1 2170 ? 159.367 112.804 163.250 1.00 109.99 ? 3387 ASN A CG    1 
ATOM   12856 O  OD1   . ASN A 1 2170 ? 159.610 111.827 162.544 1.00 116.14 ? 3387 ASN A OD1   1 
ATOM   12857 N  ND2   . ASN A 1 2170 ? 159.359 114.045 162.777 1.00 102.99 ? 3387 ASN A ND2   1 
ATOM   12858 N  N     . ASP A 1 2171 ? 159.656 110.815 167.261 1.00 107.59 ? 3388 ASP A N     1 
ATOM   12859 C  CA    . ASP A 1 2171 ? 159.678 110.822 168.719 1.00 108.42 ? 3388 ASP A CA    1 
ATOM   12860 C  C     . ASP A 1 2171 ? 159.495 112.229 169.278 1.00 109.79 ? 3388 ASP A C     1 
ATOM   12861 O  O     . ASP A 1 2171 ? 158.943 112.392 170.374 1.00 107.35 ? 3388 ASP A O     1 
ATOM   12862 C  CB    . ASP A 1 2171 ? 160.977 110.184 169.221 1.00 111.88 ? 3388 ASP A CB    1 
ATOM   12863 C  CG    . ASP A 1 2171 ? 162.226 110.926 168.760 1.00 113.03 ? 3388 ASP A CG    1 
ATOM   12864 O  OD1   . ASP A 1 2171 ? 162.119 111.914 168.002 1.00 111.86 ? 3388 ASP A OD1   1 
ATOM   12865 O  OD2   . ASP A 1 2171 ? 163.333 110.509 169.160 1.00 112.60 ? 3388 ASP A OD2   1 
ATOM   12866 N  N     . TYR A 1 2172 ? 159.948 113.242 168.532 1.00 109.35 ? 3389 TYR A N     1 
ATOM   12867 C  CA    . TYR A 1 2172 ? 159.816 114.633 168.958 1.00 103.46 ? 3389 TYR A CA    1 
ATOM   12868 C  C     . TYR A 1 2172 ? 158.353 115.013 169.156 1.00 101.83 ? 3389 TYR A C     1 
ATOM   12869 O  O     . TYR A 1 2172 ? 157.967 115.506 170.221 1.00 103.39 ? 3389 TYR A O     1 
ATOM   12870 C  CB    . TYR A 1 2172 ? 160.476 115.543 167.920 1.00 100.65 ? 3389 TYR A CB    1 
ATOM   12871 C  CG    . TYR A 1 2172 ? 160.635 116.996 168.322 1.00 103.54 ? 3389 TYR A CG    1 
ATOM   12872 C  CD1   . TYR A 1 2172 ? 160.563 117.392 169.653 1.00 104.55 ? 3389 TYR A CD1   1 
ATOM   12873 C  CD2   . TYR A 1 2172 ? 160.862 117.973 167.361 1.00 103.98 ? 3389 TYR A CD2   1 
ATOM   12874 C  CE1   . TYR A 1 2172 ? 160.708 118.720 170.012 1.00 99.80  ? 3389 TYR A CE1   1 
ATOM   12875 C  CE2   . TYR A 1 2172 ? 161.009 119.300 167.710 1.00 106.38 ? 3389 TYR A CE2   1 
ATOM   12876 C  CZ    . TYR A 1 2172 ? 160.932 119.668 169.037 1.00 102.97 ? 3389 TYR A CZ    1 
ATOM   12877 O  OH    . TYR A 1 2172 ? 161.079 120.990 169.386 1.00 100.29 ? 3389 TYR A OH    1 
ATOM   12878 N  N     . PHE A 1 2173 ? 157.517 114.768 168.147 1.00 98.93  ? 3390 PHE A N     1 
ATOM   12879 C  CA    . PHE A 1 2173 ? 156.113 115.145 168.265 1.00 99.79  ? 3390 PHE A CA    1 
ATOM   12880 C  C     . PHE A 1 2173 ? 155.363 114.226 169.220 1.00 103.13 ? 3390 PHE A C     1 
ATOM   12881 O  O     . PHE A 1 2173 ? 154.387 114.653 169.847 1.00 108.45 ? 3390 PHE A O     1 
ATOM   12882 C  CB    . PHE A 1 2173 ? 155.450 115.160 166.887 1.00 101.68 ? 3390 PHE A CB    1 
ATOM   12883 C  CG    . PHE A 1 2173 ? 155.914 116.285 165.999 1.00 105.45 ? 3390 PHE A CG    1 
ATOM   12884 C  CD1   . PHE A 1 2173 ? 156.669 117.330 166.509 1.00 103.43 ? 3390 PHE A CD1   1 
ATOM   12885 C  CD2   . PHE A 1 2173 ? 155.587 116.302 164.654 1.00 111.72 ? 3390 PHE A CD2   1 
ATOM   12886 C  CE1   . PHE A 1 2173 ? 157.095 118.362 165.695 1.00 104.80 ? 3390 PHE A CE1   1 
ATOM   12887 C  CE2   . PHE A 1 2173 ? 156.010 117.334 163.835 1.00 110.37 ? 3390 PHE A CE2   1 
ATOM   12888 C  CZ    . PHE A 1 2173 ? 156.764 118.364 164.358 1.00 108.68 ? 3390 PHE A CZ    1 
ATOM   12889 N  N     . LEU A 1 2174 ? 155.817 112.980 169.370 1.00 102.52 ? 3391 LEU A N     1 
ATOM   12890 C  CA    . LEU A 1 2174 ? 155.204 112.079 170.341 1.00 102.88 ? 3391 LEU A CA    1 
ATOM   12891 C  C     . LEU A 1 2174 ? 155.412 112.584 171.766 1.00 102.57 ? 3391 LEU A C     1 
ATOM   12892 O  O     . LEU A 1 2174 ? 154.458 112.672 172.553 1.00 106.11 ? 3391 LEU A O     1 
ATOM   12893 C  CB    . LEU A 1 2174 ? 155.774 110.671 170.173 1.00 107.31 ? 3391 LEU A CB    1 
ATOM   12894 C  CG    . LEU A 1 2174 ? 154.917 109.502 170.659 1.00 110.98 ? 3391 LEU A CG    1 
ATOM   12895 C  CD1   . LEU A 1 2174 ? 153.686 109.340 169.783 1.00 109.99 ? 3391 LEU A CD1   1 
ATOM   12896 C  CD2   . LEU A 1 2174 ? 155.736 108.224 170.667 1.00 112.98 ? 3391 LEU A CD2   1 
ATOM   12897 N  N     . GLU A 1 2175 ? 156.648 112.957 172.109 1.00 101.01 ? 3392 GLU A N     1 
ATOM   12898 C  CA    . GLU A 1 2175 ? 156.884 113.491 173.446 1.00 101.04 ? 3392 GLU A CA    1 
ATOM   12899 C  C     . GLU A 1 2175 ? 156.299 114.891 173.597 1.00 99.70  ? 3392 GLU A C     1 
ATOM   12900 O  O     . GLU A 1 2175 ? 155.932 115.286 174.709 1.00 99.20  ? 3392 GLU A O     1 
ATOM   12901 C  CB    . GLU A 1 2175 ? 158.380 113.462 173.780 1.00 99.18  ? 3392 GLU A CB    1 
ATOM   12902 C  CG    . GLU A 1 2175 ? 159.290 114.328 172.922 1.00 97.64  ? 3392 GLU A CG    1 
ATOM   12903 C  CD    . GLU A 1 2175 ? 159.498 115.718 173.489 1.00 96.32  ? 3392 GLU A CD    1 
ATOM   12904 O  OE1   . GLU A 1 2175 ? 159.253 115.912 174.698 1.00 95.09  ? 3392 GLU A OE1   1 
ATOM   12905 O  OE2   . GLU A 1 2175 ? 159.931 116.611 172.733 1.00 96.61  ? 3392 GLU A OE2   1 
ATOM   12906 N  N     . ASN A 1 2176 ? 156.168 115.636 172.494 1.00 96.85  ? 3393 ASN A N     1 
ATOM   12907 C  CA    . ASN A 1 2176 ? 155.463 116.914 172.537 1.00 91.03  ? 3393 ASN A CA    1 
ATOM   12908 C  C     . ASN A 1 2176 ? 154.005 116.723 172.936 1.00 92.89  ? 3393 ASN A C     1 
ATOM   12909 O  O     . ASN A 1 2176 ? 153.486 117.438 173.800 1.00 97.76  ? 3393 ASN A O     1 
ATOM   12910 C  CB    . ASN A 1 2176 ? 155.554 117.609 171.178 1.00 89.03  ? 3393 ASN A CB    1 
ATOM   12911 C  CG    . ASN A 1 2176 ? 156.856 118.356 170.991 1.00 89.23  ? 3393 ASN A CG    1 
ATOM   12912 O  OD1   . ASN A 1 2176 ? 157.801 118.180 171.754 1.00 87.40  ? 3393 ASN A OD1   1 
ATOM   12913 N  ND2   . ASN A 1 2176 ? 156.908 119.204 169.972 1.00 91.65  ? 3393 ASN A ND2   1 
ATOM   12914 N  N     . MET A 1 2177 ? 153.330 115.752 172.316 1.00 96.84  ? 3394 MET A N     1 
ATOM   12915 C  CA    . MET A 1 2177 ? 151.940 115.472 172.664 1.00 101.05 ? 3394 MET A CA    1 
ATOM   12916 C  C     . MET A 1 2177 ? 151.830 114.955 174.092 1.00 102.22 ? 3394 MET A C     1 
ATOM   12917 O  O     . MET A 1 2177 ? 150.866 115.277 174.800 1.00 103.09 ? 3394 MET A O     1 
ATOM   12918 C  CB    . MET A 1 2177 ? 151.345 114.493 171.641 1.00 108.41 ? 3394 MET A CB    1 
ATOM   12919 C  CG    . MET A 1 2177 ? 150.059 113.701 171.991 1.00 114.11 ? 3394 MET A CG    1 
ATOM   12920 S  SD    . MET A 1 2177 ? 150.057 112.426 173.281 1.00 120.60 ? 3394 MET A SD    1 
ATOM   12921 C  CE    . MET A 1 2177 ? 151.224 111.252 172.598 1.00 116.68 ? 3394 MET A CE    1 
ATOM   12922 N  N     . SER A 1 2178 ? 152.794 114.135 174.525 1.00 103.00 ? 3395 SER A N     1 
ATOM   12923 C  CA    . SER A 1 2178 ? 152.782 113.651 175.903 1.00 103.66 ? 3395 SER A CA    1 
ATOM   12924 C  C     . SER A 1 2178 ? 152.908 114.803 176.894 1.00 102.43 ? 3395 SER A C     1 
ATOM   12925 O  O     . SER A 1 2178 ? 152.191 114.848 177.900 1.00 102.16 ? 3395 SER A O     1 
ATOM   12926 C  CB    . SER A 1 2178 ? 153.902 112.634 176.116 1.00 105.10 ? 3395 SER A CB    1 
ATOM   12927 O  OG    . SER A 1 2178 ? 155.159 113.276 176.240 1.00 101.96 ? 3395 SER A OG    1 
ATOM   12928 N  N     . ILE A 1 2179 ? 153.803 115.755 176.615 1.00 102.18 ? 3396 ILE A N     1 
ATOM   12929 C  CA    . ILE A 1 2179 ? 153.953 116.920 177.481 1.00 100.42 ? 3396 ILE A CA    1 
ATOM   12930 C  C     . ILE A 1 2179 ? 152.704 117.793 177.441 1.00 99.55  ? 3396 ILE A C     1 
ATOM   12931 O  O     . ILE A 1 2179 ? 152.335 118.404 178.451 1.00 98.74  ? 3396 ILE A O     1 
ATOM   12932 C  CB    . ILE A 1 2179 ? 155.210 117.717 177.090 1.00 93.88  ? 3396 ILE A CB    1 
ATOM   12933 N  N     . VAL A 1 2180 ? 152.044 117.879 176.283 1.00 100.24 ? 3397 VAL A N     1 
ATOM   12934 C  CA    . VAL A 1 2180 ? 150.843 118.703 176.165 1.00 98.35  ? 3397 VAL A CA    1 
ATOM   12935 C  C     . VAL A 1 2180 ? 149.703 118.116 176.991 1.00 102.00 ? 3397 VAL A C     1 
ATOM   12936 O  O     . VAL A 1 2180 ? 149.046 118.825 177.763 1.00 105.45 ? 3397 VAL A O     1 
ATOM   12937 C  CB    . VAL A 1 2180 ? 150.444 118.857 174.685 1.00 95.12  ? 3397 VAL A CB    1 
ATOM   12938 C  CG1   . VAL A 1 2180 ? 148.984 119.262 174.556 1.00 94.81  ? 3397 VAL A CG1   1 
ATOM   12939 C  CG2   . VAL A 1 2180 ? 151.327 119.876 174.003 1.00 91.08  ? 3397 VAL A CG2   1 
ATOM   12940 N  N     . MET A 1 2181 ? 149.463 116.813 176.860 1.00 103.66 ? 3398 MET A N     1 
ATOM   12941 C  CA    . MET A 1 2181 ? 148.305 116.182 177.480 1.00 106.65 ? 3398 MET A CA    1 
ATOM   12942 C  C     . MET A 1 2181 ? 148.633 115.485 178.795 1.00 107.54 ? 3398 MET A C     1 
ATOM   12943 O  O     . MET A 1 2181 ? 147.798 114.736 179.312 1.00 107.08 ? 3398 MET A O     1 
ATOM   12944 C  CB    . MET A 1 2181 ? 147.653 115.204 176.501 1.00 108.26 ? 3398 MET A CB    1 
ATOM   12945 C  CG    . MET A 1 2181 ? 146.132 115.192 176.569 1.00 109.42 ? 3398 MET A CG    1 
ATOM   12946 S  SD    . MET A 1 2181 ? 145.379 116.738 176.022 1.00 112.42 ? 3398 MET A SD    1 
ATOM   12947 C  CE    . MET A 1 2181 ? 146.103 116.932 174.398 1.00 107.48 ? 3398 MET A CE    1 
ATOM   12948 N  N     . ASN A 1 2182 ? 149.820 115.713 179.349 1.00 107.45 ? 3399 ASN A N     1 
ATOM   12949 C  CA    . ASN A 1 2182 ? 150.152 115.290 180.706 1.00 108.66 ? 3399 ASN A CA    1 
ATOM   12950 C  C     . ASN A 1 2182 ? 150.347 116.501 181.614 1.00 109.89 ? 3399 ASN A C     1 
ATOM   12951 O  O     . ASN A 1 2182 ? 151.244 116.532 182.458 1.00 109.39 ? 3399 ASN A O     1 
ATOM   12952 C  CB    . ASN A 1 2182 ? 151.391 114.400 180.712 1.00 106.45 ? 3399 ASN A CB    1 
ATOM   12953 C  CG    . ASN A 1 2182 ? 151.123 113.025 180.130 1.00 108.83 ? 3399 ASN A CG    1 
ATOM   12954 O  OD1   . ASN A 1 2182 ? 150.065 112.439 180.355 1.00 111.20 ? 3399 ASN A OD1   1 
ATOM   12955 N  ND2   . ASN A 1 2182 ? 152.084 112.503 179.376 1.00 109.19 ? 3399 ASN A ND2   1 
ATOM   12956 N  N     . SER A 1 2183 ? 149.496 117.514 181.443 1.00 109.17 ? 3400 SER A N     1 
ATOM   12957 C  CA    . SER A 1 2183 ? 149.586 118.784 182.165 1.00 104.68 ? 3400 SER A CA    1 
ATOM   12958 C  C     . SER A 1 2183 ? 148.197 119.128 182.694 1.00 107.53 ? 3400 SER A C     1 
ATOM   12959 O  O     . SER A 1 2183 ? 147.404 119.774 182.004 1.00 109.82 ? 3400 SER A O     1 
ATOM   12960 C  CB    . SER A 1 2183 ? 150.130 119.882 181.258 1.00 98.94  ? 3400 SER A CB    1 
ATOM   12961 O  OG    . SER A 1 2183 ? 150.196 121.123 181.936 1.00 97.61  ? 3400 SER A OG    1 
ATOM   12962 N  N     . GLN A 1 2184 ? 147.903 118.696 183.919 1.00 105.47 ? 3401 GLN A N     1 
ATOM   12963 C  CA    . GLN A 1 2184 ? 146.598 118.928 184.520 1.00 105.44 ? 3401 GLN A CA    1 
ATOM   12964 C  C     . GLN A 1 2184 ? 146.520 120.220 185.324 1.00 103.34 ? 3401 GLN A C     1 
ATOM   12965 O  O     . GLN A 1 2184 ? 145.413 120.645 185.672 1.00 103.11 ? 3401 GLN A O     1 
ATOM   12966 C  CB    . GLN A 1 2184 ? 146.217 117.749 185.422 1.00 106.68 ? 3401 GLN A CB    1 
ATOM   12967 C  CG    . GLN A 1 2184 ? 147.184 117.501 186.570 1.00 106.40 ? 3401 GLN A CG    1 
ATOM   12968 C  CD    . GLN A 1 2184 ? 146.710 118.111 187.875 1.00 110.67 ? 3401 GLN A CD    1 
ATOM   12969 O  OE1   . GLN A 1 2184 ? 145.595 118.625 187.965 1.00 112.25 ? 3401 GLN A OE1   1 
ATOM   12970 N  NE2   . GLN A 1 2184 ? 147.557 118.056 188.896 1.00 111.35 ? 3401 GLN A NE2   1 
ATOM   12971 N  N     . ASP A 1 2185 ? 147.650 120.853 185.625 1.00 101.46 ? 3402 ASP A N     1 
ATOM   12972 C  CA    . ASP A 1 2185 ? 147.676 122.035 186.481 1.00 101.45 ? 3402 ASP A CA    1 
ATOM   12973 C  C     . ASP A 1 2185 ? 147.923 123.331 185.728 1.00 100.26 ? 3402 ASP A C     1 
ATOM   12974 O  O     . ASP A 1 2185 ? 147.402 124.375 186.126 1.00 103.43 ? 3402 ASP A O     1 
ATOM   12975 C  CB    . ASP A 1 2185 ? 148.741 121.872 187.574 1.00 102.18 ? 3402 ASP A CB    1 
ATOM   12976 C  CG    . ASP A 1 2185 ? 150.092 121.459 187.021 1.00 99.36  ? 3402 ASP A CG    1 
ATOM   12977 O  OD1   . ASP A 1 2185 ? 150.213 121.288 185.790 1.00 95.99  ? 3402 ASP A OD1   1 
ATOM   12978 O  OD2   . ASP A 1 2185 ? 151.036 121.297 187.823 1.00 97.92  ? 3402 ASP A OD2   1 
ATOM   12979 N  N     . ALA A 1 2186 ? 148.703 123.298 184.653 1.00 95.04  ? 3403 ALA A N     1 
ATOM   12980 C  CA    . ALA A 1 2186 ? 148.986 124.477 183.849 1.00 90.79  ? 3403 ALA A CA    1 
ATOM   12981 C  C     . ALA A 1 2186 ? 148.353 124.326 182.474 1.00 92.03  ? 3403 ALA A C     1 
ATOM   12982 O  O     . ALA A 1 2186 ? 148.319 123.226 181.914 1.00 90.78  ? 3403 ALA A O     1 
ATOM   12983 C  CB    . ALA A 1 2186 ? 150.493 124.700 183.711 1.00 86.55  ? 3403 ALA A CB    1 
ATOM   12984 N  N     . VAL A 1 2187 ? 147.846 125.429 181.938 1.00 93.20  ? 3404 VAL A N     1 
ATOM   12985 C  CA    . VAL A 1 2187 ? 147.263 125.395 180.592 1.00 87.20  ? 3404 VAL A CA    1 
ATOM   12986 C  C     . VAL A 1 2187 ? 148.380 125.225 179.565 1.00 83.75  ? 3404 VAL A C     1 
ATOM   12987 O  O     . VAL A 1 2187 ? 149.377 125.969 179.602 1.00 85.20  ? 3404 VAL A O     1 
ATOM   12988 C  CB    . VAL A 1 2187 ? 146.435 126.661 180.330 1.00 85.90  ? 3404 VAL A CB    1 
ATOM   12989 C  CG1   . VAL A 1 2187 ? 145.152 126.618 181.145 1.00 87.47  ? 3404 VAL A CG1   1 
ATOM   12990 C  CG2   . VAL A 1 2187 ? 147.211 127.919 180.692 1.00 85.61  ? 3404 VAL A CG2   1 
ATOM   12991 N  N     . PRO A 1 2188 ? 148.293 124.239 178.676 1.00 81.13  ? 3405 PRO A N     1 
ATOM   12992 C  CA    . PRO A 1 2188 ? 149.390 123.996 177.734 1.00 77.57  ? 3405 PRO A CA    1 
ATOM   12993 C  C     . PRO A 1 2188 ? 149.519 125.099 176.695 1.00 73.08  ? 3405 PRO A C     1 
ATOM   12994 O  O     . PRO A 1 2188 ? 148.553 125.783 176.351 1.00 79.81  ? 3405 PRO A O     1 
ATOM   12995 C  CB    . PRO A 1 2188 ? 149.011 122.662 177.080 1.00 82.42  ? 3405 PRO A CB    1 
ATOM   12996 C  CG    . PRO A 1 2188 ? 147.551 122.514 177.317 1.00 83.57  ? 3405 PRO A CG    1 
ATOM   12997 C  CD    . PRO A 1 2188 ? 147.255 123.198 178.608 1.00 83.93  ? 3405 PRO A CD    1 
ATOM   12998 N  N     . PHE A 1 2189 ? 150.742 125.264 176.201 1.00 69.70  ? 3406 PHE A N     1 
ATOM   12999 C  CA    . PHE A 1 2189 ? 151.060 126.205 175.139 1.00 72.96  ? 3406 PHE A CA    1 
ATOM   13000 C  C     . PHE A 1 2189 ? 151.469 125.424 173.899 1.00 82.88  ? 3406 PHE A C     1 
ATOM   13001 O  O     . PHE A 1 2189 ? 152.235 124.460 173.989 1.00 90.35  ? 3406 PHE A O     1 
ATOM   13002 C  CB    . PHE A 1 2189 ? 152.188 127.148 175.564 1.00 72.90  ? 3406 PHE A CB    1 
ATOM   13003 C  CG    . PHE A 1 2189 ? 152.230 128.444 174.800 1.00 77.55  ? 3406 PHE A CG    1 
ATOM   13004 C  CD1   . PHE A 1 2189 ? 152.688 128.486 173.494 1.00 81.65  ? 3406 PHE A CD1   1 
ATOM   13005 C  CD2   . PHE A 1 2189 ? 151.833 129.626 175.400 1.00 84.25  ? 3406 PHE A CD2   1 
ATOM   13006 C  CE1   . PHE A 1 2189 ? 152.735 129.679 172.798 1.00 88.42  ? 3406 PHE A CE1   1 
ATOM   13007 C  CE2   . PHE A 1 2189 ? 151.880 130.822 174.710 1.00 87.43  ? 3406 PHE A CE2   1 
ATOM   13008 C  CZ    . PHE A 1 2189 ? 152.330 130.848 173.407 1.00 89.81  ? 3406 PHE A CZ    1 
ATOM   13009 N  N     . LEU A 1 2190 ? 150.955 125.837 172.744 1.00 85.93  ? 3407 LEU A N     1 
ATOM   13010 C  CA    . LEU A 1 2190 ? 151.189 125.145 171.478 1.00 86.42  ? 3407 LEU A CA    1 
ATOM   13011 C  C     . LEU A 1 2190 ? 151.784 126.141 170.486 1.00 91.96  ? 3407 LEU A C     1 
ATOM   13012 O  O     . LEU A 1 2190 ? 151.058 126.754 169.700 1.00 99.07  ? 3407 LEU A O     1 
ATOM   13013 C  CB    . LEU A 1 2190 ? 149.888 124.537 170.938 1.00 89.41  ? 3407 LEU A CB    1 
ATOM   13014 C  CG    . LEU A 1 2190 ? 149.545 123.076 171.245 1.00 91.07  ? 3407 LEU A CG    1 
ATOM   13015 C  CD1   . LEU A 1 2190 ? 149.498 122.812 172.737 1.00 86.50  ? 3407 LEU A CD1   1 
ATOM   13016 C  CD2   . LEU A 1 2190 ? 148.223 122.699 170.600 1.00 98.97  ? 3407 LEU A CD2   1 
ATOM   13017 N  N     . LEU A 1 2191 ? 153.107 126.297 170.511 1.00 88.27  ? 3408 LEU A N     1 
ATOM   13018 C  CA    . LEU A 1 2191 ? 153.790 127.169 169.555 1.00 93.58  ? 3408 LEU A CA    1 
ATOM   13019 C  C     . LEU A 1 2191 ? 154.063 126.328 168.317 1.00 103.06 ? 3408 LEU A C     1 
ATOM   13020 O  O     . LEU A 1 2191 ? 155.046 125.590 168.242 1.00 103.47 ? 3408 LEU A O     1 
ATOM   13021 C  CB    . LEU A 1 2191 ? 155.062 127.758 170.156 1.00 93.70  ? 3408 LEU A CB    1 
ATOM   13022 C  CG    . LEU A 1 2191 ? 155.809 128.866 169.398 1.00 101.51 ? 3408 LEU A CG    1 
ATOM   13023 C  CD1   . LEU A 1 2191 ? 156.534 129.765 170.385 1.00 103.00 ? 3408 LEU A CD1   1 
ATOM   13024 C  CD2   . LEU A 1 2191 ? 156.803 128.327 168.376 1.00 104.23 ? 3408 LEU A CD2   1 
ATOM   13025 N  N     . ASP A 1 2192 ? 153.173 126.432 167.338 1.00 109.57 ? 3409 ASP A N     1 
ATOM   13026 C  CA    . ASP A 1 2192 ? 153.230 125.608 166.132 1.00 112.84 ? 3409 ASP A CA    1 
ATOM   13027 C  C     . ASP A 1 2192 ? 153.130 126.502 164.904 1.00 115.10 ? 3409 ASP A C     1 
ATOM   13028 O  O     . ASP A 1 2192 ? 152.035 127.029 164.615 1.00 115.30 ? 3409 ASP A O     1 
ATOM   13029 C  CB    . ASP A 1 2192 ? 152.112 124.570 166.154 1.00 112.64 ? 3409 ASP A CB    1 
ATOM   13030 C  CG    . ASP A 1 2192 ? 152.134 123.664 164.949 1.00 116.42 ? 3409 ASP A CG    1 
ATOM   13031 O  OD1   . ASP A 1 2192 ? 153.226 123.436 164.387 1.00 114.82 ? 3409 ASP A OD1   1 
ATOM   13032 O  OD2   . ASP A 1 2192 ? 151.053 123.175 164.567 1.00 119.49 ? 3409 ASP A OD2   1 
ATOM   13033 N  N     . PRO A 1 2193 ? 154.222 126.706 164.162 1.00 117.99 ? 3410 PRO A N     1 
ATOM   13034 C  CA    . PRO A 1 2193 ? 154.151 127.606 163.000 1.00 120.23 ? 3410 PRO A CA    1 
ATOM   13035 C  C     . PRO A 1 2193 ? 153.433 127.005 161.806 1.00 120.78 ? 3410 PRO A C     1 
ATOM   13036 O  O     . PRO A 1 2193 ? 152.903 127.755 160.978 1.00 119.31 ? 3410 PRO A O     1 
ATOM   13037 C  CB    . PRO A 1 2193 ? 155.627 127.885 162.688 1.00 120.80 ? 3410 PRO A CB    1 
ATOM   13038 C  CG    . PRO A 1 2193 ? 156.338 126.669 163.173 1.00 119.00 ? 3410 PRO A CG    1 
ATOM   13039 C  CD    . PRO A 1 2193 ? 155.584 126.195 164.389 1.00 116.67 ? 3410 PRO A CD    1 
ATOM   13040 N  N     . SER A 1 2194 ? 153.397 125.681 161.688 1.00 122.08 ? 3411 SER A N     1 
ATOM   13041 C  CA    . SER A 1 2194 ? 152.765 125.021 160.554 1.00 122.70 ? 3411 SER A CA    1 
ATOM   13042 C  C     . SER A 1 2194 ? 151.266 124.828 160.738 1.00 120.92 ? 3411 SER A C     1 
ATOM   13043 O  O     . SER A 1 2194 ? 150.614 124.298 159.831 1.00 118.32 ? 3411 SER A O     1 
ATOM   13044 C  CB    . SER A 1 2194 ? 153.429 123.665 160.297 1.00 122.66 ? 3411 SER A CB    1 
ATOM   13045 O  OG    . SER A 1 2194 ? 153.395 122.853 161.457 1.00 119.91 ? 3411 SER A OG    1 
ATOM   13046 N  N     . SER A 1 2195 ? 150.719 125.239 161.887 1.00 121.56 ? 3412 SER A N     1 
ATOM   13047 C  CA    . SER A 1 2195 ? 149.294 125.108 162.208 1.00 119.82 ? 3412 SER A CA    1 
ATOM   13048 C  C     . SER A 1 2195 ? 148.830 123.655 162.129 1.00 121.14 ? 3412 SER A C     1 
ATOM   13049 O  O     . SER A 1 2195 ? 147.703 123.362 161.728 1.00 121.83 ? 3412 SER A O     1 
ATOM   13050 C  CB    . SER A 1 2195 ? 148.433 126.005 161.314 1.00 117.49 ? 3412 SER A CB    1 
ATOM   13051 O  OG    . SER A 1 2195 ? 148.535 127.363 161.707 1.00 117.01 ? 3412 SER A OG    1 
ATOM   13052 N  N     . HIS A 1 2196 ? 149.712 122.736 162.514 1.00 122.75 ? 3413 HIS A N     1 
ATOM   13053 C  CA    . HIS A 1 2196 ? 149.393 121.315 162.527 1.00 123.26 ? 3413 HIS A CA    1 
ATOM   13054 C  C     . HIS A 1 2196 ? 148.840 120.877 163.878 1.00 123.22 ? 3413 HIS A C     1 
ATOM   13055 O  O     . HIS A 1 2196 ? 147.947 120.023 163.940 1.00 122.21 ? 3413 HIS A O     1 
ATOM   13056 C  CB    . HIS A 1 2196 ? 150.642 120.505 162.169 1.00 123.05 ? 3413 HIS A CB    1 
ATOM   13057 C  CG    . HIS A 1 2196 ? 150.410 119.029 162.096 1.00 124.11 ? 3413 HIS A CG    1 
ATOM   13058 N  ND1   . HIS A 1 2196 ? 149.739 118.435 161.049 1.00 122.73 ? 3413 HIS A ND1   1 
ATOM   13059 C  CD2   . HIS A 1 2196 ? 150.765 118.026 162.933 1.00 124.76 ? 3413 HIS A CD2   1 
ATOM   13060 C  CE1   . HIS A 1 2196 ? 149.689 117.130 161.245 1.00 123.28 ? 3413 HIS A CE1   1 
ATOM   13061 N  NE2   . HIS A 1 2196 ? 150.303 116.856 162.382 1.00 124.02 ? 3413 HIS A NE2   1 
ATOM   13062 N  N     . MET A 1 2197 ? 149.360 121.463 164.963 1.00 124.28 ? 3414 MET A N     1 
ATOM   13063 C  CA    . MET A 1 2197 ? 148.880 121.139 166.304 1.00 125.27 ? 3414 MET A CA    1 
ATOM   13064 C  C     . MET A 1 2197 ? 147.431 121.569 166.499 1.00 125.62 ? 3414 MET A C     1 
ATOM   13065 O  O     . MET A 1 2197 ? 146.646 120.850 167.128 1.00 126.49 ? 3414 MET A O     1 
ATOM   13066 C  CB    . MET A 1 2197 ? 149.778 121.794 167.353 1.00 119.99 ? 3414 MET A CB    1 
ATOM   13067 C  CG    . MET A 1 2197 ? 151.180 121.209 167.437 1.00 121.37 ? 3414 MET A CG    1 
ATOM   13068 S  SD    . MET A 1 2197 ? 151.335 119.941 168.710 1.00 122.34 ? 3414 MET A SD    1 
ATOM   13069 C  CE    . MET A 1 2197 ? 153.114 119.879 168.912 1.00 94.29  ? 3414 MET A CE    1 
ATOM   13070 N  N     . ILE A 1 2198 ? 147.058 122.740 165.975 1.00 123.36 ? 3415 ILE A N     1 
ATOM   13071 C  CA    . ILE A 1 2198 ? 145.676 123.201 166.091 1.00 120.77 ? 3415 ILE A CA    1 
ATOM   13072 C  C     . ILE A 1 2198 ? 144.734 122.267 165.339 1.00 120.60 ? 3415 ILE A C     1 
ATOM   13073 O  O     . ILE A 1 2198 ? 143.654 121.922 165.834 1.00 119.25 ? 3415 ILE A O     1 
ATOM   13074 C  CB    . ILE A 1 2198 ? 145.553 124.663 165.613 1.00 118.49 ? 3415 ILE A CB    1 
ATOM   13075 C  CG1   . ILE A 1 2198 ? 144.087 125.107 165.588 1.00 117.88 ? 3415 ILE A CG1   1 
ATOM   13076 C  CG2   . ILE A 1 2198 ? 146.228 124.873 164.263 1.00 118.35 ? 3415 ILE A CG2   1 
ATOM   13077 C  CD1   . ILE A 1 2198 ? 143.908 126.585 165.347 1.00 110.43 ? 3415 ILE A CD1   1 
ATOM   13078 N  N     . THR A 1 2199 ? 145.139 121.816 164.148 1.00 123.28 ? 3416 THR A N     1 
ATOM   13079 C  CA    . THR A 1 2199 ? 144.312 120.886 163.387 1.00 127.57 ? 3416 THR A CA    1 
ATOM   13080 C  C     . THR A 1 2199 ? 144.183 119.543 164.097 1.00 126.90 ? 3416 THR A C     1 
ATOM   13081 O  O     . THR A 1 2199 ? 143.086 118.971 164.159 1.00 125.40 ? 3416 THR A O     1 
ATOM   13082 C  CB    . THR A 1 2199 ? 144.887 120.694 161.984 1.00 128.67 ? 3416 THR A CB    1 
ATOM   13083 O  OG1   . THR A 1 2199 ? 146.278 120.366 162.078 1.00 125.21 ? 3416 THR A OG1   1 
ATOM   13084 C  CG2   . THR A 1 2199 ? 144.725 121.966 161.165 1.00 126.79 ? 3416 THR A CG2   1 
ATOM   13085 N  N     . VAL A 1 2200 ? 145.288 119.025 164.646 1.00 126.41 ? 3417 VAL A N     1 
ATOM   13086 C  CA    . VAL A 1 2200 ? 145.221 117.721 165.300 1.00 124.93 ? 3417 VAL A CA    1 
ATOM   13087 C  C     . VAL A 1 2200 ? 144.408 117.799 166.591 1.00 124.83 ? 3417 VAL A C     1 
ATOM   13088 O  O     . VAL A 1 2200 ? 143.663 116.866 166.912 1.00 126.11 ? 3417 VAL A O     1 
ATOM   13089 C  CB    . VAL A 1 2200 ? 146.634 117.132 165.514 1.00 122.64 ? 3417 VAL A CB    1 
ATOM   13090 C  CG1   . VAL A 1 2200 ? 147.376 117.783 166.669 1.00 117.26 ? 3417 VAL A CG1   1 
ATOM   13091 C  CG2   . VAL A 1 2200 ? 146.552 115.629 165.729 1.00 128.20 ? 3417 VAL A CG2   1 
ATOM   13092 N  N     . ILE A 1 2201 ? 144.477 118.915 167.322 1.00 123.70 ? 3418 ILE A N     1 
ATOM   13093 C  CA    . ILE A 1 2201 ? 143.683 119.004 168.543 1.00 122.65 ? 3418 ILE A CA    1 
ATOM   13094 C  C     . ILE A 1 2201 ? 142.215 119.279 168.219 1.00 122.70 ? 3418 ILE A C     1 
ATOM   13095 O  O     . ILE A 1 2201 ? 141.325 118.831 168.951 1.00 123.12 ? 3418 ILE A O     1 
ATOM   13096 C  CB    . ILE A 1 2201 ? 144.278 120.046 169.512 1.00 119.35 ? 3418 ILE A CB    1 
ATOM   13097 C  CG1   . ILE A 1 2201 ? 143.696 119.865 170.915 1.00 113.57 ? 3418 ILE A CG1   1 
ATOM   13098 C  CG2   . ILE A 1 2201 ? 144.058 121.467 169.023 1.00 114.84 ? 3418 ILE A CG2   1 
ATOM   13099 C  CD1   . ILE A 1 2201 ? 144.007 118.520 171.532 1.00 114.06 ? 3418 ILE A CD1   1 
ATOM   13100 N  N     . SER A 1 2202 ? 141.929 119.973 167.111 1.00 121.89 ? 3419 SER A N     1 
ATOM   13101 C  CA    . SER A 1 2202 ? 140.544 120.131 166.680 1.00 122.39 ? 3419 SER A CA    1 
ATOM   13102 C  C     . SER A 1 2202 ? 139.945 118.793 166.269 1.00 124.52 ? 3419 SER A C     1 
ATOM   13103 O  O     . SER A 1 2202 ? 138.786 118.503 166.588 1.00 123.17 ? 3419 SER A O     1 
ATOM   13104 C  CB    . SER A 1 2202 ? 140.462 121.135 165.531 1.00 122.10 ? 3419 SER A CB    1 
ATOM   13105 O  OG    . SER A 1 2202 ? 140.865 122.426 165.953 1.00 122.34 ? 3419 SER A OG    1 
ATOM   13106 N  N     . ASN A 1 2203 ? 140.721 117.966 165.564 1.00 126.26 ? 3420 ASN A N     1 
ATOM   13107 C  CA    . ASN A 1 2203 ? 140.254 116.627 165.218 1.00 126.90 ? 3420 ASN A CA    1 
ATOM   13108 C  C     . ASN A 1 2203 ? 140.077 115.764 166.463 1.00 126.43 ? 3420 ASN A C     1 
ATOM   13109 O  O     . ASN A 1 2203 ? 139.137 114.964 166.540 1.00 127.17 ? 3420 ASN A O     1 
ATOM   13110 C  CB    . ASN A 1 2203 ? 141.224 115.966 164.240 1.00 129.58 ? 3420 ASN A CB    1 
ATOM   13111 C  CG    . ASN A 1 2203 ? 140.552 114.921 163.370 1.00 129.78 ? 3420 ASN A CG    1 
ATOM   13112 O  OD1   . ASN A 1 2203 ? 139.393 114.569 163.587 1.00 127.83 ? 3420 ASN A OD1   1 
ATOM   13113 N  ND2   . ASN A 1 2203 ? 141.279 114.420 162.379 1.00 130.84 ? 3420 ASN A ND2   1 
ATOM   13114 N  N     . TYR A 1 2204 ? 140.977 115.904 167.440 1.00 125.52 ? 3421 TYR A N     1 
ATOM   13115 C  CA    . TYR A 1 2204 ? 140.866 115.136 168.676 1.00 125.16 ? 3421 TYR A CA    1 
ATOM   13116 C  C     . TYR A 1 2204 ? 139.625 115.525 169.472 1.00 125.20 ? 3421 TYR A C     1 
ATOM   13117 O  O     . TYR A 1 2204 ? 138.938 114.656 170.022 1.00 122.94 ? 3421 TYR A O     1 
ATOM   13118 C  CB    . TYR A 1 2204 ? 142.127 115.326 169.520 1.00 123.48 ? 3421 TYR A CB    1 
ATOM   13119 C  CG    . TYR A 1 2204 ? 142.167 114.489 170.780 1.00 122.47 ? 3421 TYR A CG    1 
ATOM   13120 C  CD1   . TYR A 1 2204 ? 142.572 113.161 170.742 1.00 121.39 ? 3421 TYR A CD1   1 
ATOM   13121 C  CD2   . TYR A 1 2204 ? 141.813 115.031 172.010 1.00 119.54 ? 3421 TYR A CD2   1 
ATOM   13122 C  CE1   . TYR A 1 2204 ? 142.614 112.393 171.891 1.00 118.70 ? 3421 TYR A CE1   1 
ATOM   13123 C  CE2   . TYR A 1 2204 ? 141.852 114.272 173.164 1.00 116.71 ? 3421 TYR A CE2   1 
ATOM   13124 C  CZ    . TYR A 1 2204 ? 142.253 112.954 173.099 1.00 116.07 ? 3421 TYR A CZ    1 
ATOM   13125 O  OH    . TYR A 1 2204 ? 142.294 112.194 174.245 1.00 112.22 ? 3421 TYR A OH    1 
ATOM   13126 N  N     . TYR A 1 2205 ? 139.320 116.821 169.549 1.00 123.70 ? 3422 TYR A N     1 
ATOM   13127 C  CA    . TYR A 1 2205 ? 138.210 117.282 170.373 1.00 122.42 ? 3422 TYR A CA    1 
ATOM   13128 C  C     . TYR A 1 2205 ? 136.873 117.286 169.645 1.00 123.69 ? 3422 TYR A C     1 
ATOM   13129 O  O     . TYR A 1 2205 ? 135.830 117.375 170.304 1.00 123.70 ? 3422 TYR A O     1 
ATOM   13130 C  CB    . TYR A 1 2205 ? 138.503 118.685 170.912 1.00 118.69 ? 3422 TYR A CB    1 
ATOM   13131 C  CG    . TYR A 1 2205 ? 139.313 118.675 172.188 1.00 119.02 ? 3422 TYR A CG    1 
ATOM   13132 C  CD1   . TYR A 1 2205 ? 139.012 117.789 173.215 1.00 119.56 ? 3422 TYR A CD1   1 
ATOM   13133 C  CD2   . TYR A 1 2205 ? 140.381 119.545 172.363 1.00 116.96 ? 3422 TYR A CD2   1 
ATOM   13134 C  CE1   . TYR A 1 2205 ? 139.750 117.772 174.383 1.00 116.20 ? 3422 TYR A CE1   1 
ATOM   13135 C  CE2   . TYR A 1 2205 ? 141.125 119.535 173.528 1.00 114.21 ? 3422 TYR A CE2   1 
ATOM   13136 C  CZ    . TYR A 1 2205 ? 140.805 118.647 174.534 1.00 113.88 ? 3422 TYR A CZ    1 
ATOM   13137 O  OH    . TYR A 1 2205 ? 141.543 118.634 175.694 1.00 110.03 ? 3422 TYR A OH    1 
ATOM   13138 N  N     . GLY A 1 2206 ? 136.873 117.182 168.319 1.00 123.51 ? 3423 GLY A N     1 
ATOM   13139 C  CA    . GLY A 1 2206 ? 135.613 117.117 167.593 1.00 122.04 ? 3423 GLY A CA    1 
ATOM   13140 C  C     . GLY A 1 2206 ? 134.887 118.449 167.606 1.00 120.79 ? 3423 GLY A C     1 
ATOM   13141 O  O     . GLY A 1 2206 ? 135.456 119.499 167.289 1.00 119.61 ? 3423 GLY A O     1 
ATOM   13142 N  N     . ASN A 1 2207 ? 133.607 118.408 167.980 1.00 121.11 ? 3424 ASN A N     1 
ATOM   13143 C  CA    . ASN A 1 2207 ? 132.754 119.589 167.963 1.00 122.07 ? 3424 ASN A CA    1 
ATOM   13144 C  C     . ASN A 1 2207 ? 132.984 120.520 169.147 1.00 118.24 ? 3424 ASN A C     1 
ATOM   13145 O  O     . ASN A 1 2207 ? 132.470 121.643 169.135 1.00 115.26 ? 3424 ASN A O     1 
ATOM   13146 C  CB    . ASN A 1 2207 ? 131.282 119.169 167.929 1.00 122.21 ? 3424 ASN A CB    1 
ATOM   13147 C  CG    . ASN A 1 2207 ? 130.888 118.336 169.133 1.00 122.92 ? 3424 ASN A CG    1 
ATOM   13148 O  OD1   . ASN A 1 2207 ? 131.723 117.663 169.737 1.00 123.81 ? 3424 ASN A OD1   1 
ATOM   13149 N  ND2   . ASN A 1 2207 ? 129.610 118.379 169.490 1.00 119.82 ? 3424 ASN A ND2   1 
ATOM   13150 N  N     . LYS A 1 2208 ? 133.735 120.089 170.160 1.00 118.12 ? 3425 LYS A N     1 
ATOM   13151 C  CA    . LYS A 1 2208 ? 133.941 120.905 171.350 1.00 116.66 ? 3425 LYS A CA    1 
ATOM   13152 C  C     . LYS A 1 2208 ? 134.987 121.995 171.156 1.00 109.78 ? 3425 LYS A C     1 
ATOM   13153 O  O     . LYS A 1 2208 ? 135.153 122.833 172.048 1.00 105.07 ? 3425 LYS A O     1 
ATOM   13154 C  CB    . LYS A 1 2208 ? 134.339 120.017 172.531 1.00 117.90 ? 3425 LYS A CB    1 
ATOM   13155 C  CG    . LYS A 1 2208 ? 133.338 118.917 172.840 1.00 116.92 ? 3425 LYS A CG    1 
ATOM   13156 C  CD    . LYS A 1 2208 ? 133.664 118.226 174.153 1.00 117.50 ? 3425 LYS A CD    1 
ATOM   13157 C  CE    . LYS A 1 2208 ? 133.480 119.171 175.329 1.00 119.53 ? 3425 LYS A CE    1 
ATOM   13158 N  NZ    . LYS A 1 2208 ? 132.200 119.926 175.241 1.00 116.49 ? 3425 LYS A NZ    1 
ATOM   13159 N  N     . THR A 1 2209 ? 135.688 122.007 170.025 1.00 110.75 ? 3426 THR A N     1 
ATOM   13160 C  CA    . THR A 1 2209 ? 136.723 123.002 169.774 1.00 105.67 ? 3426 THR A CA    1 
ATOM   13161 C  C     . THR A 1 2209 ? 136.080 124.349 169.465 1.00 99.31  ? 3426 THR A C     1 
ATOM   13162 O  O     . THR A 1 2209 ? 135.284 124.465 168.528 1.00 102.73 ? 3426 THR A O     1 
ATOM   13163 C  CB    . THR A 1 2209 ? 137.617 122.558 168.618 1.00 109.68 ? 3426 THR A CB    1 
ATOM   13164 O  OG1   . THR A 1 2209 ? 138.424 121.449 169.032 1.00 114.57 ? 3426 THR A OG1   1 
ATOM   13165 C  CG2   . THR A 1 2209 ? 138.520 123.698 168.167 1.00 101.12 ? 3426 THR A CG2   1 
ATOM   13166 N  N     . VAL A 1 2210 ? 136.422 125.363 170.254 1.00 94.09  ? 3427 VAL A N     1 
ATOM   13167 C  CA    . VAL A 1 2210 ? 135.977 126.733 170.028 1.00 93.21  ? 3427 VAL A CA    1 
ATOM   13168 C  C     . VAL A 1 2210 ? 137.227 127.576 169.820 1.00 91.73  ? 3427 VAL A C     1 
ATOM   13169 O  O     . VAL A 1 2210 ? 137.981 127.826 170.768 1.00 93.11  ? 3427 VAL A O     1 
ATOM   13170 C  CB    . VAL A 1 2210 ? 135.134 127.267 171.194 1.00 92.39  ? 3427 VAL A CB    1 
ATOM   13171 C  CG1   . VAL A 1 2210 ? 134.742 128.713 170.945 1.00 90.34  ? 3427 VAL A CG1   1 
ATOM   13172 C  CG2   . VAL A 1 2210 ? 133.899 126.404 171.392 1.00 95.50  ? 3427 VAL A CG2   1 
ATOM   13173 N  N     . LEU A 1 2211 ? 137.445 128.019 168.587 1.00 90.33  ? 3428 LEU A N     1 
ATOM   13174 C  CA    . LEU A 1 2211 ? 138.680 128.687 168.201 1.00 89.62  ? 3428 LEU A CA    1 
ATOM   13175 C  C     . LEU A 1 2211 ? 138.512 130.198 168.278 1.00 90.21  ? 3428 LEU A C     1 
ATOM   13176 O  O     . LEU A 1 2211 ? 137.527 130.745 167.771 1.00 96.26  ? 3428 LEU A O     1 
ATOM   13177 C  CB    . LEU A 1 2211 ? 139.095 128.277 166.788 1.00 95.12  ? 3428 LEU A CB    1 
ATOM   13178 C  CG    . LEU A 1 2211 ? 140.357 128.950 166.252 1.00 94.50  ? 3428 LEU A CG    1 
ATOM   13179 C  CD1   . LEU A 1 2211 ? 141.516 128.686 167.190 1.00 93.88  ? 3428 LEU A CD1   1 
ATOM   13180 C  CD2   . LEU A 1 2211 ? 140.674 128.467 164.848 1.00 95.35  ? 3428 LEU A CD2   1 
ATOM   13181 N  N     . LEU A 1 2212 ? 139.473 130.866 168.915 1.00 86.53  ? 3429 LEU A N     1 
ATOM   13182 C  CA    . LEU A 1 2212 ? 139.496 132.323 168.956 1.00 87.63  ? 3429 LEU A CA    1 
ATOM   13183 C  C     . LEU A 1 2212 ? 140.859 132.859 168.544 1.00 88.22  ? 3429 LEU A C     1 
ATOM   13184 O  O     . LEU A 1 2212 ? 141.721 132.103 168.085 1.00 89.04  ? 3429 LEU A O     1 
ATOM   13185 C  CB    . LEU A 1 2212 ? 139.139 132.848 170.348 1.00 88.29  ? 3429 LEU A CB    1 
ATOM   13186 C  CG    . LEU A 1 2212 ? 137.667 132.924 170.758 1.00 97.61  ? 3429 LEU A CG    1 
ATOM   13187 C  CD1   . LEU A 1 2212 ? 137.099 131.569 171.150 1.00 92.76  ? 3429 LEU A CD1   1 
ATOM   13188 C  CD2   . LEU A 1 2212 ? 137.499 133.930 171.876 1.00 106.97 ? 3429 LEU A CD2   1 
ATOM   13189 N  N     . SER A 1 2213 ? 141.057 134.165 168.704 1.00 88.13  ? 3430 SER A N     1 
ATOM   13190 C  CA    . SER A 1 2213 ? 142.317 134.811 168.364 1.00 90.15  ? 3430 SER A CA    1 
ATOM   13191 C  C     . SER A 1 2213 ? 142.405 136.124 169.125 1.00 93.57  ? 3430 SER A C     1 
ATOM   13192 O  O     . SER A 1 2213 ? 141.415 136.609 169.678 1.00 97.83  ? 3430 SER A O     1 
ATOM   13193 C  CB    . SER A 1 2213 ? 142.443 135.057 166.856 1.00 91.83  ? 3430 SER A CB    1 
ATOM   13194 O  OG    . SER A 1 2213 ? 142.440 133.841 166.129 1.00 95.51  ? 3430 SER A OG    1 
ATOM   13195 N  N     . PHE A 1 2214 ? 143.608 136.689 169.152 1.00 97.28  ? 3431 PHE A N     1 
ATOM   13196 C  CA    . PHE A 1 2214 ? 143.813 138.007 169.740 1.00 100.82 ? 3431 PHE A CA    1 
ATOM   13197 C  C     . PHE A 1 2214 ? 143.676 139.094 168.680 1.00 96.28  ? 3431 PHE A C     1 
ATOM   13198 O  O     . PHE A 1 2214 ? 144.671 139.584 168.148 1.00 95.81  ? 3431 PHE A O     1 
ATOM   13199 C  CB    . PHE A 1 2214 ? 145.184 138.104 170.412 1.00 104.60 ? 3431 PHE A CB    1 
ATOM   13200 C  CG    . PHE A 1 2214 ? 145.227 137.527 171.800 1.00 104.70 ? 3431 PHE A CG    1 
ATOM   13201 C  CD1   . PHE A 1 2214 ? 144.569 138.156 172.844 1.00 104.52 ? 3431 PHE A CD1   1 
ATOM   13202 C  CD2   . PHE A 1 2214 ? 145.949 136.376 172.067 1.00 102.97 ? 3431 PHE A CD2   1 
ATOM   13203 C  CE1   . PHE A 1 2214 ? 144.613 137.637 174.124 1.00 107.28 ? 3431 PHE A CE1   1 
ATOM   13204 C  CE2   . PHE A 1 2214 ? 146.001 135.854 173.346 1.00 102.28 ? 3431 PHE A CE2   1 
ATOM   13205 C  CZ    . PHE A 1 2214 ? 145.331 136.484 174.375 1.00 106.43 ? 3431 PHE A CZ    1 
ATOM   13206 N  N     . GLY A 1 2218 ? 133.313 141.030 170.415 1.00 117.40 ? 3435 GLY A N     1 
ATOM   13207 C  CA    . GLY A 1 2218 ? 132.715 140.306 171.521 1.00 120.85 ? 3435 GLY A CA    1 
ATOM   13208 C  C     . GLY A 1 2218 ? 133.455 139.029 171.867 1.00 124.03 ? 3435 GLY A C     1 
ATOM   13209 O  O     . GLY A 1 2218 ? 132.842 138.026 172.242 1.00 124.88 ? 3435 GLY A O     1 
ATOM   13210 N  N     . PHE A 1 2219 ? 134.784 139.066 171.735 1.00 125.12 ? 3436 PHE A N     1 
ATOM   13211 C  CA    . PHE A 1 2219 ? 135.586 137.887 172.049 1.00 123.07 ? 3436 PHE A CA    1 
ATOM   13212 C  C     . PHE A 1 2219 ? 135.575 137.595 173.545 1.00 119.56 ? 3436 PHE A C     1 
ATOM   13213 O  O     . PHE A 1 2219 ? 135.568 136.429 173.951 1.00 114.37 ? 3436 PHE A O     1 
ATOM   13214 C  CB    . PHE A 1 2219 ? 137.015 138.053 171.522 1.00 123.32 ? 3436 PHE A CB    1 
ATOM   13215 C  CG    . PHE A 1 2219 ? 137.815 139.121 172.218 1.00 124.84 ? 3436 PHE A CG    1 
ATOM   13216 C  CD1   . PHE A 1 2219 ? 137.630 140.461 171.914 1.00 123.67 ? 3436 PHE A CD1   1 
ATOM   13217 C  CD2   . PHE A 1 2219 ? 138.773 138.780 173.158 1.00 122.84 ? 3436 PHE A CD2   1 
ATOM   13218 C  CE1   . PHE A 1 2219 ? 138.370 141.439 172.548 1.00 123.29 ? 3436 PHE A CE1   1 
ATOM   13219 C  CE2   . PHE A 1 2219 ? 139.518 139.753 173.794 1.00 124.95 ? 3436 PHE A CE2   1 
ATOM   13220 C  CZ    . PHE A 1 2219 ? 139.315 141.084 173.488 1.00 126.27 ? 3436 PHE A CZ    1 
ATOM   13221 N  N     . VAL A 1 2220 ? 135.542 138.638 174.379 1.00 122.36 ? 3437 VAL A N     1 
ATOM   13222 C  CA    . VAL A 1 2220 ? 135.410 138.434 175.820 1.00 122.66 ? 3437 VAL A CA    1 
ATOM   13223 C  C     . VAL A 1 2220 ? 134.061 137.806 176.147 1.00 121.74 ? 3437 VAL A C     1 
ATOM   13224 O  O     . VAL A 1 2220 ? 133.964 136.905 176.991 1.00 119.87 ? 3437 VAL A O     1 
ATOM   13225 C  CB    . VAL A 1 2220 ? 135.613 139.763 176.571 1.00 122.69 ? 3437 VAL A CB    1 
ATOM   13226 C  CG1   . VAL A 1 2220 ? 135.604 139.534 178.074 1.00 125.35 ? 3437 VAL A CG1   1 
ATOM   13227 C  CG2   . VAL A 1 2220 ? 136.908 140.427 176.138 1.00 119.85 ? 3437 VAL A CG2   1 
ATOM   13228 N  N     . LYS A 1 2221 ? 132.998 138.269 175.482 1.00 123.15 ? 3438 LYS A N     1 
ATOM   13229 C  CA    . LYS A 1 2221 ? 131.668 137.714 175.719 1.00 122.55 ? 3438 LYS A CA    1 
ATOM   13230 C  C     . LYS A 1 2221 ? 131.582 136.255 175.287 1.00 121.52 ? 3438 LYS A C     1 
ATOM   13231 O  O     . LYS A 1 2221 ? 130.994 135.428 175.995 1.00 122.45 ? 3438 LYS A O     1 
ATOM   13232 C  CB    . LYS A 1 2221 ? 130.613 138.551 174.997 1.00 122.56 ? 3438 LYS A CB    1 
ATOM   13233 C  CG    . LYS A 1 2221 ? 130.574 140.008 175.429 1.00 123.99 ? 3438 LYS A CG    1 
ATOM   13234 C  CD    . LYS A 1 2221 ? 130.247 140.135 176.910 1.00 122.92 ? 3438 LYS A CD    1 
ATOM   13235 C  CE    . LYS A 1 2221 ? 128.848 139.623 177.219 1.00 120.84 ? 3438 LYS A CE    1 
ATOM   13236 N  NZ    . LYS A 1 2221 ? 127.795 140.459 176.583 1.00 119.28 ? 3438 LYS A NZ    1 
ATOM   13237 N  N     . ARG A 1 2222 ? 132.162 135.911 174.133 1.00 120.14 ? 3439 ARG A N     1 
ATOM   13238 C  CA    . ARG A 1 2222 ? 132.117 134.516 173.706 1.00 117.27 ? 3439 ARG A CA    1 
ATOM   13239 C  C     . ARG A 1 2222 ? 133.033 133.643 174.558 1.00 117.45 ? 3439 ARG A C     1 
ATOM   13240 O  O     . ARG A 1 2222 ? 132.732 132.463 174.767 1.00 116.70 ? 3439 ARG A O     1 
ATOM   13241 C  CB    . ARG A 1 2222 ? 132.456 134.391 172.217 1.00 115.79 ? 3439 ARG A CB    1 
ATOM   13242 C  CG    . ARG A 1 2222 ? 133.903 134.639 171.846 1.00 113.93 ? 3439 ARG A CG    1 
ATOM   13243 C  CD    . ARG A 1 2222 ? 134.090 134.673 170.335 1.00 113.47 ? 3439 ARG A CD    1 
ATOM   13244 N  NE    . ARG A 1 2222 ? 133.466 135.842 169.727 1.00 116.49 ? 3439 ARG A NE    1 
ATOM   13245 C  CZ    . ARG A 1 2222 ? 134.119 136.763 169.031 1.00 118.41 ? 3439 ARG A CZ    1 
ATOM   13246 N  NH1   . ARG A 1 2222 ? 135.423 136.680 168.826 1.00 119.99 ? 3439 ARG A NH1   1 
ATOM   13247 N  NH2   . ARG A 1 2222 ? 133.445 137.793 168.527 1.00 114.20 ? 3439 ARG A NH2   1 
ATOM   13248 N  N     . LEU A 1 2223 ? 134.124 134.206 175.090 1.00 118.04 ? 3440 LEU A N     1 
ATOM   13249 C  CA    . LEU A 1 2223 ? 134.932 133.484 176.067 1.00 118.43 ? 3440 LEU A CA    1 
ATOM   13250 C  C     . LEU A 1 2223 ? 134.135 133.189 177.329 1.00 117.56 ? 3440 LEU A C     1 
ATOM   13251 O  O     . LEU A 1 2223 ? 134.199 132.078 177.867 1.00 116.17 ? 3440 LEU A O     1 
ATOM   13252 C  CB    . LEU A 1 2223 ? 136.186 134.289 176.411 1.00 117.40 ? 3440 LEU A CB    1 
ATOM   13253 C  CG    . LEU A 1 2223 ? 137.408 134.113 175.514 1.00 114.47 ? 3440 LEU A CG    1 
ATOM   13254 C  CD1   . LEU A 1 2223 ? 138.423 135.214 175.761 1.00 112.75 ? 3440 LEU A CD1   1 
ATOM   13255 C  CD2   . LEU A 1 2223 ? 138.035 132.751 175.744 1.00 106.95 ? 3440 LEU A CD2   1 
ATOM   13256 N  N     . GLU A 1 2224 ? 133.376 134.176 177.813 1.00 116.96 ? 3441 GLU A N     1 
ATOM   13257 C  CA    . GLU A 1 2224 ? 132.550 133.969 178.999 1.00 115.56 ? 3441 GLU A CA    1 
ATOM   13258 C  C     . GLU A 1 2224 ? 131.467 132.928 178.741 1.00 116.74 ? 3441 GLU A C     1 
ATOM   13259 O  O     . GLU A 1 2224 ? 131.195 132.076 179.597 1.00 116.55 ? 3441 GLU A O     1 
ATOM   13260 C  CB    . GLU A 1 2224 ? 131.932 135.296 179.439 1.00 118.45 ? 3441 GLU A CB    1 
ATOM   13261 C  CG    . GLU A 1 2224 ? 130.913 135.175 180.561 1.00 123.17 ? 3441 GLU A CG    1 
ATOM   13262 C  CD    . GLU A 1 2224 ? 130.258 136.499 180.900 1.00 124.47 ? 3441 GLU A CD    1 
ATOM   13263 O  OE1   . GLU A 1 2224 ? 130.267 137.406 180.041 1.00 121.62 ? 3441 GLU A OE1   1 
ATOM   13264 O  OE2   . GLU A 1 2224 ? 129.731 136.633 182.024 1.00 125.93 ? 3441 GLU A OE2   1 
ATOM   13265 N  N     . ASN A 1 2225 ? 130.845 132.977 177.559 1.00 119.02 ? 3442 ASN A N     1 
ATOM   13266 C  CA    . ASN A 1 2225 ? 129.822 131.994 177.213 1.00 119.78 ? 3442 ASN A CA    1 
ATOM   13267 C  C     . ASN A 1 2225 ? 130.408 130.591 177.114 1.00 118.38 ? 3442 ASN A C     1 
ATOM   13268 O  O     . ASN A 1 2225 ? 129.796 129.621 177.579 1.00 117.35 ? 3442 ASN A O     1 
ATOM   13269 C  CB    . ASN A 1 2225 ? 129.141 132.386 175.903 1.00 120.62 ? 3442 ASN A CB    1 
ATOM   13270 C  CG    . ASN A 1 2225 ? 128.379 133.692 176.010 1.00 121.47 ? 3442 ASN A CG    1 
ATOM   13271 O  OD1   . ASN A 1 2225 ? 127.783 133.993 177.045 1.00 121.24 ? 3442 ASN A OD1   1 
ATOM   13272 N  ND2   . ASN A 1 2225 ? 128.398 134.478 174.940 1.00 120.43 ? 3442 ASN A ND2   1 
ATOM   13273 N  N     . ALA A 1 2226 ? 131.596 130.462 176.518 1.00 118.51 ? 3443 ALA A N     1 
ATOM   13274 C  CA    . ALA A 1 2226 ? 132.241 129.157 176.419 1.00 117.38 ? 3443 ALA A CA    1 
ATOM   13275 C  C     . ALA A 1 2226 ? 132.660 128.637 177.789 1.00 117.88 ? 3443 ALA A C     1 
ATOM   13276 O  O     . ALA A 1 2226 ? 132.594 127.430 178.044 1.00 117.16 ? 3443 ALA A O     1 
ATOM   13277 C  CB    . ALA A 1 2226 ? 133.445 129.238 175.483 1.00 114.05 ? 3443 ALA A CB    1 
ATOM   13278 N  N     . VAL A 1 2227 ? 133.106 129.530 178.677 1.00 119.16 ? 3444 VAL A N     1 
ATOM   13279 C  CA    . VAL A 1 2227 ? 133.454 129.126 180.036 1.00 119.24 ? 3444 VAL A CA    1 
ATOM   13280 C  C     . VAL A 1 2227 ? 132.217 128.638 180.780 1.00 119.67 ? 3444 VAL A C     1 
ATOM   13281 O  O     . VAL A 1 2227 ? 132.252 127.610 181.469 1.00 119.25 ? 3444 VAL A O     1 
ATOM   13282 C  CB    . VAL A 1 2227 ? 134.148 130.289 180.774 1.00 117.59 ? 3444 VAL A CB    1 
ATOM   13283 C  CG1   . VAL A 1 2227 ? 134.078 130.104 182.283 1.00 116.66 ? 3444 VAL A CG1   1 
ATOM   13284 C  CG2   . VAL A 1 2227 ? 135.593 130.412 180.323 1.00 114.36 ? 3444 VAL A CG2   1 
ATOM   13285 N  N     . ARG A 1 2228 ? 131.099 129.357 180.639 1.00 119.94 ? 3445 ARG A N     1 
ATOM   13286 C  CA    . ARG A 1 2228 ? 129.861 128.950 181.296 1.00 120.65 ? 3445 ARG A CA    1 
ATOM   13287 C  C     . ARG A 1 2228 ? 129.347 127.623 180.748 1.00 121.93 ? 3445 ARG A C     1 
ATOM   13288 O  O     . ARG A 1 2228 ? 128.840 126.787 181.506 1.00 123.47 ? 3445 ARG A O     1 
ATOM   13289 C  CB    . ARG A 1 2228 ? 128.801 130.040 181.141 1.00 120.60 ? 3445 ARG A CB    1 
ATOM   13290 C  CG    . ARG A 1 2228 ? 128.548 130.844 182.406 1.00 123.06 ? 3445 ARG A CG    1 
ATOM   13291 C  CD    . ARG A 1 2228 ? 127.238 131.610 182.321 1.00 122.21 ? 3445 ARG A CD    1 
ATOM   13292 N  NE    . ARG A 1 2228 ? 127.216 132.538 181.197 1.00 121.76 ? 3445 ARG A NE    1 
ATOM   13293 C  CZ    . ARG A 1 2228 ? 127.652 133.789 181.251 1.00 121.36 ? 3445 ARG A CZ    1 
ATOM   13294 N  NH1   . ARG A 1 2228 ? 128.157 134.298 182.363 1.00 120.01 ? 3445 ARG A NH1   1 
ATOM   13295 N  NH2   . ARG A 1 2228 ? 127.580 134.549 180.161 1.00 120.14 ? 3445 ARG A NH2   1 
ATOM   13296 N  N     . PHE A 1 2229 ? 129.462 127.413 179.434 1.00 121.00 ? 3446 PHE A N     1 
ATOM   13297 C  CA    . PHE A 1 2229 ? 128.991 126.166 178.840 1.00 119.06 ? 3446 PHE A CA    1 
ATOM   13298 C  C     . PHE A 1 2229 ? 129.891 124.992 179.213 1.00 117.66 ? 3446 PHE A C     1 
ATOM   13299 O  O     . PHE A 1 2229 ? 129.399 123.894 179.500 1.00 116.62 ? 3446 PHE A O     1 
ATOM   13300 C  CB    . PHE A 1 2229 ? 128.901 126.310 177.321 1.00 116.04 ? 3446 PHE A CB    1 
ATOM   13301 N  N     . GLY A 1 2230 ? 131.205 125.201 179.217 1.00 116.46 ? 3447 GLY A N     1 
ATOM   13302 C  CA    . GLY A 1 2230 ? 132.141 124.130 179.497 1.00 117.75 ? 3447 GLY A CA    1 
ATOM   13303 C  C     . GLY A 1 2230 ? 132.786 123.567 178.247 1.00 115.89 ? 3447 GLY A C     1 
ATOM   13304 O  O     . GLY A 1 2230 ? 132.919 122.348 178.106 1.00 114.73 ? 3447 GLY A O     1 
ATOM   13305 N  N     . SER A 1 2231 ? 133.192 124.443 177.332 1.00 113.41 ? 3448 SER A N     1 
ATOM   13306 C  CA    . SER A 1 2231 ? 133.754 124.044 176.051 1.00 110.40 ? 3448 SER A CA    1 
ATOM   13307 C  C     . SER A 1 2231 ? 135.233 124.405 175.975 1.00 108.60 ? 3448 SER A C     1 
ATOM   13308 O  O     . SER A 1 2231 ? 135.671 125.425 176.517 1.00 107.13 ? 3448 SER A O     1 
ATOM   13309 C  CB    . SER A 1 2231 ? 133.000 124.703 174.893 1.00 107.53 ? 3448 SER A CB    1 
ATOM   13310 O  OG    . SER A 1 2231 ? 131.614 124.411 174.957 1.00 104.14 ? 3448 SER A OG    1 
ATOM   13311 N  N     . VAL A 1 2232 ? 135.998 123.551 175.295 1.00 107.05 ? 3449 VAL A N     1 
ATOM   13312 C  CA    . VAL A 1 2232 ? 137.432 123.766 175.141 1.00 98.76  ? 3449 VAL A CA    1 
ATOM   13313 C  C     . VAL A 1 2232 ? 137.670 124.947 174.210 1.00 93.82  ? 3449 VAL A C     1 
ATOM   13314 O  O     . VAL A 1 2232 ? 137.088 125.028 173.120 1.00 98.72  ? 3449 VAL A O     1 
ATOM   13315 C  CB    . VAL A 1 2232 ? 138.110 122.490 174.617 1.00 101.00 ? 3449 VAL A CB    1 
ATOM   13316 C  CG1   . VAL A 1 2232 ? 139.511 122.788 174.098 1.00 95.81  ? 3449 VAL A CG1   1 
ATOM   13317 C  CG2   . VAL A 1 2232 ? 138.154 121.431 175.707 1.00 104.45 ? 3449 VAL A CG2   1 
ATOM   13318 N  N     . VAL A 1 2233 ? 138.527 125.872 174.636 1.00 90.11  ? 3450 VAL A N     1 
ATOM   13319 C  CA    . VAL A 1 2233 ? 138.809 127.096 173.896 1.00 89.24  ? 3450 VAL A CA    1 
ATOM   13320 C  C     . VAL A 1 2233 ? 140.282 127.109 173.517 1.00 82.51  ? 3450 VAL A C     1 
ATOM   13321 O  O     . VAL A 1 2233 ? 141.149 126.872 174.365 1.00 87.13  ? 3450 VAL A O     1 
ATOM   13322 C  CB    . VAL A 1 2233 ? 138.448 128.349 174.715 1.00 92.83  ? 3450 VAL A CB    1 
ATOM   13323 C  CG1   . VAL A 1 2233 ? 138.709 129.607 173.905 1.00 89.41  ? 3450 VAL A CG1   1 
ATOM   13324 C  CG2   . VAL A 1 2233 ? 136.999 128.288 175.164 1.00 97.76  ? 3450 VAL A CG2   1 
ATOM   13325 N  N     . ILE A 1 2234 ? 140.560 127.381 172.245 1.00 79.20  ? 3451 ILE A N     1 
ATOM   13326 C  CA    . ILE A 1 2234 ? 141.917 127.520 171.731 1.00 78.95  ? 3451 ILE A CA    1 
ATOM   13327 C  C     . ILE A 1 2234 ? 142.081 128.943 171.222 1.00 81.71  ? 3451 ILE A C     1 
ATOM   13328 O  O     . ILE A 1 2234 ? 141.252 129.426 170.443 1.00 90.63  ? 3451 ILE A O     1 
ATOM   13329 C  CB    . ILE A 1 2234 ? 142.208 126.503 170.614 1.00 81.25  ? 3451 ILE A CB    1 
ATOM   13330 C  CG1   . ILE A 1 2234 ? 141.975 125.080 171.120 1.00 83.27  ? 3451 ILE A CG1   1 
ATOM   13331 C  CG2   . ILE A 1 2234 ? 143.628 126.669 170.093 1.00 80.71  ? 3451 ILE A CG2   1 
ATOM   13332 C  CD1   . ILE A 1 2234 ? 141.707 124.087 170.024 1.00 88.49  ? 3451 ILE A CD1   1 
ATOM   13333 N  N     . ILE A 1 2235 ? 143.142 129.612 171.660 1.00 78.68  ? 3452 ILE A N     1 
ATOM   13334 C  CA    . ILE A 1 2235 ? 143.397 131.003 171.313 1.00 83.36  ? 3452 ILE A CA    1 
ATOM   13335 C  C     . ILE A 1 2235 ? 144.692 131.073 170.517 1.00 86.31  ? 3452 ILE A C     1 
ATOM   13336 O  O     . ILE A 1 2235 ? 145.736 130.594 170.977 1.00 88.51  ? 3452 ILE A O     1 
ATOM   13337 C  CB    . ILE A 1 2235 ? 143.476 131.898 172.565 1.00 82.55  ? 3452 ILE A CB    1 
ATOM   13338 C  CG1   . ILE A 1 2235 ? 142.159 131.859 173.343 1.00 84.43  ? 3452 ILE A CG1   1 
ATOM   13339 C  CG2   . ILE A 1 2235 ? 143.801 133.324 172.177 1.00 88.38  ? 3452 ILE A CG2   1 
ATOM   13340 C  CD1   . ILE A 1 2235 ? 142.178 130.940 174.546 1.00 87.32  ? 3452 ILE A CD1   1 
ATOM   13341 N  N     . GLN A 1 2236 ? 144.624 131.666 169.328 1.00 89.25  ? 3453 GLN A N     1 
ATOM   13342 C  CA    . GLN A 1 2236 ? 145.799 131.847 168.494 1.00 91.73  ? 3453 GLN A CA    1 
ATOM   13343 C  C     . GLN A 1 2236 ? 146.462 133.188 168.803 1.00 93.56  ? 3453 GLN A C     1 
ATOM   13344 O  O     . GLN A 1 2236 ? 146.067 133.907 169.725 1.00 93.70  ? 3453 GLN A O     1 
ATOM   13345 C  CB    . GLN A 1 2236 ? 145.430 131.752 167.015 1.00 94.65  ? 3453 GLN A CB    1 
ATOM   13346 C  CG    . GLN A 1 2236 ? 144.652 130.505 166.643 1.00 94.89  ? 3453 GLN A CG    1 
ATOM   13347 C  CD    . GLN A 1 2236 ? 143.879 130.668 165.349 1.00 94.27  ? 3453 GLN A CD    1 
ATOM   13348 O  OE1   . GLN A 1 2236 ? 142.747 131.150 165.347 1.00 92.39  ? 3453 GLN A OE1   1 
ATOM   13349 N  NE2   . GLN A 1 2236 ? 144.489 130.267 164.240 1.00 93.02  ? 3453 GLN A NE2   1 
ATOM   13350 N  N     . ASP A 1 2237 ? 147.484 133.522 168.008 1.00 97.58  ? 3454 ASP A N     1 
ATOM   13351 C  CA    . ASP A 1 2237 ? 148.249 134.767 168.126 1.00 102.64 ? 3454 ASP A CA    1 
ATOM   13352 C  C     . ASP A 1 2237 ? 148.820 134.935 169.536 1.00 104.88 ? 3454 ASP A C     1 
ATOM   13353 O  O     . ASP A 1 2237 ? 148.478 135.862 170.272 1.00 106.00 ? 3454 ASP A O     1 
ATOM   13354 C  CB    . ASP A 1 2237 ? 147.399 135.976 167.720 1.00 104.96 ? 3454 ASP A CB    1 
ATOM   13355 C  CG    . ASP A 1 2237 ? 148.223 137.086 167.096 1.00 108.73 ? 3454 ASP A CG    1 
ATOM   13356 O  OD1   . ASP A 1 2237 ? 149.337 137.353 167.592 1.00 111.31 ? 3454 ASP A OD1   1 
ATOM   13357 O  OD2   . ASP A 1 2237 ? 147.756 137.690 166.108 1.00 110.07 ? 3454 ASP A OD2   1 
ATOM   13358 N  N     . GLY A 1 2238 ? 149.709 134.006 169.900 1.00 104.38 ? 3455 GLY A N     1 
ATOM   13359 C  CA    . GLY A 1 2238 ? 150.256 133.995 171.246 1.00 104.09 ? 3455 GLY A CA    1 
ATOM   13360 C  C     . GLY A 1 2238 ? 151.126 135.195 171.562 1.00 109.73 ? 3455 GLY A C     1 
ATOM   13361 O  O     . GLY A 1 2238 ? 151.235 135.594 172.724 1.00 111.85 ? 3455 GLY A O     1 
ATOM   13362 N  N     . GLU A 1 2239 ? 151.746 135.792 170.543 1.00 112.31 ? 3456 GLU A N     1 
ATOM   13363 C  CA    . GLU A 1 2239 ? 152.580 136.970 170.753 1.00 116.16 ? 3456 GLU A CA    1 
ATOM   13364 C  C     . GLU A 1 2239 ? 151.776 138.210 171.127 1.00 115.97 ? 3456 GLU A C     1 
ATOM   13365 O  O     . GLU A 1 2239 ? 152.371 139.206 171.552 1.00 114.11 ? 3456 GLU A O     1 
ATOM   13366 C  CB    . GLU A 1 2239 ? 153.412 137.253 169.501 1.00 116.93 ? 3456 GLU A CB    1 
ATOM   13367 C  CG    . GLU A 1 2239 ? 154.300 136.096 169.072 1.00 118.25 ? 3456 GLU A CG    1 
ATOM   13368 C  CD    . GLU A 1 2239 ? 155.699 136.189 169.651 1.00 118.18 ? 3456 GLU A CD    1 
ATOM   13369 O  OE1   . GLU A 1 2239 ? 155.943 137.092 170.480 1.00 116.42 ? 3456 GLU A OE1   1 
ATOM   13370 O  OE2   . GLU A 1 2239 ? 156.555 135.361 169.275 1.00 116.77 ? 3456 GLU A OE2   1 
ATOM   13371 N  N     . PHE A 1 2240 ? 150.453 138.175 170.984 1.00 113.47 ? 3457 PHE A N     1 
ATOM   13372 C  CA    . PHE A 1 2240 ? 149.581 139.303 171.291 1.00 110.81 ? 3457 PHE A CA    1 
ATOM   13373 C  C     . PHE A 1 2240 ? 148.743 139.033 172.538 1.00 111.09 ? 3457 PHE A C     1 
ATOM   13374 O  O     . PHE A 1 2240 ? 147.559 139.370 172.595 1.00 112.60 ? 3457 PHE A O     1 
ATOM   13375 C  CB    . PHE A 1 2240 ? 148.685 139.628 170.098 1.00 108.27 ? 3457 PHE A CB    1 
ATOM   13376 C  CG    . PHE A 1 2240 ? 148.149 141.032 170.105 1.00 110.83 ? 3457 PHE A CG    1 
ATOM   13377 C  CD1   . PHE A 1 2240 ? 149.001 142.113 170.261 1.00 114.71 ? 3457 PHE A CD1   1 
ATOM   13378 C  CD2   . PHE A 1 2240 ? 146.792 141.270 169.953 1.00 109.00 ? 3457 PHE A CD2   1 
ATOM   13379 C  CE1   . PHE A 1 2240 ? 148.509 143.407 170.268 1.00 113.50 ? 3457 PHE A CE1   1 
ATOM   13380 C  CE2   . PHE A 1 2240 ? 146.294 142.560 169.959 1.00 111.65 ? 3457 PHE A CE2   1 
ATOM   13381 C  CZ    . PHE A 1 2240 ? 147.154 143.629 170.116 1.00 112.50 ? 3457 PHE A CZ    1 
ATOM   13382 N  N     . PHE A 1 2241 ? 149.347 138.409 173.545 1.00 109.76 ? 3458 PHE A N     1 
ATOM   13383 C  CA    . PHE A 1 2241 ? 148.661 138.120 174.801 1.00 108.40 ? 3458 PHE A CA    1 
ATOM   13384 C  C     . PHE A 1 2241 ? 148.289 139.398 175.547 1.00 110.67 ? 3458 PHE A C     1 
ATOM   13385 O  O     . PHE A 1 2241 ? 149.012 140.393 175.493 1.00 110.97 ? 3458 PHE A O     1 
ATOM   13386 C  CB    . PHE A 1 2241 ? 149.530 137.233 175.696 1.00 105.32 ? 3458 PHE A CB    1 
ATOM   13387 C  CG    . PHE A 1 2241 ? 148.876 136.858 176.995 1.00 105.88 ? 3458 PHE A CG    1 
ATOM   13388 C  CD1   . PHE A 1 2241 ? 147.761 136.035 177.014 1.00 103.34 ? 3458 PHE A CD1   1 
ATOM   13389 C  CD2   . PHE A 1 2241 ? 149.374 137.332 178.198 1.00 104.59 ? 3458 PHE A CD2   1 
ATOM   13390 C  CE1   . PHE A 1 2241 ? 147.157 135.690 178.209 1.00 100.98 ? 3458 PHE A CE1   1 
ATOM   13391 C  CE2   . PHE A 1 2241 ? 148.773 136.991 179.396 1.00 102.86 ? 3458 PHE A CE2   1 
ATOM   13392 C  CZ    . PHE A 1 2241 ? 147.664 136.169 179.400 1.00 101.92 ? 3458 PHE A CZ    1 
ATOM   13393 N  N     . PRO A 1 2243 ? 145.634 140.207 178.258 1.00 104.95 ? 3460 PRO A N     1 
ATOM   13394 C  CA    . PRO A 1 2243 ? 145.914 140.067 179.691 1.00 102.36 ? 3460 PRO A CA    1 
ATOM   13395 C  C     . PRO A 1 2243 ? 144.646 139.888 180.518 1.00 103.00 ? 3460 PRO A C     1 
ATOM   13396 O  O     . PRO A 1 2243 ? 144.716 139.786 181.742 1.00 105.15 ? 3460 PRO A O     1 
ATOM   13397 C  CB    . PRO A 1 2243 ? 146.614 141.382 180.041 1.00 98.40  ? 3460 PRO A CB    1 
ATOM   13398 C  CG    . PRO A 1 2243 ? 147.221 141.836 178.762 1.00 97.44  ? 3460 PRO A CG    1 
ATOM   13399 C  CD    . PRO A 1 2243 ? 146.273 141.403 177.684 1.00 104.30 ? 3460 PRO A CD    1 
ATOM   13400 N  N     . ILE A 1 2244 ? 143.491 139.846 179.844 1.00 104.97 ? 3461 ILE A N     1 
ATOM   13401 C  CA    . ILE A 1 2244 ? 142.212 139.679 180.533 1.00 106.80 ? 3461 ILE A CA    1 
ATOM   13402 C  C     . ILE A 1 2244 ? 141.943 138.241 180.941 1.00 106.79 ? 3461 ILE A C     1 
ATOM   13403 O  O     . ILE A 1 2244 ? 140.903 137.968 181.555 1.00 107.59 ? 3461 ILE A O     1 
ATOM   13404 C  CB    . ILE A 1 2244 ? 141.044 140.175 179.658 1.00 107.21 ? 3461 ILE A CB    1 
ATOM   13405 N  N     . ILE A 1 2245 ? 142.842 137.313 180.620 1.00 105.91 ? 3462 ILE A N     1 
ATOM   13406 C  CA    . ILE A 1 2245 ? 142.650 135.901 180.932 1.00 105.06 ? 3462 ILE A CA    1 
ATOM   13407 C  C     . ILE A 1 2245 ? 143.680 135.529 181.994 1.00 105.21 ? 3462 ILE A C     1 
ATOM   13408 O  O     . ILE A 1 2245 ? 144.118 134.376 182.085 1.00 105.24 ? 3462 ILE A O     1 
ATOM   13409 C  CB    . ILE A 1 2245 ? 142.776 135.032 179.664 1.00 102.75 ? 3462 ILE A CB    1 
ATOM   13410 C  CG1   . ILE A 1 2245 ? 142.096 135.717 178.478 1.00 104.08 ? 3462 ILE A CG1   1 
ATOM   13411 C  CG2   . ILE A 1 2245 ? 142.080 133.690 179.839 1.00 100.69 ? 3462 ILE A CG2   1 
ATOM   13412 C  CD1   . ILE A 1 2245 ? 140.598 135.909 178.649 1.00 106.75 ? 3462 ILE A CD1   1 
ATOM   13413 N  N     . SER A 1 2246 ? 144.078 136.517 182.802 1.00 105.65 ? 3463 SER A N     1 
ATOM   13414 C  CA    . SER A 1 2246 ? 145.106 136.287 183.814 1.00 103.90 ? 3463 SER A CA    1 
ATOM   13415 C  C     . SER A 1 2246 ? 144.624 135.332 184.900 1.00 101.82 ? 3463 SER A C     1 
ATOM   13416 O  O     . SER A 1 2246 ? 145.373 134.448 185.332 1.00 103.13 ? 3463 SER A O     1 
ATOM   13417 C  CB    . SER A 1 2246 ? 145.550 137.616 184.423 1.00 104.74 ? 3463 SER A CB    1 
ATOM   13418 O  OG    . SER A 1 2246 ? 146.214 138.419 183.463 1.00 103.60 ? 3463 SER A OG    1 
ATOM   13419 N  N     . ARG A 1 2247 ? 143.376 135.487 185.348 1.00 101.02 ? 3464 ARG A N     1 
ATOM   13420 C  CA    . ARG A 1 2247 ? 142.844 134.594 186.373 1.00 102.84 ? 3464 ARG A CA    1 
ATOM   13421 C  C     . ARG A 1 2247 ? 142.752 133.161 185.862 1.00 105.27 ? 3464 ARG A C     1 
ATOM   13422 O  O     . ARG A 1 2247 ? 143.099 132.213 186.577 1.00 109.66 ? 3464 ARG A O     1 
ATOM   13423 C  CB    . ARG A 1 2247 ? 141.474 135.084 186.835 1.00 104.36 ? 3464 ARG A CB    1 
ATOM   13424 C  CG    . ARG A 1 2247 ? 141.500 136.414 187.566 1.00 106.43 ? 3464 ARG A CG    1 
ATOM   13425 C  CD    . ARG A 1 2247 ? 140.103 136.811 188.003 1.00 106.92 ? 3464 ARG A CD    1 
ATOM   13426 N  NE    . ARG A 1 2247 ? 140.055 138.155 188.566 1.00 101.60 ? 3464 ARG A NE    1 
ATOM   13427 C  CZ    . ARG A 1 2247 ? 140.201 138.434 189.853 1.00 98.72  ? 3464 ARG A CZ    1 
ATOM   13428 N  NH1   . ARG A 1 2247 ? 140.405 137.481 190.748 1.00 99.47  ? 3464 ARG A NH1   1 
ATOM   13429 N  NH2   . ARG A 1 2247 ? 140.138 139.701 190.254 1.00 95.51  ? 3464 ARG A NH2   1 
ATOM   13430 N  N     . LEU A 1 2248 ? 142.302 132.987 184.618 1.00 104.11 ? 3465 LEU A N     1 
ATOM   13431 C  CA    . LEU A 1 2248 ? 142.167 131.647 184.062 1.00 102.61 ? 3465 LEU A CA    1 
ATOM   13432 C  C     . LEU A 1 2248 ? 143.523 131.009 183.786 1.00 104.98 ? 3465 LEU A C     1 
ATOM   13433 O  O     . LEU A 1 2248 ? 143.674 129.792 183.941 1.00 107.34 ? 3465 LEU A O     1 
ATOM   13434 C  CB    . LEU A 1 2248 ? 141.331 131.693 182.785 1.00 99.89  ? 3465 LEU A CB    1 
ATOM   13435 C  CG    . LEU A 1 2248 ? 139.814 131.614 182.964 1.00 101.03 ? 3465 LEU A CG    1 
ATOM   13436 C  CD1   . LEU A 1 2248 ? 139.112 131.592 181.614 1.00 98.06  ? 3465 LEU A CD1   1 
ATOM   13437 C  CD2   . LEU A 1 2248 ? 139.430 130.405 183.798 1.00 104.97 ? 3465 LEU A CD2   1 
ATOM   13438 N  N     . ILE A 1 2249 ? 144.517 131.802 183.377 1.00 103.77 ? 3466 ILE A N     1 
ATOM   13439 C  CA    . ILE A 1 2249 ? 145.837 131.237 183.118 1.00 101.97 ? 3466 ILE A CA    1 
ATOM   13440 C  C     . ILE A 1 2249 ? 146.593 130.973 184.418 1.00 103.48 ? 3466 ILE A C     1 
ATOM   13441 O  O     . ILE A 1 2249 ? 147.476 130.108 184.448 1.00 102.92 ? 3466 ILE A O     1 
ATOM   13442 C  CB    . ILE A 1 2249 ? 146.638 132.152 182.170 1.00 100.05 ? 3466 ILE A CB    1 
ATOM   13443 C  CG1   . ILE A 1 2249 ? 147.866 131.439 181.608 1.00 98.51  ? 3466 ILE A CG1   1 
ATOM   13444 C  CG2   . ILE A 1 2249 ? 147.126 133.392 182.874 1.00 103.00 ? 3466 ILE A CG2   1 
ATOM   13445 C  CD1   . ILE A 1 2249 ? 148.499 132.177 180.451 1.00 96.05  ? 3466 ILE A CD1   1 
ATOM   13446 N  N     . SER A 1 2250 ? 146.252 131.668 185.505 1.00 104.46 ? 3467 SER A N     1 
ATOM   13447 C  CA    . SER A 1 2250 ? 146.907 131.459 186.788 1.00 102.45 ? 3467 SER A CA    1 
ATOM   13448 C  C     . SER A 1 2250 ? 146.155 130.498 187.698 1.00 102.84 ? 3467 SER A C     1 
ATOM   13449 O  O     . SER A 1 2250 ? 146.678 130.153 188.763 1.00 104.53 ? 3467 SER A O     1 
ATOM   13450 C  CB    . SER A 1 2250 ? 147.095 132.799 187.504 1.00 103.76 ? 3467 SER A CB    1 
ATOM   13451 O  OG    . SER A 1 2250 ? 145.881 133.528 187.539 1.00 110.07 ? 3467 SER A OG    1 
ATOM   13452 N  N     . ARG A 1 2251 ? 144.949 130.066 187.307 1.00 102.71 ? 3468 ARG A N     1 
ATOM   13453 C  CA    . ARG A 1 2251 ? 144.135 129.127 188.089 1.00 105.35 ? 3468 ARG A CA    1 
ATOM   13454 C  C     . ARG A 1 2251 ? 143.857 129.687 189.486 1.00 108.72 ? 3468 ARG A C     1 
ATOM   13455 O  O     . ARG A 1 2251 ? 144.287 129.138 190.503 1.00 112.98 ? 3468 ARG A O     1 
ATOM   13456 C  CB    . ARG A 1 2251 ? 144.788 127.737 188.148 1.00 104.63 ? 3468 ARG A CB    1 
ATOM   13457 C  CG    . ARG A 1 2251 ? 143.934 126.622 188.762 1.00 103.26 ? 3468 ARG A CG    1 
ATOM   13458 C  CD    . ARG A 1 2251 ? 142.714 126.307 187.917 1.00 106.51 ? 3468 ARG A CD    1 
ATOM   13459 N  NE    . ARG A 1 2251 ? 143.071 125.818 186.591 1.00 106.07 ? 3468 ARG A NE    1 
ATOM   13460 C  CZ    . ARG A 1 2251 ? 143.351 124.552 186.311 1.00 103.27 ? 3468 ARG A CZ    1 
ATOM   13461 N  NH1   . ARG A 1 2251 ? 143.326 123.616 187.245 1.00 100.58 ? 3468 ARG A NH1   1 
ATOM   13462 N  NH2   . ARG A 1 2251 ? 143.660 124.217 185.062 1.00 103.63 ? 3468 ARG A NH2   1 
ATOM   13463 N  N     . GLU A 1 2252 ? 143.174 130.830 189.532 1.00 109.40 ? 3469 GLU A N     1 
ATOM   13464 C  CA    . GLU A 1 2252 ? 142.816 131.479 190.793 1.00 113.06 ? 3469 GLU A CA    1 
ATOM   13465 C  C     . GLU A 1 2252 ? 141.297 131.508 190.887 1.00 119.02 ? 3469 GLU A C     1 
ATOM   13466 O  O     . GLU A 1 2252 ? 140.645 132.470 190.480 1.00 117.89 ? 3469 GLU A O     1 
ATOM   13467 C  CB    . GLU A 1 2252 ? 143.417 132.877 190.870 1.00 110.60 ? 3469 GLU A CB    1 
ATOM   13468 C  CG    . GLU A 1 2252 ? 144.937 132.904 190.832 1.00 109.08 ? 3469 GLU A CG    1 
ATOM   13469 C  CD    . GLU A 1 2252 ? 145.489 134.288 190.547 1.00 111.45 ? 3469 GLU A CD    1 
ATOM   13470 O  OE1   . GLU A 1 2252 ? 144.739 135.129 190.010 1.00 114.30 ? 3469 GLU A OE1   1 
ATOM   13471 O  OE2   . GLU A 1 2252 ? 146.672 134.534 190.861 1.00 107.29 ? 3469 GLU A OE2   1 
ATOM   13472 N  N     . PHE A 1 2253 ? 140.724 130.441 191.435 1.00 121.39 ? 3470 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 2253 ? 139.281 130.268 191.483 1.00 124.27 ? 3470 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 2253 ? 138.763 130.443 192.905 1.00 127.89 ? 3470 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 2253 ? 139.489 130.264 193.886 1.00 128.59 ? 3470 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 2253 ? 138.869 128.889 190.951 1.00 121.23 ? 3470 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 2253 ? 139.124 128.695 189.479 1.00 117.93 ? 3470 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 2253 ? 139.388 129.775 188.650 1.00 117.70 ? 3470 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 2253 ? 139.084 127.427 188.923 1.00 117.44 ? 3470 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 2253 ? 139.619 129.591 187.301 1.00 113.71 ? 3470 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 2253 ? 139.309 127.238 187.572 1.00 115.26 ? 3470 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 2253 ? 139.578 128.322 186.761 1.00 112.91 ? 3470 PHE A CZ    1 
ATOM   13483 N  N     . ASN A 1 2254 ? 137.484 130.796 192.999 1.00 129.69 ? 3471 ASN A N     1 
ATOM   13484 C  CA    . ASN A 1 2254 ? 136.784 130.928 194.269 1.00 131.33 ? 3471 ASN A CA    1 
ATOM   13485 C  C     . ASN A 1 2254 ? 135.758 129.810 194.384 1.00 133.59 ? 3471 ASN A C     1 
ATOM   13486 O  O     . ASN A 1 2254 ? 134.935 129.623 193.482 1.00 134.05 ? 3471 ASN A O     1 
ATOM   13487 C  CB    . ASN A 1 2254 ? 136.097 132.291 194.381 1.00 126.37 ? 3471 ASN A CB    1 
ATOM   13488 C  CG    . ASN A 1 2254 ? 137.047 133.390 194.813 1.00 125.85 ? 3471 ASN A CG    1 
ATOM   13489 O  OD1   . ASN A 1 2254 ? 137.939 133.169 195.631 1.00 126.23 ? 3471 ASN A OD1   1 
ATOM   13490 N  ND2   . ASN A 1 2254 ? 136.860 134.584 194.263 1.00 123.84 ? 3471 ASN A ND2   1 
ATOM   13491 N  N     . HIS A 1 2255 ? 135.804 129.075 195.490 1.00 135.00 ? 3472 HIS A N     1 
ATOM   13492 C  CA    . HIS A 1 2255 ? 134.929 127.932 195.704 1.00 136.42 ? 3472 HIS A CA    1 
ATOM   13493 C  C     . HIS A 1 2255 ? 133.825 128.302 196.684 1.00 137.60 ? 3472 HIS A C     1 
ATOM   13494 O  O     . HIS A 1 2255 ? 134.100 128.811 197.776 1.00 134.53 ? 3472 HIS A O     1 
ATOM   13495 C  CB    . HIS A 1 2255 ? 135.719 126.729 196.222 1.00 135.37 ? 3472 HIS A CB    1 
ATOM   13496 C  CG    . HIS A 1 2255 ? 136.931 126.406 195.404 1.00 133.82 ? 3472 HIS A CG    1 
ATOM   13497 N  ND1   . HIS A 1 2255 ? 136.996 126.637 194.047 1.00 132.30 ? 3472 HIS A ND1   1 
ATOM   13498 C  CD2   . HIS A 1 2255 ? 138.122 125.863 195.751 1.00 133.32 ? 3472 HIS A CD2   1 
ATOM   13499 C  CE1   . HIS A 1 2255 ? 138.176 126.254 193.593 1.00 132.28 ? 3472 HIS A CE1   1 
ATOM   13500 N  NE2   . HIS A 1 2255 ? 138.877 125.780 194.606 1.00 133.76 ? 3472 HIS A NE2   1 
ATOM   13501 N  N     . ALA A 1 2256 ? 132.582 128.043 196.291 1.00 138.89 ? 3473 ALA A N     1 
ATOM   13502 C  CA    . ALA A 1 2256 ? 131.429 128.351 197.127 1.00 140.78 ? 3473 ALA A CA    1 
ATOM   13503 C  C     . ALA A 1 2256 ? 130.272 127.408 196.818 1.00 139.77 ? 3473 ALA A C     1 
ATOM   13504 O  O     . ALA A 1 2256 ? 130.185 126.855 195.721 1.00 139.34 ? 3473 ALA A O     1 
ATOM   13505 C  CB    . ALA A 1 2256 ? 131.001 129.798 196.930 1.00 140.40 ? 3473 ALA A CB    1 
ATOM   13506 N  N     . VAL A 1 2260 ? 132.736 125.749 192.363 1.00 130.24 ? 3477 VAL A N     1 
ATOM   13507 C  CA    . VAL A 1 2260 ? 133.871 126.477 191.811 1.00 131.83 ? 3477 VAL A CA    1 
ATOM   13508 C  C     . VAL A 1 2260 ? 133.379 127.618 190.929 1.00 132.12 ? 3477 VAL A C     1 
ATOM   13509 O  O     . VAL A 1 2260 ? 132.683 127.394 189.939 1.00 131.42 ? 3477 VAL A O     1 
ATOM   13510 C  CB    . VAL A 1 2260 ? 134.802 125.541 191.020 1.00 133.23 ? 3477 VAL A CB    1 
ATOM   13511 C  CG1   . VAL A 1 2260 ? 135.873 126.343 190.297 1.00 132.05 ? 3477 VAL A CG1   1 
ATOM   13512 C  CG2   . VAL A 1 2260 ? 135.429 124.509 191.944 1.00 130.93 ? 3477 VAL A CG2   1 
ATOM   13513 N  N     . THR A 1 2261 ? 133.741 128.844 191.296 1.00 132.85 ? 3478 THR A N     1 
ATOM   13514 C  CA    . THR A 1 2261 ? 133.346 130.039 190.565 1.00 131.24 ? 3478 THR A CA    1 
ATOM   13515 C  C     . THR A 1 2261 ? 134.582 130.831 190.166 1.00 129.62 ? 3478 THR A C     1 
ATOM   13516 O  O     . THR A 1 2261 ? 135.524 130.968 190.953 1.00 129.98 ? 3478 THR A O     1 
ATOM   13517 C  CB    . THR A 1 2261 ? 132.414 130.924 191.403 1.00 131.90 ? 3478 THR A CB    1 
ATOM   13518 O  OG1   . THR A 1 2261 ? 133.091 131.338 192.597 1.00 132.17 ? 3478 THR A OG1   1 
ATOM   13519 C  CG2   . THR A 1 2261 ? 131.145 130.170 191.778 1.00 130.90 ? 3478 THR A CG2   1 
ATOM   13520 N  N     . VAL A 1 2262 ? 134.574 131.350 188.941 1.00 129.04 ? 3479 VAL A N     1 
ATOM   13521 C  CA    . VAL A 1 2262 ? 135.651 132.184 188.423 1.00 126.41 ? 3479 VAL A CA    1 
ATOM   13522 C  C     . VAL A 1 2262 ? 135.064 133.535 188.045 1.00 125.47 ? 3479 VAL A C     1 
ATOM   13523 O  O     . VAL A 1 2262 ? 134.098 133.604 187.276 1.00 128.37 ? 3479 VAL A O     1 
ATOM   13524 C  CB    . VAL A 1 2262 ? 136.346 131.533 187.213 1.00 125.18 ? 3479 VAL A CB    1 
ATOM   13525 N  N     . GLU A 1 2263 ? 135.646 134.604 188.582 1.00 122.78 ? 3480 GLU A N     1 
ATOM   13526 C  CA    . GLU A 1 2263 ? 135.167 135.962 188.333 1.00 125.23 ? 3480 GLU A CA    1 
ATOM   13527 C  C     . GLU A 1 2263 ? 135.911 136.523 187.128 1.00 123.54 ? 3480 GLU A C     1 
ATOM   13528 O  O     . GLU A 1 2263 ? 136.991 137.102 187.263 1.00 119.27 ? 3480 GLU A O     1 
ATOM   13529 C  CB    . GLU A 1 2263 ? 135.360 136.835 189.567 1.00 120.19 ? 3480 GLU A CB    1 
ATOM   13530 N  N     . ILE A 1 2264 ? 135.327 136.364 185.944 1.00 125.11 ? 3481 ILE A N     1 
ATOM   13531 C  CA    . ILE A 1 2264 ? 135.919 136.842 184.700 1.00 124.71 ? 3481 ILE A CA    1 
ATOM   13532 C  C     . ILE A 1 2264 ? 135.265 138.167 184.328 1.00 125.88 ? 3481 ILE A C     1 
ATOM   13533 O  O     . ILE A 1 2264 ? 134.035 138.301 184.373 1.00 127.32 ? 3481 ILE A O     1 
ATOM   13534 C  CB    . ILE A 1 2264 ? 135.775 135.797 183.576 1.00 124.35 ? 3481 ILE A CB    1 
ATOM   13535 C  CG1   . ILE A 1 2264 ? 136.306 136.344 182.247 1.00 119.71 ? 3481 ILE A CG1   1 
ATOM   13536 C  CG2   . ILE A 1 2264 ? 134.337 135.291 183.457 1.00 121.22 ? 3481 ILE A CG2   1 
ATOM   13537 C  CD1   . ILE A 1 2264 ? 137.801 136.558 182.228 1.00 114.71 ? 3481 ILE A CD1   1 
ATOM   13538 N  N     . GLY A 1 2265 ? 136.088 139.156 183.989 1.00 123.61 ? 3482 GLY A N     1 
ATOM   13539 C  CA    . GLY A 1 2265 ? 135.588 140.473 183.650 1.00 123.66 ? 3482 GLY A CA    1 
ATOM   13540 C  C     . GLY A 1 2265 ? 135.019 141.216 184.840 1.00 123.75 ? 3482 GLY A C     1 
ATOM   13541 O  O     . GLY A 1 2265 ? 135.746 141.551 185.780 1.00 122.65 ? 3482 GLY A O     1 
ATOM   13542 N  N     . ASP A 1 2266 ? 133.712 141.479 184.811 1.00 121.94 ? 3483 ASP A N     1 
ATOM   13543 C  CA    . ASP A 1 2266 ? 133.031 142.182 185.892 1.00 122.88 ? 3483 ASP A CA    1 
ATOM   13544 C  C     . ASP A 1 2266 ? 131.855 141.383 186.444 1.00 126.61 ? 3483 ASP A C     1 
ATOM   13545 O  O     . ASP A 1 2266 ? 130.937 141.963 187.032 1.00 125.96 ? 3483 ASP A O     1 
ATOM   13546 C  CB    . ASP A 1 2266 ? 132.562 143.560 185.421 1.00 121.35 ? 3483 ASP A CB    1 
ATOM   13547 N  N     . HIS A 1 2267 ? 131.862 140.063 186.266 1.00 127.26 ? 3484 HIS A N     1 
ATOM   13548 C  CA    . HIS A 1 2267 ? 130.779 139.218 186.752 1.00 125.40 ? 3484 HIS A CA    1 
ATOM   13549 C  C     . HIS A 1 2267 ? 131.318 137.823 187.025 1.00 123.25 ? 3484 HIS A C     1 
ATOM   13550 O  O     . HIS A 1 2267 ? 132.046 137.265 186.198 1.00 122.14 ? 3484 HIS A O     1 
ATOM   13551 C  CB    . HIS A 1 2267 ? 129.630 139.155 185.740 1.00 126.26 ? 3484 HIS A CB    1 
ATOM   13552 N  N     . GLU A 1 2268 ? 130.962 137.267 188.181 1.00 124.66 ? 3485 GLU A N     1 
ATOM   13553 C  CA    . GLU A 1 2268 ? 131.374 135.912 188.519 1.00 125.71 ? 3485 GLU A CA    1 
ATOM   13554 C  C     . GLU A 1 2268 ? 130.649 134.909 187.631 1.00 128.87 ? 3485 GLU A C     1 
ATOM   13555 O  O     . GLU A 1 2268 ? 129.426 134.973 187.471 1.00 128.06 ? 3485 GLU A O     1 
ATOM   13556 C  CB    . GLU A 1 2268 ? 131.090 135.622 189.992 1.00 122.13 ? 3485 GLU A CB    1 
ATOM   13557 N  N     . VAL A 1 2269 ? 131.405 133.977 187.056 1.00 129.75 ? 3486 VAL A N     1 
ATOM   13558 C  CA    . VAL A 1 2269 ? 130.879 132.999 186.113 1.00 128.70 ? 3486 VAL A CA    1 
ATOM   13559 C  C     . VAL A 1 2269 ? 131.166 131.602 186.641 1.00 128.84 ? 3486 VAL A C     1 
ATOM   13560 O  O     . VAL A 1 2269 ? 132.289 131.306 187.065 1.00 129.39 ? 3486 VAL A O     1 
ATOM   13561 C  CB    . VAL A 1 2269 ? 131.481 133.184 184.706 1.00 126.65 ? 3486 VAL A CB    1 
ATOM   13562 N  N     . ASP A 1 2270 ? 130.148 130.747 186.614 1.00 129.42 ? 3487 ASP A N     1 
ATOM   13563 C  CA    . ASP A 1 2270 ? 130.304 129.374 187.064 1.00 132.85 ? 3487 ASP A CA    1 
ATOM   13564 C  C     . ASP A 1 2270 ? 131.170 128.582 186.088 1.00 134.58 ? 3487 ASP A C     1 
ATOM   13565 O  O     . ASP A 1 2270 ? 131.336 128.946 184.920 1.00 133.55 ? 3487 ASP A O     1 
ATOM   13566 C  CB    . ASP A 1 2270 ? 128.939 128.702 187.215 1.00 133.31 ? 3487 ASP A CB    1 
ATOM   13567 C  CG    . ASP A 1 2270 ? 128.006 129.479 188.120 1.00 135.00 ? 3487 ASP A CG    1 
ATOM   13568 O  OD1   . ASP A 1 2270 ? 128.270 129.539 189.339 1.00 133.55 ? 3487 ASP A OD1   1 
ATOM   13569 O  OD2   . ASP A 1 2270 ? 127.006 130.029 187.611 1.00 137.08 ? 3487 ASP A OD2   1 
ATOM   13570 N  N     . VAL A 1 2271 ? 131.730 127.483 186.586 1.00 134.62 ? 3488 VAL A N     1 
ATOM   13571 C  CA    . VAL A 1 2271 ? 132.576 126.595 185.799 1.00 131.33 ? 3488 VAL A CA    1 
ATOM   13572 C  C     . VAL A 1 2271 ? 131.940 125.213 185.810 1.00 131.84 ? 3488 VAL A C     1 
ATOM   13573 O  O     . VAL A 1 2271 ? 131.659 124.662 186.881 1.00 130.85 ? 3488 VAL A O     1 
ATOM   13574 C  CB    . VAL A 1 2271 ? 134.013 126.544 186.342 1.00 131.38 ? 3488 VAL A CB    1 
ATOM   13575 C  CG1   . VAL A 1 2271 ? 134.834 125.511 185.583 1.00 130.60 ? 3488 VAL A CG1   1 
ATOM   13576 C  CG2   . VAL A 1 2271 ? 134.662 127.917 186.255 1.00 131.17 ? 3488 VAL A CG2   1 
ATOM   13577 N  N     . SER A 1 2272 ? 131.711 124.655 184.618 1.00 133.15 ? 3489 SER A N     1 
ATOM   13578 C  CA    . SER A 1 2272 ? 131.100 123.335 184.518 1.00 131.93 ? 3489 SER A CA    1 
ATOM   13579 C  C     . SER A 1 2272 ? 132.066 122.216 184.884 1.00 130.54 ? 3489 SER A C     1 
ATOM   13580 O  O     . SER A 1 2272 ? 131.621 121.093 185.146 1.00 128.28 ? 3489 SER A O     1 
ATOM   13581 C  CB    . SER A 1 2272 ? 130.560 123.113 183.104 1.00 127.34 ? 3489 SER A CB    1 
ATOM   13582 O  OG    . SER A 1 2272 ? 129.787 124.221 182.675 1.00 126.15 ? 3489 SER A OG    1 
ATOM   13583 N  N     . GLY A 1 2273 ? 133.369 122.493 184.908 1.00 130.30 ? 3490 GLY A N     1 
ATOM   13584 C  CA    . GLY A 1 2273 ? 134.370 121.509 185.252 1.00 128.24 ? 3490 GLY A CA    1 
ATOM   13585 C  C     . GLY A 1 2273 ? 135.018 120.815 184.073 1.00 125.04 ? 3490 GLY A C     1 
ATOM   13586 O  O     . GLY A 1 2273 ? 136.103 120.245 184.229 1.00 120.01 ? 3490 GLY A O     1 
ATOM   13587 N  N     . ASP A 1 2274 ? 134.389 120.848 182.901 1.00 125.74 ? 3491 ASP A N     1 
ATOM   13588 C  CA    . ASP A 1 2274 ? 134.949 120.269 181.689 1.00 122.75 ? 3491 ASP A CA    1 
ATOM   13589 C  C     . ASP A 1 2274 ? 135.740 121.281 180.871 1.00 119.26 ? 3491 ASP A C     1 
ATOM   13590 O  O     . ASP A 1 2274 ? 136.175 120.961 179.760 1.00 115.90 ? 3491 ASP A O     1 
ATOM   13591 C  CB    . ASP A 1 2274 ? 133.836 119.663 180.831 1.00 120.51 ? 3491 ASP A CB    1 
ATOM   13592 N  N     . PHE A 1 2275 ? 135.930 122.490 181.393 1.00 115.08 ? 3492 PHE A N     1 
ATOM   13593 C  CA    . PHE A 1 2275 ? 136.576 123.559 180.646 1.00 109.20 ? 3492 PHE A CA    1 
ATOM   13594 C  C     . PHE A 1 2275 ? 138.079 123.305 180.599 1.00 108.85 ? 3492 PHE A C     1 
ATOM   13595 O  O     . PHE A 1 2275 ? 138.716 123.091 181.635 1.00 107.53 ? 3492 PHE A O     1 
ATOM   13596 C  CB    . PHE A 1 2275 ? 136.268 124.905 181.311 1.00 107.52 ? 3492 PHE A CB    1 
ATOM   13597 C  CG    . PHE A 1 2275 ? 137.132 126.054 180.847 1.00 104.88 ? 3492 PHE A CG    1 
ATOM   13598 C  CD1   . PHE A 1 2275 ? 137.433 126.241 179.503 1.00 101.82 ? 3492 PHE A CD1   1 
ATOM   13599 C  CD2   . PHE A 1 2275 ? 137.659 126.940 181.770 1.00 106.52 ? 3492 PHE A CD2   1 
ATOM   13600 C  CE1   . PHE A 1 2275 ? 138.231 127.290 179.096 1.00 99.76  ? 3492 PHE A CE1   1 
ATOM   13601 C  CE2   . PHE A 1 2275 ? 138.458 127.991 181.366 1.00 103.46 ? 3492 PHE A CE2   1 
ATOM   13602 C  CZ    . PHE A 1 2275 ? 138.742 128.166 180.028 1.00 99.58  ? 3492 PHE A CZ    1 
ATOM   13603 N  N     . LYS A 1 2276 ? 138.641 123.326 179.392 1.00 108.18 ? 3493 LYS A N     1 
ATOM   13604 C  CA    . LYS A 1 2276 ? 140.081 123.313 179.186 1.00 102.98 ? 3493 LYS A CA    1 
ATOM   13605 C  C     . LYS A 1 2276 ? 140.454 124.459 178.258 1.00 98.00  ? 3493 LYS A C     1 
ATOM   13606 O  O     . LYS A 1 2276 ? 139.704 124.804 177.342 1.00 99.11  ? 3493 LYS A O     1 
ATOM   13607 C  CB    . LYS A 1 2276 ? 140.565 121.980 178.596 1.00 98.88  ? 3493 LYS A CB    1 
ATOM   13608 C  CG    . LYS A 1 2276 ? 140.679 120.851 179.607 1.00 98.92  ? 3493 LYS A CG    1 
ATOM   13609 C  CD    . LYS A 1 2276 ? 141.251 119.596 178.968 1.00 101.48 ? 3493 LYS A CD    1 
ATOM   13610 C  CE    . LYS A 1 2276 ? 142.692 119.809 178.535 1.00 102.17 ? 3493 LYS A CE    1 
ATOM   13611 N  NZ    . LYS A 1 2276 ? 143.613 119.902 179.701 1.00 107.88 ? 3493 LYS A NZ    1 
ATOM   13612 N  N     . LEU A 1 2277 ? 141.617 125.053 178.502 1.00 91.49  ? 3494 LEU A N     1 
ATOM   13613 C  CA    . LEU A 1 2277 ? 142.086 126.189 177.723 1.00 87.29  ? 3494 LEU A CA    1 
ATOM   13614 C  C     . LEU A 1 2277 ? 143.430 125.862 177.090 1.00 86.09  ? 3494 LEU A C     1 
ATOM   13615 O  O     . LEU A 1 2277 ? 144.266 125.183 177.694 1.00 90.86  ? 3494 LEU A O     1 
ATOM   13616 C  CB    . LEU A 1 2277 ? 142.203 127.450 178.593 1.00 86.56  ? 3494 LEU A CB    1 
ATOM   13617 C  CG    . LEU A 1 2277 ? 142.307 128.805 177.882 1.00 86.76  ? 3494 LEU A CG    1 
ATOM   13618 C  CD1   . LEU A 1 2277 ? 141.550 129.871 178.654 1.00 86.78  ? 3494 LEU A CD1   1 
ATOM   13619 C  CD2   . LEU A 1 2277 ? 143.757 129.231 177.692 1.00 86.77  ? 3494 LEU A CD2   1 
ATOM   13620 N  N     . PHE A 1 2278 ? 143.624 126.348 175.868 1.00 82.05  ? 3495 PHE A N     1 
ATOM   13621 C  CA    . PHE A 1 2278 ? 144.874 126.213 175.140 1.00 76.56  ? 3495 PHE A CA    1 
ATOM   13622 C  C     . PHE A 1 2278 ? 145.288 127.581 174.623 1.00 78.08  ? 3495 PHE A C     1 
ATOM   13623 O  O     . PHE A 1 2278 ? 144.468 128.492 174.493 1.00 84.53  ? 3495 PHE A O     1 
ATOM   13624 C  CB    . PHE A 1 2278 ? 144.753 125.236 173.960 1.00 77.36  ? 3495 PHE A CB    1 
ATOM   13625 C  CG    . PHE A 1 2278 ? 144.823 123.787 174.349 1.00 77.71  ? 3495 PHE A CG    1 
ATOM   13626 C  CD1   . PHE A 1 2278 ? 143.825 123.206 175.113 1.00 83.23  ? 3495 PHE A CD1   1 
ATOM   13627 C  CD2   . PHE A 1 2278 ? 145.879 123.000 173.927 1.00 83.62  ? 3495 PHE A CD2   1 
ATOM   13628 C  CE1   . PHE A 1 2278 ? 143.889 121.872 175.464 1.00 91.14  ? 3495 PHE A CE1   1 
ATOM   13629 C  CE2   . PHE A 1 2278 ? 145.948 121.665 174.270 1.00 90.24  ? 3495 PHE A CE2   1 
ATOM   13630 C  CZ    . PHE A 1 2278 ? 144.952 121.101 175.041 1.00 94.74  ? 3495 PHE A CZ    1 
ATOM   13631 N  N     . ILE A 1 2279 ? 146.579 127.726 174.340 1.00 76.25  ? 3496 ILE A N     1 
ATOM   13632 C  CA    . ILE A 1 2279 ? 147.114 128.918 173.695 1.00 80.44  ? 3496 ILE A CA    1 
ATOM   13633 C  C     . ILE A 1 2279 ? 147.967 128.464 172.521 1.00 84.01  ? 3496 ILE A C     1 
ATOM   13634 O  O     . ILE A 1 2279 ? 148.778 127.542 172.660 1.00 87.15  ? 3496 ILE A O     1 
ATOM   13635 C  CB    . ILE A 1 2279 ? 147.938 129.789 174.664 1.00 81.54  ? 3496 ILE A CB    1 
ATOM   13636 C  CG1   . ILE A 1 2279 ? 147.115 130.139 175.909 1.00 84.38  ? 3496 ILE A CG1   1 
ATOM   13637 C  CG2   . ILE A 1 2279 ? 148.404 131.060 173.968 1.00 81.76  ? 3496 ILE A CG2   1 
ATOM   13638 C  CD1   . ILE A 1 2279 ? 147.732 131.208 176.786 1.00 88.21  ? 3496 ILE A CD1   1 
ATOM   13639 N  N     . HIS A 1 2280 ? 147.780 129.100 171.369 1.00 88.89  ? 3497 HIS A N     1 
ATOM   13640 C  CA    . HIS A 1 2280 ? 148.493 128.740 170.155 1.00 93.71  ? 3497 HIS A CA    1 
ATOM   13641 C  C     . HIS A 1 2280 ? 149.205 129.960 169.588 1.00 96.62  ? 3497 HIS A C     1 
ATOM   13642 O  O     . HIS A 1 2280 ? 148.746 131.095 169.740 1.00 99.80  ? 3497 HIS A O     1 
ATOM   13643 C  CB    . HIS A 1 2280 ? 147.538 128.152 169.106 1.00 95.79  ? 3497 HIS A CB    1 
ATOM   13644 C  CG    . HIS A 1 2280 ? 148.230 127.564 167.917 1.00 100.97 ? 3497 HIS A CG    1 
ATOM   13645 N  ND1   . HIS A 1 2280 ? 148.666 128.327 166.855 1.00 104.76 ? 3497 HIS A ND1   1 
ATOM   13646 C  CD2   . HIS A 1 2280 ? 148.562 126.285 167.621 1.00 106.04 ? 3497 HIS A CD2   1 
ATOM   13647 C  CE1   . HIS A 1 2280 ? 149.236 127.544 165.957 1.00 110.01 ? 3497 HIS A CE1   1 
ATOM   13648 N  NE2   . HIS A 1 2280 ? 149.186 126.300 166.397 1.00 110.21 ? 3497 HIS A NE2   1 
ATOM   13649 N  N     . SER A 1 2281 ? 150.343 129.715 168.944 1.00 96.87  ? 3498 SER A N     1 
ATOM   13650 C  CA    . SER A 1 2281 ? 151.088 130.767 168.270 1.00 101.45 ? 3498 SER A CA    1 
ATOM   13651 C  C     . SER A 1 2281 ? 151.796 130.167 167.066 1.00 106.15 ? 3498 SER A C     1 
ATOM   13652 O  O     . SER A 1 2281 ? 152.254 129.023 167.114 1.00 105.13 ? 3498 SER A O     1 
ATOM   13653 C  CB    . SER A 1 2281 ? 152.102 131.432 169.207 1.00 103.48 ? 3498 SER A CB    1 
ATOM   13654 O  OG    . SER A 1 2281 ? 152.990 132.265 168.482 1.00 106.54 ? 3498 SER A OG    1 
ATOM   13655 N  N     . CYS A 1 2282 ? 151.881 130.947 165.989 1.00 113.88 ? 3499 CYS A N     1 
ATOM   13656 C  CA    . CYS A 1 2282 ? 152.508 130.498 164.751 1.00 118.71 ? 3499 CYS A CA    1 
ATOM   13657 C  C     . CYS A 1 2282 ? 153.669 131.395 164.336 1.00 120.66 ? 3499 CYS A C     1 
ATOM   13658 O  O     . CYS A 1 2282 ? 154.055 131.398 163.164 1.00 122.88 ? 3499 CYS A O     1 
ATOM   13659 C  CB    . CYS A 1 2282 ? 151.473 130.417 163.629 1.00 119.86 ? 3499 CYS A CB    1 
ATOM   13660 S  SG    . CYS A 1 2282 ? 150.488 131.918 163.414 1.00 122.76 ? 3499 CYS A SG    1 
ATOM   13661 N  N     . ASP A 1 2283 ? 154.235 132.154 165.272 1.00 119.91 ? 3500 ASP A N     1 
ATOM   13662 C  CA    . ASP A 1 2283 ? 155.319 133.094 164.989 1.00 125.13 ? 3500 ASP A CA    1 
ATOM   13663 C  C     . ASP A 1 2283 ? 156.463 132.833 165.958 1.00 126.39 ? 3500 ASP A C     1 
ATOM   13664 O  O     . ASP A 1 2283 ? 156.586 133.508 166.990 1.00 126.94 ? 3500 ASP A O     1 
ATOM   13665 C  CB    . ASP A 1 2283 ? 154.833 134.541 165.084 1.00 127.59 ? 3500 ASP A CB    1 
ATOM   13666 C  CG    . ASP A 1 2283 ? 154.226 135.039 163.787 1.00 131.08 ? 3500 ASP A CG    1 
ATOM   13667 O  OD1   . ASP A 1 2283 ? 154.278 134.301 162.781 1.00 125.06 ? 3500 ASP A OD1   1 
ATOM   13668 O  OD2   . ASP A 1 2283 ? 153.693 136.169 163.775 1.00 139.98 ? 3500 ASP A OD2   1 
ATOM   13669 N  N     . PRO A 1 2284 ? 157.327 131.851 165.659 1.00 126.28 ? 3501 PRO A N     1 
ATOM   13670 C  CA    . PRO A 1 2284 ? 158.465 131.531 166.527 1.00 126.38 ? 3501 PRO A CA    1 
ATOM   13671 C  C     . PRO A 1 2284 ? 159.543 132.611 166.494 1.00 130.65 ? 3501 PRO A C     1 
ATOM   13672 O  O     . PRO A 1 2284 ? 159.563 133.409 165.557 1.00 128.84 ? 3501 PRO A O     1 
ATOM   13673 C  CB    . PRO A 1 2284 ? 159.001 130.213 165.947 1.00 122.83 ? 3501 PRO A CB    1 
ATOM   13674 C  CG    . PRO A 1 2284 ? 157.975 129.753 164.947 1.00 123.33 ? 3501 PRO A CG    1 
ATOM   13675 C  CD    . PRO A 1 2284 ? 157.277 130.979 164.476 1.00 123.15 ? 3501 PRO A CD    1 
ATOM   13676 N  N     . ILE A 1 2288 ? 157.094 137.582 173.225 1.00 108.41 ? 3505 ILE A N     1 
ATOM   13677 C  CA    . ILE A 1 2288 ? 156.274 136.974 174.266 1.00 110.96 ? 3505 ILE A CA    1 
ATOM   13678 C  C     . ILE A 1 2288 ? 156.591 137.594 175.624 1.00 108.02 ? 3505 ILE A C     1 
ATOM   13679 O  O     . ILE A 1 2288 ? 157.750 137.632 176.036 1.00 103.94 ? 3505 ILE A O     1 
ATOM   13680 C  CB    . ILE A 1 2288 ? 156.467 135.445 174.303 1.00 110.71 ? 3505 ILE A CB    1 
ATOM   13681 C  CG1   . ILE A 1 2288 ? 155.993 134.812 172.994 1.00 110.71 ? 3505 ILE A CG1   1 
ATOM   13682 C  CG2   . ILE A 1 2288 ? 155.727 134.839 175.483 1.00 107.73 ? 3505 ILE A CG2   1 
ATOM   13683 C  CD1   . ILE A 1 2288 ? 156.239 133.320 172.912 1.00 106.92 ? 3505 ILE A CD1   1 
ATOM   13684 N  N     . PRO A 1 2289 ? 155.561 138.093 176.308 1.00 109.95 ? 3506 PRO A N     1 
ATOM   13685 C  CA    . PRO A 1 2289 ? 155.761 138.617 177.664 1.00 110.22 ? 3506 PRO A CA    1 
ATOM   13686 C  C     . PRO A 1 2289 ? 156.174 137.515 178.629 1.00 106.50 ? 3506 PRO A C     1 
ATOM   13687 O  O     . PRO A 1 2289 ? 155.836 136.342 178.452 1.00 103.54 ? 3506 PRO A O     1 
ATOM   13688 C  CB    . PRO A 1 2289 ? 154.388 139.197 178.031 1.00 112.91 ? 3506 PRO A CB    1 
ATOM   13689 C  CG    . PRO A 1 2289 ? 153.684 139.392 176.723 1.00 113.08 ? 3506 PRO A CG    1 
ATOM   13690 C  CD    . PRO A 1 2289 ? 154.186 138.306 175.827 1.00 112.28 ? 3506 PRO A CD    1 
ATOM   13691 N  N     . ILE A 1 2290 ? 156.922 137.911 179.663 1.00 106.30 ? 3507 ILE A N     1 
ATOM   13692 C  CA    . ILE A 1 2290 ? 157.474 136.937 180.601 1.00 104.08 ? 3507 ILE A CA    1 
ATOM   13693 C  C     . ILE A 1 2290 ? 156.372 136.280 181.430 1.00 99.81  ? 3507 ILE A C     1 
ATOM   13694 O  O     . ILE A 1 2290 ? 156.503 135.116 181.833 1.00 96.85  ? 3507 ILE A O     1 
ATOM   13695 C  CB    . ILE A 1 2290 ? 158.554 137.603 181.478 1.00 98.99  ? 3507 ILE A CB    1 
ATOM   13696 C  CG1   . ILE A 1 2290 ? 159.346 136.551 182.259 1.00 93.61  ? 3507 ILE A CG1   1 
ATOM   13697 C  CG2   . ILE A 1 2290 ? 157.954 138.654 182.407 1.00 91.21  ? 3507 ILE A CG2   1 
ATOM   13698 C  CD1   . ILE A 1 2290 ? 160.670 137.052 182.788 1.00 90.28  ? 3507 ILE A CD1   1 
ATOM   13699 N  N     . PHE A 1 2291 ? 155.271 136.995 181.689 1.00 97.98  ? 3508 PHE A N     1 
ATOM   13700 C  CA    . PHE A 1 2291 ? 154.154 136.393 182.412 1.00 95.07  ? 3508 PHE A CA    1 
ATOM   13701 C  C     . PHE A 1 2291 ? 153.530 135.269 181.595 1.00 95.39  ? 3508 PHE A C     1 
ATOM   13702 O  O     . PHE A 1 2291 ? 153.159 134.226 182.145 1.00 91.45  ? 3508 PHE A O     1 
ATOM   13703 C  CB    . PHE A 1 2291 ? 153.129 137.479 182.779 1.00 97.21  ? 3508 PHE A CB    1 
ATOM   13704 C  CG    . PHE A 1 2291 ? 151.866 136.964 183.449 1.00 96.64  ? 3508 PHE A CG    1 
ATOM   13705 C  CD1   . PHE A 1 2291 ? 151.685 137.142 184.811 1.00 94.82  ? 3508 PHE A CD1   1 
ATOM   13706 C  CD2   . PHE A 1 2291 ? 150.820 136.412 182.715 1.00 95.91  ? 3508 PHE A CD2   1 
ATOM   13707 C  CE1   . PHE A 1 2291 ? 150.532 136.702 185.439 1.00 92.46  ? 3508 PHE A CE1   1 
ATOM   13708 C  CE2   . PHE A 1 2291 ? 149.669 135.972 183.339 1.00 91.92  ? 3508 PHE A CE2   1 
ATOM   13709 C  CZ    . PHE A 1 2291 ? 149.523 136.122 184.700 1.00 89.04  ? 3508 PHE A CZ    1 
ATOM   13710 N  N     . LEU A 1 2292 ? 153.399 135.464 180.282 1.00 97.38  ? 3509 LEU A N     1 
ATOM   13711 C  CA    . LEU A 1 2292 ? 152.935 134.381 179.424 1.00 99.06  ? 3509 LEU A CA    1 
ATOM   13712 C  C     . LEU A 1 2292 ? 153.970 133.270 179.320 1.00 99.82  ? 3509 LEU A C     1 
ATOM   13713 O  O     . LEU A 1 2292 ? 153.607 132.090 179.244 1.00 97.00  ? 3509 LEU A O     1 
ATOM   13714 C  CB    . LEU A 1 2292 ? 152.597 134.921 178.035 1.00 99.92  ? 3509 LEU A CB    1 
ATOM   13715 C  CG    . LEU A 1 2292 ? 151.995 133.906 177.065 1.00 99.92  ? 3509 LEU A CG    1 
ATOM   13716 C  CD1   . LEU A 1 2292 ? 150.576 133.550 177.478 1.00 101.08 ? 3509 LEU A CD1   1 
ATOM   13717 C  CD2   . LEU A 1 2292 ? 152.030 134.439 175.649 1.00 103.12 ? 3509 LEU A CD2   1 
ATOM   13718 N  N     . ARG A 1 2293 ? 155.256 133.627 179.311 1.00 98.29  ? 3510 ARG A N     1 
ATOM   13719 C  CA    . ARG A 1 2293 ? 156.312 132.633 179.147 1.00 92.70  ? 3510 ARG A CA    1 
ATOM   13720 C  C     . ARG A 1 2293 ? 156.395 131.689 180.342 1.00 90.73  ? 3510 ARG A C     1 
ATOM   13721 O  O     . ARG A 1 2293 ? 156.569 130.477 180.168 1.00 85.32  ? 3510 ARG A O     1 
ATOM   13722 C  CB    . ARG A 1 2293 ? 157.650 133.336 178.922 1.00 89.94  ? 3510 ARG A CB    1 
ATOM   13723 C  CG    . ARG A 1 2293 ? 158.841 132.401 178.826 1.00 88.48  ? 3510 ARG A CG    1 
ATOM   13724 C  CD    . ARG A 1 2293 ? 159.026 131.873 177.413 1.00 85.82  ? 3510 ARG A CD    1 
ATOM   13725 N  NE    . ARG A 1 2293 ? 160.434 131.777 177.046 1.00 81.84  ? 3510 ARG A NE    1 
ATOM   13726 C  CZ    . ARG A 1 2293 ? 161.249 130.807 177.438 1.00 77.32  ? 3510 ARG A CZ    1 
ATOM   13727 N  NH1   . ARG A 1 2293 ? 160.826 129.814 178.203 1.00 74.89  ? 3510 ARG A NH1   1 
ATOM   13728 N  NH2   . ARG A 1 2293 ? 162.521 130.832 177.050 1.00 76.55  ? 3510 ARG A NH2   1 
ATOM   13729 N  N     . SER A 1 2294 ? 156.260 132.216 181.559 1.00 90.50  ? 3511 SER A N     1 
ATOM   13730 C  CA    . SER A 1 2294 ? 156.543 131.453 182.768 1.00 80.50  ? 3511 SER A CA    1 
ATOM   13731 C  C     . SER A 1 2294 ? 155.287 131.031 183.526 1.00 75.81  ? 3511 SER A C     1 
ATOM   13732 O  O     . SER A 1 2294 ? 155.353 130.811 184.740 1.00 72.59  ? 3511 SER A O     1 
ATOM   13733 C  CB    . SER A 1 2294 ? 157.465 132.255 183.687 1.00 81.10  ? 3511 SER A CB    1 
ATOM   13734 O  OG    . SER A 1 2294 ? 158.614 132.701 182.989 1.00 80.94  ? 3511 SER A OG    1 
ATOM   13735 N  N     . ARG A 1 2295 ? 154.148 130.911 182.846 1.00 79.04  ? 3512 ARG A N     1 
ATOM   13736 C  CA    . ARG A 1 2295 ? 152.917 130.469 183.489 1.00 78.54  ? 3512 ARG A CA    1 
ATOM   13737 C  C     . ARG A 1 2295 ? 152.264 129.286 182.789 1.00 81.40  ? 3512 ARG A C     1 
ATOM   13738 O  O     . ARG A 1 2295 ? 151.263 128.762 183.292 1.00 80.57  ? 3512 ARG A O     1 
ATOM   13739 C  CB    . ARG A 1 2295 ? 151.916 131.630 183.574 1.00 81.55  ? 3512 ARG A CB    1 
ATOM   13740 C  CG    . ARG A 1 2295 ? 151.049 131.626 184.824 1.00 84.40  ? 3512 ARG A CG    1 
ATOM   13741 C  CD    . ARG A 1 2295 ? 151.894 131.513 186.081 1.00 77.77  ? 3512 ARG A CD    1 
ATOM   13742 N  NE    . ARG A 1 2295 ? 152.813 132.635 186.226 1.00 79.39  ? 3512 ARG A NE    1 
ATOM   13743 C  CZ    . ARG A 1 2295 ? 152.506 133.785 186.810 1.00 76.49  ? 3512 ARG A CZ    1 
ATOM   13744 N  NH1   . ARG A 1 2295 ? 151.306 133.999 187.326 1.00 76.76  ? 3512 ARG A NH1   1 
ATOM   13745 N  NH2   . ARG A 1 2295 ? 153.425 134.743 186.880 1.00 72.36  ? 3512 ARG A NH2   1 
ATOM   13746 N  N     . VAL A 1 2296 ? 152.800 128.844 181.653 1.00 81.97  ? 3513 VAL A N     1 
ATOM   13747 C  CA    . VAL A 1 2296 ? 152.204 127.769 180.867 1.00 75.31  ? 3513 VAL A CA    1 
ATOM   13748 C  C     . VAL A 1 2296 ? 153.213 126.644 180.692 1.00 77.44  ? 3513 VAL A C     1 
ATOM   13749 O  O     . VAL A 1 2296 ? 154.332 126.710 181.211 1.00 85.20  ? 3513 VAL A O     1 
ATOM   13750 C  CB    . VAL A 1 2296 ? 151.727 128.281 179.497 1.00 76.81  ? 3513 VAL A CB    1 
ATOM   13751 C  CG1   . VAL A 1 2296 ? 150.601 129.277 179.664 1.00 83.62  ? 3513 VAL A CG1   1 
ATOM   13752 C  CG2   . VAL A 1 2296 ? 152.888 128.908 178.748 1.00 76.20  ? 3513 VAL A CG2   1 
ATOM   13753 N  N     . ARG A 1 2297 ? 152.820 125.602 179.963 1.00 76.93  ? 3514 ARG A N     1 
ATOM   13754 C  CA    . ARG A 1 2297 ? 153.716 124.506 179.600 1.00 73.89  ? 3514 ARG A CA    1 
ATOM   13755 C  C     . ARG A 1 2297 ? 154.062 124.677 178.125 1.00 68.17  ? 3514 ARG A C     1 
ATOM   13756 O  O     . ARG A 1 2297 ? 153.349 124.202 177.241 1.00 69.90  ? 3514 ARG A O     1 
ATOM   13757 C  CB    . ARG A 1 2297 ? 153.069 123.155 179.878 1.00 73.30  ? 3514 ARG A CB    1 
ATOM   13758 C  CG    . ARG A 1 2297 ? 154.014 121.979 179.726 1.00 73.65  ? 3514 ARG A CG    1 
ATOM   13759 C  CD    . ARG A 1 2297 ? 153.625 120.843 180.655 1.00 78.57  ? 3514 ARG A CD    1 
ATOM   13760 N  NE    . ARG A 1 2297 ? 153.041 121.332 181.898 1.00 81.09  ? 3514 ARG A NE    1 
ATOM   13761 C  CZ    . ARG A 1 2297 ? 153.734 121.635 182.987 1.00 79.03  ? 3514 ARG A CZ    1 
ATOM   13762 N  NH1   . ARG A 1 2297 ? 155.051 121.518 183.023 1.00 75.57  ? 3514 ARG A NH1   1 
ATOM   13763 N  NH2   . ARG A 1 2297 ? 153.090 122.068 184.067 1.00 80.01  ? 3514 ARG A NH2   1 
ATOM   13764 N  N     . LEU A 1 2298 ? 155.167 125.370 177.863 1.00 66.77  ? 3515 LEU A N     1 
ATOM   13765 C  CA    . LEU A 1 2298 ? 155.549 125.686 176.494 1.00 68.80  ? 3515 LEU A CA    1 
ATOM   13766 C  C     . LEU A 1 2298 ? 156.026 124.435 175.768 1.00 76.74  ? 3515 LEU A C     1 
ATOM   13767 O  O     . LEU A 1 2298 ? 156.850 123.677 176.288 1.00 82.37  ? 3515 LEU A O     1 
ATOM   13768 C  CB    . LEU A 1 2298 ? 156.642 126.753 176.484 1.00 69.58  ? 3515 LEU A CB    1 
ATOM   13769 C  CG    . LEU A 1 2298 ? 157.218 127.137 175.119 1.00 70.60  ? 3515 LEU A CG    1 
ATOM   13770 C  CD1   . LEU A 1 2298 ? 156.123 127.620 174.188 1.00 74.12  ? 3515 LEU A CD1   1 
ATOM   13771 C  CD2   . LEU A 1 2298 ? 158.296 128.197 175.271 1.00 73.87  ? 3515 LEU A CD2   1 
ATOM   13772 N  N     . VAL A 1 2299 ? 155.498 124.219 174.565 1.00 80.44  ? 3516 VAL A N     1 
ATOM   13773 C  CA    . VAL A 1 2299 ? 155.872 123.095 173.715 1.00 76.96  ? 3516 VAL A CA    1 
ATOM   13774 C  C     . VAL A 1 2299 ? 156.256 123.643 172.349 1.00 81.26  ? 3516 VAL A C     1 
ATOM   13775 O  O     . VAL A 1 2299 ? 155.497 124.412 171.749 1.00 86.98  ? 3516 VAL A O     1 
ATOM   13776 C  CB    . VAL A 1 2299 ? 154.736 122.062 173.598 1.00 70.18  ? 3516 VAL A CB    1 
ATOM   13777 C  CG1   . VAL A 1 2299 ? 155.140 120.940 172.675 1.00 79.27  ? 3516 VAL A CG1   1 
ATOM   13778 C  CG2   . VAL A 1 2299 ? 154.399 121.503 174.966 1.00 72.22  ? 3516 VAL A CG2   1 
ATOM   13779 N  N     . HIS A 1 2300 ? 157.426 123.243 171.858 1.00 83.70  ? 3517 HIS A N     1 
ATOM   13780 C  CA    . HIS A 1 2300 ? 158.034 123.838 170.678 1.00 91.36  ? 3517 HIS A CA    1 
ATOM   13781 C  C     . HIS A 1 2300 ? 158.277 122.777 169.611 1.00 99.34  ? 3517 HIS A C     1 
ATOM   13782 O  O     . HIS A 1 2300 ? 158.626 121.633 169.915 1.00 97.83  ? 3517 HIS A O     1 
ATOM   13783 C  CB    . HIS A 1 2300 ? 159.355 124.523 171.048 1.00 88.47  ? 3517 HIS A CB    1 
ATOM   13784 C  CG    . HIS A 1 2300 ? 159.931 125.370 169.958 1.00 95.15  ? 3517 HIS A CG    1 
ATOM   13785 N  ND1   . HIS A 1 2300 ? 159.160 125.939 168.968 1.00 102.24 ? 3517 HIS A ND1   1 
ATOM   13786 C  CD2   . HIS A 1 2300 ? 161.206 125.752 169.709 1.00 97.01  ? 3517 HIS A CD2   1 
ATOM   13787 C  CE1   . HIS A 1 2300 ? 159.936 126.632 168.153 1.00 108.92 ? 3517 HIS A CE1   1 
ATOM   13788 N  NE2   . HIS A 1 2300 ? 161.182 126.535 168.580 1.00 104.55 ? 3517 HIS A NE2   1 
ATOM   13789 N  N     . PHE A 1 2301 ? 158.083 123.171 168.353 1.00 104.57 ? 3518 PHE A N     1 
ATOM   13790 C  CA    . PHE A 1 2301 ? 158.323 122.309 167.200 1.00 103.98 ? 3518 PHE A CA    1 
ATOM   13791 C  C     . PHE A 1 2301 ? 159.234 123.047 166.231 1.00 109.38 ? 3518 PHE A C     1 
ATOM   13792 O  O     . PHE A 1 2301 ? 158.868 124.113 165.725 1.00 106.88 ? 3518 PHE A O     1 
ATOM   13793 C  CB    . PHE A 1 2301 ? 157.009 121.918 166.518 1.00 95.53  ? 3518 PHE A CB    1 
ATOM   13794 N  N     . VAL A 1 2302 ? 160.415 122.481 165.970 1.00 115.11 ? 3519 VAL A N     1 
ATOM   13795 C  CA    . VAL A 1 2302 ? 161.438 123.137 165.166 1.00 118.58 ? 3519 VAL A CA    1 
ATOM   13796 C  C     . VAL A 1 2302 ? 162.219 122.081 164.389 1.00 122.84 ? 3519 VAL A C     1 
ATOM   13797 O  O     . VAL A 1 2302 ? 162.386 120.942 164.832 1.00 118.47 ? 3519 VAL A O     1 
ATOM   13798 C  CB    . VAL A 1 2302 ? 162.380 124.004 166.046 1.00 117.26 ? 3519 VAL A CB    1 
ATOM   13799 C  CG1   . VAL A 1 2302 ? 163.223 123.138 166.981 1.00 113.52 ? 3519 VAL A CG1   1 
ATOM   13800 C  CG2   . VAL A 1 2302 ? 163.251 124.931 165.201 1.00 118.08 ? 3519 VAL A CG2   1 
ATOM   13801 N  N     . THR A 1 2303 ? 162.669 122.466 163.194 1.00 125.22 ? 3520 THR A N     1 
ATOM   13802 C  CA    . THR A 1 2303 ? 163.498 121.618 162.348 1.00 124.59 ? 3520 THR A CA    1 
ATOM   13803 C  C     . THR A 1 2303 ? 164.812 122.331 162.065 1.00 123.61 ? 3520 THR A C     1 
ATOM   13804 O  O     . THR A 1 2303 ? 164.829 123.542 161.825 1.00 121.17 ? 3520 THR A O     1 
ATOM   13805 C  CB    . THR A 1 2303 ? 162.798 121.274 161.027 1.00 121.28 ? 3520 THR A CB    1 
ATOM   13806 O  OG1   . THR A 1 2303 ? 162.531 122.478 160.297 1.00 122.76 ? 3520 THR A OG1   1 
ATOM   13807 C  CG2   . THR A 1 2303 ? 161.489 120.543 161.288 1.00 116.12 ? 3520 THR A CG2   1 
ATOM   13808 N  N     . ASN A 1 2304 ? 165.905 121.577 162.090 1.00 122.78 ? 3521 ASN A N     1 
ATOM   13809 C  CA    . ASN A 1 2304 ? 167.240 122.141 161.923 1.00 121.08 ? 3521 ASN A CA    1 
ATOM   13810 C  C     . ASN A 1 2304 ? 168.155 121.049 161.371 1.00 118.85 ? 3521 ASN A C     1 
ATOM   13811 O  O     . ASN A 1 2304 ? 167.677 120.025 160.869 1.00 117.26 ? 3521 ASN A O     1 
ATOM   13812 C  CB    . ASN A 1 2304 ? 167.746 122.727 163.253 1.00 118.29 ? 3521 ASN A CB    1 
ATOM   13813 N  N     . LYS A 1 2305 ? 169.469 121.279 161.448 1.00 118.29 ? 3522 LYS A N     1 
ATOM   13814 C  CA    . LYS A 1 2305 ? 170.435 120.290 160.976 1.00 114.62 ? 3522 LYS A CA    1 
ATOM   13815 C  C     . LYS A 1 2305 ? 170.358 119.003 161.789 1.00 114.73 ? 3522 LYS A C     1 
ATOM   13816 O  O     . LYS A 1 2305 ? 170.568 117.907 161.254 1.00 115.04 ? 3522 LYS A O     1 
ATOM   13817 C  CB    . LYS A 1 2305 ? 171.848 120.872 161.028 1.00 112.66 ? 3522 LYS A CB    1 
ATOM   13818 N  N     . GLU A 1 2306 ? 170.068 119.118 163.088 1.00 116.34 ? 3523 GLU A N     1 
ATOM   13819 C  CA    . GLU A 1 2306 ? 169.851 117.930 163.908 1.00 119.64 ? 3523 GLU A CA    1 
ATOM   13820 C  C     . GLU A 1 2306 ? 168.618 117.162 163.447 1.00 119.02 ? 3523 GLU A C     1 
ATOM   13821 O  O     . GLU A 1 2306 ? 168.617 115.925 163.438 1.00 117.71 ? 3523 GLU A O     1 
ATOM   13822 C  CB    . GLU A 1 2306 ? 169.722 118.325 165.379 1.00 116.98 ? 3523 GLU A CB    1 
ATOM   13823 N  N     . SER A 1 2307 ? 167.559 117.880 163.060 1.00 118.22 ? 3524 SER A N     1 
ATOM   13824 C  CA    . SER A 1 2307 ? 166.379 117.226 162.504 1.00 117.20 ? 3524 SER A CA    1 
ATOM   13825 C  C     . SER A 1 2307 ? 166.701 116.537 161.183 1.00 117.30 ? 3524 SER A C     1 
ATOM   13826 O  O     . SER A 1 2307 ? 166.190 115.445 160.907 1.00 119.14 ? 3524 SER A O     1 
ATOM   13827 C  CB    . SER A 1 2307 ? 165.253 118.243 162.320 1.00 114.60 ? 3524 SER A CB    1 
ATOM   13828 O  OG    . SER A 1 2307 ? 164.152 117.667 161.639 1.00 112.77 ? 3524 SER A OG    1 
ATOM   13829 N  N     . ILE A 1 2308 ? 167.545 117.162 160.357 1.00 116.16 ? 3525 ILE A N     1 
ATOM   13830 C  CA    . ILE A 1 2308 ? 167.984 116.543 159.108 1.00 113.67 ? 3525 ILE A CA    1 
ATOM   13831 C  C     . ILE A 1 2308 ? 168.739 115.251 159.392 1.00 112.88 ? 3525 ILE A C     1 
ATOM   13832 O  O     . ILE A 1 2308 ? 168.498 114.217 158.753 1.00 113.28 ? 3525 ILE A O     1 
ATOM   13833 C  CB    . ILE A 1 2308 ? 168.846 117.535 158.304 1.00 110.90 ? 3525 ILE A CB    1 
ATOM   13834 C  CG1   . ILE A 1 2308 ? 167.976 118.639 157.707 1.00 108.82 ? 3525 ILE A CG1   1 
ATOM   13835 C  CG2   . ILE A 1 2308 ? 169.623 116.821 157.206 1.00 103.46 ? 3525 ILE A CG2   1 
ATOM   13836 C  CD1   . ILE A 1 2308 ? 168.748 119.890 157.369 1.00 105.48 ? 3525 ILE A CD1   1 
ATOM   13837 N  N     . GLU A 1 2309 ? 169.654 115.293 160.366 1.00 112.07 ? 3526 GLU A N     1 
ATOM   13838 C  CA    . GLU A 1 2309 ? 170.414 114.107 160.747 1.00 113.17 ? 3526 GLU A CA    1 
ATOM   13839 C  C     . GLU A 1 2309 ? 169.496 112.999 161.245 1.00 113.85 ? 3526 GLU A C     1 
ATOM   13840 O  O     . GLU A 1 2309 ? 169.644 111.835 160.856 1.00 115.15 ? 3526 GLU A O     1 
ATOM   13841 C  CB    . GLU A 1 2309 ? 171.440 114.474 161.821 1.00 117.54 ? 3526 GLU A CB    1 
ATOM   13842 C  CG    . GLU A 1 2309 ? 172.087 113.277 162.501 1.00 118.22 ? 3526 GLU A CG    1 
ATOM   13843 C  CD    . GLU A 1 2309 ? 173.183 112.652 161.666 1.00 115.36 ? 3526 GLU A CD    1 
ATOM   13844 O  OE1   . GLU A 1 2309 ? 173.886 113.402 160.960 1.00 115.58 ? 3526 GLU A OE1   1 
ATOM   13845 O  OE2   . GLU A 1 2309 ? 173.341 111.413 161.714 1.00 111.47 ? 3526 GLU A OE2   1 
ATOM   13846 N  N     . THR A 1 2310 ? 168.525 113.350 162.093 1.00 113.08 ? 3527 THR A N     1 
ATOM   13847 C  CA    . THR A 1 2310 ? 167.603 112.352 162.626 1.00 114.28 ? 3527 THR A CA    1 
ATOM   13848 C  C     . THR A 1 2310 ? 166.749 111.735 161.523 1.00 115.41 ? 3527 THR A C     1 
ATOM   13849 O  O     . THR A 1 2310 ? 166.544 110.515 161.497 1.00 117.26 ? 3527 THR A O     1 
ATOM   13850 C  CB    . THR A 1 2310 ? 166.714 112.977 163.700 1.00 113.67 ? 3527 THR A CB    1 
ATOM   13851 N  N     . ARG A 1 2311 ? 166.255 112.560 160.595 1.00 115.40 ? 3528 ARG A N     1 
ATOM   13852 C  CA    . ARG A 1 2311 ? 165.406 112.051 159.522 1.00 112.72 ? 3528 ARG A CA    1 
ATOM   13853 C  C     . ARG A 1 2311 ? 166.182 111.129 158.588 1.00 111.66 ? 3528 ARG A C     1 
ATOM   13854 O  O     . ARG A 1 2311 ? 165.695 110.050 158.221 1.00 112.21 ? 3528 ARG A O     1 
ATOM   13855 C  CB    . ARG A 1 2311 ? 164.792 113.216 158.746 1.00 109.78 ? 3528 ARG A CB    1 
ATOM   13856 N  N     . ILE A 1 2312 ? 167.396 111.527 158.197 1.00 109.97 ? 3529 ILE A N     1 
ATOM   13857 C  CA    . ILE A 1 2312 ? 168.158 110.671 157.293 1.00 108.40 ? 3529 ILE A CA    1 
ATOM   13858 C  C     . ILE A 1 2312 ? 168.639 109.414 158.010 1.00 109.21 ? 3529 ILE A C     1 
ATOM   13859 O  O     . ILE A 1 2312 ? 168.748 108.350 157.389 1.00 111.06 ? 3529 ILE A O     1 
ATOM   13860 C  CB    . ILE A 1 2312 ? 169.320 111.440 156.634 1.00 106.27 ? 3529 ILE A CB    1 
ATOM   13861 C  CG1   . ILE A 1 2312 ? 170.383 111.839 157.655 1.00 108.54 ? 3529 ILE A CG1   1 
ATOM   13862 C  CG2   . ILE A 1 2312 ? 168.796 112.655 155.884 1.00 105.25 ? 3529 ILE A CG2   1 
ATOM   13863 C  CD1   . ILE A 1 2312 ? 171.682 112.238 157.025 1.00 104.78 ? 3529 ILE A CD1   1 
ATOM   13864 N  N     . PHE A 1 2313 ? 168.907 109.493 159.319 1.00 108.53 ? 3530 PHE A N     1 
ATOM   13865 C  CA    . PHE A 1 2313 ? 169.260 108.293 160.069 1.00 109.39 ? 3530 PHE A CA    1 
ATOM   13866 C  C     . PHE A 1 2313 ? 168.086 107.327 160.144 1.00 111.60 ? 3530 PHE A C     1 
ATOM   13867 O  O     . PHE A 1 2313 ? 168.267 106.112 160.000 1.00 112.43 ? 3530 PHE A O     1 
ATOM   13868 C  CB    . PHE A 1 2313 ? 169.737 108.669 161.471 1.00 110.79 ? 3530 PHE A CB    1 
ATOM   13869 N  N     . ASP A 1 2314 ? 166.875 107.851 160.360 1.00 114.71 ? 3531 ASP A N     1 
ATOM   13870 C  CA    . ASP A 1 2314 ? 165.688 107.002 160.371 1.00 114.12 ? 3531 ASP A CA    1 
ATOM   13871 C  C     . ASP A 1 2314 ? 165.466 106.347 159.014 1.00 111.61 ? 3531 ASP A C     1 
ATOM   13872 O  O     . ASP A 1 2314 ? 165.161 105.151 158.938 1.00 111.41 ? 3531 ASP A O     1 
ATOM   13873 C  CB    . ASP A 1 2314 ? 164.461 107.818 160.777 1.00 116.28 ? 3531 ASP A CB    1 
ATOM   13874 C  CG    . ASP A 1 2314 ? 164.433 108.131 162.260 1.00 119.45 ? 3531 ASP A CG    1 
ATOM   13875 O  OD1   . ASP A 1 2314 ? 164.968 107.325 163.049 1.00 120.01 ? 3531 ASP A OD1   1 
ATOM   13876 O  OD2   . ASP A 1 2314 ? 163.875 109.184 162.635 1.00 115.67 ? 3531 ASP A OD2   1 
ATOM   13877 N  N     . ILE A 1 2315 ? 165.637 107.110 157.930 1.00 112.20 ? 3532 ILE A N     1 
ATOM   13878 C  CA    . ILE A 1 2315 ? 165.450 106.558 156.588 1.00 110.55 ? 3532 ILE A CA    1 
ATOM   13879 C  C     . ILE A 1 2315 ? 166.490 105.479 156.297 1.00 111.12 ? 3532 ILE A C     1 
ATOM   13880 O  O     . ILE A 1 2315 ? 166.166 104.411 155.755 1.00 113.02 ? 3532 ILE A O     1 
ATOM   13881 C  CB    . ILE A 1 2315 ? 165.488 107.689 155.542 1.00 107.41 ? 3532 ILE A CB    1 
ATOM   13882 C  CG1   . ILE A 1 2315 ? 164.189 108.496 155.591 1.00 104.12 ? 3532 ILE A CG1   1 
ATOM   13883 C  CG2   . ILE A 1 2315 ? 165.717 107.138 154.140 1.00 104.79 ? 3532 ILE A CG2   1 
ATOM   13884 C  CD1   . ILE A 1 2315 ? 164.112 109.586 154.553 1.00 100.68 ? 3532 ILE A CD1   1 
ATOM   13885 N  N     . THR A 1 2316 ? 167.753 105.738 156.656 1.00 109.60 ? 3533 THR A N     1 
ATOM   13886 C  CA    . THR A 1 2316 ? 168.815 104.768 156.412 1.00 109.92 ? 3533 THR A CA    1 
ATOM   13887 C  C     . THR A 1 2316 ? 168.595 103.492 157.215 1.00 114.11 ? 3533 THR A C     1 
ATOM   13888 O  O     . THR A 1 2316 ? 168.723 102.385 156.679 1.00 116.42 ? 3533 THR A O     1 
ATOM   13889 C  CB    . THR A 1 2316 ? 170.173 105.391 156.742 1.00 107.54 ? 3533 THR A CB    1 
ATOM   13890 O  OG1   . THR A 1 2316 ? 170.466 106.427 155.795 1.00 103.09 ? 3533 THR A OG1   1 
ATOM   13891 C  CG2   . THR A 1 2316 ? 171.280 104.347 156.690 1.00 108.86 ? 3533 THR A CG2   1 
ATOM   13892 N  N     . LEU A 1 2317 ? 168.225 103.624 158.493 1.00 113.02 ? 3534 LEU A N     1 
ATOM   13893 C  CA    . LEU A 1 2317 ? 167.957 102.445 159.309 1.00 111.94 ? 3534 LEU A CA    1 
ATOM   13894 C  C     . LEU A 1 2317 ? 166.724 101.691 158.827 1.00 113.24 ? 3534 LEU A C     1 
ATOM   13895 O  O     . LEU A 1 2317 ? 166.652 100.466 158.977 1.00 117.30 ? 3534 LEU A O     1 
ATOM   13896 C  CB    . LEU A 1 2317 ? 167.793 102.845 160.774 1.00 112.59 ? 3534 LEU A CB    1 
ATOM   13897 N  N     . THR A 1 2318 ? 165.747 102.397 158.252 1.00 113.82 ? 3535 THR A N     1 
ATOM   13898 C  CA    . THR A 1 2318 ? 164.538 101.735 157.780 1.00 112.49 ? 3535 THR A CA    1 
ATOM   13899 C  C     . THR A 1 2318 ? 164.772 100.957 156.489 1.00 111.11 ? 3535 THR A C     1 
ATOM   13900 O  O     . THR A 1 2318 ? 164.307 99.819  156.361 1.00 111.68 ? 3535 THR A O     1 
ATOM   13901 C  CB    . THR A 1 2318 ? 163.424 102.764 157.579 1.00 113.63 ? 3535 THR A CB    1 
ATOM   13902 O  OG1   . THR A 1 2318 ? 163.276 103.549 158.769 1.00 118.02 ? 3535 THR A OG1   1 
ATOM   13903 C  CG2   . THR A 1 2318 ? 162.104 102.072 157.271 1.00 107.33 ? 3535 THR A CG2   1 
ATOM   13904 N  N     . GLU A 1 2319 ? 165.491 101.537 155.522 1.00 111.24 ? 3536 GLU A N     1 
ATOM   13905 C  CA    . GLU A 1 2319 ? 165.512 100.950 154.186 1.00 110.27 ? 3536 GLU A CA    1 
ATOM   13906 C  C     . GLU A 1 2319 ? 166.905 100.702 153.612 1.00 110.23 ? 3536 GLU A C     1 
ATOM   13907 O  O     . GLU A 1 2319 ? 167.020 100.434 152.410 1.00 111.35 ? 3536 GLU A O     1 
ATOM   13908 C  CB    . GLU A 1 2319 ? 164.708 101.823 153.213 1.00 111.93 ? 3536 GLU A CB    1 
ATOM   13909 C  CG    . GLU A 1 2319 ? 165.370 103.137 152.849 1.00 110.80 ? 3536 GLU A CG    1 
ATOM   13910 C  CD    . GLU A 1 2319 ? 164.779 103.754 151.600 1.00 111.98 ? 3536 GLU A CD    1 
ATOM   13911 O  OE1   . GLU A 1 2319 ? 164.354 102.995 150.704 1.00 112.78 ? 3536 GLU A OE1   1 
ATOM   13912 O  OE2   . GLU A 1 2319 ? 164.744 104.998 151.511 1.00 111.54 ? 3536 GLU A OE2   1 
ATOM   13913 N  N     . GLU A 1 2320 ? 167.962 100.753 154.420 1.00 112.17 ? 3537 GLU A N     1 
ATOM   13914 C  CA    . GLU A 1 2320 ? 169.297 100.460 153.911 1.00 114.43 ? 3537 GLU A CA    1 
ATOM   13915 C  C     . GLU A 1 2320 ? 169.786 99.078  154.321 1.00 115.70 ? 3537 GLU A C     1 
ATOM   13916 O  O     . GLU A 1 2320 ? 170.167 98.275  153.464 1.00 115.18 ? 3537 GLU A O     1 
ATOM   13917 C  CB    . GLU A 1 2320 ? 170.295 101.529 154.377 1.00 114.54 ? 3537 GLU A CB    1 
ATOM   13918 C  CG    . GLU A 1 2320 ? 171.758 101.114 154.253 1.00 116.01 ? 3537 GLU A CG    1 
ATOM   13919 C  CD    . GLU A 1 2320 ? 172.196 100.905 152.813 1.00 112.59 ? 3537 GLU A CD    1 
ATOM   13920 O  OE1   . GLU A 1 2320 ? 171.669 101.599 151.918 1.00 110.65 ? 3537 GLU A OE1   1 
ATOM   13921 O  OE2   . GLU A 1 2320 ? 173.067 100.042 152.575 1.00 110.08 ? 3537 GLU A OE2   1 
ATOM   13922 N  N     . ASN A 1 2321 ? 169.781 98.781  155.616 1.00 116.92 ? 3538 ASN A N     1 
ATOM   13923 C  CA    . ASN A 1 2321 ? 170.226 97.492  156.124 1.00 119.84 ? 3538 ASN A CA    1 
ATOM   13924 C  C     . ASN A 1 2321 ? 169.037 96.696  156.647 1.00 125.40 ? 3538 ASN A C     1 
ATOM   13925 O  O     . ASN A 1 2321 ? 168.201 97.225  157.387 1.00 124.75 ? 3538 ASN A O     1 
ATOM   13926 C  CB    . ASN A 1 2321 ? 171.287 97.671  157.214 1.00 120.47 ? 3538 ASN A CB    1 
ATOM   13927 C  CG    . ASN A 1 2321 ? 170.901 98.712  158.251 1.00 119.79 ? 3538 ASN A CG    1 
ATOM   13928 O  OD1   . ASN A 1 2321 ? 169.828 99.311  158.187 1.00 118.79 ? 3538 ASN A OD1   1 
ATOM   13929 N  ND2   . ASN A 1 2321 ? 171.786 98.934  159.216 1.00 120.26 ? 3538 ASN A ND2   1 
ATOM   13930 N  N     . ALA A 1 2322 ? 168.957 95.427  156.244 1.00 129.19 ? 3539 ALA A N     1 
ATOM   13931 C  CA    . ALA A 1 2322 ? 167.868 94.571  156.696 1.00 131.32 ? 3539 ALA A CA    1 
ATOM   13932 C  C     . ALA A 1 2322 ? 168.047 94.139  158.145 1.00 134.16 ? 3539 ALA A C     1 
ATOM   13933 O  O     . ALA A 1 2322 ? 167.056 93.857  158.828 1.00 135.38 ? 3539 ALA A O     1 
ATOM   13934 C  CB    . ALA A 1 2322 ? 167.752 93.343  155.793 1.00 127.53 ? 3539 ALA A CB    1 
ATOM   13935 N  N     . GLU A 1 2323 ? 169.293 94.080  158.623 1.00 133.47 ? 3540 GLU A N     1 
ATOM   13936 C  CA    . GLU A 1 2323 ? 169.551 93.649  159.993 1.00 133.42 ? 3540 GLU A CA    1 
ATOM   13937 C  C     . GLU A 1 2323 ? 168.969 94.629  161.005 1.00 135.94 ? 3540 GLU A C     1 
ATOM   13938 O  O     . GLU A 1 2323 ? 168.347 94.219  161.991 1.00 138.66 ? 3540 GLU A O     1 
ATOM   13939 C  CB    . GLU A 1 2323 ? 171.054 93.475  160.213 1.00 129.31 ? 3540 GLU A CB    1 
ATOM   13940 N  N     . MET A 1 2324 ? 169.157 95.932  160.774 1.00 133.17 ? 3541 MET A N     1 
ATOM   13941 C  CA    . MET A 1 2324 ? 168.652 96.931  161.713 1.00 132.97 ? 3541 MET A CA    1 
ATOM   13942 C  C     . MET A 1 2324 ? 167.129 96.953  161.741 1.00 134.98 ? 3541 MET A C     1 
ATOM   13943 O  O     . MET A 1 2324 ? 166.526 97.047  162.817 1.00 136.19 ? 3541 MET A O     1 
ATOM   13944 C  CB    . MET A 1 2324 ? 169.201 98.312  161.357 1.00 129.94 ? 3541 MET A CB    1 
ATOM   13945 N  N     . GLN A 1 2325 ? 166.490 96.863  160.571 1.00 134.63 ? 3542 GLN A N     1 
ATOM   13946 C  CA    . GLN A 1 2325 ? 165.032 96.827  160.520 1.00 137.56 ? 3542 GLN A CA    1 
ATOM   13947 C  C     . GLN A 1 2325 ? 164.485 95.563  161.173 1.00 141.49 ? 3542 GLN A C     1 
ATOM   13948 O  O     . GLN A 1 2325 ? 163.479 95.613  161.893 1.00 143.35 ? 3542 GLN A O     1 
ATOM   13949 C  CB    . GLN A 1 2325 ? 164.556 96.933  159.072 1.00 131.50 ? 3542 GLN A CB    1 
ATOM   13950 N  N     . ARG A 1 2326 ? 165.140 94.421  160.936 1.00 141.00 ? 3543 ARG A N     1 
ATOM   13951 C  CA    . ARG A 1 2326 ? 164.711 93.173  161.558 1.00 142.08 ? 3543 ARG A CA    1 
ATOM   13952 C  C     . ARG A 1 2326 ? 164.856 93.231  163.073 1.00 143.88 ? 3543 ARG A C     1 
ATOM   13953 O  O     . ARG A 1 2326 ? 163.976 92.765  163.804 1.00 145.00 ? 3543 ARG A O     1 
ATOM   13954 C  CB    . ARG A 1 2326 ? 165.508 92.001  160.985 1.00 140.12 ? 3543 ARG A CB    1 
ATOM   13955 N  N     . LYS A 1 2327 ? 165.955 93.811  163.565 1.00 142.90 ? 3544 LYS A N     1 
ATOM   13956 C  CA    . LYS A 1 2327 ? 166.139 93.943  165.006 1.00 143.81 ? 3544 LYS A CA    1 
ATOM   13957 C  C     . LYS A 1 2327 ? 165.148 94.925  165.621 1.00 146.08 ? 3544 LYS A C     1 
ATOM   13958 O  O     . LYS A 1 2327 ? 164.681 94.701  166.741 1.00 146.78 ? 3544 LYS A O     1 
ATOM   13959 C  CB    . LYS A 1 2327 ? 167.574 94.365  165.322 1.00 144.67 ? 3544 LYS A CB    1 
ATOM   13960 C  CG    . LYS A 1 2327 ? 168.480 93.214  165.742 1.00 143.87 ? 3544 LYS A CG    1 
ATOM   13961 C  CD    . LYS A 1 2327 ? 168.806 92.293  164.579 1.00 144.18 ? 3544 LYS A CD    1 
ATOM   13962 C  CE    . LYS A 1 2327 ? 169.785 91.207  164.993 1.00 149.26 ? 3544 LYS A CE    1 
ATOM   13963 N  NZ    . LYS A 1 2327 ? 170.025 90.230  163.896 1.00 154.48 ? 3544 LYS A NZ    1 
ATOM   13964 N  N     . ARG A 1 2328 ? 164.813 96.009  164.914 1.00 147.17 ? 3545 ARG A N     1 
ATOM   13965 C  CA    . ARG A 1 2328 ? 163.800 96.934  165.417 1.00 147.76 ? 3545 ARG A CA    1 
ATOM   13966 C  C     . ARG A 1 2328 ? 162.431 96.268  165.492 1.00 149.20 ? 3545 ARG A C     1 
ATOM   13967 O  O     . ARG A 1 2328 ? 161.703 96.434  166.482 1.00 150.65 ? 3545 ARG A O     1 
ATOM   13968 C  CB    . ARG A 1 2328 ? 163.743 98.181  164.536 1.00 142.35 ? 3545 ARG A CB    1 
ATOM   13969 N  N     . GLU A 1 2329 ? 162.068 95.504  164.456 1.00 148.60 ? 3546 GLU A N     1 
ATOM   13970 C  CA    . GLU A 1 2329 ? 160.806 94.770  164.478 1.00 148.87 ? 3546 GLU A CA    1 
ATOM   13971 C  C     . GLU A 1 2329 ? 160.795 93.729  165.589 1.00 150.82 ? 3546 GLU A C     1 
ATOM   13972 O  O     . GLU A 1 2329 ? 159.778 93.546  166.268 1.00 152.29 ? 3546 GLU A O     1 
ATOM   13973 C  CB    . GLU A 1 2329 ? 160.559 94.112  163.121 1.00 149.11 ? 3546 GLU A CB    1 
ATOM   13974 N  N     . ASP A 1 2330 ? 161.922 93.041  165.793 1.00 150.32 ? 3547 ASP A N     1 
ATOM   13975 C  CA    . ASP A 1 2330 ? 162.017 92.053  166.862 1.00 150.95 ? 3547 ASP A CA    1 
ATOM   13976 C  C     . ASP A 1 2330 ? 161.904 92.704  168.234 1.00 152.42 ? 3547 ASP A C     1 
ATOM   13977 O  O     . ASP A 1 2330 ? 161.278 92.144  169.137 1.00 156.17 ? 3547 ASP A O     1 
ATOM   13978 C  CB    . ASP A 1 2330 ? 163.329 91.277  166.743 1.00 148.57 ? 3547 ASP A CB    1 
ATOM   13979 N  N     . LEU A 1 2331 ? 162.502 93.885  168.411 1.00 149.40 ? 3548 LEU A N     1 
ATOM   13980 C  CA    . LEU A 1 2331 ? 162.399 94.590  169.686 1.00 148.89 ? 3548 LEU A CA    1 
ATOM   13981 C  C     . LEU A 1 2331 ? 160.971 95.053  169.951 1.00 151.76 ? 3548 LEU A C     1 
ATOM   13982 O  O     . LEU A 1 2331 ? 160.482 94.953  171.084 1.00 152.28 ? 3548 LEU A O     1 
ATOM   13983 C  CB    . LEU A 1 2331 ? 163.361 95.776  169.708 1.00 147.57 ? 3548 LEU A CB    1 
ATOM   13984 N  N     . ILE A 1 2332 ? 160.288 95.560  168.921 1.00 153.43 ? 3549 ILE A N     1 
ATOM   13985 C  CA    . ILE A 1 2332 ? 158.892 95.966  169.081 1.00 154.65 ? 3549 ILE A CA    1 
ATOM   13986 C  C     . ILE A 1 2332 ? 158.019 94.760  169.415 1.00 155.89 ? 3549 ILE A C     1 
ATOM   13987 O  O     . ILE A 1 2332 ? 157.145 94.827  170.291 1.00 156.80 ? 3549 ILE A O     1 
ATOM   13988 C  CB    . ILE A 1 2332 ? 158.396 96.692  167.817 1.00 151.90 ? 3549 ILE A CB    1 
ATOM   13989 N  N     . LYS A 1 2333 ? 158.249 93.638  168.726 1.00 156.01 ? 3550 LYS A N     1 
ATOM   13990 C  CA    . LYS A 1 2333 ? 157.493 92.421  169.001 1.00 155.83 ? 3550 LYS A CA    1 
ATOM   13991 C  C     . LYS A 1 2333 ? 157.778 91.896  170.402 1.00 156.67 ? 3550 LYS A C     1 
ATOM   13992 O  O     . LYS A 1 2333 ? 156.874 91.393  171.076 1.00 157.16 ? 3550 LYS A O     1 
ATOM   13993 C  CB    . LYS A 1 2333 ? 157.817 91.356  167.952 1.00 154.97 ? 3550 LYS A CB    1 
ATOM   13994 N  N     . LEU A 1 2334 ? 159.029 92.000  170.856 1.00 157.03 ? 3551 LEU A N     1 
ATOM   13995 C  CA    . LEU A 1 2334 ? 159.379 91.562  172.203 1.00 157.18 ? 3551 LEU A CA    1 
ATOM   13996 C  C     . LEU A 1 2334 ? 158.720 92.439  173.260 1.00 158.66 ? 3551 LEU A C     1 
ATOM   13997 O  O     . LEU A 1 2334 ? 158.272 91.936  174.294 1.00 159.31 ? 3551 LEU A O     1 
ATOM   13998 C  CB    . LEU A 1 2334 ? 160.897 91.561  172.376 1.00 155.80 ? 3551 LEU A CB    1 
ATOM   13999 N  N     . ASN A 1 2335 ? 158.658 93.752  173.021 1.00 158.80 ? 3552 ASN A N     1 
ATOM   14000 C  CA    . ASN A 1 2335 ? 157.961 94.638  173.950 1.00 159.07 ? 3552 ASN A CA    1 
ATOM   14001 C  C     . ASN A 1 2335 ? 156.470 94.319  174.005 1.00 161.44 ? 3552 ASN A C     1 
ATOM   14002 O  O     . ASN A 1 2335 ? 155.873 94.278  175.090 1.00 160.55 ? 3552 ASN A O     1 
ATOM   14003 C  CB    . ASN A 1 2335 ? 158.185 96.097  173.552 1.00 156.14 ? 3552 ASN A CB    1 
ATOM   14004 N  N     . THR A 1 2336 ? 155.857 94.080  172.840 1.00 162.91 ? 3553 THR A N     1 
ATOM   14005 C  CA    . THR A 1 2336 ? 154.444 93.709  172.807 1.00 160.00 ? 3553 THR A CA    1 
ATOM   14006 C  C     . THR A 1 2336 ? 154.204 92.376  173.507 1.00 161.71 ? 3553 THR A C     1 
ATOM   14007 O  O     . THR A 1 2336 ? 153.216 92.217  174.234 1.00 162.80 ? 3553 THR A O     1 
ATOM   14008 C  CB    . THR A 1 2336 ? 153.949 93.650  171.362 1.00 154.56 ? 3553 THR A CB    1 
ATOM   14009 N  N     . GLU A 1 2337 ? 155.103 91.410  173.304 1.00 161.12 ? 3554 GLU A N     1 
ATOM   14010 C  CA    . GLU A 1 2337 ? 154.976 90.110  173.954 1.00 158.34 ? 3554 GLU A CA    1 
ATOM   14011 C  C     . GLU A 1 2337 ? 155.151 90.224  175.462 1.00 157.40 ? 3554 GLU A C     1 
ATOM   14012 O  O     . GLU A 1 2337 ? 154.464 89.534  176.219 1.00 156.22 ? 3554 GLU A O     1 
ATOM   14013 C  CB    . GLU A 1 2337 ? 155.993 89.130  173.369 1.00 157.70 ? 3554 GLU A CB    1 
ATOM   14014 N  N     . TYR A 1 2338 ? 156.069 91.081  175.916 1.00 159.27 ? 3555 TYR A N     1 
ATOM   14015 C  CA    . TYR A 1 2338 ? 156.242 91.297  177.349 1.00 161.46 ? 3555 TYR A CA    1 
ATOM   14016 C  C     . TYR A 1 2338 ? 155.005 91.939  177.965 1.00 161.57 ? 3555 TYR A C     1 
ATOM   14017 O  O     . TYR A 1 2338 ? 154.575 91.546  179.057 1.00 159.00 ? 3555 TYR A O     1 
ATOM   14018 C  CB    . TYR A 1 2338 ? 157.478 92.158  177.604 1.00 161.69 ? 3555 TYR A CB    1 
ATOM   14019 N  N     . ARG A 1 2339 ? 154.419 92.926  177.279 1.00 162.93 ? 3556 ARG A N     1 
ATOM   14020 C  CA    . ARG A 1 2339 ? 153.189 93.540  177.775 1.00 161.56 ? 3556 ARG A CA    1 
ATOM   14021 C  C     . ARG A 1 2339 ? 152.043 92.533  177.821 1.00 161.87 ? 3556 ARG A C     1 
ATOM   14022 O  O     . ARG A 1 2339 ? 151.283 92.486  178.799 1.00 160.26 ? 3556 ARG A O     1 
ATOM   14023 C  CB    . ARG A 1 2339 ? 152.815 94.740  176.905 1.00 159.29 ? 3556 ARG A CB    1 
ATOM   14024 N  N     . LEU A 1 2340 ? 151.913 91.710  176.776 1.00 163.50 ? 3557 LEU A N     1 
ATOM   14025 C  CA    . LEU A 1 2340 ? 150.870 90.691  176.749 1.00 160.38 ? 3557 LEU A CA    1 
ATOM   14026 C  C     . LEU A 1 2340 ? 151.086 89.644  177.835 1.00 158.71 ? 3557 LEU A C     1 
ATOM   14027 O  O     . LEU A 1 2340 ? 150.123 89.176  178.451 1.00 156.52 ? 3557 LEU A O     1 
ATOM   14028 C  CB    . LEU A 1 2340 ? 150.816 90.032  175.371 1.00 158.34 ? 3557 LEU A CB    1 
ATOM   14029 N  N     . LYS A 1 2341 ? 152.342 89.263  178.081 1.00 159.66 ? 3558 LYS A N     1 
ATOM   14030 C  CA    . LYS A 1 2341 ? 152.643 88.298  179.132 1.00 158.30 ? 3558 LYS A CA    1 
ATOM   14031 C  C     . LYS A 1 2341 ? 152.338 88.869  180.510 1.00 156.80 ? 3558 LYS A C     1 
ATOM   14032 O  O     . LYS A 1 2341 ? 151.836 88.153  181.382 1.00 154.89 ? 3558 LYS A O     1 
ATOM   14033 C  CB    . LYS A 1 2341 ? 154.106 87.864  179.042 1.00 160.11 ? 3558 LYS A CB    1 
ATOM   14034 N  N     . LEU A 1 2342 ? 152.637 90.153  180.726 1.00 158.35 ? 3559 LEU A N     1 
ATOM   14035 C  CA    . LEU A 1 2342 ? 152.292 90.787  181.995 1.00 158.51 ? 3559 LEU A CA    1 
ATOM   14036 C  C     . LEU A 1 2342 ? 150.781 90.844  182.190 1.00 157.11 ? 3559 LEU A C     1 
ATOM   14037 O  O     . LEU A 1 2342 ? 150.278 90.576  183.290 1.00 155.49 ? 3559 LEU A O     1 
ATOM   14038 C  CB    . LEU A 1 2342 ? 152.898 92.188  182.064 1.00 157.48 ? 3559 LEU A CB    1 
ATOM   14039 N  N     . LYS A 1 2343 ? 150.040 91.181  181.128 1.00 156.60 ? 3560 LYS A N     1 
ATOM   14040 C  CA    . LYS A 1 2343 ? 148.582 91.202  181.217 1.00 153.76 ? 3560 LYS A CA    1 
ATOM   14041 C  C     . LYS A 1 2343 ? 148.020 89.811  181.495 1.00 154.50 ? 3560 LYS A C     1 
ATOM   14042 O  O     . LYS A 1 2343 ? 147.103 89.654  182.311 1.00 152.24 ? 3560 LYS A O     1 
ATOM   14043 C  CB    . LYS A 1 2343 ? 147.987 91.774  179.931 1.00 152.34 ? 3560 LYS A CB    1 
ATOM   14044 N  N     . ASN A 1 2344 ? 148.563 88.789  180.827 1.00 156.44 ? 3561 ASN A N     1 
ATOM   14045 C  CA    . ASN A 1 2344 ? 148.103 87.421  181.042 1.00 153.28 ? 3561 ASN A CA    1 
ATOM   14046 C  C     . ASN A 1 2344 ? 148.433 86.938  182.448 1.00 150.01 ? 3561 ASN A C     1 
ATOM   14047 O  O     . ASN A 1 2344 ? 147.631 86.231  183.067 1.00 148.05 ? 3561 ASN A O     1 
ATOM   14048 C  CB    . ASN A 1 2344 ? 148.718 86.491  179.996 1.00 152.49 ? 3561 ASN A CB    1 
ATOM   14049 N  N     . LEU A 1 2345 ? 149.609 87.301  182.966 1.00 151.02 ? 3562 LEU A N     1 
ATOM   14050 C  CA    . LEU A 1 2345 ? 149.969 86.937  184.332 1.00 150.32 ? 3562 LEU A CA    1 
ATOM   14051 C  C     . LEU A 1 2345 ? 149.056 87.617  185.343 1.00 151.28 ? 3562 LEU A C     1 
ATOM   14052 O  O     . LEU A 1 2345 ? 148.648 86.996  186.332 1.00 152.16 ? 3562 LEU A O     1 
ATOM   14053 C  CB    . LEU A 1 2345 ? 151.431 87.291  184.602 1.00 149.70 ? 3562 LEU A CB    1 
ATOM   14054 N  N     . GLU A 1 2346 ? 148.723 88.891  185.113 1.00 151.57 ? 3563 GLU A N     1 
ATOM   14055 C  CA    . GLU A 1 2346 ? 147.788 89.583  185.996 1.00 149.04 ? 3563 GLU A CA    1 
ATOM   14056 C  C     . GLU A 1 2346 ? 146.407 88.939  185.956 1.00 148.37 ? 3563 GLU A C     1 
ATOM   14057 O  O     . GLU A 1 2346 ? 145.766 88.761  187.000 1.00 147.01 ? 3563 GLU A O     1 
ATOM   14058 C  CB    . GLU A 1 2346 ? 147.702 91.061  185.615 1.00 150.07 ? 3563 GLU A CB    1 
ATOM   14059 N  N     . LYS A 1 2347 ? 145.936 88.576  184.759 1.00 149.66 ? 3564 LYS A N     1 
ATOM   14060 C  CA    . LYS A 1 2347 ? 144.636 87.920  184.636 1.00 149.01 ? 3564 LYS A CA    1 
ATOM   14061 C  C     . LYS A 1 2347 ? 144.636 86.551  185.307 1.00 149.54 ? 3564 LYS A C     1 
ATOM   14062 O  O     . LYS A 1 2347 ? 143.655 86.173  185.958 1.00 149.24 ? 3564 LYS A O     1 
ATOM   14063 C  CB    . LYS A 1 2347 ? 144.247 87.797  183.163 1.00 145.54 ? 3564 LYS A CB    1 
ATOM   14064 N  N     . ARG A 1 2348 ? 145.729 85.796  185.163 1.00 149.38 ? 3565 ARG A N     1 
ATOM   14065 C  CA    . ARG A 1 2348 ? 145.828 84.490  185.807 1.00 146.68 ? 3565 ARG A CA    1 
ATOM   14066 C  C     . ARG A 1 2348 ? 145.875 84.621  187.324 1.00 147.29 ? 3565 ARG A C     1 
ATOM   14067 O  O     . ARG A 1 2348 ? 145.276 83.811  188.039 1.00 146.95 ? 3565 ARG A O     1 
ATOM   14068 C  CB    . ARG A 1 2348 ? 147.061 83.746  185.293 1.00 145.57 ? 3565 ARG A CB    1 
ATOM   14069 N  N     . LEU A 1 2349 ? 146.585 85.633  187.832 1.00 147.87 ? 3566 LEU A N     1 
ATOM   14070 C  CA    . LEU A 1 2349 ? 146.610 85.872  189.272 1.00 144.72 ? 3566 LEU A CA    1 
ATOM   14071 C  C     . LEU A 1 2349 ? 145.231 86.259  189.790 1.00 147.25 ? 3566 LEU A C     1 
ATOM   14072 O  O     . LEU A 1 2349 ? 144.817 85.811  190.866 1.00 147.22 ? 3566 LEU A O     1 
ATOM   14073 C  CB    . LEU A 1 2349 ? 147.635 86.956  189.605 1.00 140.64 ? 3566 LEU A CB    1 
ATOM   14074 N  N     . LEU A 1 2350 ? 144.505 87.090  189.036 1.00 149.31 ? 3567 LEU A N     1 
ATOM   14075 C  CA    . LEU A 1 2350 ? 143.145 87.454  189.426 1.00 148.57 ? 3567 LEU A CA    1 
ATOM   14076 C  C     . LEU A 1 2350 ? 142.223 86.239  189.425 1.00 149.29 ? 3567 LEU A C     1 
ATOM   14077 O  O     . LEU A 1 2350 ? 141.385 86.086  190.322 1.00 148.20 ? 3567 LEU A O     1 
ATOM   14078 C  CB    . LEU A 1 2350 ? 142.605 88.539  188.494 1.00 146.51 ? 3567 LEU A CB    1 
ATOM   14079 N  N     . GLU A 1 2351 ? 142.361 85.368  188.422 1.00 151.06 ? 3568 GLU A N     1 
ATOM   14080 C  CA    . GLU A 1 2351 ? 141.551 84.154  188.366 1.00 150.02 ? 3568 GLU A CA    1 
ATOM   14081 C  C     . GLU A 1 2351 ? 141.876 83.211  189.520 1.00 148.77 ? 3568 GLU A C     1 
ATOM   14082 O  O     . GLU A 1 2351 ? 140.973 82.591  190.094 1.00 147.30 ? 3568 GLU A O     1 
ATOM   14083 C  CB    . GLU A 1 2351 ? 141.754 83.450  187.025 1.00 148.29 ? 3568 GLU A CB    1 
ATOM   14084 N  N     . GLU A 1 2352 ? 143.161 83.082  189.863 1.00 147.81 ? 3569 GLU A N     1 
ATOM   14085 C  CA    . GLU A 1 2352 ? 143.553 82.231  190.983 1.00 144.42 ? 3569 GLU A CA    1 
ATOM   14086 C  C     . GLU A 1 2352 ? 143.050 82.790  192.308 1.00 144.17 ? 3569 GLU A C     1 
ATOM   14087 O  O     . GLU A 1 2352 ? 142.633 82.030  193.190 1.00 143.54 ? 3569 GLU A O     1 
ATOM   14088 C  CB    . GLU A 1 2352 ? 145.073 82.069  191.010 1.00 142.58 ? 3569 GLU A CB    1 
ATOM   14089 N  N     . LEU A 1 2353 ? 143.089 84.116  192.470 1.00 144.91 ? 3570 LEU A N     1 
ATOM   14090 C  CA    . LEU A 1 2353 ? 142.566 84.728  193.687 1.00 144.06 ? 3570 LEU A CA    1 
ATOM   14091 C  C     . LEU A 1 2353 ? 141.050 84.608  193.771 1.00 144.19 ? 3570 LEU A C     1 
ATOM   14092 O  O     . LEU A 1 2353 ? 140.501 84.479  194.871 1.00 143.03 ? 3570 LEU A O     1 
ATOM   14093 C  CB    . LEU A 1 2353 ? 142.988 86.195  193.760 1.00 145.49 ? 3570 LEU A CB    1 
ATOM   14094 N  N     . ASN A 1 2354 ? 140.359 84.652  192.629 1.00 145.34 ? 3571 ASN A N     1 
ATOM   14095 C  CA    . ASN A 1 2354 ? 138.906 84.518  192.640 1.00 143.96 ? 3571 ASN A CA    1 
ATOM   14096 C  C     . ASN A 1 2354 ? 138.472 83.080  192.893 1.00 143.99 ? 3571 ASN A C     1 
ATOM   14097 O  O     . ASN A 1 2354 ? 137.384 82.849  193.432 1.00 143.91 ? 3571 ASN A O     1 
ATOM   14098 C  CB    . ASN A 1 2354 ? 138.323 85.024  191.321 1.00 143.94 ? 3571 ASN A CB    1 
ATOM   14099 N  N     . ASN A 1 2355 ? 139.298 82.107  192.515 1.00 143.86 ? 3572 ASN A N     1 
ATOM   14100 C  CA    . ASN A 1 2355 ? 138.974 80.699  192.693 1.00 141.32 ? 3572 ASN A CA    1 
ATOM   14101 C  C     . ASN A 1 2355 ? 139.537 80.115  193.982 1.00 140.28 ? 3572 ASN A C     1 
ATOM   14102 O  O     . ASN A 1 2355 ? 139.367 78.916  194.227 1.00 140.32 ? 3572 ASN A O     1 
ATOM   14103 C  CB    . ASN A 1 2355 ? 139.483 79.886  191.498 1.00 138.59 ? 3572 ASN A CB    1 
ATOM   14104 N  N     . SER A 1 2356 ? 140.198 80.923  194.805 1.00 139.44 ? 3573 SER A N     1 
ATOM   14105 C  CA    . SER A 1 2356 ? 140.770 80.438  196.056 1.00 133.47 ? 3573 SER A CA    1 
ATOM   14106 C  C     . SER A 1 2356 ? 139.700 80.324  197.137 1.00 132.03 ? 3573 SER A C     1 
ATOM   14107 O  O     . SER A 1 2356 ? 139.103 79.263  197.324 1.00 135.13 ? 3573 SER A O     1 
ATOM   14108 C  CB    . SER A 1 2356 ? 141.893 81.353  196.515 1.00 134.36 ? 3573 SER A CB    1 
ATOM   14109 N  N     . LYS A 1 2375 ? 155.740 79.062  181.449 1.00 161.55 ? 3592 LYS A N     1 
ATOM   14110 C  CA    . LYS A 1 2375 ? 156.839 79.042  180.491 1.00 163.10 ? 3592 LYS A CA    1 
ATOM   14111 C  C     . LYS A 1 2375 ? 156.852 80.314  179.649 1.00 164.71 ? 3592 LYS A C     1 
ATOM   14112 O  O     . LYS A 1 2375 ? 157.887 80.693  179.099 1.00 165.97 ? 3592 LYS A O     1 
ATOM   14113 C  CB    . LYS A 1 2375 ? 156.742 77.812  179.587 1.00 160.09 ? 3592 LYS A CB    1 
ATOM   14114 N  N     . GLU A 1 2376 ? 155.688 80.962  179.548 1.00 162.92 ? 3593 GLU A N     1 
ATOM   14115 C  CA    . GLU A 1 2376 ? 155.596 82.213  178.801 1.00 162.48 ? 3593 GLU A CA    1 
ATOM   14116 C  C     . GLU A 1 2376 ? 156.419 83.313  179.460 1.00 164.72 ? 3593 GLU A C     1 
ATOM   14117 O  O     . GLU A 1 2376 ? 157.090 84.091  178.770 1.00 165.55 ? 3593 GLU A O     1 
ATOM   14118 C  CB    . GLU A 1 2376 ? 154.134 82.639  178.671 1.00 160.19 ? 3593 GLU A CB    1 
ATOM   14119 N  N     . ALA A 1 2377 ? 156.381 83.392  180.793 1.00 165.78 ? 3594 ALA A N     1 
ATOM   14120 C  CA    . ALA A 1 2377 ? 157.186 84.381  181.504 1.00 166.00 ? 3594 ALA A CA    1 
ATOM   14121 C  C     . ALA A 1 2377 ? 158.675 84.115  181.326 1.00 167.16 ? 3594 ALA A C     1 
ATOM   14122 O  O     . ALA A 1 2377 ? 159.464 85.052  181.155 1.00 167.30 ? 3594 ALA A O     1 
ATOM   14123 C  CB    . ALA A 1 2377 ? 156.815 84.393  182.987 1.00 164.23 ? 3594 ALA A CB    1 
ATOM   14124 N  N     . MET A 1 2378 ? 159.079 82.841  181.362 1.00 167.40 ? 3595 MET A N     1 
ATOM   14125 C  CA    . MET A 1 2378 ? 160.481 82.496  181.143 1.00 167.98 ? 3595 MET A CA    1 
ATOM   14126 C  C     . MET A 1 2378 ? 160.922 82.838  179.724 1.00 167.69 ? 3595 MET A C     1 
ATOM   14127 O  O     . MET A 1 2378 ? 162.036 83.336  179.518 1.00 166.53 ? 3595 MET A O     1 
ATOM   14128 C  CB    . MET A 1 2378 ? 160.707 81.013  181.433 1.00 163.83 ? 3595 MET A CB    1 
ATOM   14129 N  N     . ASN A 1 2379 ? 160.063 82.577  178.734 1.00 166.10 ? 3596 ASN A N     1 
ATOM   14130 C  CA    . ASN A 1 2379 ? 160.387 82.932  177.355 1.00 163.44 ? 3596 ASN A CA    1 
ATOM   14131 C  C     . ASN A 1 2379 ? 160.491 84.442  177.181 1.00 166.89 ? 3596 ASN A C     1 
ATOM   14132 O  O     . ASN A 1 2379 ? 161.373 84.931  176.464 1.00 167.72 ? 3596 ASN A O     1 
ATOM   14133 C  CB    . ASN A 1 2379 ? 159.342 82.351  176.404 1.00 158.81 ? 3596 ASN A CB    1 
ATOM   14134 N  N     . ILE A 1 2380 ? 159.601 85.196  177.833 1.00 167.27 ? 3597 ILE A N     1 
ATOM   14135 C  CA    . ILE A 1 2380 ? 159.663 86.653  177.770 1.00 164.55 ? 3597 ILE A CA    1 
ATOM   14136 C  C     . ILE A 1 2380 ? 160.940 87.166  178.424 1.00 165.59 ? 3597 ILE A C     1 
ATOM   14137 O  O     . ILE A 1 2380 ? 161.577 88.100  177.923 1.00 164.67 ? 3597 ILE A O     1 
ATOM   14138 C  CB    . ILE A 1 2380 ? 158.409 87.269  178.415 1.00 162.64 ? 3597 ILE A CB    1 
ATOM   14139 N  N     . GLU A 1 2381 ? 161.331 86.569  179.554 1.00 167.26 ? 3598 GLU A N     1 
ATOM   14140 C  CA    . GLU A 1 2381 ? 162.569 86.966  180.219 1.00 167.17 ? 3598 GLU A CA    1 
ATOM   14141 C  C     . GLU A 1 2381 ? 163.787 86.659  179.355 1.00 166.19 ? 3598 GLU A C     1 
ATOM   14142 O  O     . GLU A 1 2381 ? 164.723 87.463  179.281 1.00 166.25 ? 3598 GLU A O     1 
ATOM   14143 C  CB    . GLU A 1 2381 ? 162.683 86.269  181.574 1.00 162.71 ? 3598 GLU A CB    1 
ATOM   14144 N  N     . LYS A 1 2382 ? 163.792 85.497  178.694 1.00 164.49 ? 3599 LYS A N     1 
ATOM   14145 C  CA    . LYS A 1 2382 ? 164.897 85.152  177.804 1.00 164.14 ? 3599 LYS A CA    1 
ATOM   14146 C  C     . LYS A 1 2382 ? 164.968 86.102  176.614 1.00 165.77 ? 3599 LYS A C     1 
ATOM   14147 O  O     . LYS A 1 2382 ? 166.059 86.527  176.212 1.00 166.42 ? 3599 LYS A O     1 
ATOM   14148 C  CB    . LYS A 1 2382 ? 164.756 83.706  177.329 1.00 163.23 ? 3599 LYS A CB    1 
ATOM   14149 N  N     . LYS A 1 2383 ? 163.812 86.451  176.041 1.00 166.07 ? 3600 LYS A N     1 
ATOM   14150 C  CA    . LYS A 1 2383 ? 163.787 87.396  174.928 1.00 164.90 ? 3600 LYS A CA    1 
ATOM   14151 C  C     . LYS A 1 2383 ? 164.263 88.776  175.363 1.00 163.17 ? 3600 LYS A C     1 
ATOM   14152 O  O     . LYS A 1 2383 ? 164.989 89.451  174.623 1.00 161.16 ? 3600 LYS A O     1 
ATOM   14153 C  CB    . LYS A 1 2383 ? 162.379 87.474  174.337 1.00 163.47 ? 3600 LYS A CB    1 
ATOM   14154 N  N     . LEU A 1 2384 ? 163.865 89.213  176.562 1.00 163.84 ? 3601 LEU A N     1 
ATOM   14155 C  CA    . LEU A 1 2384 ? 164.325 90.497  177.081 1.00 163.58 ? 3601 LEU A CA    1 
ATOM   14156 C  C     . LEU A 1 2384 ? 165.828 90.490  177.329 1.00 162.45 ? 3601 LEU A C     1 
ATOM   14157 O  O     . LEU A 1 2384 ? 166.515 91.476  177.038 1.00 162.95 ? 3601 LEU A O     1 
ATOM   14158 C  CB    . LEU A 1 2384 ? 163.568 90.845  178.363 1.00 163.99 ? 3601 LEU A CB    1 
ATOM   14159 N  N     . SER A 1 2385 ? 166.358 89.386  177.864 1.00 161.64 ? 3602 SER A N     1 
ATOM   14160 C  CA    . SER A 1 2385 ? 167.797 89.283  178.083 1.00 161.60 ? 3602 SER A CA    1 
ATOM   14161 C  C     . SER A 1 2385 ? 168.560 89.298  176.763 1.00 160.64 ? 3602 SER A C     1 
ATOM   14162 O  O     . SER A 1 2385 ? 169.641 89.892  176.668 1.00 159.56 ? 3602 SER A O     1 
ATOM   14163 C  CB    . SER A 1 2385 ? 168.118 88.016  178.876 1.00 162.97 ? 3602 SER A CB    1 
ATOM   14164 N  N     . GLU A 1 2386 ? 168.017 88.640  175.735 1.00 161.09 ? 3603 GLU A N     1 
ATOM   14165 C  CA    . GLU A 1 2386 ? 168.665 88.650  174.427 1.00 158.58 ? 3603 GLU A CA    1 
ATOM   14166 C  C     . GLU A 1 2386 ? 168.609 90.033  173.785 1.00 158.34 ? 3603 GLU A C     1 
ATOM   14167 O  O     . GLU A 1 2386 ? 169.580 90.471  173.157 1.00 155.88 ? 3603 GLU A O     1 
ATOM   14168 C  CB    . GLU A 1 2386 ? 168.018 87.609  173.514 1.00 157.78 ? 3603 GLU A CB    1 
ATOM   14169 N  N     . SER A 1 2387 ? 167.484 90.736  173.931 1.00 159.51 ? 3604 SER A N     1 
ATOM   14170 C  CA    . SER A 1 2387 ? 167.316 92.048  173.320 1.00 156.85 ? 3604 SER A CA    1 
ATOM   14171 C  C     . SER A 1 2387 ? 167.913 93.177  174.148 1.00 154.82 ? 3604 SER A C     1 
ATOM   14172 O  O     . SER A 1 2387 ? 167.920 94.323  173.683 1.00 152.36 ? 3604 SER A O     1 
ATOM   14173 C  CB    . SER A 1 2387 ? 165.830 92.326  173.076 1.00 154.89 ? 3604 SER A CB    1 
ATOM   14174 N  N     . GLU A 1 2388 ? 168.394 92.889  175.361 1.00 154.84 ? 3605 GLU A N     1 
ATOM   14175 C  CA    . GLU A 1 2388 ? 169.033 93.916  176.177 1.00 150.19 ? 3605 GLU A CA    1 
ATOM   14176 C  C     . GLU A 1 2388 ? 170.300 94.470  175.540 1.00 148.44 ? 3605 GLU A C     1 
ATOM   14177 O  O     . GLU A 1 2388 ? 170.699 95.594  175.865 1.00 148.97 ? 3605 GLU A O     1 
ATOM   14178 C  CB    . GLU A 1 2388 ? 169.352 93.357  177.565 1.00 148.49 ? 3605 GLU A CB    1 
ATOM   14179 N  N     . GLU A 1 2389 ? 170.942 93.720  174.648 1.00 148.36 ? 3606 GLU A N     1 
ATOM   14180 C  CA    . GLU A 1 2389 ? 172.120 94.198  173.931 1.00 145.96 ? 3606 GLU A CA    1 
ATOM   14181 C  C     . GLU A 1 2389 ? 171.744 94.358  172.460 1.00 148.70 ? 3606 GLU A C     1 
ATOM   14182 O  O     . GLU A 1 2389 ? 172.006 93.491  171.625 1.00 148.89 ? 3606 GLU A O     1 
ATOM   14183 C  CB    . GLU A 1 2389 ? 173.299 93.237  174.117 1.00 140.16 ? 3606 GLU A CB    1 
ATOM   14184 N  N     . PHE A 1 2390 ? 171.121 95.484  172.151 1.00 149.70 ? 3607 PHE A N     1 
ATOM   14185 C  CA    . PHE A 1 2390 ? 170.837 95.943  170.796 1.00 147.74 ? 3607 PHE A CA    1 
ATOM   14186 C  C     . PHE A 1 2390 ? 171.251 97.389  170.583 1.00 146.25 ? 3607 PHE A C     1 
ATOM   14187 O  O     . PHE A 1 2390 ? 171.681 97.746  169.483 1.00 142.77 ? 3607 PHE A O     1 
ATOM   14188 C  CB    . PHE A 1 2390 ? 169.342 95.773  170.478 1.00 146.03 ? 3607 PHE A CB    1 
ATOM   14189 N  N     . PHE A 1 2391 ? 171.114 98.230  171.608 1.00 147.70 ? 3608 PHE A N     1 
ATOM   14190 C  CA    . PHE A 1 2391 ? 171.514 99.631  171.502 1.00 146.23 ? 3608 PHE A CA    1 
ATOM   14191 C  C     . PHE A 1 2391 ? 172.994 99.855  171.186 1.00 146.27 ? 3608 PHE A C     1 
ATOM   14192 O  O     . PHE A 1 2391 ? 173.281 100.788 170.415 1.00 146.99 ? 3608 PHE A O     1 
ATOM   14193 C  CB    . PHE A 1 2391 ? 171.113 100.375 172.785 1.00 141.53 ? 3608 PHE A CB    1 
ATOM   14194 N  N     . PRO A 1 2392 ? 173.968 99.121  171.761 1.00 146.34 ? 3609 PRO A N     1 
ATOM   14195 C  CA    . PRO A 1 2392 ? 175.368 99.358  171.350 1.00 144.74 ? 3609 PRO A CA    1 
ATOM   14196 C  C     . PRO A 1 2392 ? 175.630 99.141  169.868 1.00 141.74 ? 3609 PRO A C     1 
ATOM   14197 O  O     . PRO A 1 2392 ? 176.419 99.887  169.275 1.00 140.72 ? 3609 PRO A O     1 
ATOM   14198 C  CB    . PRO A 1 2392 ? 176.155 98.364  172.214 1.00 144.41 ? 3609 PRO A CB    1 
ATOM   14199 C  CG    . PRO A 1 2392 ? 175.336 98.208  173.424 1.00 144.97 ? 3609 PRO A CG    1 
ATOM   14200 C  CD    . PRO A 1 2392 ? 173.917 98.233  172.942 1.00 146.02 ? 3609 PRO A CD    1 
ATOM   14201 N  N     . GLN A 1 2393 ? 174.987 98.147  169.250 1.00 140.80 ? 3610 GLN A N     1 
ATOM   14202 C  CA    . GLN A 1 2393 ? 175.171 97.927  167.817 1.00 141.85 ? 3610 GLN A CA    1 
ATOM   14203 C  C     . GLN A 1 2393 ? 174.625 99.095  167.003 1.00 139.32 ? 3610 GLN A C     1 
ATOM   14204 O  O     . GLN A 1 2393 ? 175.267 99.548  166.046 1.00 136.75 ? 3610 GLN A O     1 
ATOM   14205 C  CB    . GLN A 1 2393 ? 174.503 96.618  167.396 1.00 142.41 ? 3610 GLN A CB    1 
ATOM   14206 N  N     . PHE A 1 2394 ? 173.446 99.600  167.376 1.00 139.36 ? 3611 PHE A N     1 
ATOM   14207 C  CA    . PHE A 1 2394 ? 172.876 100.754 166.688 1.00 137.65 ? 3611 PHE A CA    1 
ATOM   14208 C  C     . PHE A 1 2394 ? 173.735 101.996 166.884 1.00 135.79 ? 3611 PHE A C     1 
ATOM   14209 O  O     . PHE A 1 2394 ? 173.909 102.788 165.953 1.00 134.26 ? 3611 PHE A O     1 
ATOM   14210 C  CB    . PHE A 1 2394 ? 171.449 101.004 167.175 1.00 140.44 ? 3611 PHE A CB    1 
ATOM   14211 N  N     . ASP A 1 2395 ? 174.280 102.181 168.090 1.00 138.35 ? 3612 ASP A N     1 
ATOM   14212 C  CA    . ASP A 1 2395 ? 175.158 103.320 168.345 1.00 136.59 ? 3612 ASP A CA    1 
ATOM   14213 C  C     . ASP A 1 2395 ? 176.440 103.228 167.526 1.00 135.18 ? 3612 ASP A C     1 
ATOM   14214 O  O     . ASP A 1 2395 ? 176.918 104.239 166.999 1.00 133.60 ? 3612 ASP A O     1 
ATOM   14215 C  CB    . ASP A 1 2395 ? 175.479 103.411 169.837 1.00 136.06 ? 3612 ASP A CB    1 
ATOM   14216 N  N     . ASN A 1 2396 ? 177.010 102.025 167.409 1.00 135.18 ? 3613 ASN A N     1 
ATOM   14217 C  CA    . ASN A 1 2396 ? 178.198 101.842 166.581 1.00 132.53 ? 3613 ASN A CA    1 
ATOM   14218 C  C     . ASN A 1 2396 ? 177.893 102.107 165.111 1.00 130.94 ? 3613 ASN A C     1 
ATOM   14219 O  O     . ASN A 1 2396 ? 178.705 102.711 164.400 1.00 129.26 ? 3613 ASN A O     1 
ATOM   14220 C  CB    . ASN A 1 2396 ? 178.757 100.432 166.769 1.00 130.73 ? 3613 ASN A CB    1 
ATOM   14221 N  N     . LEU A 1 2397 ? 176.726 101.657 164.638 1.00 131.22 ? 3614 LEU A N     1 
ATOM   14222 C  CA    . LEU A 1 2397 ? 176.335 101.918 163.255 1.00 129.45 ? 3614 LEU A CA    1 
ATOM   14223 C  C     . LEU A 1 2397 ? 176.131 103.408 163.006 1.00 128.12 ? 3614 LEU A C     1 
ATOM   14224 O  O     . LEU A 1 2397 ? 176.494 103.922 161.941 1.00 126.77 ? 3614 LEU A O     1 
ATOM   14225 C  CB    . LEU A 1 2397 ? 175.065 101.138 162.914 1.00 128.13 ? 3614 LEU A CB    1 
ATOM   14226 N  N     . VAL A 1 2398 ? 175.541 104.114 163.974 1.00 128.70 ? 3615 VAL A N     1 
ATOM   14227 C  CA    . VAL A 1 2398 ? 175.357 105.558 163.853 1.00 125.75 ? 3615 VAL A CA    1 
ATOM   14228 C  C     . VAL A 1 2398 ? 176.705 106.271 163.831 1.00 124.59 ? 3615 VAL A C     1 
ATOM   14229 O  O     . VAL A 1 2398 ? 176.927 107.182 163.023 1.00 122.72 ? 3615 VAL A O     1 
ATOM   14230 C  CB    . VAL A 1 2398 ? 174.452 106.071 164.990 1.00 125.37 ? 3615 VAL A CB    1 
ATOM   14231 C  CG1   . VAL A 1 2398 ? 174.567 107.580 165.144 1.00 126.70 ? 3615 VAL A CG1   1 
ATOM   14232 C  CG2   . VAL A 1 2398 ? 173.006 105.680 164.728 1.00 124.03 ? 3615 VAL A CG2   1 
ATOM   14233 N  N     . GLU A 1 2399 ? 177.629 105.859 164.704 1.00 127.08 ? 3616 GLU A N     1 
ATOM   14234 C  CA    . GLU A 1 2399 ? 178.957 106.465 164.729 1.00 123.93 ? 3616 GLU A CA    1 
ATOM   14235 C  C     . GLU A 1 2399 ? 179.731 106.186 163.447 1.00 120.98 ? 3616 GLU A C     1 
ATOM   14236 O  O     . GLU A 1 2399 ? 180.529 107.024 163.012 1.00 118.44 ? 3616 GLU A O     1 
ATOM   14237 C  CB    . GLU A 1 2399 ? 179.741 105.962 165.941 1.00 125.10 ? 3616 GLU A CB    1 
ATOM   14238 N  N     . GLU A 1 2400 ? 179.513 105.023 162.830 1.00 123.15 ? 3617 GLU A N     1 
ATOM   14239 C  CA    . GLU A 1 2400 ? 180.165 104.709 161.565 1.00 122.52 ? 3617 GLU A CA    1 
ATOM   14240 C  C     . GLU A 1 2400 ? 179.528 105.438 160.388 1.00 121.76 ? 3617 GLU A C     1 
ATOM   14241 O  O     . GLU A 1 2400 ? 180.151 105.539 159.325 1.00 119.91 ? 3617 GLU A O     1 
ATOM   14242 C  CB    . GLU A 1 2400 ? 180.137 103.195 161.332 1.00 120.29 ? 3617 GLU A CB    1 
ATOM   14243 C  CG    . GLU A 1 2400 ? 181.200 102.669 160.374 1.00 118.79 ? 3617 GLU A CG    1 
ATOM   14244 C  CD    . GLU A 1 2400 ? 180.678 102.478 158.964 1.00 117.05 ? 3617 GLU A CD    1 
ATOM   14245 O  OE1   . GLU A 1 2400 ? 179.460 102.254 158.806 1.00 117.26 ? 3617 GLU A OE1   1 
ATOM   14246 O  OE2   . GLU A 1 2400 ? 181.487 102.548 158.015 1.00 114.44 ? 3617 GLU A OE2   1 
ATOM   14247 N  N     . TYR A 1 2401 ? 178.315 105.961 160.557 1.00 122.46 ? 3618 TYR A N     1 
ATOM   14248 C  CA    . TYR A 1 2401 ? 177.588 106.670 159.510 1.00 119.34 ? 3618 TYR A CA    1 
ATOM   14249 C  C     . TYR A 1 2401 ? 177.260 108.099 159.935 1.00 114.77 ? 3618 TYR A C     1 
ATOM   14250 O  O     . TYR A 1 2401 ? 176.132 108.570 159.777 1.00 110.48 ? 3618 TYR A O     1 
ATOM   14251 C  CB    . TYR A 1 2401 ? 176.315 105.918 159.128 1.00 118.28 ? 3618 TYR A CB    1 
ATOM   14252 C  CG    . TYR A 1 2401 ? 176.505 104.888 158.036 1.00 113.64 ? 3618 TYR A CG    1 
ATOM   14253 C  CD1   . TYR A 1 2401 ? 177.003 105.251 156.791 1.00 109.33 ? 3618 TYR A CD1   1 
ATOM   14254 C  CD2   . TYR A 1 2401 ? 176.182 103.554 158.248 1.00 112.72 ? 3618 TYR A CD2   1 
ATOM   14255 C  CE1   . TYR A 1 2401 ? 177.175 104.314 155.788 1.00 105.47 ? 3618 TYR A CE1   1 
ATOM   14256 C  CE2   . TYR A 1 2401 ? 176.351 102.609 157.251 1.00 110.45 ? 3618 TYR A CE2   1 
ATOM   14257 C  CZ    . TYR A 1 2401 ? 176.848 102.996 156.024 1.00 105.89 ? 3618 TYR A CZ    1 
ATOM   14258 O  OH    . TYR A 1 2401 ? 177.019 102.061 155.029 1.00 97.90  ? 3618 TYR A OH    1 
ATOM   14259 N  N     . SER A 1 2402 ? 178.242 108.803 160.496 1.00 114.49 ? 3619 SER A N     1 
ATOM   14260 C  CA    . SER A 1 2402 ? 178.065 110.205 160.854 1.00 111.60 ? 3619 SER A CA    1 
ATOM   14261 C  C     . SER A 1 2402 ? 178.606 111.152 159.792 1.00 106.72 ? 3619 SER A C     1 
ATOM   14262 O  O     . SER A 1 2402 ? 178.120 112.287 159.673 1.00 107.18 ? 3619 SER A O     1 
ATOM   14263 C  CB    . SER A 1 2402 ? 178.746 110.498 162.194 1.00 117.01 ? 3619 SER A CB    1 
ATOM   14264 O  OG    . SER A 1 2402 ? 178.006 109.952 163.272 1.00 123.48 ? 3619 SER A OG    1 
ATOM   14265 N  N     . ILE A 1 2403 ? 179.603 110.709 159.023 1.00 105.45 ? 3620 ILE A N     1 
ATOM   14266 C  CA    . ILE A 1 2403 ? 180.161 111.545 157.965 1.00 104.06 ? 3620 ILE A CA    1 
ATOM   14267 C  C     . ILE A 1 2403 ? 179.124 111.784 156.872 1.00 100.99 ? 3620 ILE A C     1 
ATOM   14268 O  O     . ILE A 1 2403 ? 179.048 112.878 156.299 1.00 97.13  ? 3620 ILE A O     1 
ATOM   14269 C  CB    . ILE A 1 2403 ? 181.461 110.918 157.420 1.00 101.73 ? 3620 ILE A CB    1 
ATOM   14270 C  CG1   . ILE A 1 2403 ? 182.064 111.780 156.309 1.00 98.16  ? 3620 ILE A CG1   1 
ATOM   14271 C  CG2   . ILE A 1 2403 ? 181.238 109.479 156.956 1.00 99.69  ? 3620 ILE A CG2   1 
ATOM   14272 C  CD1   . ILE A 1 2403 ? 182.592 113.114 156.791 1.00 93.94  ? 3620 ILE A CD1   1 
ATOM   14273 N  N     . ILE A 1 2404 ? 178.284 110.782 156.595 1.00 102.55 ? 3621 ILE A N     1 
ATOM   14274 C  CA    . ILE A 1 2404 ? 177.208 110.961 155.626 1.00 102.84 ? 3621 ILE A CA    1 
ATOM   14275 C  C     . ILE A 1 2404 ? 176.192 111.980 156.136 1.00 101.91 ? 3621 ILE A C     1 
ATOM   14276 O  O     . ILE A 1 2404 ? 175.650 112.775 155.359 1.00 99.80  ? 3621 ILE A O     1 
ATOM   14277 C  CB    . ILE A 1 2404 ? 176.561 109.601 155.286 1.00 102.84 ? 3621 ILE A CB    1 
ATOM   14278 C  CG1   . ILE A 1 2404 ? 175.525 109.751 154.171 1.00 96.82  ? 3621 ILE A CG1   1 
ATOM   14279 C  CG2   . ILE A 1 2404 ? 175.966 108.924 156.518 1.00 104.92 ? 3621 ILE A CG2   1 
ATOM   14280 C  CD1   . ILE A 1 2404 ? 176.133 109.927 152.810 1.00 89.00  ? 3621 ILE A CD1   1 
ATOM   14281 N  N     . GLY A 1 2405 ? 175.948 112.001 157.448 1.00 104.72 ? 3622 GLY A N     1 
ATOM   14282 C  CA    . GLY A 1 2405 ? 175.054 113.001 158.008 1.00 100.86 ? 3622 GLY A CA    1 
ATOM   14283 C  C     . GLY A 1 2405 ? 175.620 114.405 157.930 1.00 96.57  ? 3622 GLY A C     1 
ATOM   14284 O  O     . GLY A 1 2405 ? 174.899 115.359 157.615 1.00 96.64  ? 3622 GLY A O     1 
ATOM   14285 N  N     . LYS A 1 2406 ? 176.917 114.552 158.213 1.00 96.57  ? 3623 LYS A N     1 
ATOM   14286 C  CA    . LYS A 1 2406 ? 177.559 115.855 158.067 1.00 97.27  ? 3623 LYS A CA    1 
ATOM   14287 C  C     . LYS A 1 2406 ? 177.528 116.319 156.616 1.00 96.34  ? 3623 LYS A C     1 
ATOM   14288 O  O     . LYS A 1 2406 ? 177.310 117.505 156.336 1.00 94.86  ? 3623 LYS A O     1 
ATOM   14289 C  CB    . LYS A 1 2406 ? 178.996 115.794 158.582 1.00 95.98  ? 3623 LYS A CB    1 
ATOM   14290 N  N     . HIS A 1 2407 ? 177.727 115.391 155.678 1.00 94.61  ? 3624 HIS A N     1 
ATOM   14291 C  CA    . HIS A 1 2407 ? 177.674 115.737 154.262 1.00 91.32  ? 3624 HIS A CA    1 
ATOM   14292 C  C     . HIS A 1 2407 ? 176.267 116.147 153.838 1.00 88.26  ? 3624 HIS A C     1 
ATOM   14293 O  O     . HIS A 1 2407 ? 176.102 117.082 153.047 1.00 85.95  ? 3624 HIS A O     1 
ATOM   14294 C  CB    . HIS A 1 2407 ? 178.177 114.563 153.425 1.00 88.86  ? 3624 HIS A CB    1 
ATOM   14295 C  CG    . HIS A 1 2407 ? 179.669 114.481 153.345 1.00 89.26  ? 3624 HIS A CG    1 
ATOM   14296 N  ND1   . HIS A 1 2407 ? 180.441 115.506 152.843 1.00 89.14  ? 3624 HIS A ND1   1 
ATOM   14297 C  CD2   . HIS A 1 2407 ? 180.530 113.498 153.694 1.00 90.87  ? 3624 HIS A CD2   1 
ATOM   14298 C  CE1   . HIS A 1 2407 ? 181.715 115.159 152.889 1.00 87.59  ? 3624 HIS A CE1   1 
ATOM   14299 N  NE2   . HIS A 1 2407 ? 181.796 113.945 153.402 1.00 88.87  ? 3624 HIS A NE2   1 
ATOM   14300 N  N     . SER A 1 2408 ? 175.243 115.460 154.352 1.00 90.34  ? 3625 SER A N     1 
ATOM   14301 C  CA    . SER A 1 2408 ? 173.865 115.850 154.062 1.00 88.20  ? 3625 SER A CA    1 
ATOM   14302 C  C     . SER A 1 2408 ? 173.551 117.234 154.617 1.00 87.43  ? 3625 SER A C     1 
ATOM   14303 O  O     . SER A 1 2408 ? 172.871 118.036 153.962 1.00 86.88  ? 3625 SER A O     1 
ATOM   14304 C  CB    . SER A 1 2408 ? 172.896 114.814 154.631 1.00 92.90  ? 3625 SER A CB    1 
ATOM   14305 O  OG    . SER A 1 2408 ? 171.591 115.351 154.757 1.00 90.43  ? 3625 SER A OG    1 
ATOM   14306 N  N     . VAL A 1 2409 ? 174.033 117.527 155.828 1.00 87.93  ? 3626 VAL A N     1 
ATOM   14307 C  CA    . VAL A 1 2409 ? 173.835 118.852 156.413 1.00 85.99  ? 3626 VAL A CA    1 
ATOM   14308 C  C     . VAL A 1 2409 ? 174.520 119.916 155.562 1.00 83.98  ? 3626 VAL A C     1 
ATOM   14309 O  O     . VAL A 1 2409 ? 173.956 120.988 155.310 1.00 84.85  ? 3626 VAL A O     1 
ATOM   14310 C  CB    . VAL A 1 2409 ? 174.334 118.868 157.871 1.00 88.47  ? 3626 VAL A CB    1 
ATOM   14311 C  CG1   . VAL A 1 2409 ? 174.497 120.292 158.379 1.00 90.34  ? 3626 VAL A CG1   1 
ATOM   14312 C  CG2   . VAL A 1 2409 ? 173.379 118.090 158.765 1.00 92.94  ? 3626 VAL A CG2   1 
ATOM   14313 N  N     . LYS A 1 2410 ? 175.736 119.624 155.086 1.00 84.71  ? 3627 LYS A N     1 
ATOM   14314 C  CA    . LYS A 1 2410 ? 176.446 120.555 154.211 1.00 84.69  ? 3627 LYS A CA    1 
ATOM   14315 C  C     . LYS A 1 2410 ? 175.687 120.788 152.907 1.00 81.38  ? 3627 LYS A C     1 
ATOM   14316 O  O     . LYS A 1 2410 ? 175.587 121.929 152.430 1.00 78.35  ? 3627 LYS A O     1 
ATOM   14317 C  CB    . LYS A 1 2410 ? 177.849 120.020 153.919 1.00 84.09  ? 3627 LYS A CB    1 
ATOM   14318 C  CG    . LYS A 1 2410 ? 178.898 120.413 154.942 1.00 83.27  ? 3627 LYS A CG    1 
ATOM   14319 C  CD    . LYS A 1 2410 ? 180.298 120.156 154.411 1.00 80.44  ? 3627 LYS A CD    1 
ATOM   14320 C  CE    . LYS A 1 2410 ? 180.523 118.674 154.152 1.00 76.05  ? 3627 LYS A CE    1 
ATOM   14321 N  NZ    . LYS A 1 2410 ? 181.972 118.335 154.099 1.00 67.52  ? 3627 LYS A NZ    1 
ATOM   14322 N  N     . ILE A 1 2411 ? 175.142 119.715 152.322 1.00 81.97  ? 3628 ILE A N     1 
ATOM   14323 C  CA    . ILE A 1 2411 ? 174.389 119.833 151.075 1.00 77.09  ? 3628 ILE A CA    1 
ATOM   14324 C  C     . ILE A 1 2411 ? 173.163 120.710 151.277 1.00 75.74  ? 3628 ILE A C     1 
ATOM   14325 O  O     . ILE A 1 2411 ? 172.879 121.605 150.472 1.00 77.09  ? 3628 ILE A O     1 
ATOM   14326 C  CB    . ILE A 1 2411 ? 173.986 118.444 150.550 1.00 75.35  ? 3628 ILE A CB    1 
ATOM   14327 C  CG1   . ILE A 1 2411 ? 175.186 117.684 150.005 1.00 73.53  ? 3628 ILE A CG1   1 
ATOM   14328 C  CG2   . ILE A 1 2411 ? 172.949 118.569 149.449 1.00 68.28  ? 3628 ILE A CG2   1 
ATOM   14329 C  CD1   . ILE A 1 2411 ? 174.829 116.275 149.628 1.00 77.05  ? 3628 ILE A CD1   1 
ATOM   14330 N  N     . PHE A 1 2412 ? 172.413 120.461 152.353 1.00 76.78  ? 3629 PHE A N     1 
ATOM   14331 C  CA    . PHE A 1 2412 ? 171.199 121.238 152.572 1.00 76.82  ? 3629 PHE A CA    1 
ATOM   14332 C  C     . PHE A 1 2412 ? 171.522 122.689 152.898 1.00 76.25  ? 3629 PHE A C     1 
ATOM   14333 O  O     . PHE A 1 2412 ? 170.784 123.595 152.496 1.00 74.26  ? 3629 PHE A O     1 
ATOM   14334 C  CB    . PHE A 1 2412 ? 170.346 120.625 153.674 1.00 80.25  ? 3629 PHE A CB    1 
ATOM   14335 C  CG    . PHE A 1 2412 ? 168.957 121.180 153.720 1.00 82.68  ? 3629 PHE A CG    1 
ATOM   14336 C  CD1   . PHE A 1 2412 ? 168.000 120.733 152.828 1.00 84.17  ? 3629 PHE A CD1   1 
ATOM   14337 C  CD2   . PHE A 1 2412 ? 168.613 122.164 154.631 1.00 86.76  ? 3629 PHE A CD2   1 
ATOM   14338 C  CE1   . PHE A 1 2412 ? 166.722 121.243 152.853 1.00 88.51  ? 3629 PHE A CE1   1 
ATOM   14339 C  CE2   . PHE A 1 2412 ? 167.333 122.679 154.662 1.00 88.65  ? 3629 PHE A CE2   1 
ATOM   14340 C  CZ    . PHE A 1 2412 ? 166.385 122.217 153.772 1.00 90.72  ? 3629 PHE A CZ    1 
ATOM   14341 N  N     . SER A 1 2413 ? 172.626 122.932 153.611 1.00 79.43  ? 3630 SER A N     1 
ATOM   14342 C  CA    . SER A 1 2413 ? 173.045 124.305 153.873 1.00 77.29  ? 3630 SER A CA    1 
ATOM   14343 C  C     . SER A 1 2413 ? 173.375 125.034 152.577 1.00 71.42  ? 3630 SER A C     1 
ATOM   14344 O  O     . SER A 1 2413 ? 172.975 126.188 152.390 1.00 73.58  ? 3630 SER A O     1 
ATOM   14345 C  CB    . SER A 1 2413 ? 174.246 124.320 154.818 1.00 82.23  ? 3630 SER A CB    1 
ATOM   14346 O  OG    . SER A 1 2413 ? 175.441 123.991 154.130 1.00 79.88  ? 3630 SER A OG    1 
ATOM   14347 N  N     . MET A 1 2414 ? 174.083 124.368 151.660 1.00 68.39  ? 3631 MET A N     1 
ATOM   14348 C  CA    . MET A 1 2414 ? 174.392 125.006 150.382 1.00 67.99  ? 3631 MET A CA    1 
ATOM   14349 C  C     . MET A 1 2414 ? 173.136 125.258 149.554 1.00 67.65  ? 3631 MET A C     1 
ATOM   14350 O  O     . MET A 1 2414 ? 172.970 126.345 148.984 1.00 68.31  ? 3631 MET A O     1 
ATOM   14351 C  CB    . MET A 1 2414 ? 175.372 124.158 149.579 1.00 67.33  ? 3631 MET A CB    1 
ATOM   14352 C  CG    . MET A 1 2414 ? 175.750 124.814 148.266 1.00 63.06  ? 3631 MET A CG    1 
ATOM   14353 S  SD    . MET A 1 2414 ? 176.899 123.842 147.300 1.00 59.18  ? 3631 MET A SD    1 
ATOM   14354 C  CE    . MET A 1 2414 ? 175.825 122.519 146.774 1.00 60.38  ? 3631 MET A CE    1 
ATOM   14355 N  N     . LEU A 1 2415 ? 172.246 124.267 149.462 1.00 67.45  ? 3632 LEU A N     1 
ATOM   14356 C  CA    . LEU A 1 2415 ? 171.044 124.443 148.650 1.00 64.23  ? 3632 LEU A CA    1 
ATOM   14357 C  C     . LEU A 1 2415 ? 170.094 125.469 149.258 1.00 66.68  ? 3632 LEU A C     1 
ATOM   14358 O  O     . LEU A 1 2415 ? 169.322 126.098 148.527 1.00 68.99  ? 3632 LEU A O     1 
ATOM   14359 C  CB    . LEU A 1 2415 ? 170.335 123.104 148.431 1.00 62.47  ? 3632 LEU A CB    1 
ATOM   14360 C  CG    . LEU A 1 2415 ? 170.787 122.190 147.279 1.00 56.58  ? 3632 LEU A CG    1 
ATOM   14361 C  CD1   . LEU A 1 2415 ? 170.534 122.879 145.948 1.00 62.50  ? 3632 LEU A CD1   1 
ATOM   14362 C  CD2   . LEU A 1 2415 ? 172.236 121.738 147.364 1.00 54.61  ? 3632 LEU A CD2   1 
ATOM   14363 N  N     . GLU A 1 2416 ? 170.137 125.663 150.578 1.00 69.89  ? 3633 GLU A N     1 
ATOM   14364 C  CA    . GLU A 1 2416 ? 169.397 126.765 151.180 1.00 70.84  ? 3633 GLU A CA    1 
ATOM   14365 C  C     . GLU A 1 2416 ? 170.086 128.104 150.943 1.00 72.06  ? 3633 GLU A C     1 
ATOM   14366 O  O     . GLU A 1 2416 ? 169.408 129.131 150.833 1.00 73.27  ? 3633 GLU A O     1 
ATOM   14367 C  CB    . GLU A 1 2416 ? 169.215 126.524 152.679 1.00 73.82  ? 3633 GLU A CB    1 
ATOM   14368 N  N     . LYS A 1 2417 ? 171.421 128.113 150.871 1.00 74.11  ? 3634 LYS A N     1 
ATOM   14369 C  CA    . LYS A 1 2417 ? 172.139 129.330 150.506 1.00 71.98  ? 3634 LYS A CA    1 
ATOM   14370 C  C     . LYS A 1 2417 ? 171.819 129.757 149.081 1.00 70.54  ? 3634 LYS A C     1 
ATOM   14371 O  O     . LYS A 1 2417 ? 171.795 130.956 148.782 1.00 70.91  ? 3634 LYS A O     1 
ATOM   14372 C  CB    . LYS A 1 2417 ? 173.646 129.123 150.664 1.00 71.95  ? 3634 LYS A CB    1 
ATOM   14373 C  CG    . LYS A 1 2417 ? 174.156 129.246 152.089 1.00 74.28  ? 3634 LYS A CG    1 
ATOM   14374 C  CD    . LYS A 1 2417 ? 174.205 130.693 152.543 1.00 77.36  ? 3634 LYS A CD    1 
ATOM   14375 C  CE    . LYS A 1 2417 ? 175.216 130.878 153.661 1.00 76.88  ? 3634 LYS A CE    1 
ATOM   14376 N  NZ    . LYS A 1 2417 ? 175.009 129.898 154.763 1.00 71.54  ? 3634 LYS A NZ    1 
ATOM   14377 N  N     . PHE A 1 2418 ? 171.581 128.791 148.189 1.00 68.60  ? 3635 PHE A N     1 
ATOM   14378 C  CA    . PHE A 1 2418 ? 171.218 129.119 146.814 1.00 65.65  ? 3635 PHE A CA    1 
ATOM   14379 C  C     . PHE A 1 2418 ? 169.854 129.791 146.731 1.00 70.04  ? 3635 PHE A C     1 
ATOM   14380 O  O     . PHE A 1 2418 ? 169.605 130.568 145.802 1.00 73.14  ? 3635 PHE A O     1 
ATOM   14381 C  CB    . PHE A 1 2418 ? 171.247 127.860 145.951 1.00 62.61  ? 3635 PHE A CB    1 
ATOM   14382 C  CG    . PHE A 1 2418 ? 172.617 127.499 145.463 1.00 57.82  ? 3635 PHE A CG    1 
ATOM   14383 C  CD1   . PHE A 1 2418 ? 173.619 128.453 145.408 1.00 56.81  ? 3635 PHE A CD1   1 
ATOM   14384 C  CD2   . PHE A 1 2418 ? 172.906 126.208 145.066 1.00 57.14  ? 3635 PHE A CD2   1 
ATOM   14385 C  CE1   . PHE A 1 2418 ? 174.882 128.125 144.960 1.00 59.24  ? 3635 PHE A CE1   1 
ATOM   14386 C  CE2   . PHE A 1 2418 ? 174.166 125.875 144.621 1.00 55.12  ? 3635 PHE A CE2   1 
ATOM   14387 C  CZ    . PHE A 1 2418 ? 175.155 126.834 144.567 1.00 56.75  ? 3635 PHE A CZ    1 
ATOM   14388 N  N     . GLY A 1 2419 ? 168.964 129.515 147.683 1.00 72.09  ? 3636 GLY A N     1 
ATOM   14389 C  CA    . GLY A 1 2419 ? 167.705 130.234 147.750 1.00 73.91  ? 3636 GLY A CA    1 
ATOM   14390 C  C     . GLY A 1 2419 ? 167.830 131.658 148.243 1.00 73.81  ? 3636 GLY A C     1 
ATOM   14391 O  O     . GLY A 1 2419 ? 166.855 132.413 148.159 1.00 71.60  ? 3636 GLY A O     1 
ATOM   14392 N  N     . GLN A 1 2420 ? 169.000 132.036 148.756 1.00 76.62  ? 3637 GLN A N     1 
ATOM   14393 C  CA    . GLN A 1 2420 ? 169.272 133.403 149.178 1.00 77.86  ? 3637 GLN A CA    1 
ATOM   14394 C  C     . GLN A 1 2420 ? 170.023 134.210 148.129 1.00 74.38  ? 3637 GLN A C     1 
ATOM   14395 O  O     . GLN A 1 2420 ? 169.881 135.436 148.093 1.00 72.78  ? 3637 GLN A O     1 
ATOM   14396 C  CB    . GLN A 1 2420 ? 170.074 133.404 150.485 1.00 80.39  ? 3637 GLN A CB    1 
ATOM   14397 C  CG    . GLN A 1 2420 ? 169.494 132.509 151.570 1.00 80.38  ? 3637 GLN A CG    1 
ATOM   14398 C  CD    . GLN A 1 2420 ? 168.018 132.756 151.812 1.00 81.59  ? 3637 GLN A CD    1 
ATOM   14399 O  OE1   . GLN A 1 2420 ? 167.166 132.004 151.339 1.00 81.77  ? 3637 GLN A OE1   1 
ATOM   14400 N  NE2   . GLN A 1 2420 ? 167.708 133.810 152.558 1.00 80.74  ? 3637 GLN A NE2   1 
ATOM   14401 N  N     . PHE A 1 2421 ? 170.827 133.555 147.283 1.00 72.77  ? 3638 PHE A N     1 
ATOM   14402 C  CA    . PHE A 1 2421 ? 171.521 134.267 146.213 1.00 72.42  ? 3638 PHE A CA    1 
ATOM   14403 C  C     . PHE A 1 2421 ? 170.531 134.816 145.190 1.00 72.90  ? 3638 PHE A C     1 
ATOM   14404 O  O     . PHE A 1 2421 ? 170.627 135.979 144.780 1.00 74.99  ? 3638 PHE A O     1 
ATOM   14405 C  CB    . PHE A 1 2421 ? 172.545 133.346 145.544 1.00 76.14  ? 3638 PHE A CB    1 
ATOM   14406 C  CG    . PHE A 1 2421 ? 173.867 133.262 146.272 1.00 75.93  ? 3638 PHE A CG    1 
ATOM   14407 C  CD1   . PHE A 1 2421 ? 174.022 133.809 147.536 1.00 75.18  ? 3638 PHE A CD1   1 
ATOM   14408 C  CD2   . PHE A 1 2421 ? 174.953 132.630 145.686 1.00 70.86  ? 3638 PHE A CD2   1 
ATOM   14409 C  CE1   . PHE A 1 2421 ? 175.233 133.727 148.200 1.00 71.96  ? 3638 PHE A CE1   1 
ATOM   14410 C  CE2   . PHE A 1 2421 ? 176.165 132.546 146.345 1.00 66.32  ? 3638 PHE A CE2   1 
ATOM   14411 C  CZ    . PHE A 1 2421 ? 176.305 133.095 147.602 1.00 67.53  ? 3638 PHE A CZ    1 
ATOM   14412 N  N     . HIS A 1 2422 ? 169.572 133.995 144.766 1.00 71.60  ? 3639 HIS A N     1 
ATOM   14413 C  CA    . HIS A 1 2422 ? 168.420 134.457 144.005 1.00 74.65  ? 3639 HIS A CA    1 
ATOM   14414 C  C     . HIS A 1 2422 ? 167.160 133.828 144.574 1.00 76.89  ? 3639 HIS A C     1 
ATOM   14415 O  O     . HIS A 1 2422 ? 167.197 132.760 145.190 1.00 77.95  ? 3639 HIS A O     1 
ATOM   14416 C  CB    . HIS A 1 2422 ? 168.525 134.138 142.511 1.00 73.25  ? 3639 HIS A CB    1 
ATOM   14417 C  CG    . HIS A 1 2422 ? 169.613 134.885 141.810 1.00 78.20  ? 3639 HIS A CG    1 
ATOM   14418 N  ND1   . HIS A 1 2422 ? 170.903 134.417 141.728 1.00 78.48  ? 3639 HIS A ND1   1 
ATOM   14419 C  CD2   . HIS A 1 2422 ? 169.603 136.067 141.149 1.00 78.26  ? 3639 HIS A CD2   1 
ATOM   14420 C  CE1   . HIS A 1 2422 ? 171.641 135.276 141.048 1.00 78.93  ? 3639 HIS A CE1   1 
ATOM   14421 N  NE2   . HIS A 1 2422 ? 170.877 136.289 140.687 1.00 81.41  ? 3639 HIS A NE2   1 
ATOM   14422 N  N     . TRP A 1 2423 ? 166.040 134.508 144.361 1.00 80.44  ? 3640 TRP A N     1 
ATOM   14423 C  CA    . TRP A 1 2423 ? 164.793 134.163 145.026 1.00 84.67  ? 3640 TRP A CA    1 
ATOM   14424 C  C     . TRP A 1 2423 ? 164.014 133.050 144.326 1.00 80.09  ? 3640 TRP A C     1 
ATOM   14425 O  O     . TRP A 1 2423 ? 163.011 132.584 144.876 1.00 78.66  ? 3640 TRP A O     1 
ATOM   14426 C  CB    . TRP A 1 2423 ? 163.946 135.432 145.168 1.00 90.27  ? 3640 TRP A CB    1 
ATOM   14427 C  CG    . TRP A 1 2423 ? 163.964 136.307 143.941 1.00 95.45  ? 3640 TRP A CG    1 
ATOM   14428 C  CD1   . TRP A 1 2423 ? 163.350 136.051 142.756 1.00 91.70  ? 3640 TRP A CD1   1 
ATOM   14429 C  CD2   . TRP A 1 2423 ? 164.648 137.560 143.775 1.00 99.31  ? 3640 TRP A CD2   1 
ATOM   14430 N  NE1   . TRP A 1 2423 ? 163.592 137.064 141.867 1.00 91.54  ? 3640 TRP A NE1   1 
ATOM   14431 C  CE2   . TRP A 1 2423 ? 164.387 138.003 142.465 1.00 99.57  ? 3640 TRP A CE2   1 
ATOM   14432 C  CE3   . TRP A 1 2423 ? 165.448 138.350 144.605 1.00 95.66  ? 3640 TRP A CE3   1 
ATOM   14433 C  CZ2   . TRP A 1 2423 ? 164.896 139.202 141.962 1.00 101.07 ? 3640 TRP A CZ2   1 
ATOM   14434 C  CZ3   . TRP A 1 2423 ? 165.955 139.542 144.103 1.00 96.47  ? 3640 TRP A CZ3   1 
ATOM   14435 C  CH2   . TRP A 1 2423 ? 165.676 139.955 142.793 1.00 99.22  ? 3640 TRP A CH2   1 
ATOM   14436 N  N     . PHE A 1 2424 ? 164.451 132.601 143.150 1.00 77.69  ? 3641 PHE A N     1 
ATOM   14437 C  CA    . PHE A 1 2424 ? 163.795 131.505 142.444 1.00 76.43  ? 3641 PHE A CA    1 
ATOM   14438 C  C     . PHE A 1 2424 ? 164.351 130.126 142.787 1.00 72.95  ? 3641 PHE A C     1 
ATOM   14439 O  O     . PHE A 1 2424 ? 163.893 129.136 142.208 1.00 71.75  ? 3641 PHE A O     1 
ATOM   14440 C  CB    . PHE A 1 2424 ? 163.903 131.690 140.926 1.00 76.49  ? 3641 PHE A CB    1 
ATOM   14441 C  CG    . PHE A 1 2424 ? 162.940 132.685 140.339 1.00 83.50  ? 3641 PHE A CG    1 
ATOM   14442 C  CD1   . PHE A 1 2424 ? 163.292 134.017 140.196 1.00 83.47  ? 3641 PHE A CD1   1 
ATOM   14443 C  CD2   . PHE A 1 2424 ? 161.689 132.272 139.900 1.00 83.09  ? 3641 PHE A CD2   1 
ATOM   14444 C  CE1   . PHE A 1 2424 ? 162.409 134.926 139.643 1.00 84.19  ? 3641 PHE A CE1   1 
ATOM   14445 C  CE2   . PHE A 1 2424 ? 160.803 133.173 139.346 1.00 80.85  ? 3641 PHE A CE2   1 
ATOM   14446 C  CZ    . PHE A 1 2424 ? 161.159 134.499 139.216 1.00 82.87  ? 3641 PHE A CZ    1 
ATOM   14447 N  N     . TYR A 1 2425 ? 165.307 130.021 143.706 1.00 74.58  ? 3642 TYR A N     1 
ATOM   14448 C  CA    . TYR A 1 2425 ? 166.010 128.767 143.958 1.00 70.74  ? 3642 TYR A CA    1 
ATOM   14449 C  C     . TYR A 1 2425 ? 165.682 128.205 145.335 1.00 74.77  ? 3642 TYR A C     1 
ATOM   14450 O  O     . TYR A 1 2425 ? 166.565 127.750 146.064 1.00 72.64  ? 3642 TYR A O     1 
ATOM   14451 C  CB    . TYR A 1 2425 ? 167.519 128.946 143.815 1.00 66.12  ? 3642 TYR A CB    1 
ATOM   14452 C  CG    . TYR A 1 2425 ? 167.961 129.403 142.449 1.00 59.70  ? 3642 TYR A CG    1 
ATOM   14453 C  CD1   . TYR A 1 2425 ? 167.297 128.985 141.307 1.00 57.92  ? 3642 TYR A CD1   1 
ATOM   14454 C  CD2   . TYR A 1 2425 ? 169.038 130.265 142.304 1.00 58.16  ? 3642 TYR A CD2   1 
ATOM   14455 C  CE1   . TYR A 1 2425 ? 167.699 129.407 140.057 1.00 58.26  ? 3642 TYR A CE1   1 
ATOM   14456 C  CE2   . TYR A 1 2425 ? 169.446 130.692 141.060 1.00 56.32  ? 3642 TYR A CE2   1 
ATOM   14457 C  CZ    . TYR A 1 2425 ? 168.775 130.261 139.940 1.00 57.42  ? 3642 TYR A CZ    1 
ATOM   14458 O  OH    . TYR A 1 2425 ? 169.185 130.688 138.699 1.00 61.47  ? 3642 TYR A OH    1 
ATOM   14459 N  N     . GLY A 1 2426 ? 164.404 128.220 145.705 1.00 78.91  ? 3643 GLY A N     1 
ATOM   14460 C  CA    . GLY A 1 2426 ? 164.012 127.727 147.016 1.00 80.25  ? 3643 GLY A CA    1 
ATOM   14461 C  C     . GLY A 1 2426 ? 164.098 126.212 147.088 1.00 79.53  ? 3643 GLY A C     1 
ATOM   14462 O  O     . GLY A 1 2426 ? 163.463 125.500 146.301 1.00 83.10  ? 3643 GLY A O     1 
ATOM   14463 N  N     . ILE A 1 2427 ? 164.889 125.712 148.035 1.00 77.00  ? 3644 ILE A N     1 
ATOM   14464 C  CA    . ILE A 1 2427 ? 165.038 124.282 148.287 1.00 80.19  ? 3644 ILE A CA    1 
ATOM   14465 C  C     . ILE A 1 2427 ? 164.632 124.025 149.731 1.00 86.69  ? 3644 ILE A C     1 
ATOM   14466 O  O     . ILE A 1 2427 ? 165.162 124.662 150.650 1.00 88.64  ? 3644 ILE A O     1 
ATOM   14467 C  CB    . ILE A 1 2427 ? 166.475 123.801 148.028 1.00 77.77  ? 3644 ILE A CB    1 
ATOM   14468 C  CG1   . ILE A 1 2427 ? 166.956 124.245 146.642 1.00 74.47  ? 3644 ILE A CG1   1 
ATOM   14469 C  CG2   . ILE A 1 2427 ? 166.570 122.289 148.176 1.00 75.17  ? 3644 ILE A CG2   1 
ATOM   14470 C  CD1   . ILE A 1 2427 ? 166.240 123.574 145.493 1.00 73.28  ? 3644 ILE A CD1   1 
ATOM   14471 N  N     . SER A 1 2428 ? 163.700 123.098 149.934 1.00 89.53  ? 3645 SER A N     1 
ATOM   14472 C  CA    . SER A 1 2428 ? 163.149 122.824 151.254 1.00 90.29  ? 3645 SER A CA    1 
ATOM   14473 C  C     . SER A 1 2428 ? 163.527 121.419 151.717 1.00 92.54  ? 3645 SER A C     1 
ATOM   14474 O  O     . SER A 1 2428 ? 164.162 120.643 150.997 1.00 93.84  ? 3645 SER A O     1 
ATOM   14475 C  CB    . SER A 1 2428 ? 161.631 123.008 151.256 1.00 89.73  ? 3645 SER A CB    1 
ATOM   14476 N  N     . ILE A 1 2429 ? 163.118 121.103 152.949 1.00 92.61  ? 3646 ILE A N     1 
ATOM   14477 C  CA    . ILE A 1 2429 ? 163.494 119.840 153.578 1.00 95.32  ? 3646 ILE A CA    1 
ATOM   14478 C  C     . ILE A 1 2429 ? 162.789 118.663 152.907 1.00 96.63  ? 3646 ILE A C     1 
ATOM   14479 O  O     . ILE A 1 2429 ? 163.372 117.582 152.755 1.00 96.13  ? 3646 ILE A O     1 
ATOM   14480 C  CB    . ILE A 1 2429 ? 163.210 119.906 155.093 1.00 93.52  ? 3646 ILE A CB    1 
ATOM   14481 C  CG1   . ILE A 1 2429 ? 163.491 118.563 155.774 1.00 92.06  ? 3646 ILE A CG1   1 
ATOM   14482 C  CG2   . ILE A 1 2429 ? 161.789 120.388 155.368 1.00 98.26  ? 3646 ILE A CG2   1 
ATOM   14483 C  CD1   . ILE A 1 2429 ? 164.930 118.110 155.668 1.00 93.89  ? 3646 ILE A CD1   1 
ATOM   14484 N  N     . GLY A 1 2430 ? 161.534 118.852 152.491 1.00 95.49  ? 3647 GLY A N     1 
ATOM   14485 C  CA    . GLY A 1 2430 ? 160.775 117.751 151.916 1.00 93.35  ? 3647 GLY A CA    1 
ATOM   14486 C  C     . GLY A 1 2430 ? 161.346 117.250 150.602 1.00 93.36  ? 3647 GLY A C     1 
ATOM   14487 O  O     . GLY A 1 2430 ? 161.403 116.041 150.362 1.00 94.92  ? 3647 GLY A O     1 
ATOM   14488 N  N     . GLN A 1 2431 ? 161.780 118.170 149.736 1.00 92.08  ? 3648 GLN A N     1 
ATOM   14489 C  CA    . GLN A 1 2431 ? 162.370 117.772 148.461 1.00 92.63  ? 3648 GLN A CA    1 
ATOM   14490 C  C     . GLN A 1 2431 ? 163.672 117.006 148.665 1.00 93.10  ? 3648 GLN A C     1 
ATOM   14491 O  O     . GLN A 1 2431 ? 163.929 116.010 147.976 1.00 95.46  ? 3648 GLN A O     1 
ATOM   14492 C  CB    . GLN A 1 2431 ? 162.601 119.002 147.585 1.00 87.43  ? 3648 GLN A CB    1 
ATOM   14493 N  N     . PHE A 1 2432 ? 164.505 117.453 149.607 1.00 89.32  ? 3649 PHE A N     1 
ATOM   14494 C  CA    . PHE A 1 2432 ? 165.761 116.756 149.861 1.00 87.59  ? 3649 PHE A CA    1 
ATOM   14495 C  C     . PHE A 1 2432 ? 165.519 115.400 150.512 1.00 92.20  ? 3649 PHE A C     1 
ATOM   14496 O  O     . PHE A 1 2432 ? 166.245 114.437 150.239 1.00 95.11  ? 3649 PHE A O     1 
ATOM   14497 C  CB    . PHE A 1 2432 ? 166.678 117.616 150.725 1.00 84.71  ? 3649 PHE A CB    1 
ATOM   14498 C  CG    . PHE A 1 2432 ? 168.031 117.014 150.939 1.00 85.64  ? 3649 PHE A CG    1 
ATOM   14499 C  CD1   . PHE A 1 2432 ? 168.963 117.004 149.919 1.00 81.56  ? 3649 PHE A CD1   1 
ATOM   14500 C  CD2   . PHE A 1 2432 ? 168.369 116.451 152.157 1.00 89.92  ? 3649 PHE A CD2   1 
ATOM   14501 C  CE1   . PHE A 1 2432 ? 170.208 116.444 150.107 1.00 81.79  ? 3649 PHE A CE1   1 
ATOM   14502 C  CE2   . PHE A 1 2432 ? 169.614 115.892 152.352 1.00 90.46  ? 3649 PHE A CE2   1 
ATOM   14503 C  CZ    . PHE A 1 2432 ? 170.536 115.889 151.325 1.00 87.20  ? 3649 PHE A CZ    1 
ATOM   14504 N  N     . LEU A 1 2433 ? 164.503 115.301 151.371 1.00 92.58  ? 3650 LEU A N     1 
ATOM   14505 C  CA    . LEU A 1 2433 ? 164.133 114.001 151.920 1.00 93.28  ? 3650 LEU A CA    1 
ATOM   14506 C  C     . LEU A 1 2433 ? 163.656 113.062 150.819 1.00 94.50  ? 3650 LEU A C     1 
ATOM   14507 O  O     . LEU A 1 2433 ? 164.000 111.872 150.811 1.00 95.00  ? 3650 LEU A O     1 
ATOM   14508 C  CB    . LEU A 1 2433 ? 163.053 114.174 152.988 1.00 92.19  ? 3650 LEU A CB    1 
ATOM   14509 C  CG    . LEU A 1 2433 ? 163.019 113.124 154.097 1.00 91.63  ? 3650 LEU A CG    1 
ATOM   14510 C  CD1   . LEU A 1 2433 ? 164.205 113.310 155.028 1.00 92.31  ? 3650 LEU A CD1   1 
ATOM   14511 C  CD2   . LEU A 1 2433 ? 161.711 113.202 154.867 1.00 93.45  ? 3650 LEU A CD2   1 
ATOM   14512 N  N     . SER A 1 2434 ? 162.880 113.589 149.867 1.00 95.37  ? 3651 SER A N     1 
ATOM   14513 C  CA    . SER A 1 2434 ? 162.417 112.784 148.742 1.00 93.53  ? 3651 SER A CA    1 
ATOM   14514 C  C     . SER A 1 2434 ? 163.580 112.302 147.883 1.00 93.79  ? 3651 SER A C     1 
ATOM   14515 O  O     . SER A 1 2434 ? 163.603 111.143 147.455 1.00 94.41  ? 3651 SER A O     1 
ATOM   14516 C  CB    . SER A 1 2434 ? 161.429 113.585 147.896 1.00 93.32  ? 3651 SER A CB    1 
ATOM   14517 O  OG    . SER A 1 2434 ? 162.104 114.542 147.098 1.00 91.50  ? 3651 SER A OG    1 
ATOM   14518 N  N     . CYS A 1 2435 ? 164.557 113.175 147.618 1.00 92.80  ? 3652 CYS A N     1 
ATOM   14519 C  CA    . CYS A 1 2435 ? 165.692 112.757 146.797 1.00 92.66  ? 3652 CYS A CA    1 
ATOM   14520 C  C     . CYS A 1 2435 ? 166.582 111.762 147.534 1.00 94.25  ? 3652 CYS A C     1 
ATOM   14521 O  O     . CYS A 1 2435 ? 167.096 110.819 146.919 1.00 95.92  ? 3652 CYS A O     1 
ATOM   14522 C  CB    . CYS A 1 2435 ? 166.504 113.968 146.335 1.00 86.90  ? 3652 CYS A CB    1 
ATOM   14523 S  SG    . CYS A 1 2435 ? 167.720 114.591 147.507 1.00 84.87  ? 3652 CYS A SG    1 
ATOM   14524 N  N     . PHE A 1 2436 ? 166.759 111.932 148.848 1.00 92.89  ? 3653 PHE A N     1 
ATOM   14525 C  CA    . PHE A 1 2436 ? 167.531 110.956 149.611 1.00 92.91  ? 3653 PHE A CA    1 
ATOM   14526 C  C     . PHE A 1 2436 ? 166.821 109.609 149.683 1.00 95.52  ? 3653 PHE A C     1 
ATOM   14527 O  O     . PHE A 1 2436 ? 167.481 108.565 149.729 1.00 98.67  ? 3653 PHE A O     1 
ATOM   14528 C  CB    . PHE A 1 2436 ? 167.817 111.486 151.016 1.00 94.17  ? 3653 PHE A CB    1 
ATOM   14529 C  CG    . PHE A 1 2436 ? 168.598 110.532 151.876 1.00 98.31  ? 3653 PHE A CG    1 
ATOM   14530 C  CD1   . PHE A 1 2436 ? 169.905 110.205 151.556 1.00 96.49  ? 3653 PHE A CD1   1 
ATOM   14531 C  CD2   . PHE A 1 2436 ? 168.028 109.966 153.005 1.00 100.48 ? 3653 PHE A CD2   1 
ATOM   14532 C  CE1   . PHE A 1 2436 ? 170.630 109.328 152.342 1.00 95.78  ? 3653 PHE A CE1   1 
ATOM   14533 C  CE2   . PHE A 1 2436 ? 168.748 109.088 153.797 1.00 100.56 ? 3653 PHE A CE2   1 
ATOM   14534 C  CZ    . PHE A 1 2436 ? 170.050 108.770 153.465 1.00 98.68  ? 3653 PHE A CZ    1 
ATOM   14535 N  N     . LYS A 1 2437 ? 165.485 109.606 149.702 1.00 96.21  ? 3654 LYS A N     1 
ATOM   14536 C  CA    . LYS A 1 2437 ? 164.755 108.343 149.635 1.00 98.45  ? 3654 LYS A CA    1 
ATOM   14537 C  C     . LYS A 1 2437 ? 164.858 107.718 148.247 1.00 97.62  ? 3654 LYS A C     1 
ATOM   14538 O  O     . LYS A 1 2437 ? 164.978 106.493 148.115 1.00 97.32  ? 3654 LYS A O     1 
ATOM   14539 C  CB    . LYS A 1 2437 ? 163.294 108.563 150.025 1.00 98.65  ? 3654 LYS A CB    1 
ATOM   14540 C  CG    . LYS A 1 2437 ? 162.704 107.446 150.867 1.00 97.68  ? 3654 LYS A CG    1 
ATOM   14541 C  CD    . LYS A 1 2437 ? 161.225 107.667 151.127 1.00 95.19  ? 3654 LYS A CD    1 
ATOM   14542 C  CE    . LYS A 1 2437 ? 160.995 108.922 151.952 1.00 97.75  ? 3654 LYS A CE    1 
ATOM   14543 N  NZ    . LYS A 1 2437 ? 159.546 109.227 152.106 1.00 105.43 ? 3654 LYS A NZ    1 
ATOM   14544 N  N     . ARG A 1 2438 ? 164.816 108.545 147.200 1.00 97.20  ? 3655 ARG A N     1 
ATOM   14545 C  CA    . ARG A 1 2438 ? 164.965 108.047 145.838 1.00 97.38  ? 3655 ARG A CA    1 
ATOM   14546 C  C     . ARG A 1 2438 ? 166.378 107.556 145.554 1.00 97.53  ? 3655 ARG A C     1 
ATOM   14547 O  O     . ARG A 1 2438 ? 166.584 106.850 144.560 1.00 98.44  ? 3655 ARG A O     1 
ATOM   14548 C  CB    . ARG A 1 2438 ? 164.579 109.134 144.835 1.00 94.83  ? 3655 ARG A CB    1 
ATOM   14549 N  N     . VAL A 1 2439 ? 167.353 107.946 146.380 1.00 96.73  ? 3656 VAL A N     1 
ATOM   14550 C  CA    . VAL A 1 2439 ? 168.684 107.345 146.303 1.00 97.64  ? 3656 VAL A CA    1 
ATOM   14551 C  C     . VAL A 1 2439 ? 168.588 105.834 146.482 1.00 98.91  ? 3656 VAL A C     1 
ATOM   14552 O  O     . VAL A 1 2439 ? 169.168 105.058 145.712 1.00 98.68  ? 3656 VAL A O     1 
ATOM   14553 C  CB    . VAL A 1 2439 ? 169.623 107.971 147.352 1.00 96.25  ? 3656 VAL A CB    1 
ATOM   14554 C  CG1   . VAL A 1 2439 ? 170.875 107.121 147.534 1.00 93.02  ? 3656 VAL A CG1   1 
ATOM   14555 C  CG2   . VAL A 1 2439 ? 169.998 109.386 146.968 1.00 92.91  ? 3656 VAL A CG2   1 
ATOM   14556 N  N     . PHE A 1 2440 ? 167.837 105.395 147.492 1.00 100.05 ? 3657 PHE A N     1 
ATOM   14557 C  CA    . PHE A 1 2440 ? 167.673 103.975 147.773 1.00 101.98 ? 3657 PHE A CA    1 
ATOM   14558 C  C     . PHE A 1 2440 ? 166.556 103.331 146.968 1.00 102.17 ? 3657 PHE A C     1 
ATOM   14559 O  O     . PHE A 1 2440 ? 166.567 102.107 146.794 1.00 99.61  ? 3657 PHE A O     1 
ATOM   14560 C  CB    . PHE A 1 2440 ? 167.397 103.753 149.263 1.00 102.86 ? 3657 PHE A CB    1 
ATOM   14561 C  CG    . PHE A 1 2440 ? 168.386 104.420 150.167 1.00 102.64 ? 3657 PHE A CG    1 
ATOM   14562 C  CD1   . PHE A 1 2440 ? 169.728 104.460 149.835 1.00 101.49 ? 3657 PHE A CD1   1 
ATOM   14563 C  CD2   . PHE A 1 2440 ? 167.974 105.012 151.348 1.00 103.25 ? 3657 PHE A CD2   1 
ATOM   14564 C  CE1   . PHE A 1 2440 ? 170.633 105.078 150.657 1.00 103.18 ? 3657 PHE A CE1   1 
ATOM   14565 C  CE2   . PHE A 1 2440 ? 168.881 105.629 152.181 1.00 103.71 ? 3657 PHE A CE2   1 
ATOM   14566 C  CZ    . PHE A 1 2440 ? 170.213 105.661 151.836 1.00 104.04 ? 3657 PHE A CZ    1 
ATOM   14567 N  N     . ILE A 1 2441 ? 165.585 104.121 146.497 1.00 103.08 ? 3658 ILE A N     1 
ATOM   14568 C  CA    . ILE A 1 2441 ? 164.484 103.566 145.713 1.00 102.65 ? 3658 ILE A CA    1 
ATOM   14569 C  C     . ILE A 1 2441 ? 165.000 102.965 144.411 1.00 100.90 ? 3658 ILE A C     1 
ATOM   14570 O  O     . ILE A 1 2441 ? 164.577 101.877 144.001 1.00 97.23  ? 3658 ILE A O     1 
ATOM   14571 C  CB    . ILE A 1 2441 ? 163.414 104.643 145.454 1.00 104.61 ? 3658 ILE A CB    1 
ATOM   14572 N  N     . LYS A 1 2442 ? 165.917 103.657 143.743 1.00 103.06 ? 3659 LYS A N     1 
ATOM   14573 C  CA    . LYS A 1 2442 ? 166.504 103.151 142.509 1.00 103.01 ? 3659 LYS A CA    1 
ATOM   14574 C  C     . LYS A 1 2442 ? 167.575 102.105 142.804 1.00 102.07 ? 3659 LYS A C     1 
ATOM   14575 O  O     . LYS A 1 2442 ? 168.721 102.237 142.372 1.00 102.27 ? 3659 LYS A O     1 
ATOM   14576 C  CB    . LYS A 1 2442 ? 167.098 104.296 141.687 1.00 104.20 ? 3659 LYS A CB    1 
ATOM   14577 N  N     . THR A 1 2452 ? 183.231 98.856  150.515 1.00 87.98  ? 3669 THR A N     1 
ATOM   14578 C  CA    . THR A 1 2452 ? 183.053 100.292 150.694 1.00 87.43  ? 3669 THR A CA    1 
ATOM   14579 C  C     . THR A 1 2452 ? 181.582 100.675 150.589 1.00 88.94  ? 3669 THR A C     1 
ATOM   14580 O  O     . THR A 1 2452 ? 181.186 101.393 149.670 1.00 89.85  ? 3669 THR A O     1 
ATOM   14581 C  CB    . THR A 1 2452 ? 183.858 101.097 149.655 1.00 85.40  ? 3669 THR A CB    1 
ATOM   14582 O  OG1   . THR A 1 2452 ? 183.517 100.657 148.335 1.00 82.34  ? 3669 THR A OG1   1 
ATOM   14583 C  CG2   . THR A 1 2452 ? 185.351 100.913 149.877 1.00 82.38  ? 3669 THR A CG2   1 
ATOM   14584 N  N     . ARG A 1 2453 ? 180.776 100.182 151.533 1.00 90.00  ? 3670 ARG A N     1 
ATOM   14585 C  CA    . ARG A 1 2453 ? 179.351 100.502 151.534 1.00 89.89  ? 3670 ARG A CA    1 
ATOM   14586 C  C     . ARG A 1 2453 ? 179.111 101.979 151.824 1.00 92.38  ? 3670 ARG A C     1 
ATOM   14587 O  O     . ARG A 1 2453 ? 178.239 102.602 151.208 1.00 91.93  ? 3670 ARG A O     1 
ATOM   14588 C  CB    . ARG A 1 2453 ? 178.617 99.629  152.552 1.00 87.38  ? 3670 ARG A CB    1 
ATOM   14589 N  N     . VAL A 1 2454 ? 179.870 102.552 152.762 1.00 95.22  ? 3671 VAL A N     1 
ATOM   14590 C  CA    . VAL A 1 2454 ? 179.725 103.969 153.087 1.00 93.37  ? 3671 VAL A CA    1 
ATOM   14591 C  C     . VAL A 1 2454 ? 180.137 104.838 151.905 1.00 89.18  ? 3671 VAL A C     1 
ATOM   14592 O  O     . VAL A 1 2454 ? 179.456 105.816 151.566 1.00 87.91  ? 3671 VAL A O     1 
ATOM   14593 C  CB    . VAL A 1 2454 ? 180.535 104.313 154.350 1.00 95.28  ? 3671 VAL A CB    1 
ATOM   14594 N  N     . ASP A 1 2455 ? 181.251 104.495 151.255 1.00 88.18  ? 3672 ASP A N     1 
ATOM   14595 C  CA    . ASP A 1 2455 ? 181.698 105.258 150.095 1.00 88.71  ? 3672 ASP A CA    1 
ATOM   14596 C  C     . ASP A 1 2455 ? 180.682 105.186 148.963 1.00 89.58  ? 3672 ASP A C     1 
ATOM   14597 O  O     . ASP A 1 2455 ? 180.386 106.200 148.321 1.00 91.17  ? 3672 ASP A O     1 
ATOM   14598 C  CB    . ASP A 1 2455 ? 183.061 104.750 149.628 1.00 86.50  ? 3672 ASP A CB    1 
ATOM   14599 N  N     . GLU A 1 2456 ? 180.114 104.002 148.723 1.00 88.03  ? 3673 GLU A N     1 
ATOM   14600 C  CA    . GLU A 1 2456 ? 179.159 103.853 147.630 1.00 86.11  ? 3673 GLU A CA    1 
ATOM   14601 C  C     . GLU A 1 2456 ? 177.841 104.558 147.934 1.00 87.13  ? 3673 GLU A C     1 
ATOM   14602 O  O     . GLU A 1 2456 ? 177.246 105.172 147.040 1.00 88.44  ? 3673 GLU A O     1 
ATOM   14603 C  CB    . GLU A 1 2456 ? 178.926 102.373 147.334 1.00 88.00  ? 3673 GLU A CB    1 
ATOM   14604 C  CG    . GLU A 1 2456 ? 178.188 102.119 146.029 1.00 90.78  ? 3673 GLU A CG    1 
ATOM   14605 C  CD    . GLU A 1 2456 ? 179.005 102.505 144.809 1.00 91.56  ? 3673 GLU A CD    1 
ATOM   14606 O  OE1   . GLU A 1 2456 ? 180.250 102.424 144.870 1.00 88.44  ? 3673 GLU A OE1   1 
ATOM   14607 O  OE2   . GLU A 1 2456 ? 178.399 102.892 143.788 1.00 92.42  ? 3673 GLU A OE2   1 
ATOM   14608 N  N     . ILE A 1 2457 ? 177.366 104.488 149.182 1.00 87.41  ? 3674 ILE A N     1 
ATOM   14609 C  CA    . ILE A 1 2457 ? 176.118 105.165 149.529 1.00 87.31  ? 3674 ILE A CA    1 
ATOM   14610 C  C     . ILE A 1 2457 ? 176.298 106.681 149.465 1.00 87.77  ? 3674 ILE A C     1 
ATOM   14611 O  O     . ILE A 1 2457 ? 175.396 107.409 149.029 1.00 90.24  ? 3674 ILE A O     1 
ATOM   14612 C  CB    . ILE A 1 2457 ? 175.599 104.680 150.902 1.00 89.73  ? 3674 ILE A CB    1 
ATOM   14613 C  CG1   . ILE A 1 2457 ? 174.158 105.115 151.143 1.00 88.36  ? 3674 ILE A CG1   1 
ATOM   14614 C  CG2   . ILE A 1 2457 ? 176.424 105.187 152.064 1.00 93.93  ? 3674 ILE A CG2   1 
ATOM   14615 C  CD1   . ILE A 1 2457 ? 173.571 104.471 152.383 1.00 92.98  ? 3674 ILE A CD1   1 
ATOM   14616 N  N     . LEU A 1 2458 ? 177.484 107.176 149.835 1.00 86.55  ? 3675 LEU A N     1 
ATOM   14617 C  CA    . LEU A 1 2458 ? 177.743 108.609 149.754 1.00 85.39  ? 3675 LEU A CA    1 
ATOM   14618 C  C     . LEU A 1 2458 ? 177.877 109.062 148.303 1.00 85.09  ? 3675 LEU A C     1 
ATOM   14619 O  O     . LEU A 1 2458 ? 177.402 110.146 147.935 1.00 86.36  ? 3675 LEU A O     1 
ATOM   14620 C  CB    . LEU A 1 2458 ? 178.993 108.933 150.572 1.00 84.65  ? 3675 LEU A CB    1 
ATOM   14621 C  CG    . LEU A 1 2458 ? 179.337 110.366 150.961 1.00 82.92  ? 3675 LEU A CG    1 
ATOM   14622 C  CD1   . LEU A 1 2458 ? 179.967 110.361 152.335 1.00 90.89  ? 3675 LEU A CD1   1 
ATOM   14623 C  CD2   . LEU A 1 2458 ? 180.301 110.944 149.968 1.00 80.18  ? 3675 LEU A CD2   1 
ATOM   14624 N  N     . TRP A 1 2459 ? 178.509 108.235 147.463 1.00 82.64  ? 3676 TRP A N     1 
ATOM   14625 C  CA    . TRP A 1 2459 ? 178.574 108.515 146.032 1.00 78.39  ? 3676 TRP A CA    1 
ATOM   14626 C  C     . TRP A 1 2459 ? 177.179 108.560 145.422 1.00 80.58  ? 3676 TRP A C     1 
ATOM   14627 O  O     . TRP A 1 2459 ? 176.881 109.442 144.609 1.00 81.99  ? 3676 TRP A O     1 
ATOM   14628 C  CB    . TRP A 1 2459 ? 179.460 107.460 145.351 1.00 79.77  ? 3676 TRP A CB    1 
ATOM   14629 C  CG    . TRP A 1 2459 ? 179.613 107.528 143.837 1.00 79.72  ? 3676 TRP A CG    1 
ATOM   14630 C  CD1   . TRP A 1 2459 ? 178.622 107.479 142.895 1.00 80.05  ? 3676 TRP A CD1   1 
ATOM   14631 C  CD2   . TRP A 1 2459 ? 180.842 107.647 143.109 1.00 82.33  ? 3676 TRP A CD2   1 
ATOM   14632 N  NE1   . TRP A 1 2459 ? 179.157 107.563 141.635 1.00 81.65  ? 3676 TRP A NE1   1 
ATOM   14633 C  CE2   . TRP A 1 2459 ? 180.519 107.667 141.738 1.00 83.68  ? 3676 TRP A CE2   1 
ATOM   14634 C  CE3   . TRP A 1 2459 ? 182.185 107.739 143.485 1.00 82.12  ? 3676 TRP A CE3   1 
ATOM   14635 C  CZ2   . TRP A 1 2459 ? 181.487 107.777 140.744 1.00 84.04  ? 3676 TRP A CZ2   1 
ATOM   14636 C  CZ3   . TRP A 1 2459 ? 183.146 107.849 142.496 1.00 82.67  ? 3676 TRP A CZ3   1 
ATOM   14637 C  CH2   . TRP A 1 2459 ? 182.792 107.867 141.142 1.00 85.13  ? 3676 TRP A CH2   1 
ATOM   14638 N  N     . LEU A 1 2460 ? 176.313 107.615 145.800 1.00 83.44  ? 3677 LEU A N     1 
ATOM   14639 C  CA    . LEU A 1 2460 ? 174.947 107.613 145.288 1.00 83.41  ? 3677 LEU A CA    1 
ATOM   14640 C  C     . LEU A 1 2460 ? 174.189 108.856 145.732 1.00 82.13  ? 3677 LEU A C     1 
ATOM   14641 O  O     . LEU A 1 2460 ? 173.440 109.447 144.942 1.00 83.87  ? 3677 LEU A O     1 
ATOM   14642 C  CB    . LEU A 1 2460 ? 174.214 106.349 145.737 1.00 86.97  ? 3677 LEU A CB    1 
ATOM   14643 C  CG    . LEU A 1 2460 ? 174.319 105.133 144.813 1.00 89.13  ? 3677 LEU A CG    1 
ATOM   14644 C  CD1   . LEU A 1 2460 ? 173.387 104.023 145.276 1.00 94.04  ? 3677 LEU A CD1   1 
ATOM   14645 C  CD2   . LEU A 1 2460 ? 174.019 105.523 143.374 1.00 82.64  ? 3677 LEU A CD2   1 
ATOM   14646 N  N     . LEU A 1 2461 ? 174.382 109.276 146.987 1.00 81.48  ? 3678 LEU A N     1 
ATOM   14647 C  CA    . LEU A 1 2461 ? 173.724 110.487 147.469 1.00 80.96  ? 3678 LEU A CA    1 
ATOM   14648 C  C     . LEU A 1 2461 ? 174.167 111.709 146.674 1.00 80.24  ? 3678 LEU A C     1 
ATOM   14649 O  O     . LEU A 1 2461 ? 173.329 112.494 146.211 1.00 83.03  ? 3678 LEU A O     1 
ATOM   14650 C  CB    . LEU A 1 2461 ? 174.002 110.692 148.959 1.00 82.48  ? 3678 LEU A CB    1 
ATOM   14651 C  CG    . LEU A 1 2461 ? 173.588 112.070 149.487 1.00 78.21  ? 3678 LEU A CG    1 
ATOM   14652 C  CD1   . LEU A 1 2461 ? 172.076 112.217 149.475 1.00 80.80  ? 3678 LEU A CD1   1 
ATOM   14653 C  CD2   . LEU A 1 2461 ? 174.137 112.323 150.879 1.00 79.04  ? 3678 LEU A CD2   1 
ATOM   14654 N  N     . TYR A 1 2462 ? 175.482 111.875 146.485 1.00 79.59  ? 3679 TYR A N     1 
ATOM   14655 C  CA    . TYR A 1 2462 ? 175.975 113.015 145.710 1.00 77.41  ? 3679 TYR A CA    1 
ATOM   14656 C  C     . TYR A 1 2462 ? 175.474 112.988 144.272 1.00 77.33  ? 3679 TYR A C     1 
ATOM   14657 O  O     . TYR A 1 2462 ? 175.043 114.018 143.740 1.00 76.60  ? 3679 TYR A O     1 
ATOM   14658 C  CB    . TYR A 1 2462 ? 177.502 113.079 145.726 1.00 76.47  ? 3679 TYR A CB    1 
ATOM   14659 C  CG    . TYR A 1 2462 ? 178.104 113.603 147.003 1.00 75.14  ? 3679 TYR A CG    1 
ATOM   14660 C  CD1   . TYR A 1 2462 ? 177.321 114.235 147.956 1.00 72.95  ? 3679 TYR A CD1   1 
ATOM   14661 C  CD2   . TYR A 1 2462 ? 179.471 113.538 147.220 1.00 75.93  ? 3679 TYR A CD2   1 
ATOM   14662 C  CE1   . TYR A 1 2462 ? 177.878 114.738 149.111 1.00 74.46  ? 3679 TYR A CE1   1 
ATOM   14663 C  CE2   . TYR A 1 2462 ? 180.032 114.047 148.368 1.00 76.83  ? 3679 TYR A CE2   1 
ATOM   14664 C  CZ    . TYR A 1 2462 ? 179.232 114.642 149.309 1.00 77.74  ? 3679 TYR A CZ    1 
ATOM   14665 O  OH    . TYR A 1 2462 ? 179.793 115.149 150.452 1.00 84.47  ? 3679 TYR A OH    1 
ATOM   14666 N  N     . GLN A 1 2463 ? 175.527 111.821 143.622 1.00 77.61  ? 3680 GLN A N     1 
ATOM   14667 C  CA    . GLN A 1 2463 ? 175.127 111.752 142.221 1.00 74.95  ? 3680 GLN A CA    1 
ATOM   14668 C  C     . GLN A 1 2463 ? 173.643 112.044 142.050 1.00 74.58  ? 3680 GLN A C     1 
ATOM   14669 O  O     . GLN A 1 2463 ? 173.258 112.802 141.153 1.00 78.74  ? 3680 GLN A O     1 
ATOM   14670 C  CB    . GLN A 1 2463 ? 175.482 110.391 141.627 1.00 77.78  ? 3680 GLN A CB    1 
ATOM   14671 C  CG    . GLN A 1 2463 ? 176.974 110.160 141.468 1.00 82.30  ? 3680 GLN A CG    1 
ATOM   14672 C  CD    . GLN A 1 2463 ? 177.600 111.071 140.433 1.00 85.00  ? 3680 GLN A CD    1 
ATOM   14673 O  OE1   . GLN A 1 2463 ? 178.105 112.145 140.759 1.00 84.84  ? 3680 GLN A OE1   1 
ATOM   14674 N  NE2   . GLN A 1 2463 ? 177.571 110.646 139.175 1.00 89.05  ? 3680 GLN A NE2   1 
ATOM   14675 N  N     . GLU A 1 2464 ? 172.794 111.479 142.915 1.00 75.55  ? 3681 GLU A N     1 
ATOM   14676 C  CA    . GLU A 1 2464 ? 171.365 111.749 142.801 1.00 76.81  ? 3681 GLU A CA    1 
ATOM   14677 C  C     . GLU A 1 2464 ? 171.041 113.204 143.119 1.00 73.43  ? 3681 GLU A C     1 
ATOM   14678 O  O     . GLU A 1 2464 ? 170.225 113.823 142.424 1.00 72.13  ? 3681 GLU A O     1 
ATOM   14679 C  CB    . GLU A 1 2464 ? 170.573 110.810 143.709 1.00 81.33  ? 3681 GLU A CB    1 
ATOM   14680 C  CG    . GLU A 1 2464 ? 169.070 111.070 143.709 1.00 87.33  ? 3681 GLU A CG    1 
ATOM   14681 C  CD    . GLU A 1 2464 ? 168.331 110.300 142.627 1.00 95.63  ? 3681 GLU A CD    1 
ATOM   14682 O  OE1   . GLU A 1 2464 ? 168.981 109.822 141.674 1.00 96.84  ? 3681 GLU A OE1   1 
ATOM   14683 O  OE2   . GLU A 1 2464 ? 167.092 110.179 142.727 1.00 94.20  ? 3681 GLU A OE2   1 
ATOM   14684 N  N     . VAL A 1 2465 ? 171.680 113.776 144.146 1.00 73.86  ? 3682 VAL A N     1 
ATOM   14685 C  CA    . VAL A 1 2465 ? 171.395 115.162 144.513 1.00 71.49  ? 3682 VAL A CA    1 
ATOM   14686 C  C     . VAL A 1 2465 ? 171.809 116.106 143.390 1.00 70.08  ? 3682 VAL A C     1 
ATOM   14687 O  O     . VAL A 1 2465 ? 171.055 117.010 143.012 1.00 70.59  ? 3682 VAL A O     1 
ATOM   14688 C  CB    . VAL A 1 2465 ? 172.081 115.521 145.844 1.00 70.98  ? 3682 VAL A CB    1 
ATOM   14689 C  CG1   . VAL A 1 2465 ? 172.171 117.026 146.013 1.00 66.62  ? 3682 VAL A CG1   1 
ATOM   14690 C  CG2   . VAL A 1 2465 ? 171.317 114.917 147.006 1.00 75.82  ? 3682 VAL A CG2   1 
ATOM   14691 N  N     . TYR A 1 2466 ? 173.001 115.895 142.820 1.00 70.25  ? 3683 TYR A N     1 
ATOM   14692 C  CA    . TYR A 1 2466 ? 173.444 116.729 141.706 1.00 64.29  ? 3683 TYR A CA    1 
ATOM   14693 C  C     . TYR A 1 2466 ? 172.535 116.564 140.496 1.00 63.97  ? 3683 TYR A C     1 
ATOM   14694 O  O     . TYR A 1 2466 ? 172.086 117.552 139.905 1.00 63.13  ? 3683 TYR A O     1 
ATOM   14695 C  CB    . TYR A 1 2466 ? 174.884 116.389 141.326 1.00 64.29  ? 3683 TYR A CB    1 
ATOM   14696 C  CG    . TYR A 1 2466 ? 175.340 117.066 140.052 1.00 64.40  ? 3683 TYR A CG    1 
ATOM   14697 C  CD1   . TYR A 1 2466 ? 175.490 118.443 139.992 1.00 60.60  ? 3683 TYR A CD1   1 
ATOM   14698 C  CD2   . TYR A 1 2466 ? 175.601 116.331 138.903 1.00 67.20  ? 3683 TYR A CD2   1 
ATOM   14699 C  CE1   . TYR A 1 2466 ? 175.904 119.071 138.833 1.00 57.35  ? 3683 TYR A CE1   1 
ATOM   14700 C  CE2   . TYR A 1 2466 ? 176.015 116.952 137.736 1.00 68.42  ? 3683 TYR A CE2   1 
ATOM   14701 C  CZ    . TYR A 1 2466 ? 176.163 118.324 137.709 1.00 61.64  ? 3683 TYR A CZ    1 
ATOM   14702 O  OH    . TYR A 1 2466 ? 176.572 118.952 136.556 1.00 52.11  ? 3683 TYR A OH    1 
ATOM   14703 N  N     . CYS A 1 2467 ? 172.230 115.318 140.128 1.00 67.03  ? 3684 CYS A N     1 
ATOM   14704 C  CA    . CYS A 1 2467 ? 171.456 115.054 138.925 1.00 65.68  ? 3684 CYS A CA    1 
ATOM   14705 C  C     . CYS A 1 2467 ? 170.014 115.530 139.049 1.00 68.99  ? 3684 CYS A C     1 
ATOM   14706 O  O     . CYS A 1 2467 ? 169.380 115.814 138.028 1.00 71.19  ? 3684 CYS A O     1 
ATOM   14707 C  CB    . CYS A 1 2467 ? 171.519 113.556 138.613 1.00 67.06  ? 3684 CYS A CB    1 
ATOM   14708 S  SG    . CYS A 1 2467 ? 170.439 112.958 137.307 1.00 69.44  ? 3684 CYS A SG    1 
ATOM   14709 N  N     . GLN A 1 2468 ? 169.491 115.654 140.268 1.00 68.74  ? 3685 GLN A N     1 
ATOM   14710 C  CA    . GLN A 1 2468 ? 168.132 116.143 140.450 1.00 67.44  ? 3685 GLN A CA    1 
ATOM   14711 C  C     . GLN A 1 2468 ? 168.062 117.648 140.675 1.00 66.10  ? 3685 GLN A C     1 
ATOM   14712 O  O     . GLN A 1 2468 ? 167.084 118.275 140.256 1.00 69.34  ? 3685 GLN A O     1 
ATOM   14713 C  CB    . GLN A 1 2468 ? 167.465 115.408 141.622 1.00 66.18  ? 3685 GLN A CB    1 
ATOM   14714 C  CG    . GLN A 1 2468 ? 165.962 115.647 141.784 1.00 68.36  ? 3685 GLN A CG    1 
ATOM   14715 C  CD    . GLN A 1 2468 ? 165.629 116.877 142.602 1.00 67.84  ? 3685 GLN A CD    1 
ATOM   14716 O  OE1   . GLN A 1 2468 ? 166.388 117.271 143.483 1.00 64.99  ? 3685 GLN A OE1   1 
ATOM   14717 N  NE2   . GLN A 1 2468 ? 164.490 117.492 142.311 1.00 69.96  ? 3685 GLN A NE2   1 
ATOM   14718 N  N     . PHE A 1 2469 ? 169.069 118.252 141.311 1.00 63.04  ? 3686 PHE A N     1 
ATOM   14719 C  CA    . PHE A 1 2469 ? 169.050 119.676 141.617 1.00 56.59  ? 3686 PHE A CA    1 
ATOM   14720 C  C     . PHE A 1 2469 ? 169.830 120.524 140.620 1.00 53.20  ? 3686 PHE A C     1 
ATOM   14721 O  O     . PHE A 1 2469 ? 169.887 121.745 140.789 1.00 53.93  ? 3686 PHE A O     1 
ATOM   14722 C  CB    . PHE A 1 2469 ? 169.604 119.921 143.025 1.00 57.50  ? 3686 PHE A CB    1 
ATOM   14723 C  CG    . PHE A 1 2469 ? 168.658 119.544 144.133 1.00 61.69  ? 3686 PHE A CG    1 
ATOM   14724 C  CD1   . PHE A 1 2469 ? 167.508 120.279 144.360 1.00 60.77  ? 3686 PHE A CD1   1 
ATOM   14725 C  CD2   . PHE A 1 2469 ? 168.934 118.469 144.961 1.00 63.58  ? 3686 PHE A CD2   1 
ATOM   14726 C  CE1   . PHE A 1 2469 ? 166.642 119.940 145.384 1.00 62.08  ? 3686 PHE A CE1   1 
ATOM   14727 C  CE2   . PHE A 1 2469 ? 168.073 118.126 145.987 1.00 64.23  ? 3686 PHE A CE2   1 
ATOM   14728 C  CZ    . PHE A 1 2469 ? 166.926 118.862 146.198 1.00 67.31  ? 3686 PHE A CZ    1 
ATOM   14729 N  N     . SER A 1 2470 ? 170.438 119.921 139.596 1.00 54.56  ? 3687 SER A N     1 
ATOM   14730 C  CA    . SER A 1 2470 ? 171.179 120.719 138.627 1.00 54.04  ? 3687 SER A CA    1 
ATOM   14731 C  C     . SER A 1 2470 ? 170.256 121.446 137.658 1.00 54.70  ? 3687 SER A C     1 
ATOM   14732 O  O     . SER A 1 2470 ? 170.534 122.586 137.274 1.00 55.77  ? 3687 SER A O     1 
ATOM   14733 C  CB    . SER A 1 2470 ? 172.154 119.832 137.854 1.00 57.70  ? 3687 SER A CB    1 
ATOM   14734 O  OG    . SER A 1 2470 ? 171.498 119.164 136.791 1.00 56.19  ? 3687 SER A OG    1 
ATOM   14735 N  N     . THR A 1 2471 ? 169.159 120.803 137.251 1.00 54.84  ? 3688 THR A N     1 
ATOM   14736 C  CA    . THR A 1 2471 ? 168.295 121.360 136.216 1.00 50.89  ? 3688 THR A CA    1 
ATOM   14737 C  C     . THR A 1 2471 ? 167.612 122.653 136.642 1.00 50.64  ? 3688 THR A C     1 
ATOM   14738 O  O     . THR A 1 2471 ? 167.240 123.452 135.778 1.00 55.63  ? 3688 THR A O     1 
ATOM   14739 C  CB    . THR A 1 2471 ? 167.242 120.333 135.809 1.00 57.72  ? 3688 THR A CB    1 
ATOM   14740 O  OG1   . THR A 1 2471 ? 166.293 120.172 136.871 1.00 59.29  ? 3688 THR A OG1   1 
ATOM   14741 C  CG2   . THR A 1 2471 ? 167.902 118.996 135.517 1.00 66.08  ? 3688 THR A CG2   1 
ATOM   14742 N  N     . ALA A 1 2472 ? 167.453 122.885 137.944 1.00 50.17  ? 3689 ALA A N     1 
ATOM   14743 C  CA    . ALA A 1 2472 ? 166.798 124.083 138.448 1.00 52.44  ? 3689 ALA A CA    1 
ATOM   14744 C  C     . ALA A 1 2472 ? 167.741 125.276 138.559 1.00 52.59  ? 3689 ALA A C     1 
ATOM   14745 O  O     . ALA A 1 2472 ? 167.424 126.235 139.271 1.00 54.25  ? 3689 ALA A O     1 
ATOM   14746 C  CB    . ALA A 1 2472 ? 166.158 123.796 139.808 1.00 51.04  ? 3689 ALA A CB    1 
ATOM   14747 N  N     . LEU A 1 2473 ? 168.881 125.243 137.874 1.00 51.66  ? 3690 LEU A N     1 
ATOM   14748 C  CA    . LEU A 1 2473 ? 169.893 126.283 137.973 1.00 50.25  ? 3690 LEU A CA    1 
ATOM   14749 C  C     . LEU A 1 2473 ? 170.349 126.698 136.581 1.00 51.46  ? 3690 LEU A C     1 
ATOM   14750 O  O     . LEU A 1 2473 ? 170.277 125.925 135.622 1.00 53.83  ? 3690 LEU A O     1 
ATOM   14751 C  CB    . LEU A 1 2473 ? 171.108 125.810 138.789 1.00 50.09  ? 3690 LEU A CB    1 
ATOM   14752 C  CG    . LEU A 1 2473 ? 171.206 126.096 140.289 1.00 50.88  ? 3690 LEU A CG    1 
ATOM   14753 C  CD1   . LEU A 1 2473 ? 170.103 125.413 141.077 1.00 48.22  ? 3690 LEU A CD1   1 
ATOM   14754 C  CD2   . LEU A 1 2473 ? 172.563 125.650 140.800 1.00 51.31  ? 3690 LEU A CD2   1 
ATOM   14755 N  N     . ASP A 1 2474 ? 170.825 127.936 136.484 1.00 45.57  ? 3691 ASP A N     1 
ATOM   14756 C  CA    . ASP A 1 2474 ? 171.459 128.429 135.271 1.00 41.37  ? 3691 ASP A CA    1 
ATOM   14757 C  C     . ASP A 1 2474 ? 172.874 127.861 135.147 1.00 46.24  ? 3691 ASP A C     1 
ATOM   14758 O  O     . ASP A 1 2474 ? 173.369 127.173 136.042 1.00 54.95  ? 3691 ASP A O     1 
ATOM   14759 C  CB    . ASP A 1 2474 ? 171.375 129.960 135.240 1.00 43.58  ? 3691 ASP A CB    1 
ATOM   14760 C  CG    . ASP A 1 2474 ? 172.236 130.651 136.300 1.00 51.23  ? 3691 ASP A CG    1 
ATOM   14761 O  OD1   . ASP A 1 2474 ? 171.759 131.671 136.840 1.00 54.69  ? 3691 ASP A OD1   1 
ATOM   14762 O  OD2   . ASP A 1 2474 ? 173.358 130.218 136.617 1.00 54.83  ? 3691 ASP A OD2   1 
ATOM   14763 N  N     . LYS A 1 2475 ? 173.546 128.167 134.032 1.00 46.92  ? 3692 LYS A N     1 
ATOM   14764 C  CA    . LYS A 1 2475 ? 174.794 127.474 133.708 1.00 49.84  ? 3692 LYS A CA    1 
ATOM   14765 C  C     . LYS A 1 2475 ? 175.920 127.822 134.680 1.00 51.59  ? 3692 LYS A C     1 
ATOM   14766 O  O     . LYS A 1 2475 ? 176.682 126.935 135.089 1.00 52.73  ? 3692 LYS A O     1 
ATOM   14767 C  CB    . LYS A 1 2475 ? 175.212 127.765 132.263 1.00 52.36  ? 3692 LYS A CB    1 
ATOM   14768 C  CG    . LYS A 1 2475 ? 175.448 129.228 131.918 1.00 59.77  ? 3692 LYS A CG    1 
ATOM   14769 C  CD    . LYS A 1 2475 ? 176.379 129.357 130.723 1.00 64.63  ? 3692 LYS A CD    1 
ATOM   14770 C  CE    . LYS A 1 2475 ? 176.769 130.804 130.472 1.00 60.22  ? 3692 LYS A CE    1 
ATOM   14771 N  NZ    . LYS A 1 2475 ? 177.516 130.963 129.193 1.00 56.27  ? 3692 LYS A NZ    1 
ATOM   14772 N  N     . LYS A 1 2476 ? 176.039 129.093 135.076 1.00 51.01  ? 3693 LYS A N     1 
ATOM   14773 C  CA    . LYS A 1 2476 ? 177.137 129.466 135.962 1.00 52.18  ? 3693 LYS A CA    1 
ATOM   14774 C  C     . LYS A 1 2476 ? 176.935 128.890 137.357 1.00 54.25  ? 3693 LYS A C     1 
ATOM   14775 O  O     . LYS A 1 2476 ? 177.871 128.331 137.937 1.00 60.21  ? 3693 LYS A O     1 
ATOM   14776 C  CB    . LYS A 1 2476 ? 177.313 130.987 136.009 1.00 51.84  ? 3693 LYS A CB    1 
ATOM   14777 C  CG    . LYS A 1 2476 ? 176.047 131.788 136.222 1.00 58.72  ? 3693 LYS A CG    1 
ATOM   14778 C  CD    . LYS A 1 2476 ? 176.246 133.249 135.869 1.00 65.29  ? 3693 LYS A CD    1 
ATOM   14779 C  CE    . LYS A 1 2476 ? 176.134 133.483 134.372 1.00 60.02  ? 3693 LYS A CE    1 
ATOM   14780 N  NZ    . LYS A 1 2476 ? 174.726 133.378 133.901 1.00 48.34  ? 3693 LYS A NZ    1 
ATOM   14781 N  N     . PHE A 1 2477 ? 175.716 128.975 137.897 1.00 52.43  ? 3694 PHE A N     1 
ATOM   14782 C  CA    . PHE A 1 2477 ? 175.460 128.341 139.185 1.00 50.74  ? 3694 PHE A CA    1 
ATOM   14783 C  C     . PHE A 1 2477 ? 175.519 126.824 139.096 1.00 51.82  ? 3694 PHE A C     1 
ATOM   14784 O  O     . PHE A 1 2477 ? 175.849 126.168 140.088 1.00 56.68  ? 3694 PHE A O     1 
ATOM   14785 C  CB    . PHE A 1 2477 ? 174.111 128.770 139.757 1.00 49.83  ? 3694 PHE A CB    1 
ATOM   14786 C  CG    . PHE A 1 2477 ? 174.089 130.172 140.281 1.00 58.28  ? 3694 PHE A CG    1 
ATOM   14787 C  CD1   . PHE A 1 2477 ? 175.257 130.898 140.416 1.00 64.45  ? 3694 PHE A CD1   1 
ATOM   14788 C  CD2   . PHE A 1 2477 ? 172.901 130.744 140.691 1.00 62.94  ? 3694 PHE A CD2   1 
ATOM   14789 C  CE1   . PHE A 1 2477 ? 175.236 132.184 140.918 1.00 73.53  ? 3694 PHE A CE1   1 
ATOM   14790 C  CE2   . PHE A 1 2477 ? 172.872 132.021 141.193 1.00 71.65  ? 3694 PHE A CE2   1 
ATOM   14791 C  CZ    . PHE A 1 2477 ? 174.041 132.744 141.307 1.00 76.06  ? 3694 PHE A CZ    1 
ATOM   14792 N  N     . LYS A 1 2478 ? 175.201 126.245 137.935 1.00 51.43  ? 3695 LYS A N     1 
ATOM   14793 C  CA    . LYS A 1 2478 ? 175.401 124.808 137.767 1.00 50.25  ? 3695 LYS A CA    1 
ATOM   14794 C  C     . LYS A 1 2478 ? 176.874 124.447 137.896 1.00 54.01  ? 3695 LYS A C     1 
ATOM   14795 O  O     . LYS A 1 2478 ? 177.226 123.503 138.612 1.00 61.81  ? 3695 LYS A O     1 
ATOM   14796 C  CB    . LYS A 1 2478 ? 174.853 124.339 136.419 1.00 51.21  ? 3695 LYS A CB    1 
ATOM   14797 C  CG    . LYS A 1 2478 ? 173.454 123.749 136.491 1.00 49.42  ? 3695 LYS A CG    1 
ATOM   14798 C  CD    . LYS A 1 2478 ? 172.738 123.804 135.145 1.00 47.46  ? 3695 LYS A CD    1 
ATOM   14799 C  CE    . LYS A 1 2478 ? 173.460 122.990 134.082 1.00 48.06  ? 3695 LYS A CE    1 
ATOM   14800 N  NZ    . LYS A 1 2478 ? 173.332 121.527 134.322 1.00 55.43  ? 3695 LYS A NZ    1 
ATOM   14801 N  N     . MET A 1 2479 ? 177.749 125.211 137.236 1.00 51.01  ? 3696 MET A N     1 
ATOM   14802 C  CA    . MET A 1 2479 ? 179.186 124.975 137.361 1.00 54.53  ? 3696 MET A CA    1 
ATOM   14803 C  C     . MET A 1 2479 ? 179.659 125.185 138.797 1.00 57.82  ? 3696 MET A C     1 
ATOM   14804 O  O     . MET A 1 2479 ? 180.467 124.401 139.318 1.00 59.70  ? 3696 MET A O     1 
ATOM   14805 C  CB    . MET A 1 2479 ? 179.936 125.895 136.398 1.00 55.79  ? 3696 MET A CB    1 
ATOM   14806 C  CG    . MET A 1 2479 ? 179.833 125.466 134.940 1.00 64.46  ? 3696 MET A CG    1 
ATOM   14807 S  SD    . MET A 1 2479 ? 180.233 126.757 133.742 1.00 75.26  ? 3696 MET A SD    1 
ATOM   14808 C  CE    . MET A 1 2479 ? 181.287 127.829 134.708 1.00 64.66  ? 3696 MET A CE    1 
ATOM   14809 N  N     . ILE A 1 2480 ? 179.142 126.225 139.455 1.00 55.92  ? 3697 ILE A N     1 
ATOM   14810 C  CA    . ILE A 1 2480 ? 179.527 126.538 140.831 1.00 53.66  ? 3697 ILE A CA    1 
ATOM   14811 C  C     . ILE A 1 2480 ? 179.150 125.398 141.766 1.00 55.19  ? 3697 ILE A C     1 
ATOM   14812 O  O     . ILE A 1 2480 ? 179.966 124.928 142.570 1.00 64.22  ? 3697 ILE A O     1 
ATOM   14813 C  CB    . ILE A 1 2480 ? 178.874 127.861 141.270 1.00 54.32  ? 3697 ILE A CB    1 
ATOM   14814 C  CG1   . ILE A 1 2480 ? 179.569 129.038 140.591 1.00 55.69  ? 3697 ILE A CG1   1 
ATOM   14815 C  CG2   . ILE A 1 2480 ? 178.896 128.006 142.784 1.00 53.90  ? 3697 ILE A CG2   1 
ATOM   14816 C  CD1   . ILE A 1 2480 ? 178.687 130.240 140.387 1.00 59.68  ? 3697 ILE A CD1   1 
ATOM   14817 N  N     . MET A 1 2481 ? 177.908 124.927 141.664 1.00 53.27  ? 3698 MET A N     1 
ATOM   14818 C  CA    . MET A 1 2481 ? 177.436 123.877 142.555 1.00 55.13  ? 3698 MET A CA    1 
ATOM   14819 C  C     . MET A 1 2481 ? 178.126 122.553 142.254 1.00 57.87  ? 3698 MET A C     1 
ATOM   14820 O  O     . MET A 1 2481 ? 178.453 121.799 143.178 1.00 62.20  ? 3698 MET A O     1 
ATOM   14821 C  CB    . MET A 1 2481 ? 175.910 123.782 142.453 1.00 50.17  ? 3698 MET A CB    1 
ATOM   14822 C  CG    . MET A 1 2481 ? 175.241 122.614 143.158 1.00 50.74  ? 3698 MET A CG    1 
ATOM   14823 S  SD    . MET A 1 2481 ? 175.136 121.125 142.162 1.00 59.85  ? 3698 MET A SD    1 
ATOM   14824 C  CE    . MET A 1 2481 ? 174.652 121.854 140.601 1.00 58.52  ? 3698 MET A CE    1 
ATOM   14825 N  N     . ALA A 1 2482 ? 178.394 122.271 140.974 1.00 53.47  ? 3699 ALA A N     1 
ATOM   14826 C  CA    . ALA A 1 2482 ? 179.121 121.058 140.617 1.00 55.66  ? 3699 ALA A CA    1 
ATOM   14827 C  C     . ALA A 1 2482 ? 180.522 121.059 141.210 1.00 60.27  ? 3699 ALA A C     1 
ATOM   14828 O  O     . ALA A 1 2482 ? 180.969 120.048 141.764 1.00 68.12  ? 3699 ALA A O     1 
ATOM   14829 C  CB    . ALA A 1 2482 ? 179.183 120.913 139.097 1.00 60.49  ? 3699 ALA A CB    1 
ATOM   14830 N  N     . MET A 1 2483 ? 181.220 122.196 141.137 1.00 59.10  ? 3700 MET A N     1 
ATOM   14831 C  CA    . MET A 1 2483 ? 182.554 122.251 141.727 1.00 60.87  ? 3700 MET A CA    1 
ATOM   14832 C  C     . MET A 1 2483 ? 182.516 122.236 143.246 1.00 61.17  ? 3700 MET A C     1 
ATOM   14833 O  O     . MET A 1 2483 ? 183.447 121.723 143.877 1.00 65.97  ? 3700 MET A O     1 
ATOM   14834 C  CB    . MET A 1 2483 ? 183.312 123.470 141.219 1.00 57.81  ? 3700 MET A CB    1 
ATOM   14835 C  CG    . MET A 1 2483 ? 183.643 123.389 139.745 1.00 69.09  ? 3700 MET A CG    1 
ATOM   14836 S  SD    . MET A 1 2483 ? 184.711 121.969 139.413 1.00 63.84  ? 3700 MET A SD    1 
ATOM   14837 C  CE    . MET A 1 2483 ? 183.580 120.770 138.689 1.00 68.94  ? 3700 MET A CE    1 
ATOM   14838 N  N     . THR A 1 2484 ? 181.454 122.762 143.854 1.00 56.93  ? 3701 THR A N     1 
ATOM   14839 C  CA    . THR A 1 2484 ? 181.378 122.687 145.307 1.00 55.35  ? 3701 THR A CA    1 
ATOM   14840 C  C     . THR A 1 2484 ? 181.159 121.249 145.771 1.00 62.74  ? 3701 THR A C     1 
ATOM   14841 O  O     . THR A 1 2484 ? 181.761 120.821 146.761 1.00 69.12  ? 3701 THR A O     1 
ATOM   14842 C  CB    . THR A 1 2484 ? 180.288 123.609 145.841 1.00 53.93  ? 3701 THR A CB    1 
ATOM   14843 O  OG1   . THR A 1 2484 ? 180.506 124.931 145.336 1.00 61.38  ? 3701 THR A OG1   1 
ATOM   14844 C  CG2   . THR A 1 2484 ? 180.385 123.675 147.352 1.00 60.75  ? 3701 THR A CG2   1 
ATOM   14845 N  N     . MET A 1 2485 ? 180.326 120.476 145.062 1.00 62.27  ? 3702 MET A N     1 
ATOM   14846 C  CA    . MET A 1 2485 ? 180.221 119.051 145.392 1.00 62.04  ? 3702 MET A CA    1 
ATOM   14847 C  C     . MET A 1 2485 ? 181.514 118.301 145.095 1.00 64.48  ? 3702 MET A C     1 
ATOM   14848 O  O     . MET A 1 2485 ? 181.877 117.373 145.830 1.00 67.43  ? 3702 MET A O     1 
ATOM   14849 C  CB    . MET A 1 2485 ? 179.050 118.384 144.669 1.00 56.35  ? 3702 MET A CB    1 
ATOM   14850 C  CG    . MET A 1 2485 ? 177.783 119.184 144.615 1.00 53.49  ? 3702 MET A CG    1 
ATOM   14851 S  SD    . MET A 1 2485 ? 176.966 119.176 146.213 1.00 46.54  ? 3702 MET A SD    1 
ATOM   14852 C  CE    . MET A 1 2485 ? 175.682 117.979 145.900 1.00 66.43  ? 3702 MET A CE    1 
ATOM   14853 N  N     . PHE A 1 2486 ? 182.221 118.680 144.024 1.00 65.20  ? 3703 PHE A N     1 
ATOM   14854 C  CA    . PHE A 1 2486 ? 183.517 118.068 143.743 1.00 64.46  ? 3703 PHE A CA    1 
ATOM   14855 C  C     . PHE A 1 2486 ? 184.484 118.281 144.897 1.00 67.38  ? 3703 PHE A C     1 
ATOM   14856 O  O     . PHE A 1 2486 ? 185.179 117.349 145.317 1.00 73.96  ? 3703 PHE A O     1 
ATOM   14857 C  CB    . PHE A 1 2486 ? 184.097 118.637 142.448 1.00 67.34  ? 3703 PHE A CB    1 
ATOM   14858 C  CG    . PHE A 1 2486 ? 185.541 118.278 142.214 1.00 70.46  ? 3703 PHE A CG    1 
ATOM   14859 C  CD1   . PHE A 1 2486 ? 185.884 117.044 141.692 1.00 69.90  ? 3703 PHE A CD1   1 
ATOM   14860 C  CD2   . PHE A 1 2486 ? 186.553 119.185 142.492 1.00 71.68  ? 3703 PHE A CD2   1 
ATOM   14861 C  CE1   . PHE A 1 2486 ? 187.206 116.714 141.462 1.00 70.10  ? 3703 PHE A CE1   1 
ATOM   14862 C  CE2   . PHE A 1 2486 ? 187.878 118.858 142.270 1.00 72.56  ? 3703 PHE A CE2   1 
ATOM   14863 C  CZ    . PHE A 1 2486 ? 188.204 117.621 141.754 1.00 71.67  ? 3703 PHE A CZ    1 
ATOM   14864 N  N     . CYS A 1 2487 ? 184.530 119.502 145.429 1.00 66.86  ? 3704 CYS A N     1 
ATOM   14865 C  CA    . CYS A 1 2487 ? 185.388 119.783 146.574 1.00 74.97  ? 3704 CYS A CA    1 
ATOM   14866 C  C     . CYS A 1 2487 ? 184.910 119.041 147.819 1.00 75.61  ? 3704 CYS A C     1 
ATOM   14867 O  O     . CYS A 1 2487 ? 185.712 118.427 148.530 1.00 79.74  ? 3704 CYS A O     1 
ATOM   14868 C  CB    . CYS A 1 2487 ? 185.448 121.289 146.820 1.00 74.99  ? 3704 CYS A CB    1 
ATOM   14869 S  SG    . CYS A 1 2487 ? 186.347 122.203 145.542 1.00 68.11  ? 3704 CYS A SG    1 
ATOM   14870 N  N     . LEU A 1 2488 ? 183.599 119.059 148.080 1.00 71.30  ? 3705 LEU A N     1 
ATOM   14871 C  CA    . LEU A 1 2488 ? 183.050 118.404 149.264 1.00 72.50  ? 3705 LEU A CA    1 
ATOM   14872 C  C     . LEU A 1 2488 ? 183.225 116.890 149.235 1.00 74.65  ? 3705 LEU A C     1 
ATOM   14873 O  O     . LEU A 1 2488 ? 183.151 116.252 150.290 1.00 77.14  ? 3705 LEU A O     1 
ATOM   14874 C  CB    . LEU A 1 2488 ? 181.567 118.749 149.413 1.00 68.72  ? 3705 LEU A CB    1 
ATOM   14875 C  CG    . LEU A 1 2488 ? 181.185 119.830 150.427 1.00 67.62  ? 3705 LEU A CG    1 
ATOM   14876 C  CD1   . LEU A 1 2488 ? 181.767 121.177 150.039 1.00 63.81  ? 3705 LEU A CD1   1 
ATOM   14877 C  CD2   . LEU A 1 2488 ? 179.673 119.922 150.563 1.00 73.55  ? 3705 LEU A CD2   1 
ATOM   14878 N  N     . TYR A 1 2489 ? 183.445 116.303 148.060 1.00 70.87  ? 3706 TYR A N     1 
ATOM   14879 C  CA    . TYR A 1 2489 ? 183.729 114.876 147.979 1.00 71.69  ? 3706 TYR A CA    1 
ATOM   14880 C  C     . TYR A 1 2489 ? 185.228 114.594 148.041 1.00 75.29  ? 3706 TYR A C     1 
ATOM   14881 O  O     . TYR A 1 2489 ? 185.679 113.760 148.840 1.00 83.71  ? 3706 TYR A O     1 
ATOM   14882 C  CB    . TYR A 1 2489 ? 183.123 114.301 146.695 1.00 74.29  ? 3706 TYR A CB    1 
ATOM   14883 C  CG    . TYR A 1 2489 ? 183.225 112.799 146.563 1.00 74.40  ? 3706 TYR A CG    1 
ATOM   14884 C  CD1   . TYR A 1 2489 ? 182.617 111.963 147.486 1.00 76.21  ? 3706 TYR A CD1   1 
ATOM   14885 C  CD2   . TYR A 1 2489 ? 183.891 112.216 145.495 1.00 74.99  ? 3706 TYR A CD2   1 
ATOM   14886 C  CE1   . TYR A 1 2489 ? 182.690 110.591 147.370 1.00 78.13  ? 3706 TYR A CE1   1 
ATOM   14887 C  CE2   . TYR A 1 2489 ? 183.962 110.841 145.363 1.00 80.66  ? 3706 TYR A CE2   1 
ATOM   14888 C  CZ    . TYR A 1 2489 ? 183.364 110.034 146.309 1.00 82.62  ? 3706 TYR A CZ    1 
ATOM   14889 O  OH    . TYR A 1 2489 ? 183.432 108.664 146.199 1.00 84.75  ? 3706 TYR A OH    1 
ATOM   14890 N  N     . LYS A 1 2490 ? 186.014 115.301 147.223 1.00 74.02  ? 3707 LYS A N     1 
ATOM   14891 C  CA    . LYS A 1 2490 ? 187.442 115.039 147.122 1.00 79.34  ? 3707 LYS A CA    1 
ATOM   14892 C  C     . LYS A 1 2490 ? 188.233 115.558 148.315 1.00 83.87  ? 3707 LYS A C     1 
ATOM   14893 O  O     . LYS A 1 2490 ? 189.421 115.236 148.427 1.00 85.36  ? 3707 LYS A O     1 
ATOM   14894 C  CB    . LYS A 1 2490 ? 187.996 115.656 145.838 1.00 77.50  ? 3707 LYS A CB    1 
ATOM   14895 C  CG    . LYS A 1 2490 ? 187.436 115.057 144.557 1.00 73.51  ? 3707 LYS A CG    1 
ATOM   14896 C  CD    . LYS A 1 2490 ? 187.361 113.544 144.615 1.00 73.63  ? 3707 LYS A CD    1 
ATOM   14897 C  CE    . LYS A 1 2490 ? 187.216 112.944 143.228 1.00 69.26  ? 3707 LYS A CE    1 
ATOM   14898 N  NZ    . LYS A 1 2490 ? 187.127 111.460 143.276 1.00 70.57  ? 3707 LYS A NZ    1 
ATOM   14899 N  N     . PHE A 1 2491 ? 187.626 116.351 149.199 1.00 82.23  ? 3708 PHE A N     1 
ATOM   14900 C  CA    . PHE A 1 2491 ? 188.333 116.795 150.391 1.00 85.16  ? 3708 PHE A CA    1 
ATOM   14901 C  C     . PHE A 1 2491 ? 188.115 115.867 151.571 1.00 88.88  ? 3708 PHE A C     1 
ATOM   14902 O  O     . PHE A 1 2491 ? 188.860 115.948 152.555 1.00 88.06  ? 3708 PHE A O     1 
ATOM   14903 C  CB    . PHE A 1 2491 ? 187.897 118.210 150.789 1.00 83.40  ? 3708 PHE A CB    1 
ATOM   14904 C  CG    . PHE A 1 2491 ? 188.301 119.280 149.809 1.00 83.74  ? 3708 PHE A CG    1 
ATOM   14905 C  CD1   . PHE A 1 2491 ? 189.113 118.993 148.720 1.00 81.89  ? 3708 PHE A CD1   1 
ATOM   14906 C  CD2   . PHE A 1 2491 ? 187.845 120.575 149.970 1.00 79.58  ? 3708 PHE A CD2   1 
ATOM   14907 C  CE1   . PHE A 1 2491 ? 189.462 119.973 147.822 1.00 79.39  ? 3708 PHE A CE1   1 
ATOM   14908 C  CE2   . PHE A 1 2491 ? 188.196 121.559 149.077 1.00 79.96  ? 3708 PHE A CE2   1 
ATOM   14909 C  CZ    . PHE A 1 2491 ? 189.003 121.255 148.001 1.00 80.08  ? 3708 PHE A CZ    1 
ATOM   14910 N  N     . ASP A 1 2492 ? 187.113 114.992 151.496 1.00 91.23  ? 3709 ASP A N     1 
ATOM   14911 C  CA    . ASP A 1 2492 ? 186.841 114.040 152.557 1.00 88.58  ? 3709 ASP A CA    1 
ATOM   14912 C  C     . ASP A 1 2492 ? 187.053 112.593 152.144 1.00 84.73  ? 3709 ASP A C     1 
ATOM   14913 O  O     . ASP A 1 2492 ? 186.940 111.707 152.998 1.00 84.17  ? 3709 ASP A O     1 
ATOM   14914 C  CB    . ASP A 1 2492 ? 185.411 114.222 153.086 1.00 86.84  ? 3709 ASP A CB    1 
ATOM   14915 C  CG    . ASP A 1 2492 ? 185.337 115.238 154.209 1.00 89.67  ? 3709 ASP A CG    1 
ATOM   14916 O  OD1   . ASP A 1 2492 ? 186.369 115.458 154.877 1.00 91.98  ? 3709 ASP A OD1   1 
ATOM   14917 O  OD2   . ASP A 1 2492 ? 184.255 115.820 154.427 1.00 89.31  ? 3709 ASP A OD2   1 
ATOM   14918 N  N     . ILE A 1 2493 ? 187.352 112.317 150.870 1.00 83.86  ? 3710 ILE A N     1 
ATOM   14919 C  CA    . ILE A 1 2493 ? 187.860 110.991 150.521 1.00 84.46  ? 3710 ILE A CA    1 
ATOM   14920 C  C     . ILE A 1 2493 ? 189.366 110.983 150.304 1.00 86.98  ? 3710 ILE A C     1 
ATOM   14921 O  O     . ILE A 1 2493 ? 189.962 109.896 150.234 1.00 92.35  ? 3710 ILE A O     1 
ATOM   14922 C  CB    . ILE A 1 2493 ? 187.195 110.407 149.257 1.00 83.47  ? 3710 ILE A CB    1 
ATOM   14923 C  CG1   . ILE A 1 2493 ? 187.529 111.261 148.038 1.00 80.74  ? 3710 ILE A CG1   1 
ATOM   14924 C  CG2   . ILE A 1 2493 ? 185.692 110.300 149.449 1.00 85.23  ? 3710 ILE A CG2   1 
ATOM   14925 C  CD1   . ILE A 1 2493 ? 187.139 110.614 146.744 1.00 77.98  ? 3710 ILE A CD1   1 
ATOM   14926 N  N     . GLU A 1 2494 ? 190.001 112.148 150.188 1.00 85.59  ? 3711 GLU A N     1 
ATOM   14927 C  CA    . GLU A 1 2494 ? 191.409 112.192 149.818 1.00 89.68  ? 3711 GLU A CA    1 
ATOM   14928 C  C     . GLU A 1 2494 ? 192.230 113.006 150.811 1.00 91.89  ? 3711 GLU A C     1 
ATOM   14929 O  O     . GLU A 1 2494 ? 191.736 113.382 151.879 1.00 89.74  ? 3711 GLU A O     1 
ATOM   14930 C  CB    . GLU A 1 2494 ? 191.563 112.749 148.400 1.00 90.51  ? 3711 GLU A CB    1 
ATOM   14931 C  CG    . GLU A 1 2494 ? 191.175 111.753 147.316 1.00 89.25  ? 3711 GLU A CG    1 
ATOM   14932 C  CD    . GLU A 1 2494 ? 191.394 112.289 145.916 1.00 88.32  ? 3711 GLU A CD    1 
ATOM   14933 O  OE1   . GLU A 1 2494 ? 191.677 113.496 145.776 1.00 85.74  ? 3711 GLU A OE1   1 
ATOM   14934 O  OE2   . GLU A 1 2494 ? 191.284 111.500 144.953 1.00 86.38  ? 3711 GLU A OE2   1 
ATOM   14935 N  N     . SER A 1 2495 ? 193.483 113.284 150.461 1.00 93.41  ? 3712 SER A N     1 
ATOM   14936 C  CA    . SER A 1 2495 ? 194.456 113.825 151.401 1.00 94.89  ? 3712 SER A CA    1 
ATOM   14937 C  C     . SER A 1 2495 ? 194.270 115.333 151.572 1.00 93.46  ? 3712 SER A C     1 
ATOM   14938 O  O     . SER A 1 2495 ? 193.302 115.931 151.095 1.00 91.51  ? 3712 SER A O     1 
ATOM   14939 C  CB    . SER A 1 2495 ? 195.869 113.485 150.939 1.00 93.96  ? 3712 SER A CB    1 
ATOM   14940 O  OG    . SER A 1 2495 ? 196.219 114.237 149.790 1.00 92.87  ? 3712 SER A OG    1 
ATOM   14941 N  N     . GLU A 1 2496 ? 195.219 115.959 152.271 1.00 93.66  ? 3713 GLU A N     1 
ATOM   14942 C  CA    . GLU A 1 2496 ? 195.194 117.393 152.535 1.00 92.36  ? 3713 GLU A CA    1 
ATOM   14943 C  C     . GLU A 1 2496 ? 195.988 118.190 151.510 1.00 93.02  ? 3713 GLU A C     1 
ATOM   14944 O  O     . GLU A 1 2496 ? 195.621 119.332 151.203 1.00 96.26  ? 3713 GLU A O     1 
ATOM   14945 C  CB    . GLU A 1 2496 ? 195.741 117.670 153.940 1.00 90.29  ? 3713 GLU A CB    1 
ATOM   14946 C  CG    . GLU A 1 2496 ? 195.562 119.098 154.427 1.00 88.31  ? 3713 GLU A CG    1 
ATOM   14947 C  CD    . GLU A 1 2496 ? 194.132 119.579 154.310 1.00 86.11  ? 3713 GLU A CD    1 
ATOM   14948 O  OE1   . GLU A 1 2496 ? 193.229 118.896 154.836 1.00 85.60  ? 3713 GLU A OE1   1 
ATOM   14949 O  OE2   . GLU A 1 2496 ? 193.911 120.644 153.696 1.00 86.47  ? 3713 GLU A OE2   1 
ATOM   14950 N  N     . GLN A 1 2497 ? 197.067 117.613 150.974 1.00 89.99  ? 3714 GLN A N     1 
ATOM   14951 C  CA    . GLN A 1 2497 ? 197.812 118.282 149.914 1.00 92.29  ? 3714 GLN A CA    1 
ATOM   14952 C  C     . GLN A 1 2497 ? 196.971 118.432 148.653 1.00 94.75  ? 3714 GLN A C     1 
ATOM   14953 O  O     . GLN A 1 2497 ? 197.084 119.441 147.950 1.00 94.49  ? 3714 GLN A O     1 
ATOM   14954 C  CB    . GLN A 1 2497 ? 199.110 117.525 149.620 1.00 94.37  ? 3714 GLN A CB    1 
ATOM   14955 C  CG    . GLN A 1 2497 ? 198.943 116.031 149.383 1.00 94.88  ? 3714 GLN A CG    1 
ATOM   14956 C  CD    . GLN A 1 2497 ? 198.709 115.689 147.925 1.00 99.13  ? 3714 GLN A CD    1 
ATOM   14957 O  OE1   . GLN A 1 2497 ? 199.143 116.412 147.029 1.00 103.19 ? 3714 GLN A OE1   1 
ATOM   14958 N  NE2   . GLN A 1 2497 ? 198.018 114.581 147.681 1.00 96.89  ? 3714 GLN A NE2   1 
ATOM   14959 N  N     . TYR A 1 2498 ? 196.114 117.449 148.363 1.00 94.96  ? 3715 TYR A N     1 
ATOM   14960 C  CA    . TYR A 1 2498 ? 195.172 117.584 147.257 1.00 89.80  ? 3715 TYR A CA    1 
ATOM   14961 C  C     . TYR A 1 2498 ? 194.198 118.728 147.504 1.00 86.67  ? 3715 TYR A C     1 
ATOM   14962 O  O     . TYR A 1 2498 ? 193.867 119.480 146.581 1.00 90.21  ? 3715 TYR A O     1 
ATOM   14963 C  CB    . TYR A 1 2498 ? 194.417 116.271 147.050 1.00 90.58  ? 3715 TYR A CB    1 
ATOM   14964 C  CG    . TYR A 1 2498 ? 193.583 116.226 145.789 1.00 90.76  ? 3715 TYR A CG    1 
ATOM   14965 C  CD1   . TYR A 1 2498 ? 194.134 115.814 144.584 1.00 92.60  ? 3715 TYR A CD1   1 
ATOM   14966 C  CD2   . TYR A 1 2498 ? 192.241 116.588 145.807 1.00 90.34  ? 3715 TYR A CD2   1 
ATOM   14967 C  CE1   . TYR A 1 2498 ? 193.375 115.768 143.430 1.00 92.38  ? 3715 TYR A CE1   1 
ATOM   14968 C  CE2   . TYR A 1 2498 ? 191.474 116.544 144.659 1.00 90.04  ? 3715 TYR A CE2   1 
ATOM   14969 C  CZ    . TYR A 1 2498 ? 192.046 116.135 143.474 1.00 91.25  ? 3715 TYR A CZ    1 
ATOM   14970 O  OH    . TYR A 1 2498 ? 191.287 116.091 142.329 1.00 90.68  ? 3715 TYR A OH    1 
ATOM   14971 N  N     . LYS A 1 2499 ? 193.725 118.871 148.746 1.00 85.54  ? 3716 LYS A N     1 
ATOM   14972 C  CA    . LYS A 1 2499 ? 192.824 119.970 149.081 1.00 84.65  ? 3716 LYS A CA    1 
ATOM   14973 C  C     . LYS A 1 2499 ? 193.506 121.320 148.902 1.00 86.21  ? 3716 LYS A C     1 
ATOM   14974 O  O     . LYS A 1 2499 ? 192.917 122.254 148.343 1.00 87.02  ? 3716 LYS A O     1 
ATOM   14975 C  CB    . LYS A 1 2499 ? 192.315 119.806 150.513 1.00 81.33  ? 3716 LYS A CB    1 
ATOM   14976 C  CG    . LYS A 1 2499 ? 191.496 120.978 151.031 1.00 81.26  ? 3716 LYS A CG    1 
ATOM   14977 C  CD    . LYS A 1 2499 ? 190.864 120.653 152.376 1.00 81.01  ? 3716 LYS A CD    1 
ATOM   14978 C  CE    . LYS A 1 2499 ? 189.950 121.771 152.850 1.00 76.05  ? 3716 LYS A CE    1 
ATOM   14979 N  NZ    . LYS A 1 2499 ? 190.716 122.967 153.292 1.00 71.19  ? 3716 LYS A NZ    1 
ATOM   14980 N  N     . GLU A 1 2500 ? 194.757 121.437 149.356 1.00 87.89  ? 3717 GLU A N     1 
ATOM   14981 C  CA    . GLU A 1 2500 ? 195.489 122.688 149.184 1.00 89.75  ? 3717 GLU A CA    1 
ATOM   14982 C  C     . GLU A 1 2500 ? 195.754 122.982 147.711 1.00 89.81  ? 3717 GLU A C     1 
ATOM   14983 O  O     . GLU A 1 2500 ? 195.672 124.139 147.282 1.00 92.79  ? 3717 GLU A O     1 
ATOM   14984 C  CB    . GLU A 1 2500 ? 196.798 122.648 149.969 1.00 94.11  ? 3717 GLU A CB    1 
ATOM   14985 C  CG    . GLU A 1 2500 ? 197.452 124.009 150.134 1.00 95.61  ? 3717 GLU A CG    1 
ATOM   14986 C  CD    . GLU A 1 2500 ? 196.482 125.071 150.611 1.00 97.08  ? 3717 GLU A CD    1 
ATOM   14987 O  OE1   . GLU A 1 2500 ? 195.872 124.885 151.685 1.00 98.32  ? 3717 GLU A OE1   1 
ATOM   14988 O  OE2   . GLU A 1 2500 ? 196.328 126.094 149.911 1.00 95.07  ? 3717 GLU A OE2   1 
ATOM   14989 N  N     . ALA A 1 2501 ? 196.073 121.950 146.924 1.00 89.39  ? 3718 ALA A N     1 
ATOM   14990 C  CA    . ALA A 1 2501 ? 196.291 122.143 145.494 1.00 93.15  ? 3718 ALA A CA    1 
ATOM   14991 C  C     . ALA A 1 2501 ? 195.016 122.599 144.794 1.00 91.78  ? 3718 ALA A C     1 
ATOM   14992 O  O     . ALA A 1 2501 ? 195.052 123.491 143.936 1.00 93.66  ? 3718 ALA A O     1 
ATOM   14993 C  CB    . ALA A 1 2501 ? 196.817 120.854 144.867 1.00 96.83  ? 3718 ALA A CB    1 
ATOM   14994 N  N     . VAL A 1 2502 ? 193.877 122.002 145.153 1.00 88.10  ? 3719 VAL A N     1 
ATOM   14995 C  CA    . VAL A 1 2502 ? 192.605 122.402 144.559 1.00 81.59  ? 3719 VAL A CA    1 
ATOM   14996 C  C     . VAL A 1 2502 ? 192.274 123.841 144.932 1.00 82.26  ? 3719 VAL A C     1 
ATOM   14997 O  O     . VAL A 1 2502 ? 191.854 124.632 144.080 1.00 86.34  ? 3719 VAL A O     1 
ATOM   14998 C  CB    . VAL A 1 2502 ? 191.489 121.425 144.974 1.00 79.85  ? 3719 VAL A CB    1 
ATOM   14999 C  CG1   . VAL A 1 2502 ? 190.118 122.028 144.727 1.00 78.29  ? 3719 VAL A CG1   1 
ATOM   15000 C  CG2   . VAL A 1 2502 ? 191.631 120.120 144.213 1.00 81.31  ? 3719 VAL A CG2   1 
ATOM   15001 N  N     . LEU A 1 2503 ? 192.484 124.213 146.201 1.00 80.44  ? 3720 LEU A N     1 
ATOM   15002 C  CA    . LEU A 1 2503 ? 192.233 125.593 146.614 1.00 80.91  ? 3720 LEU A CA    1 
ATOM   15003 C  C     . LEU A 1 2503 ? 193.133 126.584 145.885 1.00 84.48  ? 3720 LEU A C     1 
ATOM   15004 O  O     . LEU A 1 2503 ? 192.663 127.633 145.433 1.00 85.56  ? 3720 LEU A O     1 
ATOM   15005 C  CB    . LEU A 1 2503 ? 192.400 125.751 148.126 1.00 80.28  ? 3720 LEU A CB    1 
ATOM   15006 C  CG    . LEU A 1 2503 ? 191.160 125.625 149.013 1.00 75.71  ? 3720 LEU A CG    1 
ATOM   15007 C  CD1   . LEU A 1 2503 ? 190.203 126.766 148.710 1.00 75.81  ? 3720 LEU A CD1   1 
ATOM   15008 C  CD2   . LEU A 1 2503 ? 190.467 124.306 148.832 1.00 76.77  ? 3720 LEU A CD2   1 
ATOM   15009 N  N     . THR A 1 2504 ? 194.425 126.275 145.746 1.00 87.01  ? 3721 THR A N     1 
ATOM   15010 C  CA    . THR A 1 2504 ? 195.309 127.253 145.117 1.00 89.50  ? 3721 THR A CA    1 
ATOM   15011 C  C     . THR A 1 2504 ? 195.078 127.336 143.611 1.00 90.77  ? 3721 THR A C     1 
ATOM   15012 O  O     . THR A 1 2504 ? 195.236 128.415 143.024 1.00 93.37  ? 3721 THR A O     1 
ATOM   15013 C  CB    . THR A 1 2504 ? 196.780 126.958 145.442 1.00 96.18  ? 3721 THR A CB    1 
ATOM   15014 O  OG1   . THR A 1 2504 ? 197.602 128.023 144.946 1.00 104.98 ? 3721 THR A OG1   1 
ATOM   15015 C  CG2   . THR A 1 2504 ? 197.246 125.654 144.829 1.00 95.73  ? 3721 THR A CG2   1 
ATOM   15016 N  N     . MET A 1 2505 ? 194.651 126.244 142.968 1.00 90.19  ? 3722 MET A N     1 
ATOM   15017 C  CA    . MET A 1 2505 ? 194.363 126.352 141.543 1.00 93.65  ? 3722 MET A CA    1 
ATOM   15018 C  C     . MET A 1 2505 ? 192.996 126.978 141.284 1.00 89.58  ? 3722 MET A C     1 
ATOM   15019 O  O     . MET A 1 2505 ? 192.802 127.621 140.246 1.00 91.63  ? 3722 MET A O     1 
ATOM   15020 C  CB    . MET A 1 2505 ? 194.482 124.987 140.867 1.00 97.53  ? 3722 MET A CB    1 
ATOM   15021 C  CG    . MET A 1 2505 ? 195.933 124.602 140.620 1.00 106.97 ? 3722 MET A CG    1 
ATOM   15022 S  SD    . MET A 1 2505 ? 196.612 125.314 139.107 1.00 119.08 ? 3722 MET A SD    1 
ATOM   15023 C  CE    . MET A 1 2505 ? 196.574 123.910 138.005 1.00 116.77 ? 3722 MET A CE    1 
ATOM   15024 N  N     . ILE A 1 2506 ? 192.052 126.832 142.215 1.00 84.07  ? 3723 ILE A N     1 
ATOM   15025 C  CA    . ILE A 1 2506 ? 190.823 127.613 142.143 1.00 77.78  ? 3723 ILE A CA    1 
ATOM   15026 C  C     . ILE A 1 2506 ? 191.132 129.094 142.336 1.00 81.68  ? 3723 ILE A C     1 
ATOM   15027 O  O     . ILE A 1 2506 ? 190.554 129.959 141.666 1.00 84.28  ? 3723 ILE A O     1 
ATOM   15028 C  CB    . ILE A 1 2506 ? 189.805 127.087 143.173 1.00 71.80  ? 3723 ILE A CB    1 
ATOM   15029 C  CG1   . ILE A 1 2506 ? 189.160 125.795 142.668 1.00 67.32  ? 3723 ILE A CG1   1 
ATOM   15030 C  CG2   . ILE A 1 2506 ? 188.728 128.115 143.466 1.00 69.77  ? 3723 ILE A CG2   1 
ATOM   15031 C  CD1   . ILE A 1 2506 ? 188.086 125.251 143.584 1.00 61.51  ? 3723 ILE A CD1   1 
ATOM   15032 N  N     . GLY A 1 2507 ? 192.071 129.406 143.233 1.00 83.79  ? 3724 GLY A N     1 
ATOM   15033 C  CA    . GLY A 1 2507 ? 192.469 130.790 143.432 1.00 86.12  ? 3724 GLY A CA    1 
ATOM   15034 C  C     . GLY A 1 2507 ? 193.131 131.403 142.213 1.00 88.88  ? 3724 GLY A C     1 
ATOM   15035 O  O     . GLY A 1 2507 ? 192.833 132.542 141.845 1.00 87.42  ? 3724 GLY A O     1 
ATOM   15036 N  N     . VAL A 1 2508 ? 194.042 130.664 141.572 1.00 90.54  ? 3725 VAL A N     1 
ATOM   15037 C  CA    . VAL A 1 2508 ? 194.637 131.169 140.339 1.00 92.82  ? 3725 VAL A CA    1 
ATOM   15038 C  C     . VAL A 1 2508 ? 193.611 131.193 139.211 1.00 88.95  ? 3725 VAL A C     1 
ATOM   15039 O  O     . VAL A 1 2508 ? 193.765 131.958 138.252 1.00 88.72  ? 3725 VAL A O     1 
ATOM   15040 C  CB    . VAL A 1 2508 ? 195.893 130.360 139.947 1.00 99.05  ? 3725 VAL A CB    1 
ATOM   15041 C  CG1   . VAL A 1 2508 ? 195.529 129.022 139.337 1.00 91.95  ? 3725 VAL A CG1   1 
ATOM   15042 C  CG2   . VAL A 1 2508 ? 196.775 131.159 138.997 1.00 103.85 ? 3725 VAL A CG2   1 
ATOM   15043 N  N     . LEU A 1 2509 ? 192.551 130.385 139.308 1.00 89.66  ? 3726 LEU A N     1 
ATOM   15044 C  CA    . LEU A 1 2509 ? 191.444 130.513 138.368 1.00 86.61  ? 3726 LEU A CA    1 
ATOM   15045 C  C     . LEU A 1 2509 ? 190.602 131.750 138.659 1.00 82.53  ? 3726 LEU A C     1 
ATOM   15046 O  O     . LEU A 1 2509 ? 189.975 132.298 137.746 1.00 76.25  ? 3726 LEU A O     1 
ATOM   15047 C  CB    . LEU A 1 2509 ? 190.573 129.257 138.413 1.00 80.59  ? 3726 LEU A CB    1 
ATOM   15048 C  CG    . LEU A 1 2509 ? 189.723 128.938 137.183 1.00 74.53  ? 3726 LEU A CG    1 
ATOM   15049 C  CD1   . LEU A 1 2509 ? 190.560 128.259 136.114 1.00 74.35  ? 3726 LEU A CD1   1 
ATOM   15050 C  CD2   . LEU A 1 2509 ? 188.541 128.067 137.575 1.00 73.93  ? 3726 LEU A CD2   1 
ATOM   15051 N  N     . SER A 1 2510 ? 190.581 132.204 139.911 1.00 83.63  ? 3727 SER A N     1 
ATOM   15052 C  CA    . SER A 1 2510 ? 189.740 133.315 140.337 1.00 80.83  ? 3727 SER A CA    1 
ATOM   15053 C  C     . SER A 1 2510 ? 190.476 134.649 140.360 1.00 85.13  ? 3727 SER A C     1 
ATOM   15054 O  O     . SER A 1 2510 ? 189.897 135.649 140.798 1.00 83.08  ? 3727 SER A O     1 
ATOM   15055 C  CB    . SER A 1 2510 ? 189.153 133.031 141.720 1.00 78.30  ? 3727 SER A CB    1 
ATOM   15056 O  OG    . SER A 1 2510 ? 188.512 134.179 142.247 1.00 74.43  ? 3727 SER A OG    1 
ATOM   15057 N  N     . GLU A 1 2511 ? 191.733 134.680 139.904 1.00 91.75  ? 3728 GLU A N     1 
ATOM   15058 C  CA    . GLU A 1 2511 ? 192.560 135.892 139.877 1.00 94.60  ? 3728 GLU A CA    1 
ATOM   15059 C  C     . GLU A 1 2511 ? 192.682 136.524 141.264 1.00 94.37  ? 3728 GLU A C     1 
ATOM   15060 O  O     . GLU A 1 2511 ? 192.650 137.747 141.415 1.00 91.79  ? 3728 GLU A O     1 
ATOM   15061 C  CB    . GLU A 1 2511 ? 192.030 136.908 138.861 1.00 85.86  ? 3728 GLU A CB    1 
ATOM   15062 N  N     . SER A 1 2512 ? 192.820 135.682 142.287 1.00 95.35  ? 3729 SER A N     1 
ATOM   15063 C  CA    . SER A 1 2512 ? 192.940 136.141 143.665 1.00 95.70  ? 3729 SER A CA    1 
ATOM   15064 C  C     . SER A 1 2512 ? 194.269 135.759 144.296 1.00 95.78  ? 3729 SER A C     1 
ATOM   15065 O  O     . SER A 1 2512 ? 194.930 136.612 144.900 1.00 97.35  ? 3729 SER A O     1 
ATOM   15066 C  CB    . SER A 1 2512 ? 191.780 135.585 144.508 1.00 94.38  ? 3729 SER A CB    1 
ATOM   15067 O  OG    . SER A 1 2512 ? 190.527 135.963 143.964 1.00 92.81  ? 3729 SER A OG    1 
ATOM   15068 N  N     . SER A 1 2513 ? 194.682 134.499 144.175 1.00 96.80  ? 3730 SER A N     1 
ATOM   15069 C  CA    . SER A 1 2513 ? 195.942 134.025 144.729 1.00 100.39 ? 3730 SER A CA    1 
ATOM   15070 C  C     . SER A 1 2513 ? 196.699 133.257 143.658 1.00 103.02 ? 3730 SER A C     1 
ATOM   15071 O  O     . SER A 1 2513 ? 196.151 132.334 143.049 1.00 101.78 ? 3730 SER A O     1 
ATOM   15072 C  CB    . SER A 1 2513 ? 195.709 133.138 145.956 1.00 98.00  ? 3730 SER A CB    1 
ATOM   15073 O  OG    . SER A 1 2513 ? 195.311 131.834 145.572 1.00 97.20  ? 3730 SER A OG    1 
ATOM   15074 N  N     . ASP A 1 2514 ? 197.957 133.631 143.438 1.00 108.33 ? 3731 ASP A N     1 
ATOM   15075 C  CA    . ASP A 1 2514 ? 198.789 133.034 142.404 1.00 112.05 ? 3731 ASP A CA    1 
ATOM   15076 C  C     . ASP A 1 2514 ? 199.982 132.325 143.029 1.00 119.00 ? 3731 ASP A C     1 
ATOM   15077 O  O     . ASP A 1 2514 ? 200.622 132.852 143.945 1.00 119.54 ? 3731 ASP A O     1 
ATOM   15078 C  CB    . ASP A 1 2514 ? 199.272 134.092 141.407 1.00 112.64 ? 3731 ASP A CB    1 
ATOM   15079 C  CG    . ASP A 1 2514 ? 199.434 133.540 140.004 1.00 112.56 ? 3731 ASP A CG    1 
ATOM   15080 O  OD1   . ASP A 1 2514 ? 199.681 132.324 139.869 1.00 110.47 ? 3731 ASP A OD1   1 
ATOM   15081 O  OD2   . ASP A 1 2514 ? 199.312 134.322 139.038 1.00 114.78 ? 3731 ASP A OD2   1 
ATOM   15082 N  N     . GLY A 1 2515 ? 200.277 131.130 142.523 1.00 120.54 ? 3732 GLY A N     1 
ATOM   15083 C  CA    . GLY A 1 2515 ? 201.405 130.351 142.995 1.00 123.53 ? 3732 GLY A CA    1 
ATOM   15084 C  C     . GLY A 1 2515 ? 201.469 128.982 142.351 1.00 127.15 ? 3732 GLY A C     1 
ATOM   15085 O  O     . GLY A 1 2515 ? 200.463 128.489 141.830 1.00 125.96 ? 3732 GLY A O     1 
ATOM   15086 N  N     . VAL A 1 2516 ? 202.641 128.355 142.377 1.00 132.07 ? 3733 VAL A N     1 
ATOM   15087 C  CA    . VAL A 1 2516 ? 202.814 127.027 141.795 1.00 134.71 ? 3733 VAL A CA    1 
ATOM   15088 C  C     . VAL A 1 2516 ? 202.256 125.991 142.764 1.00 135.19 ? 3733 VAL A C     1 
ATOM   15089 O  O     . VAL A 1 2516 ? 202.716 125.905 143.912 1.00 134.82 ? 3733 VAL A O     1 
ATOM   15090 C  CB    . VAL A 1 2516 ? 204.288 126.745 141.466 1.00 136.18 ? 3733 VAL A CB    1 
ATOM   15091 C  CG1   . VAL A 1 2516 ? 204.426 125.400 140.769 1.00 132.81 ? 3733 VAL A CG1   1 
ATOM   15092 C  CG2   . VAL A 1 2516 ? 204.858 127.858 140.601 1.00 135.85 ? 3733 VAL A CG2   1 
ATOM   15093 N  N     . PRO A 1 2517 ? 201.274 125.195 142.354 1.00 133.97 ? 3734 PRO A N     1 
ATOM   15094 C  CA    . PRO A 1 2517 ? 200.684 124.209 143.263 1.00 130.75 ? 3734 PRO A CA    1 
ATOM   15095 C  C     . PRO A 1 2517 ? 201.592 123.007 143.480 1.00 130.57 ? 3734 PRO A C     1 
ATOM   15096 O  O     . PRO A 1 2517 ? 202.497 122.718 142.695 1.00 129.70 ? 3734 PRO A O     1 
ATOM   15097 C  CB    . PRO A 1 2517 ? 199.398 123.793 142.540 1.00 124.68 ? 3734 PRO A CB    1 
ATOM   15098 C  CG    . PRO A 1 2517 ? 199.698 124.025 141.097 1.00 128.07 ? 3734 PRO A CG    1 
ATOM   15099 C  CD    . PRO A 1 2517 ? 200.590 125.231 141.050 1.00 130.64 ? 3734 PRO A CD    1 
ATOM   15100 N  N     . LYS A 1 2518 ? 201.330 122.304 144.579 1.00 127.83 ? 3735 LYS A N     1 
ATOM   15101 C  CA    . LYS A 1 2518 ? 201.951 121.004 144.834 1.00 124.89 ? 3735 LYS A CA    1 
ATOM   15102 C  C     . LYS A 1 2518 ? 201.051 119.866 144.358 1.00 122.87 ? 3735 LYS A C     1 
ATOM   15103 O  O     . LYS A 1 2518 ? 200.635 118.999 145.126 1.00 118.58 ? 3735 LYS A O     1 
ATOM   15104 C  CB    . LYS A 1 2518 ? 202.295 120.859 146.312 1.00 118.60 ? 3735 LYS A CB    1 
ATOM   15105 C  CG    . LYS A 1 2518 ? 201.198 121.267 147.286 1.00 113.52 ? 3735 LYS A CG    1 
ATOM   15106 C  CD    . LYS A 1 2518 ? 201.561 120.839 148.700 1.00 108.95 ? 3735 LYS A CD    1 
ATOM   15107 C  CE    . LYS A 1 2518 ? 200.494 121.236 149.702 1.00 103.31 ? 3735 LYS A CE    1 
ATOM   15108 N  NZ    . LYS A 1 2518 ? 200.497 122.704 149.935 1.00 103.52 ? 3735 LYS A NZ    1 
ATOM   15109 N  N     . LEU A 1 2519 ? 200.747 119.878 143.062 1.00 123.32 ? 3736 LEU A N     1 
ATOM   15110 C  CA    . LEU A 1 2519 ? 199.853 118.889 142.477 1.00 122.38 ? 3736 LEU A CA    1 
ATOM   15111 C  C     . LEU A 1 2519 ? 200.461 117.493 142.539 1.00 121.85 ? 3736 LEU A C     1 
ATOM   15112 O  O     . LEU A 1 2519 ? 201.641 117.295 142.238 1.00 121.42 ? 3736 LEU A O     1 
ATOM   15113 C  CB    . LEU A 1 2519 ? 199.540 119.258 141.028 1.00 122.25 ? 3736 LEU A CB    1 
ATOM   15114 C  CG    . LEU A 1 2519 ? 198.665 120.486 140.775 1.00 124.39 ? 3736 LEU A CG    1 
ATOM   15115 C  CD1   . LEU A 1 2519 ? 198.662 120.837 139.297 1.00 127.21 ? 3736 LEU A CD1   1 
ATOM   15116 C  CD2   . LEU A 1 2519 ? 197.248 120.238 141.261 1.00 120.85 ? 3736 LEU A CD2   1 
ATOM   15117 N  N     . THR A 1 2520 ? 199.641 116.522 142.931 1.00 119.40 ? 3737 THR A N     1 
ATOM   15118 C  CA    . THR A 1 2520 ? 200.081 115.137 143.035 1.00 116.35 ? 3737 THR A CA    1 
ATOM   15119 C  C     . THR A 1 2520 ? 198.979 114.184 142.584 1.00 110.05 ? 3737 THR A C     1 
ATOM   15120 O  O     . THR A 1 2520 ? 197.794 114.500 142.686 1.00 102.52 ? 3737 THR A O     1 
ATOM   15121 C  CB    . THR A 1 2520 ? 200.500 114.782 144.473 1.00 115.35 ? 3737 THR A CB    1 
ATOM   15122 O  OG1   . THR A 1 2520 ? 201.642 115.563 144.847 1.00 117.54 ? 3737 THR A OG1   1 
ATOM   15123 C  CG2   . THR A 1 2520 ? 200.845 113.304 144.580 1.00 115.78 ? 3737 THR A CG2   1 
ATOM   15124 N  N     . ASN A 1 2524 ? 200.269 112.273 136.518 1.00 127.90 ? 3741 ASN A N     1 
ATOM   15125 C  CA    . ASN A 1 2524 ? 199.347 111.650 135.575 1.00 128.66 ? 3741 ASN A CA    1 
ATOM   15126 C  C     . ASN A 1 2524 ? 199.000 112.596 134.429 1.00 128.85 ? 3741 ASN A C     1 
ATOM   15127 O  O     . ASN A 1 2524 ? 199.359 113.774 134.454 1.00 127.68 ? 3741 ASN A O     1 
ATOM   15128 C  CB    . ASN A 1 2524 ? 198.072 111.197 136.293 1.00 127.71 ? 3741 ASN A CB    1 
ATOM   15129 C  CG    . ASN A 1 2524 ? 197.471 112.284 137.164 1.00 123.94 ? 3741 ASN A CG    1 
ATOM   15130 O  OD1   . ASN A 1 2524 ? 198.002 113.391 137.253 1.00 123.93 ? 3741 ASN A OD1   1 
ATOM   15131 N  ND2   . ASN A 1 2524 ? 196.355 111.973 137.812 1.00 118.07 ? 3741 ASN A ND2   1 
ATOM   15132 N  N     . ASP A 1 2525 ? 198.291 112.072 133.426 1.00 129.84 ? 3742 ASP A N     1 
ATOM   15133 C  CA    . ASP A 1 2525 ? 197.890 112.872 132.274 1.00 128.75 ? 3742 ASP A CA    1 
ATOM   15134 C  C     . ASP A 1 2525 ? 196.837 113.916 132.619 1.00 128.72 ? 3742 ASP A C     1 
ATOM   15135 O  O     . ASP A 1 2525 ? 196.598 114.819 131.809 1.00 128.94 ? 3742 ASP A O     1 
ATOM   15136 C  CB    . ASP A 1 2525 ? 197.371 111.962 131.159 1.00 127.52 ? 3742 ASP A CB    1 
ATOM   15137 N  N     . ASP A 1 2526 ? 196.194 113.802 133.784 1.00 129.02 ? 3743 ASP A N     1 
ATOM   15138 C  CA    . ASP A 1 2526 ? 195.265 114.832 134.234 1.00 127.15 ? 3743 ASP A CA    1 
ATOM   15139 C  C     . ASP A 1 2526 ? 195.981 116.158 134.463 1.00 123.66 ? 3743 ASP A C     1 
ATOM   15140 O  O     . ASP A 1 2526 ? 195.489 117.223 134.062 1.00 118.91 ? 3743 ASP A O     1 
ATOM   15141 C  CB    . ASP A 1 2526 ? 194.572 114.368 135.515 1.00 124.65 ? 3743 ASP A CB    1 
ATOM   15142 N  N     . LEU A 1 2527 ? 197.153 116.105 135.101 1.00 125.98 ? 3744 LEU A N     1 
ATOM   15143 C  CA    . LEU A 1 2527 ? 197.939 117.304 135.362 1.00 125.18 ? 3744 LEU A CA    1 
ATOM   15144 C  C     . LEU A 1 2527 ? 198.402 117.965 134.073 1.00 125.08 ? 3744 LEU A C     1 
ATOM   15145 O  O     . LEU A 1 2527 ? 198.439 119.198 133.992 1.00 124.31 ? 3744 LEU A O     1 
ATOM   15146 C  CB    . LEU A 1 2527 ? 199.144 116.949 136.231 1.00 125.64 ? 3744 LEU A CB    1 
ATOM   15147 C  CG    . LEU A 1 2527 ? 198.869 116.546 137.680 1.00 121.70 ? 3744 LEU A CG    1 
ATOM   15148 C  CD1   . LEU A 1 2527 ? 200.125 116.721 138.511 1.00 118.27 ? 3744 LEU A CD1   1 
ATOM   15149 C  CD2   . LEU A 1 2527 ? 197.715 117.348 138.267 1.00 119.85 ? 3744 LEU A CD2   1 
ATOM   15150 N  N     . ARG A 1 2528 ? 198.773 117.164 133.071 1.00 125.30 ? 3745 ARG A N     1 
ATOM   15151 C  CA    . ARG A 1 2528 ? 199.200 117.714 131.789 1.00 125.01 ? 3745 ARG A CA    1 
ATOM   15152 C  C     . ARG A 1 2528 ? 198.074 118.499 131.128 1.00 125.66 ? 3745 ARG A C     1 
ATOM   15153 O  O     . ARG A 1 2528 ? 198.287 119.611 130.633 1.00 124.84 ? 3745 ARG A O     1 
ATOM   15154 C  CB    . ARG A 1 2528 ? 199.684 116.589 130.874 1.00 121.99 ? 3745 ARG A CB    1 
ATOM   15155 N  N     . TYR A 1 2529 ? 196.861 117.940 131.129 1.00 125.58 ? 3746 TYR A N     1 
ATOM   15156 C  CA    . TYR A 1 2529 ? 195.718 118.639 130.550 1.00 121.85 ? 3746 TYR A CA    1 
ATOM   15157 C  C     . TYR A 1 2529 ? 195.382 119.903 131.333 1.00 118.35 ? 3746 TYR A C     1 
ATOM   15158 O  O     . TYR A 1 2529 ? 195.088 120.947 130.738 1.00 116.40 ? 3746 TYR A O     1 
ATOM   15159 C  CB    . TYR A 1 2529 ? 194.508 117.707 130.490 1.00 118.59 ? 3746 TYR A CB    1 
ATOM   15160 N  N     . LEU A 1 2530 ? 195.434 119.833 132.667 1.00 119.18 ? 3747 LEU A N     1 
ATOM   15161 C  CA    . LEU A 1 2530 ? 195.112 121.004 133.480 1.00 118.25 ? 3747 LEU A CA    1 
ATOM   15162 C  C     . LEU A 1 2530 ? 196.118 122.130 133.262 1.00 119.24 ? 3747 LEU A C     1 
ATOM   15163 O  O     . LEU A 1 2530 ? 195.733 123.301 133.133 1.00 118.76 ? 3747 LEU A O     1 
ATOM   15164 C  CB    . LEU A 1 2530 ? 195.053 120.614 134.956 1.00 118.42 ? 3747 LEU A CB    1 
ATOM   15165 C  CG    . LEU A 1 2530 ? 194.527 121.671 135.927 1.00 112.21 ? 3747 LEU A CG    1 
ATOM   15166 C  CD1   . LEU A 1 2530 ? 193.233 122.279 135.417 1.00 107.92 ? 3747 LEU A CD1   1 
ATOM   15167 C  CD2   . LEU A 1 2530 ? 194.326 121.068 137.307 1.00 115.59 ? 3747 LEU A CD2   1 
ATOM   15168 N  N     . TRP A 1 2531 ? 197.412 121.796 133.224 1.00 120.81 ? 3748 TRP A N     1 
ATOM   15169 C  CA    . TRP A 1 2531 ? 198.438 122.801 132.962 1.00 120.83 ? 3748 TRP A CA    1 
ATOM   15170 C  C     . TRP A 1 2531 ? 198.330 123.354 131.547 1.00 118.78 ? 3748 TRP A C     1 
ATOM   15171 O  O     . TRP A 1 2531 ? 198.456 124.565 131.342 1.00 116.11 ? 3748 TRP A O     1 
ATOM   15172 C  CB    . TRP A 1 2531 ? 199.825 122.208 133.216 1.00 123.36 ? 3748 TRP A CB    1 
ATOM   15173 C  CG    . TRP A 1 2531 ? 200.322 122.389 134.629 1.00 126.97 ? 3748 TRP A CG    1 
ATOM   15174 C  CD1   . TRP A 1 2531 ? 200.764 121.409 135.469 1.00 129.25 ? 3748 TRP A CD1   1 
ATOM   15175 C  CD2   . TRP A 1 2531 ? 200.486 123.627 135.340 1.00 128.04 ? 3748 TRP A CD2   1 
ATOM   15176 N  NE1   . TRP A 1 2531 ? 201.155 121.953 136.669 1.00 129.15 ? 3748 TRP A NE1   1 
ATOM   15177 C  CE2   . TRP A 1 2531 ? 200.999 123.312 136.613 1.00 128.02 ? 3748 TRP A CE2   1 
ATOM   15178 C  CE3   . TRP A 1 2531 ? 200.238 124.968 135.027 1.00 126.07 ? 3748 TRP A CE3   1 
ATOM   15179 C  CZ2   . TRP A 1 2531 ? 201.267 124.286 137.573 1.00 125.80 ? 3748 TRP A CZ2   1 
ATOM   15180 C  CZ3   . TRP A 1 2531 ? 200.501 125.933 135.981 1.00 126.05 ? 3748 TRP A CZ3   1 
ATOM   15181 C  CH2   . TRP A 1 2531 ? 201.012 125.588 137.238 1.00 126.15 ? 3748 TRP A CH2   1 
ATOM   15182 N  N     . ASP A 1 2532 ? 198.078 122.489 130.558 1.00 119.58 ? 3749 ASP A N     1 
ATOM   15183 C  CA    . ASP A 1 2532 ? 197.894 122.956 129.189 1.00 118.87 ? 3749 ASP A CA    1 
ATOM   15184 C  C     . ASP A 1 2532 ? 196.643 123.809 129.033 1.00 117.24 ? 3749 ASP A C     1 
ATOM   15185 O  O     . ASP A 1 2532 ? 196.545 124.572 128.068 1.00 114.45 ? 3749 ASP A O     1 
ATOM   15186 C  CB    . ASP A 1 2532 ? 197.834 121.765 128.231 1.00 116.15 ? 3749 ASP A CB    1 
ATOM   15187 N  N     . TYR A 1 2533 ? 195.684 123.687 129.951 1.00 116.61 ? 3750 TYR A N     1 
ATOM   15188 C  CA    . TYR A 1 2533 ? 194.523 124.568 129.924 1.00 109.97 ? 3750 TYR A CA    1 
ATOM   15189 C  C     . TYR A 1 2533 ? 194.824 125.916 130.570 1.00 107.65 ? 3750 TYR A C     1 
ATOM   15190 O  O     . TYR A 1 2533 ? 194.577 126.967 129.967 1.00 106.03 ? 3750 TYR A O     1 
ATOM   15191 C  CB    . TYR A 1 2533 ? 193.336 123.895 130.615 1.00 105.64 ? 3750 TYR A CB    1 
ATOM   15192 C  CG    . TYR A 1 2533 ? 192.664 122.834 129.775 1.00 104.64 ? 3750 TYR A CG    1 
ATOM   15193 C  CD1   . TYR A 1 2533 ? 192.942 122.714 128.419 1.00 106.27 ? 3750 TYR A CD1   1 
ATOM   15194 C  CD2   . TYR A 1 2533 ? 191.746 121.958 130.335 1.00 103.46 ? 3750 TYR A CD2   1 
ATOM   15195 C  CE1   . TYR A 1 2533 ? 192.327 121.748 127.647 1.00 107.71 ? 3750 TYR A CE1   1 
ATOM   15196 C  CE2   . TYR A 1 2533 ? 191.127 120.990 129.570 1.00 105.20 ? 3750 TYR A CE2   1 
ATOM   15197 C  CZ    . TYR A 1 2533 ? 191.421 120.889 128.228 1.00 107.69 ? 3750 TYR A CZ    1 
ATOM   15198 O  OH    . TYR A 1 2533 ? 190.805 119.924 127.465 1.00 109.51 ? 3750 TYR A OH    1 
ATOM   15199 N  N     . VAL A 1 2534 ? 195.356 125.909 131.796 1.00 108.81 ? 3751 VAL A N     1 
ATOM   15200 C  CA    . VAL A 1 2534 ? 195.538 127.175 132.509 1.00 108.25 ? 3751 VAL A CA    1 
ATOM   15201 C  C     . VAL A 1 2534 ? 196.667 128.006 131.904 1.00 109.71 ? 3751 VAL A C     1 
ATOM   15202 O  O     . VAL A 1 2534 ? 196.616 129.242 131.938 1.00 108.49 ? 3751 VAL A O     1 
ATOM   15203 C  CB    . VAL A 1 2534 ? 195.753 126.943 134.018 1.00 107.71 ? 3751 VAL A CB    1 
ATOM   15204 C  CG1   . VAL A 1 2534 ? 194.488 126.378 134.654 1.00 103.17 ? 3751 VAL A CG1   1 
ATOM   15205 C  CG2   . VAL A 1 2534 ? 196.944 126.041 134.271 1.00 112.86 ? 3751 VAL A CG2   1 
ATOM   15206 N  N     . THR A 1 2535 ? 197.703 127.366 131.350 1.00 111.09 ? 3752 THR A N     1 
ATOM   15207 C  CA    . THR A 1 2535 ? 198.760 128.132 130.695 1.00 110.57 ? 3752 THR A CA    1 
ATOM   15208 C  C     . THR A 1 2535 ? 198.302 128.691 129.354 1.00 106.60 ? 3752 THR A C     1 
ATOM   15209 O  O     . THR A 1 2535 ? 198.825 129.715 128.901 1.00 104.06 ? 3752 THR A O     1 
ATOM   15210 C  CB    . THR A 1 2535 ? 200.014 127.276 130.515 1.00 113.32 ? 3752 THR A CB    1 
ATOM   15211 O  OG1   . THR A 1 2535 ? 199.700 126.107 129.745 1.00 114.65 ? 3752 THR A OG1   1 
ATOM   15212 C  CG2   . THR A 1 2535 ? 200.600 126.879 131.866 1.00 111.57 ? 3752 THR A CG2   1 
ATOM   15213 N  N     . THR A 1 2536 ? 197.339 128.040 128.707 1.00 105.22 ? 3753 THR A N     1 
ATOM   15214 C  CA    . THR A 1 2536 ? 196.723 128.574 127.501 1.00 104.92 ? 3753 THR A CA    1 
ATOM   15215 C  C     . THR A 1 2536 ? 195.543 129.487 127.805 1.00 103.33 ? 3753 THR A C     1 
ATOM   15216 O  O     . THR A 1 2536 ? 194.922 130.000 126.867 1.00 101.64 ? 3753 THR A O     1 
ATOM   15217 C  CB    . THR A 1 2536 ? 196.266 127.437 126.583 1.00 104.16 ? 3753 THR A CB    1 
ATOM   15218 N  N     . LYS A 1 2537 ? 195.227 129.686 129.090 1.00 101.95 ? 3754 LYS A N     1 
ATOM   15219 C  CA    . LYS A 1 2537 ? 194.148 130.571 129.542 1.00 97.01  ? 3754 LYS A CA    1 
ATOM   15220 C  C     . LYS A 1 2537 ? 192.798 130.154 128.965 1.00 91.95  ? 3754 LYS A C     1 
ATOM   15221 O  O     . LYS A 1 2537 ? 191.970 130.992 128.603 1.00 89.56  ? 3754 LYS A O     1 
ATOM   15222 C  CB    . LYS A 1 2537 ? 194.455 132.034 129.211 1.00 97.11  ? 3754 LYS A CB    1 
ATOM   15223 C  CG    . LYS A 1 2537 ? 195.613 132.618 130.002 1.00 99.45  ? 3754 LYS A CG    1 
ATOM   15224 C  CD    . LYS A 1 2537 ? 196.155 133.872 129.336 1.00 99.62  ? 3754 LYS A CD    1 
ATOM   15225 C  CE    . LYS A 1 2537 ? 196.829 133.546 128.013 1.00 103.02 ? 3754 LYS A CE    1 
ATOM   15226 N  NZ    . LYS A 1 2537 ? 197.616 132.283 128.081 1.00 106.11 ? 3754 LYS A NZ    1 
ATOM   15227 N  N     . SER A 1 2538 ? 192.572 128.843 128.878 1.00 91.57  ? 3755 SER A N     1 
ATOM   15228 C  CA    . SER A 1 2538 ? 191.310 128.302 128.378 1.00 86.85  ? 3755 SER A CA    1 
ATOM   15229 C  C     . SER A 1 2538 ? 190.447 127.953 129.587 1.00 82.93  ? 3755 SER A C     1 
ATOM   15230 O  O     . SER A 1 2538 ? 190.339 126.800 130.006 1.00 86.10  ? 3755 SER A O     1 
ATOM   15231 C  CB    . SER A 1 2538 ? 191.560 127.099 127.474 1.00 89.48  ? 3755 SER A CB    1 
ATOM   15232 O  OG    . SER A 1 2538 ? 190.442 126.852 126.642 1.00 86.63  ? 3755 SER A OG    1 
ATOM   15233 N  N     . TYR A 1 2539 ? 189.833 128.993 130.158 1.00 80.06  ? 3756 TYR A N     1 
ATOM   15234 C  CA    . TYR A 1 2539 ? 189.095 128.852 131.410 1.00 80.73  ? 3756 TYR A CA    1 
ATOM   15235 C  C     . TYR A 1 2539 ? 187.877 127.952 131.251 1.00 85.03  ? 3756 TYR A C     1 
ATOM   15236 O  O     . TYR A 1 2539 ? 187.606 127.101 132.112 1.00 90.03  ? 3756 TYR A O     1 
ATOM   15237 C  CB    . TYR A 1 2539 ? 188.671 130.231 131.912 1.00 75.08  ? 3756 TYR A CB    1 
ATOM   15238 C  CG    . TYR A 1 2539 ? 189.788 131.248 131.947 1.00 77.31  ? 3756 TYR A CG    1 
ATOM   15239 C  CD1   . TYR A 1 2539 ? 190.644 131.330 133.036 1.00 79.13  ? 3756 TYR A CD1   1 
ATOM   15240 C  CD2   . TYR A 1 2539 ? 189.981 132.131 130.893 1.00 76.16  ? 3756 TYR A CD2   1 
ATOM   15241 C  CE1   . TYR A 1 2539 ? 191.665 132.260 133.072 1.00 80.06  ? 3756 TYR A CE1   1 
ATOM   15242 C  CE2   . TYR A 1 2539 ? 191.000 133.062 130.918 1.00 75.31  ? 3756 TYR A CE2   1 
ATOM   15243 C  CZ    . TYR A 1 2539 ? 191.838 133.123 132.011 1.00 80.44  ? 3756 TYR A CZ    1 
ATOM   15244 O  OH    . TYR A 1 2539 ? 192.852 134.051 132.041 1.00 83.93  ? 3756 TYR A OH    1 
ATOM   15245 N  N     . ILE A 1 2540 ? 187.128 128.128 130.160 1.00 82.93  ? 3757 ILE A N     1 
ATOM   15246 C  CA    . ILE A 1 2540 ? 185.951 127.300 129.928 1.00 86.20  ? 3757 ILE A CA    1 
ATOM   15247 C  C     . ILE A 1 2540 ? 186.358 125.847 129.718 1.00 90.40  ? 3757 ILE A C     1 
ATOM   15248 O  O     . ILE A 1 2540 ? 185.667 124.926 130.167 1.00 92.74  ? 3757 ILE A O     1 
ATOM   15249 C  CB    . ILE A 1 2540 ? 185.125 127.855 128.749 1.00 82.46  ? 3757 ILE A CB    1 
ATOM   15250 C  CG1   . ILE A 1 2540 ? 183.866 127.013 128.523 1.00 79.58  ? 3757 ILE A CG1   1 
ATOM   15251 C  CG2   . ILE A 1 2540 ? 185.964 127.967 127.478 1.00 79.14  ? 3757 ILE A CG2   1 
ATOM   15252 C  CD1   . ILE A 1 2540 ? 182.937 126.970 129.719 1.00 76.68  ? 3757 ILE A CD1   1 
ATOM   15253 N  N     . SER A 1 2541 ? 187.508 125.617 129.077 1.00 87.68  ? 3758 SER A N     1 
ATOM   15254 C  CA    . SER A 1 2541 ? 188.000 124.254 128.916 1.00 88.66  ? 3758 SER A CA    1 
ATOM   15255 C  C     . SER A 1 2541 ? 188.422 123.657 130.252 1.00 92.16  ? 3758 SER A C     1 
ATOM   15256 O  O     . SER A 1 2541 ? 188.242 122.459 130.479 1.00 96.04  ? 3758 SER A O     1 
ATOM   15257 C  CB    . SER A 1 2541 ? 189.159 124.221 127.923 1.00 91.86  ? 3758 SER A CB    1 
ATOM   15258 O  OG    . SER A 1 2541 ? 188.687 124.274 126.588 1.00 92.62  ? 3758 SER A OG    1 
ATOM   15259 N  N     . ALA A 1 2542 ? 188.978 124.475 131.151 1.00 91.14  ? 3759 ALA A N     1 
ATOM   15260 C  CA    . ALA A 1 2542 ? 189.350 123.973 132.472 1.00 92.04  ? 3759 ALA A CA    1 
ATOM   15261 C  C     . ALA A 1 2542 ? 188.120 123.579 133.284 1.00 91.05  ? 3759 ALA A C     1 
ATOM   15262 O  O     . ALA A 1 2542 ? 188.105 122.521 133.929 1.00 93.63  ? 3759 ALA A O     1 
ATOM   15263 C  CB    . ALA A 1 2542 ? 190.174 125.020 133.220 1.00 89.88  ? 3759 ALA A CB    1 
ATOM   15264 N  N     . LEU A 1 2543 ? 187.078 124.413 133.259 1.00 86.57  ? 3760 LEU A N     1 
ATOM   15265 C  CA    . LEU A 1 2543 ? 185.846 124.062 133.961 1.00 87.45  ? 3760 LEU A CA    1 
ATOM   15266 C  C     . LEU A 1 2543 ? 185.177 122.844 133.333 1.00 92.41  ? 3760 LEU A C     1 
ATOM   15267 O  O     . LEU A 1 2543 ? 184.647 121.982 134.047 1.00 92.41  ? 3760 LEU A O     1 
ATOM   15268 C  CB    . LEU A 1 2543 ? 184.897 125.256 133.975 1.00 83.30  ? 3760 LEU A CB    1 
ATOM   15269 C  CG    . LEU A 1 2543 ? 185.467 126.499 134.654 1.00 80.86  ? 3760 LEU A CG    1 
ATOM   15270 C  CD1   . LEU A 1 2543 ? 184.879 127.758 134.046 1.00 79.21  ? 3760 LEU A CD1   1 
ATOM   15271 C  CD2   . LEU A 1 2543 ? 185.210 126.447 136.152 1.00 78.11  ? 3760 LEU A CD2   1 
ATOM   15272 N  N     . ASN A 1 2544 ? 185.202 122.753 131.999 1.00 94.69  ? 3761 ASN A N     1 
ATOM   15273 C  CA    . ASN A 1 2544 ? 184.670 121.584 131.308 1.00 98.11  ? 3761 ASN A CA    1 
ATOM   15274 C  C     . ASN A 1 2544 ? 185.438 120.326 131.692 1.00 98.05  ? 3761 ASN A C     1 
ATOM   15275 O  O     . ASN A 1 2544 ? 184.842 119.259 131.881 1.00 97.26  ? 3761 ASN A O     1 
ATOM   15276 C  CB    . ASN A 1 2544 ? 184.730 121.814 129.796 1.00 97.99  ? 3761 ASN A CB    1 
ATOM   15277 C  CG    . ASN A 1 2544 ? 183.782 120.917 129.020 1.00 101.10 ? 3761 ASN A CG    1 
ATOM   15278 O  OD1   . ASN A 1 2544 ? 183.615 119.739 129.333 1.00 99.74  ? 3761 ASN A OD1   1 
ATOM   15279 N  ND2   . ASN A 1 2544 ? 183.156 121.477 127.991 1.00 102.08 ? 3761 ASN A ND2   1 
ATOM   15280 N  N     . TRP A 1 2545 ? 186.762 120.435 131.809 1.00 97.07  ? 3762 TRP A N     1 
ATOM   15281 C  CA    . TRP A 1 2545 ? 187.574 119.290 132.196 1.00 97.98  ? 3762 TRP A CA    1 
ATOM   15282 C  C     . TRP A 1 2545 ? 187.278 118.850 133.623 1.00 96.73  ? 3762 TRP A C     1 
ATOM   15283 O  O     . TRP A 1 2545 ? 187.193 117.650 133.895 1.00 97.29  ? 3762 TRP A O     1 
ATOM   15284 C  CB    . TRP A 1 2545 ? 189.055 119.615 132.041 1.00 100.84 ? 3762 TRP A CB    1 
ATOM   15285 C  CG    . TRP A 1 2545 ? 189.913 118.469 132.415 1.00 105.20 ? 3762 TRP A CG    1 
ATOM   15286 C  CD1   . TRP A 1 2545 ? 190.009 117.270 131.773 1.00 106.79 ? 3762 TRP A CD1   1 
ATOM   15287 C  CD2   . TRP A 1 2545 ? 190.770 118.386 133.553 1.00 105.20 ? 3762 TRP A CD2   1 
ATOM   15288 N  NE1   . TRP A 1 2545 ? 190.892 116.453 132.431 1.00 107.92 ? 3762 TRP A NE1   1 
ATOM   15289 C  CE2   . TRP A 1 2545 ? 191.372 117.117 133.529 1.00 109.19 ? 3762 TRP A CE2   1 
ATOM   15290 C  CE3   . TRP A 1 2545 ? 191.099 119.268 134.583 1.00 102.65 ? 3762 TRP A CE3   1 
ATOM   15291 C  CZ2   . TRP A 1 2545 ? 192.277 116.708 134.495 1.00 114.13 ? 3762 TRP A CZ2   1 
ATOM   15292 C  CZ3   . TRP A 1 2545 ? 191.998 118.858 135.543 1.00 106.66 ? 3762 TRP A CZ3   1 
ATOM   15293 C  CH2   . TRP A 1 2545 ? 192.579 117.592 135.492 1.00 113.53 ? 3762 TRP A CH2   1 
ATOM   15294 N  N     . PHE A 1 2546 ? 187.125 119.804 134.547 1.00 93.43  ? 3763 PHE A N     1 
ATOM   15295 C  CA    . PHE A 1 2546 ? 186.706 119.457 135.906 1.00 91.01  ? 3763 PHE A CA    1 
ATOM   15296 C  C     . PHE A 1 2546 ? 185.362 118.732 135.910 1.00 89.10  ? 3763 PHE A C     1 
ATOM   15297 O  O     . PHE A 1 2546 ? 185.209 117.676 136.546 1.00 89.84  ? 3763 PHE A O     1 
ATOM   15298 C  CB    . PHE A 1 2546 ? 186.617 120.711 136.775 1.00 90.66  ? 3763 PHE A CB    1 
ATOM   15299 C  CG    . PHE A 1 2546 ? 187.939 121.328 137.137 1.00 97.27  ? 3763 PHE A CG    1 
ATOM   15300 C  CD1   . PHE A 1 2546 ? 189.124 120.634 136.986 1.00 102.42 ? 3763 PHE A CD1   1 
ATOM   15301 C  CD2   . PHE A 1 2546 ? 187.983 122.610 137.665 1.00 93.23  ? 3763 PHE A CD2   1 
ATOM   15302 C  CE1   . PHE A 1 2546 ? 190.332 121.214 137.340 1.00 100.24 ? 3763 PHE A CE1   1 
ATOM   15303 C  CE2   . PHE A 1 2546 ? 189.186 123.194 138.016 1.00 96.42  ? 3763 PHE A CE2   1 
ATOM   15304 C  CZ    . PHE A 1 2546 ? 190.362 122.494 137.853 1.00 99.63  ? 3763 PHE A CZ    1 
ATOM   15305 N  N     . LYS A 1 2547 ? 184.379 119.286 135.192 1.00 92.54  ? 3764 LYS A N     1 
ATOM   15306 C  CA    . LYS A 1 2547 ? 183.033 118.719 135.197 1.00 94.03  ? 3764 LYS A CA    1 
ATOM   15307 C  C     . LYS A 1 2547 ? 183.009 117.327 134.575 1.00 93.61  ? 3764 LYS A C     1 
ATOM   15308 O  O     . LYS A 1 2547 ? 182.300 116.437 135.058 1.00 89.91  ? 3764 LYS A O     1 
ATOM   15309 C  CB    . LYS A 1 2547 ? 182.071 119.652 134.462 1.00 95.58  ? 3764 LYS A CB    1 
ATOM   15310 N  N     . ASN A 1 2548 ? 183.774 117.121 133.501 1.00 92.02  ? 3765 ASN A N     1 
ATOM   15311 C  CA    . ASN A 1 2548 ? 183.839 115.802 132.881 1.00 89.01  ? 3765 ASN A CA    1 
ATOM   15312 C  C     . ASN A 1 2548 ? 184.677 114.833 133.704 1.00 91.38  ? 3765 ASN A C     1 
ATOM   15313 O  O     . ASN A 1 2548 ? 184.462 113.618 133.634 1.00 90.54  ? 3765 ASN A O     1 
ATOM   15314 C  CB    . ASN A 1 2548 ? 184.400 115.916 131.464 1.00 88.53  ? 3765 ASN A CB    1 
ATOM   15315 N  N     . GLU A 1 2549 ? 185.633 115.345 134.483 1.00 93.46  ? 3766 GLU A N     1 
ATOM   15316 C  CA    . GLU A 1 2549 ? 186.474 114.476 135.294 1.00 92.59  ? 3766 GLU A CA    1 
ATOM   15317 C  C     . GLU A 1 2549 ? 185.704 113.906 136.474 1.00 87.62  ? 3766 GLU A C     1 
ATOM   15318 O  O     . GLU A 1 2549 ? 185.804 112.708 136.763 1.00 85.13  ? 3766 GLU A O     1 
ATOM   15319 C  CB    . GLU A 1 2549 ? 187.707 115.240 135.776 1.00 95.71  ? 3766 GLU A CB    1 
ATOM   15320 N  N     . PHE A 1 2550 ? 184.932 114.737 137.174 1.00 86.13  ? 3767 PHE A N     1 
ATOM   15321 C  CA    . PHE A 1 2550 ? 184.185 114.191 138.305 1.00 81.19  ? 3767 PHE A CA    1 
ATOM   15322 C  C     . PHE A 1 2550 ? 182.844 113.601 137.872 1.00 81.82  ? 3767 PHE A C     1 
ATOM   15323 O  O     . PHE A 1 2550 ? 182.604 112.402 138.042 1.00 83.71  ? 3767 PHE A O     1 
ATOM   15324 C  CB    . PHE A 1 2550 ? 183.964 115.257 139.381 1.00 78.93  ? 3767 PHE A CB    1 
ATOM   15325 C  CG    . PHE A 1 2550 ? 183.332 114.721 140.641 1.00 76.16  ? 3767 PHE A CG    1 
ATOM   15326 C  CD1   . PHE A 1 2550 ? 183.586 113.425 141.068 1.00 76.07  ? 3767 PHE A CD1   1 
ATOM   15327 C  CD2   . PHE A 1 2550 ? 182.472 115.505 141.386 1.00 73.77  ? 3767 PHE A CD2   1 
ATOM   15328 C  CE1   . PHE A 1 2550 ? 183.001 112.931 142.216 1.00 70.38  ? 3767 PHE A CE1   1 
ATOM   15329 C  CE2   . PHE A 1 2550 ? 181.883 115.015 142.536 1.00 73.26  ? 3767 PHE A CE2   1 
ATOM   15330 C  CZ    . PHE A 1 2550 ? 182.148 113.727 142.950 1.00 70.91  ? 3767 PHE A CZ    1 
ATOM   15331 N  N     . PHE A 1 2551 ? 181.966 114.428 137.315 1.00 82.64  ? 3768 PHE A N     1 
ATOM   15332 C  CA    . PHE A 1 2551 ? 180.606 114.007 137.011 1.00 85.93  ? 3768 PHE A CA    1 
ATOM   15333 C  C     . PHE A 1 2551 ? 180.550 113.365 135.633 1.00 92.75  ? 3768 PHE A C     1 
ATOM   15334 O  O     . PHE A 1 2551 ? 181.031 113.937 134.650 1.00 93.04  ? 3768 PHE A O     1 
ATOM   15335 C  CB    . PHE A 1 2551 ? 179.645 115.192 137.092 1.00 81.81  ? 3768 PHE A CB    1 
ATOM   15336 C  CG    . PHE A 1 2551 ? 179.521 115.777 138.469 1.00 76.53  ? 3768 PHE A CG    1 
ATOM   15337 C  CD1   . PHE A 1 2551 ? 178.799 115.118 139.452 1.00 72.87  ? 3768 PHE A CD1   1 
ATOM   15338 C  CD2   . PHE A 1 2551 ? 180.121 116.985 138.781 1.00 74.35  ? 3768 PHE A CD2   1 
ATOM   15339 C  CE1   . PHE A 1 2551 ? 178.680 115.652 140.721 1.00 69.36  ? 3768 PHE A CE1   1 
ATOM   15340 C  CE2   . PHE A 1 2551 ? 180.004 117.524 140.049 1.00 69.76  ? 3768 PHE A CE2   1 
ATOM   15341 C  CZ    . PHE A 1 2551 ? 179.283 116.856 141.020 1.00 66.45  ? 3768 PHE A CZ    1 
ATOM   15342 N  N     . VAL A 1 2552 ? 179.958 112.174 135.567 1.00 94.41  ? 3769 VAL A N     1 
ATOM   15343 C  CA    . VAL A 1 2552 ? 179.864 111.420 134.321 1.00 93.67  ? 3769 VAL A CA    1 
ATOM   15344 C  C     . VAL A 1 2552 ? 178.452 111.374 133.763 1.00 92.51  ? 3769 VAL A C     1 
ATOM   15345 O  O     . VAL A 1 2552 ? 178.272 110.921 132.620 1.00 91.60  ? 3769 VAL A O     1 
ATOM   15346 C  CB    . VAL A 1 2552 ? 180.408 109.986 134.489 1.00 94.97  ? 3769 VAL A CB    1 
ATOM   15347 C  CG1   . VAL A 1 2552 ? 181.899 110.016 134.786 1.00 95.13  ? 3769 VAL A CG1   1 
ATOM   15348 C  CG2   . VAL A 1 2552 ? 179.656 109.262 135.593 1.00 93.43  ? 3769 VAL A CG2   1 
ATOM   15349 N  N     . ASP A 1 2553 ? 177.450 111.825 134.513 1.00 93.84  ? 3770 ASP A N     1 
ATOM   15350 C  CA    . ASP A 1 2553 ? 176.067 111.783 134.069 1.00 94.54  ? 3770 ASP A CA    1 
ATOM   15351 C  C     . ASP A 1 2553 ? 175.435 113.161 134.204 1.00 95.83  ? 3770 ASP A C     1 
ATOM   15352 O  O     . ASP A 1 2553 ? 175.869 113.994 135.004 1.00 96.26  ? 3770 ASP A O     1 
ATOM   15353 C  CB    . ASP A 1 2553 ? 175.245 110.752 134.860 1.00 93.40  ? 3770 ASP A CB    1 
ATOM   15354 C  CG    . ASP A 1 2553 ? 175.312 110.975 136.361 1.00 96.00  ? 3770 ASP A CG    1 
ATOM   15355 O  OD1   . ASP A 1 2553 ? 176.187 111.739 136.820 1.00 96.59  ? 3770 ASP A OD1   1 
ATOM   15356 O  OD2   . ASP A 1 2553 ? 174.483 110.384 137.084 1.00 96.51  ? 3770 ASP A OD2   1 
ATOM   15357 N  N     . GLU A 1 2554 ? 174.398 113.389 133.402 1.00 93.72  ? 3771 GLU A N     1 
ATOM   15358 C  CA    . GLU A 1 2554 ? 173.637 114.628 133.457 1.00 89.03  ? 3771 GLU A CA    1 
ATOM   15359 C  C     . GLU A 1 2554 ? 172.265 114.379 132.852 1.00 90.00  ? 3771 GLU A C     1 
ATOM   15360 O  O     . GLU A 1 2554 ? 172.061 113.421 132.102 1.00 90.96  ? 3771 GLU A O     1 
ATOM   15361 C  CB    . GLU A 1 2554 ? 174.354 115.766 132.721 1.00 90.71  ? 3771 GLU A CB    1 
ATOM   15362 N  N     . TRP A 1 2555 ? 171.326 115.258 133.187 1.00 91.11  ? 3772 TRP A N     1 
ATOM   15363 C  CA    . TRP A 1 2555 ? 169.983 115.223 132.630 1.00 93.03  ? 3772 TRP A CA    1 
ATOM   15364 C  C     . TRP A 1 2555 ? 169.795 116.355 131.631 1.00 97.12  ? 3772 TRP A C     1 
ATOM   15365 O  O     . TRP A 1 2555 ? 170.142 117.508 131.907 1.00 96.49  ? 3772 TRP A O     1 
ATOM   15366 C  CB    . TRP A 1 2555 ? 168.912 115.331 133.720 1.00 87.35  ? 3772 TRP A CB    1 
ATOM   15367 C  CG    . TRP A 1 2555 ? 168.538 114.031 134.358 1.00 87.14  ? 3772 TRP A CG    1 
ATOM   15368 C  CD1   . TRP A 1 2555 ? 168.977 112.788 134.010 1.00 89.55  ? 3772 TRP A CD1   1 
ATOM   15369 C  CD2   . TRP A 1 2555 ? 167.604 113.842 135.427 1.00 84.47  ? 3772 TRP A CD2   1 
ATOM   15370 N  NE1   . TRP A 1 2555 ? 168.392 111.838 134.812 1.00 88.26  ? 3772 TRP A NE1   1 
ATOM   15371 C  CE2   . TRP A 1 2555 ? 167.541 112.459 135.687 1.00 86.07  ? 3772 TRP A CE2   1 
ATOM   15372 C  CE3   . TRP A 1 2555 ? 166.822 114.709 136.195 1.00 82.98  ? 3772 TRP A CE3   1 
ATOM   15373 C  CZ2   . TRP A 1 2555 ? 166.732 111.923 136.687 1.00 83.32  ? 3772 TRP A CZ2   1 
ATOM   15374 C  CZ3   . TRP A 1 2555 ? 166.016 114.174 137.186 1.00 81.71  ? 3772 TRP A CZ3   1 
ATOM   15375 C  CH2   . TRP A 1 2555 ? 165.977 112.795 137.422 1.00 78.78  ? 3772 TRP A CH2   1 
ATOM   15376 N  N     . ASN A 1 2556 ? 169.246 116.016 130.470 1.00 96.08  ? 3773 ASN A N     1 
ATOM   15377 C  CA    . ASN A 1 2556 ? 168.766 117.010 129.525 1.00 92.30  ? 3773 ASN A CA    1 
ATOM   15378 C  C     . ASN A 1 2556 ? 167.330 117.374 129.899 1.00 91.42  ? 3773 ASN A C     1 
ATOM   15379 O  O     . ASN A 1 2556 ? 166.823 116.979 130.952 1.00 93.62  ? 3773 ASN A O     1 
ATOM   15380 C  CB    . ASN A 1 2556 ? 168.883 116.487 128.095 1.00 94.20  ? 3773 ASN A CB    1 
ATOM   15381 C  CG    . ASN A 1 2556 ? 168.415 115.052 127.960 1.00 101.06 ? 3773 ASN A CG    1 
ATOM   15382 O  OD1   . ASN A 1 2556 ? 167.228 114.758 128.102 1.00 101.64 ? 3773 ASN A OD1   1 
ATOM   15383 N  ND2   . ASN A 1 2556 ? 169.348 114.149 127.684 1.00 102.83 ? 3773 ASN A ND2   1 
ATOM   15384 N  N     . ILE A 1 2557 ? 166.659 118.144 129.041 1.00 89.95  ? 3774 ILE A N     1 
ATOM   15385 C  CA    . ILE A 1 2557 ? 165.272 118.509 129.309 1.00 93.56  ? 3774 ILE A CA    1 
ATOM   15386 C  C     . ILE A 1 2557 ? 164.375 117.277 129.248 1.00 91.95  ? 3774 ILE A C     1 
ATOM   15387 O  O     . ILE A 1 2557 ? 163.499 117.086 130.102 1.00 92.69  ? 3774 ILE A O     1 
ATOM   15388 C  CB    . ILE A 1 2557 ? 164.811 119.601 128.327 1.00 98.76  ? 3774 ILE A CB    1 
ATOM   15389 C  CG1   . ILE A 1 2557 ? 165.746 120.811 128.395 1.00 95.07  ? 3774 ILE A CG1   1 
ATOM   15390 C  CG2   . ILE A 1 2557 ? 163.383 120.026 128.629 1.00 95.67  ? 3774 ILE A CG2   1 
ATOM   15391 C  CD1   . ILE A 1 2557 ? 165.937 121.369 129.788 1.00 85.18  ? 3774 ILE A CD1   1 
ATOM   15392 N  N     . ALA A 1 2558 ? 164.590 116.417 128.248 1.00 89.19  ? 3775 ALA A N     1 
ATOM   15393 C  CA    . ALA A 1 2558 ? 163.786 115.206 128.121 1.00 91.07  ? 3775 ALA A CA    1 
ATOM   15394 C  C     . ALA A 1 2558 ? 163.991 114.276 129.310 1.00 94.12  ? 3775 ALA A C     1 
ATOM   15395 O  O     . ALA A 1 2558 ? 163.036 113.659 129.797 1.00 96.66  ? 3775 ALA A O     1 
ATOM   15396 C  CB    . ALA A 1 2558 ? 164.123 114.488 126.814 1.00 94.77  ? 3775 ALA A CB    1 
ATOM   15397 N  N     . ASP A 1 2559 ? 165.229 114.170 129.797 1.00 95.34  ? 3776 ASP A N     1 
ATOM   15398 C  CA    . ASP A 1 2559 ? 165.501 113.311 130.945 1.00 95.26  ? 3776 ASP A CA    1 
ATOM   15399 C  C     . ASP A 1 2559 ? 164.845 113.844 132.215 1.00 93.27  ? 3776 ASP A C     1 
ATOM   15400 O  O     . ASP A 1 2559 ? 164.294 113.066 133.003 1.00 91.88  ? 3776 ASP A O     1 
ATOM   15401 C  CB    . ASP A 1 2559 ? 167.008 113.160 131.141 1.00 96.36  ? 3776 ASP A CB    1 
ATOM   15402 C  CG    . ASP A 1 2559 ? 167.607 112.091 130.249 1.00 101.15 ? 3776 ASP A CG    1 
ATOM   15403 O  OD1   . ASP A 1 2559 ? 166.974 111.744 129.229 1.00 100.24 ? 3776 ASP A OD1   1 
ATOM   15404 O  OD2   . ASP A 1 2559 ? 168.708 111.595 130.568 1.00 104.33 ? 3776 ASP A OD2   1 
ATOM   15405 N  N     . VAL A 1 2560 ? 164.896 115.161 132.437 1.00 93.03  ? 3777 VAL A N     1 
ATOM   15406 C  CA    . VAL A 1 2560 ? 164.325 115.702 133.668 1.00 90.49  ? 3777 VAL A CA    1 
ATOM   15407 C  C     . VAL A 1 2560 ? 162.799 115.663 133.626 1.00 88.38  ? 3777 VAL A C     1 
ATOM   15408 O  O     . VAL A 1 2560 ? 162.153 115.463 134.662 1.00 85.67  ? 3777 VAL A O     1 
ATOM   15409 C  CB    . VAL A 1 2560 ? 164.871 117.118 133.964 1.00 84.89  ? 3777 VAL A CB    1 
ATOM   15410 C  CG1   . VAL A 1 2560 ? 164.420 118.135 132.935 1.00 78.57  ? 3777 VAL A CG1   1 
ATOM   15411 C  CG2   . VAL A 1 2560 ? 164.475 117.566 135.366 1.00 81.03  ? 3777 VAL A CG2   1 
ATOM   15412 N  N     . VAL A 1 2561 ? 162.188 115.825 132.448 1.00 90.24  ? 3778 VAL A N     1 
ATOM   15413 C  CA    . VAL A 1 2561 ? 160.732 115.718 132.395 1.00 91.99  ? 3778 VAL A CA    1 
ATOM   15414 C  C     . VAL A 1 2561 ? 160.302 114.255 132.413 1.00 94.40  ? 3778 VAL A C     1 
ATOM   15415 O  O     . VAL A 1 2561 ? 159.161 113.937 132.770 1.00 96.79  ? 3778 VAL A O     1 
ATOM   15416 C  CB    . VAL A 1 2561 ? 160.162 116.461 131.172 1.00 92.72  ? 3778 VAL A CB    1 
ATOM   15417 C  CG1   . VAL A 1 2561 ? 160.572 117.928 131.193 1.00 91.89  ? 3778 VAL A CG1   1 
ATOM   15418 C  CG2   . VAL A 1 2561 ? 160.571 115.780 129.881 1.00 93.40  ? 3778 VAL A CG2   1 
ATOM   15419 N  N     . ALA A 1 2562 ? 161.200 113.343 132.028 1.00 95.10  ? 3779 ALA A N     1 
ATOM   15420 C  CA    . ALA A 1 2562 ? 160.847 111.927 132.010 1.00 94.66  ? 3779 ALA A CA    1 
ATOM   15421 C  C     . ALA A 1 2562 ? 160.761 111.354 133.420 1.00 94.94  ? 3779 ALA A C     1 
ATOM   15422 O  O     . ALA A 1 2562 ? 159.808 110.639 133.750 1.00 97.57  ? 3779 ALA A O     1 
ATOM   15423 C  CB    . ALA A 1 2562 ? 161.859 111.144 131.174 1.00 95.56  ? 3779 ALA A CB    1 
ATOM   15424 N  N     . ASN A 1 2563 ? 161.746 111.658 134.267 1.00 93.91  ? 3780 ASN A N     1 
ATOM   15425 C  CA    . ASN A 1 2563 ? 161.787 111.135 135.634 1.00 96.65  ? 3780 ASN A CA    1 
ATOM   15426 C  C     . ASN A 1 2563 ? 161.115 112.131 136.581 1.00 100.83 ? 3780 ASN A C     1 
ATOM   15427 O  O     . ASN A 1 2563 ? 161.731 112.722 137.470 1.00 103.73 ? 3780 ASN A O     1 
ATOM   15428 C  CB    . ASN A 1 2563 ? 163.222 110.844 136.050 1.00 90.06  ? 3780 ASN A CB    1 
ATOM   15429 N  N     . SER A 1 2564 ? 159.813 112.306 136.373 1.00 98.67  ? 3781 SER A N     1 
ATOM   15430 C  CA    . SER A 1 2564 ? 159.031 113.246 137.163 1.00 98.75  ? 3781 SER A CA    1 
ATOM   15431 C  C     . SER A 1 2564 ? 157.721 112.584 137.561 1.00 99.29  ? 3781 SER A C     1 
ATOM   15432 O  O     . SER A 1 2564 ? 157.240 111.667 136.891 1.00 98.98  ? 3781 SER A O     1 
ATOM   15433 C  CB    . SER A 1 2564 ? 158.771 114.545 136.393 1.00 98.76  ? 3781 SER A CB    1 
ATOM   15434 O  OG    . SER A 1 2564 ? 159.973 115.076 135.862 1.00 95.38  ? 3781 SER A OG    1 
ATOM   15435 N  N     . GLU A 1 2565 ? 157.145 113.064 138.663 1.00 102.16 ? 3782 GLU A N     1 
ATOM   15436 C  CA    . GLU A 1 2565 ? 155.953 112.434 139.219 1.00 105.78 ? 3782 GLU A CA    1 
ATOM   15437 C  C     . GLU A 1 2565 ? 154.788 113.406 139.365 1.00 109.79 ? 3782 GLU A C     1 
ATOM   15438 O  O     . GLU A 1 2565 ? 153.636 113.038 139.110 1.00 109.44 ? 3782 GLU A O     1 
ATOM   15439 C  CB    . GLU A 1 2565 ? 156.277 111.805 140.576 1.00 100.00 ? 3782 GLU A CB    1 
ATOM   15440 N  N     . ASN A 1 2566 ? 155.070 114.642 139.774 1.00 108.17 ? 3783 ASN A N     1 
ATOM   15441 C  CA    . ASN A 1 2566 ? 154.002 115.593 140.052 1.00 108.25 ? 3783 ASN A CA    1 
ATOM   15442 C  C     . ASN A 1 2566 ? 153.371 116.097 138.760 1.00 105.94 ? 3783 ASN A C     1 
ATOM   15443 O  O     . ASN A 1 2566 ? 153.969 116.029 137.682 1.00 104.01 ? 3783 ASN A O     1 
ATOM   15444 C  CB    . ASN A 1 2566 ? 154.534 116.772 140.873 1.00 106.74 ? 3783 ASN A CB    1 
ATOM   15445 C  CG    . ASN A 1 2566 ? 153.493 117.340 141.822 1.00 106.97 ? 3783 ASN A CG    1 
ATOM   15446 O  OD1   . ASN A 1 2566 ? 152.300 117.349 141.522 1.00 106.08 ? 3783 ASN A OD1   1 
ATOM   15447 N  ND2   . ASN A 1 2566 ? 153.944 117.818 142.976 1.00 106.64 ? 3783 ASN A ND2   1 
ATOM   15448 N  N     . ASN A 1 2567 ? 152.143 116.599 138.879 1.00 106.43 ? 3784 ASN A N     1 
ATOM   15449 C  CA    . ASN A 1 2567 ? 151.387 117.116 137.747 1.00 106.84 ? 3784 ASN A CA    1 
ATOM   15450 C  C     . ASN A 1 2567 ? 151.548 118.617 137.556 1.00 106.14 ? 3784 ASN A C     1 
ATOM   15451 O  O     . ASN A 1 2567 ? 150.951 119.176 136.629 1.00 107.61 ? 3784 ASN A O     1 
ATOM   15452 C  CB    . ASN A 1 2567 ? 149.900 116.782 137.914 1.00 109.57 ? 3784 ASN A CB    1 
ATOM   15453 N  N     . TYR A 1 2568 ? 152.327 119.282 138.404 1.00 103.94 ? 3785 TYR A N     1 
ATOM   15454 C  CA    . TYR A 1 2568 ? 152.582 120.709 138.287 1.00 97.70  ? 3785 TYR A CA    1 
ATOM   15455 C  C     . TYR A 1 2568 ? 154.049 120.912 137.940 1.00 92.78  ? 3785 TYR A C     1 
ATOM   15456 O  O     . TYR A 1 2568 ? 154.926 120.304 138.563 1.00 97.61  ? 3785 TYR A O     1 
ATOM   15457 C  CB    . TYR A 1 2568 ? 152.253 121.445 139.590 1.00 101.05 ? 3785 TYR A CB    1 
ATOM   15458 C  CG    . TYR A 1 2568 ? 150.909 121.094 140.191 1.00 107.25 ? 3785 TYR A CG    1 
ATOM   15459 C  CD1   . TYR A 1 2568 ? 149.730 121.415 139.533 1.00 110.00 ? 3785 TYR A CD1   1 
ATOM   15460 C  CD2   . TYR A 1 2568 ? 150.822 120.450 141.417 1.00 110.92 ? 3785 TYR A CD2   1 
ATOM   15461 C  CE1   . TYR A 1 2568 ? 148.500 121.100 140.084 1.00 115.73 ? 3785 TYR A CE1   1 
ATOM   15462 C  CE2   . TYR A 1 2568 ? 149.590 120.133 141.969 1.00 114.47 ? 3785 TYR A CE2   1 
ATOM   15463 C  CZ    . TYR A 1 2568 ? 148.434 120.462 141.296 1.00 116.60 ? 3785 TYR A CZ    1 
ATOM   15464 O  OH    . TYR A 1 2568 ? 147.205 120.154 141.829 1.00 114.78 ? 3785 TYR A OH    1 
ATOM   15465 N  N     . PHE A 1 2569 ? 154.316 121.761 136.954 1.00 83.31  ? 3786 PHE A N     1 
ATOM   15466 C  CA    . PHE A 1 2569 ? 155.678 122.081 136.562 1.00 75.84  ? 3786 PHE A CA    1 
ATOM   15467 C  C     . PHE A 1 2569 ? 155.834 123.590 136.444 1.00 74.19  ? 3786 PHE A C     1 
ATOM   15468 O  O     . PHE A 1 2569 ? 154.862 124.328 136.263 1.00 78.88  ? 3786 PHE A O     1 
ATOM   15469 C  CB    . PHE A 1 2569 ? 156.069 121.420 135.233 1.00 81.36  ? 3786 PHE A CB    1 
ATOM   15470 C  CG    . PHE A 1 2569 ? 156.263 119.934 135.322 1.00 87.63  ? 3786 PHE A CG    1 
ATOM   15471 C  CD1   . PHE A 1 2569 ? 155.178 119.072 135.297 1.00 92.11  ? 3786 PHE A CD1   1 
ATOM   15472 C  CD2   . PHE A 1 2569 ? 157.536 119.395 135.412 1.00 86.97  ? 3786 PHE A CD2   1 
ATOM   15473 C  CE1   . PHE A 1 2569 ? 155.360 117.705 135.371 1.00 94.57  ? 3786 PHE A CE1   1 
ATOM   15474 C  CE2   . PHE A 1 2569 ? 157.723 118.030 135.487 1.00 88.24  ? 3786 PHE A CE2   1 
ATOM   15475 C  CZ    . PHE A 1 2569 ? 156.633 117.185 135.465 1.00 92.64  ? 3786 PHE A CZ    1 
ATOM   15476 N  N     . THR A 1 2570 ? 157.077 124.038 136.576 1.00 72.28  ? 3787 THR A N     1 
ATOM   15477 C  CA    . THR A 1 2570 ? 157.449 125.430 136.376 1.00 66.39  ? 3787 THR A CA    1 
ATOM   15478 C  C     . THR A 1 2570 ? 158.735 125.468 135.566 1.00 55.47  ? 3787 THR A C     1 
ATOM   15479 O  O     . THR A 1 2570 ? 159.638 124.658 135.785 1.00 62.19  ? 3787 THR A O     1 
ATOM   15480 C  CB    . THR A 1 2570 ? 157.627 126.162 137.714 1.00 69.48  ? 3787 THR A CB    1 
ATOM   15481 O  OG1   . THR A 1 2570 ? 156.465 125.961 138.525 1.00 75.11  ? 3787 THR A OG1   1 
ATOM   15482 C  CG2   . THR A 1 2570 ? 157.813 127.656 137.493 1.00 65.70  ? 3787 THR A CG2   1 
ATOM   15483 N  N     . MET A 1 2571 ? 158.807 126.397 134.622 1.00 48.74  ? 3788 MET A N     1 
ATOM   15484 C  CA    . MET A 1 2571 ? 159.946 126.519 133.728 1.00 49.81  ? 3788 MET A CA    1 
ATOM   15485 C  C     . MET A 1 2571 ? 160.333 127.987 133.636 1.00 53.61  ? 3788 MET A C     1 
ATOM   15486 O  O     . MET A 1 2571 ? 159.464 128.861 133.573 1.00 60.92  ? 3788 MET A O     1 
ATOM   15487 C  CB    . MET A 1 2571 ? 159.599 125.948 132.348 1.00 49.20  ? 3788 MET A CB    1 
ATOM   15488 C  CG    . MET A 1 2571 ? 160.609 126.183 131.247 1.00 46.92  ? 3788 MET A CG    1 
ATOM   15489 S  SD    . MET A 1 2571 ? 160.627 124.764 130.138 1.00 59.62  ? 3788 MET A SD    1 
ATOM   15490 C  CE    . MET A 1 2571 ? 161.795 125.304 128.900 1.00 61.45  ? 3788 MET A CE    1 
ATOM   15491 N  N     . ALA A 1 2572 ? 161.635 128.255 133.639 1.00 51.67  ? 3789 ALA A N     1 
ATOM   15492 C  CA    . ALA A 1 2572 ? 162.138 129.619 133.638 1.00 50.83  ? 3789 ALA A CA    1 
ATOM   15493 C  C     . ALA A 1 2572 ? 163.306 129.724 132.672 1.00 53.13  ? 3789 ALA A C     1 
ATOM   15494 O  O     . ALA A 1 2572 ? 163.972 128.734 132.363 1.00 59.44  ? 3789 ALA A O     1 
ATOM   15495 C  CB    . ALA A 1 2572 ? 162.570 130.063 135.040 1.00 53.05  ? 3789 ALA A CB    1 
ATOM   15496 N  N     . SER A 1 2573 ? 163.549 130.943 132.200 1.00 52.04  ? 3790 SER A N     1 
ATOM   15497 C  CA    . SER A 1 2573 ? 164.626 131.204 131.254 1.00 53.55  ? 3790 SER A CA    1 
ATOM   15498 C  C     . SER A 1 2573 ? 164.896 132.700 131.226 1.00 57.33  ? 3790 SER A C     1 
ATOM   15499 O  O     . SER A 1 2573 ? 164.109 133.502 131.731 1.00 61.53  ? 3790 SER A O     1 
ATOM   15500 C  CB    . SER A 1 2573 ? 164.273 130.691 129.854 1.00 53.11  ? 3790 SER A CB    1 
ATOM   15501 O  OG    . SER A 1 2573 ? 163.081 131.291 129.380 1.00 52.12  ? 3790 SER A OG    1 
ATOM   15502 N  N     . GLU A 1 2574 ? 166.028 133.067 130.633 1.00 52.69  ? 3791 GLU A N     1 
ATOM   15503 C  CA    . GLU A 1 2574 ? 166.262 134.466 130.317 1.00 50.85  ? 3791 GLU A CA    1 
ATOM   15504 C  C     . GLU A 1 2574 ? 165.338 134.893 129.180 1.00 58.83  ? 3791 GLU A C     1 
ATOM   15505 O  O     . GLU A 1 2574 ? 164.838 134.068 128.412 1.00 64.05  ? 3791 GLU A O     1 
ATOM   15506 C  CB    . GLU A 1 2574 ? 167.724 134.698 129.936 1.00 50.24  ? 3791 GLU A CB    1 
ATOM   15507 C  CG    . GLU A 1 2574 ? 168.247 136.076 130.308 1.00 51.28  ? 3791 GLU A CG    1 
ATOM   15508 C  CD    . GLU A 1 2574 ? 169.739 136.222 130.075 1.00 51.81  ? 3791 GLU A CD    1 
ATOM   15509 O  OE1   . GLU A 1 2574 ? 170.353 135.284 129.524 1.00 49.92  ? 3791 GLU A OE1   1 
ATOM   15510 O  OE2   . GLU A 1 2574 ? 170.299 137.275 130.445 1.00 49.83  ? 3791 GLU A OE2   1 
ATOM   15511 N  N     . ARG A 1 2575 ? 165.100 136.202 129.081 1.00 56.64  ? 3792 ARG A N     1 
ATOM   15512 C  CA    . ARG A 1 2575 ? 164.149 136.696 128.090 1.00 54.35  ? 3792 ARG A CA    1 
ATOM   15513 C  C     . ARG A 1 2575 ? 164.656 136.550 126.660 1.00 53.63  ? 3792 ARG A C     1 
ATOM   15514 O  O     . ARG A 1 2575 ? 163.859 136.663 125.723 1.00 59.68  ? 3792 ARG A O     1 
ATOM   15515 C  CB    . ARG A 1 2575 ? 163.797 138.157 128.372 1.00 47.86  ? 3792 ARG A CB    1 
ATOM   15516 C  CG    . ARG A 1 2575 ? 163.102 138.382 129.705 1.00 48.41  ? 3792 ARG A CG    1 
ATOM   15517 C  CD    . ARG A 1 2575 ? 162.153 139.569 129.640 1.00 48.87  ? 3792 ARG A CD    1 
ATOM   15518 N  NE    . ARG A 1 2575 ? 162.719 140.762 130.258 1.00 45.37  ? 3792 ARG A NE    1 
ATOM   15519 C  CZ    . ARG A 1 2575 ? 162.916 141.910 129.625 1.00 44.51  ? 3792 ARG A CZ    1 
ATOM   15520 N  NH1   . ARG A 1 2575 ? 162.604 142.058 128.348 1.00 44.42  ? 3792 ARG A NH1   1 
ATOM   15521 N  NH2   . ARG A 1 2575 ? 163.443 142.935 130.289 1.00 40.79  ? 3792 ARG A NH2   1 
ATOM   15522 N  N     . ASP A 1 2576 ? 165.951 136.299 126.468 1.00 50.98  ? 3793 ASP A N     1 
ATOM   15523 C  CA    . ASP A 1 2576 ? 166.489 136.085 125.131 1.00 53.68  ? 3793 ASP A CA    1 
ATOM   15524 C  C     . ASP A 1 2576 ? 166.364 134.644 124.654 1.00 59.00  ? 3793 ASP A C     1 
ATOM   15525 O  O     . ASP A 1 2576 ? 166.677 134.368 123.491 1.00 58.24  ? 3793 ASP A O     1 
ATOM   15526 C  CB    . ASP A 1 2576 ? 167.959 136.506 125.076 1.00 50.03  ? 3793 ASP A CB    1 
ATOM   15527 C  CG    . ASP A 1 2576 ? 168.135 137.960 124.694 1.00 48.60  ? 3793 ASP A CG    1 
ATOM   15528 O  OD1   . ASP A 1 2576 ? 167.722 138.338 123.577 1.00 45.74  ? 3793 ASP A OD1   1 
ATOM   15529 O  OD2   . ASP A 1 2576 ? 168.696 138.725 125.504 1.00 46.74  ? 3793 ASP A OD2   1 
ATOM   15530 N  N     . VAL A 1 2577 ? 165.923 133.724 125.508 1.00 63.27  ? 3794 VAL A N     1 
ATOM   15531 C  CA    . VAL A 1 2577 ? 165.798 132.314 125.157 1.00 69.52  ? 3794 VAL A CA    1 
ATOM   15532 C  C     . VAL A 1 2577 ? 164.371 131.866 125.454 1.00 70.34  ? 3794 VAL A C     1 
ATOM   15533 O  O     . VAL A 1 2577 ? 163.796 132.239 126.483 1.00 67.07  ? 3794 VAL A O     1 
ATOM   15534 C  CB    . VAL A 1 2577 ? 166.832 131.444 125.900 1.00 67.05  ? 3794 VAL A CB    1 
ATOM   15535 C  CG1   . VAL A 1 2577 ? 168.232 131.739 125.383 1.00 67.42  ? 3794 VAL A CG1   1 
ATOM   15536 C  CG2   . VAL A 1 2577 ? 166.783 131.683 127.396 1.00 62.68  ? 3794 VAL A CG2   1 
ATOM   15537 N  N     . ASP A 1 2578 ? 163.795 131.091 124.539 1.00 74.94  ? 3795 ASP A N     1 
ATOM   15538 C  CA    . ASP A 1 2578 ? 162.406 130.664 124.628 1.00 77.99  ? 3795 ASP A CA    1 
ATOM   15539 C  C     . ASP A 1 2578 ? 162.318 129.146 124.571 1.00 80.32  ? 3795 ASP A C     1 
ATOM   15540 O  O     . ASP A 1 2578 ? 162.928 128.510 123.705 1.00 80.34  ? 3795 ASP A O     1 
ATOM   15541 C  CB    . ASP A 1 2578 ? 161.572 131.281 123.502 1.00 81.09  ? 3795 ASP A CB    1 
ATOM   15542 C  CG    . ASP A 1 2578 ? 162.279 131.233 122.162 1.00 82.06  ? 3795 ASP A CG    1 
ATOM   15543 O  OD1   . ASP A 1 2578 ? 163.481 130.899 122.134 1.00 80.19  ? 3795 ASP A OD1   1 
ATOM   15544 O  OD2   . ASP A 1 2578 ? 161.632 131.532 121.136 1.00 86.98  ? 3795 ASP A OD2   1 
ATOM   15545 N  N     . GLY A 1 2579 ? 161.557 128.570 125.498 1.00 82.35  ? 3796 GLY A N     1 
ATOM   15546 C  CA    . GLY A 1 2579 ? 161.410 127.129 125.570 1.00 88.31  ? 3796 GLY A CA    1 
ATOM   15547 C  C     . GLY A 1 2579 ? 160.086 126.612 125.044 1.00 94.41  ? 3796 GLY A C     1 
ATOM   15548 O  O     . GLY A 1 2579 ? 159.716 125.464 125.309 1.00 93.68  ? 3796 GLY A O     1 
ATOM   15549 N  N     . THR A 1 2580 ? 159.355 127.454 124.309 1.00 94.95  ? 3797 THR A N     1 
ATOM   15550 C  CA    . THR A 1 2580 ? 158.063 127.039 123.769 1.00 94.43  ? 3797 THR A CA    1 
ATOM   15551 C  C     . THR A 1 2580 ? 158.229 125.953 122.712 1.00 98.23  ? 3797 THR A C     1 
ATOM   15552 O  O     . THR A 1 2580 ? 157.582 124.901 122.779 1.00 102.11 ? 3797 THR A O     1 
ATOM   15553 C  CB    . THR A 1 2580 ? 157.327 128.244 123.186 1.00 92.99  ? 3797 THR A CB    1 
ATOM   15554 O  OG1   . THR A 1 2580 ? 157.875 128.561 121.901 1.00 93.62  ? 3797 THR A OG1   1 
ATOM   15555 C  CG2   . THR A 1 2580 ? 157.482 129.447 124.100 1.00 93.76  ? 3797 THR A CG2   1 
ATOM   15556 N  N     . PHE A 1 2581 ? 159.106 126.183 121.732 1.00 96.79  ? 3798 PHE A N     1 
ATOM   15557 C  CA    . PHE A 1 2581 ? 159.322 125.174 120.702 1.00 98.03  ? 3798 PHE A CA    1 
ATOM   15558 C  C     . PHE A 1 2581 ? 160.111 123.983 121.227 1.00 97.52  ? 3798 PHE A C     1 
ATOM   15559 O  O     . PHE A 1 2581 ? 160.002 122.891 120.661 1.00 99.96  ? 3798 PHE A O     1 
ATOM   15560 C  CB    . PHE A 1 2581 ? 160.027 125.772 119.480 1.00 98.82  ? 3798 PHE A CB    1 
ATOM   15561 C  CG    . PHE A 1 2581 ? 161.371 126.374 119.774 1.00 100.33 ? 3798 PHE A CG    1 
ATOM   15562 C  CD1   . PHE A 1 2581 ? 161.480 127.651 120.301 1.00 96.74  ? 3798 PHE A CD1   1 
ATOM   15563 C  CD2   . PHE A 1 2581 ? 162.529 125.660 119.513 1.00 100.58 ? 3798 PHE A CD2   1 
ATOM   15564 C  CE1   . PHE A 1 2581 ? 162.716 128.200 120.563 1.00 90.74  ? 3798 PHE A CE1   1 
ATOM   15565 C  CE2   . PHE A 1 2581 ? 163.767 126.205 119.776 1.00 96.32  ? 3798 PHE A CE2   1 
ATOM   15566 C  CZ    . PHE A 1 2581 ? 163.861 127.476 120.302 1.00 89.45  ? 3798 PHE A CZ    1 
ATOM   15567 N  N     . LYS A 1 2582 ? 160.892 124.162 122.296 1.00 94.02  ? 3799 LYS A N     1 
ATOM   15568 C  CA    . LYS A 1 2582 ? 161.489 123.010 122.963 1.00 97.53  ? 3799 LYS A CA    1 
ATOM   15569 C  C     . LYS A 1 2582 ? 160.411 122.099 123.535 1.00 99.94  ? 3799 LYS A C     1 
ATOM   15570 O  O     . LYS A 1 2582 ? 160.476 120.874 123.377 1.00 103.46 ? 3799 LYS A O     1 
ATOM   15571 C  CB    . LYS A 1 2582 ? 162.448 123.466 124.062 1.00 95.38  ? 3799 LYS A CB    1 
ATOM   15572 C  CG    . LYS A 1 2582 ? 162.794 122.386 125.085 1.00 94.57  ? 3799 LYS A CG    1 
ATOM   15573 C  CD    . LYS A 1 2582 ? 163.609 121.252 124.471 1.00 95.26  ? 3799 LYS A CD    1 
ATOM   15574 C  CE    . LYS A 1 2582 ? 165.069 121.637 124.301 1.00 94.89  ? 3799 LYS A CE    1 
ATOM   15575 N  NZ    . LYS A 1 2582 ? 165.849 120.578 123.602 1.00 93.59  ? 3799 LYS A NZ    1 
ATOM   15576 N  N     . LEU A 1 2583 ? 159.399 122.680 124.183 1.00 97.50  ? 3800 LEU A N     1 
ATOM   15577 C  CA    . LEU A 1 2583 ? 158.273 121.881 124.653 1.00 99.76  ? 3800 LEU A CA    1 
ATOM   15578 C  C     . LEU A 1 2583 ? 157.472 121.302 123.493 1.00 103.89 ? 3800 LEU A C     1 
ATOM   15579 O  O     . LEU A 1 2583 ? 156.917 120.205 123.617 1.00 107.18 ? 3800 LEU A O     1 
ATOM   15580 C  CB    . LEU A 1 2583 ? 157.371 122.714 125.562 1.00 95.16  ? 3800 LEU A CB    1 
ATOM   15581 C  CG    . LEU A 1 2583 ? 157.886 122.936 126.985 1.00 88.03  ? 3800 LEU A CG    1 
ATOM   15582 C  CD1   . LEU A 1 2583 ? 156.918 123.785 127.786 1.00 79.60  ? 3800 LEU A CD1   1 
ATOM   15583 C  CD2   . LEU A 1 2583 ? 158.121 121.604 127.673 1.00 91.94  ? 3800 LEU A CD2   1 
ATOM   15584 N  N     . ILE A 1 2584 ? 157.408 122.013 122.364 1.00 103.42 ? 3801 ILE A N     1 
ATOM   15585 C  CA    . ILE A 1 2584 ? 156.721 121.486 121.185 1.00 105.02 ? 3801 ILE A CA    1 
ATOM   15586 C  C     . ILE A 1 2584 ? 157.427 120.234 120.673 1.00 105.71 ? 3801 ILE A C     1 
ATOM   15587 O  O     . ILE A 1 2584 ? 156.792 119.208 120.394 1.00 110.48 ? 3801 ILE A O     1 
ATOM   15588 C  CB    . ILE A 1 2584 ? 156.623 122.569 120.095 1.00 103.98 ? 3801 ILE A CB    1 
ATOM   15589 C  CG1   . ILE A 1 2584 ? 155.570 123.614 120.475 1.00 101.24 ? 3801 ILE A CG1   1 
ATOM   15590 C  CG2   . ILE A 1 2584 ? 156.317 121.953 118.734 1.00 103.38 ? 3801 ILE A CG2   1 
ATOM   15591 C  CD1   . ILE A 1 2584 ? 154.143 123.144 120.300 1.00 104.25 ? 3801 ILE A CD1   1 
ATOM   15592 N  N     . GLU A 1 2585 ? 158.755 120.297 120.557 1.00 102.59 ? 3802 GLU A N     1 
ATOM   15593 C  CA    . GLU A 1 2585 ? 159.528 119.135 120.129 1.00 105.87 ? 3802 GLU A CA    1 
ATOM   15594 C  C     . GLU A 1 2585 ? 159.462 118.009 121.152 1.00 106.86 ? 3802 GLU A C     1 
ATOM   15595 O  O     . GLU A 1 2585 ? 159.448 116.832 120.776 1.00 109.97 ? 3802 GLU A O     1 
ATOM   15596 C  CB    . GLU A 1 2585 ? 160.981 119.533 119.873 1.00 105.25 ? 3802 GLU A CB    1 
ATOM   15597 N  N     . LEU A 1 2586 ? 159.427 118.352 122.442 1.00 104.53 ? 3803 LEU A N     1 
ATOM   15598 C  CA    . LEU A 1 2586 ? 159.284 117.341 123.484 1.00 106.29 ? 3803 LEU A CA    1 
ATOM   15599 C  C     . LEU A 1 2586 ? 157.950 116.614 123.375 1.00 111.19 ? 3803 LEU A C     1 
ATOM   15600 O  O     . LEU A 1 2586 ? 157.894 115.384 123.484 1.00 114.29 ? 3803 LEU A O     1 
ATOM   15601 C  CB    . LEU A 1 2586 ? 159.425 117.997 124.856 1.00 103.01 ? 3803 LEU A CB    1 
ATOM   15602 C  CG    . LEU A 1 2586 ? 159.148 117.123 126.077 1.00 101.89 ? 3803 LEU A CG    1 
ATOM   15603 C  CD1   . LEU A 1 2586 ? 160.176 116.008 126.180 1.00 104.39 ? 3803 LEU A CD1   1 
ATOM   15604 C  CD2   . LEU A 1 2586 ? 159.130 117.975 127.333 1.00 100.92 ? 3803 LEU A CD2   1 
ATOM   15605 N  N     . ALA A 1 2587 ? 156.864 117.360 123.157 1.00 109.69 ? 3804 ALA A N     1 
ATOM   15606 C  CA    . ALA A 1 2587 ? 155.550 116.745 123.016 1.00 111.11 ? 3804 ALA A CA    1 
ATOM   15607 C  C     . ALA A 1 2587 ? 155.439 115.942 121.727 1.00 112.15 ? 3804 ALA A C     1 
ATOM   15608 O  O     . ALA A 1 2587 ? 154.743 114.921 121.695 1.00 113.51 ? 3804 ALA A O     1 
ATOM   15609 C  CB    . ALA A 1 2587 ? 154.461 117.814 123.072 1.00 111.44 ? 3804 ALA A CB    1 
ATOM   15610 N  N     . LYS A 1 2588 ? 156.097 116.394 120.656 1.00 110.38 ? 3805 LYS A N     1 
ATOM   15611 C  CA    . LYS A 1 2588 ? 156.133 115.610 119.426 1.00 110.26 ? 3805 LYS A CA    1 
ATOM   15612 C  C     . LYS A 1 2588 ? 156.891 114.304 119.628 1.00 112.52 ? 3805 LYS A C     1 
ATOM   15613 O  O     . LYS A 1 2588 ? 156.479 113.254 119.120 1.00 115.66 ? 3805 LYS A O     1 
ATOM   15614 C  CB    . LYS A 1 2588 ? 156.761 116.429 118.299 1.00 110.38 ? 3805 LYS A CB    1 
ATOM   15615 N  N     . ALA A 1 2589 ? 158.005 114.349 120.364 1.00 111.83 ? 3806 ALA A N     1 
ATOM   15616 C  CA    . ALA A 1 2589 ? 158.761 113.134 120.641 1.00 111.94 ? 3806 ALA A CA    1 
ATOM   15617 C  C     . ALA A 1 2589 ? 158.030 112.223 121.619 1.00 114.53 ? 3806 ALA A C     1 
ATOM   15618 O  O     . ALA A 1 2589 ? 158.128 110.996 121.510 1.00 114.98 ? 3806 ALA A O     1 
ATOM   15619 C  CB    . ALA A 1 2589 ? 160.148 113.487 121.178 1.00 108.01 ? 3806 ALA A CB    1 
ATOM   15620 N  N     . SER A 1 2590 ? 157.299 112.795 122.572 1.00 113.54 ? 3807 SER A N     1 
ATOM   15621 C  CA    . SER A 1 2590 ? 156.564 112.017 123.559 1.00 114.38 ? 3807 SER A CA    1 
ATOM   15622 C  C     . SER A 1 2590 ? 155.135 111.709 123.131 1.00 115.23 ? 3807 SER A C     1 
ATOM   15623 O  O     . SER A 1 2590 ? 154.401 111.082 123.903 1.00 115.21 ? 3807 SER A O     1 
ATOM   15624 C  CB    . SER A 1 2590 ? 156.548 112.748 124.905 1.00 114.49 ? 3807 SER A CB    1 
ATOM   15625 O  OG    . SER A 1 2590 ? 157.857 112.869 125.434 1.00 112.40 ? 3807 SER A OG    1 
ATOM   15626 N  N     . LYS A 1 2591 ? 154.735 112.135 121.927 1.00 116.12 ? 3808 LYS A N     1 
ATOM   15627 C  CA    . LYS A 1 2591 ? 153.397 111.889 121.376 1.00 115.56 ? 3808 LYS A CA    1 
ATOM   15628 C  C     . LYS A 1 2591 ? 152.299 112.414 122.299 1.00 118.28 ? 3808 LYS A C     1 
ATOM   15629 O  O     . LYS A 1 2591 ? 151.259 111.778 122.483 1.00 122.03 ? 3808 LYS A O     1 
ATOM   15630 C  CB    . LYS A 1 2591 ? 153.187 110.404 121.066 1.00 111.23 ? 3808 LYS A CB    1 
ATOM   15631 N  N     . GLU A 1 2592 ? 152.531 113.584 122.885 1.00 117.61 ? 3809 GLU A N     1 
ATOM   15632 C  CA    . GLU A 1 2592 ? 151.583 114.212 123.791 1.00 117.64 ? 3809 GLU A CA    1 
ATOM   15633 C  C     . GLU A 1 2592 ? 150.996 115.462 123.149 1.00 116.53 ? 3809 GLU A C     1 
ATOM   15634 O  O     . GLU A 1 2592 ? 151.667 116.164 122.387 1.00 117.06 ? 3809 GLU A O     1 
ATOM   15635 C  CB    . GLU A 1 2592 ? 152.250 114.572 125.122 1.00 116.87 ? 3809 GLU A CB    1 
ATOM   15636 C  CG    . GLU A 1 2592 ? 152.697 113.368 125.936 1.00 115.65 ? 3809 GLU A CG    1 
ATOM   15637 C  CD    . GLU A 1 2592 ? 151.532 112.577 126.496 1.00 116.22 ? 3809 GLU A CD    1 
ATOM   15638 O  OE1   . GLU A 1 2592 ? 150.473 113.182 126.766 1.00 116.11 ? 3809 GLU A OE1   1 
ATOM   15639 O  OE2   . GLU A 1 2592 ? 151.675 111.348 126.666 1.00 113.46 ? 3809 GLU A OE2   1 
ATOM   15640 N  N     . SER A 1 2593 ? 149.732 115.732 123.463 1.00 116.21 ? 3810 SER A N     1 
ATOM   15641 C  CA    . SER A 1 2593 ? 149.008 116.857 122.882 1.00 118.23 ? 3810 SER A CA    1 
ATOM   15642 C  C     . SER A 1 2593 ? 149.362 118.124 123.651 1.00 117.21 ? 3810 SER A C     1 
ATOM   15643 O  O     . SER A 1 2593 ? 148.975 118.283 124.813 1.00 115.21 ? 3810 SER A O     1 
ATOM   15644 C  CB    . SER A 1 2593 ? 147.504 116.602 122.910 1.00 120.88 ? 3810 SER A CB    1 
ATOM   15645 O  OG    . SER A 1 2593 ? 146.967 116.873 124.192 1.00 126.26 ? 3810 SER A OG    1 
ATOM   15646 N  N     . LEU A 1 2594 ? 150.095 119.024 123.002 1.00 118.14 ? 3811 LEU A N     1 
ATOM   15647 C  CA    . LEU A 1 2594 ? 150.478 120.304 123.581 1.00 116.29 ? 3811 LEU A CA    1 
ATOM   15648 C  C     . LEU A 1 2594 ? 149.729 121.428 122.883 1.00 113.80 ? 3811 LEU A C     1 
ATOM   15649 O  O     . LEU A 1 2594 ? 149.701 121.491 121.650 1.00 112.92 ? 3811 LEU A O     1 
ATOM   15650 C  CB    . LEU A 1 2594 ? 151.985 120.536 123.466 1.00 115.31 ? 3811 LEU A CB    1 
ATOM   15651 C  CG    . LEU A 1 2594 ? 152.520 121.768 124.203 1.00 110.53 ? 3811 LEU A CG    1 
ATOM   15652 C  CD1   . LEU A 1 2594 ? 152.032 121.809 125.644 1.00 105.05 ? 3811 LEU A CD1   1 
ATOM   15653 C  CD2   . LEU A 1 2594 ? 154.036 121.817 124.143 1.00 108.19 ? 3811 LEU A CD2   1 
ATOM   15654 N  N     . LYS A 1 2595 ? 149.126 122.312 123.674 1.00 112.89 ? 3812 LYS A N     1 
ATOM   15655 C  CA    . LYS A 1 2595 ? 148.478 123.515 123.163 1.00 111.21 ? 3812 LYS A CA    1 
ATOM   15656 C  C     . LYS A 1 2595 ? 149.034 124.717 123.918 1.00 103.48 ? 3812 LYS A C     1 
ATOM   15657 O  O     . LYS A 1 2595 ? 148.894 124.812 125.141 1.00 101.80 ? 3812 LYS A O     1 
ATOM   15658 C  CB    . LYS A 1 2595 ? 146.953 123.414 123.276 1.00 111.58 ? 3812 LYS A CB    1 
ATOM   15659 C  CG    . LYS A 1 2595 ? 146.416 122.953 124.625 1.00 111.12 ? 3812 LYS A CG    1 
ATOM   15660 C  CD    . LYS A 1 2595 ? 144.912 122.752 124.560 1.00 111.43 ? 3812 LYS A CD    1 
ATOM   15661 C  CE    . LYS A 1 2595 ? 144.370 122.174 125.853 1.00 114.18 ? 3812 LYS A CE    1 
ATOM   15662 N  NZ    . LYS A 1 2595 ? 144.841 120.782 126.089 1.00 116.30 ? 3812 LYS A NZ    1 
ATOM   15663 N  N     . ILE A 1 2596 ? 149.686 125.617 123.191 1.00 99.72  ? 3813 ILE A N     1 
ATOM   15664 C  CA    . ILE A 1 2596 ? 150.318 126.779 123.802 1.00 96.93  ? 3813 ILE A CA    1 
ATOM   15665 C  C     . ILE A 1 2596 ? 149.247 127.807 124.147 1.00 95.17  ? 3813 ILE A C     1 
ATOM   15666 O  O     . ILE A 1 2596 ? 148.340 128.077 123.350 1.00 99.69  ? 3813 ILE A O     1 
ATOM   15667 C  CB    . ILE A 1 2596 ? 151.404 127.358 122.876 1.00 97.30  ? 3813 ILE A CB    1 
ATOM   15668 C  CG1   . ILE A 1 2596 ? 150.831 127.779 121.520 1.00 97.30  ? 3813 ILE A CG1   1 
ATOM   15669 C  CG2   . ILE A 1 2596 ? 152.515 126.341 122.666 1.00 95.74  ? 3813 ILE A CG2   1 
ATOM   15670 C  CD1   . ILE A 1 2596 ? 151.806 128.555 120.659 1.00 93.66  ? 3813 ILE A CD1   1 
ATOM   15671 N  N     . ILE A 1 2597 ? 149.316 128.343 125.358 1.00 90.04  ? 3814 ILE A N     1 
ATOM   15672 C  CA    . ILE A 1 2597 ? 148.345 129.306 125.855 1.00 92.94  ? 3814 ILE A CA    1 
ATOM   15673 C  C     . ILE A 1 2597 ? 149.095 130.545 126.329 1.00 89.47  ? 3814 ILE A C     1 
ATOM   15674 O  O     . ILE A 1 2597 ? 149.551 130.608 127.471 1.00 87.82  ? 3814 ILE A O     1 
ATOM   15675 C  CB    . ILE A 1 2597 ? 147.485 128.715 126.987 1.00 97.89  ? 3814 ILE A CB    1 
ATOM   15676 C  CG1   . ILE A 1 2597 ? 146.809 127.421 126.539 1.00 99.05  ? 3814 ILE A CG1   1 
ATOM   15677 C  CG2   . ILE A 1 2597 ? 146.432 129.715 127.428 1.00 102.13 ? 3814 ILE A CG2   1 
ATOM   15678 C  CD1   . ILE A 1 2597 ? 145.976 126.779 127.617 1.00 100.35 ? 3814 ILE A CD1   1 
ATOM   15679 N  N     . PRO A 1 2598 ? 149.265 131.544 125.467 1.00 92.23  ? 3815 PRO A N     1 
ATOM   15680 C  CA    . PRO A 1 2598 ? 149.774 132.835 125.938 1.00 92.45  ? 3815 PRO A CA    1 
ATOM   15681 C  C     . PRO A 1 2598 ? 148.781 133.502 126.875 1.00 90.83  ? 3815 PRO A C     1 
ATOM   15682 O  O     . PRO A 1 2598 ? 147.564 133.356 126.736 1.00 92.68  ? 3815 PRO A O     1 
ATOM   15683 C  CB    . PRO A 1 2598 ? 149.952 133.645 124.647 1.00 93.68  ? 3815 PRO A CB    1 
ATOM   15684 C  CG    . PRO A 1 2598 ? 149.970 132.629 123.545 1.00 94.62  ? 3815 PRO A CG    1 
ATOM   15685 C  CD    . PRO A 1 2598 ? 149.084 131.517 124.008 1.00 94.80  ? 3815 PRO A CD    1 
ATOM   15686 N  N     . LEU A 1 2599 ? 149.315 134.239 127.845 1.00 87.69  ? 3816 LEU A N     1 
ATOM   15687 C  CA    . LEU A 1 2599 ? 148.484 134.973 128.782 1.00 89.65  ? 3816 LEU A CA    1 
ATOM   15688 C  C     . LEU A 1 2599 ? 148.248 136.390 128.262 1.00 96.72  ? 3816 LEU A C     1 
ATOM   15689 O  O     . LEU A 1 2599 ? 148.708 136.768 127.182 1.00 100.11 ? 3816 LEU A O     1 
ATOM   15690 C  CB    . LEU A 1 2599 ? 149.118 134.980 130.172 1.00 84.99  ? 3816 LEU A CB    1 
ATOM   15691 C  CG    . LEU A 1 2599 ? 149.102 133.658 130.946 1.00 84.10  ? 3816 LEU A CG    1 
ATOM   15692 C  CD1   . LEU A 1 2599 ? 149.227 133.911 132.441 1.00 81.93  ? 3816 LEU A CD1   1 
ATOM   15693 C  CD2   . LEU A 1 2599 ? 147.846 132.852 130.645 1.00 88.08  ? 3816 LEU A CD2   1 
ATOM   15694 N  N     . GLY A 1 2600 ? 147.525 137.191 129.040 1.00 97.00  ? 3817 GLY A N     1 
ATOM   15695 C  CA    . GLY A 1 2600 ? 147.145 138.511 128.579 1.00 93.20  ? 3817 GLY A CA    1 
ATOM   15696 C  C     . GLY A 1 2600 ? 145.799 138.983 129.088 1.00 96.87  ? 3817 GLY A C     1 
ATOM   15697 O  O     . GLY A 1 2600 ? 145.581 139.068 130.301 1.00 98.86  ? 3817 GLY A O     1 
ATOM   15698 N  N     . SER A 1 2601 ? 144.894 139.303 128.164 1.00 100.94 ? 3818 SER A N     1 
ATOM   15699 C  CA    . SER A 1 2601 ? 143.608 139.894 128.500 1.00 106.69 ? 3818 SER A CA    1 
ATOM   15700 C  C     . SER A 1 2601 ? 142.728 138.911 129.275 1.00 111.67 ? 3818 SER A C     1 
ATOM   15701 O  O     . SER A 1 2601 ? 143.067 137.739 129.471 1.00 111.05 ? 3818 SER A O     1 
ATOM   15702 C  CB    . SER A 1 2601 ? 142.887 140.352 127.233 1.00 107.13 ? 3818 SER A CB    1 
ATOM   15703 O  OG    . SER A 1 2601 ? 142.507 139.244 126.436 1.00 106.80 ? 3818 SER A OG    1 
ATOM   15704 N  N     . ILE A 1 2602 ? 141.572 139.415 129.717 1.00 113.17 ? 3819 ILE A N     1 
ATOM   15705 C  CA    . ILE A 1 2602 ? 140.646 138.612 130.510 1.00 112.06 ? 3819 ILE A CA    1 
ATOM   15706 C  C     . ILE A 1 2602 ? 140.065 137.471 129.685 1.00 115.30 ? 3819 ILE A C     1 
ATOM   15707 O  O     . ILE A 1 2602 ? 139.801 136.385 130.217 1.00 115.75 ? 3819 ILE A O     1 
ATOM   15708 C  CB    . ILE A 1 2602 ? 139.535 139.502 131.095 1.00 109.15 ? 3819 ILE A CB    1 
ATOM   15709 N  N     . GLU A 1 2603 ? 139.837 137.697 128.388 1.00 115.75 ? 3820 GLU A N     1 
ATOM   15710 C  CA    . GLU A 1 2603 ? 139.390 136.617 127.515 1.00 114.38 ? 3820 GLU A CA    1 
ATOM   15711 C  C     . GLU A 1 2603 ? 140.442 135.519 127.421 1.00 116.34 ? 3820 GLU A C     1 
ATOM   15712 O  O     . GLU A 1 2603 ? 140.108 134.328 127.408 1.00 115.52 ? 3820 GLU A O     1 
ATOM   15713 C  CB    . GLU A 1 2603 ? 139.058 137.165 126.128 1.00 107.83 ? 3820 GLU A CB    1 
ATOM   15714 N  N     . ASN A 1 2604 ? 141.720 135.904 127.361 1.00 117.47 ? 3821 ASN A N     1 
ATOM   15715 C  CA    . ASN A 1 2604 ? 142.797 134.919 127.373 1.00 114.74 ? 3821 ASN A CA    1 
ATOM   15716 C  C     . ASN A 1 2604 ? 142.824 134.148 128.687 1.00 114.17 ? 3821 ASN A C     1 
ATOM   15717 O  O     . ASN A 1 2604 ? 143.081 132.940 128.698 1.00 115.08 ? 3821 ASN A O     1 
ATOM   15718 C  CB    . ASN A 1 2604 ? 144.139 135.604 127.125 1.00 109.97 ? 3821 ASN A CB    1 
ATOM   15719 C  CG    . ASN A 1 2604 ? 144.404 135.851 125.653 1.00 107.84 ? 3821 ASN A CG    1 
ATOM   15720 O  OD1   . ASN A 1 2604 ? 143.778 135.240 124.787 1.00 110.31 ? 3821 ASN A OD1   1 
ATOM   15721 N  ND2   . ASN A 1 2604 ? 145.335 136.752 125.362 1.00 102.96 ? 3821 ASN A ND2   1 
ATOM   15722 N  N     . LEU A 1 2605 ? 142.564 134.830 129.806 1.00 113.65 ? 3822 LEU A N     1 
ATOM   15723 C  CA    . LEU A 1 2605 ? 142.515 134.152 131.099 1.00 115.89 ? 3822 LEU A CA    1 
ATOM   15724 C  C     . LEU A 1 2605 ? 141.362 133.155 131.165 1.00 119.19 ? 3822 LEU A C     1 
ATOM   15725 O  O     . LEU A 1 2605 ? 141.526 132.042 131.680 1.00 119.39 ? 3822 LEU A O     1 
ATOM   15726 C  CB    . LEU A 1 2605 ? 142.403 135.179 132.224 1.00 110.04 ? 3822 LEU A CB    1 
ATOM   15727 C  CG    . LEU A 1 2605 ? 143.567 136.164 132.351 1.00 105.58 ? 3822 LEU A CG    1 
ATOM   15728 C  CD1   . LEU A 1 2605 ? 143.378 137.066 133.558 1.00 107.85 ? 3822 LEU A CD1   1 
ATOM   15729 C  CD2   . LEU A 1 2605 ? 144.890 135.422 132.437 1.00 102.92 ? 3822 LEU A CD2   1 
ATOM   15730 N  N     . ASN A 1 2606 ? 140.189 133.537 130.651 1.00 117.94 ? 3823 ASN A N     1 
ATOM   15731 C  CA    . ASN A 1 2606 ? 139.055 132.617 130.624 1.00 119.58 ? 3823 ASN A CA    1 
ATOM   15732 C  C     . ASN A 1 2606 ? 139.328 131.428 129.710 1.00 120.91 ? 3823 ASN A C     1 
ATOM   15733 O  O     . ASN A 1 2606 ? 138.959 130.291 130.032 1.00 122.20 ? 3823 ASN A O     1 
ATOM   15734 C  CB    . ASN A 1 2606 ? 137.791 133.355 130.184 1.00 119.99 ? 3823 ASN A CB    1 
ATOM   15735 N  N     . TYR A 1 2607 ? 139.971 131.675 128.565 1.00 120.07 ? 3824 TYR A N     1 
ATOM   15736 C  CA    . TYR A 1 2607 ? 140.356 130.589 127.669 1.00 120.67 ? 3824 TYR A CA    1 
ATOM   15737 C  C     . TYR A 1 2607 ? 141.341 129.642 128.343 1.00 120.45 ? 3824 TYR A C     1 
ATOM   15738 O  O     . TYR A 1 2607 ? 141.225 128.418 128.213 1.00 118.76 ? 3824 TYR A O     1 
ATOM   15739 C  CB    . TYR A 1 2607 ? 140.960 131.165 126.388 1.00 120.80 ? 3824 TYR A CB    1 
ATOM   15740 C  CG    . TYR A 1 2607 ? 141.416 130.122 125.396 1.00 122.02 ? 3824 TYR A CG    1 
ATOM   15741 C  CD1   . TYR A 1 2607 ? 140.515 129.224 124.839 1.00 121.16 ? 3824 TYR A CD1   1 
ATOM   15742 C  CD2   . TYR A 1 2607 ? 142.749 130.033 125.018 1.00 121.28 ? 3824 TYR A CD2   1 
ATOM   15743 C  CE1   . TYR A 1 2607 ? 140.928 128.270 123.930 1.00 120.48 ? 3824 TYR A CE1   1 
ATOM   15744 C  CE2   . TYR A 1 2607 ? 143.172 129.081 124.112 1.00 119.64 ? 3824 TYR A CE2   1 
ATOM   15745 C  CZ    . TYR A 1 2607 ? 142.258 128.202 123.572 1.00 119.88 ? 3824 TYR A CZ    1 
ATOM   15746 O  OH    . TYR A 1 2607 ? 142.676 127.252 122.668 1.00 117.44 ? 3824 TYR A OH    1 
ATOM   15747 N  N     . ALA A 1 2608 ? 142.314 130.196 129.072 1.00 121.88 ? 3825 ALA A N     1 
ATOM   15748 C  CA    . ALA A 1 2608 ? 143.272 129.369 129.797 1.00 120.75 ? 3825 ALA A CA    1 
ATOM   15749 C  C     . ALA A 1 2608 ? 142.581 128.538 130.869 1.00 120.52 ? 3825 ALA A C     1 
ATOM   15750 O  O     . ALA A 1 2608 ? 142.899 127.358 131.045 1.00 123.13 ? 3825 ALA A O     1 
ATOM   15751 C  CB    . ALA A 1 2608 ? 144.358 130.246 130.419 1.00 113.93 ? 3825 ALA A CB    1 
ATOM   15752 N  N     . GLN A 1 2609 ? 141.632 129.140 131.591 1.00 117.86 ? 3826 GLN A N     1 
ATOM   15753 C  CA    . GLN A 1 2609 ? 140.894 128.406 132.615 1.00 120.51 ? 3826 GLN A CA    1 
ATOM   15754 C  C     . GLN A 1 2609 ? 140.087 127.265 132.007 1.00 122.66 ? 3826 GLN A C     1 
ATOM   15755 O  O     . GLN A 1 2609 ? 140.100 126.138 132.522 1.00 122.45 ? 3826 GLN A O     1 
ATOM   15756 C  CB    . GLN A 1 2609 ? 139.977 129.360 133.381 1.00 119.59 ? 3826 GLN A CB    1 
ATOM   15757 N  N     . GLU A 1 2610 ? 139.395 127.533 130.895 1.00 122.66 ? 3827 GLU A N     1 
ATOM   15758 C  CA    . GLU A 1 2610 ? 138.612 126.492 130.238 1.00 120.87 ? 3827 GLU A CA    1 
ATOM   15759 C  C     . GLU A 1 2610 ? 139.504 125.372 129.718 1.00 122.21 ? 3827 GLU A C     1 
ATOM   15760 O  O     . GLU A 1 2610 ? 139.169 124.188 129.849 1.00 123.66 ? 3827 GLU A O     1 
ATOM   15761 C  CB    . GLU A 1 2610 ? 137.788 127.094 129.100 1.00 116.21 ? 3827 GLU A CB    1 
ATOM   15762 N  N     . GLU A 1 2611 ? 140.659 125.722 129.147 1.00 120.98 ? 3828 GLU A N     1 
ATOM   15763 C  CA    . GLU A 1 2611 ? 141.529 124.692 128.594 1.00 118.25 ? 3828 GLU A CA    1 
ATOM   15764 C  C     . GLU A 1 2611 ? 142.215 123.874 129.681 1.00 117.66 ? 3828 GLU A C     1 
ATOM   15765 O  O     . GLU A 1 2611 ? 142.413 122.669 129.503 1.00 120.33 ? 3828 GLU A O     1 
ATOM   15766 C  CB    . GLU A 1 2611 ? 142.564 125.311 127.654 1.00 117.17 ? 3828 GLU A CB    1 
ATOM   15767 C  CG    . GLU A 1 2611 ? 141.990 125.869 126.349 1.00 118.49 ? 3828 GLU A CG    1 
ATOM   15768 C  CD    . GLU A 1 2611 ? 141.705 124.808 125.287 1.00 118.81 ? 3828 GLU A CD    1 
ATOM   15769 O  OE1   . GLU A 1 2611 ? 141.487 123.627 125.630 1.00 118.38 ? 3828 GLU A OE1   1 
ATOM   15770 O  OE2   . GLU A 1 2611 ? 141.702 125.164 124.090 1.00 116.81 ? 3828 GLU A OE2   1 
ATOM   15771 N  N     . ILE A 1 2612 ? 142.573 124.486 130.815 1.00 116.27 ? 3829 ILE A N     1 
ATOM   15772 C  CA    . ILE A 1 2612 ? 143.168 123.674 131.873 1.00 118.31 ? 3829 ILE A CA    1 
ATOM   15773 C  C     . ILE A 1 2612 ? 142.102 122.826 132.554 1.00 123.19 ? 3829 ILE A C     1 
ATOM   15774 O  O     . ILE A 1 2612 ? 142.399 121.729 133.038 1.00 124.26 ? 3829 ILE A O     1 
ATOM   15775 C  CB    . ILE A 1 2612 ? 143.951 124.526 132.893 1.00 114.14 ? 3829 ILE A CB    1 
ATOM   15776 C  CG1   . ILE A 1 2612 ? 143.044 125.511 133.629 1.00 116.07 ? 3829 ILE A CG1   1 
ATOM   15777 C  CG2   . ILE A 1 2612 ? 145.105 125.247 132.213 1.00 114.58 ? 3829 ILE A CG2   1 
ATOM   15778 C  CD1   . ILE A 1 2612 ? 143.723 126.196 134.791 1.00 115.27 ? 3829 ILE A CD1   1 
ATOM   15779 N  N     . SER A 1 2613 ? 140.846 123.287 132.581 1.00 123.26 ? 3830 SER A N     1 
ATOM   15780 C  CA    . SER A 1 2613 ? 139.765 122.418 133.038 1.00 124.23 ? 3830 SER A CA    1 
ATOM   15781 C  C     . SER A 1 2613 ? 139.590 121.222 132.106 1.00 123.90 ? 3830 SER A C     1 
ATOM   15782 O  O     . SER A 1 2613 ? 139.429 120.083 132.563 1.00 124.49 ? 3830 SER A O     1 
ATOM   15783 C  CB    . SER A 1 2613 ? 138.463 123.211 133.147 1.00 125.73 ? 3830 SER A CB    1 
ATOM   15784 N  N     . LYS A 1 2614 ? 139.644 121.462 130.793 1.00 123.71 ? 3831 LYS A N     1 
ATOM   15785 C  CA    . LYS A 1 2614 ? 139.533 120.370 129.830 1.00 124.98 ? 3831 LYS A CA    1 
ATOM   15786 C  C     . LYS A 1 2614 ? 140.704 119.400 129.949 1.00 125.46 ? 3831 LYS A C     1 
ATOM   15787 O  O     . LYS A 1 2614 ? 140.529 118.183 129.813 1.00 127.80 ? 3831 LYS A O     1 
ATOM   15788 C  CB    . LYS A 1 2614 ? 139.442 120.929 128.411 1.00 124.47 ? 3831 LYS A CB    1 
ATOM   15789 N  N     . SER A 1 2615 ? 141.909 119.919 130.195 1.00 121.42 ? 3832 SER A N     1 
ATOM   15790 C  CA    . SER A 1 2615 ? 143.075 119.053 130.332 1.00 120.94 ? 3832 SER A CA    1 
ATOM   15791 C  C     . SER A 1 2615 ? 143.085 118.317 131.666 1.00 123.82 ? 3832 SER A C     1 
ATOM   15792 O  O     . SER A 1 2615 ? 143.676 117.239 131.771 1.00 125.25 ? 3832 SER A O     1 
ATOM   15793 C  CB    . SER A 1 2615 ? 144.354 119.867 130.160 1.00 117.84 ? 3832 SER A CB    1 
ATOM   15794 O  OG    . SER A 1 2615 ? 144.288 120.650 128.981 1.00 117.26 ? 3832 SER A OG    1 
ATOM   15795 N  N     . LYS A 1 2616 ? 142.460 118.884 132.698 1.00 122.57 ? 3833 LYS A N     1 
ATOM   15796 C  CA    . LYS A 1 2616 ? 142.244 118.120 133.920 1.00 123.19 ? 3833 LYS A CA    1 
ATOM   15797 C  C     . LYS A 1 2616 ? 141.186 117.048 133.712 1.00 126.90 ? 3833 LYS A C     1 
ATOM   15798 O  O     . LYS A 1 2616 ? 141.206 116.013 134.389 1.00 126.27 ? 3833 LYS A O     1 
ATOM   15799 C  CB    . LYS A 1 2616 ? 141.845 119.055 135.062 1.00 120.78 ? 3833 LYS A CB    1 
ATOM   15800 C  CG    . LYS A 1 2616 ? 142.077 118.484 136.454 1.00 120.89 ? 3833 LYS A CG    1 
ATOM   15801 C  CD    . LYS A 1 2616 ? 143.473 117.898 136.597 1.00 122.24 ? 3833 LYS A CD    1 
ATOM   15802 C  CE    . LYS A 1 2616 ? 143.683 117.314 137.986 1.00 125.31 ? 3833 LYS A CE    1 
ATOM   15803 N  NZ    . LYS A 1 2616 ? 145.002 116.637 138.119 1.00 121.43 ? 3833 LYS A NZ    1 
ATOM   15804 N  N     . ILE A 1 2617 ? 140.258 117.278 132.784 1.00 127.50 ? 3834 ILE A N     1 
ATOM   15805 C  CA    . ILE A 1 2617 ? 139.222 116.290 132.496 1.00 124.68 ? 3834 ILE A CA    1 
ATOM   15806 C  C     . ILE A 1 2617 ? 139.794 115.111 131.716 1.00 125.69 ? 3834 ILE A C     1 
ATOM   15807 O  O     . ILE A 1 2617 ? 139.724 113.960 132.160 1.00 128.08 ? 3834 ILE A O     1 
ATOM   15808 C  CB    . ILE A 1 2617 ? 138.051 116.945 131.742 1.00 124.62 ? 3834 ILE A CB    1 
ATOM   15809 N  N     . GLU A 1 2618 ? 140.368 115.378 130.541 1.00 125.88 ? 3835 GLU A N     1 
ATOM   15810 C  CA    . GLU A 1 2618 ? 140.742 114.322 129.605 1.00 127.09 ? 3835 GLU A CA    1 
ATOM   15811 C  C     . GLU A 1 2618 ? 142.248 114.154 129.437 1.00 126.01 ? 3835 GLU A C     1 
ATOM   15812 O  O     . GLU A 1 2618 ? 142.679 113.427 128.536 1.00 125.12 ? 3835 GLU A O     1 
ATOM   15813 C  CB    . GLU A 1 2618 ? 140.097 114.577 128.239 1.00 129.00 ? 3835 GLU A CB    1 
ATOM   15814 C  CG    . GLU A 1 2618 ? 140.554 115.858 127.555 1.00 128.54 ? 3835 GLU A CG    1 
ATOM   15815 C  CD    . GLU A 1 2618 ? 141.649 115.622 126.531 1.00 131.12 ? 3835 GLU A CD    1 
ATOM   15816 O  OE1   . GLU A 1 2618 ? 141.740 114.493 126.003 1.00 133.29 ? 3835 GLU A OE1   1 
ATOM   15817 O  OE2   . GLU A 1 2618 ? 142.422 116.563 126.257 1.00 128.56 ? 3835 GLU A OE2   1 
ATOM   15818 N  N     . GLY A 1 2619 ? 143.060 114.793 130.273 1.00 125.93 ? 3836 GLY A N     1 
ATOM   15819 C  CA    . GLY A 1 2619 ? 144.498 114.694 130.127 1.00 126.66 ? 3836 GLY A CA    1 
ATOM   15820 C  C     . GLY A 1 2619 ? 145.037 115.660 129.088 1.00 125.97 ? 3836 GLY A C     1 
ATOM   15821 O  O     . GLY A 1 2619 ? 144.323 116.486 128.517 1.00 125.63 ? 3836 GLY A O     1 
ATOM   15822 N  N     . GLY A 1 2620 ? 146.335 115.546 128.842 1.00 124.68 ? 3837 GLY A N     1 
ATOM   15823 C  CA    . GLY A 1 2620 ? 147.023 116.373 127.873 1.00 121.16 ? 3837 GLY A CA    1 
ATOM   15824 C  C     . GLY A 1 2620 ? 148.122 117.200 128.512 1.00 120.05 ? 3837 GLY A C     1 
ATOM   15825 O  O     . GLY A 1 2620 ? 148.443 117.061 129.691 1.00 119.13 ? 3837 GLY A O     1 
ATOM   15826 N  N     . TRP A 1 2621 ? 148.702 118.075 127.694 1.00 118.02 ? 3838 TRP A N     1 
ATOM   15827 C  CA    . TRP A 1 2621 ? 149.769 118.965 128.124 1.00 113.05 ? 3838 TRP A CA    1 
ATOM   15828 C  C     . TRP A 1 2621 ? 149.334 120.415 127.953 1.00 110.02 ? 3838 TRP A C     1 
ATOM   15829 O  O     . TRP A 1 2621 ? 148.666 120.770 126.978 1.00 111.32 ? 3838 TRP A O     1 
ATOM   15830 C  CB    . TRP A 1 2621 ? 151.061 118.706 127.338 1.00 112.64 ? 3838 TRP A CB    1 
ATOM   15831 C  CG    . TRP A 1 2621 ? 151.875 117.565 127.873 1.00 112.29 ? 3838 TRP A CG    1 
ATOM   15832 C  CD1   . TRP A 1 2621 ? 151.468 116.616 128.766 1.00 112.49 ? 3838 TRP A CD1   1 
ATOM   15833 C  CD2   . TRP A 1 2621 ? 153.236 117.255 127.551 1.00 111.40 ? 3838 TRP A CD2   1 
ATOM   15834 N  NE1   . TRP A 1 2621 ? 152.491 115.734 129.017 1.00 113.47 ? 3838 TRP A NE1   1 
ATOM   15835 C  CE2   . TRP A 1 2621 ? 153.587 116.105 128.285 1.00 113.47 ? 3838 TRP A CE2   1 
ATOM   15836 C  CE3   . TRP A 1 2621 ? 154.191 117.839 126.714 1.00 108.62 ? 3838 TRP A CE3   1 
ATOM   15837 C  CZ2   . TRP A 1 2621 ? 154.852 115.527 128.206 1.00 113.46 ? 3838 TRP A CZ2   1 
ATOM   15838 C  CZ3   . TRP A 1 2621 ? 155.446 117.263 126.637 1.00 109.97 ? 3838 TRP A CZ3   1 
ATOM   15839 C  CH2   . TRP A 1 2621 ? 155.765 116.120 127.379 1.00 112.57 ? 3838 TRP A CH2   1 
ATOM   15840 N  N     . ILE A 1 2622 ? 149.721 121.252 128.915 1.00 105.46 ? 3839 ILE A N     1 
ATOM   15841 C  CA    . ILE A 1 2622 ? 149.336 122.658 128.951 1.00 102.99 ? 3839 ILE A CA    1 
ATOM   15842 C  C     . ILE A 1 2622 ? 150.590 123.500 129.134 1.00 96.62  ? 3839 ILE A C     1 
ATOM   15843 O  O     . ILE A 1 2622 ? 151.380 123.253 130.051 1.00 96.13  ? 3839 ILE A O     1 
ATOM   15844 C  CB    . ILE A 1 2622 ? 148.328 122.941 130.082 1.00 103.91 ? 3839 ILE A CB    1 
ATOM   15845 C  CG1   . ILE A 1 2622 ? 146.942 122.422 129.711 1.00 107.60 ? 3839 ILE A CG1   1 
ATOM   15846 C  CG2   . ILE A 1 2622 ? 148.274 124.430 130.408 1.00 100.18 ? 3839 ILE A CG2   1 
ATOM   15847 C  CD1   . ILE A 1 2622 ? 146.221 123.289 128.721 1.00 110.28 ? 3839 ILE A CD1   1 
ATOM   15848 N  N     . LEU A 1 2623 ? 150.771 124.492 128.267 1.00 91.78  ? 3840 LEU A N     1 
ATOM   15849 C  CA    . LEU A 1 2623 ? 151.843 125.467 128.403 1.00 81.09  ? 3840 LEU A CA    1 
ATOM   15850 C  C     . LEU A 1 2623 ? 151.235 126.854 128.548 1.00 81.36  ? 3840 LEU A C     1 
ATOM   15851 O  O     . LEU A 1 2623 ? 150.414 127.265 127.722 1.00 86.92  ? 3840 LEU A O     1 
ATOM   15852 C  CB    . LEU A 1 2623 ? 152.789 125.425 127.201 1.00 86.74  ? 3840 LEU A CB    1 
ATOM   15853 C  CG    . LEU A 1 2623 ? 153.747 126.609 127.061 1.00 82.84  ? 3840 LEU A CG    1 
ATOM   15854 C  CD1   . LEU A 1 2623 ? 154.674 126.686 128.258 1.00 80.08  ? 3840 LEU A CD1   1 
ATOM   15855 C  CD2   . LEU A 1 2623 ? 154.546 126.511 125.774 1.00 85.54  ? 3840 LEU A CD2   1 
ATOM   15856 N  N     . LEU A 1 2624 ? 151.641 127.570 129.592 1.00 78.90  ? 3841 LEU A N     1 
ATOM   15857 C  CA    . LEU A 1 2624 ? 151.235 128.955 129.814 1.00 79.58  ? 3841 LEU A CA    1 
ATOM   15858 C  C     . LEU A 1 2624 ? 152.445 129.837 129.526 1.00 74.02  ? 3841 LEU A C     1 
ATOM   15859 O  O     . LEU A 1 2624 ? 153.318 130.009 130.381 1.00 70.59  ? 3841 LEU A O     1 
ATOM   15860 C  CB    . LEU A 1 2624 ? 150.716 129.164 131.233 1.00 74.71  ? 3841 LEU A CB    1 
ATOM   15861 C  CG    . LEU A 1 2624 ? 149.421 128.458 131.637 1.00 73.04  ? 3841 LEU A CG    1 
ATOM   15862 C  CD1   . LEU A 1 2624 ? 149.720 127.193 132.415 1.00 75.64  ? 3841 LEU A CD1   1 
ATOM   15863 C  CD2   . LEU A 1 2624 ? 148.540 129.388 132.452 1.00 80.39  ? 3841 LEU A CD2   1 
ATOM   15864 N  N     . GLN A 1 2625 ? 152.497 130.386 128.316 1.00 78.69  ? 3842 GLN A N     1 
ATOM   15865 C  CA    . GLN A 1 2625 ? 153.611 131.237 127.925 1.00 75.96  ? 3842 GLN A CA    1 
ATOM   15866 C  C     . GLN A 1 2625 ? 153.543 132.567 128.663 1.00 75.71  ? 3842 GLN A C     1 
ATOM   15867 O  O     . GLN A 1 2625 ? 152.494 133.218 128.684 1.00 84.56  ? 3842 GLN A O     1 
ATOM   15868 C  CB    . GLN A 1 2625 ? 153.588 131.478 126.418 1.00 79.68  ? 3842 GLN A CB    1 
ATOM   15869 C  CG    . GLN A 1 2625 ? 154.115 130.329 125.584 1.00 80.21  ? 3842 GLN A CG    1 
ATOM   15870 C  CD    . GLN A 1 2625 ? 154.193 130.679 124.113 1.00 83.61  ? 3842 GLN A CD    1 
ATOM   15871 O  OE1   . GLN A 1 2625 ? 153.794 129.894 123.254 1.00 86.62  ? 3842 GLN A OE1   1 
ATOM   15872 N  NE2   . GLN A 1 2625 ? 154.707 131.866 123.815 1.00 83.90  ? 3842 GLN A NE2   1 
ATOM   15873 N  N     . ASN A 1 2626 ? 154.668 132.965 129.262 1.00 69.13  ? 3843 ASN A N     1 
ATOM   15874 C  CA    . ASN A 1 2626 ? 154.839 134.274 129.897 1.00 69.84  ? 3843 ASN A CA    1 
ATOM   15875 C  C     . ASN A 1 2626 ? 153.795 134.497 130.997 1.00 70.19  ? 3843 ASN A C     1 
ATOM   15876 O  O     . ASN A 1 2626 ? 152.907 135.342 130.896 1.00 73.78  ? 3843 ASN A O     1 
ATOM   15877 C  CB    . ASN A 1 2626 ? 154.793 135.398 128.854 1.00 68.54  ? 3843 ASN A CB    1 
ATOM   15878 C  CG    . ASN A 1 2626 ? 156.160 135.723 128.290 1.00 63.32  ? 3843 ASN A CG    1 
ATOM   15879 O  OD1   . ASN A 1 2626 ? 157.170 135.624 128.985 1.00 63.11  ? 3843 ASN A OD1   1 
ATOM   15880 N  ND2   . ASN A 1 2626 ? 156.199 136.118 127.022 1.00 59.28  ? 3843 ASN A ND2   1 
ATOM   15881 N  N     . ILE A 1 2627 ? 153.928 133.705 132.061 1.00 68.86  ? 3844 ILE A N     1 
ATOM   15882 C  CA    . ILE A 1 2627 ? 153.033 133.809 133.212 1.00 72.48  ? 3844 ILE A CA    1 
ATOM   15883 C  C     . ILE A 1 2627 ? 153.318 135.084 133.998 1.00 71.34  ? 3844 ILE A C     1 
ATOM   15884 O  O     . ILE A 1 2627 ? 152.622 135.393 134.972 1.00 77.77  ? 3844 ILE A O     1 
ATOM   15885 C  CB    . ILE A 1 2627 ? 153.142 132.574 134.125 1.00 74.38  ? 3844 ILE A CB    1 
ATOM   15886 C  CG1   . ILE A 1 2627 ? 154.553 132.450 134.696 1.00 67.81  ? 3844 ILE A CG1   1 
ATOM   15887 C  CG2   . ILE A 1 2627 ? 152.767 131.317 133.369 1.00 76.47  ? 3844 ILE A CG2   1 
ATOM   15888 C  CD1   . ILE A 1 2627 ? 154.678 131.400 135.773 1.00 66.11  ? 3844 ILE A CD1   1 
ATOM   15889 N  N     . GLN A 1 2628 ? 154.350 135.827 133.590 1.00 65.47  ? 3845 GLN A N     1 
ATOM   15890 C  CA    . GLN A 1 2628 ? 154.615 137.139 134.163 1.00 67.41  ? 3845 GLN A CA    1 
ATOM   15891 C  C     . GLN A 1 2628 ? 153.539 138.160 133.809 1.00 71.50  ? 3845 GLN A C     1 
ATOM   15892 O  O     . GLN A 1 2628 ? 153.438 139.187 134.488 1.00 72.51  ? 3845 GLN A O     1 
ATOM   15893 C  CB    . GLN A 1 2628 ? 155.978 137.649 133.688 1.00 65.94  ? 3845 GLN A CB    1 
ATOM   15894 C  CG    . GLN A 1 2628 ? 157.144 136.726 133.997 1.00 64.40  ? 3845 GLN A CG    1 
ATOM   15895 C  CD    . GLN A 1 2628 ? 157.488 136.689 135.470 1.00 66.44  ? 3845 GLN A CD    1 
ATOM   15896 O  OE1   . GLN A 1 2628 ? 157.791 135.634 136.022 1.00 68.24  ? 3845 GLN A OE1   1 
ATOM   15897 N  NE2   . GLN A 1 2628 ? 157.451 137.848 136.114 1.00 71.17  ? 3845 GLN A NE2   1 
ATOM   15898 N  N     . MET A 1 2629 ? 152.744 137.906 132.764 1.00 70.41  ? 3846 MET A N     1 
ATOM   15899 C  CA    . MET A 1 2629 ? 151.756 138.862 132.273 1.00 65.12  ? 3846 MET A CA    1 
ATOM   15900 C  C     . MET A 1 2629 ? 150.700 139.189 133.321 1.00 71.99  ? 3846 MET A C     1 
ATOM   15901 O  O     . MET A 1 2629 ? 150.632 140.319 133.812 1.00 72.49  ? 3846 MET A O     1 
ATOM   15902 C  CB    . MET A 1 2629 ? 151.066 138.318 131.018 1.00 65.36  ? 3846 MET A CB    1 
ATOM   15903 C  CG    . MET A 1 2629 ? 151.941 138.227 129.780 1.00 64.85  ? 3846 MET A CG    1 
ATOM   15904 S  SD    . MET A 1 2629 ? 152.946 139.690 129.494 1.00 50.16  ? 3846 MET A SD    1 
ATOM   15905 C  CE    . MET A 1 2629 ? 152.877 139.799 127.708 1.00 45.71  ? 3846 MET A CE    1 
ATOM   15906 N  N     . SER A 1 2630 ? 149.880 138.202 133.675 1.00 82.69  ? 3847 SER A N     1 
ATOM   15907 C  CA    . SER A 1 2630 ? 148.822 138.380 134.667 1.00 91.55  ? 3847 SER A CA    1 
ATOM   15908 C  C     . SER A 1 2630 ? 149.304 137.779 135.983 1.00 96.57  ? 3847 SER A C     1 
ATOM   15909 O  O     . SER A 1 2630 ? 148.944 136.665 136.359 1.00 102.72 ? 3847 SER A O     1 
ATOM   15910 C  CB    . SER A 1 2630 ? 147.524 137.742 134.185 1.00 95.53  ? 3847 SER A CB    1 
ATOM   15911 O  OG    . SER A 1 2630 ? 147.578 136.330 134.302 1.00 95.04  ? 3847 SER A OG    1 
ATOM   15912 N  N     . LEU A 1 2631 ? 150.140 138.545 136.689 1.00 94.18  ? 3848 LEU A N     1 
ATOM   15913 C  CA    . LEU A 1 2631 ? 150.776 138.039 137.903 1.00 101.81 ? 3848 LEU A CA    1 
ATOM   15914 C  C     . LEU A 1 2631 ? 149.755 137.777 139.004 1.00 108.45 ? 3848 LEU A C     1 
ATOM   15915 O  O     . LEU A 1 2631 ? 149.776 136.718 139.642 1.00 108.71 ? 3848 LEU A O     1 
ATOM   15916 C  CB    . LEU A 1 2631 ? 151.841 139.025 138.382 1.00 101.54 ? 3848 LEU A CB    1 
ATOM   15917 C  CG    . LEU A 1 2631 ? 152.973 138.435 139.223 1.00 99.86  ? 3848 LEU A CG    1 
ATOM   15918 C  CD1   . LEU A 1 2631 ? 153.772 137.423 138.417 1.00 93.83  ? 3848 LEU A CD1   1 
ATOM   15919 C  CD2   . LEU A 1 2631 ? 153.871 139.537 139.754 1.00 95.50  ? 3848 LEU A CD2   1 
ATOM   15920 N  N     . SER A 1 2632 ? 148.851 138.731 139.240 1.00 109.68 ? 3849 SER A N     1 
ATOM   15921 C  CA    . SER A 1 2632 ? 147.832 138.550 140.270 1.00 111.88 ? 3849 SER A CA    1 
ATOM   15922 C  C     . SER A 1 2632 ? 146.865 137.431 139.902 1.00 111.53 ? 3849 SER A C     1 
ATOM   15923 O  O     . SER A 1 2632 ? 146.450 136.650 140.769 1.00 114.79 ? 3849 SER A O     1 
ATOM   15924 C  CB    . SER A 1 2632 ? 147.078 139.860 140.495 1.00 116.05 ? 3849 SER A CB    1 
ATOM   15925 O  OG    . SER A 1 2632 ? 147.967 140.907 140.848 1.00 114.27 ? 3849 SER A OG    1 
ATOM   15926 N  N     . TRP A 1 2633 ? 146.500 137.338 138.621 1.00 108.76 ? 3850 TRP A N     1 
ATOM   15927 C  CA    . TRP A 1 2633 ? 145.622 136.263 138.175 1.00 112.08 ? 3850 TRP A CA    1 
ATOM   15928 C  C     . TRP A 1 2633 ? 146.278 134.902 138.365 1.00 116.62 ? 3850 TRP A C     1 
ATOM   15929 O  O     . TRP A 1 2633 ? 145.613 133.937 138.753 1.00 118.29 ? 3850 TRP A O     1 
ATOM   15930 C  CB    . TRP A 1 2633 ? 145.232 136.471 136.713 1.00 110.20 ? 3850 TRP A CB    1 
ATOM   15931 N  N     . VAL A 1 2634 ? 147.584 134.807 138.098 1.00 117.34 ? 3851 VAL A N     1 
ATOM   15932 C  CA    . VAL A 1 2634 ? 148.305 133.563 138.355 1.00 116.60 ? 3851 VAL A CA    1 
ATOM   15933 C  C     . VAL A 1 2634 ? 148.283 133.245 139.844 1.00 115.33 ? 3851 VAL A C     1 
ATOM   15934 O  O     . VAL A 1 2634 ? 147.824 132.172 140.257 1.00 115.60 ? 3851 VAL A O     1 
ATOM   15935 C  CB    . VAL A 1 2634 ? 149.746 133.657 137.819 1.00 111.54 ? 3851 VAL A CB    1 
ATOM   15936 C  CG1   . VAL A 1 2634 ? 150.631 132.597 138.463 1.00 108.53 ? 3851 VAL A CG1   1 
ATOM   15937 C  CG2   . VAL A 1 2634 ? 149.766 133.526 136.303 1.00 103.83 ? 3851 VAL A CG2   1 
ATOM   15938 N  N     . LYS A 1 2635 ? 148.682 134.222 140.670 1.00 115.25 ? 3852 LYS A N     1 
ATOM   15939 C  CA    . LYS A 1 2635 ? 148.808 134.029 142.111 1.00 117.69 ? 3852 LYS A CA    1 
ATOM   15940 C  C     . LYS A 1 2635 ? 147.482 133.707 142.780 1.00 119.20 ? 3852 LYS A C     1 
ATOM   15941 O  O     . LYS A 1 2635 ? 147.477 133.148 143.882 1.00 119.41 ? 3852 LYS A O     1 
ATOM   15942 C  CB    . LYS A 1 2635 ? 149.411 135.277 142.759 1.00 114.19 ? 3852 LYS A CB    1 
ATOM   15943 C  CG    . LYS A 1 2635 ? 150.868 135.510 142.421 1.00 112.69 ? 3852 LYS A CG    1 
ATOM   15944 C  CD    . LYS A 1 2635 ? 151.454 136.656 143.228 1.00 110.92 ? 3852 LYS A CD    1 
ATOM   15945 C  CE    . LYS A 1 2635 ? 151.019 138.004 142.678 1.00 110.21 ? 3852 LYS A CE    1 
ATOM   15946 N  NZ    . LYS A 1 2635 ? 151.694 139.128 143.386 1.00 112.95 ? 3852 LYS A NZ    1 
ATOM   15947 N  N     . THR A 1 2636 ? 146.361 134.064 142.159 1.00 119.91 ? 3853 THR A N     1 
ATOM   15948 C  CA    . THR A 1 2636 ? 145.074 133.632 142.692 1.00 120.76 ? 3853 THR A CA    1 
ATOM   15949 C  C     . THR A 1 2636 ? 144.642 132.295 142.093 1.00 122.14 ? 3853 THR A C     1 
ATOM   15950 O  O     . THR A 1 2636 ? 144.541 131.293 142.809 1.00 125.06 ? 3853 THR A O     1 
ATOM   15951 C  CB    . THR A 1 2636 ? 144.009 134.705 142.440 1.00 119.65 ? 3853 THR A CB    1 
ATOM   15952 O  OG1   . THR A 1 2636 ? 143.939 134.993 141.038 1.00 119.97 ? 3853 THR A OG1   1 
ATOM   15953 C  CG2   . THR A 1 2636 ? 144.340 135.977 143.206 1.00 121.22 ? 3853 THR A CG2   1 
ATOM   15954 N  N     . TYR A 1 2637 ? 144.437 132.256 140.772 1.00 120.45 ? 3854 TYR A N     1 
ATOM   15955 C  CA    . TYR A 1 2637 ? 143.789 131.109 140.145 1.00 120.43 ? 3854 TYR A CA    1 
ATOM   15956 C  C     . TYR A 1 2637 ? 144.670 129.865 140.179 1.00 120.59 ? 3854 TYR A C     1 
ATOM   15957 O  O     . TYR A 1 2637 ? 144.223 128.794 140.608 1.00 121.18 ? 3854 TYR A O     1 
ATOM   15958 C  CB    . TYR A 1 2637 ? 143.404 131.452 138.707 1.00 119.45 ? 3854 TYR A CB    1 
ATOM   15959 C  CG    . TYR A 1 2637 ? 142.481 130.440 138.072 1.00 117.91 ? 3854 TYR A CG    1 
ATOM   15960 C  CD1   . TYR A 1 2637 ? 141.300 130.063 138.697 1.00 120.07 ? 3854 TYR A CD1   1 
ATOM   15961 C  CD2   . TYR A 1 2637 ? 142.796 129.854 136.855 1.00 118.69 ? 3854 TYR A CD2   1 
ATOM   15962 C  CE1   . TYR A 1 2637 ? 140.453 129.136 138.122 1.00 120.10 ? 3854 TYR A CE1   1 
ATOM   15963 C  CE2   . TYR A 1 2637 ? 141.957 128.926 136.275 1.00 120.12 ? 3854 TYR A CE2   1 
ATOM   15964 C  CZ    . TYR A 1 2637 ? 140.787 128.570 136.910 1.00 119.41 ? 3854 TYR A CZ    1 
ATOM   15965 O  OH    . TYR A 1 2637 ? 139.949 127.645 136.332 1.00 119.61 ? 3854 TYR A OH    1 
ATOM   15966 N  N     . LEU A 1 2638 ? 145.926 129.975 139.726 1.00 120.55 ? 3855 LEU A N     1 
ATOM   15967 C  CA    . LEU A 1 2638 ? 146.750 128.775 139.652 1.00 121.00 ? 3855 LEU A CA    1 
ATOM   15968 C  C     . LEU A 1 2638 ? 147.167 128.302 141.035 1.00 121.96 ? 3855 LEU A C     1 
ATOM   15969 O  O     . LEU A 1 2638 ? 147.278 127.094 141.264 1.00 121.21 ? 3855 LEU A O     1 
ATOM   15970 C  CB    . LEU A 1 2638 ? 147.976 129.014 138.771 1.00 117.35 ? 3855 LEU A CB    1 
ATOM   15971 C  CG    . LEU A 1 2638 ? 147.689 129.181 137.277 1.00 113.40 ? 3855 LEU A CG    1 
ATOM   15972 C  CD1   . LEU A 1 2638 ? 148.760 130.015 136.600 1.00 113.10 ? 3855 LEU A CD1   1 
ATOM   15973 C  CD2   . LEU A 1 2638 ? 147.561 127.823 136.603 1.00 103.63 ? 3855 LEU A CD2   1 
ATOM   15974 N  N     . HIS A 1 2639 ? 147.385 129.228 141.971 1.00 122.32 ? 3856 HIS A N     1 
ATOM   15975 C  CA    . HIS A 1 2639 ? 147.710 128.821 143.333 1.00 121.03 ? 3856 HIS A CA    1 
ATOM   15976 C  C     . HIS A 1 2639 ? 146.523 128.142 144.005 1.00 121.60 ? 3856 HIS A C     1 
ATOM   15977 O  O     . HIS A 1 2639 ? 146.702 127.177 144.757 1.00 121.25 ? 3856 HIS A O     1 
ATOM   15978 C  CB    . HIS A 1 2639 ? 148.182 130.020 144.150 1.00 121.01 ? 3856 HIS A CB    1 
ATOM   15979 C  CG    . HIS A 1 2639 ? 148.690 129.657 145.510 1.00 123.94 ? 3856 HIS A CG    1 
ATOM   15980 N  ND1   . HIS A 1 2639 ? 147.864 129.542 146.607 1.00 126.55 ? 3856 HIS A ND1   1 
ATOM   15981 C  CD2   . HIS A 1 2639 ? 149.939 129.373 145.948 1.00 120.35 ? 3856 HIS A CD2   1 
ATOM   15982 C  CE1   . HIS A 1 2639 ? 148.583 129.208 147.664 1.00 124.74 ? 3856 HIS A CE1   1 
ATOM   15983 N  NE2   . HIS A 1 2639 ? 149.845 129.098 147.291 1.00 121.02 ? 3856 HIS A NE2   1 
ATOM   15984 N  N     . LYS A 1 2640 ? 145.300 128.619 143.742 1.00 123.96 ? 3857 LYS A N     1 
ATOM   15985 C  CA    . LYS A 1 2640 ? 144.124 127.939 144.274 1.00 127.15 ? 3857 LYS A CA    1 
ATOM   15986 C  C     . LYS A 1 2640 ? 143.916 126.580 143.618 1.00 126.63 ? 3857 LYS A C     1 
ATOM   15987 O  O     . LYS A 1 2640 ? 143.433 125.646 144.270 1.00 128.28 ? 3857 LYS A O     1 
ATOM   15988 C  CB    . LYS A 1 2640 ? 142.884 128.814 144.091 1.00 127.18 ? 3857 LYS A CB    1 
ATOM   15989 N  N     . HIS A 1 2641 ? 144.260 126.454 142.334 1.00 124.32 ? 3858 HIS A N     1 
ATOM   15990 C  CA    . HIS A 1 2641 ? 144.149 125.163 141.660 1.00 125.80 ? 3858 HIS A CA    1 
ATOM   15991 C  C     . HIS A 1 2641 ? 145.160 124.161 142.204 1.00 126.78 ? 3858 HIS A C     1 
ATOM   15992 O  O     . HIS A 1 2641 ? 144.828 122.988 142.412 1.00 125.91 ? 3858 HIS A O     1 
ATOM   15993 C  CB    . HIS A 1 2641 ? 144.331 125.343 140.153 1.00 124.54 ? 3858 HIS A CB    1 
ATOM   15994 C  CG    . HIS A 1 2641 ? 144.252 124.064 139.379 1.00 122.94 ? 3858 HIS A CG    1 
ATOM   15995 N  ND1   . HIS A 1 2641 ? 145.062 123.798 138.297 1.00 122.45 ? 3858 HIS A ND1   1 
ATOM   15996 C  CD2   . HIS A 1 2641 ? 143.462 122.975 139.535 1.00 121.91 ? 3858 HIS A CD2   1 
ATOM   15997 C  CE1   . HIS A 1 2641 ? 144.774 122.601 137.818 1.00 122.00 ? 3858 HIS A CE1   1 
ATOM   15998 N  NE2   . HIS A 1 2641 ? 143.806 122.081 138.551 1.00 122.45 ? 3858 HIS A NE2   1 
ATOM   15999 N  N     . VAL A 1 2642 ? 146.399 124.601 142.432 1.00 125.12 ? 3859 VAL A N     1 
ATOM   16000 C  CA    . VAL A 1 2642 ? 147.427 123.703 142.950 1.00 121.39 ? 3859 VAL A CA    1 
ATOM   16001 C  C     . VAL A 1 2642 ? 147.141 123.336 144.402 1.00 121.78 ? 3859 VAL A C     1 
ATOM   16002 O  O     . VAL A 1 2642 ? 147.233 122.165 144.789 1.00 120.93 ? 3859 VAL A O     1 
ATOM   16003 C  CB    . VAL A 1 2642 ? 148.820 124.337 142.780 1.00 119.79 ? 3859 VAL A CB    1 
ATOM   16004 C  CG1   . VAL A 1 2642 ? 149.877 123.482 143.439 1.00 118.15 ? 3859 VAL A CG1   1 
ATOM   16005 C  CG2   . VAL A 1 2642 ? 149.145 124.502 141.306 1.00 115.99 ? 3859 VAL A CG2   1 
ATOM   16006 N  N     . GLU A 1 2643 ? 146.777 124.317 145.222 1.00 124.94 ? 3860 GLU A N     1 
ATOM   16007 C  CA    . GLU A 1 2643 ? 146.433 124.056 146.616 1.00 126.70 ? 3860 GLU A CA    1 
ATOM   16008 C  C     . GLU A 1 2643 ? 144.974 124.402 146.892 1.00 128.47 ? 3860 GLU A C     1 
ATOM   16009 O  O     . GLU A 1 2643 ? 144.064 123.727 146.412 1.00 128.20 ? 3860 GLU A O     1 
ATOM   16010 C  CB    . GLU A 1 2643 ? 147.348 124.846 147.554 1.00 124.64 ? 3860 GLU A CB    1 
ATOM   16011 C  CG    . GLU A 1 2643 ? 148.654 124.143 147.879 1.00 122.98 ? 3860 GLU A CG    1 
ATOM   16012 C  CD    . GLU A 1 2643 ? 149.734 125.099 148.349 1.00 124.69 ? 3860 GLU A CD    1 
ATOM   16013 O  OE1   . GLU A 1 2643 ? 150.483 125.617 147.494 1.00 125.61 ? 3860 GLU A OE1   1 
ATOM   16014 O  OE2   . GLU A 1 2643 ? 149.836 125.329 149.572 1.00 122.64 ? 3860 GLU A OE2   1 
ATOM   16015 N  N     . GLU A 1 2650 ? 143.040 114.888 140.726 1.00 123.79 ? 3867 GLU A N     1 
ATOM   16016 C  CA    . GLU A 1 2650 ? 144.199 114.014 140.589 1.00 127.22 ? 3867 GLU A CA    1 
ATOM   16017 C  C     . GLU A 1 2650 ? 144.043 113.083 139.391 1.00 128.62 ? 3867 GLU A C     1 
ATOM   16018 O  O     . GLU A 1 2650 ? 144.095 111.862 139.531 1.00 129.59 ? 3867 GLU A O     1 
ATOM   16019 C  CB    . GLU A 1 2650 ? 144.410 113.198 141.866 1.00 125.64 ? 3867 GLU A CB    1 
ATOM   16020 N  N     . HIS A 1 2651 ? 143.848 113.671 138.213 1.00 128.75 ? 3868 HIS A N     1 
ATOM   16021 C  CA    . HIS A 1 2651 ? 143.685 112.885 137.000 1.00 130.17 ? 3868 HIS A CA    1 
ATOM   16022 C  C     . HIS A 1 2651 ? 145.010 112.258 136.579 1.00 129.51 ? 3868 HIS A C     1 
ATOM   16023 O  O     . HIS A 1 2651 ? 146.092 112.765 136.887 1.00 128.09 ? 3868 HIS A O     1 
ATOM   16024 C  CB    . HIS A 1 2651 ? 143.138 113.756 135.870 1.00 130.65 ? 3868 HIS A CB    1 
ATOM   16025 C  CG    . HIS A 1 2651 ? 142.539 112.976 134.741 1.00 132.63 ? 3868 HIS A CG    1 
ATOM   16026 N  ND1   . HIS A 1 2651 ? 143.283 112.516 133.676 1.00 132.26 ? 3868 HIS A ND1   1 
ATOM   16027 C  CD2   . HIS A 1 2651 ? 141.266 112.576 134.510 1.00 132.48 ? 3868 HIS A CD2   1 
ATOM   16028 C  CE1   . HIS A 1 2651 ? 142.495 111.866 132.839 1.00 131.58 ? 3868 HIS A CE1   1 
ATOM   16029 N  NE2   . HIS A 1 2651 ? 141.266 111.888 133.321 1.00 132.30 ? 3868 HIS A NE2   1 
ATOM   16030 N  N     . GLU A 1 2652 ? 144.913 111.141 135.866 1.00 129.44 ? 3869 GLU A N     1 
ATOM   16031 C  CA    . GLU A 1 2652 ? 146.085 110.440 135.367 1.00 129.02 ? 3869 GLU A CA    1 
ATOM   16032 C  C     . GLU A 1 2652 ? 146.455 110.941 133.977 1.00 130.50 ? 3869 GLU A C     1 
ATOM   16033 O  O     . GLU A 1 2652 ? 145.602 111.414 133.219 1.00 131.46 ? 3869 GLU A O     1 
ATOM   16034 C  CB    . GLU A 1 2652 ? 145.838 108.931 135.325 1.00 130.63 ? 3869 GLU A CB    1 
ATOM   16035 N  N     . LYS A 1 2653 ? 147.748 110.824 133.655 1.00 128.43 ? 3870 LYS A N     1 
ATOM   16036 C  CA    . LYS A 1 2653 ? 148.308 111.235 132.363 1.00 126.49 ? 3870 LYS A CA    1 
ATOM   16037 C  C     . LYS A 1 2653 ? 148.029 112.707 132.069 1.00 128.61 ? 3870 LYS A C     1 
ATOM   16038 O  O     . LYS A 1 2653 ? 147.742 113.089 130.933 1.00 129.54 ? 3870 LYS A O     1 
ATOM   16039 C  CB    . LYS A 1 2653 ? 147.797 110.346 131.225 1.00 123.24 ? 3870 LYS A CB    1 
ATOM   16040 N  N     . PHE A 1 2654 ? 148.114 113.542 133.102 1.00 126.54 ? 3871 PHE A N     1 
ATOM   16041 C  CA    . PHE A 1 2654 ? 147.917 114.980 132.972 1.00 121.52 ? 3871 PHE A CA    1 
ATOM   16042 C  C     . PHE A 1 2654 ? 149.174 115.692 133.451 1.00 117.46 ? 3871 PHE A C     1 
ATOM   16043 O  O     . PHE A 1 2654 ? 149.585 115.524 134.604 1.00 116.31 ? 3871 PHE A O     1 
ATOM   16044 C  CB    . PHE A 1 2654 ? 146.696 115.445 133.770 1.00 122.13 ? 3871 PHE A CB    1 
ATOM   16045 C  CG    . PHE A 1 2654 ? 146.765 116.884 134.200 1.00 120.38 ? 3871 PHE A CG    1 
ATOM   16046 C  CD1   . PHE A 1 2654 ? 146.635 117.905 133.271 1.00 118.46 ? 3871 PHE A CD1   1 
ATOM   16047 C  CD2   . PHE A 1 2654 ? 146.961 117.215 135.530 1.00 119.71 ? 3871 PHE A CD2   1 
ATOM   16048 C  CE1   . PHE A 1 2654 ? 146.699 119.228 133.662 1.00 114.23 ? 3871 PHE A CE1   1 
ATOM   16049 C  CE2   . PHE A 1 2654 ? 147.026 118.539 135.927 1.00 116.20 ? 3871 PHE A CE2   1 
ATOM   16050 C  CZ    . PHE A 1 2654 ? 146.894 119.546 134.991 1.00 112.04 ? 3871 PHE A CZ    1 
ATOM   16051 N  N     . LYS A 1 2655 ? 149.779 116.483 132.566 1.00 113.21 ? 3872 LYS A N     1 
ATOM   16052 C  CA    . LYS A 1 2655 ? 150.929 117.313 132.891 1.00 107.95 ? 3872 LYS A CA    1 
ATOM   16053 C  C     . LYS A 1 2655 ? 150.687 118.714 132.348 1.00 108.47 ? 3872 LYS A C     1 
ATOM   16054 O  O     . LYS A 1 2655 ? 149.957 118.901 131.372 1.00 113.12 ? 3872 LYS A O     1 
ATOM   16055 C  CB    . LYS A 1 2655 ? 152.227 116.741 132.299 1.00 107.00 ? 3872 LYS A CB    1 
ATOM   16056 C  CG    . LYS A 1 2655 ? 152.509 115.293 132.655 1.00 111.17 ? 3872 LYS A CG    1 
ATOM   16057 C  CD    . LYS A 1 2655 ? 152.776 115.089 134.133 1.00 110.24 ? 3872 LYS A CD    1 
ATOM   16058 C  CE    . LYS A 1 2655 ? 153.255 113.669 134.365 1.00 104.25 ? 3872 LYS A CE    1 
ATOM   16059 N  NZ    . LYS A 1 2655 ? 153.977 113.504 135.650 1.00 98.83  ? 3872 LYS A NZ    1 
ATOM   16060 N  N     . MET A 1 2656 ? 151.298 119.707 132.994 1.00 101.62 ? 3873 MET A N     1 
ATOM   16061 C  CA    . MET A 1 2656 ? 151.257 121.072 132.490 1.00 95.74  ? 3873 MET A CA    1 
ATOM   16062 C  C     . MET A 1 2656 ? 152.575 121.756 132.808 1.00 89.83  ? 3873 MET A C     1 
ATOM   16063 O  O     . MET A 1 2656 ? 153.394 121.231 133.564 1.00 92.75  ? 3873 MET A O     1 
ATOM   16064 C  CB    . MET A 1 2656 ? 150.097 121.896 133.063 1.00 95.53  ? 3873 MET A CB    1 
ATOM   16065 C  CG    . MET A 1 2656 ? 150.142 122.208 134.548 1.00 99.37  ? 3873 MET A CG    1 
ATOM   16066 S  SD    . MET A 1 2656 ? 148.663 123.156 134.972 1.00 113.95 ? 3873 MET A SD    1 
ATOM   16067 C  CE    . MET A 1 2656 ? 148.909 123.407 136.733 1.00 102.71 ? 3873 MET A CE    1 
ATOM   16068 N  N     . PHE A 1 2657 ? 152.786 122.917 132.191 1.00 88.54  ? 3874 PHE A N     1 
ATOM   16069 C  CA    . PHE A 1 2657 ? 154.019 123.670 132.347 1.00 83.50  ? 3874 PHE A CA    1 
ATOM   16070 C  C     . PHE A 1 2657 ? 153.688 125.148 132.501 1.00 76.43  ? 3874 PHE A C     1 
ATOM   16071 O  O     . PHE A 1 2657 ? 152.639 125.621 132.058 1.00 80.01  ? 3874 PHE A O     1 
ATOM   16072 C  CB    . PHE A 1 2657 ? 154.960 123.457 131.150 1.00 85.50  ? 3874 PHE A CB    1 
ATOM   16073 C  CG    . PHE A 1 2657 ? 155.285 122.012 130.877 1.00 86.66  ? 3874 PHE A CG    1 
ATOM   16074 C  CD1   . PHE A 1 2657 ? 156.305 121.374 131.562 1.00 87.21  ? 3874 PHE A CD1   1 
ATOM   16075 C  CD2   . PHE A 1 2657 ? 154.578 121.296 129.923 1.00 91.09  ? 3874 PHE A CD2   1 
ATOM   16076 C  CE1   . PHE A 1 2657 ? 156.608 120.047 131.309 1.00 88.84  ? 3874 PHE A CE1   1 
ATOM   16077 C  CE2   . PHE A 1 2657 ? 154.876 119.969 129.665 1.00 94.76  ? 3874 PHE A CE2   1 
ATOM   16078 C  CZ    . PHE A 1 2657 ? 155.892 119.344 130.358 1.00 92.53  ? 3874 PHE A CZ    1 
ATOM   16079 N  N     . MET A 1 2658 ? 154.599 125.873 133.144 1.00 70.03  ? 3875 MET A N     1 
ATOM   16080 C  CA    . MET A 1 2658 ? 154.519 127.320 133.288 1.00 64.02  ? 3875 MET A CA    1 
ATOM   16081 C  C     . MET A 1 2658 ? 155.839 127.908 132.819 1.00 61.17  ? 3875 MET A C     1 
ATOM   16082 O  O     . MET A 1 2658 ? 156.901 127.444 133.237 1.00 67.60  ? 3875 MET A O     1 
ATOM   16083 C  CB    . MET A 1 2658 ? 154.262 127.728 134.741 1.00 63.09  ? 3875 MET A CB    1 
ATOM   16084 C  CG    . MET A 1 2658 ? 153.037 127.113 135.378 1.00 68.25  ? 3875 MET A CG    1 
ATOM   16085 S  SD    . MET A 1 2658 ? 153.182 127.155 137.174 1.00 81.65  ? 3875 MET A SD    1 
ATOM   16086 C  CE    . MET A 1 2658 ? 151.461 127.148 137.657 1.00 98.01  ? 3875 MET A CE    1 
ATOM   16087 N  N     . THR A 1 2659 ? 155.781 128.923 131.966 1.00 58.89  ? 3876 THR A N     1 
ATOM   16088 C  CA    . THR A 1 2659 ? 156.981 129.587 131.474 1.00 58.45  ? 3876 THR A CA    1 
ATOM   16089 C  C     . THR A 1 2659 ? 157.058 130.984 132.073 1.00 62.09  ? 3876 THR A C     1 
ATOM   16090 O  O     . THR A 1 2659 ? 156.156 131.802 131.868 1.00 70.53  ? 3876 THR A O     1 
ATOM   16091 C  CB    . THR A 1 2659 ? 156.996 129.659 129.947 1.00 60.39  ? 3876 THR A CB    1 
ATOM   16092 O  OG1   . THR A 1 2659 ? 157.202 128.348 129.408 1.00 57.45  ? 3876 THR A OG1   1 
ATOM   16093 C  CG2   . THR A 1 2659 ? 158.114 130.573 129.470 1.00 56.82  ? 3876 THR A CG2   1 
ATOM   16094 N  N     . CYS A 1 2660 ? 158.137 131.250 132.808 1.00 56.45  ? 3877 CYS A N     1 
ATOM   16095 C  CA    . CYS A 1 2660 ? 158.382 132.563 133.390 1.00 60.17  ? 3877 CYS A CA    1 
ATOM   16096 C  C     . CYS A 1 2660 ? 159.792 133.024 133.045 1.00 63.61  ? 3877 CYS A C     1 
ATOM   16097 O  O     . CYS A 1 2660 ? 160.468 132.396 132.225 1.00 61.91  ? 3877 CYS A O     1 
ATOM   16098 C  CB    . CYS A 1 2660 ? 158.177 132.533 134.904 1.00 62.54  ? 3877 CYS A CB    1 
ATOM   16099 S  SG    . CYS A 1 2660 ? 159.334 131.483 135.802 1.00 73.95  ? 3877 CYS A SG    1 
ATOM   16100 N  N     . HIS A 1 2661 ? 160.248 134.113 133.658 1.00 65.97  ? 3878 HIS A N     1 
ATOM   16101 C  CA    . HIS A 1 2661 ? 161.560 134.667 133.357 1.00 62.22  ? 3878 HIS A CA    1 
ATOM   16102 C  C     . HIS A 1 2661 ? 162.363 134.850 134.635 1.00 61.40  ? 3878 HIS A C     1 
ATOM   16103 O  O     . HIS A 1 2661 ? 161.808 135.164 135.692 1.00 64.07  ? 3878 HIS A O     1 
ATOM   16104 C  CB    . HIS A 1 2661 ? 161.445 136.003 132.619 1.00 62.10  ? 3878 HIS A CB    1 
ATOM   16105 C  CG    . HIS A 1 2661 ? 160.885 135.880 131.238 1.00 57.51  ? 3878 HIS A CG    1 
ATOM   16106 N  ND1   . HIS A 1 2661 ? 161.621 135.400 130.177 1.00 56.39  ? 3878 HIS A ND1   1 
ATOM   16107 C  CD2   . HIS A 1 2661 ? 159.660 136.174 130.744 1.00 58.21  ? 3878 HIS A CD2   1 
ATOM   16108 C  CE1   . HIS A 1 2661 ? 160.874 135.402 129.089 1.00 57.51  ? 3878 HIS A CE1   1 
ATOM   16109 N  NE2   . HIS A 1 2661 ? 159.679 135.868 129.405 1.00 59.43  ? 3878 HIS A NE2   1 
ATOM   16110 N  N     . LEU A 1 2662 ? 163.677 134.635 134.526 1.00 61.55  ? 3879 LEU A N     1 
ATOM   16111 C  CA    . LEU A 1 2662 ? 164.571 134.879 135.653 1.00 66.28  ? 3879 LEU A CA    1 
ATOM   16112 C  C     . LEU A 1 2662 ? 164.624 136.359 136.007 1.00 67.74  ? 3879 LEU A C     1 
ATOM   16113 O  O     . LEU A 1 2662 ? 164.595 136.723 137.189 1.00 70.86  ? 3879 LEU A O     1 
ATOM   16114 C  CB    . LEU A 1 2662 ? 165.970 134.354 135.332 1.00 64.42  ? 3879 LEU A CB    1 
ATOM   16115 C  CG    . LEU A 1 2662 ? 166.106 132.834 135.255 1.00 57.04  ? 3879 LEU A CG    1 
ATOM   16116 C  CD1   . LEU A 1 2662 ? 167.470 132.440 134.721 1.00 52.00  ? 3879 LEU A CD1   1 
ATOM   16117 C  CD2   . LEU A 1 2662 ? 165.892 132.250 136.628 1.00 50.79  ? 3879 LEU A CD2   1 
ATOM   16118 N  N     . THR A 1 2663 ? 164.695 137.226 135.000 1.00 66.63  ? 3880 THR A N     1 
ATOM   16119 C  CA    . THR A 1 2663 ? 164.711 138.672 135.220 1.00 66.40  ? 3880 THR A CA    1 
ATOM   16120 C  C     . THR A 1 2663 ? 163.285 139.225 135.210 1.00 69.92  ? 3880 THR A C     1 
ATOM   16121 O  O     . THR A 1 2663 ? 162.919 140.097 134.423 1.00 66.82  ? 3880 THR A O     1 
ATOM   16122 C  CB    . THR A 1 2663 ? 165.582 139.355 134.173 1.00 59.75  ? 3880 THR A CB    1 
ATOM   16123 O  OG1   . THR A 1 2663 ? 165.099 139.031 132.864 1.00 56.59  ? 3880 THR A OG1   1 
ATOM   16124 C  CG2   . THR A 1 2663 ? 167.022 138.889 134.300 1.00 57.95  ? 3880 THR A CG2   1 
ATOM   16125 N  N     . GLY A 1 2664 ? 162.474 138.688 136.118 1.00 70.42  ? 3881 GLY A N     1 
ATOM   16126 C  CA    . GLY A 1 2664 ? 161.088 139.092 136.243 1.00 69.53  ? 3881 GLY A CA    1 
ATOM   16127 C  C     . GLY A 1 2664 ? 160.677 139.311 137.683 1.00 73.24  ? 3881 GLY A C     1 
ATOM   16128 O  O     . GLY A 1 2664 ? 161.527 139.364 138.576 1.00 77.85  ? 3881 GLY A O     1 
ATOM   16129 N  N     . ASP A 1 2665 ? 159.377 139.439 137.922 1.00 71.67  ? 3882 ASP A N     1 
ATOM   16130 C  CA    . ASP A 1 2665 ? 158.878 139.682 139.264 1.00 76.58  ? 3882 ASP A CA    1 
ATOM   16131 C  C     . ASP A 1 2665 ? 158.953 138.409 140.105 1.00 84.85  ? 3882 ASP A C     1 
ATOM   16132 O  O     . ASP A 1 2665 ? 159.119 137.298 139.596 1.00 87.42  ? 3882 ASP A O     1 
ATOM   16133 C  CB    . ASP A 1 2665 ? 157.446 140.209 139.214 1.00 78.37  ? 3882 ASP A CB    1 
ATOM   16134 N  N     . LYS A 1 2666 ? 158.821 138.587 141.417 1.00 89.80  ? 3883 LYS A N     1 
ATOM   16135 C  CA    . LYS A 1 2666 ? 158.939 137.489 142.371 1.00 92.49  ? 3883 LYS A CA    1 
ATOM   16136 C  C     . LYS A 1 2666 ? 157.625 136.717 142.426 1.00 94.12  ? 3883 LYS A C     1 
ATOM   16137 O  O     . LYS A 1 2666 ? 156.605 137.240 142.887 1.00 92.07  ? 3883 LYS A O     1 
ATOM   16138 C  CB    . LYS A 1 2666 ? 159.322 138.033 143.746 1.00 94.67  ? 3883 LYS A CB    1 
ATOM   16139 C  CG    . LYS A 1 2666 ? 159.538 136.986 144.836 1.00 97.82  ? 3883 LYS A CG    1 
ATOM   16140 C  CD    . LYS A 1 2666 ? 160.291 135.760 144.343 1.00 95.94  ? 3883 LYS A CD    1 
ATOM   16141 C  CE    . LYS A 1 2666 ? 160.339 134.684 145.417 1.00 93.43  ? 3883 LYS A CE    1 
ATOM   16142 N  NZ    . LYS A 1 2666 ? 160.828 133.388 144.881 1.00 88.92  ? 3883 LYS A NZ    1 
ATOM   16143 N  N     . LEU A 1 2667 ? 157.652 135.472 141.956 1.00 94.83  ? 3884 LEU A N     1 
ATOM   16144 C  CA    . LEU A 1 2667 ? 156.516 134.581 142.122 1.00 98.15  ? 3884 LEU A CA    1 
ATOM   16145 C  C     . LEU A 1 2667 ? 156.397 134.162 143.588 1.00 100.20 ? 3884 LEU A C     1 
ATOM   16146 O  O     . LEU A 1 2667 ? 157.385 134.182 144.325 1.00 99.00  ? 3884 LEU A O     1 
ATOM   16147 C  CB    . LEU A 1 2667 ? 156.674 133.349 141.230 1.00 97.84  ? 3884 LEU A CB    1 
ATOM   16148 C  CG    . LEU A 1 2667 ? 156.284 133.476 139.756 1.00 90.60  ? 3884 LEU A CG    1 
ATOM   16149 C  CD1   . LEU A 1 2667 ? 157.395 134.107 138.934 1.00 86.67  ? 3884 LEU A CD1   1 
ATOM   16150 C  CD2   . LEU A 1 2667 ? 155.905 132.116 139.194 1.00 86.68  ? 3884 LEU A CD2   1 
ATOM   16151 N  N     . PRO A 1 2668 ? 155.196 133.798 144.044 1.00 101.79 ? 3885 PRO A N     1 
ATOM   16152 C  CA    . PRO A 1 2668 ? 155.040 133.398 145.449 1.00 101.34 ? 3885 PRO A CA    1 
ATOM   16153 C  C     . PRO A 1 2668 ? 155.798 132.117 145.765 1.00 103.55 ? 3885 PRO A C     1 
ATOM   16154 O  O     . PRO A 1 2668 ? 155.949 131.230 144.922 1.00 107.19 ? 3885 PRO A O     1 
ATOM   16155 C  CB    . PRO A 1 2668 ? 153.527 133.205 145.604 1.00 106.03 ? 3885 PRO A CB    1 
ATOM   16156 C  CG    . PRO A 1 2668 ? 153.007 133.043 144.224 1.00 104.40 ? 3885 PRO A CG    1 
ATOM   16157 C  CD    . PRO A 1 2668 ? 153.906 133.836 143.336 1.00 103.68 ? 3885 PRO A CD    1 
ATOM   16158 N  N     . ALA A 1 2669 ? 156.289 132.042 147.003 1.00 106.74 ? 3886 ALA A N     1 
ATOM   16159 C  CA    . ALA A 1 2669 ? 157.024 130.860 147.452 1.00 112.60 ? 3886 ALA A CA    1 
ATOM   16160 C  C     . ALA A 1 2669 ? 156.191 129.578 147.465 1.00 112.06 ? 3886 ALA A C     1 
ATOM   16161 O  O     . ALA A 1 2669 ? 156.707 128.544 147.006 1.00 110.13 ? 3886 ALA A O     1 
ATOM   16162 C  CB    . ALA A 1 2669 ? 157.655 131.138 148.822 1.00 112.22 ? 3886 ALA A CB    1 
ATOM   16163 N  N     . PRO A 1 2670 ? 154.950 129.541 147.988 1.00 111.81 ? 3887 PRO A N     1 
ATOM   16164 C  CA    . PRO A 1 2670 ? 154.193 128.275 147.927 1.00 113.69 ? 3887 PRO A CA    1 
ATOM   16165 C  C     . PRO A 1 2670 ? 153.904 127.791 146.516 1.00 112.71 ? 3887 PRO A C     1 
ATOM   16166 O  O     . PRO A 1 2670 ? 153.853 126.575 146.291 1.00 113.48 ? 3887 PRO A O     1 
ATOM   16167 C  CB    . PRO A 1 2670 ? 152.898 128.598 148.686 1.00 112.73 ? 3887 PRO A CB    1 
ATOM   16168 C  CG    . PRO A 1 2670 ? 152.787 130.068 148.644 1.00 111.18 ? 3887 PRO A CG    1 
ATOM   16169 C  CD    . PRO A 1 2670 ? 154.189 130.556 148.744 1.00 110.50 ? 3887 PRO A CD    1 
ATOM   16170 N  N     . LEU A 1 2671 ? 153.703 128.700 145.560 1.00 112.03 ? 3888 LEU A N     1 
ATOM   16171 C  CA    . LEU A 1 2671 ? 153.526 128.280 144.174 1.00 112.83 ? 3888 LEU A CA    1 
ATOM   16172 C  C     . LEU A 1 2671 ? 154.814 127.697 143.607 1.00 109.14 ? 3888 LEU A C     1 
ATOM   16173 O  O     . LEU A 1 2671 ? 154.784 126.702 142.873 1.00 106.55 ? 3888 LEU A O     1 
ATOM   16174 C  CB    . LEU A 1 2671 ? 153.047 129.458 143.324 1.00 113.17 ? 3888 LEU A CB    1 
ATOM   16175 C  CG    . LEU A 1 2671 ? 153.003 129.251 141.808 1.00 111.86 ? 3888 LEU A CG    1 
ATOM   16176 C  CD1   . LEU A 1 2671 ? 151.793 128.415 141.415 1.00 112.95 ? 3888 LEU A CD1   1 
ATOM   16177 C  CD2   . LEU A 1 2671 ? 152.998 130.587 141.082 1.00 107.75 ? 3888 LEU A CD2   1 
ATOM   16178 N  N     . LEU A 1 2672 ? 155.956 128.295 143.946 1.00 108.94 ? 3889 LEU A N     1 
ATOM   16179 C  CA    . LEU A 1 2672 ? 157.245 127.815 143.466 1.00 108.13 ? 3889 LEU A CA    1 
ATOM   16180 C  C     . LEU A 1 2672 ? 157.761 126.607 144.236 1.00 107.09 ? 3889 LEU A C     1 
ATOM   16181 O  O     . LEU A 1 2672 ? 158.789 126.043 143.846 1.00 107.19 ? 3889 LEU A O     1 
ATOM   16182 C  CB    . LEU A 1 2672 ? 158.289 128.933 143.536 1.00 102.50 ? 3889 LEU A CB    1 
ATOM   16183 C  CG    . LEU A 1 2672 ? 158.131 130.106 142.571 1.00 94.27  ? 3889 LEU A CG    1 
ATOM   16184 C  CD1   . LEU A 1 2672 ? 159.168 131.172 142.874 1.00 92.35  ? 3889 LEU A CD1   1 
ATOM   16185 C  CD2   . LEU A 1 2672 ? 158.248 129.633 141.132 1.00 87.10  ? 3889 LEU A CD2   1 
ATOM   16186 N  N     . GLN A 1 2673 ? 157.091 126.198 145.313 1.00 105.40 ? 3890 GLN A N     1 
ATOM   16187 C  CA    . GLN A 1 2673 ? 157.606 125.105 146.130 1.00 107.01 ? 3890 GLN A CA    1 
ATOM   16188 C  C     . GLN A 1 2673 ? 157.149 123.738 145.626 1.00 107.75 ? 3890 GLN A C     1 
ATOM   16189 O  O     . GLN A 1 2673 ? 157.978 122.900 145.256 1.00 106.24 ? 3890 GLN A O     1 
ATOM   16190 C  CB    . GLN A 1 2673 ? 157.203 125.299 147.594 1.00 108.07 ? 3890 GLN A CB    1 
ATOM   16191 C  CG    . GLN A 1 2673 ? 157.770 124.223 148.489 1.00 107.46 ? 3890 GLN A CG    1 
ATOM   16192 C  CD    . GLN A 1 2673 ? 159.280 124.279 148.555 1.00 105.93 ? 3890 GLN A CD    1 
ATOM   16193 O  OE1   . GLN A 1 2673 ? 159.873 125.354 148.642 1.00 104.96 ? 3890 GLN A OE1   1 
ATOM   16194 N  NE2   . GLN A 1 2673 ? 159.915 123.116 148.473 1.00 105.02 ? 3890 GLN A NE2   1 
ATOM   16195 N  N     . ARG A 1 2674 ? 155.837 123.496 145.602 1.00 109.83 ? 3891 ARG A N     1 
ATOM   16196 C  CA    . ARG A 1 2674 ? 155.311 122.198 145.178 1.00 109.69 ? 3891 ARG A CA    1 
ATOM   16197 C  C     . ARG A 1 2674 ? 155.185 122.143 143.653 1.00 104.90 ? 3891 ARG A C     1 
ATOM   16198 O  O     . ARG A 1 2674 ? 154.103 122.023 143.077 1.00 103.02 ? 3891 ARG A O     1 
ATOM   16199 C  CB    . ARG A 1 2674 ? 153.986 121.906 145.871 1.00 112.66 ? 3891 ARG A CB    1 
ATOM   16200 C  CG    . ARG A 1 2674 ? 153.005 123.061 145.909 1.00 114.19 ? 3891 ARG A CG    1 
ATOM   16201 C  CD    . ARG A 1 2674 ? 151.701 122.622 146.553 1.00 121.31 ? 3891 ARG A CD    1 
ATOM   16202 N  NE    . ARG A 1 2674 ? 151.079 121.522 145.824 1.00 124.69 ? 3891 ARG A NE    1 
ATOM   16203 C  CZ    . ARG A 1 2674 ? 150.147 120.720 146.322 1.00 124.15 ? 3891 ARG A CZ    1 
ATOM   16204 N  NH1   . ARG A 1 2674 ? 149.702 120.862 147.560 1.00 122.38 ? 3891 ARG A NH1   1 
ATOM   16205 N  NH2   . ARG A 1 2674 ? 149.648 119.753 145.558 1.00 121.35 ? 3891 ARG A NH2   1 
ATOM   16206 N  N     . THR A 1 2675 ? 156.343 122.224 143.003 1.00 100.15 ? 3892 THR A N     1 
ATOM   16207 C  CA    . THR A 1 2675 ? 156.439 122.177 141.553 1.00 93.05  ? 3892 THR A CA    1 
ATOM   16208 C  C     . THR A 1 2675 ? 157.856 121.768 141.183 1.00 89.77  ? 3892 THR A C     1 
ATOM   16209 O  O     . THR A 1 2675 ? 158.782 121.880 141.990 1.00 91.62  ? 3892 THR A O     1 
ATOM   16210 C  CB    . THR A 1 2675 ? 156.083 123.526 140.920 1.00 92.93  ? 3892 THR A CB    1 
ATOM   16211 O  OG1   . THR A 1 2675 ? 156.236 123.446 139.499 1.00 89.56  ? 3892 THR A OG1   1 
ATOM   16212 C  CG2   . THR A 1 2675 ? 156.989 124.616 141.457 1.00 97.11  ? 3892 THR A CG2   1 
ATOM   16213 N  N     . ASP A 1 2676 ? 158.013 121.294 139.953 1.00 86.23  ? 3893 ASP A N     1 
ATOM   16214 C  CA    . ASP A 1 2676 ? 159.312 120.899 139.424 1.00 83.86  ? 3893 ASP A CA    1 
ATOM   16215 C  C     . ASP A 1 2676 ? 159.837 122.020 138.537 1.00 77.78  ? 3893 ASP A C     1 
ATOM   16216 O  O     . ASP A 1 2676 ? 159.181 122.405 137.564 1.00 82.50  ? 3893 ASP A O     1 
ATOM   16217 C  CB    . ASP A 1 2676 ? 159.208 119.588 138.645 1.00 89.04  ? 3893 ASP A CB    1 
ATOM   16218 C  CG    . ASP A 1 2676 ? 158.637 118.459 139.481 1.00 93.13  ? 3893 ASP A CG    1 
ATOM   16219 O  OD1   . ASP A 1 2676 ? 157.405 118.429 139.681 1.00 93.03  ? 3893 ASP A OD1   1 
ATOM   16220 O  OD2   . ASP A 1 2676 ? 159.422 117.602 139.939 1.00 95.02  ? 3893 ASP A OD2   1 
ATOM   16221 N  N     . ARG A 1 2677 ? 161.015 122.537 138.870 1.00 67.00  ? 3894 ARG A N     1 
ATOM   16222 C  CA    . ARG A 1 2677 ? 161.568 123.717 138.221 1.00 59.02  ? 3894 ARG A CA    1 
ATOM   16223 C  C     . ARG A 1 2677 ? 162.704 123.336 137.281 1.00 52.48  ? 3894 ARG A C     1 
ATOM   16224 O  O     . ARG A 1 2677 ? 163.590 122.558 137.650 1.00 52.27  ? 3894 ARG A O     1 
ATOM   16225 C  CB    . ARG A 1 2677 ? 162.053 124.730 139.261 1.00 62.79  ? 3894 ARG A CB    1 
ATOM   16226 C  CG    . ARG A 1 2677 ? 163.164 125.626 138.757 1.00 63.12  ? 3894 ARG A CG    1 
ATOM   16227 C  CD    . ARG A 1 2677 ? 162.622 126.751 137.902 1.00 60.63  ? 3894 ARG A CD    1 
ATOM   16228 N  NE    . ARG A 1 2677 ? 163.589 127.831 137.790 1.00 61.40  ? 3894 ARG A NE    1 
ATOM   16229 C  CZ    . ARG A 1 2677 ? 163.547 128.943 138.506 1.00 64.73  ? 3894 ARG A CZ    1 
ATOM   16230 N  NH1   . ARG A 1 2677 ? 162.568 129.174 139.363 1.00 59.32  ? 3894 ARG A NH1   1 
ATOM   16231 N  NH2   . ARG A 1 2677 ? 164.511 129.843 138.357 1.00 67.81  ? 3894 ARG A NH2   1 
ATOM   16232 N  N     . VAL A 1 2678 ? 162.666 123.885 136.066 1.00 50.97  ? 3895 VAL A N     1 
ATOM   16233 C  CA    . VAL A 1 2678 ? 163.723 123.735 135.074 1.00 52.18  ? 3895 VAL A CA    1 
ATOM   16234 C  C     . VAL A 1 2678 ? 164.144 125.125 134.614 1.00 50.76  ? 3895 VAL A C     1 
ATOM   16235 O  O     . VAL A 1 2678 ? 163.308 126.027 134.498 1.00 56.01  ? 3895 VAL A O     1 
ATOM   16236 C  CB    . VAL A 1 2678 ? 163.264 122.884 133.867 1.00 53.34  ? 3895 VAL A CB    1 
ATOM   16237 C  CG1   . VAL A 1 2678 ? 164.446 122.513 132.985 1.00 55.26  ? 3895 VAL A CG1   1 
ATOM   16238 C  CG2   . VAL A 1 2678 ? 162.529 121.633 134.327 1.00 55.70  ? 3895 VAL A CG2   1 
ATOM   16239 N  N     . VAL A 1 2679 ? 165.438 125.302 134.361 1.00 49.17  ? 3896 VAL A N     1 
ATOM   16240 C  CA    . VAL A 1 2679 ? 165.979 126.529 133.786 1.00 46.76  ? 3896 VAL A CA    1 
ATOM   16241 C  C     . VAL A 1 2679 ? 166.511 126.202 132.399 1.00 52.86  ? 3896 VAL A C     1 
ATOM   16242 O  O     . VAL A 1 2679 ? 167.304 125.266 132.236 1.00 60.03  ? 3896 VAL A O     1 
ATOM   16243 C  CB    . VAL A 1 2679 ? 167.077 127.137 134.675 1.00 48.00  ? 3896 VAL A CB    1 
ATOM   16244 C  CG1   . VAL A 1 2679 ? 167.843 128.210 133.920 1.00 50.41  ? 3896 VAL A CG1   1 
ATOM   16245 C  CG2   . VAL A 1 2679 ? 166.466 127.711 135.940 1.00 51.61  ? 3896 VAL A CG2   1 
ATOM   16246 N  N     . TYR A 1 2680 ? 166.079 126.970 131.403 1.00 55.74  ? 3897 TYR A N     1 
ATOM   16247 C  CA    . TYR A 1 2680 ? 166.331 126.654 130.006 1.00 60.35  ? 3897 TYR A CA    1 
ATOM   16248 C  C     . TYR A 1 2680 ? 167.409 127.563 129.432 1.00 62.47  ? 3897 TYR A C     1 
ATOM   16249 O  O     . TYR A 1 2680 ? 167.619 128.684 129.900 1.00 64.71  ? 3897 TYR A O     1 
ATOM   16250 C  CB    . TYR A 1 2680 ? 165.042 126.788 129.194 1.00 63.03  ? 3897 TYR A CB    1 
ATOM   16251 C  CG    . TYR A 1 2680 ? 165.168 126.419 127.734 1.00 70.36  ? 3897 TYR A CG    1 
ATOM   16252 C  CD1   . TYR A 1 2680 ? 165.242 125.090 127.342 1.00 76.22  ? 3897 TYR A CD1   1 
ATOM   16253 C  CD2   . TYR A 1 2680 ? 165.199 127.395 126.748 1.00 75.31  ? 3897 TYR A CD2   1 
ATOM   16254 C  CE1   . TYR A 1 2680 ? 165.355 124.744 126.011 1.00 77.39  ? 3897 TYR A CE1   1 
ATOM   16255 C  CE2   . TYR A 1 2680 ? 165.309 127.056 125.412 1.00 79.01  ? 3897 TYR A CE2   1 
ATOM   16256 C  CZ    . TYR A 1 2680 ? 165.386 125.729 125.051 1.00 78.54  ? 3897 TYR A CZ    1 
ATOM   16257 O  OH    . TYR A 1 2680 ? 165.496 125.385 123.724 1.00 81.82  ? 3897 TYR A OH    1 
ATOM   16258 N  N     . GLU A 1 2681 ? 168.099 127.060 128.407 1.00 64.12  ? 3898 GLU A N     1 
ATOM   16259 C  CA    . GLU A 1 2681 ? 169.134 127.831 127.722 1.00 69.18  ? 3898 GLU A CA    1 
ATOM   16260 C  C     . GLU A 1 2681 ? 169.119 127.420 126.252 1.00 74.09  ? 3898 GLU A C     1 
ATOM   16261 O  O     . GLU A 1 2681 ? 169.609 126.343 125.903 1.00 74.02  ? 3898 GLU A O     1 
ATOM   16262 C  CB    . GLU A 1 2681 ? 170.499 127.597 128.355 1.00 69.28  ? 3898 GLU A CB    1 
ATOM   16263 C  CG    . GLU A 1 2681 ? 171.607 128.456 127.774 1.00 70.06  ? 3898 GLU A CG    1 
ATOM   16264 C  CD    . GLU A 1 2681 ? 172.900 128.345 128.556 1.00 68.51  ? 3898 GLU A CD    1 
ATOM   16265 O  OE1   . GLU A 1 2681 ? 172.980 127.485 129.457 1.00 65.68  ? 3898 GLU A OE1   1 
ATOM   16266 O  OE2   . GLU A 1 2681 ? 173.836 129.118 128.269 1.00 66.68  ? 3898 GLU A OE2   1 
ATOM   16267 N  N     . ASP A 1 2682 ? 168.557 128.279 125.404 1.00 77.52  ? 3899 ASP A N     1 
ATOM   16268 C  CA    . ASP A 1 2682 ? 168.553 128.027 123.973 1.00 78.88  ? 3899 ASP A CA    1 
ATOM   16269 C  C     . ASP A 1 2682 ? 169.942 128.279 123.388 1.00 77.49  ? 3899 ASP A C     1 
ATOM   16270 O  O     . ASP A 1 2682 ? 170.822 128.865 124.025 1.00 71.65  ? 3899 ASP A O     1 
ATOM   16271 C  CB    . ASP A 1 2682 ? 167.516 128.905 123.272 1.00 77.33  ? 3899 ASP A CB    1 
ATOM   16272 C  CG    . ASP A 1 2682 ? 167.050 128.324 121.952 1.00 82.99  ? 3899 ASP A CG    1 
ATOM   16273 O  OD1   . ASP A 1 2682 ? 167.318 127.132 121.694 1.00 84.95  ? 3899 ASP A OD1   1 
ATOM   16274 O  OD2   . ASP A 1 2682 ? 166.426 129.067 121.165 1.00 85.60  ? 3899 ASP A OD2   1 
ATOM   16275 N  N     . ILE A 1 2683 ? 170.131 127.821 122.155 1.00 82.05  ? 3900 ILE A N     1 
ATOM   16276 C  CA    . ILE A 1 2683 ? 171.409 127.959 121.463 1.00 81.60  ? 3900 ILE A CA    1 
ATOM   16277 C  C     . ILE A 1 2683 ? 171.660 129.430 121.142 1.00 75.21  ? 3900 ILE A C     1 
ATOM   16278 O  O     . ILE A 1 2683 ? 170.781 130.118 120.602 1.00 66.61  ? 3900 ILE A O     1 
ATOM   16279 C  CB    . ILE A 1 2683 ? 171.461 127.064 120.207 1.00 84.65  ? 3900 ILE A CB    1 
ATOM   16280 C  CG1   . ILE A 1 2683 ? 172.860 127.076 119.578 1.00 77.98  ? 3900 ILE A CG1   1 
ATOM   16281 C  CG2   . ILE A 1 2683 ? 170.356 127.404 119.195 1.00 77.88  ? 3900 ILE A CG2   1 
ATOM   16282 C  CD1   . ILE A 1 2683 ? 173.926 126.416 120.427 1.00 78.72  ? 3900 ILE A CD1   1 
ATOM   16283 N  N     . PRO A 1 2684 ? 172.820 129.971 121.516 1.00 76.70  ? 3901 PRO A N     1 
ATOM   16284 C  CA    . PRO A 1 2684 ? 173.210 131.307 121.056 1.00 70.07  ? 3901 PRO A CA    1 
ATOM   16285 C  C     . PRO A 1 2684 ? 173.846 131.329 119.676 1.00 71.15  ? 3901 PRO A C     1 
ATOM   16286 O  O     . PRO A 1 2684 ? 174.445 132.345 119.311 1.00 72.11  ? 3901 PRO A O     1 
ATOM   16287 C  CB    . PRO A 1 2684 ? 174.219 131.749 122.126 1.00 67.26  ? 3901 PRO A CB    1 
ATOM   16288 C  CG    . PRO A 1 2684 ? 174.827 130.484 122.606 1.00 74.50  ? 3901 PRO A CG    1 
ATOM   16289 C  CD    . PRO A 1 2684 ? 173.759 129.427 122.513 1.00 78.59  ? 3901 PRO A CD    1 
ATOM   16290 N  N     . GLY A 1 2685 ? 173.741 130.236 118.922 1.00 66.13  ? 3902 GLY A N     1 
ATOM   16291 C  CA    . GLY A 1 2685 ? 174.310 130.142 117.594 1.00 56.34  ? 3902 GLY A CA    1 
ATOM   16292 C  C     . GLY A 1 2685 ? 173.746 131.165 116.634 1.00 49.64  ? 3902 GLY A C     1 
ATOM   16293 O  O     . GLY A 1 2685 ? 172.528 131.350 116.555 1.00 48.46  ? 3902 GLY A O     1 
ATOM   16294 N  N     . ILE A 1 2686 ? 174.635 131.847 115.912 1.00 44.91  ? 3903 ILE A N     1 
ATOM   16295 C  CA    . ILE A 1 2686 ? 174.206 132.884 114.980 1.00 39.01  ? 3903 ILE A CA    1 
ATOM   16296 C  C     . ILE A 1 2686 ? 173.427 132.275 113.822 1.00 38.34  ? 3903 ILE A C     1 
ATOM   16297 O  O     . ILE A 1 2686 ? 172.323 132.723 113.494 1.00 38.80  ? 3903 ILE A O     1 
ATOM   16298 C  CB    . ILE A 1 2686 ? 175.422 133.682 114.480 1.00 34.03  ? 3903 ILE A CB    1 
ATOM   16299 C  CG1   . ILE A 1 2686 ? 176.066 134.444 115.634 1.00 30.78  ? 3903 ILE A CG1   1 
ATOM   16300 C  CG2   . ILE A 1 2686 ? 175.015 134.628 113.368 1.00 31.26  ? 3903 ILE A CG2   1 
ATOM   16301 C  CD1   . ILE A 1 2686 ? 177.242 135.277 115.218 1.00 24.19  ? 3903 ILE A CD1   1 
ATOM   16302 N  N     . LEU A 1 2687 ? 173.979 131.228 113.203 1.00 38.09  ? 3904 LEU A N     1 
ATOM   16303 C  CA    . LEU A 1 2687 ? 173.369 130.670 112.001 1.00 37.55  ? 3904 LEU A CA    1 
ATOM   16304 C  C     . LEU A 1 2687 ? 172.040 129.992 112.307 1.00 37.92  ? 3904 LEU A C     1 
ATOM   16305 O  O     . LEU A 1 2687 ? 171.135 130.004 111.466 1.00 40.02  ? 3904 LEU A O     1 
ATOM   16306 C  CB    . LEU A 1 2687 ? 174.334 129.690 111.334 1.00 36.72  ? 3904 LEU A CB    1 
ATOM   16307 C  CG    . LEU A 1 2687 ? 173.899 129.063 110.009 1.00 39.63  ? 3904 LEU A CG    1 
ATOM   16308 C  CD1   . LEU A 1 2687 ? 173.725 130.140 108.953 1.00 36.27  ? 3904 LEU A CD1   1 
ATOM   16309 C  CD2   . LEU A 1 2687 ? 174.904 128.021 109.548 1.00 48.84  ? 3904 LEU A CD2   1 
ATOM   16310 N  N     . ASP A 1 2688 ? 171.900 129.411 113.501 1.00 38.74  ? 3905 ASP A N     1 
ATOM   16311 C  CA    . ASP A 1 2688 ? 170.622 128.824 113.892 1.00 39.47  ? 3905 ASP A CA    1 
ATOM   16312 C  C     . ASP A 1 2688 ? 169.540 129.888 114.011 1.00 38.54  ? 3905 ASP A C     1 
ATOM   16313 O  O     . ASP A 1 2688 ? 168.393 129.666 113.606 1.00 43.75  ? 3905 ASP A O     1 
ATOM   16314 C  CB    . ASP A 1 2688 ? 170.772 128.062 115.209 1.00 47.53  ? 3905 ASP A CB    1 
ATOM   16315 C  CG    . ASP A 1 2688 ? 171.328 126.664 115.015 1.00 53.60  ? 3905 ASP A CG    1 
ATOM   16316 O  OD1   . ASP A 1 2688 ? 170.870 125.966 114.086 1.00 53.38  ? 3905 ASP A OD1   1 
ATOM   16317 O  OD2   . ASP A 1 2688 ? 172.220 126.262 115.791 1.00 56.99  ? 3905 ASP A OD2   1 
ATOM   16318 N  N     . THR A 1 2689 ? 169.890 131.060 114.547 1.00 34.51  ? 3906 THR A N     1 
ATOM   16319 C  CA    . THR A 1 2689 ? 168.906 132.129 114.685 1.00 36.18  ? 3906 THR A CA    1 
ATOM   16320 C  C     . THR A 1 2689 ? 168.545 132.723 113.326 1.00 35.48  ? 3906 THR A C     1 
ATOM   16321 O  O     . THR A 1 2689 ? 167.375 133.042 113.074 1.00 34.89  ? 3906 THR A O     1 
ATOM   16322 C  CB    . THR A 1 2689 ? 169.435 133.203 115.635 1.00 38.42  ? 3906 THR A CB    1 
ATOM   16323 O  OG1   . THR A 1 2689 ? 169.698 132.614 116.914 1.00 40.54  ? 3906 THR A OG1   1 
ATOM   16324 C  CG2   . THR A 1 2689 ? 168.410 134.309 115.823 1.00 37.90  ? 3906 THR A CG2   1 
ATOM   16325 N  N     . VAL A 1 2690 ? 169.528 132.853 112.428 1.00 35.26  ? 3907 VAL A N     1 
ATOM   16326 C  CA    . VAL A 1 2690 ? 169.238 133.297 111.065 1.00 32.77  ? 3907 VAL A CA    1 
ATOM   16327 C  C     . VAL A 1 2690 ? 168.306 132.312 110.374 1.00 32.69  ? 3907 VAL A C     1 
ATOM   16328 O  O     . VAL A 1 2690 ? 167.347 132.711 109.703 1.00 33.44  ? 3907 VAL A O     1 
ATOM   16329 C  CB    . VAL A 1 2690 ? 170.535 133.484 110.255 1.00 31.84  ? 3907 VAL A CB    1 
ATOM   16330 C  CG1   . VAL A 1 2690 ? 170.203 133.966 108.865 1.00 30.10  ? 3907 VAL A CG1   1 
ATOM   16331 C  CG2   . VAL A 1 2690 ? 171.465 134.465 110.920 1.00 28.84  ? 3907 VAL A CG2   1 
ATOM   16332 N  N     . LYS A 1 2691 ? 168.575 131.012 110.523 1.00 35.01  ? 3908 LYS A N     1 
ATOM   16333 C  CA    . LYS A 1 2691 ? 167.734 129.997 109.895 1.00 35.05  ? 3908 LYS A CA    1 
ATOM   16334 C  C     . LYS A 1 2691 ? 166.323 130.009 110.467 1.00 35.58  ? 3908 LYS A C     1 
ATOM   16335 O  O     . LYS A 1 2691 ? 165.348 129.859 109.724 1.00 39.03  ? 3908 LYS A O     1 
ATOM   16336 C  CB    . LYS A 1 2691 ? 168.367 128.616 110.057 1.00 35.90  ? 3908 LYS A CB    1 
ATOM   16337 C  CG    . LYS A 1 2691 ? 169.504 128.346 109.090 1.00 37.24  ? 3908 LYS A CG    1 
ATOM   16338 C  CD    . LYS A 1 2691 ? 170.376 127.199 109.565 1.00 37.77  ? 3908 LYS A CD    1 
ATOM   16339 C  CE    . LYS A 1 2691 ? 170.816 126.328 108.403 1.00 40.53  ? 3908 LYS A CE    1 
ATOM   16340 N  NZ    . LYS A 1 2691 ? 171.859 125.350 108.814 1.00 43.24  ? 3908 LYS A NZ    1 
ATOM   16341 N  N     . ASP A 1 2692 ? 166.193 130.186 111.784 1.00 34.30  ? 3909 ASP A N     1 
ATOM   16342 C  CA    . ASP A 1 2692 ? 164.870 130.258 112.396 1.00 37.35  ? 3909 ASP A CA    1 
ATOM   16343 C  C     . ASP A 1 2692 ? 164.093 131.476 111.908 1.00 41.40  ? 3909 ASP A C     1 
ATOM   16344 O  O     . ASP A 1 2692 ? 162.901 131.373 111.587 1.00 45.03  ? 3909 ASP A O     1 
ATOM   16345 C  CB    . ASP A 1 2692 ? 164.999 130.283 113.918 1.00 41.02  ? 3909 ASP A CB    1 
ATOM   16346 C  CG    . ASP A 1 2692 ? 163.658 130.367 114.613 1.00 48.64  ? 3909 ASP A CG    1 
ATOM   16347 O  OD1   . ASP A 1 2692 ? 162.849 129.427 114.464 1.00 51.32  ? 3909 ASP A OD1   1 
ATOM   16348 O  OD2   . ASP A 1 2692 ? 163.410 131.374 115.309 1.00 52.65  ? 3909 ASP A OD2   1 
ATOM   16349 N  N     . LEU A 1 2693 ? 164.754 132.636 111.836 1.00 38.96  ? 3910 LEU A N     1 
ATOM   16350 C  CA    . LEU A 1 2693 ? 164.088 133.840 111.346 1.00 35.69  ? 3910 LEU A CA    1 
ATOM   16351 C  C     . LEU A 1 2693 ? 163.693 133.697 109.882 1.00 36.33  ? 3910 LEU A C     1 
ATOM   16352 O  O     . LEU A 1 2693 ? 162.598 134.110 109.483 1.00 38.65  ? 3910 LEU A O     1 
ATOM   16353 C  CB    . LEU A 1 2693 ? 164.993 135.058 111.539 1.00 33.95  ? 3910 LEU A CB    1 
ATOM   16354 C  CG    . LEU A 1 2693 ? 165.190 135.561 112.971 1.00 32.41  ? 3910 LEU A CG    1 
ATOM   16355 C  CD1   . LEU A 1 2693 ? 166.175 136.717 112.994 1.00 25.76  ? 3910 LEU A CD1   1 
ATOM   16356 C  CD2   . LEU A 1 2693 ? 163.865 135.970 113.592 1.00 31.36  ? 3910 LEU A CD2   1 
ATOM   16357 N  N     . TRP A 1 2694 ? 164.575 133.115 109.067 1.00 36.26  ? 3911 TRP A N     1 
ATOM   16358 C  CA    . TRP A 1 2694 ? 164.282 132.913 107.652 1.00 38.21  ? 3911 TRP A CA    1 
ATOM   16359 C  C     . TRP A 1 2694 ? 163.129 131.938 107.453 1.00 40.73  ? 3911 TRP A C     1 
ATOM   16360 O  O     . TRP A 1 2694 ? 162.265 132.159 106.597 1.00 41.63  ? 3911 TRP A O     1 
ATOM   16361 C  CB    . TRP A 1 2694 ? 165.539 132.417 106.940 1.00 38.67  ? 3911 TRP A CB    1 
ATOM   16362 C  CG    . TRP A 1 2694 ? 165.450 132.413 105.453 1.00 38.97  ? 3911 TRP A CG    1 
ATOM   16363 C  CD1   . TRP A 1 2694 ? 165.538 131.329 104.632 1.00 42.39  ? 3911 TRP A CD1   1 
ATOM   16364 C  CD2   . TRP A 1 2694 ? 165.269 133.548 104.601 1.00 38.51  ? 3911 TRP A CD2   1 
ATOM   16365 N  NE1   . TRP A 1 2694 ? 165.420 131.717 103.321 1.00 45.68  ? 3911 TRP A NE1   1 
ATOM   16366 C  CE2   . TRP A 1 2694 ? 165.253 133.076 103.275 1.00 43.09  ? 3911 TRP A CE2   1 
ATOM   16367 C  CE3   . TRP A 1 2694 ? 165.115 134.918 104.829 1.00 35.59  ? 3911 TRP A CE3   1 
ATOM   16368 C  CZ2   . TRP A 1 2694 ? 165.092 133.923 102.185 1.00 38.66  ? 3911 TRP A CZ2   1 
ATOM   16369 C  CZ3   . TRP A 1 2694 ? 164.953 135.755 103.746 1.00 33.08  ? 3911 TRP A CZ3   1 
ATOM   16370 C  CH2   . TRP A 1 2694 ? 164.945 135.256 102.443 1.00 32.03  ? 3911 TRP A CH2   1 
ATOM   16371 N  N     . GLY A 1 2695 ? 163.098 130.854 108.231 1.00 39.41  ? 3912 GLY A N     1 
ATOM   16372 C  CA    . GLY A 1 2695 ? 162.023 129.889 108.105 1.00 38.47  ? 3912 GLY A CA    1 
ATOM   16373 C  C     . GLY A 1 2695 ? 160.694 130.404 108.612 1.00 41.63  ? 3912 GLY A C     1 
ATOM   16374 O  O     . GLY A 1 2695 ? 159.640 130.013 108.101 1.00 47.17  ? 3912 GLY A O     1 
ATOM   16375 N  N     . SER A 1 2696 ? 160.716 131.282 109.618 1.00 41.54  ? 3913 SER A N     1 
ATOM   16376 C  CA    . SER A 1 2696 ? 159.469 131.862 110.100 1.00 43.91  ? 3913 SER A CA    1 
ATOM   16377 C  C     . SER A 1 2696 ? 158.884 132.872 109.121 1.00 50.81  ? 3913 SER A C     1 
ATOM   16378 O  O     . SER A 1 2696 ? 157.676 133.126 109.163 1.00 55.33  ? 3913 SER A O     1 
ATOM   16379 C  CB    . SER A 1 2696 ? 159.683 132.518 111.464 1.00 45.44  ? 3913 SER A CB    1 
ATOM   16380 O  OG    . SER A 1 2696 ? 159.735 131.545 112.492 1.00 51.28  ? 3913 SER A OG    1 
ATOM   16381 N  N     . GLN A 1 2697 ? 159.703 133.447 108.244 1.00 50.39  ? 3914 GLN A N     1 
ATOM   16382 C  CA    . GLN A 1 2697 ? 159.224 134.389 107.244 1.00 51.65  ? 3914 GLN A CA    1 
ATOM   16383 C  C     . GLN A 1 2697 ? 158.818 133.661 105.969 1.00 55.75  ? 3914 GLN A C     1 
ATOM   16384 O  O     . GLN A 1 2697 ? 159.430 132.665 105.573 1.00 56.97  ? 3914 GLN A O     1 
ATOM   16385 C  CB    . GLN A 1 2697 ? 160.290 135.438 106.922 1.00 47.81  ? 3914 GLN A CB    1 
ATOM   16386 C  CG    . GLN A 1 2697 ? 160.675 136.310 108.101 1.00 47.34  ? 3914 GLN A CG    1 
ATOM   16387 C  CD    . GLN A 1 2697 ? 159.470 136.823 108.862 1.00 48.76  ? 3914 GLN A CD    1 
ATOM   16388 O  OE1   . GLN A 1 2697 ? 158.689 137.622 108.345 1.00 53.02  ? 3914 GLN A OE1   1 
ATOM   16389 N  NE2   . GLN A 1 2697 ? 159.310 136.363 110.097 1.00 43.63  ? 3914 GLN A NE2   1 
ATOM   16390 N  N     . PHE A 1 2698 ? 157.771 134.175 105.325 1.00 58.79  ? 3915 PHE A N     1 
ATOM   16391 C  CA    . PHE A 1 2698 ? 157.250 133.602 104.091 1.00 60.23  ? 3915 PHE A CA    1 
ATOM   16392 C  C     . PHE A 1 2698 ? 157.541 134.477 102.880 1.00 58.42  ? 3915 PHE A C     1 
ATOM   16393 O  O     . PHE A 1 2698 ? 156.975 134.240 101.806 1.00 58.83  ? 3915 PHE A O     1 
ATOM   16394 C  CB    . PHE A 1 2698 ? 155.743 133.360 104.216 1.00 62.99  ? 3915 PHE A CB    1 
ATOM   16395 C  CG    . PHE A 1 2698 ? 155.333 132.785 105.541 1.00 66.96  ? 3915 PHE A CG    1 
ATOM   16396 C  CD1   . PHE A 1 2698 ? 155.470 131.430 105.794 1.00 65.09  ? 3915 PHE A CD1   1 
ATOM   16397 C  CD2   . PHE A 1 2698 ? 154.815 133.600 106.536 1.00 67.17  ? 3915 PHE A CD2   1 
ATOM   16398 C  CE1   . PHE A 1 2698 ? 155.097 130.897 107.013 1.00 65.15  ? 3915 PHE A CE1   1 
ATOM   16399 C  CE2   . PHE A 1 2698 ? 154.441 133.073 107.757 1.00 72.56  ? 3915 PHE A CE2   1 
ATOM   16400 C  CZ    . PHE A 1 2698 ? 154.581 131.720 107.996 1.00 70.87  ? 3915 PHE A CZ    1 
ATOM   16401 N  N     . PHE A 1 2699 ? 158.403 135.477 103.024 1.00 57.96  ? 3916 PHE A N     1 
ATOM   16402 C  CA    . PHE A 1 2699 ? 158.728 136.385 101.931 1.00 54.96  ? 3916 PHE A CA    1 
ATOM   16403 C  C     . PHE A 1 2699 ? 160.168 136.866 102.045 1.00 49.06  ? 3916 PHE A C     1 
ATOM   16404 O  O     . PHE A 1 2699 ? 161.000 136.213 102.675 1.00 48.84  ? 3916 PHE A O     1 
ATOM   16405 C  CB    . PHE A 1 2699 ? 157.765 137.578 101.913 1.00 53.60  ? 3916 PHE A CB    1 
ATOM   16406 C  CG    . PHE A 1 2699 ? 157.902 138.493 103.099 1.00 53.70  ? 3916 PHE A CG    1 
ATOM   16407 C  CD1   . PHE A 1 2699 ? 157.319 138.169 104.314 1.00 54.69  ? 3916 PHE A CD1   1 
ATOM   16408 C  CD2   . PHE A 1 2699 ? 158.602 139.685 102.997 1.00 46.91  ? 3916 PHE A CD2   1 
ATOM   16409 C  CE1   . PHE A 1 2699 ? 157.440 139.006 105.404 1.00 45.91  ? 3916 PHE A CE1   1 
ATOM   16410 C  CE2   . PHE A 1 2699 ? 158.725 140.527 104.084 1.00 42.22  ? 3916 PHE A CE2   1 
ATOM   16411 C  CZ    . PHE A 1 2699 ? 158.145 140.184 105.289 1.00 40.67  ? 3916 PHE A CZ    1 
ATOM   16412 N  N     . ILE A 1 2703 ? 155.121 140.375 100.815 1.00 60.13  ? 3920 ILE A N     1 
ATOM   16413 C  CA    . ILE A 1 2703 ? 155.547 139.963 99.485  1.00 62.77  ? 3920 ILE A CA    1 
ATOM   16414 C  C     . ILE A 1 2703 ? 155.524 141.160 98.543  1.00 64.31  ? 3920 ILE A C     1 
ATOM   16415 O  O     . ILE A 1 2703 ? 154.455 141.629 98.149  1.00 65.02  ? 3920 ILE A O     1 
ATOM   16416 C  CB    . ILE A 1 2703 ? 154.665 138.821 98.940  1.00 67.93  ? 3920 ILE A CB    1 
ATOM   16417 C  CG1   . ILE A 1 2703 ? 154.772 137.581 99.830  1.00 66.19  ? 3920 ILE A CG1   1 
ATOM   16418 C  CG2   . ILE A 1 2703 ? 155.060 138.475 97.512  1.00 67.11  ? 3920 ILE A CG2   1 
ATOM   16419 C  CD1   . ILE A 1 2703 ? 153.587 137.379 100.753 1.00 62.61  ? 3920 ILE A CD1   1 
ATOM   16420 N  N     . SER A 1 2704 ? 156.708 141.667 98.193  1.00 64.54  ? 3921 SER A N     1 
ATOM   16421 C  CA    . SER A 1 2704 ? 156.809 142.779 97.245  1.00 63.05  ? 3921 SER A CA    1 
ATOM   16422 C  C     . SER A 1 2704 ? 158.124 142.622 96.478  1.00 57.58  ? 3921 SER A C     1 
ATOM   16423 O  O     . SER A 1 2704 ? 159.170 143.108 96.911  1.00 51.43  ? 3921 SER A O     1 
ATOM   16424 C  CB    . SER A 1 2704 ? 156.730 144.123 97.954  1.00 55.17  ? 3921 SER A CB    1 
ATOM   16425 O  OG    . SER A 1 2704 ? 155.427 144.361 98.454  1.00 55.95  ? 3921 SER A OG    1 
ATOM   16426 N  N     . GLY A 1 2705 ? 158.046 141.960 95.324  1.00 58.05  ? 3922 GLY A N     1 
ATOM   16427 C  CA    . GLY A 1 2705 ? 159.213 141.806 94.478  1.00 53.14  ? 3922 GLY A CA    1 
ATOM   16428 C  C     . GLY A 1 2705 ? 160.283 140.928 95.108  1.00 50.01  ? 3922 GLY A C     1 
ATOM   16429 O  O     . GLY A 1 2705 ? 160.007 140.031 95.909  1.00 46.32  ? 3922 GLY A O     1 
ATOM   16430 N  N     . VAL A 1 2706 ? 161.531 141.203 94.734  1.00 49.85  ? 3923 VAL A N     1 
ATOM   16431 C  CA    . VAL A 1 2706 ? 162.677 140.444 95.221  1.00 48.19  ? 3923 VAL A CA    1 
ATOM   16432 C  C     . VAL A 1 2706 ? 163.378 141.234 96.318  1.00 43.10  ? 3923 VAL A C     1 
ATOM   16433 O  O     . VAL A 1 2706 ? 164.035 140.658 97.195  1.00 40.21  ? 3923 VAL A O     1 
ATOM   16434 C  CB    . VAL A 1 2706 ? 163.647 140.108 94.073  1.00 46.93  ? 3923 VAL A CB    1 
ATOM   16435 C  CG1   . VAL A 1 2706 ? 163.020 139.100 93.135  1.00 51.97  ? 3923 VAL A CG1   1 
ATOM   16436 C  CG2   . VAL A 1 2706 ? 164.032 141.365 93.309  1.00 44.48  ? 3923 VAL A CG2   1 
ATOM   16437 N  N     . TRP A 1 2707 ? 163.236 142.561 96.279  1.00 39.98  ? 3924 TRP A N     1 
ATOM   16438 C  CA    . TRP A 1 2707 ? 163.955 143.405 97.225  1.00 35.34  ? 3924 TRP A CA    1 
ATOM   16439 C  C     . TRP A 1 2707 ? 163.382 143.301 98.630  1.00 33.54  ? 3924 TRP A C     1 
ATOM   16440 O  O     . TRP A 1 2707 ? 164.126 143.443 99.603  1.00 34.67  ? 3924 TRP A O     1 
ATOM   16441 C  CB    . TRP A 1 2707 ? 163.947 144.854 96.751  1.00 33.50  ? 3924 TRP A CB    1 
ATOM   16442 C  CG    . TRP A 1 2707 ? 165.049 145.160 95.796  1.00 36.99  ? 3924 TRP A CG    1 
ATOM   16443 C  CD1   . TRP A 1 2707 ? 164.960 145.233 94.440  1.00 41.89  ? 3924 TRP A CD1   1 
ATOM   16444 C  CD2   . TRP A 1 2707 ? 166.417 145.426 96.125  1.00 36.97  ? 3924 TRP A CD2   1 
ATOM   16445 N  NE1   . TRP A 1 2707 ? 166.187 145.535 93.901  1.00 46.30  ? 3924 TRP A NE1   1 
ATOM   16446 C  CE2   . TRP A 1 2707 ? 167.098 145.658 94.916  1.00 42.12  ? 3924 TRP A CE2   1 
ATOM   16447 C  CE3   . TRP A 1 2707 ? 167.130 145.493 97.324  1.00 33.51  ? 3924 TRP A CE3   1 
ATOM   16448 C  CZ2   . TRP A 1 2707 ? 168.458 145.952 94.871  1.00 43.49  ? 3924 TRP A CZ2   1 
ATOM   16449 C  CZ3   . TRP A 1 2707 ? 168.480 145.785 97.278  1.00 32.01  ? 3924 TRP A CZ3   1 
ATOM   16450 C  CH2   . TRP A 1 2707 ? 169.130 146.011 96.060  1.00 39.29  ? 3924 TRP A CH2   1 
ATOM   16451 N  N     . SER A 1 2708 ? 162.077 143.053 98.762  1.00 33.99  ? 3925 SER A N     1 
ATOM   16452 C  CA    . SER A 1 2708 ? 161.510 142.813 100.086 1.00 34.12  ? 3925 SER A CA    1 
ATOM   16453 C  C     . SER A 1 2708 ? 162.089 141.550 100.708 1.00 35.23  ? 3925 SER A C     1 
ATOM   16454 O  O     . SER A 1 2708 ? 162.420 141.530 101.899 1.00 37.49  ? 3925 SER A O     1 
ATOM   16455 C  CB    . SER A 1 2708 ? 159.988 142.718 100.002 1.00 39.68  ? 3925 SER A CB    1 
ATOM   16456 O  OG    . SER A 1 2708 ? 159.439 142.272 101.229 1.00 39.69  ? 3925 SER A OG    1 
ATOM   16457 N  N     . VAL A 1 2709 ? 162.243 140.492 99.909  1.00 33.98  ? 3926 VAL A N     1 
ATOM   16458 C  CA    . VAL A 1 2709 ? 162.835 139.253 100.403 1.00 31.57  ? 3926 VAL A CA    1 
ATOM   16459 C  C     . VAL A 1 2709 ? 164.305 139.460 100.754 1.00 28.98  ? 3926 VAL A C     1 
ATOM   16460 O  O     . VAL A 1 2709 ? 164.789 138.964 101.780 1.00 30.46  ? 3926 VAL A O     1 
ATOM   16461 C  CB    . VAL A 1 2709 ? 162.648 138.135 99.361  1.00 35.65  ? 3926 VAL A CB    1 
ATOM   16462 C  CG1   . VAL A 1 2709 ? 163.008 136.793 99.950  1.00 41.11  ? 3926 VAL A CG1   1 
ATOM   16463 C  CG2   . VAL A 1 2709 ? 161.217 138.123 98.853  1.00 42.84  ? 3926 VAL A CG2   1 
ATOM   16464 N  N     . TYR A 1 2710 ? 165.035 140.197 99.912  1.00 27.07  ? 3927 TYR A N     1 
ATOM   16465 C  CA    . TYR A 1 2710 ? 166.442 140.482 100.188 1.00 25.90  ? 3927 TYR A CA    1 
ATOM   16466 C  C     . TYR A 1 2710 ? 166.609 141.296 101.468 1.00 27.02  ? 3927 TYR A C     1 
ATOM   16467 O  O     . TYR A 1 2710 ? 167.500 141.018 102.282 1.00 27.37  ? 3927 TYR A O     1 
ATOM   16468 C  CB    . TYR A 1 2710 ? 167.055 141.214 98.996  1.00 27.74  ? 3927 TYR A CB    1 
ATOM   16469 C  CG    . TYR A 1 2710 ? 168.491 141.639 99.181  1.00 24.89  ? 3927 TYR A CG    1 
ATOM   16470 C  CD1   . TYR A 1 2710 ? 169.522 140.716 99.124  1.00 27.52  ? 3927 TYR A CD1   1 
ATOM   16471 C  CD2   . TYR A 1 2710 ? 168.815 142.970 99.392  1.00 26.72  ? 3927 TYR A CD2   1 
ATOM   16472 C  CE1   . TYR A 1 2710 ? 170.836 141.105 99.282  1.00 27.04  ? 3927 TYR A CE1   1 
ATOM   16473 C  CE2   . TYR A 1 2710 ? 170.123 143.368 99.552  1.00 26.89  ? 3927 TYR A CE2   1 
ATOM   16474 C  CZ    . TYR A 1 2710 ? 171.130 142.432 99.497  1.00 25.24  ? 3927 TYR A CZ    1 
ATOM   16475 O  OH    . TYR A 1 2710 ? 172.436 142.830 99.657  1.00 29.73  ? 3927 TYR A OH    1 
ATOM   16476 N  N     . CYS A 1 2711 ? 165.751 142.299 101.670 1.00 27.59  ? 3928 CYS A N     1 
ATOM   16477 C  CA    . CYS A 1 2711 ? 165.829 143.107 102.880 1.00 22.89  ? 3928 CYS A CA    1 
ATOM   16478 C  C     . CYS A 1 2711 ? 165.397 142.320 104.108 1.00 23.94  ? 3928 CYS A C     1 
ATOM   16479 O  O     . CYS A 1 2711 ? 165.921 142.555 105.199 1.00 27.99  ? 3928 CYS A O     1 
ATOM   16480 C  CB    . CYS A 1 2711 ? 164.982 144.367 102.724 1.00 23.04  ? 3928 CYS A CB    1 
ATOM   16481 S  SG    . CYS A 1 2711 ? 165.730 145.629 101.670 1.00 36.03  ? 3928 CYS A SG    1 
ATOM   16482 N  N     . THR A 1 2712 ? 164.460 141.382 103.957 1.00 21.79  ? 3929 THR A N     1 
ATOM   16483 C  CA    . THR A 1 2712 ? 164.121 140.501 105.070 1.00 22.05  ? 3929 THR A CA    1 
ATOM   16484 C  C     . THR A 1 2712 ? 165.294 139.599 105.434 1.00 25.10  ? 3929 THR A C     1 
ATOM   16485 O  O     . THR A 1 2712 ? 165.535 139.334 106.617 1.00 24.30  ? 3929 THR A O     1 
ATOM   16486 C  CB    . THR A 1 2712 ? 162.891 139.665 104.727 1.00 26.89  ? 3929 THR A CB    1 
ATOM   16487 O  OG1   . THR A 1 2712 ? 161.904 140.501 104.113 1.00 32.47  ? 3929 THR A OG1   1 
ATOM   16488 C  CG2   . THR A 1 2712 ? 162.307 139.042 105.984 1.00 26.96  ? 3929 THR A CG2   1 
ATOM   16489 N  N     . PHE A 1 2713 ? 166.035 139.125 104.430 1.00 27.27  ? 3930 PHE A N     1 
ATOM   16490 C  CA    . PHE A 1 2713 ? 167.242 138.344 104.693 1.00 25.43  ? 3930 PHE A CA    1 
ATOM   16491 C  C     . PHE A 1 2713 ? 168.273 139.169 105.455 1.00 24.04  ? 3930 PHE A C     1 
ATOM   16492 O  O     . PHE A 1 2713 ? 168.849 138.708 106.454 1.00 30.88  ? 3930 PHE A O     1 
ATOM   16493 C  CB    . PHE A 1 2713 ? 167.824 137.843 103.372 1.00 28.21  ? 3930 PHE A CB    1 
ATOM   16494 C  CG    . PHE A 1 2713 ? 168.810 136.722 103.521 1.00 33.62  ? 3930 PHE A CG    1 
ATOM   16495 C  CD1   . PHE A 1 2713 ? 168.442 135.534 104.126 1.00 36.94  ? 3930 PHE A CD1   1 
ATOM   16496 C  CD2   . PHE A 1 2713 ? 170.099 136.847 103.032 1.00 34.45  ? 3930 PHE A CD2   1 
ATOM   16497 C  CE1   . PHE A 1 2713 ? 169.343 134.497 104.257 1.00 37.24  ? 3930 PHE A CE1   1 
ATOM   16498 C  CE2   . PHE A 1 2713 ? 171.003 135.811 103.158 1.00 36.45  ? 3930 PHE A CE2   1 
ATOM   16499 C  CZ    . PHE A 1 2713 ? 170.624 134.635 103.770 1.00 36.26  ? 3930 PHE A CZ    1 
ATOM   16500 N  N     . LEU A 1 2714 ? 168.506 140.402 104.997 1.00 18.10  ? 3931 LEU A N     1 
ATOM   16501 C  CA    . LEU A 1 2714 ? 169.454 141.284 105.672 1.00 14.24  ? 3931 LEU A CA    1 
ATOM   16502 C  C     . LEU A 1 2714 ? 169.017 141.581 107.100 1.00 13.94  ? 3931 LEU A C     1 
ATOM   16503 O  O     . LEU A 1 2714 ? 169.841 141.585 108.022 1.00 14.48  ? 3931 LEU A O     1 
ATOM   16504 C  CB    . LEU A 1 2714 ? 169.612 142.581 104.884 1.00 15.49  ? 3931 LEU A CB    1 
ATOM   16505 C  CG    . LEU A 1 2714 ? 170.629 142.553 103.750 1.00 17.11  ? 3931 LEU A CG    1 
ATOM   16506 C  CD1   . LEU A 1 2714 ? 170.738 143.921 103.112 1.00 17.85  ? 3931 LEU A CD1   1 
ATOM   16507 C  CD2   . LEU A 1 2714 ? 171.964 142.102 104.285 1.00 15.54  ? 3931 LEU A CD2   1 
ATOM   16508 N  N     . LEU A 1 2715 ? 167.723 141.826 107.302 1.00 14.98  ? 3932 LEU A N     1 
ATOM   16509 C  CA    . LEU A 1 2715 ? 167.218 142.122 108.636 1.00 15.87  ? 3932 LEU A CA    1 
ATOM   16510 C  C     . LEU A 1 2715 ? 167.328 140.913 109.554 1.00 19.88  ? 3932 LEU A C     1 
ATOM   16511 O  O     . LEU A 1 2715 ? 167.627 141.063 110.743 1.00 22.67  ? 3932 LEU A O     1 
ATOM   16512 C  CB    . LEU A 1 2715 ? 165.771 142.604 108.552 1.00 14.17  ? 3932 LEU A CB    1 
ATOM   16513 C  CG    . LEU A 1 2715 ? 165.038 142.743 109.883 1.00 13.54  ? 3932 LEU A CG    1 
ATOM   16514 C  CD1   . LEU A 1 2715 ? 165.722 143.777 110.756 1.00 15.27  ? 3932 LEU A CD1   1 
ATOM   16515 C  CD2   . LEU A 1 2715 ? 163.598 143.109 109.648 1.00 19.42  ? 3932 LEU A CD2   1 
ATOM   16516 N  N     . SER A 1 2716 ? 167.084 139.709 109.031 1.00 19.26  ? 3933 SER A N     1 
ATOM   16517 C  CA    . SER A 1 2716 ? 167.237 138.513 109.853 1.00 16.04  ? 3933 SER A CA    1 
ATOM   16518 C  C     . SER A 1 2716 ? 168.686 138.323 110.279 1.00 17.35  ? 3933 SER A C     1 
ATOM   16519 O  O     . SER A 1 2716 ? 168.960 138.019 111.449 1.00 20.38  ? 3933 SER A O     1 
ATOM   16520 C  CB    . SER A 1 2716 ? 166.728 137.285 109.101 1.00 18.56  ? 3933 SER A CB    1 
ATOM   16521 O  OG    . SER A 1 2716 ? 167.210 137.266 107.772 1.00 18.71  ? 3933 SER A OG    1 
ATOM   16522 N  N     . TRP A 1 2717 ? 169.630 138.526 109.350 1.00 17.74  ? 3934 TRP A N     1 
ATOM   16523 C  CA    . TRP A 1 2717 ? 171.041 138.426 109.720 1.00 19.92  ? 3934 TRP A CA    1 
ATOM   16524 C  C     . TRP A 1 2717 ? 171.416 139.474 110.760 1.00 19.20  ? 3934 TRP A C     1 
ATOM   16525 O  O     . TRP A 1 2717 ? 172.111 139.168 111.736 1.00 19.35  ? 3934 TRP A O     1 
ATOM   16526 C  CB    . TRP A 1 2717 ? 171.946 138.568 108.496 1.00 17.79  ? 3934 TRP A CB    1 
ATOM   16527 C  CG    . TRP A 1 2717 ? 172.253 137.276 107.807 1.00 24.82  ? 3934 TRP A CG    1 
ATOM   16528 C  CD1   . TRP A 1 2717 ? 171.451 136.603 106.938 1.00 27.87  ? 3934 TRP A CD1   1 
ATOM   16529 C  CD2   . TRP A 1 2717 ? 173.428 136.470 107.974 1.00 30.20  ? 3934 TRP A CD2   1 
ATOM   16530 N  NE1   . TRP A 1 2717 ? 172.066 135.447 106.523 1.00 28.32  ? 3934 TRP A NE1   1 
ATOM   16531 C  CE2   . TRP A 1 2717 ? 173.278 135.339 107.150 1.00 28.94  ? 3934 TRP A CE2   1 
ATOM   16532 C  CE3   . TRP A 1 2717 ? 174.594 136.600 108.733 1.00 33.32  ? 3934 TRP A CE3   1 
ATOM   16533 C  CZ2   . TRP A 1 2717 ? 174.251 134.346 107.061 1.00 29.38  ? 3934 TRP A CZ2   1 
ATOM   16534 C  CZ3   . TRP A 1 2717 ? 175.561 135.615 108.641 1.00 30.73  ? 3934 TRP A CZ3   1 
ATOM   16535 C  CH2   . TRP A 1 2717 ? 175.382 134.503 107.812 1.00 31.11  ? 3934 TRP A CH2   1 
ATOM   16536 N  N     . PHE A 1 2718 ? 170.952 140.714 110.576 1.00 17.43  ? 3935 PHE A N     1 
ATOM   16537 C  CA    . PHE A 1 2718 ? 171.274 141.781 111.520 1.00 14.83  ? 3935 PHE A CA    1 
ATOM   16538 C  C     . PHE A 1 2718 ? 170.678 141.517 112.897 1.00 15.03  ? 3935 PHE A C     1 
ATOM   16539 O  O     . PHE A 1 2718 ? 171.334 141.755 113.917 1.00 16.07  ? 3935 PHE A O     1 
ATOM   16540 C  CB    . PHE A 1 2718 ? 170.782 143.123 110.986 1.00 12.04  ? 3935 PHE A CB    1 
ATOM   16541 C  CG    . PHE A 1 2718 ? 170.897 144.239 111.975 1.00 11.15  ? 3935 PHE A CG    1 
ATOM   16542 C  CD1   . PHE A 1 2718 ? 172.125 144.794 112.268 1.00 12.82  ? 3935 PHE A CD1   1 
ATOM   16543 C  CD2   . PHE A 1 2718 ? 169.778 144.728 112.620 1.00 12.79  ? 3935 PHE A CD2   1 
ATOM   16544 C  CE1   . PHE A 1 2718 ? 172.233 145.820 113.182 1.00 13.55  ? 3935 PHE A CE1   1 
ATOM   16545 C  CE2   . PHE A 1 2718 ? 169.888 145.750 113.535 1.00 12.79  ? 3935 PHE A CE2   1 
ATOM   16546 C  CZ    . PHE A 1 2718 ? 171.114 146.291 113.818 1.00 11.89  ? 3935 PHE A CZ    1 
ATOM   16547 N  N     . HIS A 1 2719 ? 169.430 141.048 112.947 1.00 15.56  ? 3936 HIS A N     1 
ATOM   16548 C  CA    . HIS A 1 2719 ? 168.788 140.766 114.224 1.00 15.60  ? 3936 HIS A CA    1 
ATOM   16549 C  C     . HIS A 1 2719 ? 169.486 139.626 114.950 1.00 19.74  ? 3936 HIS A C     1 
ATOM   16550 O  O     . HIS A 1 2719 ? 169.680 139.690 116.170 1.00 20.81  ? 3936 HIS A O     1 
ATOM   16551 C  CB    . HIS A 1 2719 ? 167.310 140.448 114.008 1.00 14.59  ? 3936 HIS A CB    1 
ATOM   16552 C  CG    . HIS A 1 2719 ? 166.552 140.200 115.273 1.00 12.99  ? 3936 HIS A CG    1 
ATOM   16553 N  ND1   . HIS A 1 2719 ? 165.780 141.168 115.877 1.00 14.12  ? 3936 HIS A ND1   1 
ATOM   16554 C  CD2   . HIS A 1 2719 ? 166.433 139.092 116.041 1.00 15.42  ? 3936 HIS A CD2   1 
ATOM   16555 C  CE1   . HIS A 1 2719 ? 165.226 140.670 116.967 1.00 15.19  ? 3936 HIS A CE1   1 
ATOM   16556 N  NE2   . HIS A 1 2719 ? 165.606 139.412 117.089 1.00 16.72  ? 3936 HIS A NE2   1 
ATOM   16557 N  N     . ALA A 1 2720 ? 169.881 138.578 114.220 1.00 19.93  ? 3937 ALA A N     1 
ATOM   16558 C  CA    . ALA A 1 2720 ? 170.625 137.493 114.851 1.00 17.34  ? 3937 ALA A CA    1 
ATOM   16559 C  C     . ALA A 1 2720 ? 171.977 137.971 115.364 1.00 17.61  ? 3937 ALA A C     1 
ATOM   16560 O  O     . ALA A 1 2720 ? 172.390 137.606 116.472 1.00 18.68  ? 3937 ALA A O     1 
ATOM   16561 C  CB    . ALA A 1 2720 ? 170.803 136.340 113.872 1.00 19.91  ? 3937 ALA A CB    1 
ATOM   16562 N  N     . LEU A 1 2721 ? 172.674 138.800 114.580 1.00 14.94  ? 3938 LEU A N     1 
ATOM   16563 C  CA    . LEU A 1 2721 ? 173.969 139.314 115.015 1.00 13.05  ? 3938 LEU A CA    1 
ATOM   16564 C  C     . LEU A 1 2721 ? 173.836 140.184 116.259 1.00 15.34  ? 3938 LEU A C     1 
ATOM   16565 O  O     . LEU A 1 2721 ? 174.635 140.065 117.194 1.00 15.68  ? 3938 LEU A O     1 
ATOM   16566 C  CB    . LEU A 1 2721 ? 174.632 140.101 113.886 1.00 12.72  ? 3938 LEU A CB    1 
ATOM   16567 C  CG    . LEU A 1 2721 ? 175.206 139.314 112.706 1.00 17.54  ? 3938 LEU A CG    1 
ATOM   16568 C  CD1   . LEU A 1 2721 ? 175.956 140.239 111.762 1.00 17.56  ? 3938 LEU A CD1   1 
ATOM   16569 C  CD2   . LEU A 1 2721 ? 176.108 138.197 113.184 1.00 21.48  ? 3938 LEU A CD2   1 
ATOM   16570 N  N     . ILE A 1 2722 ? 172.823 141.053 116.300 1.00 16.60  ? 3939 ILE A N     1 
ATOM   16571 C  CA    . ILE A 1 2722 ? 172.678 141.942 117.449 1.00 15.41  ? 3939 ILE A CA    1 
ATOM   16572 C  C     . ILE A 1 2722 ? 172.203 141.173 118.680 1.00 16.90  ? 3939 ILE A C     1 
ATOM   16573 O  O     . ILE A 1 2722 ? 172.618 141.481 119.804 1.00 20.59  ? 3939 ILE A O     1 
ATOM   16574 C  CB    . ILE A 1 2722 ? 171.764 143.139 117.103 1.00 12.68  ? 3939 ILE A CB    1 
ATOM   16575 C  CG1   . ILE A 1 2722 ? 172.013 144.299 118.067 1.00 11.62  ? 3939 ILE A CG1   1 
ATOM   16576 C  CG2   . ILE A 1 2722 ? 170.291 142.764 117.097 1.00 15.63  ? 3939 ILE A CG2   1 
ATOM   16577 C  CD1   . ILE A 1 2722 ? 173.251 145.095 117.769 1.00 13.65  ? 3939 ILE A CD1   1 
ATOM   16578 N  N     . THR A 1 2723 ? 171.379 140.134 118.500 1.00 16.07  ? 3940 THR A N     1 
ATOM   16579 C  CA    . THR A 1 2723 ? 170.964 139.331 119.644 1.00 18.26  ? 3940 THR A CA    1 
ATOM   16580 C  C     . THR A 1 2723 ? 172.127 138.507 120.186 1.00 21.03  ? 3940 THR A C     1 
ATOM   16581 O  O     . THR A 1 2723 ? 172.242 138.323 121.403 1.00 24.83  ? 3940 THR A O     1 
ATOM   16582 C  CB    . THR A 1 2723 ? 169.791 138.431 119.250 1.00 24.28  ? 3940 THR A CB    1 
ATOM   16583 O  OG1   . THR A 1 2723 ? 168.719 139.239 118.754 1.00 25.46  ? 3940 THR A OG1   1 
ATOM   16584 C  CG2   . THR A 1 2723 ? 169.277 137.657 120.452 1.00 29.60  ? 3940 THR A CG2   1 
ATOM   16585 N  N     . ALA A 1 2724 ? 173.012 138.031 119.306 1.00 18.29  ? 3941 ALA A N     1 
ATOM   16586 C  CA    . ALA A 1 2724 ? 174.207 137.334 119.768 1.00 19.36  ? 3941 ALA A CA    1 
ATOM   16587 C  C     . ALA A 1 2724 ? 175.191 138.283 120.441 1.00 18.89  ? 3941 ALA A C     1 
ATOM   16588 O  O     . ALA A 1 2724 ? 175.881 137.887 121.386 1.00 22.51  ? 3941 ALA A O     1 
ATOM   16589 C  CB    . ALA A 1 2724 ? 174.879 136.614 118.601 1.00 21.55  ? 3941 ALA A CB    1 
ATOM   16590 N  N     . ARG A 1 2725 ? 175.277 139.530 119.970 1.00 15.92  ? 3942 ARG A N     1 
ATOM   16591 C  CA    . ARG A 1 2725 ? 176.169 140.499 120.600 1.00 14.38  ? 3942 ARG A CA    1 
ATOM   16592 C  C     . ARG A 1 2725 ? 175.632 140.969 121.945 1.00 14.89  ? 3942 ARG A C     1 
ATOM   16593 O  O     . ARG A 1 2725 ? 176.410 141.387 122.809 1.00 15.73  ? 3942 ARG A O     1 
ATOM   16594 C  CB    . ARG A 1 2725 ? 176.389 141.692 119.671 1.00 11.94  ? 3942 ARG A CB    1 
ATOM   16595 C  CG    . ARG A 1 2725 ? 177.561 142.569 120.062 1.00 9.96   ? 3942 ARG A CG    1 
ATOM   16596 C  CD    . ARG A 1 2725 ? 177.632 143.816 119.214 1.00 11.18  ? 3942 ARG A CD    1 
ATOM   16597 N  NE    . ARG A 1 2725 ? 178.865 144.555 119.456 1.00 13.77  ? 3942 ARG A NE    1 
ATOM   16598 C  CZ    . ARG A 1 2725 ? 179.765 144.833 118.524 1.00 15.64  ? 3942 ARG A CZ    1 
ATOM   16599 N  NH1   . ARG A 1 2725 ? 179.603 144.447 117.270 1.00 14.75  ? 3942 ARG A NH1   1 
ATOM   16600 N  NH2   . ARG A 1 2725 ? 180.856 145.516 118.859 1.00 17.72  ? 3942 ARG A NH2   1 
ATOM   16601 N  N     . THR A 1 2726 ? 174.312 140.917 122.135 1.00 15.11  ? 3943 THR A N     1 
ATOM   16602 C  CA    . THR A 1 2726 ? 173.723 141.342 123.403 1.00 16.32  ? 3943 THR A CA    1 
ATOM   16603 C  C     . THR A 1 2726 ? 174.192 140.468 124.562 1.00 20.59  ? 3943 THR A C     1 
ATOM   16604 O  O     . THR A 1 2726 ? 174.412 140.966 125.673 1.00 22.56  ? 3943 THR A O     1 
ATOM   16605 C  CB    . THR A 1 2726 ? 172.197 141.325 123.292 1.00 18.39  ? 3943 THR A CB    1 
ATOM   16606 O  OG1   . THR A 1 2726 ? 171.786 142.219 122.252 1.00 20.94  ? 3943 THR A OG1   1 
ATOM   16607 C  CG2   . THR A 1 2726 ? 171.549 141.757 124.591 1.00 19.96  ? 3943 THR A CG2   1 
ATOM   16608 N  N     . ARG A 1 2727 ? 174.379 139.167 124.315 1.00 22.38  ? 3944 ARG A N     1 
ATOM   16609 C  CA    . ARG A 1 2727 ? 174.658 138.215 125.389 1.00 21.54  ? 3944 ARG A CA    1 
ATOM   16610 C  C     . ARG A 1 2727 ? 175.981 138.479 126.097 1.00 24.32  ? 3944 ARG A C     1 
ATOM   16611 O  O     . ARG A 1 2727 ? 176.133 138.088 127.259 1.00 29.78  ? 3944 ARG A O     1 
ATOM   16612 C  CB    . ARG A 1 2727 ? 174.652 136.790 124.838 1.00 19.23  ? 3944 ARG A CB    1 
ATOM   16613 C  CG    . ARG A 1 2727 ? 173.459 136.472 123.960 1.00 20.57  ? 3944 ARG A CG    1 
ATOM   16614 C  CD    . ARG A 1 2727 ? 173.381 134.988 123.663 1.00 33.03  ? 3944 ARG A CD    1 
ATOM   16615 N  NE    . ARG A 1 2727 ? 172.444 134.694 122.586 1.00 38.93  ? 3944 ARG A NE    1 
ATOM   16616 C  CZ    . ARG A 1 2727 ? 171.133 134.582 122.744 1.00 40.14  ? 3944 ARG A CZ    1 
ATOM   16617 N  NH1   . ARG A 1 2727 ? 170.565 134.736 123.929 1.00 39.47  ? 3944 ARG A NH1   1 
ATOM   16618 N  NH2   . ARG A 1 2727 ? 170.373 134.310 121.688 1.00 38.29  ? 3944 ARG A NH2   1 
ATOM   16619 N  N     . LEU A 1 2728 ? 176.936 139.130 125.437 1.00 22.63  ? 3945 LEU A N     1 
ATOM   16620 C  CA    . LEU A 1 2728 ? 178.224 139.452 126.049 1.00 23.36  ? 3945 LEU A CA    1 
ATOM   16621 C  C     . LEU A 1 2728 ? 178.097 140.814 126.721 1.00 24.96  ? 3945 LEU A C     1 
ATOM   16622 O  O     . LEU A 1 2728 ? 178.259 141.854 126.080 1.00 26.24  ? 3945 LEU A O     1 
ATOM   16623 C  CB    . LEU A 1 2728 ? 179.337 139.431 125.009 1.00 19.78  ? 3945 LEU A CB    1 
ATOM   16624 C  CG    . LEU A 1 2728 ? 179.216 138.362 123.923 1.00 18.16  ? 3945 LEU A CG    1 
ATOM   16625 C  CD1   . LEU A 1 2728 ? 180.304 138.540 122.888 1.00 19.42  ? 3945 LEU A CD1   1 
ATOM   16626 C  CD2   . LEU A 1 2728 ? 179.289 136.971 124.525 1.00 22.99  ? 3945 LEU A CD2   1 
ATOM   16627 N  N     . VAL A 1 2729 ? 177.811 140.800 128.019 1.00 24.11  ? 3946 VAL A N     1 
ATOM   16628 C  CA    . VAL A 1 2729 ? 177.451 141.992 128.789 1.00 26.27  ? 3946 VAL A CA    1 
ATOM   16629 C  C     . VAL A 1 2729 ? 178.542 143.064 128.828 1.00 28.27  ? 3946 VAL A C     1 
ATOM   16630 O  O     . VAL A 1 2729 ? 178.237 144.223 128.516 1.00 32.53  ? 3946 VAL A O     1 
ATOM   16631 C  CB    . VAL A 1 2729 ? 177.025 141.598 130.215 1.00 26.21  ? 3946 VAL A CB    1 
ATOM   16632 C  CG1   . VAL A 1 2729 ? 176.846 142.831 131.087 1.00 24.00  ? 3946 VAL A CG1   1 
ATOM   16633 C  CG2   . VAL A 1 2729 ? 175.744 140.783 130.174 1.00 25.88  ? 3946 VAL A CG2   1 
ATOM   16634 N  N     . PRO A 1 2730 ? 179.820 142.776 129.190 1.00 27.07  ? 3947 PRO A N     1 
ATOM   16635 C  CA    . PRO A 1 2730 ? 180.758 143.894 129.363 1.00 29.51  ? 3947 PRO A CA    1 
ATOM   16636 C  C     . PRO A 1 2730 ? 181.351 144.421 128.064 1.00 32.40  ? 3947 PRO A C     1 
ATOM   16637 O  O     . PRO A 1 2730 ? 181.761 145.584 128.001 1.00 32.63  ? 3947 PRO A O     1 
ATOM   16638 C  CB    . PRO A 1 2730 ? 181.843 143.298 130.265 1.00 37.10  ? 3947 PRO A CB    1 
ATOM   16639 C  CG    . PRO A 1 2730 ? 181.886 141.879 129.885 1.00 39.07  ? 3947 PRO A CG    1 
ATOM   16640 C  CD    . PRO A 1 2730 ? 180.489 141.486 129.467 1.00 34.52  ? 3947 PRO A CD    1 
ATOM   16641 N  N     . HIS A 1 2731 ? 181.410 143.588 127.029 1.00 31.54  ? 3948 HIS A N     1 
ATOM   16642 C  CA    . HIS A 1 2731 ? 182.134 143.930 125.809 1.00 32.85  ? 3948 HIS A CA    1 
ATOM   16643 C  C     . HIS A 1 2731 ? 181.255 144.040 124.575 1.00 28.64  ? 3948 HIS A C     1 
ATOM   16644 O  O     . HIS A 1 2731 ? 181.465 144.943 123.761 1.00 30.67  ? 3948 HIS A O     1 
ATOM   16645 C  CB    . HIS A 1 2731 ? 183.239 142.899 125.560 1.00 34.75  ? 3948 HIS A CB    1 
ATOM   16646 C  CG    . HIS A 1 2731 ? 184.350 142.962 126.559 1.00 40.27  ? 3948 HIS A CG    1 
ATOM   16647 N  ND1   . HIS A 1 2731 ? 185.340 142.008 126.634 1.00 45.57  ? 3948 HIS A ND1   1 
ATOM   16648 C  CD2   . HIS A 1 2731 ? 184.635 143.876 127.516 1.00 45.73  ? 3948 HIS A CD2   1 
ATOM   16649 C  CE1   . HIS A 1 2731 ? 186.184 142.328 127.599 1.00 52.01  ? 3948 HIS A CE1   1 
ATOM   16650 N  NE2   . HIS A 1 2731 ? 185.779 143.457 128.150 1.00 49.34  ? 3948 HIS A NE2   1 
ATOM   16651 N  N     . GLY A 1 2732 ? 180.289 143.138 124.397 1.00 26.29  ? 3949 GLY A N     1 
ATOM   16652 C  CA    . GLY A 1 2732 ? 179.375 143.267 123.274 1.00 21.89  ? 3949 GLY A CA    1 
ATOM   16653 C  C     . GLY A 1 2732 ? 178.499 144.498 123.388 1.00 17.30  ? 3949 GLY A C     1 
ATOM   16654 O  O     . GLY A 1 2732 ? 178.189 145.148 122.387 1.00 14.97  ? 3949 GLY A O     1 
ATOM   16655 N  N     . PHE A 1 2733 ? 178.093 144.833 124.608 1.00 18.79  ? 3950 PHE A N     1 
ATOM   16656 C  CA    . PHE A 1 2733 ? 177.324 146.032 124.902 1.00 18.71  ? 3950 PHE A CA    1 
ATOM   16657 C  C     . PHE A 1 2733 ? 177.846 146.598 126.216 1.00 21.54  ? 3950 PHE A C     1 
ATOM   16658 O  O     . PHE A 1 2733 ? 178.932 146.239 126.680 1.00 27.75  ? 3950 PHE A O     1 
ATOM   16659 C  CB    . PHE A 1 2733 ? 175.823 145.719 124.952 1.00 17.53  ? 3950 PHE A CB    1 
ATOM   16660 C  CG    . PHE A 1 2733 ? 175.122 145.891 123.635 1.00 16.67  ? 3950 PHE A CG    1 
ATOM   16661 C  CD1   . PHE A 1 2733 ? 175.136 147.108 122.983 1.00 14.70  ? 3950 PHE A CD1   1 
ATOM   16662 C  CD2   . PHE A 1 2733 ? 174.447 144.836 123.051 1.00 17.40  ? 3950 PHE A CD2   1 
ATOM   16663 C  CE1   . PHE A 1 2733 ? 174.491 147.269 121.776 1.00 12.12  ? 3950 PHE A CE1   1 
ATOM   16664 C  CE2   . PHE A 1 2733 ? 173.802 144.991 121.842 1.00 12.79  ? 3950 PHE A CE2   1 
ATOM   16665 C  CZ    . PHE A 1 2733 ? 173.826 146.209 121.205 1.00 10.57  ? 3950 PHE A CZ    1 
ATOM   16666 N  N     . SER A 1 2734 ? 177.087 147.515 126.813 1.00 17.95  ? 3951 SER A N     1 
ATOM   16667 C  CA    . SER A 1 2734 ? 177.368 147.968 128.167 1.00 18.17  ? 3951 SER A CA    1 
ATOM   16668 C  C     . SER A 1 2734 ? 176.306 147.548 129.169 1.00 19.29  ? 3951 SER A C     1 
ATOM   16669 O  O     . SER A 1 2734 ? 176.555 147.619 130.375 1.00 18.94  ? 3951 SER A O     1 
ATOM   16670 C  CB    . SER A 1 2734 ? 177.516 149.495 128.205 1.00 19.88  ? 3951 SER A CB    1 
ATOM   16671 O  OG    . SER A 1 2734 ? 178.357 149.946 127.158 1.00 19.58  ? 3951 SER A OG    1 
ATOM   16672 N  N     . LYS A 1 2735 ? 175.141 147.111 128.700 1.00 21.52  ? 3952 LYS A N     1 
ATOM   16673 C  CA    . LYS A 1 2735 ? 174.060 146.648 129.555 1.00 21.82  ? 3952 LYS A CA    1 
ATOM   16674 C  C     . LYS A 1 2735 ? 173.454 145.409 128.908 1.00 22.25  ? 3952 LYS A C     1 
ATOM   16675 O  O     . LYS A 1 2735 ? 173.965 144.893 127.910 1.00 21.94  ? 3952 LYS A O     1 
ATOM   16676 C  CB    . LYS A 1 2735 ? 173.023 147.758 129.767 1.00 23.36  ? 3952 LYS A CB    1 
ATOM   16677 C  CG    . LYS A 1 2735 ? 173.334 148.695 130.917 1.00 26.40  ? 3952 LYS A CG    1 
ATOM   16678 C  CD    . LYS A 1 2735 ? 172.559 149.997 130.791 1.00 30.15  ? 3952 LYS A CD    1 
ATOM   16679 C  CE    . LYS A 1 2735 ? 171.069 149.749 130.608 1.00 27.01  ? 3952 LYS A CE    1 
ATOM   16680 N  NZ    . LYS A 1 2735 ? 170.499 148.920 131.707 1.00 32.60  ? 3952 LYS A NZ    1 
ATOM   16681 N  N     . LYS A 1 2736 ? 172.354 144.929 129.474 1.00 21.09  ? 3953 LYS A N     1 
ATOM   16682 C  CA    . LYS A 1 2736 ? 171.646 143.765 128.951 1.00 24.09  ? 3953 LYS A CA    1 
ATOM   16683 C  C     . LYS A 1 2736 ? 170.308 144.232 128.389 1.00 27.26  ? 3953 LYS A C     1 
ATOM   16684 O  O     . LYS A 1 2736 ? 169.375 144.524 129.141 1.00 29.67  ? 3953 LYS A O     1 
ATOM   16685 C  CB    . LYS A 1 2736 ? 171.456 142.707 130.032 1.00 30.11  ? 3953 LYS A CB    1 
ATOM   16686 C  CG    . LYS A 1 2736 ? 170.681 141.489 129.564 1.00 30.79  ? 3953 LYS A CG    1 
ATOM   16687 C  CD    . LYS A 1 2736 ? 171.574 140.534 128.793 1.00 26.49  ? 3953 LYS A CD    1 
ATOM   16688 C  CE    . LYS A 1 2736 ? 170.758 139.656 127.865 1.00 27.42  ? 3953 LYS A CE    1 
ATOM   16689 N  NZ    . LYS A 1 2736 ? 171.616 138.947 126.881 1.00 27.13  ? 3953 LYS A NZ    1 
ATOM   16690 N  N     . TYR A 1 2737 ? 170.223 144.302 127.065 1.00 27.41  ? 3954 TYR A N     1 
ATOM   16691 C  CA    . TYR A 1 2737 ? 168.999 144.661 126.372 1.00 22.48  ? 3954 TYR A CA    1 
ATOM   16692 C  C     . TYR A 1 2737 ? 168.270 143.397 125.929 1.00 25.48  ? 3954 TYR A C     1 
ATOM   16693 O  O     . TYR A 1 2737 ? 168.739 142.275 126.124 1.00 31.11  ? 3954 TYR A O     1 
ATOM   16694 C  CB    . TYR A 1 2737 ? 169.308 145.573 125.186 1.00 18.94  ? 3954 TYR A CB    1 
ATOM   16695 C  CG    . TYR A 1 2737 ? 170.077 146.814 125.568 1.00 19.30  ? 3954 TYR A CG    1 
ATOM   16696 C  CD1   . TYR A 1 2737 ? 169.557 147.717 126.484 1.00 22.70  ? 3954 TYR A CD1   1 
ATOM   16697 C  CD2   . TYR A 1 2737 ? 171.322 147.078 125.020 1.00 16.69  ? 3954 TYR A CD2   1 
ATOM   16698 C  CE1   . TYR A 1 2737 ? 170.254 148.853 126.838 1.00 23.87  ? 3954 TYR A CE1   1 
ATOM   16699 C  CE2   . TYR A 1 2737 ? 172.025 148.210 125.369 1.00 17.26  ? 3954 TYR A CE2   1 
ATOM   16700 C  CZ    . TYR A 1 2737 ? 171.487 149.093 126.278 1.00 21.03  ? 3954 TYR A CZ    1 
ATOM   16701 O  OH    . TYR A 1 2737 ? 172.185 150.224 126.630 1.00 21.78  ? 3954 TYR A OH    1 
ATOM   16702 N  N     . TYR A 1 2738 ? 167.096 143.582 125.329 1.00 22.12  ? 3955 TYR A N     1 
ATOM   16703 C  CA    . TYR A 1 2738 ? 166.298 142.440 124.883 1.00 24.44  ? 3955 TYR A CA    1 
ATOM   16704 C  C     . TYR A 1 2738 ? 165.597 142.840 123.584 1.00 22.76  ? 3955 TYR A C     1 
ATOM   16705 O  O     . TYR A 1 2738 ? 164.526 143.447 123.605 1.00 26.72  ? 3955 TYR A O     1 
ATOM   16706 C  CB    . TYR A 1 2738 ? 165.304 142.007 125.949 1.00 31.23  ? 3955 TYR A CB    1 
ATOM   16707 C  CG    . TYR A 1 2738 ? 165.950 141.484 127.213 1.00 34.08  ? 3955 TYR A CG    1 
ATOM   16708 C  CD1   . TYR A 1 2738 ? 166.467 140.198 127.270 1.00 37.11  ? 3955 TYR A CD1   1 
ATOM   16709 C  CD2   . TYR A 1 2738 ? 166.051 142.280 128.346 1.00 33.52  ? 3955 TYR A CD2   1 
ATOM   16710 C  CE1   . TYR A 1 2738 ? 167.059 139.716 128.420 1.00 37.50  ? 3955 TYR A CE1   1 
ATOM   16711 C  CE2   . TYR A 1 2738 ? 166.641 141.806 129.501 1.00 34.03  ? 3955 TYR A CE2   1 
ATOM   16712 C  CZ    . TYR A 1 2738 ? 167.144 140.524 129.531 1.00 37.29  ? 3955 TYR A CZ    1 
ATOM   16713 O  OH    . TYR A 1 2738 ? 167.734 140.048 130.678 1.00 42.54  ? 3955 TYR A OH    1 
ATOM   16714 N  N     . PHE A 1 2739 ? 166.218 142.490 122.461 1.00 19.36  ? 3956 PHE A N     1 
ATOM   16715 C  CA    . PHE A 1 2739 ? 165.611 142.672 121.150 1.00 19.07  ? 3956 PHE A CA    1 
ATOM   16716 C  C     . PHE A 1 2739 ? 164.853 141.405 120.780 1.00 22.60  ? 3956 PHE A C     1 
ATOM   16717 O  O     . PHE A 1 2739 ? 165.408 140.304 120.848 1.00 27.83  ? 3956 PHE A O     1 
ATOM   16718 C  CB    . PHE A 1 2739 ? 166.674 142.992 120.100 1.00 13.88  ? 3956 PHE A CB    1 
ATOM   16719 C  CG    . PHE A 1 2739 ? 167.535 144.168 120.452 1.00 12.33  ? 3956 PHE A CG    1 
ATOM   16720 C  CD1   . PHE A 1 2739 ? 166.985 145.294 121.035 1.00 15.08  ? 3956 PHE A CD1   1 
ATOM   16721 C  CD2   . PHE A 1 2739 ? 168.892 144.148 120.204 1.00 11.69  ? 3956 PHE A CD2   1 
ATOM   16722 C  CE1   . PHE A 1 2739 ? 167.773 146.376 121.360 1.00 13.02  ? 3956 PHE A CE1   1 
ATOM   16723 C  CE2   . PHE A 1 2739 ? 169.683 145.229 120.531 1.00 12.64  ? 3956 PHE A CE2   1 
ATOM   16724 C  CZ    . PHE A 1 2739 ? 169.123 146.342 121.106 1.00 11.50  ? 3956 PHE A CZ    1 
ATOM   16725 N  N     . ASN A 1 2740 ? 163.591 141.561 120.386 1.00 21.79  ? 3957 ASN A N     1 
ATOM   16726 C  CA    . ASN A 1 2740 ? 162.711 140.407 120.251 1.00 20.93  ? 3957 ASN A CA    1 
ATOM   16727 C  C     . ASN A 1 2740 ? 161.911 140.440 118.956 1.00 21.81  ? 3957 ASN A C     1 
ATOM   16728 O  O     . ASN A 1 2740 ? 162.216 141.218 118.047 1.00 21.38  ? 3957 ASN A O     1 
ATOM   16729 C  CB    . ASN A 1 2740 ? 161.771 140.317 121.455 1.00 21.19  ? 3957 ASN A CB    1 
ATOM   16730 C  CG    . ASN A 1 2740 ? 160.995 141.595 121.689 1.00 23.15  ? 3957 ASN A CG    1 
ATOM   16731 O  OD1   . ASN A 1 2740 ? 160.080 141.926 120.938 1.00 24.65  ? 3957 ASN A OD1   1 
ATOM   16732 N  ND2   . ASN A 1 2740 ? 161.356 142.322 122.738 1.00 23.79  ? 3957 ASN A ND2   1 
ATOM   16733 N  N     . ASP A 1 2741 ? 160.895 139.577 118.865 1.00 23.87  ? 3958 ASP A N     1 
ATOM   16734 C  CA    . ASP A 1 2741 ? 160.149 139.410 117.622 1.00 22.83  ? 3958 ASP A CA    1 
ATOM   16735 C  C     . ASP A 1 2741 ? 159.342 140.650 117.256 1.00 23.15  ? 3958 ASP A C     1 
ATOM   16736 O  O     . ASP A 1 2741 ? 159.164 140.933 116.068 1.00 22.90  ? 3958 ASP A O     1 
ATOM   16737 C  CB    . ASP A 1 2741 ? 159.230 138.193 117.724 1.00 26.76  ? 3958 ASP A CB    1 
ATOM   16738 C  CG    . ASP A 1 2741 ? 158.320 138.249 118.937 1.00 33.80  ? 3958 ASP A CG    1 
ATOM   16739 O  OD1   . ASP A 1 2741 ? 157.293 138.957 118.883 1.00 32.93  ? 3958 ASP A OD1   1 
ATOM   16740 O  OD2   . ASP A 1 2741 ? 158.630 137.579 119.946 1.00 36.59  ? 3958 ASP A OD2   1 
ATOM   16741 N  N     . CYS A 1 2742 ? 158.830 141.384 118.249 1.00 24.62  ? 3959 CYS A N     1 
ATOM   16742 C  CA    . CYS A 1 2742 ? 158.088 142.612 117.967 1.00 21.91  ? 3959 CYS A CA    1 
ATOM   16743 C  C     . CYS A 1 2742 ? 158.974 143.657 117.300 1.00 19.93  ? 3959 CYS A C     1 
ATOM   16744 O  O     . CYS A 1 2742 ? 158.548 144.347 116.364 1.00 20.13  ? 3959 CYS A O     1 
ATOM   16745 C  CB    . CYS A 1 2742 ? 157.496 143.166 119.261 1.00 19.54  ? 3959 CYS A CB    1 
ATOM   16746 S  SG    . CYS A 1 2742 ? 156.867 144.847 119.126 1.00 30.73  ? 3959 CYS A SG    1 
ATOM   16747 N  N     . ASP A 1 2743 ? 160.208 143.787 117.780 1.00 19.69  ? 3960 ASP A N     1 
ATOM   16748 C  CA    . ASP A 1 2743 ? 161.163 144.720 117.196 1.00 17.57  ? 3960 ASP A CA    1 
ATOM   16749 C  C     . ASP A 1 2743 ? 161.513 144.305 115.768 1.00 16.97  ? 3960 ASP A C     1 
ATOM   16750 O  O     . ASP A 1 2743 ? 161.636 145.153 114.869 1.00 18.00  ? 3960 ASP A O     1 
ATOM   16751 C  CB    . ASP A 1 2743 ? 162.389 144.764 118.109 1.00 16.92  ? 3960 ASP A CB    1 
ATOM   16752 C  CG    . ASP A 1 2743 ? 163.335 145.883 117.789 1.00 15.55  ? 3960 ASP A CG    1 
ATOM   16753 O  OD1   . ASP A 1 2743 ? 163.115 146.615 116.809 1.00 14.87  ? 3960 ASP A OD1   1 
ATOM   16754 O  OD2   . ASP A 1 2743 ? 164.279 146.065 118.579 1.00 16.99  ? 3960 ASP A OD2   1 
ATOM   16755 N  N     . PHE A 1 2744 ? 161.633 142.995 115.538 1.00 17.68  ? 3961 PHE A N     1 
ATOM   16756 C  CA    . PHE A 1 2744 ? 161.826 142.472 114.189 1.00 19.06  ? 3961 PHE A CA    1 
ATOM   16757 C  C     . PHE A 1 2744 ? 160.641 142.802 113.290 1.00 20.93  ? 3961 PHE A C     1 
ATOM   16758 O  O     . PHE A 1 2744 ? 160.823 143.152 112.118 1.00 22.57  ? 3961 PHE A O     1 
ATOM   16759 C  CB    . PHE A 1 2744 ? 162.050 140.960 114.255 1.00 20.15  ? 3961 PHE A CB    1 
ATOM   16760 C  CG    . PHE A 1 2744 ? 162.130 140.295 112.912 1.00 20.95  ? 3961 PHE A CG    1 
ATOM   16761 C  CD1   . PHE A 1 2744 ? 163.277 140.383 112.144 1.00 17.05  ? 3961 PHE A CD1   1 
ATOM   16762 C  CD2   . PHE A 1 2744 ? 161.058 139.567 112.424 1.00 25.81  ? 3961 PHE A CD2   1 
ATOM   16763 C  CE1   . PHE A 1 2744 ? 163.349 139.764 110.911 1.00 17.65  ? 3961 PHE A CE1   1 
ATOM   16764 C  CE2   . PHE A 1 2744 ? 161.125 138.951 111.192 1.00 27.49  ? 3961 PHE A CE2   1 
ATOM   16765 C  CZ    . PHE A 1 2744 ? 162.271 139.050 110.435 1.00 24.06  ? 3961 PHE A CZ    1 
ATOM   16766 N  N     . GLN A 1 2745 ? 159.420 142.692 113.820 1.00 21.75  ? 3962 GLN A N     1 
ATOM   16767 C  CA    . GLN A 1 2745 ? 158.232 143.016 113.036 1.00 22.25  ? 3962 GLN A CA    1 
ATOM   16768 C  C     . GLN A 1 2745 ? 158.204 144.490 112.660 1.00 21.25  ? 3962 GLN A C     1 
ATOM   16769 O  O     . GLN A 1 2745 ? 157.878 144.839 111.518 1.00 21.18  ? 3962 GLN A O     1 
ATOM   16770 C  CB    . GLN A 1 2745 ? 156.968 142.642 113.810 1.00 22.67  ? 3962 GLN A CB    1 
ATOM   16771 C  CG    . GLN A 1 2745 ? 156.734 141.145 113.943 1.00 26.82  ? 3962 GLN A CG    1 
ATOM   16772 C  CD    . GLN A 1 2745 ? 156.559 140.455 112.604 1.00 34.89  ? 3962 GLN A CD    1 
ATOM   16773 O  OE1   . GLN A 1 2745 ? 155.939 140.997 111.688 1.00 42.48  ? 3962 GLN A OE1   1 
ATOM   16774 N  NE2   . GLN A 1 2745 ? 157.110 139.254 112.482 1.00 34.33  ? 3962 GLN A NE2   1 
ATOM   16775 N  N     . PHE A 1 2746 ? 158.545 145.369 113.608 1.00 19.85  ? 3963 PHE A N     1 
ATOM   16776 C  CA    . PHE A 1 2746 ? 158.573 146.801 113.315 1.00 18.11  ? 3963 PHE A CA    1 
ATOM   16777 C  C     . PHE A 1 2746 ? 159.595 147.122 112.234 1.00 17.06  ? 3963 PHE A C     1 
ATOM   16778 O  O     . PHE A 1 2746 ? 159.306 147.880 111.298 1.00 22.07  ? 3963 PHE A O     1 
ATOM   16779 C  CB    . PHE A 1 2746 ? 158.886 147.605 114.575 1.00 16.10  ? 3963 PHE A CB    1 
ATOM   16780 C  CG    . PHE A 1 2746 ? 157.672 148.036 115.342 1.00 16.54  ? 3963 PHE A CG    1 
ATOM   16781 C  CD1   . PHE A 1 2746 ? 156.906 147.113 116.029 1.00 19.05  ? 3963 PHE A CD1   1 
ATOM   16782 C  CD2   . PHE A 1 2746 ? 157.285 149.363 115.360 1.00 17.22  ? 3963 PHE A CD2   1 
ATOM   16783 C  CE1   . PHE A 1 2746 ? 155.796 147.511 116.744 1.00 17.73  ? 3963 PHE A CE1   1 
ATOM   16784 C  CE2   . PHE A 1 2746 ? 156.169 149.763 116.061 1.00 17.67  ? 3963 PHE A CE2   1 
ATOM   16785 C  CZ    . PHE A 1 2746 ? 155.422 148.836 116.753 1.00 15.68  ? 3963 PHE A CZ    1 
ATOM   16786 N  N     . ALA A 1 2747 ? 160.793 146.540 112.337 1.00 14.61  ? 3964 ALA A N     1 
ATOM   16787 C  CA    . ALA A 1 2747 ? 161.813 146.785 111.322 1.00 14.71  ? 3964 ALA A CA    1 
ATOM   16788 C  C     . ALA A 1 2747 ? 161.394 146.241 109.959 1.00 17.29  ? 3964 ALA A C     1 
ATOM   16789 O  O     . ALA A 1 2747 ? 161.608 146.896 108.931 1.00 19.78  ? 3964 ALA A O     1 
ATOM   16790 C  CB    . ALA A 1 2747 ? 163.140 146.174 111.762 1.00 15.31  ? 3964 ALA A CB    1 
ATOM   16791 N  N     . SER A 1 2748 ? 160.783 145.052 109.931 1.00 17.31  ? 3965 SER A N     1 
ATOM   16792 C  CA    . SER A 1 2748 ? 160.349 144.463 108.667 1.00 17.90  ? 3965 SER A CA    1 
ATOM   16793 C  C     . SER A 1 2748 ? 159.263 145.298 108.006 1.00 21.35  ? 3965 SER A C     1 
ATOM   16794 O  O     . SER A 1 2748 ? 159.271 145.485 106.783 1.00 23.54  ? 3965 SER A O     1 
ATOM   16795 C  CB    . SER A 1 2748 ? 159.853 143.037 108.900 1.00 19.67  ? 3965 SER A CB    1 
ATOM   16796 O  OG    . SER A 1 2748 ? 159.104 142.574 107.793 1.00 19.23  ? 3965 SER A OG    1 
ATOM   16797 N  N     . VAL A 1 2749 ? 158.320 145.811 108.797 1.00 22.26  ? 3966 VAL A N     1 
ATOM   16798 C  CA    . VAL A 1 2749 ? 157.273 146.654 108.234 1.00 21.61  ? 3966 VAL A CA    1 
ATOM   16799 C  C     . VAL A 1 2749 ? 157.857 147.970 107.737 1.00 18.61  ? 3966 VAL A C     1 
ATOM   16800 O  O     . VAL A 1 2749 ? 157.422 148.505 106.711 1.00 18.84  ? 3966 VAL A O     1 
ATOM   16801 C  CB    . VAL A 1 2749 ? 156.150 146.870 109.263 1.00 17.41  ? 3966 VAL A CB    1 
ATOM   16802 C  CG1   . VAL A 1 2749 ? 155.156 147.913 108.778 1.00 18.18  ? 3966 VAL A CG1   1 
ATOM   16803 C  CG2   . VAL A 1 2749 ? 155.433 145.560 109.535 1.00 19.34  ? 3966 VAL A CG2   1 
ATOM   16804 N  N     . TYR A 1 2750 ? 158.861 148.507 108.436 1.00 15.85  ? 3967 TYR A N     1 
ATOM   16805 C  CA    . TYR A 1 2750 ? 159.501 149.720 107.939 1.00 15.30  ? 3967 TYR A CA    1 
ATOM   16806 C  C     . TYR A 1 2750 ? 160.196 149.475 106.604 1.00 17.48  ? 3967 TYR A C     1 
ATOM   16807 O  O     . TYR A 1 2750 ? 160.128 150.318 105.703 1.00 20.50  ? 3967 TYR A O     1 
ATOM   16808 C  CB    . TYR A 1 2750 ? 160.496 150.275 108.953 1.00 14.45  ? 3967 TYR A CB    1 
ATOM   16809 C  CG    . TYR A 1 2750 ? 161.175 151.526 108.447 1.00 12.24  ? 3967 TYR A CG    1 
ATOM   16810 C  CD1   . TYR A 1 2750 ? 160.452 152.696 108.262 1.00 13.25  ? 3967 TYR A CD1   1 
ATOM   16811 C  CD2   . TYR A 1 2750 ? 162.523 151.535 108.132 1.00 12.21  ? 3967 TYR A CD2   1 
ATOM   16812 C  CE1   . TYR A 1 2750 ? 161.056 153.843 107.794 1.00 13.44  ? 3967 TYR A CE1   1 
ATOM   16813 C  CE2   . TYR A 1 2750 ? 163.135 152.679 107.663 1.00 11.79  ? 3967 TYR A CE2   1 
ATOM   16814 C  CZ    . TYR A 1 2750 ? 162.397 153.830 107.498 1.00 13.26  ? 3967 TYR A CZ    1 
ATOM   16815 O  OH    . TYR A 1 2750 ? 163.003 154.973 107.028 1.00 14.05  ? 3967 TYR A OH    1 
ATOM   16816 N  N     . LEU A 1 2751 ? 160.870 148.329 106.455 1.00 17.91  ? 3968 LEU A N     1 
ATOM   16817 C  CA    . LEU A 1 2751 ? 161.471 147.996 105.161 1.00 18.61  ? 3968 LEU A CA    1 
ATOM   16818 C  C     . LEU A 1 2751 ? 160.415 147.816 104.074 1.00 22.30  ? 3968 LEU A C     1 
ATOM   16819 O  O     . LEU A 1 2751 ? 160.613 148.255 102.933 1.00 24.64  ? 3968 LEU A O     1 
ATOM   16820 C  CB    . LEU A 1 2751 ? 162.350 146.747 105.263 1.00 19.20  ? 3968 LEU A CB    1 
ATOM   16821 C  CG    . LEU A 1 2751 ? 163.822 146.861 105.682 1.00 19.48  ? 3968 LEU A CG    1 
ATOM   16822 C  CD1   . LEU A 1 2751 ? 164.574 147.651 104.626 1.00 17.29  ? 3968 LEU A CD1   1 
ATOM   16823 C  CD2   . LEU A 1 2751 ? 164.037 147.488 107.037 1.00 17.72  ? 3968 LEU A CD2   1 
ATOM   16824 N  N     . GLU A 1 2752 ? 159.290 147.175 104.406 1.00 23.32  ? 3969 GLU A N     1 
ATOM   16825 C  CA    . GLU A 1 2752 ? 158.214 147.022 103.429 1.00 23.93  ? 3969 GLU A CA    1 
ATOM   16826 C  C     . GLU A 1 2752 ? 157.672 148.374 102.988 1.00 26.22  ? 3969 GLU A C     1 
ATOM   16827 O  O     . GLU A 1 2752 ? 157.430 148.596 101.797 1.00 25.51  ? 3969 GLU A O     1 
ATOM   16828 C  CB    . GLU A 1 2752 ? 157.079 146.178 104.005 1.00 23.97  ? 3969 GLU A CB    1 
ATOM   16829 C  CG    . GLU A 1 2752 ? 157.400 144.717 104.217 1.00 28.29  ? 3969 GLU A CG    1 
ATOM   16830 C  CD    . GLU A 1 2752 ? 156.482 144.085 105.240 1.00 29.18  ? 3969 GLU A CD    1 
ATOM   16831 O  OE1   . GLU A 1 2752 ? 155.508 144.749 105.650 1.00 22.89  ? 3969 GLU A OE1   1 
ATOM   16832 O  OE2   . GLU A 1 2752 ? 156.729 142.929 105.636 1.00 32.94  ? 3969 GLU A OE2   1 
ATOM   16833 N  N     . ASN A 1 2753 ? 157.476 149.289 103.938 1.00 26.37  ? 3970 ASN A N     1 
ATOM   16834 C  CA    . ASN A 1 2753 ? 156.942 150.605 103.609 1.00 24.54  ? 3970 ASN A CA    1 
ATOM   16835 C  C     . ASN A 1 2753 ? 157.945 151.428 102.810 1.00 25.60  ? 3970 ASN A C     1 
ATOM   16836 O  O     . ASN A 1 2753 ? 157.557 152.172 101.903 1.00 28.94  ? 3970 ASN A O     1 
ATOM   16837 C  CB    . ASN A 1 2753 ? 156.536 151.336 104.887 1.00 19.83  ? 3970 ASN A CB    1 
ATOM   16838 C  CG    . ASN A 1 2753 ? 156.290 152.808 104.660 1.00 19.86  ? 3970 ASN A CG    1 
ATOM   16839 O  OD1   . ASN A 1 2753 ? 157.188 153.633 104.826 1.00 18.67  ? 3970 ASN A OD1   1 
ATOM   16840 N  ND2   . ASN A 1 2753 ? 155.069 153.147 104.269 1.00 21.96  ? 3970 ASN A ND2   1 
ATOM   16841 N  N     . VAL A 1 2754 ? 159.236 151.312 103.135 1.00 23.38  ? 3971 VAL A N     1 
ATOM   16842 C  CA    . VAL A 1 2754 ? 160.267 152.016 102.377 1.00 20.63  ? 3971 VAL A CA    1 
ATOM   16843 C  C     . VAL A 1 2754 ? 160.312 151.512 100.941 1.00 27.76  ? 3971 VAL A C     1 
ATOM   16844 O  O     . VAL A 1 2754 ? 160.392 152.302 99.992  1.00 33.51  ? 3971 VAL A O     1 
ATOM   16845 C  CB    . VAL A 1 2754 ? 161.631 151.872 103.077 1.00 18.44  ? 3971 VAL A CB    1 
ATOM   16846 C  CG1   . VAL A 1 2754 ? 162.766 152.162 102.119 1.00 19.94  ? 3971 VAL A CG1   1 
ATOM   16847 C  CG2   . VAL A 1 2754 ? 161.708 152.806 104.259 1.00 21.21  ? 3971 VAL A CG2   1 
ATOM   16848 N  N     . LEU A 1 2755 ? 160.246 150.191 100.756 1.00 28.36  ? 3972 LEU A N     1 
ATOM   16849 C  CA    . LEU A 1 2755 ? 160.254 149.641 99.404  1.00 31.45  ? 3972 LEU A CA    1 
ATOM   16850 C  C     . LEU A 1 2755 ? 158.973 149.971 98.648  1.00 35.32  ? 3972 LEU A C     1 
ATOM   16851 O  O     . LEU A 1 2755 ? 159.005 150.127 97.422  1.00 38.94  ? 3972 LEU A O     1 
ATOM   16852 C  CB    . LEU A 1 2755 ? 160.472 148.128 99.446  1.00 28.38  ? 3972 LEU A CB    1 
ATOM   16853 C  CG    . LEU A 1 2755 ? 161.913 147.618 99.361  1.00 29.24  ? 3972 LEU A CG    1 
ATOM   16854 C  CD1   . LEU A 1 2755 ? 162.492 147.980 98.010  1.00 32.01  ? 3972 LEU A CD1   1 
ATOM   16855 C  CD2   . LEU A 1 2755 ? 162.799 148.146 100.477 1.00 26.16  ? 3972 LEU A CD2   1 
ATOM   16856 N  N     . ALA A 1 2756 ? 157.843 150.071 99.350  1.00 31.33  ? 3973 ALA A N     1 
ATOM   16857 C  CA    . ALA A 1 2756 ? 156.579 150.367 98.683  1.00 32.95  ? 3973 ALA A CA    1 
ATOM   16858 C  C     . ALA A 1 2756 ? 156.547 151.799 98.162  1.00 37.12  ? 3973 ALA A C     1 
ATOM   16859 O  O     . ALA A 1 2756 ? 156.206 152.038 96.998  1.00 42.73  ? 3973 ALA A O     1 
ATOM   16860 C  CB    . ALA A 1 2756 ? 155.412 150.114 99.637  1.00 34.42  ? 3973 ALA A CB    1 
ATOM   16861 N  N     . THR A 1 2757 ? 156.909 152.767 99.005  1.00 35.95  ? 3974 THR A N     1 
ATOM   16862 C  CA    . THR A 1 2757 ? 156.854 154.166 98.602  1.00 37.06  ? 3974 THR A CA    1 
ATOM   16863 C  C     . THR A 1 2757 ? 158.005 154.564 97.689  1.00 36.63  ? 3974 THR A C     1 
ATOM   16864 O  O     . THR A 1 2757 ? 157.963 155.652 97.106  1.00 37.28  ? 3974 THR A O     1 
ATOM   16865 C  CB    . THR A 1 2757 ? 156.845 155.081 99.830  1.00 35.23  ? 3974 THR A CB    1 
ATOM   16866 O  OG1   . THR A 1 2757 ? 156.600 156.430 99.416  1.00 36.78  ? 3974 THR A OG1   1 
ATOM   16867 C  CG2   . THR A 1 2757 ? 158.187 155.034 100.538 1.00 32.03  ? 3974 THR A CG2   1 
ATOM   16868 N  N     . ASN A 1 2758 ? 159.024 153.720 97.553  1.00 35.91  ? 3975 ASN A N     1 
ATOM   16869 C  CA    . ASN A 1 2758 ? 160.164 153.975 96.679  1.00 41.09  ? 3975 ASN A CA    1 
ATOM   16870 C  C     . ASN A 1 2758 ? 160.273 152.785 95.730  1.00 47.47  ? 3975 ASN A C     1 
ATOM   16871 O  O     . ASN A 1 2758 ? 160.999 151.826 95.999  1.00 48.18  ? 3975 ASN A O     1 
ATOM   16872 C  CB    . ASN A 1 2758 ? 161.445 154.177 97.483  1.00 38.19  ? 3975 ASN A CB    1 
ATOM   16873 C  CG    . ASN A 1 2758 ? 162.497 154.950 96.716  1.00 44.85  ? 3975 ASN A CG    1 
ATOM   16874 O  OD1   . ASN A 1 2758 ? 163.241 154.382 95.916  1.00 50.77  ? 3975 ASN A OD1   1 
ATOM   16875 N  ND2   . ASN A 1 2758 ? 162.572 156.252 96.962  1.00 42.90  ? 3975 ASN A ND2   1 
ATOM   16876 N  N     . SER A 1 2759 ? 159.543 152.850 94.619  1.00 52.43  ? 3976 SER A N     1 
ATOM   16877 C  CA    . SER A 1 2759 ? 159.528 151.785 93.628  1.00 56.57  ? 3976 SER A CA    1 
ATOM   16878 C  C     . SER A 1 2759 ? 160.446 152.071 92.448  1.00 65.36  ? 3976 SER A C     1 
ATOM   16879 O  O     . SER A 1 2759 ? 160.397 151.349 91.447  1.00 68.29  ? 3976 SER A O     1 
ATOM   16880 C  CB    . SER A 1 2759 ? 158.100 151.544 93.133  1.00 55.84  ? 3976 SER A CB    1 
ATOM   16881 O  OG    . SER A 1 2759 ? 157.529 152.736 92.624  1.00 53.56  ? 3976 SER A OG    1 
ATOM   16882 N  N     . THR A 1 2760 ? 161.278 153.106 92.540  1.00 65.98  ? 3977 THR A N     1 
ATOM   16883 C  CA    . THR A 1 2760 ? 162.237 153.442 91.497  1.00 65.26  ? 3977 THR A CA    1 
ATOM   16884 C  C     . THR A 1 2760 ? 163.579 152.747 91.690  1.00 62.81  ? 3977 THR A C     1 
ATOM   16885 O  O     . THR A 1 2760 ? 164.574 153.186 91.105  1.00 63.61  ? 3977 THR A O     1 
ATOM   16886 C  CB    . THR A 1 2760 ? 162.445 154.958 91.435  1.00 65.18  ? 3977 THR A CB    1 
ATOM   16887 O  OG1   . THR A 1 2760 ? 163.170 155.392 92.593  1.00 61.74  ? 3977 THR A OG1   1 
ATOM   16888 C  CG2   . THR A 1 2760 ? 161.105 155.677 91.384  1.00 62.26  ? 3977 THR A CG2   1 
ATOM   16889 N  N     . ASN A 1 2761 ? 163.623 151.708 92.534  1.00 58.04  ? 3978 ASN A N     1 
ATOM   16890 C  CA    . ASN A 1 2761 ? 164.791 150.862 92.834  1.00 53.65  ? 3978 ASN A CA    1 
ATOM   16891 C  C     . ASN A 1 2761 ? 166.042 151.663 93.211  1.00 57.76  ? 3978 ASN A C     1 
ATOM   16892 O  O     . ASN A 1 2761 ? 167.162 151.150 93.127  1.00 62.49  ? 3978 ASN A O     1 
ATOM   16893 C  CB    . ASN A 1 2761 ? 165.089 149.860 91.700  1.00 58.22  ? 3978 ASN A CB    1 
ATOM   16894 C  CG    . ASN A 1 2761 ? 165.546 150.514 90.403  1.00 63.74  ? 3978 ASN A CG    1 
ATOM   16895 O  OD1   . ASN A 1 2761 ? 166.618 151.116 90.329  1.00 67.29  ? 3978 ASN A OD1   1 
ATOM   16896 N  ND2   . ASN A 1 2761 ? 164.723 150.394 89.368  1.00 60.82  ? 3978 ASN A ND2   1 
ATOM   16897 N  N     . ASN A 1 2762 ? 165.873 152.915 93.639  1.00 56.72  ? 3979 ASN A N     1 
ATOM   16898 C  CA    . ASN A 1 2762 ? 166.945 153.677 94.277  1.00 53.86  ? 3979 ASN A CA    1 
ATOM   16899 C  C     . ASN A 1 2762 ? 166.642 153.683 95.772  1.00 47.64  ? 3979 ASN A C     1 
ATOM   16900 O  O     . ASN A 1 2762 ? 166.073 154.626 96.321  1.00 46.73  ? 3979 ASN A O     1 
ATOM   16901 C  CB    . ASN A 1 2762 ? 167.041 155.084 93.698  1.00 55.45  ? 3979 ASN A CB    1 
ATOM   16902 C  CG    . ASN A 1 2762 ? 167.218 155.083 92.194  1.00 58.67  ? 3979 ASN A CG    1 
ATOM   16903 O  OD1   . ASN A 1 2762 ? 167.937 154.248 91.644  1.00 50.88  ? 3979 ASN A OD1   1 
ATOM   16904 N  ND2   . ASN A 1 2762 ? 166.565 156.021 91.520  1.00 62.78  ? 3979 ASN A ND2   1 
ATOM   16905 N  N     . ILE A 1 2763 ? 167.034 152.599 96.427  1.00 43.73  ? 3980 ILE A N     1 
ATOM   16906 C  CA    . ILE A 1 2763 ? 166.586 152.331 97.798  1.00 39.67  ? 3980 ILE A CA    1 
ATOM   16907 C  C     . ILE A 1 2763 ? 167.283 153.293 98.753  1.00 35.40  ? 3980 ILE A C     1 
ATOM   16908 O  O     . ILE A 1 2763 ? 168.520 153.419 98.710  1.00 37.24  ? 3980 ILE A O     1 
ATOM   16909 C  CB    . ILE A 1 2763 ? 166.872 150.875 98.176  1.00 37.49  ? 3980 ILE A CB    1 
ATOM   16910 C  CG1   . ILE A 1 2763 ? 166.650 149.948 96.977  1.00 42.06  ? 3980 ILE A CG1   1 
ATOM   16911 C  CG2   . ILE A 1 2763 ? 165.985 150.439 99.331  1.00 31.74  ? 3980 ILE A CG2   1 
ATOM   16912 C  CD1   . ILE A 1 2763 ? 165.218 149.898 96.480  1.00 45.81  ? 3980 ILE A CD1   1 
ATOM   16913 N  N     . PRO A 1 2764 ? 166.549 153.993 99.617  1.00 31.65  ? 3981 PRO A N     1 
ATOM   16914 C  CA    . PRO A 1 2764 ? 167.180 154.908 100.588 1.00 31.99  ? 3981 PRO A CA    1 
ATOM   16915 C  C     . PRO A 1 2764 ? 167.813 154.143 101.747 1.00 30.16  ? 3981 PRO A C     1 
ATOM   16916 O  O     . PRO A 1 2764 ? 167.233 153.939 102.813 1.00 28.70  ? 3981 PRO A O     1 
ATOM   16917 C  CB    . PRO A 1 2764 ? 166.008 155.783 101.035 1.00 32.32  ? 3981 PRO A CB    1 
ATOM   16918 C  CG    . PRO A 1 2764 ? 164.819 154.906 100.898 1.00 32.48  ? 3981 PRO A CG    1 
ATOM   16919 C  CD    . PRO A 1 2764 ? 165.080 153.984 99.739  1.00 33.28  ? 3981 PRO A CD    1 
ATOM   16920 N  N     . TRP A 1 2765 ? 169.046 153.685 101.517 1.00 28.46  ? 3982 TRP A N     1 
ATOM   16921 C  CA    . TRP A 1 2765 ? 169.741 152.903 102.532 1.00 23.02  ? 3982 TRP A CA    1 
ATOM   16922 C  C     . TRP A 1 2765 ? 170.082 153.743 103.755 1.00 21.82  ? 3982 TRP A C     1 
ATOM   16923 O  O     . TRP A 1 2765 ? 170.110 153.219 104.874 1.00 24.94  ? 3982 TRP A O     1 
ATOM   16924 C  CB    . TRP A 1 2765 ? 171.001 152.274 101.939 1.00 27.46  ? 3982 TRP A CB    1 
ATOM   16925 C  CG    . TRP A 1 2765 ? 170.711 151.176 100.955 1.00 29.42  ? 3982 TRP A CG    1 
ATOM   16926 C  CD1   . TRP A 1 2765 ? 171.052 151.151 99.635  1.00 30.20  ? 3982 TRP A CD1   1 
ATOM   16927 C  CD2   . TRP A 1 2765 ? 170.021 149.945 101.213 1.00 28.00  ? 3982 TRP A CD2   1 
ATOM   16928 N  NE1   . TRP A 1 2765 ? 170.617 149.985 99.055  1.00 30.07  ? 3982 TRP A NE1   1 
ATOM   16929 C  CE2   . TRP A 1 2765 ? 169.982 149.227 100.003 1.00 29.03  ? 3982 TRP A CE2   1 
ATOM   16930 C  CE3   . TRP A 1 2765 ? 169.434 149.380 102.349 1.00 25.86  ? 3982 TRP A CE3   1 
ATOM   16931 C  CZ2   . TRP A 1 2765 ? 169.379 147.977 99.896  1.00 27.23  ? 3982 TRP A CZ2   1 
ATOM   16932 C  CZ3   . TRP A 1 2765 ? 168.835 148.139 102.240 1.00 24.35  ? 3982 TRP A CZ3   1 
ATOM   16933 C  CH2   . TRP A 1 2765 ? 168.812 147.452 101.024 1.00 24.08  ? 3982 TRP A CH2   1 
ATOM   16934 N  N     . ALA A 1 2766 ? 170.327 155.042 103.568 1.00 21.90  ? 3983 ALA A N     1 
ATOM   16935 C  CA    . ALA A 1 2766 ? 170.539 155.922 104.711 1.00 23.00  ? 3983 ALA A CA    1 
ATOM   16936 C  C     . ALA A 1 2766 ? 169.290 156.004 105.580 1.00 19.85  ? 3983 ALA A C     1 
ATOM   16937 O  O     . ALA A 1 2766 ? 169.385 156.036 106.813 1.00 18.33  ? 3983 ALA A O     1 
ATOM   16938 C  CB    . ALA A 1 2766 ? 170.957 157.311 104.234 1.00 25.93  ? 3983 ALA A CB    1 
ATOM   16939 N  N     . GLN A 1 2767 ? 168.110 156.023 104.953 1.00 19.93  ? 3984 GLN A N     1 
ATOM   16940 C  CA    . GLN A 1 2767 ? 166.863 156.096 105.709 1.00 17.21  ? 3984 GLN A CA    1 
ATOM   16941 C  C     . GLN A 1 2767 ? 166.689 154.880 106.605 1.00 16.99  ? 3984 GLN A C     1 
ATOM   16942 O  O     . GLN A 1 2767 ? 166.431 155.017 107.806 1.00 18.74  ? 3984 GLN A O     1 
ATOM   16943 C  CB    . GLN A 1 2767 ? 165.670 156.226 104.762 1.00 21.91  ? 3984 GLN A CB    1 
ATOM   16944 C  CG    . GLN A 1 2767 ? 165.358 157.642 104.321 1.00 27.95  ? 3984 GLN A CG    1 
ATOM   16945 C  CD    . GLN A 1 2767 ? 163.941 157.785 103.805 1.00 26.72  ? 3984 GLN A CD    1 
ATOM   16946 O  OE1   . GLN A 1 2767 ? 163.032 157.089 104.256 1.00 22.97  ? 3984 GLN A OE1   1 
ATOM   16947 N  NE2   . GLN A 1 2767 ? 163.746 158.692 102.857 1.00 29.82  ? 3984 GLN A NE2   1 
ATOM   16948 N  N     . VAL A 1 2768 ? 166.832 153.677 106.040 1.00 16.57  ? 3985 VAL A N     1 
ATOM   16949 C  CA    . VAL A 1 2768 ? 166.637 152.468 106.836 1.00 13.96  ? 3985 VAL A CA    1 
ATOM   16950 C  C     . VAL A 1 2768 ? 167.744 152.328 107.873 1.00 13.08  ? 3985 VAL A C     1 
ATOM   16951 O  O     . VAL A 1 2768 ? 167.488 151.907 109.006 1.00 12.10  ? 3985 VAL A O     1 
ATOM   16952 C  CB    . VAL A 1 2768 ? 166.525 151.222 105.936 1.00 13.93  ? 3985 VAL A CB    1 
ATOM   16953 C  CG1   . VAL A 1 2768 ? 165.213 151.238 105.177 1.00 17.28  ? 3985 VAL A CG1   1 
ATOM   16954 C  CG2   . VAL A 1 2768 ? 167.676 151.131 104.970 1.00 16.51  ? 3985 VAL A CG2   1 
ATOM   16955 N  N     . ARG A 1 2769 ? 168.975 152.722 107.523 1.00 14.93  ? 3986 ARG A N     1 
ATOM   16956 C  CA    . ARG A 1 2769 ? 170.079 152.668 108.477 1.00 13.91  ? 3986 ARG A CA    1 
ATOM   16957 C  C     . ARG A 1 2769 ? 169.802 153.538 109.697 1.00 13.55  ? 3986 ARG A C     1 
ATOM   16958 O  O     . ARG A 1 2769 ? 169.849 153.059 110.835 1.00 13.11  ? 3986 ARG A O     1 
ATOM   16959 C  CB    . ARG A 1 2769 ? 171.378 153.111 107.805 1.00 18.10  ? 3986 ARG A CB    1 
ATOM   16960 C  CG    . ARG A 1 2769 ? 172.119 152.020 107.072 1.00 21.13  ? 3986 ARG A CG    1 
ATOM   16961 C  CD    . ARG A 1 2769 ? 173.599 152.329 107.001 1.00 23.20  ? 3986 ARG A CD    1 
ATOM   16962 N  NE    . ARG A 1 2769 ? 173.862 153.647 106.439 1.00 26.30  ? 3986 ARG A NE    1 
ATOM   16963 C  CZ    . ARG A 1 2769 ? 174.071 153.883 105.152 1.00 28.91  ? 3986 ARG A CZ    1 
ATOM   16964 N  NH1   . ARG A 1 2769 ? 174.053 152.907 104.259 1.00 27.82  ? 3986 ARG A NH1   1 
ATOM   16965 N  NH2   . ARG A 1 2769 ? 174.306 155.128 104.750 1.00 31.96  ? 3986 ARG A NH2   1 
ATOM   16966 N  N     . ASP A 1 2770 ? 169.474 154.815 109.476 1.00 15.10  ? 3987 ASP A N     1 
ATOM   16967 C  CA    . ASP A 1 2770 ? 169.270 155.723 110.601 1.00 13.11  ? 3987 ASP A CA    1 
ATOM   16968 C  C     . ASP A 1 2770 ? 167.993 155.397 111.364 1.00 9.87   ? 3987 ASP A C     1 
ATOM   16969 O  O     . ASP A 1 2770 ? 167.961 155.507 112.595 1.00 10.66  ? 3987 ASP A O     1 
ATOM   16970 C  CB    . ASP A 1 2770 ? 169.258 157.171 110.118 1.00 13.94  ? 3987 ASP A CB    1 
ATOM   16971 C  CG    . ASP A 1 2770 ? 170.637 157.665 109.731 1.00 20.91  ? 3987 ASP A CG    1 
ATOM   16972 O  OD1   . ASP A 1 2770 ? 171.117 157.313 108.636 1.00 24.49  ? 3987 ASP A OD1   1 
ATOM   16973 O  OD2   . ASP A 1 2770 ? 171.245 158.407 110.529 1.00 23.01  ? 3987 ASP A OD2   1 
ATOM   16974 N  N     . HIS A 1 2771 ? 166.936 154.981 110.664 1.00 7.67   ? 3988 HIS A N     1 
ATOM   16975 C  CA    . HIS A 1 2771 ? 165.689 154.669 111.350 1.00 7.86   ? 3988 HIS A CA    1 
ATOM   16976 C  C     . HIS A 1 2771 ? 165.821 153.415 112.201 1.00 10.16  ? 3988 HIS A C     1 
ATOM   16977 O  O     . HIS A 1 2771 ? 165.281 153.355 113.311 1.00 11.56  ? 3988 HIS A O     1 
ATOM   16978 C  CB    . HIS A 1 2771 ? 164.562 154.515 110.335 1.00 9.49   ? 3988 HIS A CB    1 
ATOM   16979 C  CG    . HIS A 1 2771 ? 163.204 154.423 110.953 1.00 9.70   ? 3988 HIS A CG    1 
ATOM   16980 N  ND1   . HIS A 1 2771 ? 162.410 153.304 110.836 1.00 9.67   ? 3988 HIS A ND1   1 
ATOM   16981 C  CD2   . HIS A 1 2771 ? 162.497 155.311 111.691 1.00 9.43   ? 3988 HIS A CD2   1 
ATOM   16982 C  CE1   . HIS A 1 2771 ? 161.272 153.506 111.475 1.00 10.11  ? 3988 HIS A CE1   1 
ATOM   16983 N  NE2   . HIS A 1 2771 ? 161.300 154.715 112.004 1.00 9.54   ? 3988 HIS A NE2   1 
ATOM   16984 N  N     . ILE A 1 2772 ? 166.526 152.398 111.700 1.00 12.07  ? 3989 ILE A N     1 
ATOM   16985 C  CA    . ILE A 1 2772 ? 166.726 151.178 112.471 1.00 9.43   ? 3989 ILE A CA    1 
ATOM   16986 C  C     . ILE A 1 2772 ? 167.691 151.423 113.627 1.00 8.69   ? 3989 ILE A C     1 
ATOM   16987 O  O     . ILE A 1 2772 ? 167.484 150.928 114.741 1.00 8.88   ? 3989 ILE A O     1 
ATOM   16988 C  CB    . ILE A 1 2772 ? 167.200 150.050 111.534 1.00 8.34   ? 3989 ILE A CB    1 
ATOM   16989 C  CG1   . ILE A 1 2772 ? 166.017 149.482 110.751 1.00 7.79   ? 3989 ILE A CG1   1 
ATOM   16990 C  CG2   . ILE A 1 2772 ? 167.867 148.944 112.294 1.00 9.86   ? 3989 ILE A CG2   1 
ATOM   16991 C  CD1   . ILE A 1 2772 ? 166.412 148.465 109.716 1.00 8.87   ? 3989 ILE A CD1   1 
ATOM   16992 N  N     . ALA A 1 2773 ? 168.741 152.216 113.397 1.00 9.42   ? 3990 ALA A N     1 
ATOM   16993 C  CA    . ALA A 1 2773 ? 169.746 152.421 114.432 1.00 10.23  ? 3990 ALA A CA    1 
ATOM   16994 C  C     . ALA A 1 2773 ? 169.239 153.324 115.549 1.00 9.51   ? 3990 ALA A C     1 
ATOM   16995 O  O     . ALA A 1 2773 ? 169.567 153.106 116.720 1.00 9.65   ? 3990 ALA A O     1 
ATOM   16996 C  CB    . ALA A 1 2773 ? 171.018 153.001 113.816 1.00 10.98  ? 3990 ALA A CB    1 
ATOM   16997 N  N     . THR A 1 2774 ? 168.450 154.346 115.218 1.00 7.94   ? 3991 THR A N     1 
ATOM   16998 C  CA    . THR A 1 2774 ? 168.111 155.374 116.195 1.00 8.76   ? 3991 THR A CA    1 
ATOM   16999 C  C     . THR A 1 2774 ? 166.711 155.244 116.773 1.00 9.06   ? 3991 THR A C     1 
ATOM   17000 O  O     . THR A 1 2774 ? 166.496 155.630 117.926 1.00 10.85  ? 3991 THR A O     1 
ATOM   17001 C  CB    . THR A 1 2774 ? 168.248 156.766 115.570 1.00 7.76   ? 3991 THR A CB    1 
ATOM   17002 O  OG1   . THR A 1 2774 ? 167.403 156.857 114.418 1.00 9.72   ? 3991 THR A OG1   1 
ATOM   17003 C  CG2   . THR A 1 2774 ? 169.685 157.023 115.154 1.00 9.86   ? 3991 THR A CG2   1 
ATOM   17004 N  N     . ILE A 1 2775 ? 165.751 154.717 116.013 1.00 7.97   ? 3992 ILE A N     1 
ATOM   17005 C  CA    . ILE A 1 2775 ? 164.350 154.732 116.402 1.00 6.56   ? 3992 ILE A CA    1 
ATOM   17006 C  C     . ILE A 1 2775 ? 163.803 153.330 116.632 1.00 7.41   ? 3992 ILE A C     1 
ATOM   17007 O  O     . ILE A 1 2775 ? 163.039 153.105 117.578 1.00 7.86   ? 3992 ILE A O     1 
ATOM   17008 C  CB    . ILE A 1 2775 ? 163.499 155.483 115.357 1.00 7.52   ? 3992 ILE A CB    1 
ATOM   17009 C  CG1   . ILE A 1 2775 ? 164.120 156.851 115.065 1.00 8.10   ? 3992 ILE A CG1   1 
ATOM   17010 C  CG2   . ILE A 1 2775 ? 162.074 155.645 115.842 1.00 8.68   ? 3992 ILE A CG2   1 
ATOM   17011 C  CD1   . ILE A 1 2775 ? 163.329 157.705 114.109 1.00 8.42   ? 3992 ILE A CD1   1 
ATOM   17012 N  N     . VAL A 1 2776 ? 164.186 152.370 115.795 1.00 8.10   ? 3993 VAL A N     1 
ATOM   17013 C  CA    . VAL A 1 2776 ? 163.612 151.030 115.882 1.00 7.29   ? 3993 VAL A CA    1 
ATOM   17014 C  C     . VAL A 1 2776 ? 164.331 150.202 116.941 1.00 9.54   ? 3993 VAL A C     1 
ATOM   17015 O  O     . VAL A 1 2776 ? 163.720 149.730 117.907 1.00 12.49  ? 3993 VAL A O     1 
ATOM   17016 C  CB    . VAL A 1 2776 ? 163.652 150.346 114.505 1.00 6.57   ? 3993 VAL A CB    1 
ATOM   17017 C  CG1   . VAL A 1 2776 ? 163.143 148.934 114.606 1.00 8.00   ? 3993 VAL A CG1   1 
ATOM   17018 C  CG2   . VAL A 1 2776 ? 162.837 151.131 113.504 1.00 10.44  ? 3993 VAL A CG2   1 
ATOM   17019 N  N     . TYR A 1 2777 ? 165.640 150.011 116.772 1.00 10.19  ? 3994 TYR A N     1 
ATOM   17020 C  CA    . TYR A 1 2777 ? 166.470 149.267 117.713 1.00 7.92   ? 3994 TYR A CA    1 
ATOM   17021 C  C     . TYR A 1 2777 ? 167.068 150.149 118.801 1.00 8.94   ? 3994 TYR A C     1 
ATOM   17022 O  O     . TYR A 1 2777 ? 167.142 149.730 119.959 1.00 12.90  ? 3994 TYR A O     1 
ATOM   17023 C  CB    . TYR A 1 2777 ? 167.584 148.538 116.956 1.00 9.54   ? 3994 TYR A CB    1 
ATOM   17024 C  CG    . TYR A 1 2777 ? 167.165 147.200 116.392 1.00 10.61  ? 3994 TYR A CG    1 
ATOM   17025 C  CD1   . TYR A 1 2777 ? 167.029 147.010 115.031 1.00 9.53   ? 3994 TYR A CD1   1 
ATOM   17026 C  CD2   . TYR A 1 2777 ? 166.987 146.107 117.220 1.00 11.75  ? 3994 TYR A CD2   1 
ATOM   17027 C  CE1   . TYR A 1 2777 ? 166.655 145.791 114.513 1.00 8.45   ? 3994 TYR A CE1   1 
ATOM   17028 C  CE2   . TYR A 1 2777 ? 166.620 144.880 116.713 1.00 12.02  ? 3994 TYR A CE2   1 
ATOM   17029 C  CZ    . TYR A 1 2777 ? 166.461 144.728 115.357 1.00 12.31  ? 3994 TYR A CZ    1 
ATOM   17030 O  OH    . TYR A 1 2777 ? 166.102 143.507 114.843 1.00 21.48  ? 3994 TYR A OH    1 
ATOM   17031 N  N     . GLY A 1 2778 ? 167.494 151.359 118.458 1.00 9.21   ? 3995 GLY A N     1 
ATOM   17032 C  CA    . GLY A 1 2778 ? 168.115 152.241 119.420 1.00 9.57   ? 3995 GLY A CA    1 
ATOM   17033 C  C     . GLY A 1 2778 ? 167.176 153.100 120.232 1.00 11.07  ? 3995 GLY A C     1 
ATOM   17034 O  O     . GLY A 1 2778 ? 167.637 154.001 120.935 1.00 12.82  ? 3995 GLY A O     1 
ATOM   17035 N  N     . GLY A 1 2779 ? 165.867 152.868 120.141 1.00 10.22  ? 3996 GLY A N     1 
ATOM   17036 C  CA    . GLY A 1 2779 ? 164.937 153.630 120.958 1.00 9.03   ? 3996 GLY A CA    1 
ATOM   17037 C  C     . GLY A 1 2779 ? 165.075 153.323 122.437 1.00 11.65  ? 3996 GLY A C     1 
ATOM   17038 O  O     . GLY A 1 2779 ? 165.116 154.231 123.271 1.00 16.22  ? 3996 GLY A O     1 
ATOM   17039 N  N     . LYS A 1 2780 ? 165.164 152.039 122.782 1.00 10.90  ? 3997 LYS A N     1 
ATOM   17040 C  CA    . LYS A 1 2780 ? 165.229 151.635 124.182 1.00 11.43  ? 3997 LYS A CA    1 
ATOM   17041 C  C     . LYS A 1 2780 ? 166.594 151.877 124.806 1.00 11.40  ? 3997 LYS A C     1 
ATOM   17042 O  O     . LYS A 1 2780 ? 166.725 151.763 126.029 1.00 12.74  ? 3997 LYS A O     1 
ATOM   17043 C  CB    . LYS A 1 2780 ? 164.868 150.156 124.317 1.00 11.76  ? 3997 LYS A CB    1 
ATOM   17044 C  CG    . LYS A 1 2780 ? 165.837 149.219 123.615 1.00 12.63  ? 3997 LYS A CG    1 
ATOM   17045 C  CD    . LYS A 1 2780 ? 165.305 147.799 123.571 1.00 10.52  ? 3997 LYS A CD    1 
ATOM   17046 C  CE    . LYS A 1 2780 ? 164.183 147.668 122.560 1.00 13.83  ? 3997 LYS A CE    1 
ATOM   17047 N  NZ    . LYS A 1 2780 ? 164.654 147.971 121.182 1.00 13.37  ? 3997 LYS A NZ    1 
ATOM   17048 N  N     . ILE A 1 2781 ? 167.600 152.210 124.010 1.00 12.88  ? 3998 ILE A N     1 
ATOM   17049 C  CA    . ILE A 1 2781 ? 168.977 152.298 124.479 1.00 16.38  ? 3998 ILE A CA    1 
ATOM   17050 C  C     . ILE A 1 2781 ? 169.260 153.731 124.912 1.00 20.80  ? 3998 ILE A C     1 
ATOM   17051 O  O     . ILE A 1 2781 ? 169.146 154.665 124.110 1.00 25.52  ? 3998 ILE A O     1 
ATOM   17052 C  CB    . ILE A 1 2781 ? 169.954 151.849 123.385 1.00 14.93  ? 3998 ILE A CB    1 
ATOM   17053 C  CG1   . ILE A 1 2781 ? 169.832 150.342 123.165 1.00 12.41  ? 3998 ILE A CG1   1 
ATOM   17054 C  CG2   . ILE A 1 2781 ? 171.369 152.243 123.745 1.00 19.21  ? 3998 ILE A CG2   1 
ATOM   17055 C  CD1   . ILE A 1 2781 ? 170.406 149.871 121.860 1.00 11.96  ? 3998 ILE A CD1   1 
ATOM   17056 N  N     . ASP A 1 2782 ? 169.636 153.905 126.178 1.00 19.35  ? 3999 ASP A N     1 
ATOM   17057 C  CA    . ASP A 1 2782 ? 169.902 155.224 126.735 1.00 22.47  ? 3999 ASP A CA    1 
ATOM   17058 C  C     . ASP A 1 2782 ? 171.376 155.605 126.706 1.00 25.02  ? 3999 ASP A C     1 
ATOM   17059 O  O     . ASP A 1 2782 ? 171.699 156.772 126.466 1.00 31.70  ? 3999 ASP A O     1 
ATOM   17060 C  CB    . ASP A 1 2782 ? 169.389 155.298 128.176 1.00 19.89  ? 3999 ASP A CB    1 
ATOM   17061 C  CG    . ASP A 1 2782 ? 169.790 154.095 128.997 1.00 22.84  ? 3999 ASP A CG    1 
ATOM   17062 O  OD1   . ASP A 1 2782 ? 170.363 153.147 128.418 1.00 27.79  ? 3999 ASP A OD1   1 
ATOM   17063 O  OD2   . ASP A 1 2782 ? 169.532 154.093 130.217 1.00 21.71  ? 3999 ASP A OD2   1 
ATOM   17064 N  N     . GLU A 1 2783 ? 172.282 154.661 126.949 1.00 21.56  ? 4000 GLU A N     1 
ATOM   17065 C  CA    . GLU A 1 2783 ? 173.701 154.969 126.903 1.00 22.45  ? 4000 GLU A CA    1 
ATOM   17066 C  C     . GLU A 1 2783 ? 174.158 155.190 125.468 1.00 24.29  ? 4000 GLU A C     1 
ATOM   17067 O  O     . GLU A 1 2783 ? 173.633 154.596 124.525 1.00 27.56  ? 4000 GLU A O     1 
ATOM   17068 C  CB    . GLU A 1 2783 ? 174.517 153.850 127.549 1.00 25.95  ? 4000 GLU A CB    1 
ATOM   17069 C  CG    . GLU A 1 2783 ? 175.907 154.287 127.977 1.00 34.13  ? 4000 GLU A CG    1 
ATOM   17070 C  CD    . GLU A 1 2783 ? 176.441 153.471 129.126 1.00 35.08  ? 4000 GLU A CD    1 
ATOM   17071 O  OE1   . GLU A 1 2783 ? 175.664 153.187 130.058 1.00 33.32  ? 4000 GLU A OE1   1 
ATOM   17072 O  OE2   . GLU A 1 2783 ? 177.633 153.103 129.091 1.00 30.04  ? 4000 GLU A OE2   1 
ATOM   17073 N  N     . GLU A 1 2784 ? 175.140 156.075 125.302 1.00 23.47  ? 4001 GLU A N     1 
ATOM   17074 C  CA    . GLU A 1 2784 ? 175.580 156.418 123.955 1.00 25.82  ? 4001 GLU A CA    1 
ATOM   17075 C  C     . GLU A 1 2784 ? 176.449 155.321 123.344 1.00 27.39  ? 4001 GLU A C     1 
ATOM   17076 O  O     . GLU A 1 2784 ? 176.350 155.078 122.137 1.00 27.35  ? 4001 GLU A O     1 
ATOM   17077 C  CB    . GLU A 1 2784 ? 176.323 157.750 123.963 1.00 31.53  ? 4001 GLU A CB    1 
ATOM   17078 C  CG    . GLU A 1 2784 ? 176.785 158.255 122.601 1.00 34.62  ? 4001 GLU A CG    1 
ATOM   17079 C  CD    . GLU A 1 2784 ? 175.685 158.956 121.812 1.00 42.90  ? 4001 GLU A CD    1 
ATOM   17080 O  OE1   . GLU A 1 2784 ? 174.519 158.966 122.263 1.00 38.14  ? 4001 GLU A OE1   1 
ATOM   17081 O  OE2   . GLU A 1 2784 ? 175.997 159.532 120.747 1.00 54.42  ? 4001 GLU A OE2   1 
ATOM   17082 N  N     . LYS A 1 2785 ? 177.266 154.642 124.162 1.00 25.26  ? 4002 LYS A N     1 
ATOM   17083 C  CA    . LYS A 1 2785 ? 178.200 153.651 123.647 1.00 25.78  ? 4002 LYS A CA    1 
ATOM   17084 C  C     . LYS A 1 2785 ? 177.473 152.527 122.920 1.00 25.34  ? 4002 LYS A C     1 
ATOM   17085 O  O     . LYS A 1 2785 ? 177.848 152.148 121.797 1.00 25.77  ? 4002 LYS A O     1 
ATOM   17086 C  CB    . LYS A 1 2785 ? 179.054 153.098 124.786 1.00 28.60  ? 4002 LYS A CB    1 
ATOM   17087 C  CG    . LYS A 1 2785 ? 179.899 154.164 125.467 1.00 34.99  ? 4002 LYS A CG    1 
ATOM   17088 C  CD    . LYS A 1 2785 ? 180.786 154.887 124.465 1.00 41.61  ? 4002 LYS A CD    1 
ATOM   17089 C  CE    . LYS A 1 2785 ? 181.806 155.788 125.145 1.00 46.64  ? 4002 LYS A CE    1 
ATOM   17090 N  NZ    . LYS A 1 2785 ? 182.647 156.518 124.159 1.00 46.90  ? 4002 LYS A NZ    1 
ATOM   17091 N  N     . ASP A 1 2786 ? 176.397 152.023 123.519 1.00 21.69  ? 4003 ASP A N     1 
ATOM   17092 C  CA    . ASP A 1 2786 ? 175.585 151.011 122.863 1.00 17.39  ? 4003 ASP A CA    1 
ATOM   17093 C  C     . ASP A 1 2786 ? 174.942 151.568 121.604 1.00 18.17  ? 4003 ASP A C     1 
ATOM   17094 O  O     . ASP A 1 2786 ? 174.663 150.821 120.660 1.00 18.64  ? 4003 ASP A O     1 
ATOM   17095 C  CB    . ASP A 1 2786 ? 174.527 150.509 123.839 1.00 15.38  ? 4003 ASP A CB    1 
ATOM   17096 C  CG    . ASP A 1 2786 ? 175.121 150.121 125.168 1.00 18.93  ? 4003 ASP A CG    1 
ATOM   17097 O  OD1   . ASP A 1 2786 ? 176.333 149.829 125.206 1.00 22.64  ? 4003 ASP A OD1   1 
ATOM   17098 O  OD2   . ASP A 1 2786 ? 174.391 150.141 126.181 1.00 18.61  ? 4003 ASP A OD2   1 
ATOM   17099 N  N     . LEU A 1 2787 ? 174.729 152.884 121.560 1.00 20.17  ? 4004 LEU A N     1 
ATOM   17100 C  CA    . LEU A 1 2787 ? 174.128 153.483 120.378 1.00 20.49  ? 4004 LEU A CA    1 
ATOM   17101 C  C     . LEU A 1 2787 ? 175.086 153.491 119.193 1.00 21.09  ? 4004 LEU A C     1 
ATOM   17102 O  O     . LEU A 1 2787 ? 174.666 153.178 118.075 1.00 23.74  ? 4004 LEU A O     1 
ATOM   17103 C  CB    . LEU A 1 2787 ? 173.622 154.890 120.682 1.00 22.69  ? 4004 LEU A CB    1 
ATOM   17104 C  CG    . LEU A 1 2787 ? 172.194 154.921 121.226 1.00 21.84  ? 4004 LEU A CG    1 
ATOM   17105 C  CD1   . LEU A 1 2787 ? 171.774 156.339 121.560 1.00 26.58  ? 4004 LEU A CD1   1 
ATOM   17106 C  CD2   . LEU A 1 2787 ? 171.226 154.300 120.231 1.00 17.36  ? 4004 LEU A CD2   1 
ATOM   17107 N  N     . GLU A 1 2788 ? 176.379 153.825 119.381 1.00 19.43  ? 4005 GLU A N     1 
ATOM   17108 C  CA    . GLU A 1 2788 ? 177.178 153.667 118.161 1.00 19.42  ? 4005 GLU A CA    1 
ATOM   17109 C  C     . GLU A 1 2788 ? 177.571 152.215 117.927 1.00 21.31  ? 4005 GLU A C     1 
ATOM   17110 O  O     . GLU A 1 2788 ? 177.974 151.886 116.813 1.00 23.74  ? 4005 GLU A O     1 
ATOM   17111 C  CB    . GLU A 1 2788 ? 178.462 154.525 118.046 1.00 22.75  ? 4005 GLU A CB    1 
ATOM   17112 C  CG    . GLU A 1 2788 ? 179.721 154.166 118.854 1.00 26.10  ? 4005 GLU A CG    1 
ATOM   17113 C  CD    . GLU A 1 2788 ? 179.628 154.393 120.317 1.00 31.83  ? 4005 GLU A CD    1 
ATOM   17114 O  OE1   . GLU A 1 2788 ? 180.680 154.432 120.988 1.00 31.43  ? 4005 GLU A OE1   1 
ATOM   17115 O  OE2   . GLU A 1 2788 ? 178.532 154.685 120.774 1.00 31.39  ? 4005 GLU A OE2   1 
ATOM   17116 N  N     . VAL A 1 2789 ? 177.428 151.328 118.917 1.00 21.87  ? 4006 VAL A N     1 
ATOM   17117 C  CA    . VAL A 1 2789 ? 177.554 149.899 118.615 1.00 18.58  ? 4006 VAL A CA    1 
ATOM   17118 C  C     . VAL A 1 2789 ? 176.457 149.460 117.642 1.00 17.00  ? 4006 VAL A C     1 
ATOM   17119 O  O     . VAL A 1 2789 ? 176.726 148.831 116.603 1.00 15.52  ? 4006 VAL A O     1 
ATOM   17120 C  CB    . VAL A 1 2789 ? 177.524 149.069 119.909 1.00 16.05  ? 4006 VAL A CB    1 
ATOM   17121 C  CG1   . VAL A 1 2789 ? 177.259 147.616 119.592 1.00 13.92  ? 4006 VAL A CG1   1 
ATOM   17122 C  CG2   . VAL A 1 2789 ? 178.842 149.213 120.651 1.00 16.76  ? 4006 VAL A CG2   1 
ATOM   17123 N  N     . VAL A 1 2790 ? 175.206 149.813 117.955 1.00 17.83  ? 4007 VAL A N     1 
ATOM   17124 C  CA    . VAL A 1 2790 ? 174.088 149.505 117.063 1.00 14.69  ? 4007 VAL A CA    1 
ATOM   17125 C  C     . VAL A 1 2790 ? 174.252 150.227 115.731 1.00 14.03  ? 4007 VAL A C     1 
ATOM   17126 O  O     . VAL A 1 2790 ? 173.936 149.680 114.669 1.00 17.19  ? 4007 VAL A O     1 
ATOM   17127 C  CB    . VAL A 1 2790 ? 172.751 149.859 117.743 1.00 10.28  ? 4007 VAL A CB    1 
ATOM   17128 C  CG1   . VAL A 1 2790 ? 171.592 149.615 116.810 1.00 10.59  ? 4007 VAL A CG1   1 
ATOM   17129 C  CG2   . VAL A 1 2790 ? 172.570 149.039 118.995 1.00 9.57   ? 4007 VAL A CG2   1 
ATOM   17130 N  N     . ALA A 1 2791 ? 174.764 151.460 115.764 1.00 13.32  ? 4008 ALA A N     1 
ATOM   17131 C  CA    . ALA A 1 2791 ? 174.977 152.211 114.530 1.00 14.96  ? 4008 ALA A CA    1 
ATOM   17132 C  C     . ALA A 1 2791 ? 176.027 151.552 113.645 1.00 18.14  ? 4008 ALA A C     1 
ATOM   17133 O  O     . ALA A 1 2791 ? 175.871 151.506 112.422 1.00 21.27  ? 4008 ALA A O     1 
ATOM   17134 C  CB    . ALA A 1 2791 ? 175.378 153.648 114.854 1.00 19.99  ? 4008 ALA A CB    1 
ATOM   17135 N  N     . LYS A 1 2792 ? 177.108 151.043 114.244 1.00 18.71  ? 4009 LYS A N     1 
ATOM   17136 C  CA    . LYS A 1 2792 ? 178.138 150.355 113.473 1.00 18.75  ? 4009 LYS A CA    1 
ATOM   17137 C  C     . LYS A 1 2792 ? 177.587 149.078 112.856 1.00 18.11  ? 4009 LYS A C     1 
ATOM   17138 O  O     . LYS A 1 2792 ? 177.859 148.779 111.685 1.00 20.16  ? 4009 LYS A O     1 
ATOM   17139 C  CB    . LYS A 1 2792 ? 179.351 150.079 114.375 1.00 23.06  ? 4009 LYS A CB    1 
ATOM   17140 C  CG    . LYS A 1 2792 ? 180.654 149.573 113.709 1.00 28.64  ? 4009 LYS A CG    1 
ATOM   17141 C  CD    . LYS A 1 2792 ? 180.655 148.095 113.316 1.00 29.52  ? 4009 LYS A CD    1 
ATOM   17142 C  CE    . LYS A 1 2792 ? 181.862 147.736 112.469 1.00 36.47  ? 4009 LYS A CE    1 
ATOM   17143 N  NZ    . LYS A 1 2792 ? 181.946 146.268 112.229 1.00 39.48  ? 4009 LYS A NZ    1 
ATOM   17144 N  N     . LEU A 1 2793 ? 176.809 148.307 113.623 1.00 15.99  ? 4010 LEU A N     1 
ATOM   17145 C  CA    . LEU A 1 2793 ? 176.259 147.082 113.047 1.00 14.49  ? 4010 LEU A CA    1 
ATOM   17146 C  C     . LEU A 1 2793 ? 175.240 147.386 111.952 1.00 16.48  ? 4010 LEU A C     1 
ATOM   17147 O  O     . LEU A 1 2793 ? 175.177 146.663 110.949 1.00 17.52  ? 4010 LEU A O     1 
ATOM   17148 C  CB    . LEU A 1 2793 ? 175.647 146.200 114.133 1.00 11.49  ? 4010 LEU A CB    1 
ATOM   17149 C  CG    . LEU A 1 2793 ? 175.584 144.723 113.731 1.00 11.34  ? 4010 LEU A CG    1 
ATOM   17150 C  CD1   . LEU A 1 2793 ? 176.960 144.213 113.344 1.00 18.23  ? 4010 LEU A CD1   1 
ATOM   17151 C  CD2   . LEU A 1 2793 ? 175.008 143.875 114.841 1.00 13.74  ? 4010 LEU A CD2   1 
ATOM   17152 N  N     . CYS A 1 2794 ? 174.458 148.459 112.111 1.00 15.75  ? 4011 CYS A N     1 
ATOM   17153 C  CA    . CYS A 1 2794 ? 173.534 148.880 111.063 1.00 11.89  ? 4011 CYS A CA    1 
ATOM   17154 C  C     . CYS A 1 2794 ? 174.279 149.334 109.817 1.00 15.37  ? 4011 CYS A C     1 
ATOM   17155 O  O     . CYS A 1 2794 ? 173.843 149.067 108.693 1.00 19.68  ? 4011 CYS A O     1 
ATOM   17156 C  CB    . CYS A 1 2794 ? 172.644 150.012 111.571 1.00 11.93  ? 4011 CYS A CB    1 
ATOM   17157 S  SG    . CYS A 1 2794 ? 171.351 149.506 112.695 1.00 15.68  ? 4011 CYS A SG    1 
ATOM   17158 N  N     . ALA A 1 2795 ? 175.392 150.046 109.999 1.00 16.32  ? 4012 ALA A N     1 
ATOM   17159 C  CA    . ALA A 1 2795 ? 176.180 150.500 108.861 1.00 18.30  ? 4012 ALA A CA    1 
ATOM   17160 C  C     . ALA A 1 2795 ? 176.796 149.327 108.117 1.00 20.92  ? 4012 ALA A C     1 
ATOM   17161 O  O     . ALA A 1 2795 ? 176.890 149.348 106.885 1.00 22.27  ? 4012 ALA A O     1 
ATOM   17162 C  CB    . ALA A 1 2795 ? 177.263 151.472 109.323 1.00 22.25  ? 4012 ALA A CB    1 
ATOM   17163 N  N     . HIS A 1 2796 ? 177.230 148.297 108.847 1.00 22.71  ? 4013 HIS A N     1 
ATOM   17164 C  CA    . HIS A 1 2796 ? 177.802 147.131 108.182 1.00 24.38  ? 4013 HIS A CA    1 
ATOM   17165 C  C     . HIS A 1 2796 ? 176.735 146.329 107.445 1.00 23.93  ? 4013 HIS A C     1 
ATOM   17166 O  O     . HIS A 1 2796 ? 176.915 145.974 106.274 1.00 26.09  ? 4013 HIS A O     1 
ATOM   17167 C  CB    . HIS A 1 2796 ? 178.532 146.242 109.187 1.00 21.26  ? 4013 HIS A CB    1 
ATOM   17168 C  CG    . HIS A 1 2796 ? 179.115 145.006 108.574 1.00 25.60  ? 4013 HIS A CG    1 
ATOM   17169 N  ND1   . HIS A 1 2796 ? 180.224 145.035 107.756 1.00 29.92  ? 4013 HIS A ND1   1 
ATOM   17170 C  CD2   . HIS A 1 2796 ? 178.734 143.709 108.645 1.00 28.32  ? 4013 HIS A CD2   1 
ATOM   17171 C  CE1   . HIS A 1 2796 ? 180.505 143.808 107.356 1.00 30.76  ? 4013 HIS A CE1   1 
ATOM   17172 N  NE2   . HIS A 1 2796 ? 179.616 142.985 107.881 1.00 31.13  ? 4013 HIS A NE2   1 
ATOM   17173 N  N     . VAL A 1 2797 ? 175.617 146.030 108.112 1.00 19.09  ? 4014 VAL A N     1 
ATOM   17174 C  CA    . VAL A 1 2797 ? 174.614 145.153 107.510 1.00 15.51  ? 4014 VAL A CA    1 
ATOM   17175 C  C     . VAL A 1 2797 ? 173.902 145.851 106.358 1.00 20.08  ? 4014 VAL A C     1 
ATOM   17176 O  O     . VAL A 1 2797 ? 173.768 145.296 105.261 1.00 24.02  ? 4014 VAL A O     1 
ATOM   17177 C  CB    . VAL A 1 2797 ? 173.613 144.670 108.572 1.00 11.72  ? 4014 VAL A CB    1 
ATOM   17178 C  CG1   . VAL A 1 2797 ? 172.454 143.962 107.903 1.00 11.87  ? 4014 VAL A CG1   1 
ATOM   17179 C  CG2   . VAL A 1 2797 ? 174.299 143.752 109.561 1.00 15.15  ? 4014 VAL A CG2   1 
ATOM   17180 N  N     . PHE A 1 2798 ? 173.448 147.082 106.580 1.00 20.79  ? 4015 PHE A N     1 
ATOM   17181 C  CA    . PHE A 1 2798 ? 172.643 147.817 105.606 1.00 20.69  ? 4015 PHE A CA    1 
ATOM   17182 C  C     . PHE A 1 2798 ? 173.479 148.797 104.800 1.00 23.24  ? 4015 PHE A C     1 
ATOM   17183 O  O     . PHE A 1 2798 ? 173.026 149.902 104.495 1.00 26.07  ? 4015 PHE A O     1 
ATOM   17184 C  CB    . PHE A 1 2798 ? 171.499 148.544 106.304 1.00 14.75  ? 4015 PHE A CB    1 
ATOM   17185 C  CG    . PHE A 1 2798 ? 170.466 147.632 106.891 1.00 10.48  ? 4015 PHE A CG    1 
ATOM   17186 C  CD1   . PHE A 1 2798 ? 169.529 147.016 106.083 1.00 10.68  ? 4015 PHE A CD1   1 
ATOM   17187 C  CD2   . PHE A 1 2798 ? 170.427 147.398 108.252 1.00 9.58   ? 4015 PHE A CD2   1 
ATOM   17188 C  CE1   . PHE A 1 2798 ? 168.576 146.180 106.621 1.00 10.97  ? 4015 PHE A CE1   1 
ATOM   17189 C  CE2   . PHE A 1 2798 ? 169.477 146.563 108.795 1.00 8.57   ? 4015 PHE A CE2   1 
ATOM   17190 C  CZ    . PHE A 1 2798 ? 168.550 145.953 107.979 1.00 9.33   ? 4015 PHE A CZ    1 
ATOM   17191 N  N     . CYS A 1 2799 ? 174.713 148.421 104.459 1.00 22.71  ? 4016 CYS A N     1 
ATOM   17192 C  CA    . CYS A 1 2799 ? 175.567 149.309 103.677 1.00 32.71  ? 4016 CYS A CA    1 
ATOM   17193 C  C     . CYS A 1 2799 ? 175.037 149.501 102.262 1.00 40.01  ? 4016 CYS A C     1 
ATOM   17194 O  O     . CYS A 1 2799 ? 175.267 150.554 101.655 1.00 39.40  ? 4016 CYS A O     1 
ATOM   17195 C  CB    . CYS A 1 2799 ? 176.995 148.766 103.638 1.00 36.97  ? 4016 CYS A CB    1 
ATOM   17196 S  SG    . CYS A 1 2799 ? 178.249 149.988 103.190 1.00 61.81  ? 4016 CYS A SG    1 
ATOM   17197 N  N     . GLY A 1 2800 ? 174.326 148.511 101.729 1.00 37.29  ? 4017 GLY A N     1 
ATOM   17198 C  CA    . GLY A 1 2800 ? 173.793 148.603 100.383 1.00 38.84  ? 4017 GLY A CA    1 
ATOM   17199 C  C     . GLY A 1 2800 ? 174.841 148.643 99.295  1.00 52.52  ? 4017 GLY A C     1 
ATOM   17200 O  O     . GLY A 1 2800 ? 174.603 149.232 98.236  1.00 55.13  ? 4017 GLY A O     1 
ATOM   17201 N  N     . SER A 1 2801 ? 175.997 148.030 99.525  1.00 54.61  ? 4018 SER A N     1 
ATOM   17202 C  CA    . SER A 1 2801 ? 177.071 148.019 98.547  1.00 55.87  ? 4018 SER A CA    1 
ATOM   17203 C  C     . SER A 1 2801 ? 176.891 146.861 97.569  1.00 60.27  ? 4018 SER A C     1 
ATOM   17204 O  O     . SER A 1 2801 ? 176.038 145.989 97.744  1.00 60.70  ? 4018 SER A O     1 
ATOM   17205 C  CB    . SER A 1 2801 ? 178.428 147.927 99.244  1.00 55.15  ? 4018 SER A CB    1 
ATOM   17206 O  OG    . SER A 1 2801 ? 178.746 146.583 99.556  1.00 56.06  ? 4018 SER A OG    1 
ATOM   17207 N  N     . ASP A 1 2802 ? 177.710 146.870 96.514  1.00 63.10  ? 4019 ASP A N     1 
ATOM   17208 C  CA    . ASP A 1 2802 ? 177.637 145.815 95.509  1.00 63.68  ? 4019 ASP A CA    1 
ATOM   17209 C  C     . ASP A 1 2802 ? 178.097 144.478 96.078  1.00 61.72  ? 4019 ASP A C     1 
ATOM   17210 O  O     . ASP A 1 2802 ? 177.430 143.453 95.899  1.00 58.58  ? 4019 ASP A O     1 
ATOM   17211 C  CB    . ASP A 1 2802 ? 178.471 146.198 94.287  1.00 68.64  ? 4019 ASP A CB    1 
ATOM   17212 C  CG    . ASP A 1 2802 ? 177.889 147.375 93.530  1.00 75.05  ? 4019 ASP A CG    1 
ATOM   17213 O  OD1   . ASP A 1 2802 ? 176.655 147.562 93.576  1.00 73.47  ? 4019 ASP A OD1   1 
ATOM   17214 O  OD2   . ASP A 1 2802 ? 178.665 148.113 92.888  1.00 85.02  ? 4019 ASP A OD2   1 
ATOM   17215 N  N     . ASN A 1 2803 ? 179.230 144.470 96.772  1.00 64.25  ? 4020 ASN A N     1 
ATOM   17216 C  CA    . ASN A 1 2803 ? 179.756 143.273 97.413  1.00 62.74  ? 4020 ASN A CA    1 
ATOM   17217 C  C     . ASN A 1 2803 ? 179.615 143.405 98.922  1.00 59.33  ? 4020 ASN A C     1 
ATOM   17218 O  O     . ASN A 1 2803 ? 180.090 144.380 99.514  1.00 58.49  ? 4020 ASN A O     1 
ATOM   17219 C  CB    . ASN A 1 2803 ? 181.217 143.035 97.019  1.00 64.62  ? 4020 ASN A CB    1 
ATOM   17220 C  CG    . ASN A 1 2803 ? 182.051 144.305 97.046  1.00 71.02  ? 4020 ASN A CG    1 
ATOM   17221 O  OD1   . ASN A 1 2803 ? 181.556 145.386 97.364  1.00 68.75  ? 4020 ASN A OD1   1 
ATOM   17222 N  ND2   . ASN A 1 2803 ? 183.328 144.176 96.707  1.00 77.83  ? 4020 ASN A ND2   1 
ATOM   17223 N  N     . LEU A 1 2804 ? 178.960 142.425 99.542  1.00 55.85  ? 4021 LEU A N     1 
ATOM   17224 C  CA    . LEU A 1 2804 ? 178.637 142.475 100.967 1.00 51.10  ? 4021 LEU A CA    1 
ATOM   17225 C  C     . LEU A 1 2804 ? 179.202 141.237 101.653 1.00 47.94  ? 4021 LEU A C     1 
ATOM   17226 O  O     . LEU A 1 2804 ? 178.601 140.160 101.601 1.00 47.89  ? 4021 LEU A O     1 
ATOM   17227 C  CB    . LEU A 1 2804 ? 177.134 142.582 101.183 1.00 42.41  ? 4021 LEU A CB    1 
ATOM   17228 C  CG    . LEU A 1 2804 ? 176.704 142.729 102.641 1.00 32.62  ? 4021 LEU A CG    1 
ATOM   17229 C  CD1   . LEU A 1 2804 ? 177.143 144.071 103.198 1.00 32.30  ? 4021 LEU A CD1   1 
ATOM   17230 C  CD2   . LEU A 1 2804 ? 175.209 142.568 102.753 1.00 28.98  ? 4021 LEU A CD2   1 
ATOM   17231 N  N     . GLN A 1 2805 ? 180.355 141.397 102.296 1.00 46.81  ? 4022 GLN A N     1 
ATOM   17232 C  CA    . GLN A 1 2805 ? 180.948 140.351 103.125 1.00 43.40  ? 4022 GLN A CA    1 
ATOM   17233 C  C     . GLN A 1 2805 ? 180.406 140.537 104.535 1.00 41.57  ? 4022 GLN A C     1 
ATOM   17234 O  O     . GLN A 1 2805 ? 180.962 141.283 105.342 1.00 46.81  ? 4022 GLN A O     1 
ATOM   17235 C  CB    . GLN A 1 2805 ? 182.469 140.430 103.082 1.00 46.77  ? 4022 GLN A CB    1 
ATOM   17236 C  CG    . GLN A 1 2805 ? 183.188 139.234 103.681 1.00 46.32  ? 4022 GLN A CG    1 
ATOM   17237 C  CD    . GLN A 1 2805 ? 183.451 138.139 102.668 1.00 49.43  ? 4022 GLN A CD    1 
ATOM   17238 O  OE1   . GLN A 1 2805 ? 183.899 138.404 101.553 1.00 47.78  ? 4022 GLN A OE1   1 
ATOM   17239 N  NE2   . GLN A 1 2805 ? 183.173 136.899 103.051 1.00 48.12  ? 4022 GLN A NE2   1 
ATOM   17240 N  N     . ILE A 1 2806 ? 179.284 139.869 104.825 1.00 37.41  ? 4023 ILE A N     1 
ATOM   17241 C  CA    . ILE A 1 2806 ? 178.659 139.990 106.142 1.00 36.43  ? 4023 ILE A CA    1 
ATOM   17242 C  C     . ILE A 1 2806 ? 179.588 139.443 107.218 1.00 40.83  ? 4023 ILE A C     1 
ATOM   17243 O  O     . ILE A 1 2806 ? 179.871 140.108 108.222 1.00 46.68  ? 4023 ILE A O     1 
ATOM   17244 C  CB    . ILE A 1 2806 ? 177.298 139.271 106.156 1.00 32.21  ? 4023 ILE A CB    1 
ATOM   17245 C  CG1   . ILE A 1 2806 ? 176.250 140.081 105.390 1.00 32.88  ? 4023 ILE A CG1   1 
ATOM   17246 C  CG2   . ILE A 1 2806 ? 176.843 139.029 107.582 1.00 32.64  ? 4023 ILE A CG2   1 
ATOM   17247 C  CD1   . ILE A 1 2806 ? 175.620 141.201 106.191 1.00 31.53  ? 4023 ILE A CD1   1 
ATOM   17248 N  N     . VAL A 1 2807 ? 180.083 138.229 107.015 1.00 40.10  ? 4024 VAL A N     1 
ATOM   17249 C  CA    . VAL A 1 2807 ? 181.144 137.654 107.838 1.00 39.18  ? 4024 VAL A CA    1 
ATOM   17250 C  C     . VAL A 1 2807 ? 182.253 137.220 106.890 1.00 45.95  ? 4024 VAL A C     1 
ATOM   17251 O  O     . VAL A 1 2807 ? 182.003 137.011 105.693 1.00 49.06  ? 4024 VAL A O     1 
ATOM   17252 C  CB    . VAL A 1 2807 ? 180.628 136.472 108.695 1.00 37.42  ? 4024 VAL A CB    1 
ATOM   17253 C  CG1   . VAL A 1 2807 ? 179.460 136.906 109.568 1.00 35.36  ? 4024 VAL A CG1   1 
ATOM   17254 C  CG2   . VAL A 1 2807 ? 180.247 135.298 107.820 1.00 43.62  ? 4024 VAL A CG2   1 
ATOM   17255 N  N     . PRO A 1 2808 ? 183.504 137.091 107.385 1.00 46.77  ? 4025 PRO A N     1 
ATOM   17256 C  CA    . PRO A 1 2808 ? 184.627 136.792 106.477 1.00 47.95  ? 4025 PRO A CA    1 
ATOM   17257 C  C     . PRO A 1 2808 ? 184.511 135.500 105.671 1.00 50.93  ? 4025 PRO A C     1 
ATOM   17258 O  O     . PRO A 1 2808 ? 185.374 135.226 104.831 1.00 53.65  ? 4025 PRO A O     1 
ATOM   17259 C  CB    . PRO A 1 2808 ? 185.827 136.732 107.429 1.00 45.98  ? 4025 PRO A CB    1 
ATOM   17260 C  CG    . PRO A 1 2808 ? 185.465 137.653 108.527 1.00 43.58  ? 4025 PRO A CG    1 
ATOM   17261 C  CD    . PRO A 1 2808 ? 183.987 137.480 108.725 1.00 44.54  ? 4025 PRO A CD    1 
ATOM   17262 N  N     . GLY A 1 2809 ? 183.469 134.704 105.901 1.00 49.04  ? 4026 GLY A N     1 
ATOM   17263 C  CA    . GLY A 1 2809 ? 183.255 133.504 105.119 1.00 50.70  ? 4026 GLY A CA    1 
ATOM   17264 C  C     . GLY A 1 2809 ? 182.277 133.636 103.966 1.00 47.05  ? 4026 GLY A C     1 
ATOM   17265 O  O     . GLY A 1 2809 ? 182.599 133.250 102.839 1.00 49.00  ? 4026 GLY A O     1 
ATOM   17266 N  N     . VAL A 1 2810 ? 181.091 134.186 104.220 1.00 43.17  ? 4027 VAL A N     1 
ATOM   17267 C  CA    . VAL A 1 2810 ? 179.999 134.141 103.255 1.00 46.69  ? 4027 VAL A CA    1 
ATOM   17268 C  C     . VAL A 1 2810 ? 179.668 135.547 102.769 1.00 48.15  ? 4027 VAL A C     1 
ATOM   17269 O  O     . VAL A 1 2810 ? 180.021 136.555 103.387 1.00 49.82  ? 4027 VAL A O     1 
ATOM   17270 C  CB    . VAL A 1 2810 ? 178.741 133.460 103.834 1.00 43.87  ? 4027 VAL A CB    1 
ATOM   17271 C  CG1   . VAL A 1 2810 ? 179.050 132.028 104.240 1.00 45.82  ? 4027 VAL A CG1   1 
ATOM   17272 C  CG2   . VAL A 1 2810 ? 178.187 134.252 105.001 1.00 35.62  ? 4027 VAL A CG2   1 
ATOM   17273 N  N     . ARG A 1 2811 ? 178.975 135.600 101.632 1.00 46.39  ? 4028 ARG A N     1 
ATOM   17274 C  CA    . ARG A 1 2811 ? 178.561 136.846 101.006 1.00 46.44  ? 4028 ARG A CA    1 
ATOM   17275 C  C     . ARG A 1 2811 ? 177.137 136.698 100.491 1.00 43.93  ? 4028 ARG A C     1 
ATOM   17276 O  O     . ARG A 1 2811 ? 176.704 135.601 100.131 1.00 44.96  ? 4028 ARG A O     1 
ATOM   17277 C  CB    . ARG A 1 2811 ? 179.497 137.238 99.855  1.00 50.00  ? 4028 ARG A CB    1 
ATOM   17278 C  CG    . ARG A 1 2811 ? 180.824 137.823 100.304 1.00 49.66  ? 4028 ARG A CG    1 
ATOM   17279 C  CD    . ARG A 1 2811 ? 181.711 138.170 99.120  1.00 47.53  ? 4028 ARG A CD    1 
ATOM   17280 N  NE    . ARG A 1 2811 ? 181.020 138.989 98.131  1.00 52.93  ? 4028 ARG A NE    1 
ATOM   17281 C  CZ    . ARG A 1 2811 ? 181.224 138.912 96.823  1.00 58.24  ? 4028 ARG A CZ    1 
ATOM   17282 N  NH1   . ARG A 1 2811 ? 182.098 138.063 96.308  1.00 58.64  ? 4028 ARG A NH1   1 
ATOM   17283 N  NH2   . ARG A 1 2811 ? 180.534 139.708 96.011  1.00 59.21  ? 4028 ARG A NH2   1 
ATOM   17284 N  N     . ILE A 1 2812 ? 176.416 137.810 100.457 1.00 42.57  ? 4029 ILE A N     1 
ATOM   17285 C  CA    . ILE A 1 2812 ? 175.032 137.849 100.006 1.00 44.12  ? 4029 ILE A CA    1 
ATOM   17286 C  C     . ILE A 1 2812 ? 174.953 138.737 98.771  1.00 47.10  ? 4029 ILE A C     1 
ATOM   17287 O  O     . ILE A 1 2812 ? 174.894 139.963 98.876  1.00 50.32  ? 4029 ILE A O     1 
ATOM   17288 C  CB    . ILE A 1 2812 ? 174.091 138.359 101.113 1.00 40.40  ? 4029 ILE A CB    1 
ATOM   17289 C  CG1   . ILE A 1 2812 ? 174.415 137.687 102.446 1.00 37.49  ? 4029 ILE A CG1   1 
ATOM   17290 C  CG2   . ILE A 1 2812 ? 172.642 138.117 100.734 1.00 37.59  ? 4029 ILE A CG2   1 
ATOM   17291 C  CD1   . ILE A 1 2812 ? 173.585 138.196 103.595 1.00 34.92  ? 4029 ILE A CD1   1 
ATOM   17292 N  N     . PRO A 1 2813 ? 174.962 138.152 97.575  1.00 47.62  ? 4030 PRO A N     1 
ATOM   17293 C  CA    . PRO A 1 2813 ? 174.788 138.956 96.360  1.00 49.38  ? 4030 PRO A CA    1 
ATOM   17294 C  C     . PRO A 1 2813 ? 173.375 139.509 96.248  1.00 50.03  ? 4030 PRO A C     1 
ATOM   17295 O  O     . PRO A 1 2813 ? 172.406 138.912 96.722  1.00 48.69  ? 4030 PRO A O     1 
ATOM   17296 C  CB    . PRO A 1 2813 ? 175.090 137.970 95.224  1.00 51.10  ? 4030 PRO A CB    1 
ATOM   17297 C  CG    . PRO A 1 2813 ? 175.703 136.768 95.873  1.00 51.71  ? 4030 PRO A CG    1 
ATOM   17298 C  CD    . PRO A 1 2813 ? 175.200 136.732 97.275  1.00 49.52  ? 4030 PRO A CD    1 
ATOM   17299 N  N     . GLN A 1 2814 ? 173.273 140.669 95.602  1.00 53.96  ? 4031 GLN A N     1 
ATOM   17300 C  CA    . GLN A 1 2814 ? 172.013 141.373 95.429  1.00 53.34  ? 4031 GLN A CA    1 
ATOM   17301 C  C     . GLN A 1 2814 ? 171.146 140.677 94.381  1.00 54.15  ? 4031 GLN A C     1 
ATOM   17302 O  O     . GLN A 1 2814 ? 171.666 140.056 93.450  1.00 57.62  ? 4031 GLN A O     1 
ATOM   17303 C  CB    . GLN A 1 2814 ? 172.265 142.821 95.010  1.00 51.75  ? 4031 GLN A CB    1 
ATOM   17304 C  CG    . GLN A 1 2814 ? 173.169 142.989 93.796  1.00 55.84  ? 4031 GLN A CG    1 
ATOM   17305 C  CD    . GLN A 1 2814 ? 174.641 143.041 94.158  1.00 60.97  ? 4031 GLN A CD    1 
ATOM   17306 O  OE1   . GLN A 1 2814 ? 175.148 142.169 94.863  1.00 57.47  ? 4031 GLN A OE1   1 
ATOM   17307 N  NE2   . GLN A 1 2814 ? 175.334 144.065 93.677  1.00 65.79  ? 4031 GLN A NE2   1 
ATOM   17308 N  N     . PRO A 1 2815 ? 169.823 140.748 94.524  1.00 50.75  ? 4032 PRO A N     1 
ATOM   17309 C  CA    . PRO A 1 2815 ? 168.943 140.142 93.521  1.00 57.31  ? 4032 PRO A CA    1 
ATOM   17310 C  C     . PRO A 1 2815 ? 169.054 140.843 92.178  1.00 63.29  ? 4032 PRO A C     1 
ATOM   17311 O  O     . PRO A 1 2815 ? 169.249 142.058 92.096  1.00 63.96  ? 4032 PRO A O     1 
ATOM   17312 C  CB    . PRO A 1 2815 ? 167.543 140.317 94.121  1.00 54.83  ? 4032 PRO A CB    1 
ATOM   17313 C  CG    . PRO A 1 2815 ? 167.678 141.444 95.075  1.00 47.94  ? 4032 PRO A CG    1 
ATOM   17314 C  CD    . PRO A 1 2815 ? 169.060 141.338 95.636  1.00 47.67  ? 4032 PRO A CD    1 
ATOM   17315 N  N     . LEU A 1 2816 ? 168.927 140.056 91.116  1.00 66.44  ? 4033 LEU A N     1 
ATOM   17316 C  CA    . LEU A 1 2816 ? 168.969 140.588 89.765  1.00 75.13  ? 4033 LEU A CA    1 
ATOM   17317 C  C     . LEU A 1 2816 ? 167.557 140.913 89.285  1.00 78.03  ? 4033 LEU A C     1 
ATOM   17318 O  O     . LEU A 1 2816 ? 166.561 140.440 89.837  1.00 75.05  ? 4033 LEU A O     1 
ATOM   17319 C  CB    . LEU A 1 2816 ? 169.652 139.606 88.810  1.00 76.74  ? 4033 LEU A CB    1 
ATOM   17320 C  CG    . LEU A 1 2816 ? 171.176 139.711 88.640  1.00 70.56  ? 4033 LEU A CG    1 
ATOM   17321 C  CD1   . LEU A 1 2816 ? 171.562 141.072 88.075  1.00 70.86  ? 4033 LEU A CD1   1 
ATOM   17322 C  CD2   . LEU A 1 2816 ? 171.936 139.425 89.931  1.00 62.60  ? 4033 LEU A CD2   1 
ATOM   17323 N  N     . LEU A 1 2817 ? 167.483 141.730 88.234  1.00 81.47  ? 4034 LEU A N     1 
ATOM   17324 C  CA    . LEU A 1 2817 ? 166.241 142.372 87.822  1.00 86.07  ? 4034 LEU A CA    1 
ATOM   17325 C  C     . LEU A 1 2817 ? 165.526 141.618 86.705  1.00 89.42  ? 4034 LEU A C     1 
ATOM   17326 O  O     . LEU A 1 2817 ? 164.895 142.242 85.845  1.00 92.19  ? 4034 LEU A O     1 
ATOM   17327 C  CB    . LEU A 1 2817 ? 166.514 143.814 87.395  1.00 86.11  ? 4034 LEU A CB    1 
ATOM   17328 C  CG    . LEU A 1 2817 ? 167.285 144.679 88.394  1.00 87.03  ? 4034 LEU A CG    1 
ATOM   17329 C  CD1   . LEU A 1 2817 ? 167.815 145.937 87.722  1.00 91.00  ? 4034 LEU A CD1   1 
ATOM   17330 C  CD2   . LEU A 1 2817 ? 166.413 145.030 89.590  1.00 83.54  ? 4034 LEU A CD2   1 
ATOM   17331 N  N     . GLN A 1 2818 ? 165.613 140.284 86.693  1.00 87.76  ? 4035 GLN A N     1 
ATOM   17332 C  CA    . GLN A 1 2818 ? 164.909 139.513 85.675  1.00 87.87  ? 4035 GLN A CA    1 
ATOM   17333 C  C     . GLN A 1 2818 ? 164.268 138.244 86.233  1.00 89.15  ? 4035 GLN A C     1 
ATOM   17334 O  O     . GLN A 1 2818 ? 163.949 137.334 85.458  1.00 90.74  ? 4035 GLN A O     1 
ATOM   17335 C  CB    . GLN A 1 2818 ? 165.852 139.143 84.523  1.00 88.03  ? 4035 GLN A CB    1 
ATOM   17336 C  CG    . GLN A 1 2818 ? 167.030 138.272 84.932  1.00 90.90  ? 4035 GLN A CG    1 
ATOM   17337 C  CD    . GLN A 1 2818 ? 168.262 139.081 85.286  1.00 88.75  ? 4035 GLN A CD    1 
ATOM   17338 O  OE1   . GLN A 1 2818 ? 168.172 140.118 85.942  1.00 86.99  ? 4035 GLN A OE1   1 
ATOM   17339 N  NE2   . GLN A 1 2818 ? 169.424 138.605 84.855  1.00 90.32  ? 4035 GLN A NE2   1 
ATOM   17340 N  N     . GLN A 1 2819 ? 164.061 138.155 87.547  1.00 86.40  ? 4036 GLN A N     1 
ATOM   17341 C  CA    . GLN A 1 2819 ? 163.567 136.916 88.138  1.00 85.26  ? 4036 GLN A CA    1 
ATOM   17342 C  C     . GLN A 1 2819 ? 162.386 137.155 89.071  1.00 82.67  ? 4036 GLN A C     1 
ATOM   17343 O  O     . GLN A 1 2819 ? 161.833 138.258 89.119  1.00 81.44  ? 4036 GLN A O     1 
ATOM   17344 C  CB    . GLN A 1 2819 ? 164.684 136.209 88.901  1.00 84.89  ? 4036 GLN A CB    1 
ATOM   17345 C  CG    . GLN A 1 2819 ? 165.868 135.784 88.057  1.00 87.38  ? 4036 GLN A CG    1 
ATOM   17346 C  CD    . GLN A 1 2819 ? 167.059 136.697 88.256  1.00 87.45  ? 4036 GLN A CD    1 
ATOM   17347 O  OE1   . GLN A 1 2819 ? 166.937 137.919 88.176  1.00 86.01  ? 4036 GLN A OE1   1 
ATOM   17348 N  NE2   . GLN A 1 2819 ? 168.220 136.108 88.520  1.00 86.85  ? 4036 GLN A NE2   1 
ATOM   17349 N  N     . SER A 1 2820 ? 161.999 136.122 89.816  1.00 80.33  ? 4037 SER A N     1 
ATOM   17350 C  CA    . SER A 1 2820 ? 160.874 136.162 90.738  1.00 78.88  ? 4037 SER A CA    1 
ATOM   17351 C  C     . SER A 1 2820 ? 161.371 136.046 92.177  1.00 74.43  ? 4037 SER A C     1 
ATOM   17352 O  O     . SER A 1 2820 ? 162.571 135.935 92.442  1.00 70.94  ? 4037 SER A O     1 
ATOM   17353 C  CB    . SER A 1 2820 ? 159.874 135.051 90.413  1.00 76.43  ? 4037 SER A CB    1 
ATOM   17354 O  OG    . SER A 1 2820 ? 160.327 133.802 90.907  1.00 74.48  ? 4037 SER A OG    1 
ATOM   17355 N  N     . GLU A 1 2821 ? 160.422 136.068 93.116  1.00 73.90  ? 4038 GLU A N     1 
ATOM   17356 C  CA    . GLU A 1 2821 ? 160.768 136.060 94.534  1.00 66.94  ? 4038 GLU A CA    1 
ATOM   17357 C  C     . GLU A 1 2821 ? 161.027 134.655 95.068  1.00 67.48  ? 4038 GLU A C     1 
ATOM   17358 O  O     . GLU A 1 2821 ? 161.810 134.494 96.013  1.00 65.55  ? 4038 GLU A O     1 
ATOM   17359 C  CB    . GLU A 1 2821 ? 159.663 136.742 95.344  1.00 64.15  ? 4038 GLU A CB    1 
ATOM   17360 C  CG    . GLU A 1 2821 ? 158.289 136.097 95.225  1.00 67.54  ? 4038 GLU A CG    1 
ATOM   17361 C  CD    . GLU A 1 2821 ? 157.983 135.156 96.373  1.00 67.06  ? 4038 GLU A CD    1 
ATOM   17362 O  OE1   . GLU A 1 2821 ? 158.666 135.245 97.415  1.00 68.50  ? 4038 GLU A OE1   1 
ATOM   17363 O  OE2   . GLU A 1 2821 ? 157.057 134.329 96.236  1.00 64.86  ? 4038 GLU A OE2   1 
ATOM   17364 N  N     . GLU A 1 2822 ? 160.380 133.636 94.493  1.00 67.54  ? 4039 GLU A N     1 
ATOM   17365 C  CA    . GLU A 1 2822 ? 160.578 132.269 94.965  1.00 66.64  ? 4039 GLU A CA    1 
ATOM   17366 C  C     . GLU A 1 2822 ? 162.007 131.799 94.721  1.00 67.73  ? 4039 GLU A C     1 
ATOM   17367 O  O     . GLU A 1 2822 ? 162.613 131.158 95.590  1.00 69.17  ? 4039 GLU A O     1 
ATOM   17368 C  CB    . GLU A 1 2822 ? 159.580 131.329 94.292  1.00 66.93  ? 4039 GLU A CB    1 
ATOM   17369 C  CG    . GLU A 1 2822 ? 158.140 131.542 94.724  1.00 69.57  ? 4039 GLU A CG    1 
ATOM   17370 C  CD    . GLU A 1 2822 ? 157.354 132.380 93.736  1.00 71.70  ? 4039 GLU A CD    1 
ATOM   17371 O  OE1   . GLU A 1 2822 ? 157.970 132.933 92.801  1.00 71.76  ? 4039 GLU A OE1   1 
ATOM   17372 O  OE2   . GLU A 1 2822 ? 156.119 132.485 93.892  1.00 69.40  ? 4039 GLU A OE2   1 
ATOM   17373 N  N     . GLU A 1 2823 ? 162.569 132.121 93.552  1.00 67.22  ? 4040 GLU A N     1 
ATOM   17374 C  CA    . GLU A 1 2823 ? 163.951 131.743 93.292  1.00 67.43  ? 4040 GLU A CA    1 
ATOM   17375 C  C     . GLU A 1 2823 ? 164.905 132.510 94.197  1.00 65.08  ? 4040 GLU A C     1 
ATOM   17376 O  O     . GLU A 1 2823 ? 165.963 131.990 94.557  1.00 61.11  ? 4040 GLU A O     1 
ATOM   17377 C  CB    . GLU A 1 2823 ? 164.308 131.966 91.817  1.00 75.07  ? 4040 GLU A CB    1 
ATOM   17378 C  CG    . GLU A 1 2823 ? 164.322 133.420 91.360  1.00 75.99  ? 4040 GLU A CG    1 
ATOM   17379 C  CD    . GLU A 1 2823 ? 165.683 134.072 91.570  1.00 76.06  ? 4040 GLU A CD    1 
ATOM   17380 O  OE1   . GLU A 1 2823 ? 166.683 133.331 91.664  1.00 73.73  ? 4040 GLU A OE1   1 
ATOM   17381 O  OE2   . GLU A 1 2823 ? 165.748 135.311 91.700  1.00 75.25  ? 4040 GLU A OE2   1 
ATOM   17382 N  N     . GLU A 1 2824 ? 164.550 133.742 94.576  1.00 63.57  ? 4041 GLU A N     1 
ATOM   17383 C  CA    . GLU A 1 2824 ? 165.391 134.505 95.492  1.00 59.80  ? 4041 GLU A CA    1 
ATOM   17384 C  C     . GLU A 1 2824 ? 165.380 133.894 96.885  1.00 55.95  ? 4041 GLU A C     1 
ATOM   17385 O  O     . GLU A 1 2824 ? 166.429 133.797 97.535  1.00 54.86  ? 4041 GLU A O     1 
ATOM   17386 C  CB    . GLU A 1 2824 ? 164.931 135.960 95.543  1.00 55.35  ? 4041 GLU A CB    1 
ATOM   17387 C  CG    . GLU A 1 2824 ? 165.652 136.856 94.561  1.00 55.87  ? 4041 GLU A CG    1 
ATOM   17388 C  CD    . GLU A 1 2824 ? 167.134 136.941 94.843  1.00 55.01  ? 4041 GLU A CD    1 
ATOM   17389 O  OE1   . GLU A 1 2824 ? 167.513 136.979 96.031  1.00 55.15  ? 4041 GLU A OE1   1 
ATOM   17390 O  OE2   . GLU A 1 2824 ? 167.923 136.965 93.876  1.00 56.54  ? 4041 GLU A OE2   1 
ATOM   17391 N  N     . ARG A 1 2825 ? 164.201 133.479 97.357  1.00 55.01  ? 4042 ARG A N     1 
ATOM   17392 C  CA    . ARG A 1 2825 ? 164.121 132.762 98.624  1.00 51.08  ? 4042 ARG A CA    1 
ATOM   17393 C  C     . ARG A 1 2825 ? 164.935 131.477 98.572  1.00 51.31  ? 4042 ARG A C     1 
ATOM   17394 O  O     . ARG A 1 2825 ? 165.659 131.151 99.523  1.00 51.95  ? 4042 ARG A O     1 
ATOM   17395 C  CB    . ARG A 1 2825 ? 162.661 132.462 98.962  1.00 47.39  ? 4042 ARG A CB    1 
ATOM   17396 C  CG    . ARG A 1 2825 ? 162.380 132.313 100.443 1.00 46.79  ? 4042 ARG A CG    1 
ATOM   17397 C  CD    . ARG A 1 2825 ? 161.071 131.583 100.677 1.00 46.97  ? 4042 ARG A CD    1 
ATOM   17398 N  NE    . ARG A 1 2825 ? 160.635 131.670 102.064 1.00 47.76  ? 4042 ARG A NE    1 
ATOM   17399 C  CZ    . ARG A 1 2825 ? 161.017 130.836 103.022 1.00 46.40  ? 4042 ARG A CZ    1 
ATOM   17400 N  NH1   . ARG A 1 2825 ? 161.856 129.843 102.779 1.00 42.77  ? 4042 ARG A NH1   1 
ATOM   17401 N  NH2   . ARG A 1 2825 ? 160.546 131.004 104.254 1.00 46.65  ? 4042 ARG A NH2   1 
ATOM   17402 N  N     . ALA A 1 2826 ? 164.853 130.752 97.453  1.00 50.10  ? 4043 ALA A N     1 
ATOM   17403 C  CA    . ALA A 1 2826 ? 165.641 129.534 97.291  1.00 52.96  ? 4043 ALA A CA    1 
ATOM   17404 C  C     . ALA A 1 2826 ? 167.138 129.827 97.306  1.00 54.28  ? 4043 ALA A C     1 
ATOM   17405 O  O     . ALA A 1 2826 ? 167.913 129.088 97.921  1.00 58.26  ? 4043 ALA A O     1 
ATOM   17406 C  CB    . ALA A 1 2826 ? 165.247 128.825 95.997  1.00 58.85  ? 4043 ALA A CB    1 
ATOM   17407 N  N     . ARG A 1 2827 ? 167.562 130.905 96.639  1.00 48.19  ? 4044 ARG A N     1 
ATOM   17408 C  CA    . ARG A 1 2827 ? 168.984 131.227 96.562  1.00 46.42  ? 4044 ARG A CA    1 
ATOM   17409 C  C     . ARG A 1 2827 ? 169.527 131.625 97.929  1.00 48.61  ? 4044 ARG A C     1 
ATOM   17410 O  O     . ARG A 1 2827 ? 170.630 131.213 98.312  1.00 52.33  ? 4044 ARG A O     1 
ATOM   17411 C  CB    . ARG A 1 2827 ? 169.207 132.341 95.530  1.00 45.21  ? 4044 ARG A CB    1 
ATOM   17412 C  CG    . ARG A 1 2827 ? 170.666 132.623 95.142  1.00 44.90  ? 4044 ARG A CG    1 
ATOM   17413 C  CD    . ARG A 1 2827 ? 171.386 133.614 96.049  1.00 43.97  ? 4044 ARG A CD    1 
ATOM   17414 N  NE    . ARG A 1 2827 ? 170.707 134.899 96.164  1.00 51.75  ? 4044 ARG A NE    1 
ATOM   17415 C  CZ    . ARG A 1 2827 ? 170.821 135.888 95.288  1.00 54.32  ? 4044 ARG A CZ    1 
ATOM   17416 N  NH1   . ARG A 1 2827 ? 171.559 135.766 94.198  1.00 49.77  ? 4044 ARG A NH1   1 
ATOM   17417 N  NH2   . ARG A 1 2827 ? 170.187 137.034 95.519  1.00 54.53  ? 4044 ARG A NH2   1 
ATOM   17418 N  N     . LEU A 1 2828 ? 168.769 132.425 98.682  1.00 47.24  ? 4045 LEU A N     1 
ATOM   17419 C  CA    . LEU A 1 2828 ? 169.232 132.821 100.008 1.00 44.10  ? 4045 LEU A CA    1 
ATOM   17420 C  C     . LEU A 1 2828 ? 169.218 131.646 100.979 1.00 42.88  ? 4045 LEU A C     1 
ATOM   17421 O  O     . LEU A 1 2828 ? 170.114 131.533 101.826 1.00 44.62  ? 4045 LEU A O     1 
ATOM   17422 C  CB    . LEU A 1 2828 ? 168.388 133.983 100.530 1.00 44.23  ? 4045 LEU A CB    1 
ATOM   17423 C  CG    . LEU A 1 2828 ? 168.438 135.224 99.631  1.00 42.67  ? 4045 LEU A CG    1 
ATOM   17424 C  CD1   . LEU A 1 2828 ? 167.457 136.281 100.096 1.00 37.36  ? 4045 LEU A CD1   1 
ATOM   17425 C  CD2   . LEU A 1 2828 ? 169.846 135.793 99.548  1.00 40.71  ? 4045 LEU A CD2   1 
ATOM   17426 N  N     . THR A 1 2829 ? 168.239 130.744 100.857 1.00 42.99  ? 4046 THR A N     1 
ATOM   17427 C  CA    . THR A 1 2829 ? 168.256 129.531 101.668 1.00 46.09  ? 4046 THR A CA    1 
ATOM   17428 C  C     . THR A 1 2829 ? 169.449 128.650 101.309 1.00 46.58  ? 4046 THR A C     1 
ATOM   17429 O  O     . THR A 1 2829 ? 170.052 128.021 102.187 1.00 47.77  ? 4046 THR A O     1 
ATOM   17430 C  CB    . THR A 1 2829 ? 166.937 128.775 101.493 1.00 48.24  ? 4046 THR A CB    1 
ATOM   17431 O  OG1   . THR A 1 2829 ? 165.851 129.619 101.894 1.00 43.55  ? 4046 THR A OG1   1 
ATOM   17432 C  CG2   . THR A 1 2829 ? 166.912 127.517 102.346 1.00 52.35  ? 4046 THR A CG2   1 
ATOM   17433 N  N     . ALA A 1 2830 ? 169.815 128.606 100.025 1.00 46.04  ? 4047 ALA A N     1 
ATOM   17434 C  CA    . ALA A 1 2830 ? 170.998 127.858 99.607  1.00 49.19  ? 4047 ALA A CA    1 
ATOM   17435 C  C     . ALA A 1 2830 ? 172.274 128.477 100.164 1.00 50.30  ? 4047 ALA A C     1 
ATOM   17436 O  O     . ALA A 1 2830 ? 173.219 127.757 100.507 1.00 53.68  ? 4047 ALA A O     1 
ATOM   17437 C  CB    . ALA A 1 2830 ? 171.059 127.783 98.083  1.00 47.70  ? 4047 ALA A CB    1 
ATOM   17438 N  N     . ILE A 1 2831 ? 172.328 129.810 100.238 1.00 48.50  ? 4048 ILE A N     1 
ATOM   17439 C  CA    . ILE A 1 2831 ? 173.458 130.473 100.889 1.00 47.27  ? 4048 ILE A CA    1 
ATOM   17440 C  C     . ILE A 1 2831 ? 173.506 130.106 102.368 1.00 47.83  ? 4048 ILE A C     1 
ATOM   17441 O  O     . ILE A 1 2831 ? 174.585 129.892 102.937 1.00 47.29  ? 4048 ILE A O     1 
ATOM   17442 C  CB    . ILE A 1 2831 ? 173.383 131.999 100.680 1.00 43.89  ? 4048 ILE A CB    1 
ATOM   17443 C  CG1   . ILE A 1 2831 ? 173.683 132.358 99.225  1.00 45.82  ? 4048 ILE A CG1   1 
ATOM   17444 C  CG2   . ILE A 1 2831 ? 174.347 132.735 101.599 1.00 38.87  ? 4048 ILE A CG2   1 
ATOM   17445 C  CD1   . ILE A 1 2831 ? 173.563 133.834 98.940  1.00 43.21  ? 4048 ILE A CD1   1 
ATOM   17446 N  N     . LEU A 1 2832 ? 172.337 130.012 103.008 1.00 47.81  ? 4049 LEU A N     1 
ATOM   17447 C  CA    . LEU A 1 2832 ? 172.287 129.580 104.404 1.00 46.19  ? 4049 LEU A CA    1 
ATOM   17448 C  C     . LEU A 1 2832 ? 172.798 128.153 104.569 1.00 52.83  ? 4049 LEU A C     1 
ATOM   17449 O  O     . LEU A 1 2832 ? 173.528 127.854 105.522 1.00 54.18  ? 4049 LEU A O     1 
ATOM   17450 C  CB    . LEU A 1 2832 ? 170.864 129.691 104.947 1.00 41.59  ? 4049 LEU A CB    1 
ATOM   17451 C  CG    . LEU A 1 2832 ? 170.338 131.108 105.139 1.00 45.14  ? 4049 LEU A CG    1 
ATOM   17452 C  CD1   . LEU A 1 2832 ? 168.905 131.090 105.637 1.00 41.49  ? 4049 LEU A CD1   1 
ATOM   17453 C  CD2   . LEU A 1 2832 ? 171.240 131.853 106.095 1.00 46.45  ? 4049 LEU A CD2   1 
ATOM   17454 N  N     . SER A 1 2833 ? 172.421 127.257 103.655 1.00 51.81  ? 4050 SER A N     1 
ATOM   17455 C  CA    . SER A 1 2833 ? 172.810 125.856 103.777 1.00 48.83  ? 4050 SER A CA    1 
ATOM   17456 C  C     . SER A 1 2833 ? 174.305 125.659 103.564 1.00 50.26  ? 4050 SER A C     1 
ATOM   17457 O  O     . SER A 1 2833 ? 174.897 124.744 104.146 1.00 54.10  ? 4050 SER A O     1 
ATOM   17458 C  CB    . SER A 1 2833 ? 172.017 125.004 102.787 1.00 50.08  ? 4050 SER A CB    1 
ATOM   17459 O  OG    . SER A 1 2833 ? 170.669 124.869 103.201 1.00 52.25  ? 4050 SER A OG    1 
ATOM   17460 N  N     . ASN A 1 2834 ? 174.929 126.499 102.738 1.00 49.60  ? 4051 ASN A N     1 
ATOM   17461 C  CA    . ASN A 1 2834 ? 176.362 126.391 102.497 1.00 51.99  ? 4051 ASN A CA    1 
ATOM   17462 C  C     . ASN A 1 2834 ? 177.170 126.851 103.708 1.00 51.08  ? 4051 ASN A C     1 
ATOM   17463 O  O     . ASN A 1 2834 ? 178.278 126.353 103.932 1.00 52.62  ? 4051 ASN A O     1 
ATOM   17464 C  CB    . ASN A 1 2834 ? 176.718 127.214 101.252 1.00 53.77  ? 4051 ASN A CB    1 
ATOM   17465 C  CG    . ASN A 1 2834 ? 178.134 126.968 100.745 1.00 58.96  ? 4051 ASN A CG    1 
ATOM   17466 O  OD1   . ASN A 1 2834 ? 178.897 126.186 101.306 1.00 58.83  ? 4051 ASN A OD1   1 
ATOM   17467 N  ND2   . ASN A 1 2834 ? 178.487 127.652 99.664  1.00 61.45  ? 4051 ASN A ND2   1 
ATOM   17468 N  N     . THR A 1 2835 ? 176.622 127.758 104.513 1.00 46.96  ? 4052 THR A N     1 
ATOM   17469 C  CA    . THR A 1 2835 ? 177.354 128.351 105.623 1.00 45.91  ? 4052 THR A CA    1 
ATOM   17470 C  C     . THR A 1 2835 ? 177.604 127.336 106.733 1.00 46.61  ? 4052 THR A C     1 
ATOM   17471 O  O     . THR A 1 2835 ? 176.730 126.536 107.075 1.00 47.83  ? 4052 THR A O     1 
ATOM   17472 C  CB    . THR A 1 2835 ? 176.574 129.544 106.183 1.00 50.22  ? 4052 THR A CB    1 
ATOM   17473 O  OG1   . THR A 1 2835 ? 176.164 130.395 105.105 1.00 55.54  ? 4052 THR A OG1   1 
ATOM   17474 C  CG2   . THR A 1 2835 ? 177.427 130.348 107.155 1.00 46.59  ? 4052 THR A CG2   1 
ATOM   17475 N  N     . ILE A 1 2836 ? 178.811 127.378 107.296 1.00 44.92  ? 4053 ILE A N     1 
ATOM   17476 C  CA    . ILE A 1 2836 ? 179.177 126.599 108.472 1.00 42.68  ? 4053 ILE A CA    1 
ATOM   17477 C  C     . ILE A 1 2836 ? 179.601 127.563 109.573 1.00 40.45  ? 4053 ILE A C     1 
ATOM   17478 O  O     . ILE A 1 2836 ? 180.262 128.574 109.309 1.00 40.98  ? 4053 ILE A O     1 
ATOM   17479 C  CB    . ILE A 1 2836 ? 180.285 125.567 108.161 1.00 43.21  ? 4053 ILE A CB    1 
ATOM   17480 C  CG1   . ILE A 1 2836 ? 181.572 126.248 107.688 1.00 42.03  ? 4053 ILE A CG1   1 
ATOM   17481 C  CG2   . ILE A 1 2836 ? 179.806 124.569 107.119 1.00 44.17  ? 4053 ILE A CG2   1 
ATOM   17482 C  CD1   . ILE A 1 2836 ? 182.755 125.314 107.590 1.00 41.31  ? 4053 ILE A CD1   1 
ATOM   17483 N  N     . GLU A 1 2837 ? 179.181 127.273 110.805 1.00 38.99  ? 4054 GLU A N     1 
ATOM   17484 C  CA    . GLU A 1 2837 ? 179.453 128.156 111.931 1.00 38.05  ? 4054 GLU A CA    1 
ATOM   17485 C  C     . GLU A 1 2837 ? 180.704 127.683 112.659 1.00 41.26  ? 4054 GLU A C     1 
ATOM   17486 O  O     . GLU A 1 2837 ? 180.689 126.590 113.244 1.00 47.68  ? 4054 GLU A O     1 
ATOM   17487 C  CB    . GLU A 1 2837 ? 178.268 128.190 112.885 1.00 36.01  ? 4054 GLU A CB    1 
ATOM   17488 C  CG    . GLU A 1 2837 ? 178.184 129.456 113.721 1.00 37.59  ? 4054 GLU A CG    1 
ATOM   17489 C  CD    . GLU A 1 2837 ? 177.151 129.360 114.826 1.00 42.46  ? 4054 GLU A CD    1 
ATOM   17490 O  OE1   . GLU A 1 2837 ? 176.036 128.868 114.556 1.00 45.83  ? 4054 GLU A OE1   1 
ATOM   17491 O  OE2   . GLU A 1 2837 ? 177.451 129.780 115.963 1.00 38.86  ? 4054 GLU A OE2   1 
ATOM   17492 N  N     . PRO A 1 2838 ? 181.791 128.450 112.658 1.00 36.80  ? 4055 PRO A N     1 
ATOM   17493 C  CA    . PRO A 1 2838 ? 182.987 128.039 113.401 1.00 36.34  ? 4055 PRO A CA    1 
ATOM   17494 C  C     . PRO A 1 2838 ? 182.793 128.211 114.900 1.00 36.97  ? 4055 PRO A C     1 
ATOM   17495 O  O     . PRO A 1 2838 ? 181.809 128.781 115.376 1.00 37.37  ? 4055 PRO A O     1 
ATOM   17496 C  CB    . PRO A 1 2838 ? 184.078 128.968 112.863 1.00 33.17  ? 4055 PRO A CB    1 
ATOM   17497 C  CG    . PRO A 1 2838 ? 183.343 130.171 112.394 1.00 34.30  ? 4055 PRO A CG    1 
ATOM   17498 C  CD    . PRO A 1 2838 ? 182.011 129.689 111.893 1.00 33.56  ? 4055 PRO A CD    1 
ATOM   17499 N  N     . ALA A 1 2839 ? 183.765 127.694 115.655 1.00 37.78  ? 4056 ALA A N     1 
ATOM   17500 C  CA    . ALA A 1 2839 ? 183.693 127.754 117.110 1.00 40.21  ? 4056 ALA A CA    1 
ATOM   17501 C  C     . ALA A 1 2839 ? 183.971 129.149 117.654 1.00 41.13  ? 4056 ALA A C     1 
ATOM   17502 O  O     . ALA A 1 2839 ? 183.561 129.453 118.780 1.00 38.02  ? 4056 ALA A O     1 
ATOM   17503 C  CB    . ALA A 1 2839 ? 184.669 126.753 117.728 1.00 42.42  ? 4056 ALA A CB    1 
ATOM   17504 N  N     . ASP A 1 2840 ? 184.652 130.003 116.888 1.00 43.50  ? 4057 ASP A N     1 
ATOM   17505 C  CA    . ASP A 1 2840 ? 184.953 131.368 117.301 1.00 40.20  ? 4057 ASP A CA    1 
ATOM   17506 C  C     . ASP A 1 2840 ? 183.960 132.375 116.730 1.00 36.77  ? 4057 ASP A C     1 
ATOM   17507 O  O     . ASP A 1 2840 ? 184.334 133.512 116.424 1.00 35.40  ? 4057 ASP A O     1 
ATOM   17508 C  CB    . ASP A 1 2840 ? 186.381 131.744 116.905 1.00 40.02  ? 4057 ASP A CB    1 
ATOM   17509 C  CG    . ASP A 1 2840 ? 186.604 131.702 115.405 1.00 41.80  ? 4057 ASP A CG    1 
ATOM   17510 O  OD1   . ASP A 1 2840 ? 185.806 131.056 114.697 1.00 39.56  ? 4057 ASP A OD1   1 
ATOM   17511 O  OD2   . ASP A 1 2840 ? 187.577 132.325 114.934 1.00 46.78  ? 4057 ASP A OD2   1 
ATOM   17512 N  N     . SER A 1 2841 ? 182.697 131.972 116.574 1.00 34.02  ? 4058 SER A N     1 
ATOM   17513 C  CA    . SER A 1 2841 ? 181.693 132.851 115.985 1.00 31.39  ? 4058 SER A CA    1 
ATOM   17514 C  C     . SER A 1 2841 ? 181.342 134.030 116.882 1.00 30.45  ? 4058 SER A C     1 
ATOM   17515 O  O     . SER A 1 2841 ? 180.786 135.016 116.391 1.00 33.74  ? 4058 SER A O     1 
ATOM   17516 C  CB    . SER A 1 2841 ? 180.430 132.057 115.659 1.00 33.59  ? 4058 SER A CB    1 
ATOM   17517 O  OG    . SER A 1 2841 ? 179.600 131.936 116.800 1.00 34.80  ? 4058 SER A OG    1 
ATOM   17518 N  N     . LEU A 1 2842 ? 181.648 133.957 118.177 1.00 27.81  ? 4059 LEU A N     1 
ATOM   17519 C  CA    . LEU A 1 2842 ? 181.351 135.063 119.078 1.00 23.95  ? 4059 LEU A CA    1 
ATOM   17520 C  C     . LEU A 1 2842 ? 182.313 136.233 118.927 1.00 25.29  ? 4059 LEU A C     1 
ATOM   17521 O  O     . LEU A 1 2842 ? 182.050 137.302 119.487 1.00 31.45  ? 4059 LEU A O     1 
ATOM   17522 C  CB    . LEU A 1 2842 ? 181.360 134.581 120.530 1.00 24.38  ? 4059 LEU A CB    1 
ATOM   17523 C  CG    . LEU A 1 2842 ? 180.145 133.767 120.975 1.00 26.18  ? 4059 LEU A CG    1 
ATOM   17524 C  CD1   . LEU A 1 2842 ? 180.342 133.231 122.384 1.00 25.55  ? 4059 LEU A CD1   1 
ATOM   17525 C  CD2   . LEU A 1 2842 ? 178.878 134.601 120.890 1.00 27.49  ? 4059 LEU A CD2   1 
ATOM   17526 N  N     . SER A 1 2843 ? 183.403 136.067 118.200 1.00 25.49  ? 4060 SER A N     1 
ATOM   17527 C  CA    . SER A 1 2843 ? 184.345 137.162 118.000 1.00 27.18  ? 4060 SER A CA    1 
ATOM   17528 C  C     . SER A 1 2843 ? 184.628 137.441 116.533 1.00 28.99  ? 4060 SER A C     1 
ATOM   17529 O  O     . SER A 1 2843 ? 184.771 138.605 116.152 1.00 30.24  ? 4060 SER A O     1 
ATOM   17530 C  CB    . SER A 1 2843 ? 185.663 136.864 118.731 1.00 32.11  ? 4060 SER A CB    1 
ATOM   17531 O  OG    . SER A 1 2843 ? 186.280 135.699 118.213 1.00 39.69  ? 4060 SER A OG    1 
ATOM   17532 N  N     . SER A 1 2844 ? 184.713 136.405 115.698 1.00 30.94  ? 4061 SER A N     1 
ATOM   17533 C  CA    . SER A 1 2844 ? 184.975 136.627 114.281 1.00 33.45  ? 4061 SER A CA    1 
ATOM   17534 C  C     . SER A 1 2844 ? 183.740 137.159 113.566 1.00 30.11  ? 4061 SER A C     1 
ATOM   17535 O  O     . SER A 1 2844 ? 183.840 138.068 112.736 1.00 32.33  ? 4061 SER A O     1 
ATOM   17536 C  CB    . SER A 1 2844 ? 185.455 135.332 113.628 1.00 40.43  ? 4061 SER A CB    1 
ATOM   17537 O  OG    . SER A 1 2844 ? 184.362 134.566 113.157 1.00 42.56  ? 4061 SER A OG    1 
ATOM   17538 N  N     . TRP A 1 2845 ? 182.568 136.605 113.876 1.00 28.27  ? 4062 TRP A N     1 
ATOM   17539 C  CA    . TRP A 1 2845 ? 181.352 136.986 113.168 1.00 28.85  ? 4062 TRP A CA    1 
ATOM   17540 C  C     . TRP A 1 2845 ? 180.755 138.285 113.696 1.00 29.12  ? 4062 TRP A C     1 
ATOM   17541 O  O     . TRP A 1 2845 ? 180.079 138.998 112.947 1.00 29.88  ? 4062 TRP A O     1 
ATOM   17542 C  CB    . TRP A 1 2845 ? 180.325 135.858 113.259 1.00 30.94  ? 4062 TRP A CB    1 
ATOM   17543 C  CG    . TRP A 1 2845 ? 180.506 134.802 112.216 1.00 30.60  ? 4062 TRP A CG    1 
ATOM   17544 C  CD1   . TRP A 1 2845 ? 181.616 134.587 111.457 1.00 32.54  ? 4062 TRP A CD1   1 
ATOM   17545 C  CD2   . TRP A 1 2845 ? 179.547 133.818 111.814 1.00 29.67  ? 4062 TRP A CD2   1 
ATOM   17546 N  NE1   . TRP A 1 2845 ? 181.409 133.530 110.605 1.00 33.48  ? 4062 TRP A NE1   1 
ATOM   17547 C  CE2   . TRP A 1 2845 ? 180.146 133.040 110.806 1.00 31.80  ? 4062 TRP A CE2   1 
ATOM   17548 C  CE3   . TRP A 1 2845 ? 178.241 133.519 112.208 1.00 28.29  ? 4062 TRP A CE3   1 
ATOM   17549 C  CZ2   . TRP A 1 2845 ? 179.484 131.985 110.187 1.00 35.00  ? 4062 TRP A CZ2   1 
ATOM   17550 C  CZ3   . TRP A 1 2845 ? 177.586 132.471 111.593 1.00 30.56  ? 4062 TRP A CZ3   1 
ATOM   17551 C  CH2   . TRP A 1 2845 ? 178.207 131.717 110.594 1.00 33.26  ? 4062 TRP A CH2   1 
ATOM   17552 N  N     . LEU A 1 2846 ? 180.987 138.609 114.967 1.00 28.81  ? 4063 LEU A N     1 
ATOM   17553 C  CA    . LEU A 1 2846 ? 180.481 139.833 115.576 1.00 25.14  ? 4063 LEU A CA    1 
ATOM   17554 C  C     . LEU A 1 2846 ? 181.469 140.990 115.492 1.00 28.72  ? 4063 LEU A C     1 
ATOM   17555 O  O     . LEU A 1 2846 ? 181.214 142.043 116.086 1.00 27.16  ? 4063 LEU A O     1 
ATOM   17556 C  CB    . LEU A 1 2846 ? 180.108 139.581 117.038 1.00 20.93  ? 4063 LEU A CB    1 
ATOM   17557 C  CG    . LEU A 1 2846 ? 179.089 138.476 117.294 1.00 18.36  ? 4063 LEU A CG    1 
ATOM   17558 C  CD1   . LEU A 1 2846 ? 178.690 138.453 118.756 1.00 16.91  ? 4063 LEU A CD1   1 
ATOM   17559 C  CD2   . LEU A 1 2846 ? 177.876 138.687 116.419 1.00 19.24  ? 4063 LEU A CD2   1 
ATOM   17560 N  N     . GLN A 1 2847 ? 182.583 140.810 114.774 1.00 30.86  ? 4064 GLN A N     1 
ATOM   17561 C  CA    . GLN A 1 2847 ? 183.622 141.831 114.601 1.00 29.66  ? 4064 GLN A CA    1 
ATOM   17562 C  C     . GLN A 1 2847 ? 184.176 142.307 115.943 1.00 27.80  ? 4064 GLN A C     1 
ATOM   17563 O  O     . GLN A 1 2847 ? 184.458 143.491 116.136 1.00 27.29  ? 4064 GLN A O     1 
ATOM   17564 C  CB    . GLN A 1 2847 ? 183.113 143.014 113.770 1.00 31.95  ? 4064 GLN A CB    1 
ATOM   17565 C  CG    . GLN A 1 2847 ? 182.303 142.618 112.543 1.00 33.70  ? 4064 GLN A CG    1 
ATOM   17566 C  CD    . GLN A 1 2847 ? 183.140 141.919 111.491 1.00 36.42  ? 4064 GLN A CD    1 
ATOM   17567 O  OE1   . GLN A 1 2847 ? 184.313 142.237 111.302 1.00 39.14  ? 4064 GLN A OE1   1 
ATOM   17568 N  NE2   . GLN A 1 2847 ? 182.538 140.960 110.799 1.00 33.94  ? 4064 GLN A NE2   1 
ATOM   17569 N  N     . LEU A 1 2848 ? 184.337 141.372 116.879 1.00 27.99  ? 4065 LEU A N     1 
ATOM   17570 C  CA    . LEU A 1 2848 ? 184.904 141.644 118.189 1.00 33.64  ? 4065 LEU A CA    1 
ATOM   17571 C  C     . LEU A 1 2848 ? 186.337 141.129 118.271 1.00 38.05  ? 4065 LEU A C     1 
ATOM   17572 O  O     . LEU A 1 2848 ? 186.686 140.142 117.617 1.00 37.63  ? 4065 LEU A O     1 
ATOM   17573 C  CB    . LEU A 1 2848 ? 184.066 140.987 119.291 1.00 28.62  ? 4065 LEU A CB    1 
ATOM   17574 C  CG    . LEU A 1 2848 ? 182.926 141.812 119.888 1.00 22.00  ? 4065 LEU A CG    1 
ATOM   17575 C  CD1   . LEU A 1 2848 ? 181.925 140.913 120.582 1.00 15.24  ? 4065 LEU A CD1   1 
ATOM   17576 C  CD2   . LEU A 1 2848 ? 183.470 142.843 120.857 1.00 27.74  ? 4065 LEU A CD2   1 
ATOM   17577 N  N     . PRO A 1 2849 ? 187.196 141.785 119.048 1.00 40.83  ? 4066 PRO A N     1 
ATOM   17578 C  CA    . PRO A 1 2849 ? 188.545 141.252 119.261 1.00 44.47  ? 4066 PRO A CA    1 
ATOM   17579 C  C     . PRO A 1 2849 ? 188.508 139.962 120.064 1.00 47.70  ? 4066 PRO A C     1 
ATOM   17580 O  O     . PRO A 1 2849 ? 187.625 139.746 120.898 1.00 47.55  ? 4066 PRO A O     1 
ATOM   17581 C  CB    . PRO A 1 2849 ? 189.254 142.369 120.036 1.00 47.86  ? 4066 PRO A CB    1 
ATOM   17582 C  CG    . PRO A 1 2849 ? 188.428 143.594 119.797 1.00 47.63  ? 4066 PRO A CG    1 
ATOM   17583 C  CD    . PRO A 1 2849 ? 187.023 143.106 119.673 1.00 41.18  ? 4066 PRO A CD    1 
ATOM   17584 N  N     . ARG A 1 2850 ? 189.488 139.095 119.795 1.00 50.22  ? 4067 ARG A N     1 
ATOM   17585 C  CA    . ARG A 1 2850 ? 189.576 137.828 120.516 1.00 51.74  ? 4067 ARG A CA    1 
ATOM   17586 C  C     . ARG A 1 2850 ? 189.886 138.041 121.991 1.00 51.71  ? 4067 ARG A C     1 
ATOM   17587 O  O     . ARG A 1 2850 ? 189.405 137.281 122.841 1.00 52.44  ? 4067 ARG A O     1 
ATOM   17588 C  CB    . ARG A 1 2850 ? 190.635 136.930 119.878 1.00 51.35  ? 4067 ARG A CB    1 
ATOM   17589 C  CG    . ARG A 1 2850 ? 190.194 136.265 118.586 1.00 49.44  ? 4067 ARG A CG    1 
ATOM   17590 C  CD    . ARG A 1 2850 ? 191.362 135.565 117.902 1.00 55.14  ? 4067 ARG A CD    1 
ATOM   17591 N  NE    . ARG A 1 2850 ? 190.988 134.281 117.319 1.00 57.30  ? 4067 ARG A NE    1 
ATOM   17592 C  CZ    . ARG A 1 2850 ? 190.710 133.185 118.013 1.00 59.42  ? 4067 ARG A CZ    1 
ATOM   17593 N  NH1   . ARG A 1 2850 ? 190.788 133.160 119.334 1.00 60.40  ? 4067 ARG A NH1   1 
ATOM   17594 N  NH2   . ARG A 1 2850 ? 190.355 132.079 117.364 1.00 57.22  ? 4067 ARG A NH2   1 
ATOM   17595 N  N     . GLU A 1 2851 ? 190.682 139.065 122.310 1.00 51.86  ? 4068 GLU A N     1 
ATOM   17596 C  CA    . GLU A 1 2851 ? 190.989 139.361 123.704 1.00 51.57  ? 4068 GLU A CA    1 
ATOM   17597 C  C     . GLU A 1 2851 ? 189.743 139.769 124.478 1.00 52.68  ? 4068 GLU A C     1 
ATOM   17598 O  O     . GLU A 1 2851 ? 189.652 139.510 125.680 1.00 54.22  ? 4068 GLU A O     1 
ATOM   17599 C  CB    . GLU A 1 2851 ? 192.054 140.455 123.788 1.00 51.78  ? 4068 GLU A CB    1 
ATOM   17600 C  CG    . GLU A 1 2851 ? 191.733 141.711 122.992 1.00 57.51  ? 4068 GLU A CG    1 
ATOM   17601 C  CD    . GLU A 1 2851 ? 192.378 141.717 121.619 1.00 59.99  ? 4068 GLU A CD    1 
ATOM   17602 O  OE1   . GLU A 1 2851 ? 192.414 140.650 120.971 1.00 59.26  ? 4068 GLU A OE1   1 
ATOM   17603 O  OE2   . GLU A 1 2851 ? 192.849 142.791 121.187 1.00 58.31  ? 4068 GLU A OE2   1 
ATOM   17604 N  N     . SER A 1 2852 ? 188.761 140.371 123.803 1.00 52.17  ? 4069 SER A N     1 
ATOM   17605 C  CA    . SER A 1 2852 ? 187.531 140.776 124.477 1.00 52.63  ? 4069 SER A CA    1 
ATOM   17606 C  C     . SER A 1 2852 ? 186.722 139.566 124.936 1.00 51.34  ? 4069 SER A C     1 
ATOM   17607 O  O     . SER A 1 2852 ? 186.285 139.498 126.093 1.00 53.30  ? 4069 SER A O     1 
ATOM   17608 C  CB    . SER A 1 2852 ? 186.700 141.664 123.551 1.00 49.93  ? 4069 SER A CB    1 
ATOM   17609 O  OG    . SER A 1 2852 ? 187.510 142.647 122.930 1.00 49.81  ? 4069 SER A OG    1 
ATOM   17610 N  N     . ILE A 1 2853 ? 186.514 138.594 124.045 1.00 47.72  ? 4070 ILE A N     1 
ATOM   17611 C  CA    . ILE A 1 2853 ? 185.761 137.408 124.439 1.00 49.85  ? 4070 ILE A CA    1 
ATOM   17612 C  C     . ILE A 1 2853 ? 186.583 136.541 125.388 1.00 56.02  ? 4070 ILE A C     1 
ATOM   17613 O  O     . ILE A 1 2853 ? 186.023 135.860 126.260 1.00 57.78  ? 4070 ILE A O     1 
ATOM   17614 C  CB    . ILE A 1 2853 ? 185.279 136.637 123.192 1.00 47.27  ? 4070 ILE A CB    1 
ATOM   17615 C  CG1   . ILE A 1 2853 ? 184.177 135.645 123.571 1.00 48.15  ? 4070 ILE A CG1   1 
ATOM   17616 C  CG2   . ILE A 1 2853 ? 186.427 135.943 122.474 1.00 47.55  ? 4070 ILE A CG2   1 
ATOM   17617 C  CD1   . ILE A 1 2853 ? 183.003 136.281 124.283 1.00 38.05  ? 4070 ILE A CD1   1 
ATOM   17618 N  N     . LEU A 1 2854 ? 187.916 136.575 125.267 1.00 55.25  ? 4071 LEU A N     1 
ATOM   17619 C  CA    . LEU A 1 2854 ? 188.762 135.894 126.243 1.00 53.73  ? 4071 LEU A CA    1 
ATOM   17620 C  C     . LEU A 1 2854 ? 188.594 136.509 127.627 1.00 53.69  ? 4071 LEU A C     1 
ATOM   17621 O  O     . LEU A 1 2854 ? 188.527 135.791 128.631 1.00 57.74  ? 4071 LEU A O     1 
ATOM   17622 C  CB    . LEU A 1 2854 ? 190.223 135.937 125.781 1.00 53.37  ? 4071 LEU A CB    1 
ATOM   17623 C  CG    . LEU A 1 2854 ? 191.394 135.481 126.660 1.00 55.98  ? 4071 LEU A CG    1 
ATOM   17624 C  CD1   . LEU A 1 2854 ? 192.500 134.954 125.768 1.00 60.82  ? 4071 LEU A CD1   1 
ATOM   17625 C  CD2   . LEU A 1 2854 ? 191.950 136.611 127.523 1.00 53.96  ? 4071 LEU A CD2   1 
ATOM   17626 N  N     . ASP A 1 2855 ? 188.512 137.839 127.694 1.00 51.51  ? 4072 ASP A N     1 
ATOM   17627 C  CA    . ASP A 1 2855 ? 188.294 138.523 128.963 1.00 52.33  ? 4072 ASP A CA    1 
ATOM   17628 C  C     . ASP A 1 2855 ? 186.910 138.204 129.518 1.00 53.47  ? 4072 ASP A C     1 
ATOM   17629 O  O     . ASP A 1 2855 ? 186.746 138.056 130.731 1.00 57.18  ? 4072 ASP A O     1 
ATOM   17630 C  CB    . ASP A 1 2855 ? 188.489 140.029 128.760 1.00 52.33  ? 4072 ASP A CB    1 
ATOM   17631 C  CG    . ASP A 1 2855 ? 188.627 140.809 130.066 1.00 58.26  ? 4072 ASP A CG    1 
ATOM   17632 O  OD1   . ASP A 1 2855 ? 189.386 141.799 130.065 1.00 63.45  ? 4072 ASP A OD1   1 
ATOM   17633 O  OD2   . ASP A 1 2855 ? 188.000 140.464 131.087 1.00 58.10  ? 4072 ASP A OD2   1 
ATOM   17634 N  N     . TYR A 1 2856 ? 185.902 138.098 128.648 1.00 53.09  ? 4073 TYR A N     1 
ATOM   17635 C  CA    . TYR A 1 2856 ? 184.567 137.722 129.118 1.00 52.83  ? 4073 TYR A CA    1 
ATOM   17636 C  C     . TYR A 1 2856 ? 184.562 136.316 129.710 1.00 56.11  ? 4073 TYR A C     1 
ATOM   17637 O  O     . TYR A 1 2856 ? 183.941 136.073 130.756 1.00 58.78  ? 4073 TYR A O     1 
ATOM   17638 C  CB    . TYR A 1 2856 ? 183.554 137.816 127.979 1.00 47.87  ? 4073 TYR A CB    1 
ATOM   17639 C  CG    . TYR A 1 2856 ? 182.210 137.203 128.309 1.00 40.58  ? 4073 TYR A CG    1 
ATOM   17640 C  CD1   . TYR A 1 2856 ? 181.363 137.796 129.236 1.00 35.95  ? 4073 TYR A CD1   1 
ATOM   17641 C  CD2   . TYR A 1 2856 ? 181.788 136.033 127.691 1.00 42.55  ? 4073 TYR A CD2   1 
ATOM   17642 C  CE1   . TYR A 1 2856 ? 180.135 137.241 129.539 1.00 34.72  ? 4073 TYR A CE1   1 
ATOM   17643 C  CE2   . TYR A 1 2856 ? 180.560 135.471 127.989 1.00 40.88  ? 4073 TYR A CE2   1 
ATOM   17644 C  CZ    . TYR A 1 2856 ? 179.739 136.080 128.913 1.00 37.27  ? 4073 TYR A CZ    1 
ATOM   17645 O  OH    . TYR A 1 2856 ? 178.517 135.526 129.213 1.00 36.30  ? 4073 TYR A OH    1 
ATOM   17646 N  N     . GLU A 1 2857 ? 185.249 135.379 129.052 1.00 56.77  ? 4074 GLU A N     1 
ATOM   17647 C  CA    . GLU A 1 2857 ? 185.368 134.029 129.595 1.00 59.27  ? 4074 GLU A CA    1 
ATOM   17648 C  C     . GLU A 1 2857 ? 186.133 134.037 130.914 1.00 61.49  ? 4074 GLU A C     1 
ATOM   17649 O  O     . GLU A 1 2857 ? 185.780 133.313 131.856 1.00 61.52  ? 4074 GLU A O     1 
ATOM   17650 C  CB    . GLU A 1 2857 ? 186.050 133.116 128.576 1.00 60.37  ? 4074 GLU A CB    1 
ATOM   17651 C  CG    . GLU A 1 2857 ? 185.164 132.734 127.401 1.00 63.28  ? 4074 GLU A CG    1 
ATOM   17652 C  CD    . GLU A 1 2857 ? 185.740 131.600 126.578 1.00 75.09  ? 4074 GLU A CD    1 
ATOM   17653 O  OE1   . GLU A 1 2857 ? 186.979 131.536 126.432 1.00 77.54  ? 4074 GLU A OE1   1 
ATOM   17654 O  OE2   . GLU A 1 2857 ? 184.952 130.775 126.070 1.00 80.24  ? 4074 GLU A OE2   1 
ATOM   17655 N  N     . ARG A 1 2858 ? 187.177 134.864 130.999 1.00 61.12  ? 4075 ARG A N     1 
ATOM   17656 C  CA    . ARG A 1 2858 ? 187.934 134.992 132.238 1.00 59.77  ? 4075 ARG A CA    1 
ATOM   17657 C  C     . ARG A 1 2858 ? 187.060 135.526 133.363 1.00 55.48  ? 4075 ARG A C     1 
ATOM   17658 O  O     . ARG A 1 2858 ? 187.135 135.040 134.492 1.00 54.36  ? 4075 ARG A O     1 
ATOM   17659 C  CB    . ARG A 1 2858 ? 189.144 135.900 132.020 1.00 61.42  ? 4075 ARG A CB    1 
ATOM   17660 C  CG    . ARG A 1 2858 ? 189.833 136.344 133.301 1.00 60.24  ? 4075 ARG A CG    1 
ATOM   17661 C  CD    . ARG A 1 2858 ? 190.891 137.406 133.033 1.00 56.57  ? 4075 ARG A CD    1 
ATOM   17662 N  NE    . ARG A 1 2858 ? 190.312 138.709 132.722 1.00 55.46  ? 4075 ARG A NE    1 
ATOM   17663 C  CZ    . ARG A 1 2858 ? 189.763 139.523 133.615 1.00 57.24  ? 4075 ARG A CZ    1 
ATOM   17664 N  NH1   . ARG A 1 2858 ? 189.705 139.207 134.898 1.00 56.89  ? 4075 ARG A NH1   1 
ATOM   17665 N  NH2   . ARG A 1 2858 ? 189.266 140.688 133.209 1.00 58.72  ? 4075 ARG A NH2   1 
ATOM   17666 N  N     . LEU A 1 2859 ? 186.212 136.513 133.069 1.00 55.93  ? 4076 LEU A N     1 
ATOM   17667 C  CA    . LEU A 1 2859 ? 185.341 137.080 134.096 1.00 57.07  ? 4076 LEU A CA    1 
ATOM   17668 C  C     . LEU A 1 2859 ? 184.283 136.085 134.555 1.00 59.02  ? 4076 LEU A C     1 
ATOM   17669 O  O     . LEU A 1 2859 ? 183.988 136.005 135.753 1.00 62.69  ? 4076 LEU A O     1 
ATOM   17670 C  CB    . LEU A 1 2859 ? 184.681 138.363 133.591 1.00 55.68  ? 4076 LEU A CB    1 
ATOM   17671 C  CG    . LEU A 1 2859 ? 185.600 139.558 133.340 1.00 57.54  ? 4076 LEU A CG    1 
ATOM   17672 C  CD1   . LEU A 1 2859 ? 184.833 140.709 132.709 1.00 57.93  ? 4076 LEU A CD1   1 
ATOM   17673 C  CD2   . LEU A 1 2859 ? 186.255 139.995 134.638 1.00 56.58  ? 4076 LEU A CD2   1 
ATOM   17674 N  N     . GLN A 1 2860 ? 183.694 135.322 133.628 1.00 57.70  ? 4077 GLN A N     1 
ATOM   17675 C  CA    . GLN A 1 2860 ? 182.684 134.354 134.055 1.00 58.62  ? 4077 GLN A CA    1 
ATOM   17676 C  C     . GLN A 1 2860 ? 183.310 133.228 134.878 1.00 63.46  ? 4077 GLN A C     1 
ATOM   17677 O  O     . GLN A 1 2860 ? 182.773 132.849 135.931 1.00 63.19  ? 4077 GLN A O     1 
ATOM   17678 C  CB    . GLN A 1 2860 ? 181.897 133.820 132.849 1.00 54.38  ? 4077 GLN A CB    1 
ATOM   17679 C  CG    . GLN A 1 2860 ? 182.653 132.954 131.859 1.00 55.40  ? 4077 GLN A CG    1 
ATOM   17680 C  CD    . GLN A 1 2860 ? 181.735 132.119 130.991 1.00 59.88  ? 4077 GLN A CD    1 
ATOM   17681 O  OE1   . GLN A 1 2860 ? 180.623 131.776 131.392 1.00 65.47  ? 4077 GLN A OE1   1 
ATOM   17682 N  NE2   . GLN A 1 2860 ? 182.198 131.785 129.792 1.00 58.27  ? 4077 GLN A NE2   1 
ATOM   17683 N  N     . ALA A 1 2861 ? 184.478 132.725 134.458 1.00 62.89  ? 4078 ALA A N     1 
ATOM   17684 C  CA    . ALA A 1 2861 ? 185.161 131.715 135.258 1.00 57.13  ? 4078 ALA A CA    1 
ATOM   17685 C  C     . ALA A 1 2861 ? 185.643 132.282 136.585 1.00 58.80  ? 4078 ALA A C     1 
ATOM   17686 O  O     . ALA A 1 2861 ? 185.646 131.572 137.593 1.00 62.76  ? 4078 ALA A O     1 
ATOM   17687 C  CB    . ALA A 1 2861 ? 186.333 131.126 134.482 1.00 58.89  ? 4078 ALA A CB    1 
ATOM   17688 N  N     . LYS A 1 2862 ? 186.051 133.553 136.602 1.00 59.77  ? 4079 LYS A N     1 
ATOM   17689 C  CA    . LYS A 1 2862 ? 186.500 134.192 137.831 1.00 61.35  ? 4079 LYS A CA    1 
ATOM   17690 C  C     . LYS A 1 2862 ? 185.364 134.331 138.830 1.00 57.27  ? 4079 LYS A C     1 
ATOM   17691 O  O     . LYS A 1 2862 ? 185.549 134.058 140.020 1.00 61.66  ? 4079 LYS A O     1 
ATOM   17692 C  CB    . LYS A 1 2862 ? 187.105 135.558 137.508 1.00 59.23  ? 4079 LYS A CB    1 
ATOM   17693 C  CG    . LYS A 1 2862 ? 187.200 136.505 138.691 1.00 61.94  ? 4079 LYS A CG    1 
ATOM   17694 C  CD    . LYS A 1 2862 ? 187.796 137.840 138.282 1.00 59.91  ? 4079 LYS A CD    1 
ATOM   17695 C  CE    . LYS A 1 2862 ? 187.650 138.863 139.393 1.00 56.94  ? 4079 LYS A CE    1 
ATOM   17696 N  NZ    . LYS A 1 2862 ? 186.332 138.751 140.074 1.00 52.04  ? 4079 LYS A NZ    1 
ATOM   17697 N  N     . GLU A 1 2863 ? 184.181 134.745 138.371 1.00 52.13  ? 4080 GLU A N     1 
ATOM   17698 C  CA    . GLU A 1 2863 ? 183.056 134.852 139.292 1.00 56.17  ? 4080 GLU A CA    1 
ATOM   17699 C  C     . GLU A 1 2863 ? 182.622 133.474 139.778 1.00 63.34  ? 4080 GLU A C     1 
ATOM   17700 O  O     . GLU A 1 2863 ? 182.287 133.309 140.958 1.00 68.32  ? 4080 GLU A O     1 
ATOM   17701 C  CB    . GLU A 1 2863 ? 181.896 135.625 138.649 1.00 57.90  ? 4080 GLU A CB    1 
ATOM   17702 C  CG    . GLU A 1 2863 ? 180.975 134.841 137.723 1.00 61.34  ? 4080 GLU A CG    1 
ATOM   17703 C  CD    . GLU A 1 2863 ? 179.792 135.659 137.242 1.00 63.29  ? 4080 GLU A CD    1 
ATOM   17704 O  OE1   . GLU A 1 2863 ? 179.516 136.719 137.843 1.00 64.05  ? 4080 GLU A OE1   1 
ATOM   17705 O  OE2   . GLU A 1 2863 ? 179.136 135.242 136.265 1.00 62.41  ? 4080 GLU A OE2   1 
ATOM   17706 N  N     . VAL A 1 2864 ? 182.704 132.458 138.910 1.00 62.07  ? 4081 VAL A N     1 
ATOM   17707 C  CA    . VAL A 1 2864 ? 182.361 131.098 139.323 1.00 59.27  ? 4081 VAL A CA    1 
ATOM   17708 C  C     . VAL A 1 2864 ? 183.337 130.593 140.385 1.00 63.43  ? 4081 VAL A C     1 
ATOM   17709 O  O     . VAL A 1 2864 ? 182.926 130.080 141.435 1.00 63.35  ? 4081 VAL A O     1 
ATOM   17710 C  CB    . VAL A 1 2864 ? 182.315 130.171 138.094 1.00 58.36  ? 4081 VAL A CB    1 
ATOM   17711 C  CG1   . VAL A 1 2864 ? 182.451 128.713 138.496 1.00 58.58  ? 4081 VAL A CG1   1 
ATOM   17712 C  CG2   . VAL A 1 2864 ? 181.021 130.389 137.333 1.00 60.59  ? 4081 VAL A CG2   1 
ATOM   17713 N  N     . ALA A 1 2865 ? 184.640 130.764 140.144 1.00 63.35  ? 4082 ALA A N     1 
ATOM   17714 C  CA    . ALA A 1 2865 ? 185.649 130.273 141.077 1.00 59.03  ? 4082 ALA A CA    1 
ATOM   17715 C  C     . ALA A 1 2865 ? 185.623 131.044 142.393 1.00 61.42  ? 4082 ALA A C     1 
ATOM   17716 O  O     . ALA A 1 2865 ? 185.763 130.449 143.467 1.00 67.08  ? 4082 ALA A O     1 
ATOM   17717 C  CB    . ALA A 1 2865 ? 187.033 130.344 140.435 1.00 59.86  ? 4082 ALA A CB    1 
ATOM   17718 N  N     . SER A 1 2866 ? 185.444 132.367 142.333 1.00 59.87  ? 4083 SER A N     1 
ATOM   17719 C  CA    . SER A 1 2866 ? 185.367 133.164 143.553 1.00 63.09  ? 4083 SER A CA    1 
ATOM   17720 C  C     . SER A 1 2866 ? 184.140 132.799 144.377 1.00 66.60  ? 4083 SER A C     1 
ATOM   17721 O  O     . SER A 1 2866 ? 184.213 132.715 145.609 1.00 72.57  ? 4083 SER A O     1 
ATOM   17722 C  CB    . SER A 1 2866 ? 185.359 134.652 143.206 1.00 61.71  ? 4083 SER A CB    1 
ATOM   17723 O  OG    . SER A 1 2866 ? 185.008 135.436 144.331 1.00 60.85  ? 4083 SER A OG    1 
ATOM   17724 N  N     . SER A 1 2867 ? 183.000 132.575 143.717 1.00 64.77  ? 4084 SER A N     1 
ATOM   17725 C  CA    . SER A 1 2867 ? 181.806 132.166 144.443 1.00 65.32  ? 4084 SER A CA    1 
ATOM   17726 C  C     . SER A 1 2867 ? 181.965 130.775 145.046 1.00 66.86  ? 4084 SER A C     1 
ATOM   17727 O  O     . SER A 1 2867 ? 181.469 130.518 146.149 1.00 69.03  ? 4084 SER A O     1 
ATOM   17728 C  CB    . SER A 1 2867 ? 180.600 132.227 143.516 1.00 67.25  ? 4084 SER A CB    1 
ATOM   17729 O  OG    . SER A 1 2867 ? 180.793 131.341 142.437 1.00 66.19  ? 4084 SER A OG    1 
ATOM   17730 N  N     . THR A 1 2868 ? 182.654 129.863 144.349 1.00 64.19  ? 4085 THR A N     1 
ATOM   17731 C  CA    . THR A 1 2868 ? 182.946 128.567 144.960 1.00 66.55  ? 4085 THR A CA    1 
ATOM   17732 C  C     . THR A 1 2868 ? 183.889 128.708 146.148 1.00 69.88  ? 4085 THR A C     1 
ATOM   17733 O  O     . THR A 1 2868 ? 183.792 127.935 147.105 1.00 69.32  ? 4085 THR A O     1 
ATOM   17734 C  CB    . THR A 1 2868 ? 183.549 127.591 143.948 1.00 65.68  ? 4085 THR A CB    1 
ATOM   17735 O  OG1   . THR A 1 2868 ? 184.685 128.189 143.316 1.00 69.54  ? 4085 THR A OG1   1 
ATOM   17736 C  CG2   . THR A 1 2868 ? 182.530 127.194 142.901 1.00 65.77  ? 4085 THR A CG2   1 
ATOM   17737 N  N     . GLU A 1 2869 ? 184.815 129.669 146.096 1.00 69.11  ? 4086 GLU A N     1 
ATOM   17738 C  CA    . GLU A 1 2869 ? 185.672 129.939 147.247 1.00 65.96  ? 4086 GLU A CA    1 
ATOM   17739 C  C     . GLU A 1 2869 ? 184.856 130.420 148.440 1.00 66.41  ? 4086 GLU A C     1 
ATOM   17740 O  O     . GLU A 1 2869 ? 185.056 129.960 149.570 1.00 69.82  ? 4086 GLU A O     1 
ATOM   17741 C  CB    . GLU A 1 2869 ? 186.738 130.970 146.884 1.00 64.48  ? 4086 GLU A CB    1 
ATOM   17742 C  CG    . GLU A 1 2869 ? 187.962 130.388 146.217 1.00 66.73  ? 4086 GLU A CG    1 
ATOM   17743 C  CD    . GLU A 1 2869 ? 189.057 131.415 146.027 1.00 73.62  ? 4086 GLU A CD    1 
ATOM   17744 O  OE1   . GLU A 1 2869 ? 188.795 132.616 146.247 1.00 77.33  ? 4086 GLU A OE1   1 
ATOM   17745 O  OE2   . GLU A 1 2869 ? 190.184 131.019 145.670 1.00 73.21  ? 4086 GLU A OE2   1 
ATOM   17746 N  N     . GLN A 1 2870 ? 183.934 131.358 148.205 1.00 66.41  ? 4087 GLN A N     1 
ATOM   17747 C  CA    . GLN A 1 2870 ? 183.092 131.855 149.294 1.00 67.24  ? 4087 GLN A CA    1 
ATOM   17748 C  C     . GLN A 1 2870 ? 182.188 130.756 149.844 1.00 66.89  ? 4087 GLN A C     1 
ATOM   17749 O  O     . GLN A 1 2870 ? 181.975 130.672 151.059 1.00 67.69  ? 4087 GLN A O     1 
ATOM   17750 C  CB    . GLN A 1 2870 ? 182.254 133.057 148.843 1.00 73.18  ? 4087 GLN A CB    1 
ATOM   17751 C  CG    . GLN A 1 2870 ? 182.989 134.196 148.121 1.00 74.72  ? 4087 GLN A CG    1 
ATOM   17752 C  CD    . GLN A 1 2870 ? 184.455 134.326 148.505 1.00 72.27  ? 4087 GLN A CD    1 
ATOM   17753 O  OE1   . GLN A 1 2870 ? 184.782 134.727 149.621 1.00 69.98  ? 4087 GLN A OE1   1 
ATOM   17754 N  NE2   . GLN A 1 2870 ? 185.343 133.995 147.575 1.00 71.66  ? 4087 GLN A NE2   1 
ATOM   17755 N  N     . LEU A 1 2871 ? 181.649 129.906 148.970 1.00 70.81  ? 4088 LEU A N     1 
ATOM   17756 C  CA    . LEU A 1 2871 ? 180.828 128.782 149.401 1.00 76.01  ? 4088 LEU A CA    1 
ATOM   17757 C  C     . LEU A 1 2871 ? 181.641 127.653 150.021 1.00 75.27  ? 4088 LEU A C     1 
ATOM   17758 O  O     . LEU A 1 2871 ? 181.060 126.780 150.674 1.00 73.99  ? 4088 LEU A O     1 
ATOM   17759 C  CB    . LEU A 1 2871 ? 180.018 128.233 148.222 1.00 72.19  ? 4088 LEU A CB    1 
ATOM   17760 C  CG    . LEU A 1 2871 ? 178.605 128.775 147.978 1.00 71.76  ? 4088 LEU A CG    1 
ATOM   17761 C  CD1   . LEU A 1 2871 ? 177.679 128.405 149.131 1.00 68.74  ? 4088 LEU A CD1   1 
ATOM   17762 C  CD2   . LEU A 1 2871 ? 178.605 130.278 147.748 1.00 71.61  ? 4088 LEU A CD2   1 
ATOM   17763 N  N     . LEU A 1 2872 ? 182.958 127.645 149.834 1.00 71.77  ? 4089 LEU A N     1 
ATOM   17764 C  CA    . LEU A 1 2872 ? 183.800 126.564 150.325 1.00 69.34  ? 4089 LEU A CA    1 
ATOM   17765 C  C     . LEU A 1 2872 ? 184.477 126.882 151.647 1.00 71.70  ? 4089 LEU A C     1 
ATOM   17766 O  O     . LEU A 1 2872 ? 184.762 125.962 152.420 1.00 71.86  ? 4089 LEU A O     1 
ATOM   17767 C  CB    . LEU A 1 2872 ? 184.868 126.217 149.283 1.00 68.66  ? 4089 LEU A CB    1 
ATOM   17768 C  CG    . LEU A 1 2872 ? 185.460 124.814 149.371 1.00 70.06  ? 4089 LEU A CG    1 
ATOM   17769 C  CD1   . LEU A 1 2872 ? 184.358 123.783 149.269 1.00 73.10  ? 4089 LEU A CD1   1 
ATOM   17770 C  CD2   . LEU A 1 2872 ? 186.484 124.613 148.275 1.00 69.66  ? 4089 LEU A CD2   1 
ATOM   17771 N  N     . GLN A 1 2873 ? 184.737 128.159 151.931 1.00 74.08  ? 4090 GLN A N     1 
ATOM   17772 C  CA    . GLN A 1 2873 ? 185.331 128.544 153.204 1.00 75.46  ? 4090 GLN A CA    1 
ATOM   17773 C  C     . GLN A 1 2873 ? 184.339 128.491 154.358 1.00 75.48  ? 4090 GLN A C     1 
ATOM   17774 O  O     . GLN A 1 2873 ? 184.755 128.607 155.515 1.00 77.48  ? 4090 GLN A O     1 
ATOM   17775 C  CB    . GLN A 1 2873 ? 185.932 129.949 153.103 1.00 70.47  ? 4090 GLN A CB    1 
ATOM   17776 C  CG    . GLN A 1 2873 ? 187.117 130.059 152.149 1.00 71.05  ? 4090 GLN A CG    1 
ATOM   17777 C  CD    . GLN A 1 2873 ? 187.927 128.778 152.058 1.00 70.87  ? 4090 GLN A CD    1 
ATOM   17778 O  OE1   . GLN A 1 2873 ? 187.868 128.063 151.057 1.00 67.52  ? 4090 GLN A OE1   1 
ATOM   17779 N  NE2   . GLN A 1 2873 ? 188.699 128.488 153.099 1.00 70.40  ? 4090 GLN A NE2   1 
ATOM   17780 N  N     . GLU A 1 2874 ? 183.051 128.322 154.075 1.00 74.54  ? 4091 GLU A N     1 
ATOM   17781 C  CA    . GLU A 1 2874 ? 182.043 128.191 155.119 1.00 75.90  ? 4091 GLU A CA    1 
ATOM   17782 C  C     . GLU A 1 2874 ? 182.127 126.819 155.779 1.00 78.99  ? 4091 GLU A C     1 
ATOM   17783 O  O     . GLU A 1 2874 ? 181.481 126.567 156.796 1.00 79.99  ? 4091 GLU A O     1 
ATOM   17784 C  CB    . GLU A 1 2874 ? 180.642 128.417 154.547 1.00 73.48  ? 4091 GLU A CB    1 
ATOM   17785 C  CG    . GLU A 1 2874 ? 180.041 127.195 153.866 1.00 71.65  ? 4091 GLU A CG    1 
ATOM   17786 C  CD    . GLU A 1 2874 ? 178.934 127.553 152.893 1.00 69.57  ? 4091 GLU A CD    1 
ATOM   17787 O  OE1   . GLU A 1 2874 ? 178.424 128.690 152.963 1.00 69.58  ? 4091 GLU A OE1   1 
ATOM   17788 O  OE2   . GLU A 1 2874 ? 178.567 126.694 152.064 1.00 66.13  ? 4091 GLU A OE2   1 
HETATM 17789 P  PG    . ATP B 2 .    ? 161.822 182.437 163.720 1.00 12.50  ? 4101 ATP A PG    1 
HETATM 17790 O  O1G   . ATP B 2 .    ? 162.065 181.428 162.656 1.00 11.95  ? 4101 ATP A O1G   1 
HETATM 17791 O  O2G   . ATP B 2 .    ? 160.355 182.840 163.844 1.00 13.14  ? 4101 ATP A O2G   1 
HETATM 17792 O  O3G   . ATP B 2 .    ? 162.353 182.028 165.092 1.00 13.46  ? 4101 ATP A O3G   1 
HETATM 17793 P  PB    . ATP B 2 .    ? 162.374 185.099 162.533 1.00 7.81   ? 4101 ATP A PB    1 
HETATM 17794 O  O1B   . ATP B 2 .    ? 163.290 185.165 161.381 1.00 14.95  ? 4101 ATP A O1B   1 
HETATM 17795 O  O2B   . ATP B 2 .    ? 160.884 185.179 162.223 1.00 9.79   ? 4101 ATP A O2B   1 
HETATM 17796 O  O3B   . ATP B 2 .    ? 162.578 183.794 163.388 1.00 9.44   ? 4101 ATP A O3B   1 
HETATM 17797 P  PA    . ATP B 2 .    ? 162.224 187.731 163.834 1.00 6.58   ? 4101 ATP A PA    1 
HETATM 17798 O  O1A   . ATP B 2 .    ? 160.754 187.833 163.902 1.00 12.08  ? 4101 ATP A O1A   1 
HETATM 17799 O  O2A   . ATP B 2 .    ? 162.899 188.598 162.780 1.00 10.86  ? 4101 ATP A O2A   1 
HETATM 17800 O  O3A   . ATP B 2 .    ? 162.683 186.244 163.591 1.00 5.35   ? 4101 ATP A O3A   1 
HETATM 17801 O  "O5'" . ATP B 2 .    ? 162.869 188.069 165.232 1.00 9.52   ? 4101 ATP A "O5'" 1 
HETATM 17802 C  "C5'" . ATP B 2 .    ? 164.300 188.085 165.408 1.00 11.87  ? 4101 ATP A "C5'" 1 
HETATM 17803 C  "C4'" . ATP B 2 .    ? 164.673 189.417 165.998 1.00 12.12  ? 4101 ATP A "C4'" 1 
HETATM 17804 O  "O4'" . ATP B 2 .    ? 165.561 190.101 165.099 1.00 11.86  ? 4101 ATP A "O4'" 1 
HETATM 17805 C  "C3'" . ATP B 2 .    ? 163.514 190.387 166.181 1.00 12.15  ? 4101 ATP A "C3'" 1 
HETATM 17806 O  "O3'" . ATP B 2 .    ? 162.863 190.172 167.427 1.00 16.93  ? 4101 ATP A "O3'" 1 
HETATM 17807 C  "C2'" . ATP B 2 .    ? 164.204 191.757 166.140 1.00 12.67  ? 4101 ATP A "C2'" 1 
HETATM 17808 O  "O2'" . ATP B 2 .    ? 164.465 192.249 167.449 1.00 14.13  ? 4101 ATP A "O2'" 1 
HETATM 17809 C  "C1'" . ATP B 2 .    ? 165.520 191.479 165.400 1.00 11.90  ? 4101 ATP A "C1'" 1 
HETATM 17810 N  N9    . ATP B 2 .    ? 165.663 192.219 164.155 1.00 12.46  ? 4101 ATP A N9    1 
HETATM 17811 C  C8    . ATP B 2 .    ? 165.194 191.857 162.920 1.00 12.82  ? 4101 ATP A C8    1 
HETATM 17812 N  N7    . ATP B 2 .    ? 165.468 192.717 161.970 1.00 15.80  ? 4101 ATP A N7    1 
HETATM 17813 C  C5    . ATP B 2 .    ? 166.166 193.719 162.627 1.00 15.47  ? 4101 ATP A C5    1 
HETATM 17814 C  C6    . ATP B 2 .    ? 166.745 194.922 162.184 1.00 16.97  ? 4101 ATP A C6    1 
HETATM 17815 N  N6    . ATP B 2 .    ? 166.711 195.342 160.916 1.00 15.61  ? 4101 ATP A N6    1 
HETATM 17816 N  N1    . ATP B 2 .    ? 167.379 195.688 163.097 1.00 19.90  ? 4101 ATP A N1    1 
HETATM 17817 C  C2    . ATP B 2 .    ? 167.422 195.275 164.365 1.00 18.56  ? 4101 ATP A C2    1 
HETATM 17818 N  N3    . ATP B 2 .    ? 166.913 194.163 164.899 1.00 14.90  ? 4101 ATP A N3    1 
HETATM 17819 C  C4    . ATP B 2 .    ? 166.296 193.423 163.974 1.00 13.97  ? 4101 ATP A C4    1 
HETATM 17820 P  PB    . ADP C 3 .    ? 157.918 165.322 133.358 1.00 25.31  ? 4102 ADP A PB    1 
HETATM 17821 O  O1B   . ADP C 3 .    ? 156.950 165.075 132.228 1.00 19.64  ? 4102 ADP A O1B   1 
HETATM 17822 O  O2B   . ADP C 3 .    ? 157.284 165.843 134.624 1.00 31.82  ? 4102 ADP A O2B   1 
HETATM 17823 O  O3B   . ADP C 3 .    ? 158.918 164.211 133.565 1.00 25.31  ? 4102 ADP A O3B   1 
HETATM 17824 P  PA    . ADP C 3 .    ? 158.247 167.560 131.729 1.00 17.19  ? 4102 ADP A PA    1 
HETATM 17825 O  O1A   . ADP C 3 .    ? 158.340 166.875 130.391 1.00 16.03  ? 4102 ADP A O1A   1 
HETATM 17826 O  O2A   . ADP C 3 .    ? 156.926 168.121 132.189 1.00 19.00  ? 4102 ADP A O2A   1 
HETATM 17827 O  O3A   . ADP C 3 .    ? 158.820 166.545 132.835 1.00 16.42  ? 4102 ADP A O3A   1 
HETATM 17828 O  "O5'" . ADP C 3 .    ? 159.317 168.756 131.726 1.00 20.82  ? 4102 ADP A "O5'" 1 
HETATM 17829 C  "C5'" . ADP C 3 .    ? 159.629 169.374 130.484 1.00 16.09  ? 4102 ADP A "C5'" 1 
HETATM 17830 C  "C4'" . ADP C 3 .    ? 160.179 170.776 130.678 1.00 14.04  ? 4102 ADP A "C4'" 1 
HETATM 17831 O  "O4'" . ADP C 3 .    ? 160.913 171.151 129.515 1.00 11.19  ? 4102 ADP A "O4'" 1 
HETATM 17832 C  "C3'" . ADP C 3 .    ? 159.045 171.771 130.836 1.00 15.68  ? 4102 ADP A "C3'" 1 
HETATM 17833 O  "O3'" . ADP C 3 .    ? 159.104 172.370 132.131 1.00 19.73  ? 4102 ADP A "O3'" 1 
HETATM 17834 C  "C2'" . ADP C 3 .    ? 159.265 172.829 129.778 1.00 13.16  ? 4102 ADP A "C2'" 1 
HETATM 17835 O  "O2'" . ADP C 3 .    ? 159.309 174.108 130.410 1.00 11.48  ? 4102 ADP A "O2'" 1 
HETATM 17836 C  "C1'" . ADP C 3 .    ? 160.604 172.493 129.143 1.00 12.63  ? 4102 ADP A "C1'" 1 
HETATM 17837 N  N9    . ADP C 3 .    ? 160.549 172.662 127.666 1.00 11.35  ? 4102 ADP A N9    1 
HETATM 17838 C  C8    . ADP C 3 .    ? 160.035 173.728 127.026 1.00 11.83  ? 4102 ADP A C8    1 
HETATM 17839 N  N7    . ADP C 3 .    ? 160.145 173.603 125.681 1.00 9.21   ? 4102 ADP A N7    1 
HETATM 17840 C  C5    . ADP C 3 .    ? 160.750 172.431 125.439 1.00 7.84   ? 4102 ADP A C5    1 
HETATM 17841 C  C6    . ADP C 3 .    ? 161.168 171.682 124.235 1.00 10.91  ? 4102 ADP A C6    1 
HETATM 17842 N  N6    . ADP C 3 .    ? 160.956 172.178 122.994 1.00 11.84  ? 4102 ADP A N6    1 
HETATM 17843 N  N1    . ADP C 3 .    ? 161.771 170.490 124.411 1.00 12.04  ? 4102 ADP A N1    1 
HETATM 17844 C  C2    . ADP C 3 .    ? 161.986 169.987 125.638 1.00 13.22  ? 4102 ADP A C2    1 
HETATM 17845 N  N3    . ADP C 3 .    ? 161.632 170.612 126.773 1.00 11.26  ? 4102 ADP A N3    1 
HETATM 17846 C  C4    . ADP C 3 .    ? 161.022 171.817 126.746 1.00 8.55   ? 4102 ADP A C4    1 
HETATM 17847 P  PB    . ADP D 3 .    ? 154.969 136.998 190.350 1.00 59.20  ? 4103 ADP A PB    1 
HETATM 17848 O  O1B   . ADP D 3 .    ? 154.365 138.146 191.118 1.00 67.82  ? 4103 ADP A O1B   1 
HETATM 17849 O  O2B   . ADP D 3 .    ? 154.317 136.723 189.018 1.00 65.11  ? 4103 ADP A O2B   1 
HETATM 17850 O  O3B   . ADP D 3 .    ? 156.476 137.002 190.311 1.00 60.49  ? 4103 ADP A O3B   1 
HETATM 17851 P  PA    . ADP D 3 .    ? 153.126 135.515 191.832 1.00 56.41  ? 4103 ADP A PA    1 
HETATM 17852 O  O1A   . ADP D 3 .    ? 153.141 135.929 193.281 1.00 64.10  ? 4103 ADP A O1A   1 
HETATM 17853 O  O2A   . ADP D 3 .    ? 152.148 136.137 190.867 1.00 62.74  ? 4103 ADP A O2A   1 
HETATM 17854 O  O3A   . ADP D 3 .    ? 154.606 135.706 191.235 1.00 58.34  ? 4103 ADP A O3A   1 
HETATM 17855 O  "O5'" . ADP D 3 .    ? 152.915 133.924 191.775 1.00 65.22  ? 4103 ADP A "O5'" 1 
HETATM 17856 C  "C5'" . ADP D 3 .    ? 151.598 133.391 191.887 1.00 68.69  ? 4103 ADP A "C5'" 1 
HETATM 17857 C  "C4'" . ADP D 3 .    ? 151.620 131.877 191.727 1.00 75.86  ? 4103 ADP A "C4'" 1 
HETATM 17858 O  "O4'" . ADP D 3 .    ? 152.960 131.390 191.611 1.00 77.86  ? 4103 ADP A "O4'" 1 
HETATM 17859 C  "C3'" . ADP D 3 .    ? 150.996 131.205 192.935 1.00 77.37  ? 4103 ADP A "C3'" 1 
HETATM 17860 O  "O3'" . ADP D 3 .    ? 149.719 130.657 192.599 1.00 78.25  ? 4103 ADP A "O3'" 1 
HETATM 17861 C  "C2'" . ADP D 3 .    ? 151.952 130.101 193.328 1.00 80.27  ? 4103 ADP A "C2'" 1 
HETATM 17862 O  "O2'" . ADP D 3 .    ? 151.340 128.827 193.102 1.00 80.94  ? 4103 ADP A "O2'" 1 
HETATM 17863 C  "C1'" . ADP D 3 .    ? 153.180 130.247 192.442 1.00 76.70  ? 4103 ADP A "C1'" 1 
HETATM 17864 N  N9    . ADP D 3 .    ? 154.378 130.521 193.275 1.00 73.13  ? 4103 ADP A N9    1 
HETATM 17865 C  C8    . ADP D 3 .    ? 155.204 131.568 193.097 1.00 67.06  ? 4103 ADP A C8    1 
HETATM 17866 N  N7    . ADP D 3 .    ? 156.210 131.562 194.005 1.00 65.35  ? 4103 ADP A N7    1 
HETATM 17867 C  C5    . ADP D 3 .    ? 156.038 130.485 194.788 1.00 70.04  ? 4103 ADP A C5    1 
HETATM 17868 C  C6    . ADP D 3 .    ? 156.748 129.889 195.942 1.00 74.36  ? 4103 ADP A C6    1 
HETATM 17869 N  N6    . ADP D 3 .    ? 157.866 130.464 196.443 1.00 73.22  ? 4103 ADP A N6    1 
HETATM 17870 N  N1    . ADP D 3 .    ? 156.247 128.757 196.478 1.00 77.72  ? 4103 ADP A N1    1 
HETATM 17871 C  C2    . ADP D 3 .    ? 155.138 128.179 195.985 1.00 80.88  ? 4103 ADP A C2    1 
HETATM 17872 N  N3    . ADP D 3 .    ? 154.443 128.665 194.942 1.00 80.97  ? 4103 ADP A N3    1 
HETATM 17873 C  C4    . ADP D 3 .    ? 154.833 129.795 194.304 1.00 76.32  ? 4103 ADP A C4    1 
HETATM 17874 P  PB    . ADP E 3 .    ? 161.563 167.646 189.986 1.00 23.94  ? 4104 ADP A PB    1 
HETATM 17875 O  O1B   . ADP E 3 .    ? 162.278 168.964 189.838 1.00 25.21  ? 4104 ADP A O1B   1 
HETATM 17876 O  O2B   . ADP E 3 .    ? 160.058 167.740 189.981 1.00 20.68  ? 4104 ADP A O2B   1 
HETATM 17877 O  O3B   . ADP E 3 .    ? 162.118 166.541 189.122 1.00 27.17  ? 4104 ADP A O3B   1 
HETATM 17878 P  PA    . ADP E 3 .    ? 161.435 168.017 192.770 1.00 21.72  ? 4104 ADP A PA    1 
HETATM 17879 O  O1A   . ADP E 3 .    ? 161.934 169.430 192.634 1.00 19.18  ? 4104 ADP A O1A   1 
HETATM 17880 O  O2A   . ADP E 3 .    ? 159.965 167.781 193.015 1.00 19.17  ? 4104 ADP A O2A   1 
HETATM 17881 O  O3A   . ADP E 3 .    ? 161.920 167.180 191.483 1.00 26.88  ? 4104 ADP A O3A   1 
HETATM 17882 O  "O5'" . ADP E 3 .    ? 162.267 167.320 193.957 1.00 25.29  ? 4104 ADP A "O5'" 1 
HETATM 17883 C  "C5'" . ADP E 3 .    ? 163.125 168.102 194.780 1.00 22.74  ? 4104 ADP A "C5'" 1 
HETATM 17884 C  "C4'" . ADP E 3 .    ? 163.294 167.445 196.141 1.00 22.88  ? 4104 ADP A "C4'" 1 
HETATM 17885 O  "O4'" . ADP E 3 .    ? 164.418 168.022 196.808 1.00 21.88  ? 4104 ADP A "O4'" 1 
HETATM 17886 C  "C3'" . ADP E 3 .    ? 162.069 167.700 196.996 1.00 26.93  ? 4104 ADP A "C3'" 1 
HETATM 17887 O  "O3'" . ADP E 3 .    ? 161.579 166.478 197.548 1.00 26.13  ? 4104 ADP A "O3'" 1 
HETATM 17888 C  "C2'" . ADP E 3 .    ? 162.546 168.593 198.117 1.00 26.07  ? 4104 ADP A "C2'" 1 
HETATM 17889 O  "O2'" . ADP E 3 .    ? 162.043 168.112 199.363 1.00 23.31  ? 4104 ADP A "O2'" 1 
HETATM 17890 C  "C1'" . ADP E 3 .    ? 164.062 168.546 198.088 1.00 24.08  ? 4104 ADP A "C1'" 1 
HETATM 17891 N  N9    . ADP E 3 .    ? 164.626 169.913 198.202 1.00 23.30  ? 4104 ADP A N9    1 
HETATM 17892 C  C8    . ADP E 3 .    ? 165.506 170.449 197.339 1.00 21.69  ? 4104 ADP A C8    1 
HETATM 17893 N  N7    . ADP E 3 .    ? 165.846 171.709 197.700 1.00 22.95  ? 4104 ADP A N7    1 
HETATM 17894 C  C5    . ADP E 3 .    ? 165.175 171.999 198.826 1.00 25.69  ? 4104 ADP A C5    1 
HETATM 17895 C  C6    . ADP E 3 .    ? 165.077 173.165 199.733 1.00 30.83  ? 4104 ADP A C6    1 
HETATM 17896 N  N6    . ADP E 3 .    ? 165.781 174.297 199.497 1.00 31.27  ? 4104 ADP A N6    1 
HETATM 17897 N  N1    . ADP E 3 .    ? 164.262 173.064 200.802 1.00 31.18  ? 4104 ADP A N1    1 
HETATM 17898 C  C2    . ADP E 3 .    ? 163.555 171.947 201.046 1.00 29.60  ? 4104 ADP A C2    1 
HETATM 17899 N  N3    . ADP E 3 .    ? 163.597 170.854 200.267 1.00 25.66  ? 4104 ADP A N3    1 
HETATM 17900 C  C4    . ADP E 3 .    ? 164.375 170.813 199.159 1.00 24.09  ? 4104 ADP A C4    1 
HETATM 17901 MG MG    . MG  F 4 .    ? 158.243 168.152 188.444 1.00 23.76  ? 4105 MG  A MG    1 
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