data_9BM8
# 
_entry.id   9BM8 
# 
_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   9BM8         pdb_00009bm8 10.2210/pdb9bm8/pdb 
WWPDB D_1000283522 ?            ?                   
EMDB  EMD-44691    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-04-23 ? 
2  'EM metadata'     1 0 2025-04-23 ? 
3  'Additional map'  1 0 2025-04-23 1 
4  FSC               1 0 2025-04-23 ? 
5  'Half map'        1 0 2025-04-23 1 
6  'Half map'        1 0 2025-04-23 2 
7  Image             1 0 2025-04-23 ? 
8  Mask              1 0 2025-04-23 1 
9  'Primary map'     1 0 2025-04-23 ? 
10 'Structure model' 1 1 2025-04-30 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 10 'Structure model' 'Data collection'     
2 10 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 10 'Structure model' citation        
2 10 'Structure model' citation_author 
3 10 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 10 'Structure model' '_citation.country'                 
2 10 'Structure model' '_citation.journal_abbrev'          
3 10 'Structure model' '_citation.journal_id_CSD'          
4 10 'Structure model' '_citation.journal_id_ISSN'         
5 10 'Structure model' '_citation.pdbx_database_id_DOI'    
6 10 'Structure model' '_citation.pdbx_database_id_PubMed' 
7 10 'Structure model' '_citation.title'                   
8 10 'Structure model' '_citation.year'                    
9 10 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BM8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'State-7c of motor domain from full-length human dynein-1 in 5 mM ATP' 
_pdbx_database_related.db_id          EMD-44691 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jack.zhang@yale.edu 
_pdbx_contact_author.name_first         Jack 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8617-2855 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chai, P.'  1 0000-0001-9702-978X 
'Zhang, K.' 2 0000-0001-8617-2855 
# 
_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                     'The mechanochemical cycle of reactive full-length human dynein 1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01543-3 
_citation.pdbx_database_id_PubMed   40263469 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chai, P.'       1 0000-0001-9702-978X 
primary 'Yang, J.'       2 ?                   
primary 'Geohring, I.C.' 3 ?                   
primary 'Markus, S.M.'   4 0000-0002-3098-0236 
primary 'Wang, Y.'       5 0000-0002-8020-3937 
primary 'Zhang, K.'      6 0000-0001-8617-2855 
# 
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 'Cytoplasmic dynein 1 heavy chain 1' 533083.250 1 ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    2 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_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       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_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'-DIPHOSPHATE"  ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU 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                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 1327 GLN GLN A . n 
A 1 1328 ASP 1328 1328 1328 ASP ASP A . n 
A 1 1329 LEU 1329 1329 1329 LEU LEU A . n 
A 1 1330 LYS 1330 1330 1330 LYS LYS A . n 
A 1 1331 GLY 1331 1331 1331 GLY GLY A . n 
A 1 1332 VAL 1332 1332 1332 VAL VAL A . n 
A 1 1333 TRP 1333 1333 1333 TRP TRP A . n 
A 1 1334 SER 1334 1334 1334 SER SER A . n 
A 1 1335 GLU 1335 1335 1335 GLU GLU A . n 
A 1 1336 LEU 1336 1336 1336 LEU LEU A . n 
A 1 1337 SER 1337 1337 1337 SER SER A . n 
A 1 1338 LYS 1338 1338 1338 LYS LYS A . n 
A 1 1339 VAL 1339 1339 1339 VAL VAL A . n 
A 1 1340 TRP 1340 1340 1340 TRP TRP A . n 
A 1 1341 GLU 1341 1341 1341 GLU GLU A . n 
A 1 1342 GLN 1342 1342 1342 GLN GLN A . n 
A 1 1343 ILE 1343 1343 1343 ILE ILE A . n 
A 1 1344 ASP 1344 1344 1344 ASP ASP A . n 
A 1 1345 GLN 1345 1345 1345 GLN GLN A . n 
A 1 1346 MET 1346 1346 1346 MET MET A . n 
A 1 1347 LYS 1347 1347 1347 LYS LYS A . n 
A 1 1348 GLU 1348 1348 1348 GLU GLU A . n 
A 1 1349 GLN 1349 1349 1349 GLN GLN A . n 
A 1 1350 PRO 1350 1350 1350 PRO PRO A . n 
A 1 1351 TRP 1351 1351 1351 TRP TRP A . n 
A 1 1352 VAL 1352 1352 1352 VAL VAL A . n 
A 1 1353 SER 1353 1353 1353 SER SER A . n 
A 1 1354 VAL 1354 1354 1354 VAL VAL A . n 
A 1 1355 GLN 1355 1355 1355 GLN GLN A . n 
A 1 1356 PRO 1356 1356 1356 PRO PRO A . n 
A 1 1357 ARG 1357 1357 1357 ARG ARG A . n 
A 1 1358 LYS 1358 1358 1358 LYS LYS A . n 
A 1 1359 LEU 1359 1359 1359 LEU LEU A . n 
A 1 1360 ARG 1360 1360 1360 ARG ARG A . n 
A 1 1361 GLN 1361 1361 1361 GLN GLN A . n 
A 1 1362 ASN 1362 1362 1362 ASN ASN A . n 
A 1 1363 LEU 1363 1363 1363 LEU LEU A . n 
A 1 1364 ASP 1364 1364 1364 ASP ASP A . n 
A 1 1365 ALA 1365 1365 1365 ALA ALA A . n 
A 1 1366 LEU 1366 1366 1366 LEU LEU A . n 
A 1 1367 LEU 1367 1367 1367 LEU LEU A . n 
A 1 1368 ASN 1368 1368 1368 ASN ASN A . n 
A 1 1369 GLN 1369 1369 1369 GLN GLN A . n 
A 1 1370 LEU 1370 1370 1370 LEU LEU A . n 
A 1 1371 LYS 1371 1371 1371 LYS LYS A . n 
A 1 1372 SER 1372 1372 1372 SER SER A . n 
A 1 1373 PHE 1373 1373 1373 PHE PHE A . n 
A 1 1374 PRO 1374 1374 1374 PRO PRO A . n 
A 1 1375 ALA 1375 1375 1375 ALA ALA A . n 
A 1 1376 ARG 1376 1376 1376 ARG ARG A . n 
A 1 1377 LEU 1377 1377 1377 LEU LEU A . n 
A 1 1378 ARG 1378 1378 1378 ARG ARG A . n 
A 1 1379 GLN 1379 1379 1379 GLN GLN A . n 
A 1 1380 TYR 1380 1380 1380 TYR TYR A . n 
A 1 1381 ALA 1381 1381 1381 ALA ALA A . n 
A 1 1382 SER 1382 1382 1382 SER SER A . n 
A 1 1383 TYR 1383 1383 1383 TYR TYR A . n 
A 1 1384 GLU 1384 1384 1384 GLU GLU A . n 
A 1 1385 PHE 1385 1385 1385 PHE PHE A . n 
A 1 1386 VAL 1386 1386 1386 VAL VAL A . n 
A 1 1387 GLN 1387 1387 1387 GLN GLN A . n 
A 1 1388 ARG 1388 1388 1388 ARG ARG A . n 
A 1 1389 LEU 1389 1389 1389 LEU LEU A . n 
A 1 1390 LEU 1390 1390 1390 LEU LEU A . n 
A 1 1391 LYS 1391 1391 1391 LYS LYS A . n 
A 1 1392 GLY 1392 1392 1392 GLY GLY A . n 
A 1 1393 TYR 1393 1393 1393 TYR TYR A . n 
A 1 1394 MET 1394 1394 1394 MET MET A . n 
A 1 1395 LYS 1395 1395 1395 LYS LYS A . n 
A 1 1396 ILE 1396 1396 1396 ILE ILE A . n 
A 1 1397 ASN 1397 1397 1397 ASN ASN A . n 
A 1 1398 MET 1398 1398 1398 MET MET A . n 
A 1 1399 LEU 1399 1399 1399 LEU LEU A . n 
A 1 1400 VAL 1400 1400 1400 VAL VAL A . n 
A 1 1401 ILE 1401 1401 1401 ILE ILE A . n 
A 1 1402 GLU 1402 1402 1402 GLU GLU A . n 
A 1 1403 LEU 1403 1403 1403 LEU LEU A . n 
A 1 1404 LYS 1404 1404 1404 LYS LYS A . n 
A 1 1405 SER 1405 1405 1405 SER SER A . n 
A 1 1406 GLU 1406 1406 1406 GLU GLU A . n 
A 1 1407 ALA 1407 1407 1407 ALA ALA A . n 
A 1 1408 LEU 1408 1408 1408 LEU LEU A . n 
A 1 1409 LYS 1409 1409 1409 LYS LYS A . n 
A 1 1410 ASP 1410 1410 1410 ASP ASP A . n 
A 1 1411 ARG 1411 1411 1411 ARG ARG A . n 
A 1 1412 HIS 1412 1412 1412 HIS HIS A . n 
A 1 1413 TRP 1413 1413 1413 TRP TRP A . n 
A 1 1414 LYS 1414 1414 1414 LYS LYS A . n 
A 1 1415 GLN 1415 1415 1415 GLN GLN A . n 
A 1 1416 LEU 1416 1416 1416 LEU LEU A . n 
A 1 1417 MET 1417 1417 1417 MET MET A . n 
A 1 1418 LYS 1418 1418 1418 LYS LYS A . n 
A 1 1419 ARG 1419 1419 1419 ARG ARG A . n 
A 1 1420 LEU 1420 1420 1420 LEU LEU A . n 
A 1 1421 HIS 1421 1421 1421 HIS HIS A . n 
A 1 1422 VAL 1422 1422 1422 VAL VAL A . n 
A 1 1423 ASN 1423 1423 1423 ASN ASN A . n 
A 1 1424 TRP 1424 1424 1424 TRP TRP A . n 
A 1 1425 VAL 1425 1425 1425 VAL VAL A . n 
A 1 1426 VAL 1426 1426 1426 VAL VAL A . n 
A 1 1427 SER 1427 1427 1427 SER SER A . n 
A 1 1428 GLU 1428 1428 1428 GLU GLU A . n 
A 1 1429 LEU 1429 1429 1429 LEU LEU A . n 
A 1 1430 THR 1430 1430 1430 THR THR A . n 
A 1 1431 LEU 1431 1431 1431 LEU LEU A . n 
A 1 1432 GLY 1432 1432 1432 GLY GLY A . n 
A 1 1433 GLN 1433 1433 1433 GLN GLN A . n 
A 1 1434 ILE 1434 1434 1434 ILE ILE A . n 
A 1 1435 TRP 1435 1435 1435 TRP TRP A . n 
A 1 1436 ASP 1436 1436 1436 ASP ASP A . n 
A 1 1437 VAL 1437 1437 1437 VAL VAL A . n 
A 1 1438 ASP 1438 1438 1438 ASP ASP A . n 
A 1 1439 LEU 1439 1439 1439 LEU LEU A . n 
A 1 1440 GLN 1440 1440 1440 GLN GLN A . n 
A 1 1441 LYS 1441 1441 1441 LYS LYS A . n 
A 1 1442 ASN 1442 1442 1442 ASN ASN A . n 
A 1 1443 GLU 1443 1443 1443 GLU GLU A . n 
A 1 1444 ALA 1444 1444 1444 ALA ALA A . n 
A 1 1445 ILE 1445 1445 1445 ILE ILE A . n 
A 1 1446 VAL 1446 1446 1446 VAL VAL A . n 
A 1 1447 LYS 1447 1447 1447 LYS LYS A . n 
A 1 1448 ASP 1448 1448 1448 ASP ASP A . n 
A 1 1449 VAL 1449 1449 1449 VAL VAL A . n 
A 1 1450 LEU 1450 1450 1450 LEU LEU A . n 
A 1 1451 LEU 1451 1451 1451 LEU LEU A . n 
A 1 1452 VAL 1452 1452 1452 VAL VAL A . n 
A 1 1453 ALA 1453 1453 1453 ALA ALA A . n 
A 1 1454 GLN 1454 1454 1454 GLN GLN A . n 
A 1 1455 GLY 1455 1455 1455 GLY GLY A . n 
A 1 1456 GLU 1456 1456 1456 GLU GLU A . n 
A 1 1457 MET 1457 1457 1457 MET MET A . n 
A 1 1458 ALA 1458 1458 1458 ALA ALA A . n 
A 1 1459 LEU 1459 1459 1459 LEU LEU A . n 
A 1 1460 GLU 1460 1460 1460 GLU GLU A . n 
A 1 1461 GLU 1461 1461 1461 GLU GLU A . n 
A 1 1462 PHE 1462 1462 1462 PHE PHE A . n 
A 1 1463 LEU 1463 1463 1463 LEU LEU A . n 
A 1 1464 LYS 1464 1464 1464 LYS LYS A . n 
A 1 1465 GLN 1465 1465 1465 GLN GLN A . n 
A 1 1466 ILE 1466 1466 1466 ILE ILE A . n 
A 1 1467 ARG 1467 1467 1467 ARG ARG A . n 
A 1 1468 GLU 1468 1468 1468 GLU GLU A . n 
A 1 1469 VAL 1469 1469 1469 VAL VAL A . n 
A 1 1470 TRP 1470 1470 1470 TRP TRP A . n 
A 1 1471 ASN 1471 1471 1471 ASN ASN A . n 
A 1 1472 THR 1472 1472 1472 THR THR A . n 
A 1 1473 TYR 1473 1473 1473 TYR TYR A . n 
A 1 1474 GLU 1474 1474 1474 GLU GLU A . n 
A 1 1475 LEU 1475 1475 1475 LEU LEU A . n 
A 1 1476 ASP 1476 1476 1476 ASP ASP A . n 
A 1 1477 LEU 1477 1477 1477 LEU LEU A . n 
A 1 1478 VAL 1478 1478 1478 VAL VAL A . n 
A 1 1479 ASN 1479 1479 1479 ASN ASN A . n 
A 1 1480 TYR 1480 1480 1480 TYR TYR A . n 
A 1 1481 GLN 1481 1481 1481 GLN GLN A . n 
A 1 1482 ASN 1482 1482 1482 ASN ASN A . n 
A 1 1483 LYS 1483 1483 1483 LYS LYS A . n 
A 1 1484 CYS 1484 1484 1484 CYS CYS A . n 
A 1 1485 ARG 1485 1485 1485 ARG ARG A . n 
A 1 1486 LEU 1486 1486 1486 LEU LEU A . n 
A 1 1487 ILE 1487 1487 1487 ILE ILE A . n 
A 1 1488 ARG 1488 1488 1488 ARG ARG A . n 
A 1 1489 GLY 1489 1489 1489 GLY GLY A . n 
A 1 1490 TRP 1490 1490 1490 TRP TRP A . n 
A 1 1491 ASP 1491 1491 1491 ASP ASP A . n 
A 1 1492 ASP 1492 1492 1492 ASP ASP A . n 
A 1 1493 LEU 1493 1493 1493 LEU LEU A . n 
A 1 1494 PHE 1494 1494 1494 PHE PHE A . n 
A 1 1495 ASN 1495 1495 1495 ASN ASN A . n 
A 1 1496 LYS 1496 1496 1496 LYS LYS A . n 
A 1 1497 VAL 1497 1497 1497 VAL VAL A . n 
A 1 1498 LYS 1498 1498 1498 LYS LYS A . n 
A 1 1499 GLU 1499 1499 1499 GLU GLU A . n 
A 1 1500 HIS 1500 1500 1500 HIS HIS A . n 
A 1 1501 ILE 1501 1501 1501 ILE ILE A . n 
A 1 1502 ASN 1502 1502 1502 ASN ASN A . n 
A 1 1503 SER 1503 1503 1503 SER SER A . n 
A 1 1504 VAL 1504 1504 1504 VAL VAL A . n 
A 1 1505 SER 1505 1505 1505 SER SER A . n 
A 1 1506 ALA 1506 1506 1506 ALA ALA A . n 
A 1 1507 MET 1507 1507 1507 MET MET A . n 
A 1 1508 LYS 1508 1508 1508 LYS LYS A . n 
A 1 1509 LEU 1509 1509 1509 LEU LEU A . n 
A 1 1510 SER 1510 1510 1510 SER SER A . n 
A 1 1511 PRO 1511 1511 1511 PRO PRO A . n 
A 1 1512 TYR 1512 1512 1512 TYR TYR A . n 
A 1 1513 TYR 1513 1513 1513 TYR TYR A . n 
A 1 1514 LYS 1514 1514 1514 LYS LYS A . n 
A 1 1515 VAL 1515 1515 1515 VAL VAL A . n 
A 1 1516 PHE 1516 1516 1516 PHE PHE A . n 
A 1 1517 GLU 1517 1517 1517 GLU GLU A . n 
A 1 1518 GLU 1518 1518 1518 GLU GLU A . n 
A 1 1519 ASP 1519 1519 1519 ASP ASP A . n 
A 1 1520 ALA 1520 1520 1520 ALA ALA A . n 
A 1 1521 LEU 1521 1521 1521 LEU LEU A . n 
A 1 1522 SER 1522 1522 1522 SER SER A . n 
A 1 1523 TRP 1523 1523 1523 TRP TRP A . n 
A 1 1524 GLU 1524 1524 1524 GLU GLU A . n 
A 1 1525 ASP 1525 1525 1525 ASP ASP A . n 
A 1 1526 LYS 1526 1526 1526 LYS LYS A . n 
A 1 1527 LEU 1527 1527 1527 LEU LEU A . n 
A 1 1528 ASN 1528 1528 1528 ASN ASN A . n 
A 1 1529 ARG 1529 1529 1529 ARG ARG A . n 
A 1 1530 ILE 1530 1530 1530 ILE ILE A . n 
A 1 1531 MET 1531 1531 1531 MET MET A . n 
A 1 1532 ALA 1532 1532 1532 ALA ALA A . n 
A 1 1533 LEU 1533 1533 1533 LEU LEU A . n 
A 1 1534 PHE 1534 1534 1534 PHE PHE A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 ?    ?   ?   A . n 
A 1 2021 GLY 2021 2021 ?    ?   ?   A . n 
A 1 2022 TYR 2022 2022 ?    ?   ?   A . n 
A 1 2023 ALA 2023 2023 ?    ?   ?   A . n 
A 1 2024 GLY 2024 2024 ?    ?   ?   A . n 
A 1 2025 ARG 2025 2025 ?    ?   ?   A . n 
A 1 2026 SER 2026 2026 ?    ?   ?   A . n 
A 1 2027 ASN 2027 2027 2027 ASN ASN A . n 
A 1 2028 LEU 2028 2028 2028 LEU LEU A . n 
A 1 2029 PRO 2029 2029 2029 PRO PRO A . n 
A 1 2030 ASP 2030 2030 2030 ASP ASP A . n 
A 1 2031 ASN 2031 2031 2031 ASN ASN A . n 
A 1 2032 LEU 2032 2032 2032 LEU LEU A . n 
A 1 2033 LYS 2033 2033 2033 LYS LYS A . n 
A 1 2034 LYS 2034 2034 2034 LYS LYS A . n 
A 1 2035 LEU 2035 2035 2035 LEU LEU A . n 
A 1 2036 PHE 2036 2036 2036 PHE PHE A . n 
A 1 2037 ARG 2037 2037 2037 ARG ARG A . n 
A 1 2038 SER 2038 2038 2038 SER SER A . n 
A 1 2039 LEU 2039 2039 2039 LEU LEU A . n 
A 1 2040 ALA 2040 2040 2040 ALA ALA A . n 
A 1 2041 MET 2041 2041 2041 MET MET A . n 
A 1 2042 THR 2042 2042 2042 THR THR A . n 
A 1 2043 LYS 2043 2043 2043 LYS LYS A . n 
A 1 2044 PRO 2044 2044 2044 PRO PRO A . n 
A 1 2045 ASP 2045 2045 2045 ASP ASP A . n 
A 1 2046 ARG 2046 2046 2046 ARG ARG A . n 
A 1 2047 GLN 2047 2047 2047 GLN GLN A . n 
A 1 2048 LEU 2048 2048 2048 LEU LEU A . n 
A 1 2049 ILE 2049 2049 2049 ILE ILE A . n 
A 1 2050 ALA 2050 2050 2050 ALA ALA A . n 
A 1 2051 GLN 2051 2051 2051 GLN GLN A . n 
A 1 2052 VAL 2052 2052 2052 VAL VAL A . n 
A 1 2053 MET 2053 2053 2053 MET MET A . n 
A 1 2054 LEU 2054 2054 2054 LEU LEU A . n 
A 1 2055 TYR 2055 2055 2055 TYR TYR A . n 
A 1 2056 SER 2056 2056 2056 SER SER A . n 
A 1 2057 GLN 2057 2057 2057 GLN GLN A . n 
A 1 2058 GLY 2058 2058 2058 GLY GLY A . n 
A 1 2059 PHE 2059 2059 2059 PHE PHE A . n 
A 1 2060 ARG 2060 2060 2060 ARG ARG A . n 
A 1 2061 THR 2061 2061 2061 THR THR A . n 
A 1 2062 ALA 2062 2062 2062 ALA ALA A . n 
A 1 2063 GLU 2063 2063 2063 GLU GLU A . n 
A 1 2064 VAL 2064 2064 2064 VAL VAL A . n 
A 1 2065 LEU 2065 2065 2065 LEU LEU A . n 
A 1 2066 ALA 2066 2066 2066 ALA ALA A . n 
A 1 2067 ASN 2067 2067 2067 ASN ASN A . n 
A 1 2068 LYS 2068 2068 2068 LYS LYS A . n 
A 1 2069 ILE 2069 2069 2069 ILE ILE A . n 
A 1 2070 VAL 2070 2070 2070 VAL VAL A . n 
A 1 2071 PRO 2071 2071 2071 PRO PRO A . n 
A 1 2072 PHE 2072 2072 2072 PHE PHE A . n 
A 1 2073 PHE 2073 2073 2073 PHE PHE A . n 
A 1 2074 LYS 2074 2074 2074 LYS LYS A . n 
A 1 2075 LEU 2075 2075 2075 LEU LEU A . n 
A 1 2076 CYS 2076 2076 2076 CYS CYS A . n 
A 1 2077 ASP 2077 2077 2077 ASP ASP A . n 
A 1 2078 GLU 2078 2078 2078 GLU GLU A . n 
A 1 2079 GLN 2079 2079 2079 GLN GLN A . n 
A 1 2080 LEU 2080 2080 2080 LEU LEU A . n 
A 1 2081 SER 2081 2081 2081 SER SER A . n 
A 1 2082 SER 2082 2082 2082 SER SER A . n 
A 1 2083 GLN 2083 2083 2083 GLN GLN A . n 
A 1 2084 SER 2084 2084 2084 SER SER A . n 
A 1 2085 HIS 2085 2085 2085 HIS HIS A . n 
A 1 2086 TYR 2086 2086 2086 TYR TYR A . n 
A 1 2087 ASP 2087 2087 2087 ASP ASP A . n 
A 1 2088 PHE 2088 2088 2088 PHE PHE A . n 
A 1 2089 GLY 2089 2089 2089 GLY GLY A . n 
A 1 2090 LEU 2090 2090 2090 LEU LEU A . n 
A 1 2091 ARG 2091 2091 2091 ARG ARG A . n 
A 1 2092 ALA 2092 2092 2092 ALA ALA A . n 
A 1 2093 LEU 2093 2093 2093 LEU LEU A . n 
A 1 2094 LYS 2094 2094 2094 LYS LYS A . n 
A 1 2095 SER 2095 2095 2095 SER SER A . n 
A 1 2096 VAL 2096 2096 2096 VAL VAL A . n 
A 1 2097 LEU 2097 2097 2097 LEU LEU A . n 
A 1 2098 VAL 2098 2098 2098 VAL VAL A . n 
A 1 2099 SER 2099 2099 2099 SER SER A . n 
A 1 2100 ALA 2100 2100 2100 ALA ALA A . n 
A 1 2101 GLY 2101 2101 2101 GLY GLY A . n 
A 1 2102 ASN 2102 2102 2102 ASN ASN A . n 
A 1 2103 VAL 2103 2103 2103 VAL VAL A . n 
A 1 2104 LYS 2104 2104 2104 LYS LYS A . n 
A 1 2105 ARG 2105 2105 2105 ARG ARG A . n 
A 1 2106 GLU 2106 2106 2106 GLU GLU A . n 
A 1 2107 ARG 2107 2107 2107 ARG ARG A . n 
A 1 2108 ILE 2108 2108 2108 ILE ILE A . n 
A 1 2109 GLN 2109 2109 2109 GLN GLN A . n 
A 1 2110 LYS 2110 2110 2110 LYS LYS A . n 
A 1 2111 ILE 2111 2111 2111 ILE ILE A . n 
A 1 2112 LYS 2112 2112 2112 LYS LYS A . n 
A 1 2113 ARG 2113 2113 2113 ARG ARG A . n 
A 1 2114 GLU 2114 2114 2114 GLU GLU A . n 
A 1 2115 LYS 2115 2115 ?    ?   ?   A . n 
A 1 2116 GLU 2116 2116 ?    ?   ?   A . n 
A 1 2117 GLU 2117 2117 ?    ?   ?   A . n 
A 1 2118 ARG 2118 2118 ?    ?   ?   A . n 
A 1 2119 GLY 2119 2119 ?    ?   ?   A . n 
A 1 2120 GLU 2120 2120 ?    ?   ?   A . n 
A 1 2121 ALA 2121 2121 ?    ?   ?   A . n 
A 1 2122 VAL 2122 2122 ?    ?   ?   A . n 
A 1 2123 ASP 2123 2123 ?    ?   ?   A . n 
A 1 2124 GLU 2124 2124 ?    ?   ?   A . n 
A 1 2125 GLY 2125 2125 ?    ?   ?   A . n 
A 1 2126 GLU 2126 2126 ?    ?   ?   A . n 
A 1 2127 ILE 2127 2127 2127 ILE ILE A . n 
A 1 2128 ALA 2128 2128 2128 ALA ALA A . n 
A 1 2129 GLU 2129 2129 2129 GLU GLU A . n 
A 1 2130 ASN 2130 2130 2130 ASN ASN A . n 
A 1 2131 LEU 2131 2131 2131 LEU LEU A . n 
A 1 2132 PRO 2132 2132 2132 PRO PRO A . n 
A 1 2133 GLU 2133 2133 2133 GLU GLU A . n 
A 1 2134 GLN 2134 2134 2134 GLN GLN A . n 
A 1 2135 GLU 2135 2135 2135 GLU GLU A . n 
A 1 2136 ILE 2136 2136 2136 ILE ILE A . n 
A 1 2137 LEU 2137 2137 2137 LEU LEU A . n 
A 1 2138 ILE 2138 2138 2138 ILE ILE A . n 
A 1 2139 GLN 2139 2139 2139 GLN GLN A . n 
A 1 2140 SER 2140 2140 2140 SER SER A . n 
A 1 2141 VAL 2141 2141 2141 VAL VAL A . n 
A 1 2142 CYS 2142 2142 2142 CYS CYS A . n 
A 1 2143 GLU 2143 2143 2143 GLU GLU A . n 
A 1 2144 THR 2144 2144 2144 THR THR A . n 
A 1 2145 MET 2145 2145 2145 MET MET A . n 
A 1 2146 VAL 2146 2146 2146 VAL VAL A . n 
A 1 2147 PRO 2147 2147 2147 PRO PRO A . n 
A 1 2148 LYS 2148 2148 2148 LYS LYS A . n 
A 1 2149 LEU 2149 2149 2149 LEU LEU A . n 
A 1 2150 VAL 2150 2150 2150 VAL VAL A . n 
A 1 2151 ALA 2151 2151 2151 ALA ALA A . n 
A 1 2152 GLU 2152 2152 2152 GLU GLU A . n 
A 1 2153 ASP 2153 2153 2153 ASP ASP A . n 
A 1 2154 ILE 2154 2154 2154 ILE ILE A . n 
A 1 2155 PRO 2155 2155 2155 PRO PRO A . n 
A 1 2156 LEU 2156 2156 2156 LEU LEU A . n 
A 1 2157 LEU 2157 2157 2157 LEU LEU A . n 
A 1 2158 PHE 2158 2158 2158 PHE PHE A . n 
A 1 2159 SER 2159 2159 2159 SER SER A . n 
A 1 2160 LEU 2160 2160 2160 LEU LEU A . n 
A 1 2161 LEU 2161 2161 2161 LEU LEU A . n 
A 1 2162 SER 2162 2162 2162 SER SER A . n 
A 1 2163 ASP 2163 2163 2163 ASP ASP A . n 
A 1 2164 VAL 2164 2164 2164 VAL VAL A . n 
A 1 2165 PHE 2165 2165 2165 PHE PHE A . n 
A 1 2166 PRO 2166 2166 2166 PRO PRO A . n 
A 1 2167 GLY 2167 2167 2167 GLY GLY A . n 
A 1 2168 VAL 2168 2168 2168 VAL VAL A . n 
A 1 2169 GLN 2169 2169 2169 GLN GLN A . n 
A 1 2170 TYR 2170 2170 2170 TYR TYR A . n 
A 1 2171 HIS 2171 2171 2171 HIS HIS A . n 
A 1 2172 ARG 2172 2172 2172 ARG ARG A . n 
A 1 2173 GLY 2173 2173 2173 GLY GLY A . n 
A 1 2174 GLU 2174 2174 2174 GLU GLU A . n 
A 1 2175 MET 2175 2175 2175 MET MET A . n 
A 1 2176 THR 2176 2176 2176 THR THR A . n 
A 1 2177 ALA 2177 2177 2177 ALA ALA A . n 
A 1 2178 LEU 2178 2178 2178 LEU LEU A . n 
A 1 2179 ARG 2179 2179 2179 ARG ARG A . n 
A 1 2180 GLU 2180 2180 2180 GLU GLU A . n 
A 1 2181 GLU 2181 2181 2181 GLU GLU A . n 
A 1 2182 LEU 2182 2182 2182 LEU LEU A . n 
A 1 2183 LYS 2183 2183 2183 LYS LYS A . n 
A 1 2184 LYS 2184 2184 2184 LYS LYS A . n 
A 1 2185 VAL 2185 2185 2185 VAL VAL A . n 
A 1 2186 CYS 2186 2186 2186 CYS CYS A . n 
A 1 2187 GLN 2187 2187 2187 GLN GLN A . n 
A 1 2188 GLU 2188 2188 2188 GLU GLU A . n 
A 1 2189 MET 2189 2189 2189 MET MET A . n 
A 1 2190 TYR 2190 2190 2190 TYR TYR A . n 
A 1 2191 LEU 2191 2191 2191 LEU LEU A . n 
A 1 2192 THR 2192 2192 2192 THR THR A . n 
A 1 2193 TYR 2193 2193 2193 TYR TYR A . n 
A 1 2194 GLY 2194 2194 2194 GLY GLY A . n 
A 1 2195 ASP 2195 2195 2195 ASP ASP A . n 
A 1 2196 GLY 2196 2196 2196 GLY GLY A . n 
A 1 2197 GLU 2197 2197 2197 GLU GLU A . n 
A 1 2198 GLU 2198 2198 2198 GLU GLU A . n 
A 1 2199 VAL 2199 2199 2199 VAL VAL A . n 
A 1 2200 GLY 2200 2200 2200 GLY GLY A . n 
A 1 2201 GLY 2201 2201 2201 GLY GLY A . n 
A 1 2202 MET 2202 2202 2202 MET MET A . n 
A 1 2203 TRP 2203 2203 2203 TRP TRP A . n 
A 1 2204 VAL 2204 2204 2204 VAL VAL A . n 
A 1 2205 GLU 2205 2205 2205 GLU GLU A . n 
A 1 2206 LYS 2206 2206 2206 LYS LYS A . n 
A 1 2207 VAL 2207 2207 2207 VAL VAL A . n 
A 1 2208 LEU 2208 2208 2208 LEU LEU A . n 
A 1 2209 GLN 2209 2209 2209 GLN GLN A . n 
A 1 2210 LEU 2210 2210 2210 LEU LEU A . n 
A 1 2211 TYR 2211 2211 2211 TYR TYR A . n 
A 1 2212 GLN 2212 2212 2212 GLN GLN A . n 
A 1 2213 ILE 2213 2213 2213 ILE ILE A . n 
A 1 2214 THR 2214 2214 2214 THR THR A . n 
A 1 2215 GLN 2215 2215 2215 GLN GLN A . n 
A 1 2216 ILE 2216 2216 2216 ILE ILE A . n 
A 1 2217 ASN 2217 2217 2217 ASN ASN A . n 
A 1 2218 HIS 2218 2218 2218 HIS HIS A . n 
A 1 2219 GLY 2219 2219 2219 GLY GLY A . n 
A 1 2220 LEU 2220 2220 2220 LEU LEU A . n 
A 1 2221 MET 2221 2221 2221 MET MET A . n 
A 1 2222 MET 2222 2222 2222 MET MET A . n 
A 1 2223 VAL 2223 2223 2223 VAL VAL A . n 
A 1 2224 GLY 2224 2224 2224 GLY GLY A . n 
A 1 2225 PRO 2225 2225 2225 PRO PRO A . n 
A 1 2226 SER 2226 2226 2226 SER SER A . n 
A 1 2227 GLY 2227 2227 2227 GLY GLY A . n 
A 1 2228 SER 2228 2228 2228 SER SER A . n 
A 1 2229 GLY 2229 2229 2229 GLY GLY A . n 
A 1 2230 LYS 2230 2230 2230 LYS LYS A . n 
A 1 2231 SER 2231 2231 2231 SER SER A . n 
A 1 2232 MET 2232 2232 2232 MET MET A . n 
A 1 2233 ALA 2233 2233 2233 ALA ALA A . n 
A 1 2234 TRP 2234 2234 2234 TRP TRP A . n 
A 1 2235 ARG 2235 2235 2235 ARG ARG A . n 
A 1 2236 VAL 2236 2236 2236 VAL VAL A . n 
A 1 2237 LEU 2237 2237 2237 LEU LEU A . n 
A 1 2238 LEU 2238 2238 2238 LEU LEU A . n 
A 1 2239 LYS 2239 2239 2239 LYS LYS A . n 
A 1 2240 ALA 2240 2240 2240 ALA ALA A . n 
A 1 2241 LEU 2241 2241 2241 LEU LEU A . n 
A 1 2242 GLU 2242 2242 2242 GLU GLU A . n 
A 1 2243 ARG 2243 2243 2243 ARG ARG A . n 
A 1 2244 LEU 2244 2244 2244 LEU LEU A . n 
A 1 2245 GLU 2245 2245 2245 GLU GLU A . n 
A 1 2246 GLY 2246 2246 2246 GLY GLY A . n 
A 1 2247 VAL 2247 2247 2247 VAL VAL A . n 
A 1 2248 GLU 2248 2248 2248 GLU GLU A . n 
A 1 2249 GLY 2249 2249 2249 GLY GLY A . n 
A 1 2250 VAL 2250 2250 2250 VAL VAL A . n 
A 1 2251 ALA 2251 2251 2251 ALA ALA A . n 
A 1 2252 HIS 2252 2252 2252 HIS HIS A . n 
A 1 2253 ILE 2253 2253 2253 ILE ILE A . n 
A 1 2254 ILE 2254 2254 2254 ILE ILE A . n 
A 1 2255 ASP 2255 2255 2255 ASP ASP A . n 
A 1 2256 PRO 2256 2256 2256 PRO PRO A . n 
A 1 2257 LYS 2257 2257 2257 LYS LYS A . n 
A 1 2258 ALA 2258 2258 2258 ALA ALA A . n 
A 1 2259 ILE 2259 2259 2259 ILE ILE A . n 
A 1 2260 SER 2260 2260 2260 SER SER A . n 
A 1 2261 LYS 2261 2261 2261 LYS LYS A . n 
A 1 2262 ASP 2262 2262 2262 ASP ASP A . n 
A 1 2263 HIS 2263 2263 2263 HIS HIS A . n 
A 1 2264 LEU 2264 2264 2264 LEU LEU A . n 
A 1 2265 TYR 2265 2265 2265 TYR TYR A . n 
A 1 2266 GLY 2266 2266 2266 GLY GLY A . n 
A 1 2267 THR 2267 2267 2267 THR THR A . n 
A 1 2268 LEU 2268 2268 2268 LEU LEU A . n 
A 1 2269 ASP 2269 2269 2269 ASP ASP A . n 
A 1 2270 PRO 2270 2270 2270 PRO PRO A . n 
A 1 2271 ASN 2271 2271 2271 ASN ASN A . n 
A 1 2272 THR 2272 2272 2272 THR THR A . n 
A 1 2273 ARG 2273 2273 2273 ARG ARG A . n 
A 1 2274 GLU 2274 2274 2274 GLU GLU A . n 
A 1 2275 TRP 2275 2275 2275 TRP TRP A . n 
A 1 2276 THR 2276 2276 2276 THR THR A . n 
A 1 2277 ASP 2277 2277 2277 ASP ASP A . n 
A 1 2278 GLY 2278 2278 2278 GLY GLY A . n 
A 1 2279 LEU 2279 2279 2279 LEU LEU A . n 
A 1 2280 PHE 2280 2280 2280 PHE PHE A . n 
A 1 2281 THR 2281 2281 2281 THR THR A . n 
A 1 2282 HIS 2282 2282 2282 HIS HIS A . n 
A 1 2283 VAL 2283 2283 2283 VAL VAL A . n 
A 1 2284 LEU 2284 2284 2284 LEU LEU A . n 
A 1 2285 ARG 2285 2285 2285 ARG ARG A . n 
A 1 2286 LYS 2286 2286 2286 LYS LYS A . n 
A 1 2287 ILE 2287 2287 2287 ILE ILE A . n 
A 1 2288 ILE 2288 2288 2288 ILE ILE A . n 
A 1 2289 ASP 2289 2289 2289 ASP ASP A . n 
A 1 2290 SER 2290 2290 2290 SER SER A . n 
A 1 2291 VAL 2291 2291 2291 VAL VAL A . n 
A 1 2292 ARG 2292 2292 2292 ARG ARG A . n 
A 1 2293 GLY 2293 2293 2293 GLY GLY A . n 
A 1 2294 GLU 2294 2294 2294 GLU GLU A . n 
A 1 2295 LEU 2295 2295 2295 LEU LEU A . n 
A 1 2296 GLN 2296 2296 2296 GLN GLN A . n 
A 1 2297 LYS 2297 2297 2297 LYS LYS A . n 
A 1 2298 ARG 2298 2298 2298 ARG ARG A . n 
A 1 2299 GLN 2299 2299 2299 GLN GLN A . n 
A 1 2300 TRP 2300 2300 2300 TRP TRP A . n 
A 1 2301 ILE 2301 2301 2301 ILE ILE A . n 
A 1 2302 VAL 2302 2302 2302 VAL VAL A . n 
A 1 2303 PHE 2303 2303 2303 PHE PHE A . n 
A 1 2304 ASP 2304 2304 2304 ASP ASP A . n 
A 1 2305 GLY 2305 2305 2305 GLY GLY A . n 
A 1 2306 ASP 2306 2306 2306 ASP ASP A . n 
A 1 2307 VAL 2307 2307 2307 VAL VAL A . n 
A 1 2308 ASP 2308 2308 2308 ASP ASP A . n 
A 1 2309 PRO 2309 2309 2309 PRO PRO A . n 
A 1 2310 GLU 2310 2310 2310 GLU GLU A . n 
A 1 2311 TRP 2311 2311 2311 TRP TRP A . n 
A 1 2312 VAL 2312 2312 2312 VAL VAL A . n 
A 1 2313 GLU 2313 2313 2313 GLU GLU A . n 
A 1 2314 ASN 2314 2314 2314 ASN ASN A . n 
A 1 2315 LEU 2315 2315 2315 LEU LEU A . n 
A 1 2316 ASN 2316 2316 2316 ASN ASN A . n 
A 1 2317 SER 2317 2317 2317 SER SER A . n 
A 1 2318 VAL 2318 2318 2318 VAL VAL A . n 
A 1 2319 LEU 2319 2319 2319 LEU LEU A . n 
A 1 2320 ASP 2320 2320 2320 ASP ASP A . n 
A 1 2321 ASP 2321 2321 2321 ASP ASP A . n 
A 1 2322 ASN 2322 2322 2322 ASN ASN A . n 
A 1 2323 LYS 2323 2323 2323 LYS LYS A . n 
A 1 2324 LEU 2324 2324 2324 LEU LEU A . n 
A 1 2325 LEU 2325 2325 2325 LEU LEU A . n 
A 1 2326 THR 2326 2326 2326 THR THR A . n 
A 1 2327 LEU 2327 2327 2327 LEU LEU A . n 
A 1 2328 PRO 2328 2328 2328 PRO PRO A . n 
A 1 2329 ASN 2329 2329 2329 ASN ASN A . n 
A 1 2330 GLY 2330 2330 2330 GLY GLY A . n 
A 1 2331 GLU 2331 2331 2331 GLU GLU A . n 
A 1 2332 ARG 2332 2332 2332 ARG ARG A . n 
A 1 2333 LEU 2333 2333 2333 LEU LEU A . n 
A 1 2334 SER 2334 2334 2334 SER SER A . n 
A 1 2335 LEU 2335 2335 2335 LEU LEU A . n 
A 1 2336 PRO 2336 2336 2336 PRO PRO A . n 
A 1 2337 PRO 2337 2337 2337 PRO PRO A . n 
A 1 2338 ASN 2338 2338 2338 ASN ASN A . n 
A 1 2339 VAL 2339 2339 2339 VAL VAL A . n 
A 1 2340 ARG 2340 2340 2340 ARG ARG A . n 
A 1 2341 ILE 2341 2341 2341 ILE ILE A . n 
A 1 2342 MET 2342 2342 2342 MET MET A . n 
A 1 2343 PHE 2343 2343 2343 PHE PHE A . n 
A 1 2344 GLU 2344 2344 2344 GLU GLU A . n 
A 1 2345 VAL 2345 2345 2345 VAL VAL A . n 
A 1 2346 GLN 2346 2346 2346 GLN GLN A . n 
A 1 2347 ASP 2347 2347 2347 ASP ASP A . n 
A 1 2348 LEU 2348 2348 2348 LEU LEU A . n 
A 1 2349 LYS 2349 2349 2349 LYS LYS A . n 
A 1 2350 TYR 2350 2350 2350 TYR TYR A . n 
A 1 2351 ALA 2351 2351 2351 ALA ALA A . n 
A 1 2352 THR 2352 2352 2352 THR THR A . n 
A 1 2353 LEU 2353 2353 2353 LEU LEU A . n 
A 1 2354 ALA 2354 2354 2354 ALA ALA A . n 
A 1 2355 THR 2355 2355 2355 THR THR A . n 
A 1 2356 VAL 2356 2356 2356 VAL VAL A . n 
A 1 2357 SER 2357 2357 2357 SER SER A . n 
A 1 2358 ARG 2358 2358 2358 ARG ARG A . n 
A 1 2359 CYS 2359 2359 2359 CYS CYS A . n 
A 1 2360 GLY 2360 2360 2360 GLY GLY A . n 
A 1 2361 MET 2361 2361 2361 MET MET A . n 
A 1 2362 VAL 2362 2362 2362 VAL VAL A . n 
A 1 2363 TRP 2363 2363 2363 TRP TRP A . n 
A 1 2364 PHE 2364 2364 2364 PHE PHE A . n 
A 1 2365 SER 2365 2365 2365 SER SER A . n 
A 1 2366 GLU 2366 2366 2366 GLU GLU A . n 
A 1 2367 ASP 2367 2367 2367 ASP ASP A . n 
A 1 2368 VAL 2368 2368 2368 VAL VAL A . n 
A 1 2369 LEU 2369 2369 2369 LEU LEU A . n 
A 1 2370 SER 2370 2370 2370 SER SER A . n 
A 1 2371 THR 2371 2371 2371 THR THR A . n 
A 1 2372 ASP 2372 2372 2372 ASP ASP A . n 
A 1 2373 MET 2373 2373 2373 MET MET A . n 
A 1 2374 ILE 2374 2374 2374 ILE ILE A . n 
A 1 2375 PHE 2375 2375 2375 PHE PHE A . n 
A 1 2376 ASN 2376 2376 2376 ASN ASN A . n 
A 1 2377 ASN 2377 2377 2377 ASN ASN A . n 
A 1 2378 PHE 2378 2378 2378 PHE PHE A . n 
A 1 2379 LEU 2379 2379 2379 LEU LEU A . n 
A 1 2380 ALA 2380 2380 2380 ALA ALA A . n 
A 1 2381 ARG 2381 2381 2381 ARG ARG A . n 
A 1 2382 LEU 2382 2382 2382 LEU LEU A . n 
A 1 2383 ARG 2383 2383 2383 ARG ARG A . n 
A 1 2384 SER 2384 2384 2384 SER SER A . n 
A 1 2385 ILE 2385 2385 2385 ILE ILE A . n 
A 1 2386 PRO 2386 2386 2386 PRO PRO A . n 
A 1 2387 LEU 2387 2387 2387 LEU LEU A . n 
A 1 2388 ASP 2388 2388 2388 ASP ASP A . n 
A 1 2389 GLU 2389 2389 ?    ?   ?   A . n 
A 1 2390 GLY 2390 2390 ?    ?   ?   A . n 
A 1 2391 GLU 2391 2391 ?    ?   ?   A . n 
A 1 2392 ASP 2392 2392 ?    ?   ?   A . n 
A 1 2393 GLU 2393 2393 ?    ?   ?   A . n 
A 1 2394 ALA 2394 2394 ?    ?   ?   A . n 
A 1 2395 GLN 2395 2395 ?    ?   ?   A . n 
A 1 2396 ARG 2396 2396 ?    ?   ?   A . n 
A 1 2397 ARG 2397 2397 ?    ?   ?   A . n 
A 1 2398 ARG 2398 2398 ?    ?   ?   A . n 
A 1 2399 LYS 2399 2399 ?    ?   ?   A . n 
A 1 2400 GLY 2400 2400 ?    ?   ?   A . n 
A 1 2401 LYS 2401 2401 ?    ?   ?   A . n 
A 1 2402 GLU 2402 2402 ?    ?   ?   A . n 
A 1 2403 ASP 2403 2403 ?    ?   ?   A . n 
A 1 2404 GLU 2404 2404 ?    ?   ?   A . n 
A 1 2405 GLY 2405 2405 ?    ?   ?   A . n 
A 1 2406 GLU 2406 2406 ?    ?   ?   A . n 
A 1 2407 GLU 2407 2407 ?    ?   ?   A . n 
A 1 2408 ALA 2408 2408 ?    ?   ?   A . n 
A 1 2409 ALA 2409 2409 ?    ?   ?   A . n 
A 1 2410 SER 2410 2410 2410 SER SER A . n 
A 1 2411 PRO 2411 2411 2411 PRO PRO A . n 
A 1 2412 MET 2412 2412 2412 MET ALA A . n 
A 1 2413 LEU 2413 2413 2413 LEU LEU A . n 
A 1 2414 GLN 2414 2414 2414 GLN GLN A . n 
A 1 2415 ILE 2415 2415 2415 ILE ILE A . n 
A 1 2416 GLN 2416 2416 2416 GLN GLN A . n 
A 1 2417 ARG 2417 2417 2417 ARG ARG A . n 
A 1 2418 ASP 2418 2418 2418 ASP ASP A . n 
A 1 2419 ALA 2419 2419 2419 ALA ALA A . n 
A 1 2420 ALA 2420 2420 2420 ALA ALA A . n 
A 1 2421 THR 2421 2421 2421 THR THR A . n 
A 1 2422 ILE 2422 2422 2422 ILE ILE A . n 
A 1 2423 MET 2423 2423 2423 MET MET A . n 
A 1 2424 GLN 2424 2424 2424 GLN GLN A . n 
A 1 2425 PRO 2425 2425 2425 PRO PRO A . n 
A 1 2426 TYR 2426 2426 2426 TYR TYR A . n 
A 1 2427 PHE 2427 2427 2427 PHE PHE A . n 
A 1 2428 THR 2428 2428 2428 THR THR A . n 
A 1 2429 SER 2429 2429 2429 SER SER A . n 
A 1 2430 ASN 2430 2430 2430 ASN ASN A . n 
A 1 2431 GLY 2431 2431 2431 GLY GLY A . n 
A 1 2432 LEU 2432 2432 2432 LEU LEU A . n 
A 1 2433 VAL 2433 2433 2433 VAL VAL A . n 
A 1 2434 THR 2434 2434 2434 THR THR A . n 
A 1 2435 LYS 2435 2435 2435 LYS LYS A . n 
A 1 2436 ALA 2436 2436 2436 ALA ALA A . n 
A 1 2437 LEU 2437 2437 2437 LEU LEU A . n 
A 1 2438 GLU 2438 2438 2438 GLU GLU A . n 
A 1 2439 HIS 2439 2439 2439 HIS HIS A . n 
A 1 2440 ALA 2440 2440 2440 ALA ALA A . n 
A 1 2441 PHE 2441 2441 2441 PHE PHE A . n 
A 1 2442 GLN 2442 2442 2442 GLN GLN A . n 
A 1 2443 LEU 2443 2443 2443 LEU LEU A . n 
A 1 2444 GLU 2444 2444 2444 GLU GLU A . n 
A 1 2445 HIS 2445 2445 2445 HIS HIS A . n 
A 1 2446 ILE 2446 2446 2446 ILE ILE A . n 
A 1 2447 MET 2447 2447 2447 MET MET A . n 
A 1 2448 ASP 2448 2448 2448 ASP ASP A . n 
A 1 2449 LEU 2449 2449 2449 LEU LEU A . n 
A 1 2450 THR 2450 2450 2450 THR THR A . n 
A 1 2451 ARG 2451 2451 2451 ARG ARG A . n 
A 1 2452 LEU 2452 2452 2452 LEU LEU A . n 
A 1 2453 ARG 2453 2453 2453 ARG ARG A . n 
A 1 2454 CYS 2454 2454 2454 CYS CYS A . n 
A 1 2455 LEU 2455 2455 2455 LEU LEU A . n 
A 1 2456 GLY 2456 2456 2456 GLY GLY A . n 
A 1 2457 SER 2457 2457 2457 SER SER A . n 
A 1 2458 LEU 2458 2458 2458 LEU LEU A . n 
A 1 2459 PHE 2459 2459 2459 PHE PHE A . n 
A 1 2460 SER 2460 2460 2460 SER SER A . n 
A 1 2461 MET 2461 2461 2461 MET MET A . n 
A 1 2462 LEU 2462 2462 2462 LEU LEU A . n 
A 1 2463 HIS 2463 2463 2463 HIS HIS A . n 
A 1 2464 GLN 2464 2464 2464 GLN GLN A . n 
A 1 2465 ALA 2465 2465 2465 ALA ALA A . n 
A 1 2466 CYS 2466 2466 2466 CYS CYS A . n 
A 1 2467 ARG 2467 2467 2467 ARG ARG A . n 
A 1 2468 ASN 2468 2468 2468 ASN ASN A . n 
A 1 2469 VAL 2469 2469 2469 VAL VAL A . n 
A 1 2470 ALA 2470 2470 2470 ALA ALA A . n 
A 1 2471 GLN 2471 2471 2471 GLN GLN A . n 
A 1 2472 TYR 2472 2472 2472 TYR TYR A . n 
A 1 2473 ASN 2473 2473 2473 ASN ASN A . n 
A 1 2474 ALA 2474 2474 2474 ALA ALA A . n 
A 1 2475 ASN 2475 2475 2475 ASN ASN A . n 
A 1 2476 HIS 2476 2476 2476 HIS HIS A . n 
A 1 2477 PRO 2477 2477 2477 PRO PRO A . n 
A 1 2478 ASP 2478 2478 2478 ASP ASP A . n 
A 1 2479 PHE 2479 2479 2479 PHE PHE A . n 
A 1 2480 PRO 2480 2480 2480 PRO PRO A . n 
A 1 2481 MET 2481 2481 2481 MET MET A . n 
A 1 2482 GLN 2482 2482 2482 GLN GLN A . n 
A 1 2483 ILE 2483 2483 2483 ILE ILE A . n 
A 1 2484 GLU 2484 2484 2484 GLU GLU A . n 
A 1 2485 GLN 2485 2485 2485 GLN GLN A . n 
A 1 2486 LEU 2486 2486 2486 LEU LEU A . n 
A 1 2487 GLU 2487 2487 2487 GLU GLU A . n 
A 1 2488 ARG 2488 2488 2488 ARG ARG A . n 
A 1 2489 TYR 2489 2489 2489 TYR TYR A . n 
A 1 2490 ILE 2490 2490 2490 ILE ILE A . n 
A 1 2491 GLN 2491 2491 2491 GLN GLN A . n 
A 1 2492 ARG 2492 2492 2492 ARG ARG A . n 
A 1 2493 TYR 2493 2493 2493 TYR TYR A . n 
A 1 2494 LEU 2494 2494 2494 LEU LEU A . n 
A 1 2495 VAL 2495 2495 2495 VAL VAL A . n 
A 1 2496 TYR 2496 2496 2496 TYR TYR A . n 
A 1 2497 ALA 2497 2497 2497 ALA ALA A . n 
A 1 2498 ILE 2498 2498 2498 ILE ILE A . n 
A 1 2499 LEU 2499 2499 2499 LEU LEU A . n 
A 1 2500 TRP 2500 2500 2500 TRP TRP A . n 
A 1 2501 SER 2501 2501 2501 SER SER A . n 
A 1 2502 LEU 2502 2502 2502 LEU LEU A . n 
A 1 2503 SER 2503 2503 2503 SER SER A . n 
A 1 2504 GLY 2504 2504 2504 GLY GLY A . n 
A 1 2505 ASP 2505 2505 2505 ASP ASP A . n 
A 1 2506 SER 2506 2506 2506 SER SER A . n 
A 1 2507 ARG 2507 2507 2507 ARG ARG A . n 
A 1 2508 LEU 2508 2508 2508 LEU LEU A . n 
A 1 2509 LYS 2509 2509 2509 LYS LYS A . n 
A 1 2510 MET 2510 2510 2510 MET MET A . n 
A 1 2511 ARG 2511 2511 2511 ARG ARG A . n 
A 1 2512 ALA 2512 2512 2512 ALA ALA A . n 
A 1 2513 GLU 2513 2513 2513 GLU GLU A . n 
A 1 2514 LEU 2514 2514 2514 LEU LEU A . n 
A 1 2515 GLY 2515 2515 2515 GLY GLY A . n 
A 1 2516 GLU 2516 2516 2516 GLU GLU A . n 
A 1 2517 TYR 2517 2517 2517 TYR TYR A . n 
A 1 2518 ILE 2518 2518 2518 ILE ILE A . n 
A 1 2519 ARG 2519 2519 2519 ARG ARG A . n 
A 1 2520 ARG 2520 2520 2520 ARG ARG A . n 
A 1 2521 ILE 2521 2521 2521 ILE ILE A . n 
A 1 2522 THR 2522 2522 2522 THR THR A . n 
A 1 2523 THR 2523 2523 2523 THR THR A . n 
A 1 2524 VAL 2524 2524 2524 VAL VAL A . n 
A 1 2525 PRO 2525 2525 2525 PRO PRO A . n 
A 1 2526 LEU 2526 2526 2526 LEU LEU A . n 
A 1 2527 PRO 2527 2527 2527 PRO PRO A . n 
A 1 2528 THR 2528 2528 2528 THR THR A . n 
A 1 2529 ALA 2529 2529 2529 ALA ALA A . n 
A 1 2530 PRO 2530 2530 2530 PRO PRO A . n 
A 1 2531 ASN 2531 2531 2531 ASN ASN A . n 
A 1 2532 ILE 2532 2532 2532 ILE ILE A . n 
A 1 2533 PRO 2533 2533 2533 PRO PRO A . n 
A 1 2534 ILE 2534 2534 2534 ILE ILE A . n 
A 1 2535 ILE 2535 2535 2535 ILE ILE A . n 
A 1 2536 ASP 2536 2536 2536 ASP ASP A . n 
A 1 2537 TYR 2537 2537 2537 TYR TYR A . n 
A 1 2538 GLU 2538 2538 2538 GLU GLU A . n 
A 1 2539 VAL 2539 2539 2539 VAL VAL A . n 
A 1 2540 SER 2540 2540 2540 SER SER A . n 
A 1 2541 ILE 2541 2541 2541 ILE ILE A . n 
A 1 2542 SER 2542 2542 2542 SER SER A . n 
A 1 2543 GLY 2543 2543 2543 GLY GLY A . n 
A 1 2544 GLU 2544 2544 2544 GLU GLU A . n 
A 1 2545 TRP 2545 2545 2545 TRP TRP A . n 
A 1 2546 SER 2546 2546 2546 SER SER A . n 
A 1 2547 PRO 2547 2547 2547 PRO PRO A . n 
A 1 2548 TRP 2548 2548 2548 TRP TRP A . n 
A 1 2549 GLN 2549 2549 2549 GLN GLN A . n 
A 1 2550 ALA 2550 2550 2550 ALA ALA A . n 
A 1 2551 LYS 2551 2551 2551 LYS LYS A . n 
A 1 2552 VAL 2552 2552 2552 VAL VAL A . n 
A 1 2553 PRO 2553 2553 2553 PRO PRO A . n 
A 1 2554 GLN 2554 2554 2554 GLN GLN A . n 
A 1 2555 ILE 2555 2555 2555 ILE ILE A . n 
A 1 2556 GLU 2556 2556 2556 GLU GLU A . n 
A 1 2557 VAL 2557 2557 2557 VAL VAL A . n 
A 1 2558 GLU 2558 2558 2558 GLU GLU A . n 
A 1 2559 THR 2559 2559 2559 THR THR A . n 
A 1 2560 HIS 2560 2560 2560 HIS HIS A . n 
A 1 2561 LYS 2561 2561 2561 LYS LYS A . n 
A 1 2562 VAL 2562 2562 2562 VAL VAL A . n 
A 1 2563 ALA 2563 2563 2563 ALA ALA A . n 
A 1 2564 ALA 2564 2564 2564 ALA ALA A . n 
A 1 2565 PRO 2565 2565 2565 PRO PRO A . n 
A 1 2566 ASP 2566 2566 2566 ASP ASP A . n 
A 1 2567 VAL 2567 2567 2567 VAL VAL A . n 
A 1 2568 VAL 2568 2568 2568 VAL VAL A . n 
A 1 2569 VAL 2569 2569 2569 VAL VAL A . n 
A 1 2570 PRO 2570 2570 2570 PRO PRO A . n 
A 1 2571 THR 2571 2571 2571 THR THR A . n 
A 1 2572 LEU 2572 2572 2572 LEU LEU A . n 
A 1 2573 ASP 2573 2573 2573 ASP ASP A . n 
A 1 2574 THR 2574 2574 2574 THR THR A . n 
A 1 2575 VAL 2575 2575 2575 VAL VAL A . n 
A 1 2576 ARG 2576 2576 2576 ARG ARG A . n 
A 1 2577 HIS 2577 2577 2577 HIS HIS A . n 
A 1 2578 GLU 2578 2578 2578 GLU GLU A . n 
A 1 2579 ALA 2579 2579 2579 ALA ALA A . n 
A 1 2580 LEU 2580 2580 2580 LEU LEU A . n 
A 1 2581 LEU 2581 2581 2581 LEU LEU A . n 
A 1 2582 TYR 2582 2582 2582 TYR TYR A . n 
A 1 2583 THR 2583 2583 2583 THR THR A . n 
A 1 2584 TRP 2584 2584 2584 TRP TRP A . n 
A 1 2585 LEU 2585 2585 2585 LEU LEU A . n 
A 1 2586 ALA 2586 2586 2586 ALA ALA A . n 
A 1 2587 GLU 2587 2587 2587 GLU GLU A . n 
A 1 2588 HIS 2588 2588 2588 HIS HIS A . n 
A 1 2589 LYS 2589 2589 2589 LYS LYS A . n 
A 1 2590 PRO 2590 2590 2590 PRO PRO A . n 
A 1 2591 LEU 2591 2591 2591 LEU LEU A . n 
A 1 2592 VAL 2592 2592 2592 VAL VAL A . n 
A 1 2593 LEU 2593 2593 2593 LEU LEU A . n 
A 1 2594 CYS 2594 2594 2594 CYS CYS A . n 
A 1 2595 GLY 2595 2595 2595 GLY GLY A . n 
A 1 2596 PRO 2596 2596 2596 PRO PRO A . n 
A 1 2597 PRO 2597 2597 2597 PRO PRO A . n 
A 1 2598 GLY 2598 2598 2598 GLY GLY A . n 
A 1 2599 SER 2599 2599 2599 SER SER A . n 
A 1 2600 GLY 2600 2600 2600 GLY GLY A . n 
A 1 2601 LYS 2601 2601 2601 LYS LYS A . n 
A 1 2602 THR 2602 2602 2602 THR THR A . n 
A 1 2603 MET 2603 2603 2603 MET MET A . n 
A 1 2604 THR 2604 2604 2604 THR THR A . n 
A 1 2605 LEU 2605 2605 2605 LEU LEU A . n 
A 1 2606 PHE 2606 2606 2606 PHE PHE A . n 
A 1 2607 SER 2607 2607 2607 SER SER A . n 
A 1 2608 ALA 2608 2608 2608 ALA ALA A . n 
A 1 2609 LEU 2609 2609 2609 LEU LEU A . n 
A 1 2610 ARG 2610 2610 2610 ARG ARG A . n 
A 1 2611 ALA 2611 2611 2611 ALA ALA A . n 
A 1 2612 LEU 2612 2612 2612 LEU LEU A . n 
A 1 2613 PRO 2613 2613 2613 PRO PRO A . n 
A 1 2614 ASP 2614 2614 2614 ASP ASP A . n 
A 1 2615 MET 2615 2615 2615 MET MET A . n 
A 1 2616 GLU 2616 2616 2616 GLU GLU A . n 
A 1 2617 VAL 2617 2617 2617 VAL VAL A . n 
A 1 2618 VAL 2618 2618 2618 VAL VAL A . n 
A 1 2619 GLY 2619 2619 2619 GLY GLY A . n 
A 1 2620 LEU 2620 2620 2620 LEU LEU A . n 
A 1 2621 ASN 2621 2621 2621 ASN ASN A . n 
A 1 2622 PHE 2622 2622 2622 PHE PHE A . n 
A 1 2623 SER 2623 2623 2623 SER SER A . n 
A 1 2624 SER 2624 2624 2624 SER SER A . n 
A 1 2625 ALA 2625 2625 2625 ALA ALA A . n 
A 1 2626 THR 2626 2626 2626 THR THR A . n 
A 1 2627 THR 2627 2627 2627 THR THR A . n 
A 1 2628 PRO 2628 2628 2628 PRO PRO A . n 
A 1 2629 GLU 2629 2629 2629 GLU GLU A . n 
A 1 2630 LEU 2630 2630 2630 LEU LEU A . n 
A 1 2631 LEU 2631 2631 2631 LEU LEU A . n 
A 1 2632 LEU 2632 2632 2632 LEU LEU A . n 
A 1 2633 LYS 2633 2633 2633 LYS LYS A . n 
A 1 2634 THR 2634 2634 2634 THR THR A . n 
A 1 2635 PHE 2635 2635 2635 PHE PHE A . n 
A 1 2636 ASP 2636 2636 2636 ASP ASP A . n 
A 1 2637 HIS 2637 2637 2637 HIS HIS A . n 
A 1 2638 TYR 2638 2638 2638 TYR TYR A . n 
A 1 2639 CYS 2639 2639 2639 CYS CYS A . n 
A 1 2640 GLU 2640 2640 2640 GLU GLU A . n 
A 1 2641 TYR 2641 2641 2641 TYR TYR A . n 
A 1 2642 ARG 2642 2642 2642 ARG ARG A . n 
A 1 2643 ARG 2643 2643 2643 ARG ARG A . n 
A 1 2644 THR 2644 2644 2644 THR THR A . n 
A 1 2645 PRO 2645 2645 2645 PRO PRO A . n 
A 1 2646 ASN 2646 2646 2646 ASN ASN A . n 
A 1 2647 GLY 2647 2647 2647 GLY GLY A . n 
A 1 2648 VAL 2648 2648 2648 VAL VAL A . n 
A 1 2649 VAL 2649 2649 2649 VAL VAL A . n 
A 1 2650 LEU 2650 2650 2650 LEU LEU A . n 
A 1 2651 ALA 2651 2651 2651 ALA ALA A . n 
A 1 2652 PRO 2652 2652 2652 PRO PRO A . n 
A 1 2653 VAL 2653 2653 2653 VAL VAL A . n 
A 1 2654 GLN 2654 2654 2654 GLN GLN A . n 
A 1 2655 LEU 2655 2655 2655 LEU LEU A . n 
A 1 2656 GLY 2656 2656 2656 GLY GLY A . n 
A 1 2657 LYS 2657 2657 2657 LYS LYS A . n 
A 1 2658 TRP 2658 2658 2658 TRP TRP A . n 
A 1 2659 LEU 2659 2659 2659 LEU LEU A . n 
A 1 2660 VAL 2660 2660 2660 VAL VAL A . n 
A 1 2661 LEU 2661 2661 2661 LEU LEU A . n 
A 1 2662 PHE 2662 2662 2662 PHE PHE A . n 
A 1 2663 CYS 2663 2663 2663 CYS CYS A . n 
A 1 2664 ASP 2664 2664 2664 ASP ASP A . n 
A 1 2665 GLU 2665 2665 2665 GLU GLU A . n 
A 1 2666 ILE 2666 2666 2666 ILE ILE A . n 
A 1 2667 ASN 2667 2667 2667 ASN ASN A . n 
A 1 2668 LEU 2668 2668 2668 LEU LEU A . n 
A 1 2669 PRO 2669 2669 2669 PRO PRO A . n 
A 1 2670 ASP 2670 2670 2670 ASP ASP A . n 
A 1 2671 MET 2671 2671 2671 MET MET A . n 
A 1 2672 ASP 2672 2672 2672 ASP ASP A . n 
A 1 2673 LYS 2673 2673 2673 LYS LYS A . n 
A 1 2674 TYR 2674 2674 2674 TYR TYR A . n 
A 1 2675 GLY 2675 2675 2675 GLY GLY A . n 
A 1 2676 THR 2676 2676 2676 THR THR A . n 
A 1 2677 GLN 2677 2677 2677 GLN GLN A . n 
A 1 2678 ARG 2678 2678 2678 ARG ARG A . n 
A 1 2679 VAL 2679 2679 2679 VAL VAL A . n 
A 1 2680 ILE 2680 2680 2680 ILE ILE A . n 
A 1 2681 SER 2681 2681 2681 SER SER A . n 
A 1 2682 PHE 2682 2682 2682 PHE PHE A . n 
A 1 2683 ILE 2683 2683 2683 ILE ILE A . n 
A 1 2684 ARG 2684 2684 2684 ARG ARG A . n 
A 1 2685 GLN 2685 2685 2685 GLN GLN A . n 
A 1 2686 MET 2686 2686 2686 MET MET A . n 
A 1 2687 VAL 2687 2687 2687 VAL VAL A . n 
A 1 2688 GLU 2688 2688 2688 GLU GLU A . n 
A 1 2689 HIS 2689 2689 2689 HIS HIS A . n 
A 1 2690 GLY 2690 2690 2690 GLY GLY A . n 
A 1 2691 GLY 2691 2691 2691 GLY GLY A . n 
A 1 2692 PHE 2692 2692 2692 PHE PHE A . n 
A 1 2693 TYR 2693 2693 2693 TYR TYR A . n 
A 1 2694 ARG 2694 2694 2694 ARG ARG A . n 
A 1 2695 THR 2695 2695 2695 THR THR A . n 
A 1 2696 SER 2696 2696 2696 SER SER A . n 
A 1 2697 ASP 2697 2697 2697 ASP ASP A . n 
A 1 2698 GLN 2698 2698 2698 GLN GLN A . n 
A 1 2699 THR 2699 2699 2699 THR THR A . n 
A 1 2700 TRP 2700 2700 2700 TRP TRP A . n 
A 1 2701 VAL 2701 2701 2701 VAL VAL A . n 
A 1 2702 LYS 2702 2702 2702 LYS LYS A . n 
A 1 2703 LEU 2703 2703 2703 LEU LEU A . n 
A 1 2704 GLU 2704 2704 2704 GLU GLU A . n 
A 1 2705 ARG 2705 2705 2705 ARG ARG A . n 
A 1 2706 ILE 2706 2706 2706 ILE ILE A . n 
A 1 2707 GLN 2707 2707 2707 GLN GLN A . n 
A 1 2708 PHE 2708 2708 2708 PHE PHE A . n 
A 1 2709 VAL 2709 2709 2709 VAL VAL A . n 
A 1 2710 GLY 2710 2710 2710 GLY GLY A . n 
A 1 2711 ALA 2711 2711 2711 ALA ALA A . n 
A 1 2712 CYS 2712 2712 2712 CYS CYS A . n 
A 1 2713 ASN 2713 2713 2713 ASN ASN A . n 
A 1 2714 PRO 2714 2714 2714 PRO PRO A . n 
A 1 2715 PRO 2715 2715 2715 PRO PRO A . n 
A 1 2716 THR 2716 2716 2716 THR THR A . n 
A 1 2717 ASP 2717 2717 2717 ASP ASP A . n 
A 1 2718 PRO 2718 2718 2718 PRO PRO A . n 
A 1 2719 GLY 2719 2719 2719 GLY GLY A . n 
A 1 2720 ARG 2720 2720 2720 ARG ARG A . n 
A 1 2721 LYS 2721 2721 2721 LYS LYS A . n 
A 1 2722 PRO 2722 2722 2722 PRO PRO A . n 
A 1 2723 LEU 2723 2723 2723 LEU LEU A . n 
A 1 2724 SER 2724 2724 2724 SER SER A . n 
A 1 2725 HIS 2725 2725 2725 HIS HIS A . n 
A 1 2726 ARG 2726 2726 2726 ARG ARG A . n 
A 1 2727 PHE 2727 2727 2727 PHE PHE A . n 
A 1 2728 LEU 2728 2728 2728 LEU LEU A . n 
A 1 2729 ARG 2729 2729 2729 ARG ARG A . n 
A 1 2730 HIS 2730 2730 2730 HIS HIS A . n 
A 1 2731 VAL 2731 2731 2731 VAL VAL A . n 
A 1 2732 PRO 2732 2732 2732 PRO PRO A . n 
A 1 2733 VAL 2733 2733 2733 VAL VAL A . n 
A 1 2734 VAL 2734 2734 2734 VAL VAL A . n 
A 1 2735 TYR 2735 2735 2735 TYR TYR A . n 
A 1 2736 VAL 2736 2736 2736 VAL VAL A . n 
A 1 2737 ASP 2737 2737 2737 ASP ASP A . n 
A 1 2738 TYR 2738 2738 2738 TYR TYR A . n 
A 1 2739 PRO 2739 2739 2739 PRO PRO A . n 
A 1 2740 GLY 2740 2740 2740 GLY GLY A . n 
A 1 2741 PRO 2741 2741 2741 PRO PRO A . n 
A 1 2742 ALA 2742 2742 2742 ALA ALA A . n 
A 1 2743 SER 2743 2743 2743 SER SER A . n 
A 1 2744 LEU 2744 2744 2744 LEU LEU A . n 
A 1 2745 THR 2745 2745 2745 THR THR A . n 
A 1 2746 GLN 2746 2746 2746 GLN GLN A . n 
A 1 2747 ILE 2747 2747 2747 ILE ILE A . n 
A 1 2748 TYR 2748 2748 2748 TYR TYR A . n 
A 1 2749 GLY 2749 2749 2749 GLY GLY A . n 
A 1 2750 THR 2750 2750 2750 THR THR A . n 
A 1 2751 PHE 2751 2751 2751 PHE PHE A . n 
A 1 2752 ASN 2752 2752 2752 ASN ASN A . n 
A 1 2753 ARG 2753 2753 2753 ARG ARG A . n 
A 1 2754 ALA 2754 2754 2754 ALA ALA A . n 
A 1 2755 MET 2755 2755 2755 MET MET A . n 
A 1 2756 LEU 2756 2756 2756 LEU LEU A . n 
A 1 2757 ARG 2757 2757 2757 ARG ARG A . n 
A 1 2758 LEU 2758 2758 2758 LEU LEU A . n 
A 1 2759 ILE 2759 2759 2759 ILE ILE A . n 
A 1 2760 PRO 2760 2760 2760 PRO PRO A . n 
A 1 2761 SER 2761 2761 2761 SER SER A . n 
A 1 2762 LEU 2762 2762 2762 LEU LEU A . n 
A 1 2763 ARG 2763 2763 2763 ARG ARG A . n 
A 1 2764 THR 2764 2764 2764 THR THR A . n 
A 1 2765 TYR 2765 2765 2765 TYR TYR A . n 
A 1 2766 ALA 2766 2766 2766 ALA ALA A . n 
A 1 2767 GLU 2767 2767 2767 GLU GLU A . n 
A 1 2768 PRO 2768 2768 2768 PRO PRO A . n 
A 1 2769 LEU 2769 2769 2769 LEU LEU A . n 
A 1 2770 THR 2770 2770 2770 THR THR A . n 
A 1 2771 ALA 2771 2771 2771 ALA ALA A . n 
A 1 2772 ALA 2772 2772 2772 ALA ALA A . n 
A 1 2773 MET 2773 2773 2773 MET MET A . n 
A 1 2774 VAL 2774 2774 2774 VAL VAL A . n 
A 1 2775 GLU 2775 2775 2775 GLU GLU A . n 
A 1 2776 PHE 2776 2776 2776 PHE PHE A . n 
A 1 2777 TYR 2777 2777 2777 TYR TYR A . n 
A 1 2778 THR 2778 2778 2778 THR THR A . n 
A 1 2779 MET 2779 2779 2779 MET MET A . n 
A 1 2780 SER 2780 2780 2780 SER SER A . n 
A 1 2781 GLN 2781 2781 2781 GLN GLN A . n 
A 1 2782 GLU 2782 2782 2782 GLU GLU A . n 
A 1 2783 ARG 2783 2783 2783 ARG ARG A . n 
A 1 2784 PHE 2784 2784 2784 PHE PHE A . n 
A 1 2785 THR 2785 2785 2785 THR THR A . n 
A 1 2786 GLN 2786 2786 2786 GLN GLN A . n 
A 1 2787 ASP 2787 2787 2787 ASP ASP A . n 
A 1 2788 THR 2788 2788 2788 THR THR A . n 
A 1 2789 GLN 2789 2789 2789 GLN GLN A . n 
A 1 2790 PRO 2790 2790 2790 PRO PRO A . n 
A 1 2791 HIS 2791 2791 2791 HIS HIS A . n 
A 1 2792 TYR 2792 2792 2792 TYR TYR A . n 
A 1 2793 ILE 2793 2793 2793 ILE ILE A . n 
A 1 2794 TYR 2794 2794 2794 TYR TYR A . n 
A 1 2795 SER 2795 2795 2795 SER SER A . n 
A 1 2796 PRO 2796 2796 2796 PRO PRO A . n 
A 1 2797 ARG 2797 2797 2797 ARG ARG A . n 
A 1 2798 GLU 2798 2798 2798 GLU GLU A . n 
A 1 2799 MET 2799 2799 2799 MET MET A . n 
A 1 2800 THR 2800 2800 2800 THR THR A . n 
A 1 2801 ARG 2801 2801 2801 ARG ARG A . n 
A 1 2802 TRP 2802 2802 2802 TRP TRP A . n 
A 1 2803 VAL 2803 2803 2803 VAL VAL A . n 
A 1 2804 ARG 2804 2804 2804 ARG ARG A . n 
A 1 2805 GLY 2805 2805 2805 GLY GLY A . n 
A 1 2806 ILE 2806 2806 2806 ILE ILE A . n 
A 1 2807 PHE 2807 2807 2807 PHE PHE A . n 
A 1 2808 GLU 2808 2808 2808 GLU GLU A . n 
A 1 2809 ALA 2809 2809 2809 ALA ALA A . n 
A 1 2810 LEU 2810 2810 2810 LEU LEU A . n 
A 1 2811 ARG 2811 2811 2811 ARG ARG A . n 
A 1 2812 PRO 2812 2812 2812 PRO PRO A . n 
A 1 2813 LEU 2813 2813 2813 LEU LEU A . n 
A 1 2814 GLU 2814 2814 2814 GLU GLU A . n 
A 1 2815 THR 2815 2815 2815 THR THR A . n 
A 1 2816 LEU 2816 2816 2816 LEU LEU A . n 
A 1 2817 PRO 2817 2817 2817 PRO PRO A . n 
A 1 2818 VAL 2818 2818 2818 VAL VAL A . n 
A 1 2819 GLU 2819 2819 2819 GLU GLU A . n 
A 1 2820 GLY 2820 2820 2820 GLY GLY A . n 
A 1 2821 LEU 2821 2821 2821 LEU LEU A . n 
A 1 2822 ILE 2822 2822 2822 ILE ILE A . n 
A 1 2823 ARG 2823 2823 2823 ARG ARG A . n 
A 1 2824 ILE 2824 2824 2824 ILE ILE A . n 
A 1 2825 TRP 2825 2825 2825 TRP TRP A . n 
A 1 2826 ALA 2826 2826 2826 ALA ALA A . n 
A 1 2827 HIS 2827 2827 2827 HIS HIS A . n 
A 1 2828 GLU 2828 2828 2828 GLU GLU A . n 
A 1 2829 ALA 2829 2829 2829 ALA ALA A . n 
A 1 2830 LEU 2830 2830 2830 LEU LEU A . n 
A 1 2831 ARG 2831 2831 2831 ARG ARG A . n 
A 1 2832 LEU 2832 2832 2832 LEU LEU A . n 
A 1 2833 PHE 2833 2833 2833 PHE PHE A . n 
A 1 2834 GLN 2834 2834 2834 GLN GLN A . n 
A 1 2835 ASP 2835 2835 2835 ASP ASP A . n 
A 1 2836 ARG 2836 2836 2836 ARG ARG A . n 
A 1 2837 LEU 2837 2837 2837 LEU LEU A . n 
A 1 2838 VAL 2838 2838 2838 VAL VAL A . n 
A 1 2839 GLU 2839 2839 2839 GLU GLU A . n 
A 1 2840 ASP 2840 2840 2840 ASP ASP A . n 
A 1 2841 GLU 2841 2841 2841 GLU GLU A . n 
A 1 2842 GLU 2842 2842 2842 GLU GLU A . n 
A 1 2843 ARG 2843 2843 2843 ARG ARG A . n 
A 1 2844 ARG 2844 2844 2844 ARG ARG A . n 
A 1 2845 TRP 2845 2845 2845 TRP TRP A . n 
A 1 2846 THR 2846 2846 2846 THR THR A . n 
A 1 2847 ASP 2847 2847 2847 ASP ASP A . n 
A 1 2848 GLU 2848 2848 2848 GLU GLU A . n 
A 1 2849 ASN 2849 2849 2849 ASN ASN A . n 
A 1 2850 ILE 2850 2850 2850 ILE ILE A . n 
A 1 2851 ASP 2851 2851 2851 ASP ASP A . n 
A 1 2852 THR 2852 2852 2852 THR THR A . n 
A 1 2853 VAL 2853 2853 2853 VAL VAL A . n 
A 1 2854 ALA 2854 2854 2854 ALA ALA A . n 
A 1 2855 LEU 2855 2855 2855 LEU LEU A . n 
A 1 2856 LYS 2856 2856 2856 LYS LYS A . n 
A 1 2857 HIS 2857 2857 2857 HIS HIS A . n 
A 1 2858 PHE 2858 2858 2858 PHE PHE A . n 
A 1 2859 PRO 2859 2859 2859 PRO PRO A . n 
A 1 2860 ASN 2860 2860 2860 ASN ASN A . n 
A 1 2861 ILE 2861 2861 2861 ILE ILE A . n 
A 1 2862 ASP 2862 2862 2862 ASP ASP A . n 
A 1 2863 ARG 2863 2863 2863 ARG ARG A . n 
A 1 2864 GLU 2864 2864 2864 GLU GLU A . n 
A 1 2865 LYS 2865 2865 2865 LYS LYS A . n 
A 1 2866 ALA 2866 2866 2866 ALA ALA A . n 
A 1 2867 MET 2867 2867 2867 MET MET A . n 
A 1 2868 SER 2868 2868 2868 SER SER A . n 
A 1 2869 ARG 2869 2869 2869 ARG ARG A . n 
A 1 2870 PRO 2870 2870 2870 PRO PRO A . n 
A 1 2871 ILE 2871 2871 2871 ILE ILE A . n 
A 1 2872 LEU 2872 2872 2872 LEU LEU A . n 
A 1 2873 TYR 2873 2873 2873 TYR TYR A . n 
A 1 2874 SER 2874 2874 2874 SER SER A . n 
A 1 2875 ASN 2875 2875 2875 ASN ASN A . n 
A 1 2876 TRP 2876 2876 2876 TRP TRP A . n 
A 1 2877 LEU 2877 2877 2877 LEU LEU A . n 
A 1 2878 SER 2878 2878 2878 SER SER A . n 
A 1 2879 LYS 2879 2879 2879 LYS LYS A . n 
A 1 2880 ASP 2880 2880 2880 ASP ASP A . n 
A 1 2881 TYR 2881 2881 2881 TYR TYR A . n 
A 1 2882 ILE 2882 2882 2882 ILE ILE A . n 
A 1 2883 PRO 2883 2883 2883 PRO PRO A . n 
A 1 2884 VAL 2884 2884 2884 VAL VAL A . n 
A 1 2885 ASP 2885 2885 2885 ASP ASP A . n 
A 1 2886 GLN 2886 2886 2886 GLN GLN A . n 
A 1 2887 GLU 2887 2887 2887 GLU GLU A . n 
A 1 2888 GLU 2888 2888 2888 GLU GLU A . n 
A 1 2889 LEU 2889 2889 2889 LEU LEU A . n 
A 1 2890 ARG 2890 2890 2890 ARG ARG A . n 
A 1 2891 ASP 2891 2891 2891 ASP ASP A . n 
A 1 2892 TYR 2892 2892 2892 TYR TYR A . n 
A 1 2893 VAL 2893 2893 2893 VAL VAL A . n 
A 1 2894 LYS 2894 2894 2894 LYS LYS A . n 
A 1 2895 ALA 2895 2895 2895 ALA ALA A . n 
A 1 2896 ARG 2896 2896 2896 ARG ARG A . n 
A 1 2897 LEU 2897 2897 2897 LEU LEU A . n 
A 1 2898 LYS 2898 2898 2898 LYS LYS A . n 
A 1 2899 VAL 2899 2899 2899 VAL VAL A . n 
A 1 2900 PHE 2900 2900 2900 PHE PHE A . n 
A 1 2901 TYR 2901 2901 2901 TYR TYR A . n 
A 1 2902 GLU 2902 2902 2902 GLU GLU A . n 
A 1 2903 GLU 2903 2903 2903 GLU GLU A . n 
A 1 2904 GLU 2904 2904 2904 GLU GLU A . n 
A 1 2905 LEU 2905 2905 2905 LEU LEU A . n 
A 1 2906 ASP 2906 2906 2906 ASP ASP A . n 
A 1 2907 VAL 2907 2907 2907 VAL VAL A . n 
A 1 2908 PRO 2908 2908 2908 PRO PRO A . n 
A 1 2909 LEU 2909 2909 2909 LEU LEU A . n 
A 1 2910 VAL 2910 2910 2910 VAL VAL A . n 
A 1 2911 LEU 2911 2911 2911 LEU LEU A . n 
A 1 2912 PHE 2912 2912 2912 PHE PHE A . n 
A 1 2913 ASN 2913 2913 2913 ASN ASN A . n 
A 1 2914 GLU 2914 2914 2914 GLU GLU A . n 
A 1 2915 VAL 2915 2915 2915 VAL VAL A . n 
A 1 2916 LEU 2916 2916 2916 LEU LEU A . n 
A 1 2917 ASP 2917 2917 2917 ASP ASP A . n 
A 1 2918 HIS 2918 2918 2918 HIS HIS A . n 
A 1 2919 VAL 2919 2919 2919 VAL VAL A . n 
A 1 2920 LEU 2920 2920 2920 LEU LEU A . n 
A 1 2921 ARG 2921 2921 2921 ARG ARG A . n 
A 1 2922 ILE 2922 2922 2922 ILE ILE A . n 
A 1 2923 ASP 2923 2923 2923 ASP ASP A . n 
A 1 2924 ARG 2924 2924 2924 ARG ARG A . n 
A 1 2925 ILE 2925 2925 2925 ILE ILE A . n 
A 1 2926 PHE 2926 2926 2926 PHE PHE A . n 
A 1 2927 ARG 2927 2927 2927 ARG ARG A . n 
A 1 2928 GLN 2928 2928 2928 GLN GLN A . n 
A 1 2929 PRO 2929 2929 2929 PRO PRO A . n 
A 1 2930 GLN 2930 2930 2930 GLN GLN A . n 
A 1 2931 GLY 2931 2931 2931 GLY GLY A . n 
A 1 2932 HIS 2932 2932 2932 HIS HIS A . n 
A 1 2933 LEU 2933 2933 2933 LEU LEU A . n 
A 1 2934 LEU 2934 2934 2934 LEU LEU A . n 
A 1 2935 LEU 2935 2935 2935 LEU LEU A . n 
A 1 2936 ILE 2936 2936 2936 ILE ILE A . n 
A 1 2937 GLY 2937 2937 2937 GLY GLY A . n 
A 1 2938 VAL 2938 2938 2938 VAL VAL A . n 
A 1 2939 SER 2939 2939 2939 SER SER A . n 
A 1 2940 GLY 2940 2940 2940 GLY GLY A . n 
A 1 2941 ALA 2941 2941 2941 ALA ALA A . n 
A 1 2942 GLY 2942 2942 2942 GLY GLY A . n 
A 1 2943 LYS 2943 2943 2943 LYS LYS A . n 
A 1 2944 THR 2944 2944 2944 THR THR A . n 
A 1 2945 THR 2945 2945 2945 THR THR A . n 
A 1 2946 LEU 2946 2946 2946 LEU LEU A . n 
A 1 2947 SER 2947 2947 2947 SER SER A . n 
A 1 2948 ARG 2948 2948 2948 ARG ARG A . n 
A 1 2949 PHE 2949 2949 2949 PHE PHE A . n 
A 1 2950 VAL 2950 2950 2950 VAL VAL A . n 
A 1 2951 ALA 2951 2951 2951 ALA ALA A . n 
A 1 2952 TRP 2952 2952 2952 TRP TRP A . n 
A 1 2953 MET 2953 2953 2953 MET MET A . n 
A 1 2954 ASN 2954 2954 2954 ASN ASN A . n 
A 1 2955 GLY 2955 2955 2955 GLY GLY A . n 
A 1 2956 LEU 2956 2956 2956 LEU LEU A . n 
A 1 2957 SER 2957 2957 2957 SER SER A . n 
A 1 2958 VAL 2958 2958 2958 VAL VAL A . n 
A 1 2959 TYR 2959 2959 2959 TYR TYR A . n 
A 1 2960 GLN 2960 2960 2960 GLN GLN A . n 
A 1 2961 ILE 2961 2961 2961 ILE ILE A . n 
A 1 2962 LYS 2962 2962 2962 LYS LYS A . n 
A 1 2963 VAL 2963 2963 2963 VAL VAL A . n 
A 1 2964 HIS 2964 2964 2964 HIS HIS A . n 
A 1 2965 ARG 2965 2965 2965 ARG ARG A . n 
A 1 2966 LYS 2966 2966 2966 LYS LYS A . n 
A 1 2967 TYR 2967 2967 2967 TYR TYR A . n 
A 1 2968 THR 2968 2968 2968 THR THR A . n 
A 1 2969 GLY 2969 2969 2969 GLY GLY A . n 
A 1 2970 GLU 2970 2970 2970 GLU GLU A . n 
A 1 2971 ASP 2971 2971 2971 ASP ASP A . n 
A 1 2972 PHE 2972 2972 2972 PHE PHE A . n 
A 1 2973 ASP 2973 2973 2973 ASP ASP A . n 
A 1 2974 GLU 2974 2974 2974 GLU GLU A . n 
A 1 2975 ASP 2975 2975 2975 ASP ASP A . n 
A 1 2976 LEU 2976 2976 2976 LEU LEU A . n 
A 1 2977 ARG 2977 2977 2977 ARG ARG A . n 
A 1 2978 THR 2978 2978 2978 THR THR A . n 
A 1 2979 VAL 2979 2979 2979 VAL VAL A . n 
A 1 2980 LEU 2980 2980 2980 LEU LEU A . n 
A 1 2981 ARG 2981 2981 2981 ARG ARG A . n 
A 1 2982 ARG 2982 2982 2982 ARG ARG A . n 
A 1 2983 SER 2983 2983 2983 SER SER A . n 
A 1 2984 GLY 2984 2984 2984 GLY GLY A . n 
A 1 2985 CYS 2985 2985 2985 CYS CYS A . n 
A 1 2986 LYS 2986 2986 2986 LYS LYS A . n 
A 1 2987 ASN 2987 2987 2987 ASN ASN A . n 
A 1 2988 GLU 2988 2988 2988 GLU GLU A . n 
A 1 2989 LYS 2989 2989 2989 LYS LYS A . n 
A 1 2990 ILE 2990 2990 2990 ILE ILE A . n 
A 1 2991 ALA 2991 2991 2991 ALA ALA A . n 
A 1 2992 PHE 2992 2992 2992 PHE PHE A . n 
A 1 2993 ILE 2993 2993 2993 ILE ILE A . n 
A 1 2994 MET 2994 2994 2994 MET MET A . n 
A 1 2995 ASP 2995 2995 2995 ASP ASP A . n 
A 1 2996 GLU 2996 2996 2996 GLU GLU A . n 
A 1 2997 SER 2997 2997 2997 SER SER A . n 
A 1 2998 ASN 2998 2998 2998 ASN ASN A . n 
A 1 2999 VAL 2999 2999 2999 VAL VAL A . n 
A 1 3000 LEU 3000 3000 3000 LEU LEU A . n 
A 1 3001 ASP 3001 3001 3001 ASP ASP A . n 
A 1 3002 SER 3002 3002 3002 SER SER A . n 
A 1 3003 GLY 3003 3003 3003 GLY GLY A . n 
A 1 3004 PHE 3004 3004 3004 PHE PHE A . n 
A 1 3005 LEU 3005 3005 3005 LEU LEU A . n 
A 1 3006 GLU 3006 3006 3006 GLU GLU A . n 
A 1 3007 ARG 3007 3007 3007 ARG ARG A . n 
A 1 3008 MET 3008 3008 3008 MET MET A . n 
A 1 3009 ASN 3009 3009 3009 ASN ASN A . n 
A 1 3010 THR 3010 3010 3010 THR THR A . n 
A 1 3011 LEU 3011 3011 3011 LEU LEU A . n 
A 1 3012 LEU 3012 3012 3012 LEU LEU A . n 
A 1 3013 ALA 3013 3013 3013 ALA ALA A . n 
A 1 3014 ASN 3014 3014 3014 ASN ASN A . n 
A 1 3015 GLY 3015 3015 3015 GLY GLY A . n 
A 1 3016 GLU 3016 3016 3016 GLU GLU A . n 
A 1 3017 VAL 3017 3017 3017 VAL VAL A . n 
A 1 3018 PRO 3018 3018 3018 PRO PRO A . n 
A 1 3019 GLY 3019 3019 3019 GLY GLY A . n 
A 1 3020 LEU 3020 3020 3020 LEU LEU A . n 
A 1 3021 PHE 3021 3021 3021 PHE PHE A . n 
A 1 3022 GLU 3022 3022 3022 GLU GLU A . n 
A 1 3023 GLY 3023 3023 3023 GLY GLY A . n 
A 1 3024 ASP 3024 3024 3024 ASP ASP A . n 
A 1 3025 GLU 3025 3025 3025 GLU GLU A . n 
A 1 3026 TYR 3026 3026 3026 TYR TYR A . n 
A 1 3027 ALA 3027 3027 3027 ALA ALA A . n 
A 1 3028 THR 3028 3028 3028 THR THR A . n 
A 1 3029 LEU 3029 3029 3029 LEU LEU A . n 
A 1 3030 MET 3030 3030 3030 MET MET A . n 
A 1 3031 THR 3031 3031 3031 THR THR A . n 
A 1 3032 GLN 3032 3032 3032 GLN GLN A . n 
A 1 3033 CYS 3033 3033 3033 CYS CYS A . n 
A 1 3034 LYS 3034 3034 3034 LYS LYS A . n 
A 1 3035 GLU 3035 3035 3035 GLU GLU A . n 
A 1 3036 GLY 3036 3036 3036 GLY GLY A . n 
A 1 3037 ALA 3037 3037 3037 ALA ALA A . n 
A 1 3038 GLN 3038 3038 3038 GLN GLN A . n 
A 1 3039 LYS 3039 3039 3039 LYS LYS A . n 
A 1 3040 GLU 3040 3040 3040 GLU GLU A . n 
A 1 3041 GLY 3041 3041 3041 GLY GLY A . n 
A 1 3042 LEU 3042 3042 3042 LEU LEU A . n 
A 1 3043 MET 3043 3043 3043 MET MET A . n 
A 1 3044 LEU 3044 3044 3044 LEU LEU A . n 
A 1 3045 ASP 3045 3045 3045 ASP ASP A . n 
A 1 3046 SER 3046 3046 3046 SER SER A . n 
A 1 3047 HIS 3047 3047 3047 HIS HIS A . n 
A 1 3048 GLU 3048 3048 3048 GLU GLU A . n 
A 1 3049 GLU 3049 3049 3049 GLU GLU A . n 
A 1 3050 LEU 3050 3050 3050 LEU LEU A . n 
A 1 3051 TYR 3051 3051 3051 TYR TYR A . n 
A 1 3052 LYS 3052 3052 3052 LYS LYS A . n 
A 1 3053 TRP 3053 3053 3053 TRP TRP A . n 
A 1 3054 PHE 3054 3054 3054 PHE PHE A . n 
A 1 3055 THR 3055 3055 3055 THR THR A . n 
A 1 3056 SER 3056 3056 3056 SER SER A . n 
A 1 3057 GLN 3057 3057 3057 GLN GLN A . n 
A 1 3058 VAL 3058 3058 3058 VAL VAL A . n 
A 1 3059 ILE 3059 3059 3059 ILE ILE A . n 
A 1 3060 ARG 3060 3060 3060 ARG ARG A . n 
A 1 3061 ASN 3061 3061 3061 ASN ASN A . n 
A 1 3062 LEU 3062 3062 3062 LEU LEU A . n 
A 1 3063 HIS 3063 3063 3063 HIS HIS A . n 
A 1 3064 VAL 3064 3064 3064 VAL VAL A . n 
A 1 3065 VAL 3065 3065 3065 VAL VAL A . n 
A 1 3066 PHE 3066 3066 3066 PHE PHE A . n 
A 1 3067 THR 3067 3067 3067 THR THR A . n 
A 1 3068 MET 3068 3068 3068 MET MET A . n 
A 1 3069 ASN 3069 3069 3069 ASN ASN A . n 
A 1 3070 PRO 3070 3070 3070 PRO PRO A . n 
A 1 3071 SER 3071 3071 ?    ?   ?   A . n 
A 1 3072 SER 3072 3072 ?    ?   ?   A . n 
A 1 3073 GLU 3073 3073 ?    ?   ?   A . n 
A 1 3074 GLY 3074 3074 ?    ?   ?   A . n 
A 1 3075 LEU 3075 3075 ?    ?   ?   A . n 
A 1 3076 LYS 3076 3076 ?    ?   ?   A . n 
A 1 3077 ASP 3077 3077 ?    ?   ?   A . n 
A 1 3078 ARG 3078 3078 ?    ?   ?   A . n 
A 1 3079 ALA 3079 3079 ?    ?   ?   A . n 
A 1 3080 ALA 3080 3080 ?    ?   ?   A . n 
A 1 3081 THR 3081 3081 ?    ?   ?   A . n 
A 1 3082 SER 3082 3082 3082 SER SER A . n 
A 1 3083 PRO 3083 3083 3083 PRO PRO A . n 
A 1 3084 ALA 3084 3084 3084 ALA ALA A . n 
A 1 3085 LEU 3085 3085 3085 LEU LEU A . n 
A 1 3086 PHE 3086 3086 3086 PHE PHE A . n 
A 1 3087 ASN 3087 3087 3087 ASN ASN A . n 
A 1 3088 ARG 3088 3088 3088 ARG ARG A . n 
A 1 3089 CYS 3089 3089 3089 CYS CYS A . n 
A 1 3090 VAL 3090 3090 3090 VAL VAL A . n 
A 1 3091 LEU 3091 3091 3091 LEU LEU A . n 
A 1 3092 ASN 3092 3092 3092 ASN ASN A . n 
A 1 3093 TRP 3093 3093 3093 TRP TRP A . n 
A 1 3094 PHE 3094 3094 3094 PHE PHE A . n 
A 1 3095 GLY 3095 3095 3095 GLY GLY A . n 
A 1 3096 ASP 3096 3096 3096 ASP ASP A . n 
A 1 3097 TRP 3097 3097 3097 TRP TRP A . n 
A 1 3098 SER 3098 3098 3098 SER SER A . n 
A 1 3099 THR 3099 3099 3099 THR THR A . n 
A 1 3100 GLU 3100 3100 3100 GLU GLU A . n 
A 1 3101 ALA 3101 3101 3101 ALA ALA A . n 
A 1 3102 LEU 3102 3102 3102 LEU LEU A . n 
A 1 3103 TYR 3103 3103 3103 TYR TYR A . n 
A 1 3104 GLN 3104 3104 3104 GLN GLN A . n 
A 1 3105 VAL 3105 3105 3105 VAL VAL A . n 
A 1 3106 GLY 3106 3106 3106 GLY GLY A . n 
A 1 3107 LYS 3107 3107 3107 LYS LYS A . n 
A 1 3108 GLU 3108 3108 3108 GLU GLU A . n 
A 1 3109 PHE 3109 3109 3109 PHE PHE A . n 
A 1 3110 THR 3110 3110 3110 THR THR A . n 
A 1 3111 SER 3111 3111 3111 SER SER A . n 
A 1 3112 LYS 3112 3112 3112 LYS LYS A . n 
A 1 3113 MET 3113 3113 3113 MET MET A . n 
A 1 3114 ASP 3114 3114 3114 ASP ASP A . n 
A 1 3115 LEU 3115 3115 3115 LEU LEU A . n 
A 1 3116 GLU 3116 3116 3116 GLU GLU A . n 
A 1 3117 LYS 3117 3117 3117 LYS LYS A . n 
A 1 3118 PRO 3118 3118 3118 PRO PRO A . n 
A 1 3119 ASN 3119 3119 3119 ASN ASN A . n 
A 1 3120 TYR 3120 3120 3120 TYR TYR A . n 
A 1 3121 ILE 3121 3121 3121 ILE ILE A . n 
A 1 3122 VAL 3122 3122 3122 VAL VAL A . n 
A 1 3123 PRO 3123 3123 3123 PRO PRO A . n 
A 1 3124 ASP 3124 3124 3124 ASP ASP A . n 
A 1 3125 TYR 3125 3125 3125 TYR TYR A . n 
A 1 3126 MET 3126 3126 3126 MET MET A . n 
A 1 3127 PRO 3127 3127 3127 PRO PRO A . n 
A 1 3128 VAL 3128 3128 3128 VAL VAL A . n 
A 1 3129 VAL 3129 3129 3129 VAL VAL A . n 
A 1 3130 TYR 3130 3130 3130 TYR TYR A . n 
A 1 3131 ASP 3131 3131 3131 ASP ASP A . n 
A 1 3132 LYS 3132 3132 3132 LYS LYS A . n 
A 1 3133 LEU 3133 3133 3133 LEU LEU A . n 
A 1 3134 PRO 3134 3134 3134 PRO PRO A . n 
A 1 3135 GLN 3135 3135 3135 GLN GLN A . n 
A 1 3136 PRO 3136 3136 3136 PRO PRO A . n 
A 1 3137 PRO 3137 3137 3137 PRO PRO A . n 
A 1 3138 SER 3138 3138 3138 SER SER A . n 
A 1 3139 HIS 3139 3139 3139 HIS HIS A . n 
A 1 3140 ARG 3140 3140 3140 ARG ARG A . n 
A 1 3141 GLU 3141 3141 3141 GLU GLU A . n 
A 1 3142 ALA 3142 3142 3142 ALA ALA A . n 
A 1 3143 ILE 3143 3143 3143 ILE ILE A . n 
A 1 3144 VAL 3144 3144 3144 VAL VAL A . n 
A 1 3145 ASN 3145 3145 3145 ASN ASN A . n 
A 1 3146 SER 3146 3146 3146 SER SER A . n 
A 1 3147 CYS 3147 3147 3147 CYS CYS A . n 
A 1 3148 VAL 3148 3148 3148 VAL VAL A . n 
A 1 3149 PHE 3149 3149 3149 PHE PHE A . n 
A 1 3150 VAL 3150 3150 3150 VAL VAL A . n 
A 1 3151 HIS 3151 3151 3151 HIS HIS A . n 
A 1 3152 GLN 3152 3152 3152 GLN GLN A . n 
A 1 3153 THR 3153 3153 3153 THR THR A . n 
A 1 3154 LEU 3154 3154 3154 LEU LEU A . n 
A 1 3155 HIS 3155 3155 3155 HIS HIS A . n 
A 1 3156 GLN 3156 3156 3156 GLN GLN A . n 
A 1 3157 ALA 3157 3157 3157 ALA ALA A . n 
A 1 3158 ASN 3158 3158 3158 ASN ASN A . n 
A 1 3159 ALA 3159 3159 3159 ALA ALA A . n 
A 1 3160 ARG 3160 3160 3160 ARG ARG A . n 
A 1 3161 LEU 3161 3161 3161 LEU LEU A . n 
A 1 3162 ALA 3162 3162 3162 ALA ALA A . n 
A 1 3163 LYS 3163 3163 3163 LYS LYS A . n 
A 1 3164 ARG 3164 3164 3164 ARG ARG A . n 
A 1 3165 GLY 3165 3165 3165 GLY GLY A . n 
A 1 3166 GLY 3166 3166 3166 GLY GLY A . n 
A 1 3167 ARG 3167 3167 3167 ARG ARG A . n 
A 1 3168 THR 3168 3168 3168 THR THR A . n 
A 1 3169 MET 3169 3169 3169 MET MET A . n 
A 1 3170 ALA 3170 3170 3170 ALA ALA A . n 
A 1 3171 ILE 3171 3171 3171 ILE ILE A . n 
A 1 3172 THR 3172 3172 3172 THR THR A . n 
A 1 3173 PRO 3173 3173 3173 PRO PRO A . n 
A 1 3174 ARG 3174 3174 3174 ARG ARG A . n 
A 1 3175 HIS 3175 3175 3175 HIS HIS A . n 
A 1 3176 TYR 3176 3176 3176 TYR TYR A . n 
A 1 3177 LEU 3177 3177 3177 LEU LEU A . n 
A 1 3178 ASP 3178 3178 3178 ASP ASP A . n 
A 1 3179 PHE 3179 3179 3179 PHE PHE A . n 
A 1 3180 ILE 3180 3180 3180 ILE ILE A . n 
A 1 3181 ASN 3181 3181 3181 ASN ASN A . n 
A 1 3182 HIS 3182 3182 3182 HIS HIS A . n 
A 1 3183 TYR 3183 3183 3183 TYR TYR A . n 
A 1 3184 ALA 3184 3184 3184 ALA ALA A . n 
A 1 3185 ASN 3185 3185 3185 ASN ASN A . n 
A 1 3186 LEU 3186 3186 3186 LEU LEU A . n 
A 1 3187 PHE 3187 3187 3187 PHE PHE A . n 
A 1 3188 HIS 3188 3188 3188 HIS HIS A . n 
A 1 3189 GLU 3189 3189 3189 GLU GLU A . n 
A 1 3190 LYS 3190 3190 3190 LYS LYS A . n 
A 1 3191 ARG 3191 3191 3191 ARG ARG A . n 
A 1 3192 SER 3192 3192 3192 SER SER A . n 
A 1 3193 GLU 3193 3193 3193 GLU GLU A . n 
A 1 3194 LEU 3194 3194 3194 LEU LEU A . n 
A 1 3195 GLU 3195 3195 3195 GLU GLU A . n 
A 1 3196 GLU 3196 3196 3196 GLU GLU A . n 
A 1 3197 GLN 3197 3197 3197 GLN GLN A . n 
A 1 3198 GLN 3198 3198 3198 GLN GLN A . n 
A 1 3199 MET 3199 3199 3199 MET MET A . n 
A 1 3200 HIS 3200 3200 3200 HIS HIS A . n 
A 1 3201 LEU 3201 3201 3201 LEU LEU A . n 
A 1 3202 ASN 3202 3202 3202 ASN ASN A . n 
A 1 3203 VAL 3203 3203 3203 VAL VAL A . n 
A 1 3204 GLY 3204 3204 3204 GLY GLY A . n 
A 1 3205 LEU 3205 3205 3205 LEU LEU A . n 
A 1 3206 ARG 3206 3206 3206 ARG ARG A . n 
A 1 3207 LYS 3207 3207 3207 LYS LYS A . n 
A 1 3208 ILE 3208 3208 3208 ILE ILE A . n 
A 1 3209 LYS 3209 3209 3209 LYS LYS A . n 
A 1 3210 GLU 3210 3210 3210 GLU GLU A . n 
A 1 3211 THR 3211 3211 3211 THR THR A . n 
A 1 3212 VAL 3212 3212 3212 VAL VAL A . n 
A 1 3213 ASP 3213 3213 3213 ASP ASP A . n 
A 1 3214 GLN 3214 3214 3214 GLN GLN A . n 
A 1 3215 VAL 3215 3215 3215 VAL VAL A . n 
A 1 3216 GLU 3216 3216 3216 GLU GLU A . n 
A 1 3217 GLU 3217 3217 3217 GLU GLU A . n 
A 1 3218 LEU 3218 3218 3218 LEU LEU A . n 
A 1 3219 ARG 3219 3219 3219 ARG ARG A . n 
A 1 3220 ARG 3220 3220 3220 ARG ARG A . n 
A 1 3221 ASP 3221 3221 ?    ?   ?   A . n 
A 1 3222 LEU 3222 3222 ?    ?   ?   A . n 
A 1 3223 ARG 3223 3223 ?    ?   ?   A . n 
A 1 3224 ILE 3224 3224 ?    ?   ?   A . n 
A 1 3225 LYS 3225 3225 ?    ?   ?   A . n 
A 1 3226 SER 3226 3226 ?    ?   ?   A . n 
A 1 3227 GLN 3227 3227 ?    ?   ?   A . n 
A 1 3228 GLU 3228 3228 ?    ?   ?   A . n 
A 1 3229 LEU 3229 3229 ?    ?   ?   A . n 
A 1 3230 GLU 3230 3230 ?    ?   ?   A . n 
A 1 3231 VAL 3231 3231 ?    ?   ?   A . n 
A 1 3232 LYS 3232 3232 ?    ?   ?   A . n 
A 1 3233 ASN 3233 3233 ?    ?   ?   A . n 
A 1 3234 ALA 3234 3234 ?    ?   ?   A . n 
A 1 3235 ALA 3235 3235 ?    ?   ?   A . n 
A 1 3236 ALA 3236 3236 ?    ?   ?   A . n 
A 1 3237 ASN 3237 3237 ?    ?   ?   A . n 
A 1 3238 ASP 3238 3238 ?    ?   ?   A . n 
A 1 3239 LYS 3239 3239 ?    ?   ?   A . n 
A 1 3240 LEU 3240 3240 ?    ?   ?   A . n 
A 1 3241 LYS 3241 3241 ?    ?   ?   A . n 
A 1 3242 LYS 3242 3242 ?    ?   ?   A . n 
A 1 3243 MET 3243 3243 ?    ?   ?   A . n 
A 1 3244 VAL 3244 3244 ?    ?   ?   A . n 
A 1 3245 LYS 3245 3245 ?    ?   ?   A . n 
A 1 3246 ASP 3246 3246 ?    ?   ?   A . n 
A 1 3247 GLN 3247 3247 ?    ?   ?   A . n 
A 1 3248 GLN 3248 3248 ?    ?   ?   A . n 
A 1 3249 GLU 3249 3249 ?    ?   ?   A . n 
A 1 3250 ALA 3250 3250 ?    ?   ?   A . n 
A 1 3251 GLU 3251 3251 ?    ?   ?   A . n 
A 1 3252 LYS 3252 3252 ?    ?   ?   A . n 
A 1 3253 LYS 3253 3253 ?    ?   ?   A . n 
A 1 3254 LYS 3254 3254 ?    ?   ?   A . n 
A 1 3255 VAL 3255 3255 ?    ?   ?   A . n 
A 1 3256 MET 3256 3256 ?    ?   ?   A . n 
A 1 3257 SER 3257 3257 ?    ?   ?   A . n 
A 1 3258 GLN 3258 3258 ?    ?   ?   A . n 
A 1 3259 GLU 3259 3259 ?    ?   ?   A . n 
A 1 3260 ILE 3260 3260 ?    ?   ?   A . n 
A 1 3261 GLN 3261 3261 ?    ?   ?   A . n 
A 1 3262 GLU 3262 3262 ?    ?   ?   A . n 
A 1 3263 GLN 3263 3263 ?    ?   ?   A . n 
A 1 3264 LEU 3264 3264 ?    ?   ?   A . n 
A 1 3265 HIS 3265 3265 ?    ?   ?   A . n 
A 1 3266 LYS 3266 3266 ?    ?   ?   A . n 
A 1 3267 GLN 3267 3267 ?    ?   ?   A . n 
A 1 3268 GLN 3268 3268 ?    ?   ?   A . n 
A 1 3269 GLU 3269 3269 ?    ?   ?   A . n 
A 1 3270 VAL 3270 3270 ?    ?   ?   A . n 
A 1 3271 ILE 3271 3271 ?    ?   ?   A . n 
A 1 3272 ALA 3272 3272 ?    ?   ?   A . n 
A 1 3273 ASP 3273 3273 ?    ?   ?   A . n 
A 1 3274 LYS 3274 3274 ?    ?   ?   A . n 
A 1 3275 GLN 3275 3275 ?    ?   ?   A . n 
A 1 3276 MET 3276 3276 ?    ?   ?   A . n 
A 1 3277 SER 3277 3277 ?    ?   ?   A . n 
A 1 3278 VAL 3278 3278 ?    ?   ?   A . n 
A 1 3279 LYS 3279 3279 ?    ?   ?   A . n 
A 1 3280 GLU 3280 3280 ?    ?   ?   A . n 
A 1 3281 ASP 3281 3281 ?    ?   ?   A . n 
A 1 3282 LEU 3282 3282 ?    ?   ?   A . n 
A 1 3283 ASP 3283 3283 ?    ?   ?   A . n 
A 1 3284 LYS 3284 3284 ?    ?   ?   A . n 
A 1 3285 VAL 3285 3285 ?    ?   ?   A . n 
A 1 3286 GLU 3286 3286 ?    ?   ?   A . n 
A 1 3287 PRO 3287 3287 ?    ?   ?   A . n 
A 1 3288 ALA 3288 3288 ?    ?   ?   A . n 
A 1 3289 VAL 3289 3289 ?    ?   ?   A . n 
A 1 3290 ILE 3290 3290 ?    ?   ?   A . n 
A 1 3291 GLU 3291 3291 ?    ?   ?   A . n 
A 1 3292 ALA 3292 3292 ?    ?   ?   A . n 
A 1 3293 GLN 3293 3293 ?    ?   ?   A . n 
A 1 3294 ASN 3294 3294 ?    ?   ?   A . n 
A 1 3295 ALA 3295 3295 ?    ?   ?   A . n 
A 1 3296 VAL 3296 3296 ?    ?   ?   A . n 
A 1 3297 LYS 3297 3297 ?    ?   ?   A . n 
A 1 3298 SER 3298 3298 ?    ?   ?   A . n 
A 1 3299 ILE 3299 3299 ?    ?   ?   A . n 
A 1 3300 LYS 3300 3300 ?    ?   ?   A . n 
A 1 3301 LYS 3301 3301 ?    ?   ?   A . n 
A 1 3302 GLN 3302 3302 ?    ?   ?   A . n 
A 1 3303 HIS 3303 3303 ?    ?   ?   A . n 
A 1 3304 LEU 3304 3304 ?    ?   ?   A . n 
A 1 3305 VAL 3305 3305 ?    ?   ?   A . n 
A 1 3306 GLU 3306 3306 ?    ?   ?   A . n 
A 1 3307 VAL 3307 3307 ?    ?   ?   A . n 
A 1 3308 ARG 3308 3308 ?    ?   ?   A . n 
A 1 3309 SER 3309 3309 ?    ?   ?   A . n 
A 1 3310 MET 3310 3310 ?    ?   ?   A . n 
A 1 3311 ALA 3311 3311 ?    ?   ?   A . n 
A 1 3312 ASN 3312 3312 ?    ?   ?   A . n 
A 1 3313 PRO 3313 3313 ?    ?   ?   A . n 
A 1 3314 PRO 3314 3314 ?    ?   ?   A . n 
A 1 3315 ALA 3315 3315 ?    ?   ?   A . n 
A 1 3316 ALA 3316 3316 ?    ?   ?   A . n 
A 1 3317 VAL 3317 3317 ?    ?   ?   A . n 
A 1 3318 LYS 3318 3318 ?    ?   ?   A . n 
A 1 3319 LEU 3319 3319 ?    ?   ?   A . n 
A 1 3320 ALA 3320 3320 ?    ?   ?   A . n 
A 1 3321 LEU 3321 3321 ?    ?   ?   A . n 
A 1 3322 GLU 3322 3322 ?    ?   ?   A . n 
A 1 3323 SER 3323 3323 ?    ?   ?   A . n 
A 1 3324 ILE 3324 3324 ?    ?   ?   A . n 
A 1 3325 CYS 3325 3325 ?    ?   ?   A . n 
A 1 3326 LEU 3326 3326 ?    ?   ?   A . n 
A 1 3327 LEU 3327 3327 ?    ?   ?   A . n 
A 1 3328 LEU 3328 3328 ?    ?   ?   A . n 
A 1 3329 GLY 3329 3329 ?    ?   ?   A . n 
A 1 3330 GLU 3330 3330 ?    ?   ?   A . n 
A 1 3331 SER 3331 3331 ?    ?   ?   A . n 
A 1 3332 THR 3332 3332 ?    ?   ?   A . n 
A 1 3333 THR 3333 3333 ?    ?   ?   A . n 
A 1 3334 ASP 3334 3334 ?    ?   ?   A . n 
A 1 3335 TRP 3335 3335 ?    ?   ?   A . n 
A 1 3336 LYS 3336 3336 ?    ?   ?   A . n 
A 1 3337 GLN 3337 3337 ?    ?   ?   A . n 
A 1 3338 ILE 3338 3338 ?    ?   ?   A . n 
A 1 3339 ARG 3339 3339 ?    ?   ?   A . n 
A 1 3340 SER 3340 3340 ?    ?   ?   A . n 
A 1 3341 ILE 3341 3341 ?    ?   ?   A . n 
A 1 3342 ILE 3342 3342 ?    ?   ?   A . n 
A 1 3343 MET 3343 3343 ?    ?   ?   A . n 
A 1 3344 ARG 3344 3344 ?    ?   ?   A . n 
A 1 3345 GLU 3345 3345 ?    ?   ?   A . n 
A 1 3346 ASN 3346 3346 ?    ?   ?   A . n 
A 1 3347 PHE 3347 3347 ?    ?   ?   A . n 
A 1 3348 ILE 3348 3348 ?    ?   ?   A . n 
A 1 3349 PRO 3349 3349 ?    ?   ?   A . n 
A 1 3350 THR 3350 3350 ?    ?   ?   A . n 
A 1 3351 ILE 3351 3351 ?    ?   ?   A . n 
A 1 3352 VAL 3352 3352 ?    ?   ?   A . n 
A 1 3353 ASN 3353 3353 ?    ?   ?   A . n 
A 1 3354 PHE 3354 3354 ?    ?   ?   A . n 
A 1 3355 SER 3355 3355 ?    ?   ?   A . n 
A 1 3356 ALA 3356 3356 ?    ?   ?   A . n 
A 1 3357 GLU 3357 3357 ?    ?   ?   A . n 
A 1 3358 GLU 3358 3358 ?    ?   ?   A . n 
A 1 3359 ILE 3359 3359 ?    ?   ?   A . n 
A 1 3360 SER 3360 3360 ?    ?   ?   A . n 
A 1 3361 ASP 3361 3361 ?    ?   ?   A . n 
A 1 3362 ALA 3362 3362 ?    ?   ?   A . n 
A 1 3363 ILE 3363 3363 ?    ?   ?   A . n 
A 1 3364 ARG 3364 3364 ?    ?   ?   A . n 
A 1 3365 GLU 3365 3365 ?    ?   ?   A . n 
A 1 3366 LYS 3366 3366 ?    ?   ?   A . n 
A 1 3367 MET 3367 3367 ?    ?   ?   A . n 
A 1 3368 LYS 3368 3368 ?    ?   ?   A . n 
A 1 3369 LYS 3369 3369 ?    ?   ?   A . n 
A 1 3370 ASN 3370 3370 ?    ?   ?   A . n 
A 1 3371 TYR 3371 3371 ?    ?   ?   A . n 
A 1 3372 MET 3372 3372 ?    ?   ?   A . n 
A 1 3373 SER 3373 3373 ?    ?   ?   A . n 
A 1 3374 ASN 3374 3374 ?    ?   ?   A . n 
A 1 3375 PRO 3375 3375 ?    ?   ?   A . n 
A 1 3376 SER 3376 3376 ?    ?   ?   A . n 
A 1 3377 TYR 3377 3377 ?    ?   ?   A . n 
A 1 3378 ASN 3378 3378 ?    ?   ?   A . n 
A 1 3379 TYR 3379 3379 ?    ?   ?   A . n 
A 1 3380 GLU 3380 3380 ?    ?   ?   A . n 
A 1 3381 ILE 3381 3381 ?    ?   ?   A . n 
A 1 3382 VAL 3382 3382 ?    ?   ?   A . n 
A 1 3383 ASN 3383 3383 ?    ?   ?   A . n 
A 1 3384 ARG 3384 3384 ?    ?   ?   A . n 
A 1 3385 ALA 3385 3385 ?    ?   ?   A . n 
A 1 3386 SER 3386 3386 ?    ?   ?   A . n 
A 1 3387 LEU 3387 3387 ?    ?   ?   A . n 
A 1 3388 ALA 3388 3388 ?    ?   ?   A . n 
A 1 3389 CYS 3389 3389 ?    ?   ?   A . n 
A 1 3390 GLY 3390 3390 ?    ?   ?   A . n 
A 1 3391 PRO 3391 3391 ?    ?   ?   A . n 
A 1 3392 MET 3392 3392 ?    ?   ?   A . n 
A 1 3393 VAL 3393 3393 ?    ?   ?   A . n 
A 1 3394 LYS 3394 3394 ?    ?   ?   A . n 
A 1 3395 TRP 3395 3395 ?    ?   ?   A . n 
A 1 3396 ALA 3396 3396 ?    ?   ?   A . n 
A 1 3397 ILE 3397 3397 ?    ?   ?   A . n 
A 1 3398 ALA 3398 3398 ?    ?   ?   A . n 
A 1 3399 GLN 3399 3399 ?    ?   ?   A . n 
A 1 3400 LEU 3400 3400 ?    ?   ?   A . n 
A 1 3401 ASN 3401 3401 ?    ?   ?   A . n 
A 1 3402 TYR 3402 3402 ?    ?   ?   A . n 
A 1 3403 ALA 3403 3403 ?    ?   ?   A . n 
A 1 3404 ASP 3404 3404 ?    ?   ?   A . n 
A 1 3405 MET 3405 3405 ?    ?   ?   A . n 
A 1 3406 LEU 3406 3406 ?    ?   ?   A . n 
A 1 3407 LYS 3407 3407 ?    ?   ?   A . n 
A 1 3408 ARG 3408 3408 ?    ?   ?   A . n 
A 1 3409 VAL 3409 3409 ?    ?   ?   A . n 
A 1 3410 GLU 3410 3410 ?    ?   ?   A . n 
A 1 3411 PRO 3411 3411 ?    ?   ?   A . n 
A 1 3412 LEU 3412 3412 ?    ?   ?   A . n 
A 1 3413 ARG 3413 3413 ?    ?   ?   A . n 
A 1 3414 ASN 3414 3414 ?    ?   ?   A . n 
A 1 3415 GLU 3415 3415 ?    ?   ?   A . n 
A 1 3416 LEU 3416 3416 ?    ?   ?   A . n 
A 1 3417 GLN 3417 3417 ?    ?   ?   A . n 
A 1 3418 LYS 3418 3418 ?    ?   ?   A . n 
A 1 3419 LEU 3419 3419 ?    ?   ?   A . n 
A 1 3420 GLU 3420 3420 ?    ?   ?   A . n 
A 1 3421 ASP 3421 3421 ?    ?   ?   A . n 
A 1 3422 ASP 3422 3422 ?    ?   ?   A . n 
A 1 3423 ALA 3423 3423 ?    ?   ?   A . n 
A 1 3424 LYS 3424 3424 ?    ?   ?   A . n 
A 1 3425 ASP 3425 3425 ?    ?   ?   A . n 
A 1 3426 ASN 3426 3426 ?    ?   ?   A . n 
A 1 3427 GLN 3427 3427 ?    ?   ?   A . n 
A 1 3428 GLN 3428 3428 ?    ?   ?   A . n 
A 1 3429 LYS 3429 3429 ?    ?   ?   A . n 
A 1 3430 ALA 3430 3430 ?    ?   ?   A . n 
A 1 3431 ASN 3431 3431 ?    ?   ?   A . n 
A 1 3432 GLU 3432 3432 ?    ?   ?   A . n 
A 1 3433 VAL 3433 3433 ?    ?   ?   A . n 
A 1 3434 GLU 3434 3434 ?    ?   ?   A . n 
A 1 3435 GLN 3435 3435 ?    ?   ?   A . n 
A 1 3436 MET 3436 3436 ?    ?   ?   A . n 
A 1 3437 ILE 3437 3437 ?    ?   ?   A . n 
A 1 3438 ARG 3438 3438 ?    ?   ?   A . n 
A 1 3439 ASP 3439 3439 ?    ?   ?   A . n 
A 1 3440 LEU 3440 3440 ?    ?   ?   A . n 
A 1 3441 GLU 3441 3441 ?    ?   ?   A . n 
A 1 3442 ALA 3442 3442 ?    ?   ?   A . n 
A 1 3443 SER 3443 3443 ?    ?   ?   A . n 
A 1 3444 ILE 3444 3444 ?    ?   ?   A . n 
A 1 3445 ALA 3445 3445 ?    ?   ?   A . n 
A 1 3446 ARG 3446 3446 ?    ?   ?   A . n 
A 1 3447 TYR 3447 3447 ?    ?   ?   A . n 
A 1 3448 LYS 3448 3448 ?    ?   ?   A . n 
A 1 3449 GLU 3449 3449 ?    ?   ?   A . n 
A 1 3450 GLU 3450 3450 ?    ?   ?   A . n 
A 1 3451 TYR 3451 3451 ?    ?   ?   A . n 
A 1 3452 ALA 3452 3452 ?    ?   ?   A . n 
A 1 3453 VAL 3453 3453 ?    ?   ?   A . n 
A 1 3454 LEU 3454 3454 ?    ?   ?   A . n 
A 1 3455 ILE 3455 3455 ?    ?   ?   A . n 
A 1 3456 SER 3456 3456 ?    ?   ?   A . n 
A 1 3457 GLU 3457 3457 ?    ?   ?   A . n 
A 1 3458 ALA 3458 3458 ?    ?   ?   A . n 
A 1 3459 GLN 3459 3459 ?    ?   ?   A . n 
A 1 3460 ALA 3460 3460 ?    ?   ?   A . n 
A 1 3461 ILE 3461 3461 ?    ?   ?   A . n 
A 1 3462 LYS 3462 3462 ?    ?   ?   A . n 
A 1 3463 ALA 3463 3463 ?    ?   ?   A . n 
A 1 3464 ASP 3464 3464 ?    ?   ?   A . n 
A 1 3465 LEU 3465 3465 ?    ?   ?   A . n 
A 1 3466 ALA 3466 3466 ?    ?   ?   A . n 
A 1 3467 ALA 3467 3467 ?    ?   ?   A . n 
A 1 3468 VAL 3468 3468 ?    ?   ?   A . n 
A 1 3469 GLU 3469 3469 ?    ?   ?   A . n 
A 1 3470 ALA 3470 3470 ?    ?   ?   A . n 
A 1 3471 LYS 3471 3471 3471 LYS LYS A . n 
A 1 3472 VAL 3472 3472 3472 VAL VAL A . n 
A 1 3473 ASN 3473 3473 3473 ASN ASN A . n 
A 1 3474 ARG 3474 3474 3474 ARG ARG A . n 
A 1 3475 SER 3475 3475 3475 SER SER A . n 
A 1 3476 THR 3476 3476 3476 THR THR A . n 
A 1 3477 ALA 3477 3477 3477 ALA ALA A . n 
A 1 3478 LEU 3478 3478 3478 LEU LEU A . n 
A 1 3479 LEU 3479 3479 3479 LEU LEU A . n 
A 1 3480 LYS 3480 3480 3480 LYS LYS A . n 
A 1 3481 SER 3481 3481 3481 SER SER A . n 
A 1 3482 LEU 3482 3482 3482 LEU LEU A . n 
A 1 3483 SER 3483 3483 3483 SER SER A . n 
A 1 3484 ALA 3484 3484 3484 ALA ALA A . n 
A 1 3485 GLU 3485 3485 3485 GLU GLU A . n 
A 1 3486 ARG 3486 3486 3486 ARG ARG A . n 
A 1 3487 GLU 3487 3487 3487 GLU GLU A . n 
A 1 3488 ARG 3488 3488 3488 ARG ARG A . n 
A 1 3489 TRP 3489 3489 3489 TRP TRP A . n 
A 1 3490 GLU 3490 3490 3490 GLU GLU A . n 
A 1 3491 LYS 3491 3491 3491 LYS LYS A . n 
A 1 3492 THR 3492 3492 3492 THR THR A . n 
A 1 3493 SER 3493 3493 3493 SER SER A . n 
A 1 3494 GLU 3494 3494 3494 GLU GLU A . n 
A 1 3495 THR 3495 3495 3495 THR THR A . n 
A 1 3496 PHE 3496 3496 3496 PHE PHE A . n 
A 1 3497 LYS 3497 3497 3497 LYS LYS A . n 
A 1 3498 ASN 3498 3498 3498 ASN ASN A . n 
A 1 3499 GLN 3499 3499 3499 GLN GLN A . n 
A 1 3500 MET 3500 3500 3500 MET MET A . n 
A 1 3501 SER 3501 3501 3501 SER SER A . n 
A 1 3502 THR 3502 3502 3502 THR THR A . n 
A 1 3503 ILE 3503 3503 3503 ILE ILE A . n 
A 1 3504 ALA 3504 3504 3504 ALA ALA A . n 
A 1 3505 GLY 3505 3505 3505 GLY GLY A . n 
A 1 3506 ASP 3506 3506 3506 ASP ASP A . n 
A 1 3507 CYS 3507 3507 3507 CYS CYS A . n 
A 1 3508 LEU 3508 3508 3508 LEU LEU A . n 
A 1 3509 LEU 3509 3509 3509 LEU LEU A . n 
A 1 3510 SER 3510 3510 3510 SER SER A . n 
A 1 3511 ALA 3511 3511 3511 ALA ALA A . n 
A 1 3512 ALA 3512 3512 3512 ALA ALA A . n 
A 1 3513 PHE 3513 3513 3513 PHE PHE A . n 
A 1 3514 ILE 3514 3514 3514 ILE ILE A . n 
A 1 3515 ALA 3515 3515 3515 ALA ALA A . n 
A 1 3516 TYR 3516 3516 3516 TYR TYR A . n 
A 1 3517 ALA 3517 3517 3517 ALA ALA A . n 
A 1 3518 GLY 3518 3518 3518 GLY GLY A . n 
A 1 3519 TYR 3519 3519 3519 TYR TYR A . n 
A 1 3520 PHE 3520 3520 3520 PHE PHE A . n 
A 1 3521 ASP 3521 3521 3521 ASP ASP A . n 
A 1 3522 GLN 3522 3522 3522 GLN GLN A . n 
A 1 3523 GLN 3523 3523 3523 GLN GLN A . n 
A 1 3524 MET 3524 3524 3524 MET MET A . n 
A 1 3525 ARG 3525 3525 3525 ARG ARG A . n 
A 1 3526 GLN 3526 3526 3526 GLN GLN A . n 
A 1 3527 ASN 3527 3527 3527 ASN ASN A . n 
A 1 3528 LEU 3528 3528 3528 LEU LEU A . n 
A 1 3529 PHE 3529 3529 3529 PHE PHE A . n 
A 1 3530 THR 3530 3530 3530 THR THR A . n 
A 1 3531 THR 3531 3531 3531 THR THR A . n 
A 1 3532 TRP 3532 3532 3532 TRP TRP A . n 
A 1 3533 SER 3533 3533 3533 SER SER A . n 
A 1 3534 HIS 3534 3534 3534 HIS HIS A . n 
A 1 3535 HIS 3535 3535 3535 HIS HIS A . n 
A 1 3536 LEU 3536 3536 3536 LEU LEU A . n 
A 1 3537 GLN 3537 3537 3537 GLN GLN A . n 
A 1 3538 GLN 3538 3538 3538 GLN GLN A . n 
A 1 3539 ALA 3539 3539 3539 ALA ALA A . n 
A 1 3540 ASN 3540 3540 3540 ASN ASN A . n 
A 1 3541 ILE 3541 3541 3541 ILE ILE A . n 
A 1 3542 GLN 3542 3542 3542 GLN GLN A . n 
A 1 3543 PHE 3543 3543 3543 PHE PHE A . n 
A 1 3544 ARG 3544 3544 3544 ARG ARG A . n 
A 1 3545 THR 3545 3545 3545 THR THR A . n 
A 1 3546 ASP 3546 3546 3546 ASP ASP A . n 
A 1 3547 ILE 3547 3547 3547 ILE ILE A . n 
A 1 3548 ALA 3548 3548 3548 ALA ALA A . n 
A 1 3549 ARG 3549 3549 3549 ARG ARG A . n 
A 1 3550 THR 3550 3550 3550 THR THR A . n 
A 1 3551 GLU 3551 3551 3551 GLU GLU A . n 
A 1 3552 TYR 3552 3552 3552 TYR TYR A . n 
A 1 3553 LEU 3553 3553 3553 LEU LEU A . n 
A 1 3554 SER 3554 3554 3554 SER SER A . n 
A 1 3555 ASN 3555 3555 3555 ASN ASN A . n 
A 1 3556 ALA 3556 3556 3556 ALA ALA A . n 
A 1 3557 ASP 3557 3557 3557 ASP ASP A . n 
A 1 3558 GLU 3558 3558 3558 GLU GLU A . n 
A 1 3559 ARG 3559 3559 3559 ARG ARG A . n 
A 1 3560 LEU 3560 3560 3560 LEU LEU A . n 
A 1 3561 ARG 3561 3561 3561 ARG ARG A . n 
A 1 3562 TRP 3562 3562 3562 TRP TRP A . n 
A 1 3563 GLN 3563 3563 3563 GLN GLN A . n 
A 1 3564 ALA 3564 3564 3564 ALA ALA A . n 
A 1 3565 SER 3565 3565 3565 SER SER A . n 
A 1 3566 SER 3566 3566 3566 SER SER A . n 
A 1 3567 LEU 3567 3567 3567 LEU LEU A . n 
A 1 3568 PRO 3568 3568 3568 PRO PRO A . n 
A 1 3569 ALA 3569 3569 3569 ALA ALA A . n 
A 1 3570 ASP 3570 3570 3570 ASP ASP A . n 
A 1 3571 ASP 3571 3571 3571 ASP ASP A . n 
A 1 3572 LEU 3572 3572 3572 LEU LEU A . n 
A 1 3573 CYS 3573 3573 3573 CYS CYS A . n 
A 1 3574 THR 3574 3574 3574 THR THR A . n 
A 1 3575 GLU 3575 3575 3575 GLU GLU A . n 
A 1 3576 ASN 3576 3576 3576 ASN ASN A . n 
A 1 3577 ALA 3577 3577 3577 ALA ALA A . n 
A 1 3578 ILE 3578 3578 3578 ILE ILE A . n 
A 1 3579 MET 3579 3579 3579 MET MET A . n 
A 1 3580 LEU 3580 3580 3580 LEU LEU A . n 
A 1 3581 LYS 3581 3581 3581 LYS LYS A . n 
A 1 3582 ARG 3582 3582 3582 ARG ARG A . n 
A 1 3583 PHE 3583 3583 3583 PHE PHE A . n 
A 1 3584 ASN 3584 3584 3584 ASN ASN A . n 
A 1 3585 ARG 3585 3585 3585 ARG ARG A . n 
A 1 3586 TYR 3586 3586 3586 TYR TYR A . n 
A 1 3587 PRO 3587 3587 3587 PRO PRO A . n 
A 1 3588 LEU 3588 3588 3588 LEU LEU A . n 
A 1 3589 ILE 3589 3589 3589 ILE ILE A . n 
A 1 3590 ILE 3590 3590 3590 ILE ILE A . n 
A 1 3591 ASP 3591 3591 3591 ASP ASP A . n 
A 1 3592 PRO 3592 3592 3592 PRO PRO A . n 
A 1 3593 SER 3593 3593 3593 SER SER A . n 
A 1 3594 GLY 3594 3594 3594 GLY GLY A . n 
A 1 3595 GLN 3595 3595 3595 GLN GLN A . n 
A 1 3596 ALA 3596 3596 3596 ALA ALA A . n 
A 1 3597 THR 3597 3597 3597 THR THR A . n 
A 1 3598 GLU 3598 3598 3598 GLU GLU A . n 
A 1 3599 PHE 3599 3599 3599 PHE PHE A . n 
A 1 3600 ILE 3600 3600 3600 ILE ILE A . n 
A 1 3601 MET 3601 3601 3601 MET MET A . n 
A 1 3602 ASN 3602 3602 3602 ASN ASN A . n 
A 1 3603 GLU 3603 3603 3603 GLU GLU A . n 
A 1 3604 TYR 3604 3604 3604 TYR TYR A . n 
A 1 3605 LYS 3605 3605 3605 LYS LYS A . n 
A 1 3606 ASP 3606 3606 3606 ASP ASP A . n 
A 1 3607 ARG 3607 3607 3607 ARG ARG A . n 
A 1 3608 LYS 3608 3608 3608 LYS LYS A . n 
A 1 3609 ILE 3609 3609 3609 ILE ILE A . n 
A 1 3610 THR 3610 3610 3610 THR THR A . n 
A 1 3611 ARG 3611 3611 3611 ARG ARG A . n 
A 1 3612 THR 3612 3612 3612 THR THR A . n 
A 1 3613 SER 3613 3613 3613 SER SER A . n 
A 1 3614 PHE 3614 3614 3614 PHE PHE A . n 
A 1 3615 LEU 3615 3615 3615 LEU LEU A . n 
A 1 3616 ASP 3616 3616 3616 ASP ASP A . n 
A 1 3617 ASP 3617 3617 3617 ASP ASP A . n 
A 1 3618 ALA 3618 3618 3618 ALA ALA A . n 
A 1 3619 PHE 3619 3619 3619 PHE PHE A . n 
A 1 3620 ARG 3620 3620 3620 ARG ARG A . n 
A 1 3621 LYS 3621 3621 3621 LYS LYS A . n 
A 1 3622 ASN 3622 3622 3622 ASN ASN A . n 
A 1 3623 LEU 3623 3623 3623 LEU LEU A . n 
A 1 3624 GLU 3624 3624 3624 GLU GLU A . n 
A 1 3625 SER 3625 3625 3625 SER SER A . n 
A 1 3626 ALA 3626 3626 3626 ALA ALA A . n 
A 1 3627 LEU 3627 3627 3627 LEU LEU A . n 
A 1 3628 ARG 3628 3628 3628 ARG ARG A . n 
A 1 3629 PHE 3629 3629 3629 PHE PHE A . n 
A 1 3630 GLY 3630 3630 3630 GLY GLY A . n 
A 1 3631 ASN 3631 3631 3631 ASN ASN A . n 
A 1 3632 PRO 3632 3632 3632 PRO PRO A . n 
A 1 3633 LEU 3633 3633 3633 LEU LEU A . n 
A 1 3634 LEU 3634 3634 3634 LEU LEU A . n 
A 1 3635 VAL 3635 3635 3635 VAL VAL A . n 
A 1 3636 GLN 3636 3636 3636 GLN GLN A . n 
A 1 3637 ASP 3637 3637 3637 ASP ASP A . n 
A 1 3638 VAL 3638 3638 3638 VAL VAL A . n 
A 1 3639 GLU 3639 3639 3639 GLU GLU A . n 
A 1 3640 SER 3640 3640 3640 SER SER A . n 
A 1 3641 TYR 3641 3641 3641 TYR TYR A . n 
A 1 3642 ASP 3642 3642 3642 ASP ASP A . n 
A 1 3643 PRO 3643 3643 3643 PRO PRO A . n 
A 1 3644 VAL 3644 3644 3644 VAL VAL A . n 
A 1 3645 LEU 3645 3645 3645 LEU LEU A . n 
A 1 3646 ASN 3646 3646 3646 ASN ASN A . n 
A 1 3647 PRO 3647 3647 3647 PRO PRO A . n 
A 1 3648 VAL 3648 3648 3648 VAL VAL A . n 
A 1 3649 LEU 3649 3649 3649 LEU LEU A . n 
A 1 3650 ASN 3650 3650 3650 ASN ASN A . n 
A 1 3651 ARG 3651 3651 3651 ARG ARG A . n 
A 1 3652 GLU 3652 3652 3652 GLU GLU A . n 
A 1 3653 VAL 3653 3653 3653 VAL VAL A . n 
A 1 3654 ARG 3654 3654 3654 ARG ARG A . n 
A 1 3655 ARG 3655 3655 3655 ARG ARG A . n 
A 1 3656 THR 3656 3656 3656 THR THR A . n 
A 1 3657 GLY 3657 3657 3657 GLY GLY A . n 
A 1 3658 GLY 3658 3658 3658 GLY GLY A . n 
A 1 3659 ARG 3659 3659 3659 ARG ARG A . n 
A 1 3660 VAL 3660 3660 3660 VAL VAL A . n 
A 1 3661 LEU 3661 3661 3661 LEU LEU A . n 
A 1 3662 ILE 3662 3662 3662 ILE ILE A . n 
A 1 3663 THR 3663 3663 3663 THR THR A . n 
A 1 3664 LEU 3664 3664 3664 LEU LEU A . n 
A 1 3665 GLY 3665 3665 3665 GLY GLY A . n 
A 1 3666 ASP 3666 3666 3666 ASP ASP A . n 
A 1 3667 GLN 3667 3667 3667 GLN GLN A . n 
A 1 3668 ASP 3668 3668 3668 ASP ASP A . n 
A 1 3669 ILE 3669 3669 3669 ILE ILE A . n 
A 1 3670 ASP 3670 3670 3670 ASP ASP A . n 
A 1 3671 LEU 3671 3671 3671 LEU LEU A . n 
A 1 3672 SER 3672 3672 3672 SER SER A . n 
A 1 3673 PRO 3673 3673 3673 PRO PRO A . n 
A 1 3674 SER 3674 3674 3674 SER SER A . n 
A 1 3675 PHE 3675 3675 3675 PHE PHE A . n 
A 1 3676 VAL 3676 3676 3676 VAL VAL A . n 
A 1 3677 ILE 3677 3677 3677 ILE ILE A . n 
A 1 3678 PHE 3678 3678 3678 PHE PHE A . n 
A 1 3679 LEU 3679 3679 3679 LEU LEU A . n 
A 1 3680 SER 3680 3680 3680 SER SER A . n 
A 1 3681 THR 3681 3681 3681 THR THR A . n 
A 1 3682 ARG 3682 3682 3682 ARG ARG A . n 
A 1 3683 ASP 3683 3683 3683 ASP ASP A . n 
A 1 3684 PRO 3684 3684 3684 PRO PRO A . n 
A 1 3685 THR 3685 3685 3685 THR THR A . n 
A 1 3686 VAL 3686 3686 3686 VAL VAL A . n 
A 1 3687 GLU 3687 3687 3687 GLU GLU A . n 
A 1 3688 PHE 3688 3688 3688 PHE PHE A . n 
A 1 3689 PRO 3689 3689 3689 PRO PRO A . n 
A 1 3690 PRO 3690 3690 3690 PRO PRO A . n 
A 1 3691 ASP 3691 3691 3691 ASP ASP A . n 
A 1 3692 LEU 3692 3692 3692 LEU LEU A . n 
A 1 3693 CYS 3693 3693 3693 CYS CYS A . n 
A 1 3694 SER 3694 3694 3694 SER SER A . n 
A 1 3695 ARG 3695 3695 3695 ARG ARG A . n 
A 1 3696 VAL 3696 3696 3696 VAL VAL A . n 
A 1 3697 THR 3697 3697 3697 THR THR A . n 
A 1 3698 PHE 3698 3698 3698 PHE PHE A . n 
A 1 3699 VAL 3699 3699 3699 VAL VAL A . n 
A 1 3700 ASN 3700 3700 3700 ASN ASN A . n 
A 1 3701 PHE 3701 3701 3701 PHE PHE A . n 
A 1 3702 THR 3702 3702 3702 THR THR A . n 
A 1 3703 VAL 3703 3703 3703 VAL VAL A . n 
A 1 3704 THR 3704 3704 3704 THR THR A . n 
A 1 3705 ARG 3705 3705 3705 ARG ARG A . n 
A 1 3706 SER 3706 3706 3706 SER SER A . n 
A 1 3707 SER 3707 3707 3707 SER SER A . n 
A 1 3708 LEU 3708 3708 3708 LEU LEU A . n 
A 1 3709 GLN 3709 3709 3709 GLN GLN A . n 
A 1 3710 SER 3710 3710 3710 SER SER A . n 
A 1 3711 GLN 3711 3711 3711 GLN GLN A . n 
A 1 3712 CYS 3712 3712 3712 CYS CYS A . n 
A 1 3713 LEU 3713 3713 3713 LEU LEU A . n 
A 1 3714 ASN 3714 3714 3714 ASN ASN A . n 
A 1 3715 GLU 3715 3715 3715 GLU GLU A . n 
A 1 3716 VAL 3716 3716 3716 VAL VAL A . n 
A 1 3717 LEU 3717 3717 3717 LEU LEU A . n 
A 1 3718 LYS 3718 3718 3718 LYS LYS A . n 
A 1 3719 ALA 3719 3719 3719 ALA ALA A . n 
A 1 3720 GLU 3720 3720 3720 GLU GLU A . n 
A 1 3721 ARG 3721 3721 3721 ARG ARG A . n 
A 1 3722 PRO 3722 3722 3722 PRO PRO A . n 
A 1 3723 ASP 3723 3723 3723 ASP ASP A . n 
A 1 3724 VAL 3724 3724 3724 VAL VAL A . n 
A 1 3725 ASP 3725 3725 3725 ASP ASP A . n 
A 1 3726 GLU 3726 3726 3726 GLU GLU A . n 
A 1 3727 LYS 3727 3727 3727 LYS LYS A . n 
A 1 3728 ARG 3728 3728 3728 ARG ARG A . n 
A 1 3729 SER 3729 3729 3729 SER SER A . n 
A 1 3730 ASP 3730 3730 3730 ASP ASP A . n 
A 1 3731 LEU 3731 3731 3731 LEU LEU A . n 
A 1 3732 LEU 3732 3732 3732 LEU LEU A . n 
A 1 3733 LYS 3733 3733 3733 LYS LYS A . n 
A 1 3734 LEU 3734 3734 3734 LEU LEU A . n 
A 1 3735 GLN 3735 3735 3735 GLN GLN A . n 
A 1 3736 GLY 3736 3736 3736 GLY GLY A . n 
A 1 3737 GLU 3737 3737 3737 GLU GLU A . n 
A 1 3738 PHE 3738 3738 3738 PHE PHE A . n 
A 1 3739 GLN 3739 3739 3739 GLN GLN A . n 
A 1 3740 LEU 3740 3740 3740 LEU LEU A . n 
A 1 3741 ARG 3741 3741 3741 ARG ARG A . n 
A 1 3742 LEU 3742 3742 3742 LEU LEU A . n 
A 1 3743 ARG 3743 3743 3743 ARG ARG A . n 
A 1 3744 GLN 3744 3744 3744 GLN GLN A . n 
A 1 3745 LEU 3745 3745 3745 LEU LEU A . n 
A 1 3746 GLU 3746 3746 3746 GLU GLU A . n 
A 1 3747 LYS 3747 3747 3747 LYS LYS A . n 
A 1 3748 SER 3748 3748 3748 SER SER A . n 
A 1 3749 LEU 3749 3749 3749 LEU LEU A . n 
A 1 3750 LEU 3750 3750 3750 LEU LEU A . n 
A 1 3751 GLN 3751 3751 3751 GLN GLN A . n 
A 1 3752 ALA 3752 3752 3752 ALA ALA A . n 
A 1 3753 LEU 3753 3753 3753 LEU LEU A . n 
A 1 3754 ASN 3754 3754 3754 ASN ASN A . n 
A 1 3755 GLU 3755 3755 3755 GLU GLU A . n 
A 1 3756 VAL 3756 3756 3756 VAL VAL A . n 
A 1 3757 LYS 3757 3757 3757 LYS LYS A . n 
A 1 3758 GLY 3758 3758 3758 GLY GLY A . n 
A 1 3759 ARG 3759 3759 3759 ARG ARG A . n 
A 1 3760 ILE 3760 3760 3760 ILE ILE A . n 
A 1 3761 LEU 3761 3761 3761 LEU LEU A . n 
A 1 3762 ASP 3762 3762 3762 ASP ASP A . n 
A 1 3763 ASP 3763 3763 3763 ASP ASP A . n 
A 1 3764 ASP 3764 3764 3764 ASP ASP A . n 
A 1 3765 THR 3765 3765 3765 THR THR A . n 
A 1 3766 ILE 3766 3766 3766 ILE ILE A . n 
A 1 3767 ILE 3767 3767 3767 ILE ILE A . n 
A 1 3768 THR 3768 3768 3768 THR THR A . n 
A 1 3769 THR 3769 3769 3769 THR THR A . n 
A 1 3770 LEU 3770 3770 3770 LEU LEU A . n 
A 1 3771 GLU 3771 3771 3771 GLU GLU A . n 
A 1 3772 ASN 3772 3772 3772 ASN ASN A . n 
A 1 3773 LEU 3773 3773 3773 LEU LEU A . n 
A 1 3774 LYS 3774 3774 3774 LYS LYS A . n 
A 1 3775 ARG 3775 3775 3775 ARG ARG A . n 
A 1 3776 GLU 3776 3776 3776 GLU GLU A . n 
A 1 3777 ALA 3777 3777 3777 ALA ALA A . n 
A 1 3778 ALA 3778 3778 3778 ALA ALA A . n 
A 1 3779 GLU 3779 3779 3779 GLU GLU A . n 
A 1 3780 VAL 3780 3780 3780 VAL VAL A . n 
A 1 3781 THR 3781 3781 3781 THR THR A . n 
A 1 3782 ARG 3782 3782 3782 ARG ARG A . n 
A 1 3783 LYS 3783 3783 3783 LYS LYS A . n 
A 1 3784 VAL 3784 3784 3784 VAL VAL A . n 
A 1 3785 GLU 3785 3785 3785 GLU GLU A . n 
A 1 3786 GLU 3786 3786 3786 GLU GLU A . n 
A 1 3787 THR 3787 3787 3787 THR THR A . n 
A 1 3788 ASP 3788 3788 3788 ASP ASP A . n 
A 1 3789 ILE 3789 3789 3789 ILE ILE A . n 
A 1 3790 VAL 3790 3790 3790 VAL VAL A . n 
A 1 3791 MET 3791 3791 3791 MET MET A . n 
A 1 3792 GLN 3792 3792 3792 GLN GLN A . n 
A 1 3793 GLU 3793 3793 3793 GLU GLU A . n 
A 1 3794 VAL 3794 3794 3794 VAL VAL A . n 
A 1 3795 GLU 3795 3795 3795 GLU GLU A . n 
A 1 3796 THR 3796 3796 3796 THR THR A . n 
A 1 3797 VAL 3797 3797 3797 VAL VAL A . n 
A 1 3798 SER 3798 3798 3798 SER SER A . n 
A 1 3799 GLN 3799 3799 3799 GLN GLN A . n 
A 1 3800 GLN 3800 3800 3800 GLN GLN A . n 
A 1 3801 TYR 3801 3801 3801 TYR TYR A . n 
A 1 3802 LEU 3802 3802 3802 LEU LEU A . n 
A 1 3803 PRO 3803 3803 3803 PRO PRO A . n 
A 1 3804 LEU 3804 3804 3804 LEU LEU A . n 
A 1 3805 SER 3805 3805 3805 SER SER A . n 
A 1 3806 THR 3806 3806 3806 THR THR A . n 
A 1 3807 ALA 3807 3807 3807 ALA ALA A . n 
A 1 3808 CYS 3808 3808 3808 CYS CYS A . n 
A 1 3809 SER 3809 3809 3809 SER SER A . n 
A 1 3810 SER 3810 3810 3810 SER SER A . n 
A 1 3811 ILE 3811 3811 3811 ILE ILE A . n 
A 1 3812 TYR 3812 3812 3812 TYR TYR A . n 
A 1 3813 PHE 3813 3813 3813 PHE PHE A . n 
A 1 3814 THR 3814 3814 3814 THR THR A . n 
A 1 3815 MET 3815 3815 3815 MET MET A . n 
A 1 3816 GLU 3816 3816 3816 GLU GLU A . n 
A 1 3817 SER 3817 3817 3817 SER SER A . n 
A 1 3818 LEU 3818 3818 3818 LEU LEU A . n 
A 1 3819 LYS 3819 3819 3819 LYS LYS A . n 
A 1 3820 GLN 3820 3820 3820 GLN GLN A . n 
A 1 3821 ILE 3821 3821 3821 ILE ILE A . n 
A 1 3822 HIS 3822 3822 3822 HIS HIS A . n 
A 1 3823 PHE 3823 3823 3823 PHE PHE A . n 
A 1 3824 LEU 3824 3824 3824 LEU LEU A . n 
A 1 3825 TYR 3825 3825 3825 TYR TYR A . n 
A 1 3826 GLN 3826 3826 3826 GLN GLN A . n 
A 1 3827 TYR 3827 3827 3827 TYR TYR A . n 
A 1 3828 SER 3828 3828 3828 SER SER A . n 
A 1 3829 LEU 3829 3829 3829 LEU LEU A . n 
A 1 3830 GLN 3830 3830 3830 GLN GLN A . n 
A 1 3831 PHE 3831 3831 3831 PHE PHE A . n 
A 1 3832 PHE 3832 3832 3832 PHE PHE A . n 
A 1 3833 LEU 3833 3833 3833 LEU LEU A . n 
A 1 3834 ASP 3834 3834 3834 ASP ASP A . n 
A 1 3835 ILE 3835 3835 3835 ILE ILE A . n 
A 1 3836 TYR 3836 3836 3836 TYR TYR A . n 
A 1 3837 HIS 3837 3837 3837 HIS HIS A . n 
A 1 3838 ASN 3838 3838 3838 ASN ASN A . n 
A 1 3839 VAL 3839 3839 3839 VAL VAL A . n 
A 1 3840 LEU 3840 3840 3840 LEU LEU A . n 
A 1 3841 TYR 3841 3841 3841 TYR TYR A . n 
A 1 3842 GLU 3842 3842 3842 GLU GLU A . n 
A 1 3843 ASN 3843 3843 3843 ASN ASN A . n 
A 1 3844 PRO 3844 3844 3844 PRO PRO A . n 
A 1 3845 ASN 3845 3845 3845 ASN ASN A . n 
A 1 3846 LEU 3846 3846 3846 LEU LEU A . n 
A 1 3847 LYS 3847 3847 3847 LYS LYS A . n 
A 1 3848 GLY 3848 3848 3848 GLY GLY A . n 
A 1 3849 VAL 3849 3849 3849 VAL VAL A . n 
A 1 3850 THR 3850 3850 3850 THR THR A . n 
A 1 3851 ASP 3851 3851 3851 ASP ASP A . n 
A 1 3852 HIS 3852 3852 3852 HIS HIS A . n 
A 1 3853 THR 3853 3853 3853 THR THR A . n 
A 1 3854 GLN 3854 3854 3854 GLN GLN A . n 
A 1 3855 ARG 3855 3855 3855 ARG ARG A . n 
A 1 3856 LEU 3856 3856 3856 LEU LEU A . n 
A 1 3857 SER 3857 3857 3857 SER SER A . n 
A 1 3858 ILE 3858 3858 3858 ILE ILE A . n 
A 1 3859 ILE 3859 3859 3859 ILE ILE A . n 
A 1 3860 THR 3860 3860 3860 THR THR A . n 
A 1 3861 LYS 3861 3861 3861 LYS LYS A . n 
A 1 3862 ASP 3862 3862 3862 ASP ASP A . n 
A 1 3863 LEU 3863 3863 3863 LEU LEU A . n 
A 1 3864 PHE 3864 3864 3864 PHE PHE A . n 
A 1 3865 GLN 3865 3865 3865 GLN GLN A . n 
A 1 3866 VAL 3866 3866 3866 VAL VAL A . n 
A 1 3867 ALA 3867 3867 3867 ALA ALA A . n 
A 1 3868 PHE 3868 3868 3868 PHE PHE A . n 
A 1 3869 ASN 3869 3869 3869 ASN ASN A . n 
A 1 3870 ARG 3870 3870 3870 ARG ARG A . n 
A 1 3871 VAL 3871 3871 3871 VAL VAL A . n 
A 1 3872 ALA 3872 3872 3872 ALA ALA A . n 
A 1 3873 ARG 3873 3873 3873 ARG ARG A . n 
A 1 3874 GLY 3874 3874 3874 GLY GLY A . n 
A 1 3875 MET 3875 3875 3875 MET MET A . n 
A 1 3876 LEU 3876 3876 3876 LEU LEU A . n 
A 1 3877 HIS 3877 3877 3877 HIS HIS A . n 
A 1 3878 GLN 3878 3878 3878 GLN GLN A . n 
A 1 3879 ASP 3879 3879 3879 ASP ASP A . n 
A 1 3880 HIS 3880 3880 3880 HIS HIS A . n 
A 1 3881 ILE 3881 3881 3881 ILE ILE A . n 
A 1 3882 THR 3882 3882 3882 THR THR A . n 
A 1 3883 PHE 3883 3883 3883 PHE PHE A . n 
A 1 3884 ALA 3884 3884 3884 ALA ALA A . n 
A 1 3885 MET 3885 3885 3885 MET MET A . n 
A 1 3886 LEU 3886 3886 3886 LEU LEU A . n 
A 1 3887 LEU 3887 3887 3887 LEU LEU A . n 
A 1 3888 ALA 3888 3888 3888 ALA ALA A . n 
A 1 3889 ARG 3889 3889 3889 ARG ARG A . n 
A 1 3890 ILE 3890 3890 3890 ILE ILE A . n 
A 1 3891 LYS 3891 3891 3891 LYS LYS A . n 
A 1 3892 LEU 3892 3892 3892 LEU LEU A . n 
A 1 3893 LYS 3893 3893 3893 LYS LYS A . n 
A 1 3894 GLY 3894 3894 3894 GLY GLY A . n 
A 1 3895 THR 3895 3895 3895 THR THR A . n 
A 1 3896 VAL 3896 3896 3896 VAL VAL A . n 
A 1 3897 GLY 3897 3897 3897 GLY GLY A . n 
A 1 3898 GLU 3898 3898 3898 GLU GLU A . n 
A 1 3899 PRO 3899 3899 3899 PRO PRO A . n 
A 1 3900 THR 3900 3900 3900 THR THR A . n 
A 1 3901 TYR 3901 3901 3901 TYR TYR A . n 
A 1 3902 ASP 3902 3902 3902 ASP ASP A . n 
A 1 3903 ALA 3903 3903 3903 ALA ALA A . n 
A 1 3904 GLU 3904 3904 3904 GLU GLU A . n 
A 1 3905 PHE 3905 3905 3905 PHE PHE A . n 
A 1 3906 GLN 3906 3906 3906 GLN GLN A . n 
A 1 3907 HIS 3907 3907 3907 HIS HIS A . n 
A 1 3908 PHE 3908 3908 3908 PHE PHE A . n 
A 1 3909 LEU 3909 3909 3909 LEU LEU A . n 
A 1 3910 ARG 3910 3910 3910 ARG ARG A . n 
A 1 3911 GLY 3911 3911 3911 GLY GLY A . n 
A 1 3912 ASN 3912 3912 3912 ASN ASN A . n 
A 1 3913 GLU 3913 3913 3913 GLU GLU A . n 
A 1 3914 ILE 3914 3914 3914 ILE ILE A . n 
A 1 3915 VAL 3915 3915 3915 VAL VAL A . n 
A 1 3916 LEU 3916 3916 3916 LEU LEU A . n 
A 1 3917 SER 3917 3917 3917 SER SER A . n 
A 1 3918 ALA 3918 3918 3918 ALA ALA A . n 
A 1 3919 GLY 3919 3919 3919 GLY GLY A . n 
A 1 3920 SER 3920 3920 3920 SER SER A . n 
A 1 3921 THR 3921 3921 3921 THR THR A . n 
A 1 3922 PRO 3922 3922 3922 PRO PRO A . n 
A 1 3923 ARG 3923 3923 3923 ARG ARG A . n 
A 1 3924 ILE 3924 3924 3924 ILE ILE A . n 
A 1 3925 GLN 3925 3925 3925 GLN GLN A . n 
A 1 3926 GLY 3926 3926 3926 GLY GLY A . n 
A 1 3927 LEU 3927 3927 3927 LEU LEU A . n 
A 1 3928 THR 3928 3928 3928 THR THR A . n 
A 1 3929 VAL 3929 3929 3929 VAL VAL A . n 
A 1 3930 GLU 3930 3930 3930 GLU GLU A . n 
A 1 3931 GLN 3931 3931 3931 GLN GLN A . n 
A 1 3932 ALA 3932 3932 3932 ALA ALA A . n 
A 1 3933 GLU 3933 3933 3933 GLU GLU A . n 
A 1 3934 ALA 3934 3934 3934 ALA ALA A . n 
A 1 3935 VAL 3935 3935 3935 VAL VAL A . n 
A 1 3936 VAL 3936 3936 3936 VAL VAL A . n 
A 1 3937 ARG 3937 3937 3937 ARG ARG A . n 
A 1 3938 LEU 3938 3938 3938 LEU LEU A . n 
A 1 3939 SER 3939 3939 3939 SER SER A . n 
A 1 3940 CYS 3940 3940 3940 CYS CYS A . n 
A 1 3941 LEU 3941 3941 3941 LEU LEU A . n 
A 1 3942 PRO 3942 3942 3942 PRO PRO A . n 
A 1 3943 ALA 3943 3943 3943 ALA ALA A . n 
A 1 3944 PHE 3944 3944 3944 PHE PHE A . n 
A 1 3945 LYS 3945 3945 3945 LYS LYS A . n 
A 1 3946 ASP 3946 3946 3946 ASP ASP A . n 
A 1 3947 LEU 3947 3947 3947 LEU LEU A . n 
A 1 3948 ILE 3948 3948 3948 ILE ILE A . n 
A 1 3949 ALA 3949 3949 3949 ALA ALA A . n 
A 1 3950 LYS 3950 3950 3950 LYS LYS A . n 
A 1 3951 VAL 3951 3951 3951 VAL VAL A . n 
A 1 3952 GLN 3952 3952 3952 GLN GLN A . n 
A 1 3953 ALA 3953 3953 3953 ALA ALA A . n 
A 1 3954 ASP 3954 3954 3954 ASP ASP A . n 
A 1 3955 GLU 3955 3955 3955 GLU GLU A . n 
A 1 3956 GLN 3956 3956 3956 GLN GLN A . n 
A 1 3957 PHE 3957 3957 3957 PHE PHE A . n 
A 1 3958 GLY 3958 3958 3958 GLY GLY A . n 
A 1 3959 ILE 3959 3959 3959 ILE ILE A . n 
A 1 3960 TRP 3960 3960 3960 TRP TRP A . n 
A 1 3961 LEU 3961 3961 3961 LEU LEU A . n 
A 1 3962 ASP 3962 3962 3962 ASP ASP A . n 
A 1 3963 SER 3963 3963 3963 SER SER A . n 
A 1 3964 SER 3964 3964 3964 SER SER A . n 
A 1 3965 SER 3965 3965 3965 SER SER A . n 
A 1 3966 PRO 3966 3966 3966 PRO PRO A . n 
A 1 3967 GLU 3967 3967 3967 GLU GLU A . n 
A 1 3968 GLN 3968 3968 3968 GLN GLN A . n 
A 1 3969 THR 3969 3969 3969 THR THR A . n 
A 1 3970 VAL 3970 3970 3970 VAL VAL A . n 
A 1 3971 PRO 3971 3971 3971 PRO PRO A . n 
A 1 3972 TYR 3972 3972 3972 TYR TYR A . n 
A 1 3973 LEU 3973 3973 3973 LEU LEU A . n 
A 1 3974 TRP 3974 3974 3974 TRP TRP A . n 
A 1 3975 SER 3975 3975 3975 SER SER A . n 
A 1 3976 GLU 3976 3976 3976 GLU GLU A . n 
A 1 3977 GLU 3977 3977 3977 GLU GLU A . n 
A 1 3978 THR 3978 3978 3978 THR THR A . n 
A 1 3979 PRO 3979 3979 3979 PRO PRO A . n 
A 1 3980 ALA 3980 3980 3980 ALA ALA A . n 
A 1 3981 THR 3981 3981 3981 THR THR A . n 
A 1 3982 PRO 3982 3982 3982 PRO PRO A . n 
A 1 3983 ILE 3983 3983 3983 ILE ILE A . n 
A 1 3984 GLY 3984 3984 3984 GLY GLY A . n 
A 1 3985 GLN 3985 3985 3985 GLN GLN A . n 
A 1 3986 ALA 3986 3986 3986 ALA ALA A . n 
A 1 3987 ILE 3987 3987 3987 ILE ILE A . n 
A 1 3988 HIS 3988 3988 3988 HIS HIS A . n 
A 1 3989 ARG 3989 3989 3989 ARG ARG A . n 
A 1 3990 LEU 3990 3990 3990 LEU LEU A . n 
A 1 3991 LEU 3991 3991 3991 LEU LEU A . n 
A 1 3992 LEU 3992 3992 3992 LEU LEU A . n 
A 1 3993 ILE 3993 3993 3993 ILE ILE A . n 
A 1 3994 GLN 3994 3994 3994 GLN GLN A . n 
A 1 3995 ALA 3995 3995 3995 ALA ALA A . n 
A 1 3996 PHE 3996 3996 3996 PHE PHE A . n 
A 1 3997 ARG 3997 3997 3997 ARG ARG A . n 
A 1 3998 PRO 3998 3998 3998 PRO PRO A . n 
A 1 3999 ASP 3999 3999 3999 ASP ASP A . n 
A 1 4000 ARG 4000 4000 4000 ARG ARG A . n 
A 1 4001 LEU 4001 4001 4001 LEU LEU A . n 
A 1 4002 LEU 4002 4002 4002 LEU LEU A . n 
A 1 4003 ALA 4003 4003 4003 ALA ALA A . n 
A 1 4004 MET 4004 4004 4004 MET MET A . n 
A 1 4005 ALA 4005 4005 4005 ALA ALA A . n 
A 1 4006 HIS 4006 4006 4006 HIS HIS A . n 
A 1 4007 MET 4007 4007 4007 MET MET A . n 
A 1 4008 PHE 4008 4008 4008 PHE PHE A . n 
A 1 4009 VAL 4009 4009 4009 VAL VAL A . n 
A 1 4010 SER 4010 4010 4010 SER SER A . n 
A 1 4011 THR 4011 4011 4011 THR THR A . n 
A 1 4012 ASN 4012 4012 4012 ASN ASN A . n 
A 1 4013 LEU 4013 4013 4013 LEU LEU A . n 
A 1 4014 GLY 4014 4014 4014 GLY GLY A . n 
A 1 4015 GLU 4015 4015 4015 GLU GLU A . n 
A 1 4016 SER 4016 4016 4016 SER SER A . n 
A 1 4017 PHE 4017 4017 4017 PHE PHE A . n 
A 1 4018 MET 4018 4018 4018 MET MET A . n 
A 1 4019 SER 4019 4019 4019 SER SER A . n 
A 1 4020 ILE 4020 4020 4020 ILE ILE A . n 
A 1 4021 MET 4021 4021 4021 MET MET A . n 
A 1 4022 GLU 4022 4022 4022 GLU GLU A . n 
A 1 4023 GLN 4023 4023 4023 GLN GLN A . n 
A 1 4024 PRO 4024 4024 4024 PRO PRO A . n 
A 1 4025 LEU 4025 4025 4025 LEU LEU A . n 
A 1 4026 ASP 4026 4026 4026 ASP ASP A . n 
A 1 4027 LEU 4027 4027 4027 LEU LEU A . n 
A 1 4028 THR 4028 4028 4028 THR THR A . n 
A 1 4029 HIS 4029 4029 4029 HIS HIS A . n 
A 1 4030 ILE 4030 4030 4030 ILE ILE A . n 
A 1 4031 VAL 4031 4031 4031 VAL VAL A . n 
A 1 4032 GLY 4032 4032 4032 GLY GLY A . n 
A 1 4033 THR 4033 4033 4033 THR THR A . n 
A 1 4034 GLU 4034 4034 4034 GLU GLU A . n 
A 1 4035 VAL 4035 4035 4035 VAL VAL A . n 
A 1 4036 LYS 4036 4036 4036 LYS LYS A . n 
A 1 4037 PRO 4037 4037 4037 PRO PRO A . n 
A 1 4038 ASN 4038 4038 4038 ASN ASN A . n 
A 1 4039 THR 4039 4039 4039 THR THR A . n 
A 1 4040 PRO 4040 4040 4040 PRO PRO A . n 
A 1 4041 VAL 4041 4041 4041 VAL VAL A . n 
A 1 4042 LEU 4042 4042 4042 LEU LEU A . n 
A 1 4043 MET 4043 4043 4043 MET MET A . n 
A 1 4044 CYS 4044 4044 4044 CYS CYS A . n 
A 1 4045 SER 4045 4045 4045 SER SER A . n 
A 1 4046 VAL 4046 4046 4046 VAL VAL A . n 
A 1 4047 PRO 4047 4047 4047 PRO PRO A . n 
A 1 4048 GLY 4048 4048 4048 GLY GLY A . n 
A 1 4049 TYR 4049 4049 4049 TYR TYR A . n 
A 1 4050 ASP 4050 4050 4050 ASP ASP A . n 
A 1 4051 ALA 4051 4051 4051 ALA ALA A . n 
A 1 4052 SER 4052 4052 4052 SER SER A . n 
A 1 4053 GLY 4053 4053 4053 GLY GLY A . n 
A 1 4054 HIS 4054 4054 4054 HIS HIS A . n 
A 1 4055 VAL 4055 4055 4055 VAL VAL A . n 
A 1 4056 GLU 4056 4056 4056 GLU GLU A . n 
A 1 4057 ASP 4057 4057 4057 ASP ASP A . n 
A 1 4058 LEU 4058 4058 4058 LEU LEU A . n 
A 1 4059 ALA 4059 4059 4059 ALA ALA A . n 
A 1 4060 ALA 4060 4060 4060 ALA ALA A . n 
A 1 4061 GLU 4061 4061 4061 GLU GLU A . n 
A 1 4062 GLN 4062 4062 4062 GLN GLN A . n 
A 1 4063 ASN 4063 4063 4063 ASN ASN A . n 
A 1 4064 THR 4064 4064 4064 THR THR A . n 
A 1 4065 GLN 4065 4065 4065 GLN GLN A . n 
A 1 4066 ILE 4066 4066 4066 ILE ILE A . n 
A 1 4067 THR 4067 4067 4067 THR THR A . n 
A 1 4068 SER 4068 4068 4068 SER SER A . n 
A 1 4069 ILE 4069 4069 4069 ILE ILE A . n 
A 1 4070 ALA 4070 4070 4070 ALA ALA A . n 
A 1 4071 ILE 4071 4071 4071 ILE ILE A . n 
A 1 4072 GLY 4072 4072 4072 GLY GLY A . n 
A 1 4073 SER 4073 4073 4073 SER SER A . n 
A 1 4074 ALA 4074 4074 4074 ALA ALA A . n 
A 1 4075 GLU 4075 4075 4075 GLU GLU A . n 
A 1 4076 GLY 4076 4076 4076 GLY GLY A . n 
A 1 4077 PHE 4077 4077 4077 PHE PHE A . n 
A 1 4078 ASN 4078 4078 4078 ASN ASN A . n 
A 1 4079 GLN 4079 4079 4079 GLN GLN A . n 
A 1 4080 ALA 4080 4080 4080 ALA ALA A . n 
A 1 4081 ASP 4081 4081 4081 ASP ASP A . n 
A 1 4082 LYS 4082 4082 4082 LYS LYS A . n 
A 1 4083 ALA 4083 4083 4083 ALA ALA A . n 
A 1 4084 ILE 4084 4084 4084 ILE ILE A . n 
A 1 4085 ASN 4085 4085 4085 ASN ASN A . n 
A 1 4086 THR 4086 4086 4086 THR THR A . n 
A 1 4087 ALA 4087 4087 4087 ALA ALA A . n 
A 1 4088 VAL 4088 4088 4088 VAL VAL A . n 
A 1 4089 LYS 4089 4089 4089 LYS LYS A . n 
A 1 4090 SER 4090 4090 4090 SER SER A . n 
A 1 4091 GLY 4091 4091 4091 GLY GLY A . n 
A 1 4092 ARG 4092 4092 4092 ARG ARG A . n 
A 1 4093 TRP 4093 4093 4093 TRP TRP A . n 
A 1 4094 VAL 4094 4094 4094 VAL VAL A . n 
A 1 4095 MET 4095 4095 4095 MET MET A . n 
A 1 4096 LEU 4096 4096 4096 LEU LEU A . n 
A 1 4097 LYS 4097 4097 4097 LYS LYS A . n 
A 1 4098 ASN 4098 4098 4098 ASN ASN A . n 
A 1 4099 VAL 4099 4099 4099 VAL VAL A . n 
A 1 4100 HIS 4100 4100 4100 HIS HIS A . n 
A 1 4101 LEU 4101 4101 4101 LEU LEU A . n 
A 1 4102 ALA 4102 4102 4102 ALA ALA A . n 
A 1 4103 PRO 4103 4103 4103 PRO PRO A . n 
A 1 4104 GLY 4104 4104 4104 GLY GLY A . n 
A 1 4105 TRP 4105 4105 4105 TRP TRP A . n 
A 1 4106 LEU 4106 4106 4106 LEU LEU A . n 
A 1 4107 MET 4107 4107 4107 MET MET A . n 
A 1 4108 GLN 4108 4108 4108 GLN GLN A . n 
A 1 4109 LEU 4109 4109 4109 LEU LEU A . n 
A 1 4110 GLU 4110 4110 4110 GLU GLU A . n 
A 1 4111 LYS 4111 4111 4111 LYS LYS A . n 
A 1 4112 LYS 4112 4112 4112 LYS LYS A . n 
A 1 4113 LEU 4113 4113 4113 LEU LEU A . n 
A 1 4114 HIS 4114 4114 4114 HIS HIS A . n 
A 1 4115 SER 4115 4115 4115 SER SER A . n 
A 1 4116 LEU 4116 4116 4116 LEU LEU A . n 
A 1 4117 GLN 4117 4117 4117 GLN GLN A . n 
A 1 4118 PRO 4118 4118 4118 PRO PRO A . n 
A 1 4119 HIS 4119 4119 4119 HIS HIS A . n 
A 1 4120 ALA 4120 4120 4120 ALA ALA A . n 
A 1 4121 CYS 4121 4121 4121 CYS CYS A . n 
A 1 4122 PHE 4122 4122 4122 PHE PHE A . n 
A 1 4123 ARG 4123 4123 4123 ARG ARG A . n 
A 1 4124 LEU 4124 4124 4124 LEU LEU A . n 
A 1 4125 PHE 4125 4125 4125 PHE PHE A . n 
A 1 4126 LEU 4126 4126 4126 LEU LEU A . n 
A 1 4127 THR 4127 4127 4127 THR THR A . n 
A 1 4128 MET 4128 4128 4128 MET MET A . n 
A 1 4129 GLU 4129 4129 4129 GLU GLU A . n 
A 1 4130 ILE 4130 4130 4130 ILE ILE A . n 
A 1 4131 ASN 4131 4131 4131 ASN ASN A . n 
A 1 4132 PRO 4132 4132 4132 PRO PRO A . n 
A 1 4133 LYS 4133 4133 4133 LYS LYS A . n 
A 1 4134 VAL 4134 4134 4134 VAL VAL A . n 
A 1 4135 PRO 4135 4135 4135 PRO PRO A . n 
A 1 4136 VAL 4136 4136 4136 VAL VAL A . n 
A 1 4137 ASN 4137 4137 4137 ASN ASN A . n 
A 1 4138 LEU 4138 4138 4138 LEU LEU A . n 
A 1 4139 LEU 4139 4139 4139 LEU LEU A . n 
A 1 4140 ARG 4140 4140 4140 ARG ARG A . n 
A 1 4141 ALA 4141 4141 4141 ALA ALA A . n 
A 1 4142 GLY 4142 4142 4142 GLY GLY A . n 
A 1 4143 ARG 4143 4143 4143 ARG ARG A . n 
A 1 4144 ILE 4144 4144 4144 ILE ILE A . n 
A 1 4145 PHE 4145 4145 4145 PHE PHE A . n 
A 1 4146 VAL 4146 4146 4146 VAL VAL A . n 
A 1 4147 PHE 4147 4147 4147 PHE PHE A . n 
A 1 4148 GLU 4148 4148 4148 GLU GLU A . n 
A 1 4149 PRO 4149 4149 4149 PRO PRO A . n 
A 1 4150 PRO 4150 4150 4150 PRO PRO A . n 
A 1 4151 PRO 4151 4151 4151 PRO PRO A . n 
A 1 4152 GLY 4152 4152 4152 GLY GLY A . n 
A 1 4153 VAL 4153 4153 4153 VAL VAL A . n 
A 1 4154 LYS 4154 4154 4154 LYS LYS A . n 
A 1 4155 ALA 4155 4155 4155 ALA ALA A . n 
A 1 4156 ASN 4156 4156 4156 ASN ASN A . n 
A 1 4157 MET 4157 4157 4157 MET MET A . n 
A 1 4158 LEU 4158 4158 4158 LEU LEU A . n 
A 1 4159 ARG 4159 4159 4159 ARG ARG A . n 
A 1 4160 THR 4160 4160 4160 THR THR A . n 
A 1 4161 PHE 4161 4161 4161 PHE PHE A . n 
A 1 4162 SER 4162 4162 4162 SER SER A . n 
A 1 4163 SER 4163 4163 4163 SER SER A . n 
A 1 4164 ILE 4164 4164 4164 ILE ILE A . n 
A 1 4165 PRO 4165 4165 4165 PRO PRO A . n 
A 1 4166 VAL 4166 4166 4166 VAL VAL A . n 
A 1 4167 SER 4167 4167 4167 SER SER A . n 
A 1 4168 ARG 4168 4168 4168 ARG ARG A . n 
A 1 4169 ILE 4169 4169 4169 ILE ILE A . n 
A 1 4170 CYS 4170 4170 4170 CYS CYS A . n 
A 1 4171 LYS 4171 4171 4171 LYS LYS A . n 
A 1 4172 SER 4172 4172 4172 SER SER A . n 
A 1 4173 PRO 4173 4173 4173 PRO PRO A . n 
A 1 4174 ASN 4174 4174 4174 ASN ASN A . n 
A 1 4175 GLU 4175 4175 4175 GLU GLU A . n 
A 1 4176 ARG 4176 4176 4176 ARG ARG A . n 
A 1 4177 ALA 4177 4177 4177 ALA ALA A . n 
A 1 4178 ARG 4178 4178 4178 ARG ARG A . n 
A 1 4179 LEU 4179 4179 4179 LEU LEU A . n 
A 1 4180 TYR 4180 4180 4180 TYR TYR A . n 
A 1 4181 PHE 4181 4181 4181 PHE PHE A . n 
A 1 4182 LEU 4182 4182 4182 LEU LEU A . n 
A 1 4183 LEU 4183 4183 4183 LEU LEU A . n 
A 1 4184 ALA 4184 4184 4184 ALA ALA A . n 
A 1 4185 TRP 4185 4185 4185 TRP TRP A . n 
A 1 4186 PHE 4186 4186 4186 PHE PHE A . n 
A 1 4187 HIS 4187 4187 4187 HIS HIS A . n 
A 1 4188 ALA 4188 4188 4188 ALA ALA A . n 
A 1 4189 ILE 4189 4189 4189 ILE ILE A . n 
A 1 4190 ILE 4190 4190 4190 ILE ILE A . n 
A 1 4191 GLN 4191 4191 4191 GLN GLN A . n 
A 1 4192 GLU 4192 4192 4192 GLU GLU A . n 
A 1 4193 ARG 4193 4193 4193 ARG ARG A . n 
A 1 4194 LEU 4194 4194 4194 LEU LEU A . n 
A 1 4195 ARG 4195 4195 4195 ARG ARG A . n 
A 1 4196 TYR 4196 4196 4196 TYR TYR A . n 
A 1 4197 ALA 4197 4197 4197 ALA ALA A . n 
A 1 4198 PRO 4198 4198 4198 PRO PRO A . n 
A 1 4199 LEU 4199 4199 4199 LEU LEU A . n 
A 1 4200 GLY 4200 4200 4200 GLY GLY A . n 
A 1 4201 TRP 4201 4201 4201 TRP TRP A . n 
A 1 4202 SER 4202 4202 4202 SER SER A . n 
A 1 4203 LYS 4203 4203 4203 LYS LYS A . n 
A 1 4204 LYS 4204 4204 4204 LYS LYS A . n 
A 1 4205 TYR 4205 4205 4205 TYR TYR A . n 
A 1 4206 GLU 4206 4206 4206 GLU GLU A . n 
A 1 4207 PHE 4207 4207 4207 PHE PHE A . n 
A 1 4208 GLY 4208 4208 4208 GLY GLY A . n 
A 1 4209 GLU 4209 4209 4209 GLU GLU A . n 
A 1 4210 SER 4210 4210 4210 SER SER A . n 
A 1 4211 ASP 4211 4211 4211 ASP ASP A . n 
A 1 4212 LEU 4212 4212 4212 LEU LEU A . n 
A 1 4213 ARG 4213 4213 4213 ARG ARG A . n 
A 1 4214 SER 4214 4214 4214 SER SER A . n 
A 1 4215 ALA 4215 4215 4215 ALA ALA A . n 
A 1 4216 CYS 4216 4216 4216 CYS CYS A . n 
A 1 4217 ASP 4217 4217 4217 ASP ASP A . n 
A 1 4218 THR 4218 4218 4218 THR THR A . n 
A 1 4219 VAL 4219 4219 4219 VAL VAL A . n 
A 1 4220 ASP 4220 4220 4220 ASP ASP A . n 
A 1 4221 THR 4221 4221 4221 THR THR A . n 
A 1 4222 TRP 4222 4222 4222 TRP TRP A . n 
A 1 4223 LEU 4223 4223 4223 LEU LEU A . n 
A 1 4224 ASP 4224 4224 4224 ASP ASP A . n 
A 1 4225 ASP 4225 4225 4225 ASP ASP A . n 
A 1 4226 THR 4226 4226 4226 THR THR A . n 
A 1 4227 ALA 4227 4227 4227 ALA ALA A . n 
A 1 4228 LYS 4228 4228 4228 LYS LYS A . n 
A 1 4229 GLY 4229 4229 4229 GLY GLY A . n 
A 1 4230 ARG 4230 4230 4230 ARG ARG A . n 
A 1 4231 GLN 4231 4231 4231 GLN GLN A . n 
A 1 4232 ASN 4232 4232 4232 ASN ASN A . n 
A 1 4233 ILE 4233 4233 4233 ILE ILE A . n 
A 1 4234 SER 4234 4234 4234 SER SER A . n 
A 1 4235 PRO 4235 4235 4235 PRO PRO A . n 
A 1 4236 ASP 4236 4236 4236 ASP ASP A . n 
A 1 4237 LYS 4237 4237 4237 LYS LYS A . n 
A 1 4238 ILE 4238 4238 4238 ILE ILE A . n 
A 1 4239 PRO 4239 4239 4239 PRO PRO A . n 
A 1 4240 TRP 4240 4240 4240 TRP TRP A . n 
A 1 4241 SER 4241 4241 4241 SER SER A . n 
A 1 4242 ALA 4242 4242 4242 ALA ALA A . n 
A 1 4243 LEU 4243 4243 4243 LEU LEU A . n 
A 1 4244 LYS 4244 4244 4244 LYS LYS A . n 
A 1 4245 THR 4245 4245 4245 THR THR A . n 
A 1 4246 LEU 4246 4246 4246 LEU LEU A . n 
A 1 4247 MET 4247 4247 4247 MET MET A . n 
A 1 4248 ALA 4248 4248 4248 ALA ALA A . n 
A 1 4249 GLN 4249 4249 4249 GLN GLN A . n 
A 1 4250 SER 4250 4250 4250 SER SER A . n 
A 1 4251 ILE 4251 4251 4251 ILE ILE A . n 
A 1 4252 TYR 4252 4252 4252 TYR TYR A . n 
A 1 4253 GLY 4253 4253 4253 GLY GLY A . n 
A 1 4254 GLY 4254 4254 4254 GLY GLY A . n 
A 1 4255 ARG 4255 4255 4255 ARG ARG A . n 
A 1 4256 VAL 4256 4256 4256 VAL VAL A . n 
A 1 4257 ASP 4257 4257 4257 ASP ASP A . n 
A 1 4258 ASN 4258 4258 4258 ASN ASN A . n 
A 1 4259 GLU 4259 4259 4259 GLU GLU A . n 
A 1 4260 PHE 4260 4260 4260 PHE PHE A . n 
A 1 4261 ASP 4261 4261 4261 ASP ASP A . n 
A 1 4262 GLN 4262 4262 4262 GLN GLN A . n 
A 1 4263 ARG 4263 4263 4263 ARG ARG A . n 
A 1 4264 LEU 4264 4264 4264 LEU LEU A . n 
A 1 4265 LEU 4265 4265 4265 LEU LEU A . n 
A 1 4266 ASN 4266 4266 4266 ASN ASN A . n 
A 1 4267 THR 4267 4267 4267 THR THR A . n 
A 1 4268 PHE 4268 4268 4268 PHE PHE A . n 
A 1 4269 LEU 4269 4269 4269 LEU LEU A . n 
A 1 4270 GLU 4270 4270 4270 GLU GLU A . n 
A 1 4271 ARG 4271 4271 4271 ARG ARG A . n 
A 1 4272 LEU 4272 4272 4272 LEU LEU A . n 
A 1 4273 PHE 4273 4273 4273 PHE PHE A . n 
A 1 4274 THR 4274 4274 4274 THR THR A . n 
A 1 4275 THR 4275 4275 4275 THR THR A . n 
A 1 4276 ARG 4276 4276 4276 ARG ARG A . n 
A 1 4277 SER 4277 4277 4277 SER SER A . n 
A 1 4278 PHE 4278 4278 4278 PHE PHE A . n 
A 1 4279 ASP 4279 4279 4279 ASP ASP A . n 
A 1 4280 SER 4280 4280 4280 SER SER A . n 
A 1 4281 GLU 4281 4281 4281 GLU GLU A . n 
A 1 4282 PHE 4282 4282 4282 PHE PHE A . n 
A 1 4283 LYS 4283 4283 4283 LYS LYS A . n 
A 1 4284 LEU 4284 4284 4284 LEU LEU A . n 
A 1 4285 ALA 4285 4285 4285 ALA ALA A . n 
A 1 4286 CYS 4286 4286 4286 CYS CYS A . n 
A 1 4287 LYS 4287 4287 4287 LYS LYS A . n 
A 1 4288 VAL 4288 4288 4288 VAL VAL A . n 
A 1 4289 ASP 4289 4289 4289 ASP ALA A . n 
A 1 4290 GLY 4290 4290 4290 GLY GLY A . n 
A 1 4291 HIS 4291 4291 4291 HIS HIS A . n 
A 1 4292 LYS 4292 4292 4292 LYS LYS A . n 
A 1 4293 ASP 4293 4293 4293 ASP ASP A . n 
A 1 4294 ILE 4294 4294 4294 ILE ILE A . n 
A 1 4295 GLN 4295 4295 4295 GLN GLN A . n 
A 1 4296 MET 4296 4296 4296 MET MET A . n 
A 1 4297 PRO 4297 4297 4297 PRO PRO A . n 
A 1 4298 ASP 4298 4298 4298 ASP ASP A . n 
A 1 4299 GLY 4299 4299 4299 GLY GLY A . n 
A 1 4300 ILE 4300 4300 4300 ILE ILE A . n 
A 1 4301 ARG 4301 4301 4301 ARG ARG A . n 
A 1 4302 ARG 4302 4302 4302 ARG ARG A . n 
A 1 4303 GLU 4303 4303 4303 GLU GLU A . n 
A 1 4304 GLU 4304 4304 4304 GLU GLU A . n 
A 1 4305 PHE 4305 4305 4305 PHE PHE A . n 
A 1 4306 VAL 4306 4306 4306 VAL VAL A . n 
A 1 4307 GLN 4307 4307 4307 GLN GLN A . n 
A 1 4308 TRP 4308 4308 4308 TRP TRP A . n 
A 1 4309 VAL 4309 4309 4309 VAL VAL A . n 
A 1 4310 GLU 4310 4310 4310 GLU GLU A . n 
A 1 4311 LEU 4311 4311 4311 LEU LEU A . n 
A 1 4312 LEU 4312 4312 4312 LEU LEU A . n 
A 1 4313 PRO 4313 4313 4313 PRO PRO A . n 
A 1 4314 ASP 4314 4314 4314 ASP ASP A . n 
A 1 4315 THR 4315 4315 4315 THR THR A . n 
A 1 4316 GLN 4316 4316 4316 GLN GLN A . n 
A 1 4317 THR 4317 4317 4317 THR THR A . n 
A 1 4318 PRO 4318 4318 4318 PRO PRO A . n 
A 1 4319 SER 4319 4319 4319 SER SER A . n 
A 1 4320 TRP 4320 4320 4320 TRP TRP A . n 
A 1 4321 LEU 4321 4321 4321 LEU LEU A . n 
A 1 4322 GLY 4322 4322 4322 GLY GLY A . n 
A 1 4323 LEU 4323 4323 4323 LEU LEU A . n 
A 1 4324 PRO 4324 4324 4324 PRO PRO A . n 
A 1 4325 ASN 4325 4325 4325 ASN ASN A . n 
A 1 4326 ASN 4326 4326 4326 ASN ASN A . n 
A 1 4327 ALA 4327 4327 4327 ALA ALA A . n 
A 1 4328 GLU 4328 4328 4328 GLU GLU A . n 
A 1 4329 ARG 4329 4329 4329 ARG ARG A . n 
A 1 4330 VAL 4330 4330 4330 VAL VAL A . n 
A 1 4331 LEU 4331 4331 4331 LEU LEU A . n 
A 1 4332 LEU 4332 4332 4332 LEU LEU A . n 
A 1 4333 THR 4333 4333 4333 THR THR A . n 
A 1 4334 THR 4334 4334 4334 THR THR A . n 
A 1 4335 GLN 4335 4335 4335 GLN GLN A . n 
A 1 4336 GLY 4336 4336 4336 GLY GLY A . n 
A 1 4337 VAL 4337 4337 4337 VAL VAL A . n 
A 1 4338 ASP 4338 4338 4338 ASP ASP A . n 
A 1 4339 MET 4339 4339 4339 MET MET A . n 
A 1 4340 ILE 4340 4340 4340 ILE ILE A . n 
A 1 4341 SER 4341 4341 4341 SER SER A . n 
A 1 4342 LYS 4342 4342 4342 LYS LYS A . n 
A 1 4343 MET 4343 4343 4343 MET MET A . n 
A 1 4344 LEU 4344 4344 4344 LEU LEU A . n 
A 1 4345 LYS 4345 4345 4345 LYS LYS A . n 
A 1 4346 MET 4346 4346 4346 MET MET A . n 
A 1 4347 GLN 4347 4347 4347 GLN GLN A . n 
A 1 4348 MET 4348 4348 ?    ?   ?   A . n 
A 1 4349 LEU 4349 4349 ?    ?   ?   A . n 
A 1 4350 GLU 4350 4350 ?    ?   ?   A . n 
A 1 4351 ASP 4351 4351 ?    ?   ?   A . n 
A 1 4352 GLU 4352 4352 ?    ?   ?   A . n 
A 1 4353 ASP 4353 4353 ?    ?   ?   A . n 
A 1 4354 ASP 4354 4354 ?    ?   ?   A . n 
A 1 4355 LEU 4355 4355 ?    ?   ?   A . n 
A 1 4356 ALA 4356 4356 ?    ?   ?   A . n 
A 1 4357 TYR 4357 4357 ?    ?   ?   A . n 
A 1 4358 ALA 4358 4358 ?    ?   ?   A . n 
A 1 4359 GLU 4359 4359 ?    ?   ?   A . n 
A 1 4360 THR 4360 4360 ?    ?   ?   A . n 
A 1 4361 GLU 4361 4361 ?    ?   ?   A . n 
A 1 4362 LYS 4362 4362 ?    ?   ?   A . n 
A 1 4363 LYS 4363 4363 ?    ?   ?   A . n 
A 1 4364 THR 4364 4364 ?    ?   ?   A . n 
A 1 4365 ARG 4365 4365 ?    ?   ?   A . n 
A 1 4366 THR 4366 4366 ?    ?   ?   A . n 
A 1 4367 ASP 4367 4367 ?    ?   ?   A . n 
A 1 4368 SER 4368 4368 ?    ?   ?   A . n 
A 1 4369 THR 4369 4369 ?    ?   ?   A . n 
A 1 4370 SER 4370 4370 ?    ?   ?   A . n 
A 1 4371 ASP 4371 4371 ?    ?   ?   A . n 
A 1 4372 GLY 4372 4372 ?    ?   ?   A . n 
A 1 4373 ARG 4373 4373 ?    ?   ?   A . n 
A 1 4374 PRO 4374 4374 ?    ?   ?   A . n 
A 1 4375 ALA 4375 4375 4375 ALA ALA A . n 
A 1 4376 TRP 4376 4376 4376 TRP TRP A . n 
A 1 4377 MET 4377 4377 4377 MET MET A . n 
A 1 4378 ARG 4378 4378 4378 ARG ARG A . n 
A 1 4379 THR 4379 4379 4379 THR THR A . n 
A 1 4380 LEU 4380 4380 4380 LEU LEU A . n 
A 1 4381 HIS 4381 4381 4381 HIS HIS A . n 
A 1 4382 THR 4382 4382 4382 THR THR A . n 
A 1 4383 THR 4383 4383 4383 THR THR A . n 
A 1 4384 ALA 4384 4384 4384 ALA ALA A . n 
A 1 4385 SER 4385 4385 4385 SER SER A . n 
A 1 4386 ASN 4386 4386 4386 ASN ASN A . n 
A 1 4387 TRP 4387 4387 4387 TRP TRP A . n 
A 1 4388 LEU 4388 4388 4388 LEU LEU A . n 
A 1 4389 HIS 4389 4389 4389 HIS HIS A . n 
A 1 4390 LEU 4390 4390 4390 LEU LEU A . n 
A 1 4391 ILE 4391 4391 4391 ILE ILE A . n 
A 1 4392 PRO 4392 4392 4392 PRO PRO A . n 
A 1 4393 GLN 4393 4393 4393 GLN GLN A . n 
A 1 4394 THR 4394 4394 4394 THR THR A . n 
A 1 4395 LEU 4395 4395 4395 LEU LEU A . n 
A 1 4396 SER 4396 4396 4396 SER SER A . n 
A 1 4397 HIS 4397 4397 4397 HIS HIS A . n 
A 1 4398 LEU 4398 4398 4398 LEU LEU A . n 
A 1 4399 LYS 4399 4399 4399 LYS LYS A . n 
A 1 4400 ARG 4400 4400 4400 ARG ARG A . n 
A 1 4401 THR 4401 4401 4401 THR THR A . n 
A 1 4402 VAL 4402 4402 4402 VAL VAL A . n 
A 1 4403 GLU 4403 4403 4403 GLU GLU A . n 
A 1 4404 ASN 4404 4404 4404 ASN ASN A . n 
A 1 4405 ILE 4405 4405 4405 ILE ILE A . n 
A 1 4406 LYS 4406 4406 4406 LYS LYS A . n 
A 1 4407 ASP 4407 4407 4407 ASP ASP A . n 
A 1 4408 PRO 4408 4408 4408 PRO PRO A . n 
A 1 4409 LEU 4409 4409 4409 LEU LEU A . n 
A 1 4410 PHE 4410 4410 4410 PHE PHE A . n 
A 1 4411 ARG 4411 4411 4411 ARG ARG A . n 
A 1 4412 PHE 4412 4412 4412 PHE PHE A . n 
A 1 4413 PHE 4413 4413 4413 PHE PHE A . n 
A 1 4414 GLU 4414 4414 4414 GLU GLU A . n 
A 1 4415 ARG 4415 4415 4415 ARG ARG A . n 
A 1 4416 GLU 4416 4416 4416 GLU GLU A . n 
A 1 4417 VAL 4417 4417 4417 VAL VAL A . n 
A 1 4418 LYS 4418 4418 4418 LYS LYS A . n 
A 1 4419 MET 4419 4419 4419 MET MET A . n 
A 1 4420 GLY 4420 4420 4420 GLY GLY A . n 
A 1 4421 ALA 4421 4421 4421 ALA ALA A . n 
A 1 4422 LYS 4422 4422 4422 LYS LYS A . n 
A 1 4423 LEU 4423 4423 4423 LEU LEU A . n 
A 1 4424 LEU 4424 4424 4424 LEU LEU A . n 
A 1 4425 GLN 4425 4425 4425 GLN GLN A . n 
A 1 4426 ASP 4426 4426 4426 ASP ASP A . n 
A 1 4427 VAL 4427 4427 4427 VAL VAL A . n 
A 1 4428 ARG 4428 4428 4428 ARG ARG A . n 
A 1 4429 GLN 4429 4429 4429 GLN GLN A . n 
A 1 4430 ASP 4430 4430 4430 ASP ASP A . n 
A 1 4431 LEU 4431 4431 4431 LEU LEU A . n 
A 1 4432 ALA 4432 4432 4432 ALA ALA A . n 
A 1 4433 ASP 4433 4433 4433 ASP ASP A . n 
A 1 4434 VAL 4434 4434 4434 VAL VAL A . n 
A 1 4435 VAL 4435 4435 4435 VAL VAL A . n 
A 1 4436 GLN 4436 4436 4436 GLN GLN A . n 
A 1 4437 VAL 4437 4437 4437 VAL VAL A . n 
A 1 4438 CYS 4438 4438 4438 CYS CYS A . n 
A 1 4439 GLU 4439 4439 4439 GLU GLU A . n 
A 1 4440 GLY 4440 4440 4440 GLY GLY A . n 
A 1 4441 LYS 4441 4441 4441 LYS LYS A . n 
A 1 4442 LYS 4442 4442 4442 LYS LYS A . n 
A 1 4443 LYS 4443 4443 4443 LYS LYS A . n 
A 1 4444 GLN 4444 4444 4444 GLN GLN A . n 
A 1 4445 THR 4445 4445 4445 THR THR A . n 
A 1 4446 ASN 4446 4446 4446 ASN ASN A . n 
A 1 4447 TYR 4447 4447 4447 TYR TYR A . n 
A 1 4448 LEU 4448 4448 4448 LEU LEU A . n 
A 1 4449 ARG 4449 4449 4449 ARG ARG A . n 
A 1 4450 THR 4450 4450 4450 THR THR A . n 
A 1 4451 LEU 4451 4451 4451 LEU LEU A . n 
A 1 4452 ILE 4452 4452 4452 ILE ILE A . n 
A 1 4453 ASN 4453 4453 4453 ASN ASN A . n 
A 1 4454 GLU 4454 4454 4454 GLU GLU A . n 
A 1 4455 LEU 4455 4455 4455 LEU LEU A . n 
A 1 4456 VAL 4456 4456 4456 VAL VAL A . n 
A 1 4457 LYS 4457 4457 4457 LYS LYS A . n 
A 1 4458 GLY 4458 4458 4458 GLY GLY A . n 
A 1 4459 ILE 4459 4459 4459 ILE ILE A . n 
A 1 4460 LEU 4460 4460 4460 LEU LEU A . n 
A 1 4461 PRO 4461 4461 4461 PRO PRO A . n 
A 1 4462 ARG 4462 4462 4462 ARG ARG A . n 
A 1 4463 SER 4463 4463 4463 SER SER A . n 
A 1 4464 TRP 4464 4464 4464 TRP TRP A . n 
A 1 4465 SER 4465 4465 4465 SER SER A . n 
A 1 4466 HIS 4466 4466 4466 HIS HIS A . n 
A 1 4467 TYR 4467 4467 4467 TYR TYR A . n 
A 1 4468 THR 4468 4468 4468 THR THR A . n 
A 1 4469 VAL 4469 4469 4469 VAL VAL A . n 
A 1 4470 PRO 4470 4470 4470 PRO PRO A . n 
A 1 4471 ALA 4471 4471 4471 ALA ALA A . n 
A 1 4472 GLY 4472 4472 4472 GLY GLY A . n 
A 1 4473 MET 4473 4473 4473 MET MET A . n 
A 1 4474 THR 4474 4474 4474 THR THR A . n 
A 1 4475 VAL 4475 4475 4475 VAL VAL A . n 
A 1 4476 ILE 4476 4476 4476 ILE ILE A . n 
A 1 4477 GLN 4477 4477 4477 GLN GLN A . n 
A 1 4478 TRP 4478 4478 4478 TRP TRP A . n 
A 1 4479 VAL 4479 4479 4479 VAL VAL A . n 
A 1 4480 SER 4480 4480 4480 SER SER A . n 
A 1 4481 ASP 4481 4481 4481 ASP ASP A . n 
A 1 4482 PHE 4482 4482 4482 PHE PHE A . n 
A 1 4483 SER 4483 4483 4483 SER SER A . n 
A 1 4484 GLU 4484 4484 4484 GLU GLU A . n 
A 1 4485 ARG 4485 4485 4485 ARG ARG A . n 
A 1 4486 ILE 4486 4486 4486 ILE ILE A . n 
A 1 4487 LYS 4487 4487 4487 LYS LYS A . n 
A 1 4488 GLN 4488 4488 4488 GLN GLN A . n 
A 1 4489 LEU 4489 4489 4489 LEU LEU A . n 
A 1 4490 GLN 4490 4490 4490 GLN GLN A . n 
A 1 4491 ASN 4491 4491 4491 ASN ASN A . n 
A 1 4492 ILE 4492 4492 4492 ILE ILE A . n 
A 1 4493 SER 4493 4493 4493 SER SER A . n 
A 1 4494 LEU 4494 4494 4494 LEU LEU A . n 
A 1 4495 ALA 4495 4495 4495 ALA ALA A . n 
A 1 4496 ALA 4496 4496 4496 ALA ALA A . n 
A 1 4497 ALA 4497 4497 4497 ALA ALA A . n 
A 1 4498 SER 4498 4498 4498 SER SER A . n 
A 1 4499 GLY 4499 4499 4499 GLY GLY A . n 
A 1 4500 GLY 4500 4500 4500 GLY GLY A . n 
A 1 4501 ALA 4501 4501 4501 ALA ALA A . n 
A 1 4502 LYS 4502 4502 4502 LYS LYS A . n 
A 1 4503 GLU 4503 4503 4503 GLU GLU A . n 
A 1 4504 LEU 4504 4504 4504 LEU LEU A . n 
A 1 4505 LYS 4505 4505 4505 LYS LYS A . n 
A 1 4506 ASN 4506 4506 4506 ASN ASN A . n 
A 1 4507 ILE 4507 4507 4507 ILE ILE A . n 
A 1 4508 HIS 4508 4508 4508 HIS HIS A . n 
A 1 4509 VAL 4509 4509 4509 VAL VAL A . n 
A 1 4510 CYS 4510 4510 4510 CYS CYS A . n 
A 1 4511 LEU 4511 4511 4511 LEU LEU A . n 
A 1 4512 GLY 4512 4512 4512 GLY GLY A . n 
A 1 4513 GLY 4513 4513 4513 GLY GLY A . n 
A 1 4514 LEU 4514 4514 4514 LEU LEU A . n 
A 1 4515 PHE 4515 4515 4515 PHE PHE A . n 
A 1 4516 VAL 4516 4516 4516 VAL VAL A . n 
A 1 4517 PRO 4517 4517 4517 PRO PRO A . n 
A 1 4518 GLU 4518 4518 4518 GLU GLU A . n 
A 1 4519 ALA 4519 4519 4519 ALA ALA A . n 
A 1 4520 TYR 4520 4520 4520 TYR TYR A . n 
A 1 4521 ILE 4521 4521 4521 ILE ILE A . n 
A 1 4522 THR 4522 4522 4522 THR THR A . n 
A 1 4523 ALA 4523 4523 4523 ALA ALA A . n 
A 1 4524 THR 4524 4524 4524 THR THR A . n 
A 1 4525 ARG 4525 4525 4525 ARG ARG A . n 
A 1 4526 GLN 4526 4526 4526 GLN GLN A . n 
A 1 4527 TYR 4527 4527 4527 TYR TYR A . n 
A 1 4528 VAL 4528 4528 4528 VAL VAL A . n 
A 1 4529 ALA 4529 4529 4529 ALA ALA A . n 
A 1 4530 GLN 4530 4530 4530 GLN GLN A . n 
A 1 4531 ALA 4531 4531 4531 ALA ALA A . n 
A 1 4532 ASN 4532 4532 4532 ASN ASN A . n 
A 1 4533 SER 4533 4533 4533 SER SER A . n 
A 1 4534 TRP 4534 4534 4534 TRP TRP A . n 
A 1 4535 SER 4535 4535 4535 SER SER A . n 
A 1 4536 LEU 4536 4536 4536 LEU LEU A . n 
A 1 4537 GLU 4537 4537 4537 GLU GLU A . n 
A 1 4538 GLU 4538 4538 4538 GLU GLU A . n 
A 1 4539 LEU 4539 4539 4539 LEU LEU A . n 
A 1 4540 CYS 4540 4540 4540 CYS CYS A . n 
A 1 4541 LEU 4541 4541 4541 LEU LEU A . n 
A 1 4542 GLU 4542 4542 4542 GLU GLU A . n 
A 1 4543 VAL 4543 4543 4543 VAL VAL A . n 
A 1 4544 ASN 4544 4544 4544 ASN ASN A . n 
A 1 4545 VAL 4545 4545 4545 VAL VAL A . n 
A 1 4546 THR 4546 4546 4546 THR THR A . n 
A 1 4547 THR 4547 4547 4547 THR THR A . n 
A 1 4548 SER 4548 4548 4548 SER SER A . n 
A 1 4549 GLN 4549 4549 4549 GLN GLN A . n 
A 1 4550 GLY 4550 4550 4550 GLY GLY A . n 
A 1 4551 ALA 4551 4551 4551 ALA ALA A . n 
A 1 4552 THR 4552 4552 4552 THR THR A . n 
A 1 4553 LEU 4553 4553 4553 LEU LEU A . n 
A 1 4554 ASP 4554 4554 4554 ASP ASP A . n 
A 1 4555 ALA 4555 4555 4555 ALA ALA A . n 
A 1 4556 CYS 4556 4556 4556 CYS CYS A . n 
A 1 4557 SER 4557 4557 4557 SER SER A . n 
A 1 4558 PHE 4558 4558 4558 PHE PHE A . n 
A 1 4559 GLY 4559 4559 4559 GLY GLY A . n 
A 1 4560 VAL 4560 4560 4560 VAL VAL A . n 
A 1 4561 THR 4561 4561 4561 THR THR A . n 
A 1 4562 GLY 4562 4562 4562 GLY GLY A . n 
A 1 4563 LEU 4563 4563 4563 LEU LEU A . n 
A 1 4564 LYS 4564 4564 4564 LYS LYS A . n 
A 1 4565 LEU 4565 4565 4565 LEU LEU A . n 
A 1 4566 GLN 4566 4566 4566 GLN GLN A . n 
A 1 4567 GLY 4567 4567 4567 GLY GLY A . n 
A 1 4568 ALA 4568 4568 4568 ALA ALA A . n 
A 1 4569 THR 4569 4569 4569 THR THR A . n 
A 1 4570 CYS 4570 4570 4570 CYS CYS A . n 
A 1 4571 ASN 4571 4571 4571 ASN ASN A . n 
A 1 4572 ASN 4572 4572 4572 ASN ASN A . n 
A 1 4573 ASN 4573 4573 4573 ASN ASN A . n 
A 1 4574 LYS 4574 4574 4574 LYS LYS A . n 
A 1 4575 LEU 4575 4575 4575 LEU LEU A . n 
A 1 4576 SER 4576 4576 4576 SER SER A . n 
A 1 4577 LEU 4577 4577 4577 LEU LEU A . n 
A 1 4578 SER 4578 4578 4578 SER SER A . n 
A 1 4579 ASN 4579 4579 4579 ASN ASN A . n 
A 1 4580 ALA 4580 4580 4580 ALA ALA A . n 
A 1 4581 ILE 4581 4581 4581 ILE ILE A . n 
A 1 4582 SER 4582 4582 4582 SER SER A . n 
A 1 4583 THR 4583 4583 4583 THR THR A . n 
A 1 4584 ALA 4584 4584 4584 ALA ALA A . n 
A 1 4585 LEU 4585 4585 4585 LEU LEU A . n 
A 1 4586 PRO 4586 4586 4586 PRO PRO A . n 
A 1 4587 LEU 4587 4587 4587 LEU LEU A . n 
A 1 4588 THR 4588 4588 4588 THR THR A . n 
A 1 4589 GLN 4589 4589 4589 GLN GLN A . n 
A 1 4590 LEU 4590 4590 4590 LEU LEU A . n 
A 1 4591 ARG 4591 4591 4591 ARG ARG A . n 
A 1 4592 TRP 4592 4592 4592 TRP TRP A . n 
A 1 4593 VAL 4593 4593 4593 VAL VAL A . n 
A 1 4594 LYS 4594 4594 4594 LYS LYS A . n 
A 1 4595 GLN 4595 4595 4595 GLN GLN A . n 
A 1 4596 THR 4596 4596 4596 THR THR A . n 
A 1 4597 ASN 4597 4597 4597 ASN ASN A . n 
A 1 4598 THR 4598 4598 4598 THR THR A . n 
A 1 4599 GLU 4599 4599 4599 GLU GLU A . n 
A 1 4600 LYS 4600 4600 4600 LYS LYS A . n 
A 1 4601 LYS 4601 4601 4601 LYS LYS A . n 
A 1 4602 ALA 4602 4602 4602 ALA ALA A . n 
A 1 4603 SER 4603 4603 4603 SER SER A . n 
A 1 4604 VAL 4604 4604 4604 VAL VAL A . n 
A 1 4605 VAL 4605 4605 4605 VAL VAL A . n 
A 1 4606 THR 4606 4606 4606 THR THR A . n 
A 1 4607 LEU 4607 4607 4607 LEU LEU A . n 
A 1 4608 PRO 4608 4608 4608 PRO PRO A . n 
A 1 4609 VAL 4609 4609 4609 VAL VAL A . n 
A 1 4610 TYR 4610 4610 4610 TYR TYR A . n 
A 1 4611 LEU 4611 4611 4611 LEU LEU A . n 
A 1 4612 ASN 4612 4612 4612 ASN ASN A . n 
A 1 4613 PHE 4613 4613 4613 PHE PHE A . n 
A 1 4614 THR 4614 4614 4614 THR THR A . n 
A 1 4615 ARG 4615 4615 4615 ARG ARG A . n 
A 1 4616 ALA 4616 4616 4616 ALA ALA A . n 
A 1 4617 ASP 4617 4617 4617 ASP ASP A . n 
A 1 4618 LEU 4618 4618 4618 LEU LEU A . n 
A 1 4619 ILE 4619 4619 4619 ILE ILE A . n 
A 1 4620 PHE 4620 4620 4620 PHE PHE A . n 
A 1 4621 THR 4621 4621 4621 THR THR A . n 
A 1 4622 VAL 4622 4622 4622 VAL VAL A . n 
A 1 4623 ASP 4623 4623 4623 ASP ASP A . n 
A 1 4624 PHE 4624 4624 4624 PHE PHE A . n 
A 1 4625 GLU 4625 4625 4625 GLU GLU A . n 
A 1 4626 ILE 4626 4626 4626 ILE ILE A . n 
A 1 4627 ALA 4627 4627 4627 ALA ALA A . n 
A 1 4628 THR 4628 4628 4628 THR THR A . n 
A 1 4629 LYS 4629 4629 4629 LYS LYS A . n 
A 1 4630 GLU 4630 4630 4630 GLU GLU A . n 
A 1 4631 ASP 4631 4631 4631 ASP ASP A . n 
A 1 4632 PRO 4632 4632 4632 PRO PRO A . n 
A 1 4633 ARG 4633 4633 4633 ARG ARG A . n 
A 1 4634 SER 4634 4634 4634 SER SER A . n 
A 1 4635 PHE 4635 4635 4635 PHE PHE A . n 
A 1 4636 TYR 4636 4636 4636 TYR TYR A . n 
A 1 4637 GLU 4637 4637 4637 GLU GLU A . n 
A 1 4638 ARG 4638 4638 4638 ARG ARG A . n 
A 1 4639 GLY 4639 4639 4639 GLY GLY A . n 
A 1 4640 VAL 4640 4640 4640 VAL VAL A . n 
A 1 4641 ALA 4641 4641 4641 ALA ALA A . n 
A 1 4642 VAL 4642 4642 4642 VAL VAL A . n 
A 1 4643 LEU 4643 4643 4643 LEU LEU A . n 
A 1 4644 CYS 4644 4644 4644 CYS CYS A . n 
A 1 4645 THR 4645 4645 4645 THR THR A . n 
A 1 4646 GLU 4646 4646 ?    ?   ?   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' ? 
# 
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 ADP 1 4701 4701 ADP ADP A . 
C 3 ATP 1 4702 4702 ATP ATP A . 
D 3 ATP 1 4703 4703 ATP ATP A . 
E 2 ADP 1 4704 4704 ADP ADP 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 MET 2412 ? CG  ? A MET 2412 CG  
2 1 Y 1 A MET 2412 ? SD  ? A MET 2412 SD  
3 1 Y 1 A MET 2412 ? CE  ? A MET 2412 CE  
4 1 Y 1 A ASP 4289 ? CG  ? A ASP 4289 CG  
5 1 Y 1 A ASP 4289 ? OD1 ? A ASP 4289 OD1 
6 1 Y 1 A ASP 4289 ? OD2 ? A ASP 4289 OD2 
# 
_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                   9BM8 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BM8 
_struct.title                        'State-7c of motor domain from full-length human dynein-1 in 5 mM ATP' 
_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        9BM8 
_struct_keywords.text            'dynein-1, 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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYHC1_HUMAN 
_struct_ref.pdbx_db_accession          Q14204 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BM8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_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 
# 
_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 GLN A 1327 ? GLU A 1348 ? GLN A 1327 GLU A 1348 1 ? 22 
HELX_P HELX_P2   AA2 PRO A 1350 ? VAL A 1354 ? PRO A 1350 VAL A 1354 5 ? 5  
HELX_P HELX_P3   AA3 GLN A 1355 ? SER A 1372 ? GLN A 1355 SER A 1372 1 ? 18 
HELX_P HELX_P4   AA4 PRO A 1374 ? GLN A 1379 ? PRO A 1374 GLN A 1379 1 ? 6  
HELX_P HELX_P5   AA5 TYR A 1380 ? ILE A 1396 ? TYR A 1380 ILE A 1396 1 ? 17 
HELX_P HELX_P6   AA6 ILE A 1396 ? LYS A 1404 ? ILE A 1396 LYS A 1404 1 ? 9  
HELX_P HELX_P7   AA7 ASP A 1410 ? HIS A 1421 ? ASP A 1410 HIS A 1421 1 ? 12 
HELX_P HELX_P8   AA8 THR A 1430 ? VAL A 1437 ? THR A 1430 VAL A 1437 1 ? 8  
HELX_P HELX_P9   AA9 ASN A 1442 ? THR A 1472 ? ASN A 1442 THR A 1472 1 ? 31 
HELX_P HELX_P10  AB1 GLY A 1489 ? LEU A 1509 ? GLY A 1489 LEU A 1509 1 ? 21 
HELX_P HELX_P11  AB2 SER A 1510 ? VAL A 1515 ? SER A 1510 VAL A 1515 5 ? 6  
HELX_P HELX_P12  AB3 PHE A 1516 ? GLY A 1553 ? PHE A 1516 GLY A 1553 1 ? 38 
HELX_P HELX_P13  AB4 ASP A 1556 ? LEU A 1561 ? ASP A 1556 LEU A 1561 1 ? 6  
HELX_P HELX_P14  AB5 LEU A 1561 ? LYS A 1584 ? LEU A 1561 LYS A 1584 1 ? 24 
HELX_P HELX_P15  AB6 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P16  AB7 GLY A 1596 ? PHE A 1626 ? GLY A 1596 PHE A 1626 1 ? 31 
HELX_P HELX_P17  AB8 PRO A 1627 ? PHE A 1631 ? PRO A 1627 PHE A 1631 5 ? 5  
HELX_P HELX_P18  AB9 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P19  AC1 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P20  AC2 LYS A 1697 ? LYS A 1729 ? LYS A 1697 LYS A 1729 1 ? 33 
HELX_P HELX_P21  AC3 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P22  AC4 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P23  AC5 PRO A 1777 ? LEU A 1797 ? PRO A 1777 LEU A 1797 1 ? 21 
HELX_P HELX_P24  AC6 PRO A 1801 ? SER A 1824 ? PRO A 1801 SER A 1824 1 ? 24 
HELX_P HELX_P25  AC7 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P26  AC8 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P27  AC9 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P28  AD1 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P29  AD2 GLU A 1959 ? LEU A 1963 ? GLU A 1959 LEU A 1963 5 ? 5  
HELX_P HELX_P30  AD3 GLU A 1964 ? HIS A 1985 ? GLU A 1964 HIS A 1985 1 ? 22 
HELX_P HELX_P31  AD4 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P32  AD5 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P33  AD6 GLY A 2089 ? ARG A 2113 ? GLY A 2089 ARG A 2113 1 ? 25 
HELX_P HELX_P34  AD7 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P35  AD8 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P36  AD9 GLU A 2152 ? PHE A 2165 ? GLU A 2152 PHE A 2165 1 ? 14 
HELX_P HELX_P37  AE1 ALA A 2177 ? MET A 2189 ? ALA A 2177 MET A 2189 1 ? 13 
HELX_P HELX_P38  AE2 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P39  AE3 LYS A 2230 ? GLY A 2246 ? LYS A 2230 GLY A 2246 1 ? 17 
HELX_P HELX_P40  AE4 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P41  AE5 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P42  AE6 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P43  AE7 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P44  AE8 SER A 2365 ? LEU A 2369 ? SER A 2365 LEU A 2369 5 ? 5  
HELX_P HELX_P45  AE9 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P46  AF1 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P47  AF2 PRO A 2425 ? PHE A 2427 ? PRO A 2425 PHE A 2427 5 ? 3  
HELX_P HELX_P48  AF3 GLY A 2431 ? LEU A 2443 ? GLY A 2431 LEU A 2443 1 ? 13 
HELX_P HELX_P49  AF4 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P50  AF5 GLN A 2482 ? LEU A 2502 ? GLN A 2482 LEU A 2502 1 ? 21 
HELX_P HELX_P51  AF6 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P52  AF7 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P53  AF8 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P54  AF9 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P55  AG1 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P56  AG2 LYS A 2601 ? LEU A 2612 ? LYS A 2601 LEU A 2612 1 ? 12 
HELX_P HELX_P57  AG3 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P58  AG4 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P59  AG5 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P60  AG6 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P61  AG7 ARG A 2757 ? THR A 2764 ? ARG A 2757 THR A 2764 5 ? 8  
HELX_P HELX_P62  AG8 TYR A 2765 ? ARG A 2783 ? TYR A 2765 ARG A 2783 1 ? 19 
HELX_P HELX_P63  AG9 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P64  AH1 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P65  AH2 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P66  AH3 ASP A 2885 ? GLU A 2903 ? ASP A 2885 GLU A 2903 1 ? 19 
HELX_P HELX_P67  AH4 PHE A 2912 ? GLN A 2928 ? PHE A 2912 GLN A 2928 1 ? 17 
HELX_P HELX_P68  AH5 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P69  AH6 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P70  AH7 GLU A 3006 ? GLY A 3015 ? GLU A 3006 GLY A 3015 1 ? 10 
HELX_P HELX_P71  AH8 VAL A 3017 ? PHE A 3021 ? VAL A 3017 PHE A 3021 5 ? 5  
HELX_P HELX_P72  AH9 GLU A 3022 ? GLY A 3041 ? GLU A 3022 GLY A 3041 1 ? 20 
HELX_P HELX_P73  AI1 SER A 3046 ? LEU A 3062 ? SER A 3046 LEU A 3062 1 ? 17 
HELX_P HELX_P74  AI2 ALA A 3084 ? CYS A 3089 ? ALA A 3084 CYS A 3089 1 ? 6  
HELX_P HELX_P75  AI3 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P76  AI4 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P77  AI5 THR A 3172 ? ARG A 3220 ? THR A 3172 ARG A 3220 1 ? 49 
HELX_P HELX_P78  AI6 VAL A 3472 ? THR A 3502 ? VAL A 3472 THR A 3502 1 ? 31 
HELX_P HELX_P79  AI7 ILE A 3503 ? TYR A 3516 ? ILE A 3503 TYR A 3516 1 ? 14 
HELX_P HELX_P80  AI8 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P81  AI9 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P82  AJ1 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P83  AJ2 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P84  AJ3 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P85  AJ4 ALA A 3618 ? PHE A 3629 ? ALA A 3618 PHE A 3629 1 ? 12 
HELX_P HELX_P86  AJ5 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P87  AJ6 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P88  AJ7 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P89  AJ8 PRO A 3689 ? ARG A 3695 ? PRO A 3689 ARG A 3695 1 ? 7  
HELX_P HELX_P90  AJ9 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P91  AK1 ARG A 3721 ? LEU A 3734 ? ARG A 3721 LEU A 3734 1 ? 14 
HELX_P HELX_P92  AK2 GLY A 3736 ? LYS A 3757 ? GLY A 3736 LYS A 3757 1 ? 22 
HELX_P HELX_P93  AK3 ASP A 3762 ? GLU A 3786 ? ASP A 3762 GLU A 3786 1 ? 25 
HELX_P HELX_P94  AK4 GLU A 3786 ? LEU A 3818 ? GLU A 3786 LEU A 3818 1 ? 33 
HELX_P HELX_P95  AK5 LYS A 3819 ? ILE A 3821 ? LYS A 3819 ILE A 3821 5 ? 3  
HELX_P HELX_P96  AK6 SER A 3828 ? TYR A 3841 ? SER A 3828 TYR A 3841 1 ? 14 
HELX_P HELX_P97  AK7 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P98  AK8 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P99  AK9 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P100 AL1 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P101 AL2 ASP A 3879 ? THR A 3895 ? ASP A 3879 THR A 3895 1 ? 17 
HELX_P HELX_P102 AL3 TYR A 3901 ? ARG A 3910 ? TYR A 3901 ARG A 3910 1 ? 10 
HELX_P HELX_P103 AL4 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P104 AL5 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P105 AL6 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P106 AL7 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P107 AL8 THR A 3981 ? PHE A 3996 ? THR A 3981 PHE A 3996 1 ? 16 
HELX_P HELX_P108 AL9 ARG A 3997 ? ASP A 3999 ? ARG A 3997 ASP A 3999 5 ? 3  
HELX_P HELX_P109 AM1 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P110 AM2 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 1 ? 6  
HELX_P HELX_P111 AM3 LEU A 4027 ? THR A 4033 ? LEU A 4027 THR A 4033 1 ? 7  
HELX_P HELX_P112 AM4 ALA A 4051 ? GLN A 4062 ? ALA A 4051 GLN A 4062 1 ? 12 
HELX_P HELX_P113 AM5 ALA A 4074 ? GLY A 4091 ? ALA A 4074 GLY A 4091 1 ? 18 
HELX_P HELX_P114 AM6 VAL A 4099 ? LEU A 4101 ? VAL A 4099 LEU A 4101 5 ? 3  
HELX_P HELX_P115 AM7 ALA A 4102 ? HIS A 4114 ? ALA A 4102 HIS A 4114 1 ? 13 
HELX_P HELX_P116 AM8 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P117 AM9 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P118 AN1 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P119 AN2 ASN A 4174 ? ARG A 4193 ? ASN A 4174 ARG A 4193 1 ? 20 
HELX_P HELX_P120 AN3 LEU A 4194 ? TYR A 4196 ? LEU A 4194 TYR A 4196 5 ? 3  
HELX_P HELX_P121 AN4 ALA A 4197 ? SER A 4202 ? ALA A 4197 SER A 4202 1 ? 6  
HELX_P HELX_P122 AN5 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P123 AN6 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P124 AN7 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P125 AN8 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P126 AN9 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P127 AO1 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P128 AO2 THR A 4317 ? LEU A 4321 ? THR A 4317 LEU A 4321 5 ? 5  
HELX_P HELX_P129 AO3 ASN A 4325 ? MET A 4346 ? ASN A 4325 MET A 4346 1 ? 22 
HELX_P HELX_P130 AO4 TRP A 4376 ? ILE A 4391 ? TRP A 4376 ILE A 4391 1 ? 16 
HELX_P HELX_P131 AO5 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P132 AO6 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P133 AO7 PRO A 4461 ? SER A 4465 ? PRO A 4461 SER A 4465 5 ? 5  
HELX_P HELX_P134 AO8 THR A 4474 ? GLY A 4500 ? THR A 4474 GLY A 4500 1 ? 27 
HELX_P HELX_P135 AO9 ALA A 4501 ? ASN A 4506 ? ALA A 4501 ASN A 4506 1 ? 6  
HELX_P HELX_P136 AP1 VAL A 4516 ? ALA A 4531 ? VAL A 4516 ALA A 4531 1 ? 16 
HELX_P HELX_P137 AP2 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P138 AP3 ASP A 4631 ? ARG A 4638 ? ASP A 4631 ARG A 4638 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 5 ? 
AB6 ? 2 ? 
AB7 ? 5 ? 
AB8 ? 2 ? 
AB9 ? 4 ? 
AC1 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? 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 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB7 3 4 ? parallel      
AB7 4 5 ? parallel      
AB8 1 2 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? parallel      
AC1 3 4 ? anti-parallel 
AC1 4 5 ? parallel      
AC1 5 6 ? anti-parallel 
AC1 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 1477 ? TYR A 1480 ? LEU A 1477 TYR A 1480 
AA1 2 CYS A 1484 ? ILE A 1487 ? CYS A 1484 ILE A 1487 
AA2 1 VAL A 1661 ? LEU A 1666 ? VAL A 1661 LEU A 1666 
AA2 2 VAL A 1672 ? SER A 1678 ? VAL A 1672 SER A 1678 
AA2 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA3 1 ARG A 1843 ? PHE A 1846 ? ARG A 1843 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? PHE A 1930 ? VAL A 1927 PHE A 1930 
AA5 2 TRP A 1954 ? PHE A 1957 ? TRP A 1954 PHE A 1957 
AA5 3 ALA A 2013 ? ILE A 2016 ? ALA A 2013 ILE A 2016 
AA6 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA6 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2253 ? GLY A 2249 ILE A 2253 
AA7 2 ARG A 2298 ? VAL A 2302 ? ARG A 2298 VAL A 2302 
AA7 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA7 4 LEU A 2220 ? VAL A 2223 ? LEU A 2220 VAL A 2223 
AA7 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA8 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA8 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AB1 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB2 1 MET A 2615 ? ASN A 2621 ? MET A 2615 ASN A 2621 
AB2 2 TRP A 2658 ? ASP A 2664 ? TRP A 2658 ASP A 2664 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? ARG A 2642 ? CYS A 2639 ARG A 2642 
AB3 2 VAL A 2649 ? PRO A 2652 ? VAL A 2649 PRO A 2652 
AB3 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB3 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB4 1 SER A 2957 ? GLN A 2960 ? SER A 2957 GLN A 2960 
AB4 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB4 3 VAL A 3064 ? MET A 3068 ? VAL A 3064 MET A 3068 
AB4 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB4 5 ASN A 3092 ? PHE A 3094 ? ASN A 3092 PHE A 3094 
AB5 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB5 2 LEU A 3633 ? GLN A 3636 ? LEU A 3633 GLN A 3636 
AB5 3 ILE A 3677 ? THR A 3681 ? ILE A 3677 THR A 3681 
AB5 4 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB5 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB6 1 LEU A 3661 ? LEU A 3664 ? LEU A 3661 LEU A 3664 
AB6 2 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB7 1 ILE A 4066 ? THR A 4067 ? ILE A 4066 THR A 4067 
AB7 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB7 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB7 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB7 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB8 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB8 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AB9 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AB9 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AB9 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AB9 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC1 1 ALA A 4568 ? ASN A 4571 ? ALA A 4568 ASN A 4571 
AC1 2 LYS A 4574 ? LEU A 4577 ? LYS A 4574 LEU A 4577 
AC1 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC1 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC1 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC1 6 LYS A 4564 ? GLN A 4566 ? LYS A 4564 GLN A 4566 
AC1 7 THR A 4583 ? ALA A 4584 ? THR A 4583 ALA A 4584 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 1478 ? N VAL A 1478 O LEU A 1486 ? O LEU A 1486 
AA2 1 2 N ILE A 1665 ? N ILE A 1665 O GLY A 1675 ? O GLY A 1675 
AA2 2 3 N ILE A 1676 ? N ILE A 1676 O VAL A 1684 ? O VAL A 1684 
AA3 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA3 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA4 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O CYS A 1956 ? O CYS A 1956 
AA5 2 3 N GLY A 1955 ? N GLY A 1955 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA7 1 2 N VAL A 2250 ? N VAL A 2250 O ARG A 2298 ? O ARG A 2298 
AA7 2 3 N ILE A 2301 ? N ILE A 2301 O ARG A 2340 ? O ARG A 2340 
AA7 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA7 4 5 N VAL A 2223 ? N VAL A 2223 O VAL A 2362 ? O VAL A 2362 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB2 2 3 N LEU A 2659 ? N LEU A 2659 O GLN A 2707 ? O GLN A 2707 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB2 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB3 1 2 N ARG A 2642 ? N ARG A 2642 O VAL A 2649 ? O VAL A 2649 
AB3 2 3 N LEU A 2650 ? N LEU A 2650 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB4 1 2 N TYR A 2959 ? N TYR A 2959 O ILE A 2993 ? O ILE A 2993 
AB4 2 3 N PHE A 2992 ? N PHE A 2992 O VAL A 3065 ? O VAL A 3065 
AB4 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2935 ? N LEU A 2935 
AB4 4 5 N ILE A 2936 ? N ILE A 2936 O PHE A 3094 ? O PHE A 3094 
AB5 1 2 N THR A 3610 ? N THR A 3610 O LEU A 3634 ? O LEU A 3634 
AB5 2 3 N VAL A 3635 ? N VAL A 3635 O SER A 3680 ? O SER A 3680 
AB5 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB5 4 5 N ILE A 3590 ? N ILE A 3590 O VAL A 3699 ? O VAL A 3699 
AB6 1 2 N LEU A 3664 ? N LEU A 3664 O GLN A 3667 ? O GLN A 3667 
AB7 1 2 N THR A 4067 ? N THR A 4067 O TRP A 4093 ? O TRP A 4093 
AB7 2 3 N VAL A 4094 ? N VAL A 4094 O PHE A 4125 ? O PHE A 4125 
AB7 3 4 O LEU A 4124 ? O LEU A 4124 N VAL A 4041 ? N VAL A 4041 
AB7 4 5 N LEU A 4042 ? N LEU A 4042 O ARG A 4143 ? O ARG A 4143 
AB8 1 2 N ALA A 4285 ? N ALA A 4285 O ILE A 4294 ? O ILE A 4294 
AB9 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AB9 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AB9 3 4 O ARG A 4591 ? O ARG A 4591 N GLU A 4542 ? N GLU A 4542 
AC1 1 2 N THR A 4569 ? N THR A 4569 O SER A 4576 ? O SER A 4576 
AC1 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC1 3 4 O VAL A 4622 ? O VAL A 4622 N LEU A 4607 ? N LEU A 4607 
AC1 4 5 N PRO A 4608 ? N PRO A 4608 O VAL A 4642 ? O VAL A 4642 
AC1 5 6 O LEU A 4643 ? O LEU A 4643 N LYS A 4564 ? N LYS A 4564 
AC1 6 7 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
# 
_pdbx_entry_details.entry_id                   9BM8 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 CD1 A LEU 1451 ? ? CG2 A THR 3656 ? ? 1.72 
2 1 OD1 A ASP 1448 ? ? CA  A GLY 3657 ? ? 1.98 
3 1 OD1 A ASN 2752 ? ? OG1 A THR 2770 ? ? 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 1409 ? ? 54.61   -123.60 
2  1 ASN A 1442 ? ? -94.12  32.45   
3  1 ASN A 1643 ? ? -97.91  35.95   
4  1 ALA A 1862 ? ? 58.46   -122.98 
5  1 GLU A 1934 ? ? 53.87   7.07    
6  1 THR A 1935 ? ? -98.37  58.46   
7  1 SER A 1994 ? ? -90.49  -61.23  
8  1 LEU A 2387 ? ? -72.36  30.41   
9  1 PHE A 2427 ? ? -96.51  58.38   
10 1 PHE A 2479 ? ? 57.08   70.42   
11 1 PRO A 2645 ? ? -68.36  -174.13 
12 1 ASP A 2672 ? ? -76.81  -169.91 
13 1 GLU A 2864 ? ? -130.74 -32.35  
14 1 ILE A 2871 ? ? 35.92   59.60   
15 1 SER A 2878 ? ? 62.54   -156.49 
16 1 GLU A 2904 ? ? 73.58   163.20  
17 1 GLU A 3006 ? ? 70.74   -19.05  
18 1 ASP A 3045 ? ? 54.69   -127.57 
19 1 PHE A 3094 ? ? -101.37 79.08   
20 1 TYR A 3125 ? ? 62.63   -127.82 
21 1 MET A 3126 ? ? 38.79   46.06   
22 1 VAL A 3128 ? ? -127.23 -52.68  
23 1 ARG A 3167 ? ? 60.31   66.02   
24 1 TYR A 3519 ? ? 71.72   -7.46   
25 1 SER A 3554 ? ? -161.65 119.15  
26 1 LYS A 3608 ? ? 60.74   60.60   
27 1 ARG A 3654 ? ? -96.32  58.24   
28 1 TYR A 3825 ? ? -97.65  36.24   
29 1 LEU A 3916 ? ? -141.85 30.58   
30 1 ARG A 3923 ? ? 61.81   -121.70 
31 1 ARG A 3997 ? ? 58.23   70.80   
32 1 GLU A 4034 ? ? 69.42   -4.15   
33 1 ASN A 4063 ? ? 35.44   46.86   
34 1 SER A 4172 ? ? 65.71   -165.82 
35 1 SER A 4202 ? ? 61.47   -65.00  
36 1 PRO A 4239 ? ? -69.66  71.31   
37 1 TYR A 4252 ? ? 67.24   -4.46   
38 1 LYS A 4287 ? ? 68.30   -1.01   
39 1 MET A 4346 ? ? -108.99 45.54   
40 1 ASN A 4506 ? ? -93.26  58.27   
41 1 ASN A 4532 ? ? 69.75   -3.01   
42 1 SER A 4533 ? ? 60.29   60.69   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BM8 
_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                    9BM8 
_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                  3.22 
_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               66325 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP' 
_em_buffer.pH            7.2 
# 
_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                 'State-7c of motor domain from full-length human dynein-1 in 5mM ATP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BM8 
_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           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_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            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BM8 
_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   278 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9BM8 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 1    ? A MET 1    
2    1 Y 1 A SER 2    ? A SER 2    
3    1 Y 1 A GLU 3    ? A GLU 3    
4    1 Y 1 A PRO 4    ? A PRO 4    
5    1 Y 1 A GLY 5    ? A GLY 5    
6    1 Y 1 A GLY 6    ? A GLY 6    
7    1 Y 1 A GLY 7    ? A GLY 7    
8    1 Y 1 A GLY 8    ? A GLY 8    
9    1 Y 1 A GLY 9    ? A GLY 9    
10   1 Y 1 A GLU 10   ? A GLU 10   
11   1 Y 1 A ASP 11   ? A ASP 11   
12   1 Y 1 A GLY 12   ? A GLY 12   
13   1 Y 1 A SER 13   ? A SER 13   
14   1 Y 1 A ALA 14   ? A ALA 14   
15   1 Y 1 A GLY 15   ? A GLY 15   
16   1 Y 1 A LEU 16   ? A LEU 16   
17   1 Y 1 A GLU 17   ? A GLU 17   
18   1 Y 1 A VAL 18   ? A VAL 18   
19   1 Y 1 A SER 19   ? A SER 19   
20   1 Y 1 A ALA 20   ? A ALA 20   
21   1 Y 1 A VAL 21   ? A VAL 21   
22   1 Y 1 A GLN 22   ? A GLN 22   
23   1 Y 1 A ASN 23   ? A ASN 23   
24   1 Y 1 A VAL 24   ? A VAL 24   
25   1 Y 1 A ALA 25   ? A ALA 25   
26   1 Y 1 A ASP 26   ? A ASP 26   
27   1 Y 1 A VAL 27   ? A VAL 27   
28   1 Y 1 A SER 28   ? A SER 28   
29   1 Y 1 A VAL 29   ? A VAL 29   
30   1 Y 1 A LEU 30   ? A LEU 30   
31   1 Y 1 A GLN 31   ? A GLN 31   
32   1 Y 1 A LYS 32   ? A LYS 32   
33   1 Y 1 A HIS 33   ? A HIS 33   
34   1 Y 1 A LEU 34   ? A LEU 34   
35   1 Y 1 A ARG 35   ? A ARG 35   
36   1 Y 1 A LYS 36   ? A LYS 36   
37   1 Y 1 A LEU 37   ? A LEU 37   
38   1 Y 1 A VAL 38   ? A VAL 38   
39   1 Y 1 A PRO 39   ? A PRO 39   
40   1 Y 1 A LEU 40   ? A LEU 40   
41   1 Y 1 A LEU 41   ? A LEU 41   
42   1 Y 1 A LEU 42   ? A LEU 42   
43   1 Y 1 A GLU 43   ? A GLU 43   
44   1 Y 1 A ASP 44   ? A ASP 44   
45   1 Y 1 A GLY 45   ? A GLY 45   
46   1 Y 1 A GLY 46   ? A GLY 46   
47   1 Y 1 A GLU 47   ? A GLU 47   
48   1 Y 1 A ALA 48   ? A ALA 48   
49   1 Y 1 A PRO 49   ? A PRO 49   
50   1 Y 1 A ALA 50   ? A ALA 50   
51   1 Y 1 A ALA 51   ? A ALA 51   
52   1 Y 1 A LEU 52   ? A LEU 52   
53   1 Y 1 A GLU 53   ? A GLU 53   
54   1 Y 1 A ALA 54   ? A ALA 54   
55   1 Y 1 A ALA 55   ? A ALA 55   
56   1 Y 1 A LEU 56   ? A LEU 56   
57   1 Y 1 A GLU 57   ? A GLU 57   
58   1 Y 1 A GLU 58   ? A GLU 58   
59   1 Y 1 A LYS 59   ? A LYS 59   
60   1 Y 1 A SER 60   ? A SER 60   
61   1 Y 1 A ALA 61   ? A ALA 61   
62   1 Y 1 A LEU 62   ? A LEU 62   
63   1 Y 1 A GLU 63   ? A GLU 63   
64   1 Y 1 A GLN 64   ? A GLN 64   
65   1 Y 1 A MET 65   ? A MET 65   
66   1 Y 1 A ARG 66   ? A ARG 66   
67   1 Y 1 A LYS 67   ? A LYS 67   
68   1 Y 1 A PHE 68   ? A PHE 68   
69   1 Y 1 A LEU 69   ? A LEU 69   
70   1 Y 1 A SER 70   ? A SER 70   
71   1 Y 1 A ASP 71   ? A ASP 71   
72   1 Y 1 A PRO 72   ? A PRO 72   
73   1 Y 1 A GLN 73   ? A GLN 73   
74   1 Y 1 A VAL 74   ? A VAL 74   
75   1 Y 1 A HIS 75   ? A HIS 75   
76   1 Y 1 A THR 76   ? A THR 76   
77   1 Y 1 A VAL 77   ? A VAL 77   
78   1 Y 1 A LEU 78   ? A LEU 78   
79   1 Y 1 A VAL 79   ? A VAL 79   
80   1 Y 1 A GLU 80   ? A GLU 80   
81   1 Y 1 A ARG 81   ? A ARG 81   
82   1 Y 1 A SER 82   ? A SER 82   
83   1 Y 1 A THR 83   ? A THR 83   
84   1 Y 1 A LEU 84   ? A LEU 84   
85   1 Y 1 A LYS 85   ? A LYS 85   
86   1 Y 1 A GLU 86   ? A GLU 86   
87   1 Y 1 A ASP 87   ? A ASP 87   
88   1 Y 1 A VAL 88   ? A VAL 88   
89   1 Y 1 A GLY 89   ? A GLY 89   
90   1 Y 1 A ASP 90   ? A ASP 90   
91   1 Y 1 A GLU 91   ? A GLU 91   
92   1 Y 1 A GLY 92   ? A GLY 92   
93   1 Y 1 A GLU 93   ? A GLU 93   
94   1 Y 1 A GLU 94   ? A GLU 94   
95   1 Y 1 A GLU 95   ? A GLU 95   
96   1 Y 1 A LYS 96   ? A LYS 96   
97   1 Y 1 A GLU 97   ? A GLU 97   
98   1 Y 1 A PHE 98   ? A PHE 98   
99   1 Y 1 A ILE 99   ? A ILE 99   
100  1 Y 1 A SER 100  ? A SER 100  
101  1 Y 1 A TYR 101  ? A TYR 101  
102  1 Y 1 A ASN 102  ? A ASN 102  
103  1 Y 1 A ILE 103  ? A ILE 103  
104  1 Y 1 A ASN 104  ? A ASN 104  
105  1 Y 1 A ILE 105  ? A ILE 105  
106  1 Y 1 A ASP 106  ? A ASP 106  
107  1 Y 1 A ILE 107  ? A ILE 107  
108  1 Y 1 A HIS 108  ? A HIS 108  
109  1 Y 1 A TYR 109  ? A TYR 109  
110  1 Y 1 A GLY 110  ? A GLY 110  
111  1 Y 1 A VAL 111  ? A VAL 111  
112  1 Y 1 A LYS 112  ? A LYS 112  
113  1 Y 1 A SER 113  ? A SER 113  
114  1 Y 1 A ASN 114  ? A ASN 114  
115  1 Y 1 A SER 115  ? A SER 115  
116  1 Y 1 A LEU 116  ? A LEU 116  
117  1 Y 1 A ALA 117  ? A ALA 117  
118  1 Y 1 A PHE 118  ? A PHE 118  
119  1 Y 1 A ILE 119  ? A ILE 119  
120  1 Y 1 A LYS 120  ? A LYS 120  
121  1 Y 1 A ARG 121  ? A ARG 121  
122  1 Y 1 A THR 122  ? A THR 122  
123  1 Y 1 A PRO 123  ? A PRO 123  
124  1 Y 1 A VAL 124  ? A VAL 124  
125  1 Y 1 A ILE 125  ? A ILE 125  
126  1 Y 1 A ASP 126  ? A ASP 126  
127  1 Y 1 A ALA 127  ? A ALA 127  
128  1 Y 1 A ASP 128  ? A ASP 128  
129  1 Y 1 A LYS 129  ? A LYS 129  
130  1 Y 1 A PRO 130  ? A PRO 130  
131  1 Y 1 A VAL 131  ? A VAL 131  
132  1 Y 1 A SER 132  ? A SER 132  
133  1 Y 1 A SER 133  ? A SER 133  
134  1 Y 1 A GLN 134  ? A GLN 134  
135  1 Y 1 A LEU 135  ? A LEU 135  
136  1 Y 1 A ARG 136  ? A ARG 136  
137  1 Y 1 A VAL 137  ? A VAL 137  
138  1 Y 1 A LEU 138  ? A LEU 138  
139  1 Y 1 A THR 139  ? A THR 139  
140  1 Y 1 A LEU 140  ? A LEU 140  
141  1 Y 1 A SER 141  ? A SER 141  
142  1 Y 1 A GLU 142  ? A GLU 142  
143  1 Y 1 A ASP 143  ? A ASP 143  
144  1 Y 1 A SER 144  ? A SER 144  
145  1 Y 1 A PRO 145  ? A PRO 145  
146  1 Y 1 A TYR 146  ? A TYR 146  
147  1 Y 1 A GLU 147  ? A GLU 147  
148  1 Y 1 A THR 148  ? A THR 148  
149  1 Y 1 A LEU 149  ? A LEU 149  
150  1 Y 1 A HIS 150  ? A HIS 150  
151  1 Y 1 A SER 151  ? A SER 151  
152  1 Y 1 A PHE 152  ? A PHE 152  
153  1 Y 1 A ILE 153  ? A ILE 153  
154  1 Y 1 A SER 154  ? A SER 154  
155  1 Y 1 A ASN 155  ? A ASN 155  
156  1 Y 1 A ALA 156  ? A ALA 156  
157  1 Y 1 A VAL 157  ? A VAL 157  
158  1 Y 1 A ALA 158  ? A ALA 158  
159  1 Y 1 A PRO 159  ? A PRO 159  
160  1 Y 1 A PHE 160  ? A PHE 160  
161  1 Y 1 A PHE 161  ? A PHE 161  
162  1 Y 1 A LYS 162  ? A LYS 162  
163  1 Y 1 A SER 163  ? A SER 163  
164  1 Y 1 A TYR 164  ? A TYR 164  
165  1 Y 1 A ILE 165  ? A ILE 165  
166  1 Y 1 A ARG 166  ? A ARG 166  
167  1 Y 1 A GLU 167  ? A GLU 167  
168  1 Y 1 A SER 168  ? A SER 168  
169  1 Y 1 A GLY 169  ? A GLY 169  
170  1 Y 1 A LYS 170  ? A LYS 170  
171  1 Y 1 A ALA 171  ? A ALA 171  
172  1 Y 1 A ASP 172  ? A ASP 172  
173  1 Y 1 A ARG 173  ? A ARG 173  
174  1 Y 1 A ASP 174  ? A ASP 174  
175  1 Y 1 A GLY 175  ? A GLY 175  
176  1 Y 1 A ASP 176  ? A ASP 176  
177  1 Y 1 A LYS 177  ? A LYS 177  
178  1 Y 1 A MET 178  ? A MET 178  
179  1 Y 1 A ALA 179  ? A ALA 179  
180  1 Y 1 A PRO 180  ? A PRO 180  
181  1 Y 1 A SER 181  ? A SER 181  
182  1 Y 1 A VAL 182  ? A VAL 182  
183  1 Y 1 A GLU 183  ? A GLU 183  
184  1 Y 1 A LYS 184  ? A LYS 184  
185  1 Y 1 A LYS 185  ? A LYS 185  
186  1 Y 1 A ILE 186  ? A ILE 186  
187  1 Y 1 A ALA 187  ? A ALA 187  
188  1 Y 1 A GLU 188  ? A GLU 188  
189  1 Y 1 A LEU 189  ? A LEU 189  
190  1 Y 1 A GLU 190  ? A GLU 190  
191  1 Y 1 A MET 191  ? A MET 191  
192  1 Y 1 A GLY 192  ? A GLY 192  
193  1 Y 1 A LEU 193  ? A LEU 193  
194  1 Y 1 A LEU 194  ? A LEU 194  
195  1 Y 1 A HIS 195  ? A HIS 195  
196  1 Y 1 A LEU 196  ? A LEU 196  
197  1 Y 1 A GLN 197  ? A GLN 197  
198  1 Y 1 A GLN 198  ? A GLN 198  
199  1 Y 1 A ASN 199  ? A ASN 199  
200  1 Y 1 A ILE 200  ? A ILE 200  
201  1 Y 1 A GLU 201  ? A GLU 201  
202  1 Y 1 A ILE 202  ? A ILE 202  
203  1 Y 1 A PRO 203  ? A PRO 203  
204  1 Y 1 A GLU 204  ? A GLU 204  
205  1 Y 1 A ILE 205  ? A ILE 205  
206  1 Y 1 A SER 206  ? A SER 206  
207  1 Y 1 A LEU 207  ? A LEU 207  
208  1 Y 1 A PRO 208  ? A PRO 208  
209  1 Y 1 A ILE 209  ? A ILE 209  
210  1 Y 1 A HIS 210  ? A HIS 210  
211  1 Y 1 A PRO 211  ? A PRO 211  
212  1 Y 1 A MET 212  ? A MET 212  
213  1 Y 1 A ILE 213  ? A ILE 213  
214  1 Y 1 A THR 214  ? A THR 214  
215  1 Y 1 A ASN 215  ? A ASN 215  
216  1 Y 1 A VAL 216  ? A VAL 216  
217  1 Y 1 A ALA 217  ? A ALA 217  
218  1 Y 1 A LYS 218  ? A LYS 218  
219  1 Y 1 A GLN 219  ? A GLN 219  
220  1 Y 1 A CYS 220  ? A CYS 220  
221  1 Y 1 A TYR 221  ? A TYR 221  
222  1 Y 1 A GLU 222  ? A GLU 222  
223  1 Y 1 A ARG 223  ? A ARG 223  
224  1 Y 1 A GLY 224  ? A GLY 224  
225  1 Y 1 A GLU 225  ? A GLU 225  
226  1 Y 1 A LYS 226  ? A LYS 226  
227  1 Y 1 A PRO 227  ? A PRO 227  
228  1 Y 1 A LYS 228  ? A LYS 228  
229  1 Y 1 A VAL 229  ? A VAL 229  
230  1 Y 1 A THR 230  ? A THR 230  
231  1 Y 1 A ASP 231  ? A ASP 231  
232  1 Y 1 A PHE 232  ? A PHE 232  
233  1 Y 1 A GLY 233  ? A GLY 233  
234  1 Y 1 A ASP 234  ? A ASP 234  
235  1 Y 1 A LYS 235  ? A LYS 235  
236  1 Y 1 A VAL 236  ? A VAL 236  
237  1 Y 1 A GLU 237  ? A GLU 237  
238  1 Y 1 A ASP 238  ? A ASP 238  
239  1 Y 1 A PRO 239  ? A PRO 239  
240  1 Y 1 A THR 240  ? A THR 240  
241  1 Y 1 A PHE 241  ? A PHE 241  
242  1 Y 1 A LEU 242  ? A LEU 242  
243  1 Y 1 A ASN 243  ? A ASN 243  
244  1 Y 1 A GLN 244  ? A GLN 244  
245  1 Y 1 A LEU 245  ? A LEU 245  
246  1 Y 1 A GLN 246  ? A GLN 246  
247  1 Y 1 A SER 247  ? A SER 247  
248  1 Y 1 A GLY 248  ? A GLY 248  
249  1 Y 1 A VAL 249  ? A VAL 249  
250  1 Y 1 A ASN 250  ? A ASN 250  
251  1 Y 1 A ARG 251  ? A ARG 251  
252  1 Y 1 A TRP 252  ? A TRP 252  
253  1 Y 1 A ILE 253  ? A ILE 253  
254  1 Y 1 A ARG 254  ? A ARG 254  
255  1 Y 1 A GLU 255  ? A GLU 255  
256  1 Y 1 A ILE 256  ? A ILE 256  
257  1 Y 1 A GLN 257  ? A GLN 257  
258  1 Y 1 A LYS 258  ? A LYS 258  
259  1 Y 1 A VAL 259  ? A VAL 259  
260  1 Y 1 A THR 260  ? A THR 260  
261  1 Y 1 A LYS 261  ? A LYS 261  
262  1 Y 1 A LEU 262  ? A LEU 262  
263  1 Y 1 A ASP 263  ? A ASP 263  
264  1 Y 1 A ARG 264  ? A ARG 264  
265  1 Y 1 A ASP 265  ? A ASP 265  
266  1 Y 1 A PRO 266  ? A PRO 266  
267  1 Y 1 A ALA 267  ? A ALA 267  
268  1 Y 1 A SER 268  ? A SER 268  
269  1 Y 1 A GLY 269  ? A GLY 269  
270  1 Y 1 A THR 270  ? A THR 270  
271  1 Y 1 A ALA 271  ? A ALA 271  
272  1 Y 1 A LEU 272  ? A LEU 272  
273  1 Y 1 A GLN 273  ? A GLN 273  
274  1 Y 1 A GLU 274  ? A GLU 274  
275  1 Y 1 A ILE 275  ? A ILE 275  
276  1 Y 1 A SER 276  ? A SER 276  
277  1 Y 1 A PHE 277  ? A PHE 277  
278  1 Y 1 A TRP 278  ? A TRP 278  
279  1 Y 1 A LEU 279  ? A LEU 279  
280  1 Y 1 A ASN 280  ? A ASN 280  
281  1 Y 1 A LEU 281  ? A LEU 281  
282  1 Y 1 A GLU 282  ? A GLU 282  
283  1 Y 1 A ARG 283  ? A ARG 283  
284  1 Y 1 A ALA 284  ? A ALA 284  
285  1 Y 1 A LEU 285  ? A LEU 285  
286  1 Y 1 A TYR 286  ? A TYR 286  
287  1 Y 1 A ARG 287  ? A ARG 287  
288  1 Y 1 A ILE 288  ? A ILE 288  
289  1 Y 1 A GLN 289  ? A GLN 289  
290  1 Y 1 A GLU 290  ? A GLU 290  
291  1 Y 1 A LYS 291  ? A LYS 291  
292  1 Y 1 A ARG 292  ? A ARG 292  
293  1 Y 1 A GLU 293  ? A GLU 293  
294  1 Y 1 A SER 294  ? A SER 294  
295  1 Y 1 A PRO 295  ? A PRO 295  
296  1 Y 1 A GLU 296  ? A GLU 296  
297  1 Y 1 A VAL 297  ? A VAL 297  
298  1 Y 1 A LEU 298  ? A LEU 298  
299  1 Y 1 A LEU 299  ? A LEU 299  
300  1 Y 1 A THR 300  ? A THR 300  
301  1 Y 1 A LEU 301  ? A LEU 301  
302  1 Y 1 A ASP 302  ? A ASP 302  
303  1 Y 1 A ILE 303  ? A ILE 303  
304  1 Y 1 A LEU 304  ? A LEU 304  
305  1 Y 1 A LYS 305  ? A LYS 305  
306  1 Y 1 A HIS 306  ? A HIS 306  
307  1 Y 1 A GLY 307  ? A GLY 307  
308  1 Y 1 A LYS 308  ? A LYS 308  
309  1 Y 1 A ARG 309  ? A ARG 309  
310  1 Y 1 A PHE 310  ? A PHE 310  
311  1 Y 1 A HIS 311  ? A HIS 311  
312  1 Y 1 A ALA 312  ? A ALA 312  
313  1 Y 1 A THR 313  ? A THR 313  
314  1 Y 1 A VAL 314  ? A VAL 314  
315  1 Y 1 A SER 315  ? A SER 315  
316  1 Y 1 A PHE 316  ? A PHE 316  
317  1 Y 1 A ASP 317  ? A ASP 317  
318  1 Y 1 A THR 318  ? A THR 318  
319  1 Y 1 A ASP 319  ? A ASP 319  
320  1 Y 1 A THR 320  ? A THR 320  
321  1 Y 1 A GLY 321  ? A GLY 321  
322  1 Y 1 A LEU 322  ? A LEU 322  
323  1 Y 1 A LYS 323  ? A LYS 323  
324  1 Y 1 A GLN 324  ? A GLN 324  
325  1 Y 1 A ALA 325  ? A ALA 325  
326  1 Y 1 A LEU 326  ? A LEU 326  
327  1 Y 1 A GLU 327  ? A GLU 327  
328  1 Y 1 A THR 328  ? A THR 328  
329  1 Y 1 A VAL 329  ? A VAL 329  
330  1 Y 1 A ASN 330  ? A ASN 330  
331  1 Y 1 A ASP 331  ? A ASP 331  
332  1 Y 1 A TYR 332  ? A TYR 332  
333  1 Y 1 A ASN 333  ? A ASN 333  
334  1 Y 1 A PRO 334  ? A PRO 334  
335  1 Y 1 A LEU 335  ? A LEU 335  
336  1 Y 1 A MET 336  ? A MET 336  
337  1 Y 1 A LYS 337  ? A LYS 337  
338  1 Y 1 A ASP 338  ? A ASP 338  
339  1 Y 1 A PHE 339  ? A PHE 339  
340  1 Y 1 A PRO 340  ? A PRO 340  
341  1 Y 1 A LEU 341  ? A LEU 341  
342  1 Y 1 A ASN 342  ? A ASN 342  
343  1 Y 1 A ASP 343  ? A ASP 343  
344  1 Y 1 A LEU 344  ? A LEU 344  
345  1 Y 1 A LEU 345  ? A LEU 345  
346  1 Y 1 A SER 346  ? A SER 346  
347  1 Y 1 A ALA 347  ? A ALA 347  
348  1 Y 1 A THR 348  ? A THR 348  
349  1 Y 1 A GLU 349  ? A GLU 349  
350  1 Y 1 A LEU 350  ? A LEU 350  
351  1 Y 1 A ASP 351  ? A ASP 351  
352  1 Y 1 A LYS 352  ? A LYS 352  
353  1 Y 1 A ILE 353  ? A ILE 353  
354  1 Y 1 A ARG 354  ? A ARG 354  
355  1 Y 1 A GLN 355  ? A GLN 355  
356  1 Y 1 A ALA 356  ? A ALA 356  
357  1 Y 1 A LEU 357  ? A LEU 357  
358  1 Y 1 A VAL 358  ? A VAL 358  
359  1 Y 1 A ALA 359  ? A ALA 359  
360  1 Y 1 A ILE 360  ? A ILE 360  
361  1 Y 1 A PHE 361  ? A PHE 361  
362  1 Y 1 A THR 362  ? A THR 362  
363  1 Y 1 A HIS 363  ? A HIS 363  
364  1 Y 1 A LEU 364  ? A LEU 364  
365  1 Y 1 A ARG 365  ? A ARG 365  
366  1 Y 1 A LYS 366  ? A LYS 366  
367  1 Y 1 A ILE 367  ? A ILE 367  
368  1 Y 1 A ARG 368  ? A ARG 368  
369  1 Y 1 A ASN 369  ? A ASN 369  
370  1 Y 1 A THR 370  ? A THR 370  
371  1 Y 1 A LYS 371  ? A LYS 371  
372  1 Y 1 A TYR 372  ? A TYR 372  
373  1 Y 1 A PRO 373  ? A PRO 373  
374  1 Y 1 A ILE 374  ? A ILE 374  
375  1 Y 1 A GLN 375  ? A GLN 375  
376  1 Y 1 A ARG 376  ? A ARG 376  
377  1 Y 1 A ALA 377  ? A ALA 377  
378  1 Y 1 A LEU 378  ? A LEU 378  
379  1 Y 1 A ARG 379  ? A ARG 379  
380  1 Y 1 A LEU 380  ? A LEU 380  
381  1 Y 1 A VAL 381  ? A VAL 381  
382  1 Y 1 A GLU 382  ? A GLU 382  
383  1 Y 1 A ALA 383  ? A ALA 383  
384  1 Y 1 A ILE 384  ? A ILE 384  
385  1 Y 1 A SER 385  ? A SER 385  
386  1 Y 1 A ARG 386  ? A ARG 386  
387  1 Y 1 A ASP 387  ? A ASP 387  
388  1 Y 1 A LEU 388  ? A LEU 388  
389  1 Y 1 A SER 389  ? A SER 389  
390  1 Y 1 A SER 390  ? A SER 390  
391  1 Y 1 A GLN 391  ? A GLN 391  
392  1 Y 1 A LEU 392  ? A LEU 392  
393  1 Y 1 A LEU 393  ? A LEU 393  
394  1 Y 1 A LYS 394  ? A LYS 394  
395  1 Y 1 A VAL 395  ? A VAL 395  
396  1 Y 1 A LEU 396  ? A LEU 396  
397  1 Y 1 A GLY 397  ? A GLY 397  
398  1 Y 1 A THR 398  ? A THR 398  
399  1 Y 1 A ARG 399  ? A ARG 399  
400  1 Y 1 A LYS 400  ? A LYS 400  
401  1 Y 1 A LEU 401  ? A LEU 401  
402  1 Y 1 A MET 402  ? A MET 402  
403  1 Y 1 A HIS 403  ? A HIS 403  
404  1 Y 1 A VAL 404  ? A VAL 404  
405  1 Y 1 A ALA 405  ? A ALA 405  
406  1 Y 1 A TYR 406  ? A TYR 406  
407  1 Y 1 A GLU 407  ? A GLU 407  
408  1 Y 1 A GLU 408  ? A GLU 408  
409  1 Y 1 A PHE 409  ? A PHE 409  
410  1 Y 1 A GLU 410  ? A GLU 410  
411  1 Y 1 A LYS 411  ? A LYS 411  
412  1 Y 1 A VAL 412  ? A VAL 412  
413  1 Y 1 A MET 413  ? A MET 413  
414  1 Y 1 A VAL 414  ? A VAL 414  
415  1 Y 1 A ALA 415  ? A ALA 415  
416  1 Y 1 A CYS 416  ? A CYS 416  
417  1 Y 1 A PHE 417  ? A PHE 417  
418  1 Y 1 A GLU 418  ? A GLU 418  
419  1 Y 1 A VAL 419  ? A VAL 419  
420  1 Y 1 A PHE 420  ? A PHE 420  
421  1 Y 1 A GLN 421  ? A GLN 421  
422  1 Y 1 A THR 422  ? A THR 422  
423  1 Y 1 A TRP 423  ? A TRP 423  
424  1 Y 1 A ASP 424  ? A ASP 424  
425  1 Y 1 A ASP 425  ? A ASP 425  
426  1 Y 1 A GLU 426  ? A GLU 426  
427  1 Y 1 A TYR 427  ? A TYR 427  
428  1 Y 1 A GLU 428  ? A GLU 428  
429  1 Y 1 A LYS 429  ? A LYS 429  
430  1 Y 1 A LEU 430  ? A LEU 430  
431  1 Y 1 A GLN 431  ? A GLN 431  
432  1 Y 1 A VAL 432  ? A VAL 432  
433  1 Y 1 A LEU 433  ? A LEU 433  
434  1 Y 1 A LEU 434  ? A LEU 434  
435  1 Y 1 A ARG 435  ? A ARG 435  
436  1 Y 1 A ASP 436  ? A ASP 436  
437  1 Y 1 A ILE 437  ? A ILE 437  
438  1 Y 1 A VAL 438  ? A VAL 438  
439  1 Y 1 A LYS 439  ? A LYS 439  
440  1 Y 1 A ARG 440  ? A ARG 440  
441  1 Y 1 A LYS 441  ? A LYS 441  
442  1 Y 1 A ARG 442  ? A ARG 442  
443  1 Y 1 A GLU 443  ? A GLU 443  
444  1 Y 1 A GLU 444  ? A GLU 444  
445  1 Y 1 A ASN 445  ? A ASN 445  
446  1 Y 1 A LEU 446  ? A LEU 446  
447  1 Y 1 A LYS 447  ? A LYS 447  
448  1 Y 1 A MET 448  ? A MET 448  
449  1 Y 1 A VAL 449  ? A VAL 449  
450  1 Y 1 A TRP 450  ? A TRP 450  
451  1 Y 1 A ARG 451  ? A ARG 451  
452  1 Y 1 A ILE 452  ? A ILE 452  
453  1 Y 1 A ASN 453  ? A ASN 453  
454  1 Y 1 A PRO 454  ? A PRO 454  
455  1 Y 1 A ALA 455  ? A ALA 455  
456  1 Y 1 A HIS 456  ? A HIS 456  
457  1 Y 1 A ARG 457  ? A ARG 457  
458  1 Y 1 A LYS 458  ? A LYS 458  
459  1 Y 1 A LEU 459  ? A LEU 459  
460  1 Y 1 A GLN 460  ? A GLN 460  
461  1 Y 1 A ALA 461  ? A ALA 461  
462  1 Y 1 A ARG 462  ? A ARG 462  
463  1 Y 1 A LEU 463  ? A LEU 463  
464  1 Y 1 A ASP 464  ? A ASP 464  
465  1 Y 1 A GLN 465  ? A GLN 465  
466  1 Y 1 A MET 466  ? A MET 466  
467  1 Y 1 A ARG 467  ? A ARG 467  
468  1 Y 1 A LYS 468  ? A LYS 468  
469  1 Y 1 A PHE 469  ? A PHE 469  
470  1 Y 1 A ARG 470  ? A ARG 470  
471  1 Y 1 A ARG 471  ? A ARG 471  
472  1 Y 1 A GLN 472  ? A GLN 472  
473  1 Y 1 A HIS 473  ? A HIS 473  
474  1 Y 1 A GLU 474  ? A GLU 474  
475  1 Y 1 A GLN 475  ? A GLN 475  
476  1 Y 1 A LEU 476  ? A LEU 476  
477  1 Y 1 A ARG 477  ? A ARG 477  
478  1 Y 1 A ALA 478  ? A ALA 478  
479  1 Y 1 A VAL 479  ? A VAL 479  
480  1 Y 1 A ILE 480  ? A ILE 480  
481  1 Y 1 A VAL 481  ? A VAL 481  
482  1 Y 1 A ARG 482  ? A ARG 482  
483  1 Y 1 A VAL 483  ? A VAL 483  
484  1 Y 1 A LEU 484  ? A LEU 484  
485  1 Y 1 A ARG 485  ? A ARG 485  
486  1 Y 1 A PRO 486  ? A PRO 486  
487  1 Y 1 A GLN 487  ? A GLN 487  
488  1 Y 1 A VAL 488  ? A VAL 488  
489  1 Y 1 A THR 489  ? A THR 489  
490  1 Y 1 A ALA 490  ? A ALA 490  
491  1 Y 1 A VAL 491  ? A VAL 491  
492  1 Y 1 A ALA 492  ? A ALA 492  
493  1 Y 1 A GLN 493  ? A GLN 493  
494  1 Y 1 A GLN 494  ? A GLN 494  
495  1 Y 1 A ASN 495  ? A ASN 495  
496  1 Y 1 A GLN 496  ? A GLN 496  
497  1 Y 1 A GLY 497  ? A GLY 497  
498  1 Y 1 A GLU 498  ? A GLU 498  
499  1 Y 1 A VAL 499  ? A VAL 499  
500  1 Y 1 A PRO 500  ? A PRO 500  
501  1 Y 1 A GLU 501  ? A GLU 501  
502  1 Y 1 A PRO 502  ? A PRO 502  
503  1 Y 1 A GLN 503  ? A GLN 503  
504  1 Y 1 A ASP 504  ? A ASP 504  
505  1 Y 1 A MET 505  ? A MET 505  
506  1 Y 1 A LYS 506  ? A LYS 506  
507  1 Y 1 A VAL 507  ? A VAL 507  
508  1 Y 1 A ALA 508  ? A ALA 508  
509  1 Y 1 A GLU 509  ? A GLU 509  
510  1 Y 1 A VAL 510  ? A VAL 510  
511  1 Y 1 A LEU 511  ? A LEU 511  
512  1 Y 1 A PHE 512  ? A PHE 512  
513  1 Y 1 A ASP 513  ? A ASP 513  
514  1 Y 1 A ALA 514  ? A ALA 514  
515  1 Y 1 A ALA 515  ? A ALA 515  
516  1 Y 1 A ASP 516  ? A ASP 516  
517  1 Y 1 A ALA 517  ? A ALA 517  
518  1 Y 1 A ASN 518  ? A ASN 518  
519  1 Y 1 A ALA 519  ? A ALA 519  
520  1 Y 1 A ILE 520  ? A ILE 520  
521  1 Y 1 A GLU 521  ? A GLU 521  
522  1 Y 1 A GLU 522  ? A GLU 522  
523  1 Y 1 A VAL 523  ? A VAL 523  
524  1 Y 1 A ASN 524  ? A ASN 524  
525  1 Y 1 A LEU 525  ? A LEU 525  
526  1 Y 1 A ALA 526  ? A ALA 526  
527  1 Y 1 A TYR 527  ? A TYR 527  
528  1 Y 1 A GLU 528  ? A GLU 528  
529  1 Y 1 A ASN 529  ? A ASN 529  
530  1 Y 1 A VAL 530  ? A VAL 530  
531  1 Y 1 A LYS 531  ? A LYS 531  
532  1 Y 1 A GLU 532  ? A GLU 532  
533  1 Y 1 A VAL 533  ? A VAL 533  
534  1 Y 1 A ASP 534  ? A ASP 534  
535  1 Y 1 A GLY 535  ? A GLY 535  
536  1 Y 1 A LEU 536  ? A LEU 536  
537  1 Y 1 A ASP 537  ? A ASP 537  
538  1 Y 1 A VAL 538  ? A VAL 538  
539  1 Y 1 A SER 539  ? A SER 539  
540  1 Y 1 A LYS 540  ? A LYS 540  
541  1 Y 1 A GLU 541  ? A GLU 541  
542  1 Y 1 A GLY 542  ? A GLY 542  
543  1 Y 1 A THR 543  ? A THR 543  
544  1 Y 1 A GLU 544  ? A GLU 544  
545  1 Y 1 A ALA 545  ? A ALA 545  
546  1 Y 1 A TRP 546  ? A TRP 546  
547  1 Y 1 A GLU 547  ? A GLU 547  
548  1 Y 1 A ALA 548  ? A ALA 548  
549  1 Y 1 A ALA 549  ? A ALA 549  
550  1 Y 1 A MET 550  ? A MET 550  
551  1 Y 1 A LYS 551  ? A LYS 551  
552  1 Y 1 A ARG 552  ? A ARG 552  
553  1 Y 1 A TYR 553  ? A TYR 553  
554  1 Y 1 A ASP 554  ? A ASP 554  
555  1 Y 1 A GLU 555  ? A GLU 555  
556  1 Y 1 A ARG 556  ? A ARG 556  
557  1 Y 1 A ILE 557  ? A ILE 557  
558  1 Y 1 A ASP 558  ? A ASP 558  
559  1 Y 1 A ARG 559  ? A ARG 559  
560  1 Y 1 A VAL 560  ? A VAL 560  
561  1 Y 1 A GLU 561  ? A GLU 561  
562  1 Y 1 A THR 562  ? A THR 562  
563  1 Y 1 A ARG 563  ? A ARG 563  
564  1 Y 1 A ILE 564  ? A ILE 564  
565  1 Y 1 A THR 565  ? A THR 565  
566  1 Y 1 A ALA 566  ? A ALA 566  
567  1 Y 1 A ARG 567  ? A ARG 567  
568  1 Y 1 A LEU 568  ? A LEU 568  
569  1 Y 1 A ARG 569  ? A ARG 569  
570  1 Y 1 A ASP 570  ? A ASP 570  
571  1 Y 1 A GLN 571  ? A GLN 571  
572  1 Y 1 A LEU 572  ? A LEU 572  
573  1 Y 1 A GLY 573  ? A GLY 573  
574  1 Y 1 A THR 574  ? A THR 574  
575  1 Y 1 A ALA 575  ? A ALA 575  
576  1 Y 1 A LYS 576  ? A LYS 576  
577  1 Y 1 A ASN 577  ? A ASN 577  
578  1 Y 1 A ALA 578  ? A ALA 578  
579  1 Y 1 A ASN 579  ? A ASN 579  
580  1 Y 1 A GLU 580  ? A GLU 580  
581  1 Y 1 A MET 581  ? A MET 581  
582  1 Y 1 A PHE 582  ? A PHE 582  
583  1 Y 1 A ARG 583  ? A ARG 583  
584  1 Y 1 A ILE 584  ? A ILE 584  
585  1 Y 1 A PHE 585  ? A PHE 585  
586  1 Y 1 A SER 586  ? A SER 586  
587  1 Y 1 A ARG 587  ? A ARG 587  
588  1 Y 1 A PHE 588  ? A PHE 588  
589  1 Y 1 A ASN 589  ? A ASN 589  
590  1 Y 1 A ALA 590  ? A ALA 590  
591  1 Y 1 A LEU 591  ? A LEU 591  
592  1 Y 1 A PHE 592  ? A PHE 592  
593  1 Y 1 A VAL 593  ? A VAL 593  
594  1 Y 1 A ARG 594  ? A ARG 594  
595  1 Y 1 A PRO 595  ? A PRO 595  
596  1 Y 1 A HIS 596  ? A HIS 596  
597  1 Y 1 A ILE 597  ? A ILE 597  
598  1 Y 1 A ARG 598  ? A ARG 598  
599  1 Y 1 A GLY 599  ? A GLY 599  
600  1 Y 1 A ALA 600  ? A ALA 600  
601  1 Y 1 A ILE 601  ? A ILE 601  
602  1 Y 1 A ARG 602  ? A ARG 602  
603  1 Y 1 A GLU 603  ? A GLU 603  
604  1 Y 1 A TYR 604  ? A TYR 604  
605  1 Y 1 A GLN 605  ? A GLN 605  
606  1 Y 1 A THR 606  ? A THR 606  
607  1 Y 1 A GLN 607  ? A GLN 607  
608  1 Y 1 A LEU 608  ? A LEU 608  
609  1 Y 1 A ILE 609  ? A ILE 609  
610  1 Y 1 A GLN 610  ? A GLN 610  
611  1 Y 1 A ARG 611  ? A ARG 611  
612  1 Y 1 A VAL 612  ? A VAL 612  
613  1 Y 1 A LYS 613  ? A LYS 613  
614  1 Y 1 A ASP 614  ? A ASP 614  
615  1 Y 1 A ASP 615  ? A ASP 615  
616  1 Y 1 A ILE 616  ? A ILE 616  
617  1 Y 1 A GLU 617  ? A GLU 617  
618  1 Y 1 A SER 618  ? A SER 618  
619  1 Y 1 A LEU 619  ? A LEU 619  
620  1 Y 1 A HIS 620  ? A HIS 620  
621  1 Y 1 A ASP 621  ? A ASP 621  
622  1 Y 1 A LYS 622  ? A LYS 622  
623  1 Y 1 A PHE 623  ? A PHE 623  
624  1 Y 1 A LYS 624  ? A LYS 624  
625  1 Y 1 A VAL 625  ? A VAL 625  
626  1 Y 1 A GLN 626  ? A GLN 626  
627  1 Y 1 A TYR 627  ? A TYR 627  
628  1 Y 1 A PRO 628  ? A PRO 628  
629  1 Y 1 A GLN 629  ? A GLN 629  
630  1 Y 1 A SER 630  ? A SER 630  
631  1 Y 1 A GLN 631  ? A GLN 631  
632  1 Y 1 A ALA 632  ? A ALA 632  
633  1 Y 1 A CYS 633  ? A CYS 633  
634  1 Y 1 A LYS 634  ? A LYS 634  
635  1 Y 1 A MET 635  ? A MET 635  
636  1 Y 1 A SER 636  ? A SER 636  
637  1 Y 1 A HIS 637  ? A HIS 637  
638  1 Y 1 A VAL 638  ? A VAL 638  
639  1 Y 1 A ARG 639  ? A ARG 639  
640  1 Y 1 A ASP 640  ? A ASP 640  
641  1 Y 1 A LEU 641  ? A LEU 641  
642  1 Y 1 A PRO 642  ? A PRO 642  
643  1 Y 1 A PRO 643  ? A PRO 643  
644  1 Y 1 A VAL 644  ? A VAL 644  
645  1 Y 1 A SER 645  ? A SER 645  
646  1 Y 1 A GLY 646  ? A GLY 646  
647  1 Y 1 A SER 647  ? A SER 647  
648  1 Y 1 A ILE 648  ? A ILE 648  
649  1 Y 1 A ILE 649  ? A ILE 649  
650  1 Y 1 A TRP 650  ? A TRP 650  
651  1 Y 1 A ALA 651  ? A ALA 651  
652  1 Y 1 A LYS 652  ? A LYS 652  
653  1 Y 1 A GLN 653  ? A GLN 653  
654  1 Y 1 A ILE 654  ? A ILE 654  
655  1 Y 1 A ASP 655  ? A ASP 655  
656  1 Y 1 A ARG 656  ? A ARG 656  
657  1 Y 1 A GLN 657  ? A GLN 657  
658  1 Y 1 A LEU 658  ? A LEU 658  
659  1 Y 1 A THR 659  ? A THR 659  
660  1 Y 1 A ALA 660  ? A ALA 660  
661  1 Y 1 A TYR 661  ? A TYR 661  
662  1 Y 1 A MET 662  ? A MET 662  
663  1 Y 1 A LYS 663  ? A LYS 663  
664  1 Y 1 A ARG 664  ? A ARG 664  
665  1 Y 1 A VAL 665  ? A VAL 665  
666  1 Y 1 A GLU 666  ? A GLU 666  
667  1 Y 1 A ASP 667  ? A ASP 667  
668  1 Y 1 A VAL 668  ? A VAL 668  
669  1 Y 1 A LEU 669  ? A LEU 669  
670  1 Y 1 A GLY 670  ? A GLY 670  
671  1 Y 1 A LYS 671  ? A LYS 671  
672  1 Y 1 A GLY 672  ? A GLY 672  
673  1 Y 1 A TRP 673  ? A TRP 673  
674  1 Y 1 A GLU 674  ? A GLU 674  
675  1 Y 1 A ASN 675  ? A ASN 675  
676  1 Y 1 A HIS 676  ? A HIS 676  
677  1 Y 1 A VAL 677  ? A VAL 677  
678  1 Y 1 A GLU 678  ? A GLU 678  
679  1 Y 1 A GLY 679  ? A GLY 679  
680  1 Y 1 A GLN 680  ? A GLN 680  
681  1 Y 1 A LYS 681  ? A LYS 681  
682  1 Y 1 A LEU 682  ? A LEU 682  
683  1 Y 1 A LYS 683  ? A LYS 683  
684  1 Y 1 A GLN 684  ? A GLN 684  
685  1 Y 1 A ASP 685  ? A ASP 685  
686  1 Y 1 A GLY 686  ? A GLY 686  
687  1 Y 1 A ASP 687  ? A ASP 687  
688  1 Y 1 A SER 688  ? A SER 688  
689  1 Y 1 A PHE 689  ? A PHE 689  
690  1 Y 1 A ARG 690  ? A ARG 690  
691  1 Y 1 A MET 691  ? A MET 691  
692  1 Y 1 A LYS 692  ? A LYS 692  
693  1 Y 1 A LEU 693  ? A LEU 693  
694  1 Y 1 A ASN 694  ? A ASN 694  
695  1 Y 1 A THR 695  ? A THR 695  
696  1 Y 1 A GLN 696  ? A GLN 696  
697  1 Y 1 A GLU 697  ? A GLU 697  
698  1 Y 1 A ILE 698  ? A ILE 698  
699  1 Y 1 A PHE 699  ? A PHE 699  
700  1 Y 1 A ASP 700  ? A ASP 700  
701  1 Y 1 A ASP 701  ? A ASP 701  
702  1 Y 1 A TRP 702  ? A TRP 702  
703  1 Y 1 A ALA 703  ? A ALA 703  
704  1 Y 1 A ARG 704  ? A ARG 704  
705  1 Y 1 A LYS 705  ? A LYS 705  
706  1 Y 1 A VAL 706  ? A VAL 706  
707  1 Y 1 A GLN 707  ? A GLN 707  
708  1 Y 1 A GLN 708  ? A GLN 708  
709  1 Y 1 A ARG 709  ? A ARG 709  
710  1 Y 1 A ASN 710  ? A ASN 710  
711  1 Y 1 A LEU 711  ? A LEU 711  
712  1 Y 1 A GLY 712  ? A GLY 712  
713  1 Y 1 A VAL 713  ? A VAL 713  
714  1 Y 1 A SER 714  ? A SER 714  
715  1 Y 1 A GLY 715  ? A GLY 715  
716  1 Y 1 A ARG 716  ? A ARG 716  
717  1 Y 1 A ILE 717  ? A ILE 717  
718  1 Y 1 A PHE 718  ? A PHE 718  
719  1 Y 1 A THR 719  ? A THR 719  
720  1 Y 1 A ILE 720  ? A ILE 720  
721  1 Y 1 A GLU 721  ? A GLU 721  
722  1 Y 1 A SER 722  ? A SER 722  
723  1 Y 1 A THR 723  ? A THR 723  
724  1 Y 1 A ARG 724  ? A ARG 724  
725  1 Y 1 A VAL 725  ? A VAL 725  
726  1 Y 1 A ARG 726  ? A ARG 726  
727  1 Y 1 A GLY 727  ? A GLY 727  
728  1 Y 1 A ARG 728  ? A ARG 728  
729  1 Y 1 A THR 729  ? A THR 729  
730  1 Y 1 A GLY 730  ? A GLY 730  
731  1 Y 1 A ASN 731  ? A ASN 731  
732  1 Y 1 A VAL 732  ? A VAL 732  
733  1 Y 1 A LEU 733  ? A LEU 733  
734  1 Y 1 A LYS 734  ? A LYS 734  
735  1 Y 1 A LEU 735  ? A LEU 735  
736  1 Y 1 A LYS 736  ? A LYS 736  
737  1 Y 1 A VAL 737  ? A VAL 737  
738  1 Y 1 A ASN 738  ? A ASN 738  
739  1 Y 1 A PHE 739  ? A PHE 739  
740  1 Y 1 A LEU 740  ? A LEU 740  
741  1 Y 1 A PRO 741  ? A PRO 741  
742  1 Y 1 A GLU 742  ? A GLU 742  
743  1 Y 1 A ILE 743  ? A ILE 743  
744  1 Y 1 A ILE 744  ? A ILE 744  
745  1 Y 1 A THR 745  ? A THR 745  
746  1 Y 1 A LEU 746  ? A LEU 746  
747  1 Y 1 A SER 747  ? A SER 747  
748  1 Y 1 A LYS 748  ? A LYS 748  
749  1 Y 1 A GLU 749  ? A GLU 749  
750  1 Y 1 A VAL 750  ? A VAL 750  
751  1 Y 1 A ARG 751  ? A ARG 751  
752  1 Y 1 A ASN 752  ? A ASN 752  
753  1 Y 1 A LEU 753  ? A LEU 753  
754  1 Y 1 A LYS 754  ? A LYS 754  
755  1 Y 1 A TRP 755  ? A TRP 755  
756  1 Y 1 A LEU 756  ? A LEU 756  
757  1 Y 1 A GLY 757  ? A GLY 757  
758  1 Y 1 A PHE 758  ? A PHE 758  
759  1 Y 1 A ARG 759  ? A ARG 759  
760  1 Y 1 A VAL 760  ? A VAL 760  
761  1 Y 1 A PRO 761  ? A PRO 761  
762  1 Y 1 A LEU 762  ? A LEU 762  
763  1 Y 1 A ALA 763  ? A ALA 763  
764  1 Y 1 A ILE 764  ? A ILE 764  
765  1 Y 1 A VAL 765  ? A VAL 765  
766  1 Y 1 A ASN 766  ? A ASN 766  
767  1 Y 1 A LYS 767  ? A LYS 767  
768  1 Y 1 A ALA 768  ? A ALA 768  
769  1 Y 1 A HIS 769  ? A HIS 769  
770  1 Y 1 A GLN 770  ? A GLN 770  
771  1 Y 1 A ALA 771  ? A ALA 771  
772  1 Y 1 A ASN 772  ? A ASN 772  
773  1 Y 1 A GLN 773  ? A GLN 773  
774  1 Y 1 A LEU 774  ? A LEU 774  
775  1 Y 1 A TYR 775  ? A TYR 775  
776  1 Y 1 A PRO 776  ? A PRO 776  
777  1 Y 1 A PHE 777  ? A PHE 777  
778  1 Y 1 A ALA 778  ? A ALA 778  
779  1 Y 1 A ILE 779  ? A ILE 779  
780  1 Y 1 A SER 780  ? A SER 780  
781  1 Y 1 A LEU 781  ? A LEU 781  
782  1 Y 1 A ILE 782  ? A ILE 782  
783  1 Y 1 A GLU 783  ? A GLU 783  
784  1 Y 1 A SER 784  ? A SER 784  
785  1 Y 1 A VAL 785  ? A VAL 785  
786  1 Y 1 A ARG 786  ? A ARG 786  
787  1 Y 1 A THR 787  ? A THR 787  
788  1 Y 1 A TYR 788  ? A TYR 788  
789  1 Y 1 A GLU 789  ? A GLU 789  
790  1 Y 1 A ARG 790  ? A ARG 790  
791  1 Y 1 A THR 791  ? A THR 791  
792  1 Y 1 A CYS 792  ? A CYS 792  
793  1 Y 1 A GLU 793  ? A GLU 793  
794  1 Y 1 A LYS 794  ? A LYS 794  
795  1 Y 1 A VAL 795  ? A VAL 795  
796  1 Y 1 A GLU 796  ? A GLU 796  
797  1 Y 1 A GLU 797  ? A GLU 797  
798  1 Y 1 A ARG 798  ? A ARG 798  
799  1 Y 1 A ASN 799  ? A ASN 799  
800  1 Y 1 A THR 800  ? A THR 800  
801  1 Y 1 A ILE 801  ? A ILE 801  
802  1 Y 1 A SER 802  ? A SER 802  
803  1 Y 1 A LEU 803  ? A LEU 803  
804  1 Y 1 A LEU 804  ? A LEU 804  
805  1 Y 1 A VAL 805  ? A VAL 805  
806  1 Y 1 A ALA 806  ? A ALA 806  
807  1 Y 1 A GLY 807  ? A GLY 807  
808  1 Y 1 A LEU 808  ? A LEU 808  
809  1 Y 1 A LYS 809  ? A LYS 809  
810  1 Y 1 A LYS 810  ? A LYS 810  
811  1 Y 1 A GLU 811  ? A GLU 811  
812  1 Y 1 A VAL 812  ? A VAL 812  
813  1 Y 1 A GLN 813  ? A GLN 813  
814  1 Y 1 A ALA 814  ? A ALA 814  
815  1 Y 1 A LEU 815  ? A LEU 815  
816  1 Y 1 A ILE 816  ? A ILE 816  
817  1 Y 1 A ALA 817  ? A ALA 817  
818  1 Y 1 A GLU 818  ? A GLU 818  
819  1 Y 1 A GLY 819  ? A GLY 819  
820  1 Y 1 A ILE 820  ? A ILE 820  
821  1 Y 1 A ALA 821  ? A ALA 821  
822  1 Y 1 A LEU 822  ? A LEU 822  
823  1 Y 1 A VAL 823  ? A VAL 823  
824  1 Y 1 A TRP 824  ? A TRP 824  
825  1 Y 1 A GLU 825  ? A GLU 825  
826  1 Y 1 A SER 826  ? A SER 826  
827  1 Y 1 A TYR 827  ? A TYR 827  
828  1 Y 1 A LYS 828  ? A LYS 828  
829  1 Y 1 A LEU 829  ? A LEU 829  
830  1 Y 1 A ASP 830  ? A ASP 830  
831  1 Y 1 A PRO 831  ? A PRO 831  
832  1 Y 1 A TYR 832  ? A TYR 832  
833  1 Y 1 A VAL 833  ? A VAL 833  
834  1 Y 1 A GLN 834  ? A GLN 834  
835  1 Y 1 A ARG 835  ? A ARG 835  
836  1 Y 1 A LEU 836  ? A LEU 836  
837  1 Y 1 A ALA 837  ? A ALA 837  
838  1 Y 1 A GLU 838  ? A GLU 838  
839  1 Y 1 A THR 839  ? A THR 839  
840  1 Y 1 A VAL 840  ? A VAL 840  
841  1 Y 1 A PHE 841  ? A PHE 841  
842  1 Y 1 A ASN 842  ? A ASN 842  
843  1 Y 1 A PHE 843  ? A PHE 843  
844  1 Y 1 A GLN 844  ? A GLN 844  
845  1 Y 1 A GLU 845  ? A GLU 845  
846  1 Y 1 A LYS 846  ? A LYS 846  
847  1 Y 1 A VAL 847  ? A VAL 847  
848  1 Y 1 A ASP 848  ? A ASP 848  
849  1 Y 1 A ASP 849  ? A ASP 849  
850  1 Y 1 A LEU 850  ? A LEU 850  
851  1 Y 1 A LEU 851  ? A LEU 851  
852  1 Y 1 A ILE 852  ? A ILE 852  
853  1 Y 1 A ILE 853  ? A ILE 853  
854  1 Y 1 A GLU 854  ? A GLU 854  
855  1 Y 1 A GLU 855  ? A GLU 855  
856  1 Y 1 A LYS 856  ? A LYS 856  
857  1 Y 1 A ILE 857  ? A ILE 857  
858  1 Y 1 A ASP 858  ? A ASP 858  
859  1 Y 1 A LEU 859  ? A LEU 859  
860  1 Y 1 A GLU 860  ? A GLU 860  
861  1 Y 1 A VAL 861  ? A VAL 861  
862  1 Y 1 A ARG 862  ? A ARG 862  
863  1 Y 1 A SER 863  ? A SER 863  
864  1 Y 1 A LEU 864  ? A LEU 864  
865  1 Y 1 A GLU 865  ? A GLU 865  
866  1 Y 1 A THR 866  ? A THR 866  
867  1 Y 1 A CYS 867  ? A CYS 867  
868  1 Y 1 A MET 868  ? A MET 868  
869  1 Y 1 A TYR 869  ? A TYR 869  
870  1 Y 1 A ASP 870  ? A ASP 870  
871  1 Y 1 A HIS 871  ? A HIS 871  
872  1 Y 1 A LYS 872  ? A LYS 872  
873  1 Y 1 A THR 873  ? A THR 873  
874  1 Y 1 A PHE 874  ? A PHE 874  
875  1 Y 1 A SER 875  ? A SER 875  
876  1 Y 1 A GLU 876  ? A GLU 876  
877  1 Y 1 A ILE 877  ? A ILE 877  
878  1 Y 1 A LEU 878  ? A LEU 878  
879  1 Y 1 A ASN 879  ? A ASN 879  
880  1 Y 1 A ARG 880  ? A ARG 880  
881  1 Y 1 A VAL 881  ? A VAL 881  
882  1 Y 1 A GLN 882  ? A GLN 882  
883  1 Y 1 A LYS 883  ? A LYS 883  
884  1 Y 1 A ALA 884  ? A ALA 884  
885  1 Y 1 A VAL 885  ? A VAL 885  
886  1 Y 1 A ASP 886  ? A ASP 886  
887  1 Y 1 A ASP 887  ? A ASP 887  
888  1 Y 1 A LEU 888  ? A LEU 888  
889  1 Y 1 A ASN 889  ? A ASN 889  
890  1 Y 1 A LEU 890  ? A LEU 890  
891  1 Y 1 A HIS 891  ? A HIS 891  
892  1 Y 1 A SER 892  ? A SER 892  
893  1 Y 1 A TYR 893  ? A TYR 893  
894  1 Y 1 A SER 894  ? A SER 894  
895  1 Y 1 A ASN 895  ? A ASN 895  
896  1 Y 1 A LEU 896  ? A LEU 896  
897  1 Y 1 A PRO 897  ? A PRO 897  
898  1 Y 1 A ILE 898  ? A ILE 898  
899  1 Y 1 A TRP 899  ? A TRP 899  
900  1 Y 1 A VAL 900  ? A VAL 900  
901  1 Y 1 A ASN 901  ? A ASN 901  
902  1 Y 1 A LYS 902  ? A LYS 902  
903  1 Y 1 A LEU 903  ? A LEU 903  
904  1 Y 1 A ASP 904  ? A ASP 904  
905  1 Y 1 A MET 905  ? A MET 905  
906  1 Y 1 A GLU 906  ? A GLU 906  
907  1 Y 1 A ILE 907  ? A ILE 907  
908  1 Y 1 A GLU 908  ? A GLU 908  
909  1 Y 1 A ARG 909  ? A ARG 909  
910  1 Y 1 A ILE 910  ? A ILE 910  
911  1 Y 1 A LEU 911  ? A LEU 911  
912  1 Y 1 A GLY 912  ? A GLY 912  
913  1 Y 1 A VAL 913  ? A VAL 913  
914  1 Y 1 A ARG 914  ? A ARG 914  
915  1 Y 1 A LEU 915  ? A LEU 915  
916  1 Y 1 A GLN 916  ? A GLN 916  
917  1 Y 1 A ALA 917  ? A ALA 917  
918  1 Y 1 A GLY 918  ? A GLY 918  
919  1 Y 1 A LEU 919  ? A LEU 919  
920  1 Y 1 A ARG 920  ? A ARG 920  
921  1 Y 1 A ALA 921  ? A ALA 921  
922  1 Y 1 A TRP 922  ? A TRP 922  
923  1 Y 1 A THR 923  ? A THR 923  
924  1 Y 1 A GLN 924  ? A GLN 924  
925  1 Y 1 A VAL 925  ? A VAL 925  
926  1 Y 1 A LEU 926  ? A LEU 926  
927  1 Y 1 A LEU 927  ? A LEU 927  
928  1 Y 1 A GLY 928  ? A GLY 928  
929  1 Y 1 A GLN 929  ? A GLN 929  
930  1 Y 1 A ALA 930  ? A ALA 930  
931  1 Y 1 A GLU 931  ? A GLU 931  
932  1 Y 1 A ASP 932  ? A ASP 932  
933  1 Y 1 A LYS 933  ? A LYS 933  
934  1 Y 1 A ALA 934  ? A ALA 934  
935  1 Y 1 A GLU 935  ? A GLU 935  
936  1 Y 1 A VAL 936  ? A VAL 936  
937  1 Y 1 A ASP 937  ? A ASP 937  
938  1 Y 1 A MET 938  ? A MET 938  
939  1 Y 1 A ASP 939  ? A ASP 939  
940  1 Y 1 A THR 940  ? A THR 940  
941  1 Y 1 A ASP 941  ? A ASP 941  
942  1 Y 1 A ALA 942  ? A ALA 942  
943  1 Y 1 A PRO 943  ? A PRO 943  
944  1 Y 1 A GLN 944  ? A GLN 944  
945  1 Y 1 A VAL 945  ? A VAL 945  
946  1 Y 1 A SER 946  ? A SER 946  
947  1 Y 1 A HIS 947  ? A HIS 947  
948  1 Y 1 A LYS 948  ? A LYS 948  
949  1 Y 1 A PRO 949  ? A PRO 949  
950  1 Y 1 A GLY 950  ? A GLY 950  
951  1 Y 1 A GLY 951  ? A GLY 951  
952  1 Y 1 A GLU 952  ? A GLU 952  
953  1 Y 1 A PRO 953  ? A PRO 953  
954  1 Y 1 A LYS 954  ? A LYS 954  
955  1 Y 1 A ILE 955  ? A ILE 955  
956  1 Y 1 A LYS 956  ? A LYS 956  
957  1 Y 1 A ASN 957  ? A ASN 957  
958  1 Y 1 A VAL 958  ? A VAL 958  
959  1 Y 1 A VAL 959  ? A VAL 959  
960  1 Y 1 A HIS 960  ? A HIS 960  
961  1 Y 1 A GLU 961  ? A GLU 961  
962  1 Y 1 A LEU 962  ? A LEU 962  
963  1 Y 1 A ARG 963  ? A ARG 963  
964  1 Y 1 A ILE 964  ? A ILE 964  
965  1 Y 1 A THR 965  ? A THR 965  
966  1 Y 1 A ASN 966  ? A ASN 966  
967  1 Y 1 A GLN 967  ? A GLN 967  
968  1 Y 1 A VAL 968  ? A VAL 968  
969  1 Y 1 A ILE 969  ? A ILE 969  
970  1 Y 1 A TYR 970  ? A TYR 970  
971  1 Y 1 A LEU 971  ? A LEU 971  
972  1 Y 1 A ASN 972  ? A ASN 972  
973  1 Y 1 A PRO 973  ? A PRO 973  
974  1 Y 1 A PRO 974  ? A PRO 974  
975  1 Y 1 A ILE 975  ? A ILE 975  
976  1 Y 1 A GLU 976  ? A GLU 976  
977  1 Y 1 A GLU 977  ? A GLU 977  
978  1 Y 1 A CYS 978  ? A CYS 978  
979  1 Y 1 A ARG 979  ? A ARG 979  
980  1 Y 1 A TYR 980  ? A TYR 980  
981  1 Y 1 A LYS 981  ? A LYS 981  
982  1 Y 1 A LEU 982  ? A LEU 982  
983  1 Y 1 A TYR 983  ? A TYR 983  
984  1 Y 1 A GLN 984  ? A GLN 984  
985  1 Y 1 A GLU 985  ? A GLU 985  
986  1 Y 1 A MET 986  ? A MET 986  
987  1 Y 1 A PHE 987  ? A PHE 987  
988  1 Y 1 A ALA 988  ? A ALA 988  
989  1 Y 1 A TRP 989  ? A TRP 989  
990  1 Y 1 A LYS 990  ? A LYS 990  
991  1 Y 1 A MET 991  ? A MET 991  
992  1 Y 1 A VAL 992  ? A VAL 992  
993  1 Y 1 A VAL 993  ? A VAL 993  
994  1 Y 1 A LEU 994  ? A LEU 994  
995  1 Y 1 A SER 995  ? A SER 995  
996  1 Y 1 A LEU 996  ? A LEU 996  
997  1 Y 1 A PRO 997  ? A PRO 997  
998  1 Y 1 A ARG 998  ? A ARG 998  
999  1 Y 1 A ILE 999  ? A ILE 999  
1000 1 Y 1 A GLN 1000 ? A GLN 1000 
1001 1 Y 1 A SER 1001 ? A SER 1001 
1002 1 Y 1 A GLN 1002 ? A GLN 1002 
1003 1 Y 1 A ARG 1003 ? A ARG 1003 
1004 1 Y 1 A TYR 1004 ? A TYR 1004 
1005 1 Y 1 A GLN 1005 ? A GLN 1005 
1006 1 Y 1 A VAL 1006 ? A VAL 1006 
1007 1 Y 1 A GLY 1007 ? A GLY 1007 
1008 1 Y 1 A VAL 1008 ? A VAL 1008 
1009 1 Y 1 A HIS 1009 ? A HIS 1009 
1010 1 Y 1 A TYR 1010 ? A TYR 1010 
1011 1 Y 1 A GLU 1011 ? A GLU 1011 
1012 1 Y 1 A LEU 1012 ? A LEU 1012 
1013 1 Y 1 A THR 1013 ? A THR 1013 
1014 1 Y 1 A GLU 1014 ? A GLU 1014 
1015 1 Y 1 A GLU 1015 ? A GLU 1015 
1016 1 Y 1 A GLU 1016 ? A GLU 1016 
1017 1 Y 1 A LYS 1017 ? A LYS 1017 
1018 1 Y 1 A PHE 1018 ? A PHE 1018 
1019 1 Y 1 A TYR 1019 ? A TYR 1019 
1020 1 Y 1 A ARG 1020 ? A ARG 1020 
1021 1 Y 1 A ASN 1021 ? A ASN 1021 
1022 1 Y 1 A ALA 1022 ? A ALA 1022 
1023 1 Y 1 A LEU 1023 ? A LEU 1023 
1024 1 Y 1 A THR 1024 ? A THR 1024 
1025 1 Y 1 A ARG 1025 ? A ARG 1025 
1026 1 Y 1 A MET 1026 ? A MET 1026 
1027 1 Y 1 A PRO 1027 ? A PRO 1027 
1028 1 Y 1 A ASP 1028 ? A ASP 1028 
1029 1 Y 1 A GLY 1029 ? A GLY 1029 
1030 1 Y 1 A PRO 1030 ? A PRO 1030 
1031 1 Y 1 A VAL 1031 ? A VAL 1031 
1032 1 Y 1 A ALA 1032 ? A ALA 1032 
1033 1 Y 1 A LEU 1033 ? A LEU 1033 
1034 1 Y 1 A GLU 1034 ? A GLU 1034 
1035 1 Y 1 A GLU 1035 ? A GLU 1035 
1036 1 Y 1 A SER 1036 ? A SER 1036 
1037 1 Y 1 A TYR 1037 ? A TYR 1037 
1038 1 Y 1 A SER 1038 ? A SER 1038 
1039 1 Y 1 A ALA 1039 ? A ALA 1039 
1040 1 Y 1 A VAL 1040 ? A VAL 1040 
1041 1 Y 1 A MET 1041 ? A MET 1041 
1042 1 Y 1 A GLY 1042 ? A GLY 1042 
1043 1 Y 1 A ILE 1043 ? A ILE 1043 
1044 1 Y 1 A VAL 1044 ? A VAL 1044 
1045 1 Y 1 A SER 1045 ? A SER 1045 
1046 1 Y 1 A GLU 1046 ? A GLU 1046 
1047 1 Y 1 A VAL 1047 ? A VAL 1047 
1048 1 Y 1 A GLU 1048 ? A GLU 1048 
1049 1 Y 1 A GLN 1049 ? A GLN 1049 
1050 1 Y 1 A TYR 1050 ? A TYR 1050 
1051 1 Y 1 A VAL 1051 ? A VAL 1051 
1052 1 Y 1 A LYS 1052 ? A LYS 1052 
1053 1 Y 1 A VAL 1053 ? A VAL 1053 
1054 1 Y 1 A TRP 1054 ? A TRP 1054 
1055 1 Y 1 A LEU 1055 ? A LEU 1055 
1056 1 Y 1 A GLN 1056 ? A GLN 1056 
1057 1 Y 1 A TYR 1057 ? A TYR 1057 
1058 1 Y 1 A GLN 1058 ? A GLN 1058 
1059 1 Y 1 A CYS 1059 ? A CYS 1059 
1060 1 Y 1 A LEU 1060 ? A LEU 1060 
1061 1 Y 1 A TRP 1061 ? A TRP 1061 
1062 1 Y 1 A ASP 1062 ? A ASP 1062 
1063 1 Y 1 A MET 1063 ? A MET 1063 
1064 1 Y 1 A GLN 1064 ? A GLN 1064 
1065 1 Y 1 A ALA 1065 ? A ALA 1065 
1066 1 Y 1 A GLU 1066 ? A GLU 1066 
1067 1 Y 1 A ASN 1067 ? A ASN 1067 
1068 1 Y 1 A ILE 1068 ? A ILE 1068 
1069 1 Y 1 A TYR 1069 ? A TYR 1069 
1070 1 Y 1 A ASN 1070 ? A ASN 1070 
1071 1 Y 1 A ARG 1071 ? A ARG 1071 
1072 1 Y 1 A LEU 1072 ? A LEU 1072 
1073 1 Y 1 A GLY 1073 ? A GLY 1073 
1074 1 Y 1 A GLU 1074 ? A GLU 1074 
1075 1 Y 1 A ASP 1075 ? A ASP 1075 
1076 1 Y 1 A LEU 1076 ? A LEU 1076 
1077 1 Y 1 A ASN 1077 ? A ASN 1077 
1078 1 Y 1 A LYS 1078 ? A LYS 1078 
1079 1 Y 1 A TRP 1079 ? A TRP 1079 
1080 1 Y 1 A GLN 1080 ? A GLN 1080 
1081 1 Y 1 A ALA 1081 ? A ALA 1081 
1082 1 Y 1 A LEU 1082 ? A LEU 1082 
1083 1 Y 1 A LEU 1083 ? A LEU 1083 
1084 1 Y 1 A VAL 1084 ? A VAL 1084 
1085 1 Y 1 A GLN 1085 ? A GLN 1085 
1086 1 Y 1 A ILE 1086 ? A ILE 1086 
1087 1 Y 1 A ARG 1087 ? A ARG 1087 
1088 1 Y 1 A LYS 1088 ? A LYS 1088 
1089 1 Y 1 A ALA 1089 ? A ALA 1089 
1090 1 Y 1 A ARG 1090 ? A ARG 1090 
1091 1 Y 1 A GLY 1091 ? A GLY 1091 
1092 1 Y 1 A THR 1092 ? A THR 1092 
1093 1 Y 1 A PHE 1093 ? A PHE 1093 
1094 1 Y 1 A ASP 1094 ? A ASP 1094 
1095 1 Y 1 A ASN 1095 ? A ASN 1095 
1096 1 Y 1 A ALA 1096 ? A ALA 1096 
1097 1 Y 1 A GLU 1097 ? A GLU 1097 
1098 1 Y 1 A THR 1098 ? A THR 1098 
1099 1 Y 1 A LYS 1099 ? A LYS 1099 
1100 1 Y 1 A LYS 1100 ? A LYS 1100 
1101 1 Y 1 A GLU 1101 ? A GLU 1101 
1102 1 Y 1 A PHE 1102 ? A PHE 1102 
1103 1 Y 1 A GLY 1103 ? A GLY 1103 
1104 1 Y 1 A PRO 1104 ? A PRO 1104 
1105 1 Y 1 A VAL 1105 ? A VAL 1105 
1106 1 Y 1 A VAL 1106 ? A VAL 1106 
1107 1 Y 1 A ILE 1107 ? A ILE 1107 
1108 1 Y 1 A ASP 1108 ? A ASP 1108 
1109 1 Y 1 A TYR 1109 ? A TYR 1109 
1110 1 Y 1 A GLY 1110 ? A GLY 1110 
1111 1 Y 1 A LYS 1111 ? A LYS 1111 
1112 1 Y 1 A VAL 1112 ? A VAL 1112 
1113 1 Y 1 A GLN 1113 ? A GLN 1113 
1114 1 Y 1 A SER 1114 ? A SER 1114 
1115 1 Y 1 A LYS 1115 ? A LYS 1115 
1116 1 Y 1 A VAL 1116 ? A VAL 1116 
1117 1 Y 1 A ASN 1117 ? A ASN 1117 
1118 1 Y 1 A LEU 1118 ? A LEU 1118 
1119 1 Y 1 A LYS 1119 ? A LYS 1119 
1120 1 Y 1 A TYR 1120 ? A TYR 1120 
1121 1 Y 1 A ASP 1121 ? A ASP 1121 
1122 1 Y 1 A SER 1122 ? A SER 1122 
1123 1 Y 1 A TRP 1123 ? A TRP 1123 
1124 1 Y 1 A HIS 1124 ? A HIS 1124 
1125 1 Y 1 A LYS 1125 ? A LYS 1125 
1126 1 Y 1 A GLU 1126 ? A GLU 1126 
1127 1 Y 1 A VAL 1127 ? A VAL 1127 
1128 1 Y 1 A LEU 1128 ? A LEU 1128 
1129 1 Y 1 A SER 1129 ? A SER 1129 
1130 1 Y 1 A LYS 1130 ? A LYS 1130 
1131 1 Y 1 A PHE 1131 ? A PHE 1131 
1132 1 Y 1 A GLY 1132 ? A GLY 1132 
1133 1 Y 1 A GLN 1133 ? A GLN 1133 
1134 1 Y 1 A MET 1134 ? A MET 1134 
1135 1 Y 1 A LEU 1135 ? A LEU 1135 
1136 1 Y 1 A GLY 1136 ? A GLY 1136 
1137 1 Y 1 A SER 1137 ? A SER 1137 
1138 1 Y 1 A ASN 1138 ? A ASN 1138 
1139 1 Y 1 A MET 1139 ? A MET 1139 
1140 1 Y 1 A THR 1140 ? A THR 1140 
1141 1 Y 1 A GLU 1141 ? A GLU 1141 
1142 1 Y 1 A PHE 1142 ? A PHE 1142 
1143 1 Y 1 A HIS 1143 ? A HIS 1143 
1144 1 Y 1 A SER 1144 ? A SER 1144 
1145 1 Y 1 A GLN 1145 ? A GLN 1145 
1146 1 Y 1 A ILE 1146 ? A ILE 1146 
1147 1 Y 1 A SER 1147 ? A SER 1147 
1148 1 Y 1 A LYS 1148 ? A LYS 1148 
1149 1 Y 1 A SER 1149 ? A SER 1149 
1150 1 Y 1 A ARG 1150 ? A ARG 1150 
1151 1 Y 1 A GLN 1151 ? A GLN 1151 
1152 1 Y 1 A GLU 1152 ? A GLU 1152 
1153 1 Y 1 A LEU 1153 ? A LEU 1153 
1154 1 Y 1 A GLU 1154 ? A GLU 1154 
1155 1 Y 1 A GLN 1155 ? A GLN 1155 
1156 1 Y 1 A HIS 1156 ? A HIS 1156 
1157 1 Y 1 A SER 1157 ? A SER 1157 
1158 1 Y 1 A VAL 1158 ? A VAL 1158 
1159 1 Y 1 A ASP 1159 ? A ASP 1159 
1160 1 Y 1 A THR 1160 ? A THR 1160 
1161 1 Y 1 A ALA 1161 ? A ALA 1161 
1162 1 Y 1 A SER 1162 ? A SER 1162 
1163 1 Y 1 A THR 1163 ? A THR 1163 
1164 1 Y 1 A SER 1164 ? A SER 1164 
1165 1 Y 1 A ASP 1165 ? A ASP 1165 
1166 1 Y 1 A ALA 1166 ? A ALA 1166 
1167 1 Y 1 A VAL 1167 ? A VAL 1167 
1168 1 Y 1 A THR 1168 ? A THR 1168 
1169 1 Y 1 A PHE 1169 ? A PHE 1169 
1170 1 Y 1 A ILE 1170 ? A ILE 1170 
1171 1 Y 1 A THR 1171 ? A THR 1171 
1172 1 Y 1 A TYR 1172 ? A TYR 1172 
1173 1 Y 1 A VAL 1173 ? A VAL 1173 
1174 1 Y 1 A GLN 1174 ? A GLN 1174 
1175 1 Y 1 A SER 1175 ? A SER 1175 
1176 1 Y 1 A LEU 1176 ? A LEU 1176 
1177 1 Y 1 A LYS 1177 ? A LYS 1177 
1178 1 Y 1 A ARG 1178 ? A ARG 1178 
1179 1 Y 1 A LYS 1179 ? A LYS 1179 
1180 1 Y 1 A ILE 1180 ? A ILE 1180 
1181 1 Y 1 A LYS 1181 ? A LYS 1181 
1182 1 Y 1 A GLN 1182 ? A GLN 1182 
1183 1 Y 1 A PHE 1183 ? A PHE 1183 
1184 1 Y 1 A GLU 1184 ? A GLU 1184 
1185 1 Y 1 A LYS 1185 ? A LYS 1185 
1186 1 Y 1 A GLN 1186 ? A GLN 1186 
1187 1 Y 1 A VAL 1187 ? A VAL 1187 
1188 1 Y 1 A GLU 1188 ? A GLU 1188 
1189 1 Y 1 A LEU 1189 ? A LEU 1189 
1190 1 Y 1 A TYR 1190 ? A TYR 1190 
1191 1 Y 1 A ARG 1191 ? A ARG 1191 
1192 1 Y 1 A ASN 1192 ? A ASN 1192 
1193 1 Y 1 A GLY 1193 ? A GLY 1193 
1194 1 Y 1 A GLN 1194 ? A GLN 1194 
1195 1 Y 1 A ARG 1195 ? A ARG 1195 
1196 1 Y 1 A LEU 1196 ? A LEU 1196 
1197 1 Y 1 A LEU 1197 ? A LEU 1197 
1198 1 Y 1 A GLU 1198 ? A GLU 1198 
1199 1 Y 1 A LYS 1199 ? A LYS 1199 
1200 1 Y 1 A GLN 1200 ? A GLN 1200 
1201 1 Y 1 A ARG 1201 ? A ARG 1201 
1202 1 Y 1 A PHE 1202 ? A PHE 1202 
1203 1 Y 1 A GLN 1203 ? A GLN 1203 
1204 1 Y 1 A PHE 1204 ? A PHE 1204 
1205 1 Y 1 A PRO 1205 ? A PRO 1205 
1206 1 Y 1 A PRO 1206 ? A PRO 1206 
1207 1 Y 1 A SER 1207 ? A SER 1207 
1208 1 Y 1 A TRP 1208 ? A TRP 1208 
1209 1 Y 1 A LEU 1209 ? A LEU 1209 
1210 1 Y 1 A TYR 1210 ? A TYR 1210 
1211 1 Y 1 A ILE 1211 ? A ILE 1211 
1212 1 Y 1 A ASP 1212 ? A ASP 1212 
1213 1 Y 1 A ASN 1213 ? A ASN 1213 
1214 1 Y 1 A ILE 1214 ? A ILE 1214 
1215 1 Y 1 A GLU 1215 ? A GLU 1215 
1216 1 Y 1 A GLY 1216 ? A GLY 1216 
1217 1 Y 1 A GLU 1217 ? A GLU 1217 
1218 1 Y 1 A TRP 1218 ? A TRP 1218 
1219 1 Y 1 A GLY 1219 ? A GLY 1219 
1220 1 Y 1 A ALA 1220 ? A ALA 1220 
1221 1 Y 1 A PHE 1221 ? A PHE 1221 
1222 1 Y 1 A ASN 1222 ? A ASN 1222 
1223 1 Y 1 A ASP 1223 ? A ASP 1223 
1224 1 Y 1 A ILE 1224 ? A ILE 1224 
1225 1 Y 1 A MET 1225 ? A MET 1225 
1226 1 Y 1 A ARG 1226 ? A ARG 1226 
1227 1 Y 1 A ARG 1227 ? A ARG 1227 
1228 1 Y 1 A LYS 1228 ? A LYS 1228 
1229 1 Y 1 A ASP 1229 ? A ASP 1229 
1230 1 Y 1 A SER 1230 ? A SER 1230 
1231 1 Y 1 A ALA 1231 ? A ALA 1231 
1232 1 Y 1 A ILE 1232 ? A ILE 1232 
1233 1 Y 1 A GLN 1233 ? A GLN 1233 
1234 1 Y 1 A GLN 1234 ? A GLN 1234 
1235 1 Y 1 A GLN 1235 ? A GLN 1235 
1236 1 Y 1 A VAL 1236 ? A VAL 1236 
1237 1 Y 1 A ALA 1237 ? A ALA 1237 
1238 1 Y 1 A ASN 1238 ? A ASN 1238 
1239 1 Y 1 A LEU 1239 ? A LEU 1239 
1240 1 Y 1 A GLN 1240 ? A GLN 1240 
1241 1 Y 1 A MET 1241 ? A MET 1241 
1242 1 Y 1 A LYS 1242 ? A LYS 1242 
1243 1 Y 1 A ILE 1243 ? A ILE 1243 
1244 1 Y 1 A VAL 1244 ? A VAL 1244 
1245 1 Y 1 A GLN 1245 ? A GLN 1245 
1246 1 Y 1 A GLU 1246 ? A GLU 1246 
1247 1 Y 1 A ASP 1247 ? A ASP 1247 
1248 1 Y 1 A ARG 1248 ? A ARG 1248 
1249 1 Y 1 A ALA 1249 ? A ALA 1249 
1250 1 Y 1 A VAL 1250 ? A VAL 1250 
1251 1 Y 1 A GLU 1251 ? A GLU 1251 
1252 1 Y 1 A SER 1252 ? A SER 1252 
1253 1 Y 1 A ARG 1253 ? A ARG 1253 
1254 1 Y 1 A THR 1254 ? A THR 1254 
1255 1 Y 1 A THR 1255 ? A THR 1255 
1256 1 Y 1 A ASP 1256 ? A ASP 1256 
1257 1 Y 1 A LEU 1257 ? A LEU 1257 
1258 1 Y 1 A LEU 1258 ? A LEU 1258 
1259 1 Y 1 A THR 1259 ? A THR 1259 
1260 1 Y 1 A ASP 1260 ? A ASP 1260 
1261 1 Y 1 A TRP 1261 ? A TRP 1261 
1262 1 Y 1 A GLU 1262 ? A GLU 1262 
1263 1 Y 1 A LYS 1263 ? A LYS 1263 
1264 1 Y 1 A THR 1264 ? A THR 1264 
1265 1 Y 1 A LYS 1265 ? A LYS 1265 
1266 1 Y 1 A PRO 1266 ? A PRO 1266 
1267 1 Y 1 A VAL 1267 ? A VAL 1267 
1268 1 Y 1 A THR 1268 ? A THR 1268 
1269 1 Y 1 A GLY 1269 ? A GLY 1269 
1270 1 Y 1 A ASN 1270 ? A ASN 1270 
1271 1 Y 1 A LEU 1271 ? A LEU 1271 
1272 1 Y 1 A ARG 1272 ? A ARG 1272 
1273 1 Y 1 A PRO 1273 ? A PRO 1273 
1274 1 Y 1 A GLU 1274 ? A GLU 1274 
1275 1 Y 1 A GLU 1275 ? A GLU 1275 
1276 1 Y 1 A ALA 1276 ? A ALA 1276 
1277 1 Y 1 A LEU 1277 ? A LEU 1277 
1278 1 Y 1 A GLN 1278 ? A GLN 1278 
1279 1 Y 1 A ALA 1279 ? A ALA 1279 
1280 1 Y 1 A LEU 1280 ? A LEU 1280 
1281 1 Y 1 A THR 1281 ? A THR 1281 
1282 1 Y 1 A ILE 1282 ? A ILE 1282 
1283 1 Y 1 A TYR 1283 ? A TYR 1283 
1284 1 Y 1 A GLU 1284 ? A GLU 1284 
1285 1 Y 1 A GLY 1285 ? A GLY 1285 
1286 1 Y 1 A LYS 1286 ? A LYS 1286 
1287 1 Y 1 A PHE 1287 ? A PHE 1287 
1288 1 Y 1 A GLY 1288 ? A GLY 1288 
1289 1 Y 1 A ARG 1289 ? A ARG 1289 
1290 1 Y 1 A LEU 1290 ? A LEU 1290 
1291 1 Y 1 A LYS 1291 ? A LYS 1291 
1292 1 Y 1 A ASP 1292 ? A ASP 1292 
1293 1 Y 1 A ASP 1293 ? A ASP 1293 
1294 1 Y 1 A ARG 1294 ? A ARG 1294 
1295 1 Y 1 A GLU 1295 ? A GLU 1295 
1296 1 Y 1 A LYS 1296 ? A LYS 1296 
1297 1 Y 1 A CYS 1297 ? A CYS 1297 
1298 1 Y 1 A ALA 1298 ? A ALA 1298 
1299 1 Y 1 A LYS 1299 ? A LYS 1299 
1300 1 Y 1 A ALA 1300 ? A ALA 1300 
1301 1 Y 1 A LYS 1301 ? A LYS 1301 
1302 1 Y 1 A GLU 1302 ? A GLU 1302 
1303 1 Y 1 A ALA 1303 ? A ALA 1303 
1304 1 Y 1 A LEU 1304 ? A LEU 1304 
1305 1 Y 1 A GLU 1305 ? A GLU 1305 
1306 1 Y 1 A LEU 1306 ? A LEU 1306 
1307 1 Y 1 A THR 1307 ? A THR 1307 
1308 1 Y 1 A ASP 1308 ? A ASP 1308 
1309 1 Y 1 A THR 1309 ? A THR 1309 
1310 1 Y 1 A GLY 1310 ? A GLY 1310 
1311 1 Y 1 A LEU 1311 ? A LEU 1311 
1312 1 Y 1 A LEU 1312 ? A LEU 1312 
1313 1 Y 1 A SER 1313 ? A SER 1313 
1314 1 Y 1 A GLY 1314 ? A GLY 1314 
1315 1 Y 1 A SER 1315 ? A SER 1315 
1316 1 Y 1 A GLU 1316 ? A GLU 1316 
1317 1 Y 1 A GLU 1317 ? A GLU 1317 
1318 1 Y 1 A ARG 1318 ? A ARG 1318 
1319 1 Y 1 A VAL 1319 ? A VAL 1319 
1320 1 Y 1 A GLN 1320 ? A GLN 1320 
1321 1 Y 1 A VAL 1321 ? A VAL 1321 
1322 1 Y 1 A ALA 1322 ? A ALA 1322 
1323 1 Y 1 A LEU 1323 ? A LEU 1323 
1324 1 Y 1 A GLU 1324 ? A GLU 1324 
1325 1 Y 1 A GLU 1325 ? A GLU 1325 
1326 1 Y 1 A LEU 1326 ? A LEU 1326 
1327 1 Y 1 A PRO 2020 ? A PRO 2020 
1328 1 Y 1 A GLY 2021 ? A GLY 2021 
1329 1 Y 1 A TYR 2022 ? A TYR 2022 
1330 1 Y 1 A ALA 2023 ? A ALA 2023 
1331 1 Y 1 A GLY 2024 ? A GLY 2024 
1332 1 Y 1 A ARG 2025 ? A ARG 2025 
1333 1 Y 1 A SER 2026 ? A SER 2026 
1334 1 Y 1 A LYS 2115 ? A LYS 2115 
1335 1 Y 1 A GLU 2116 ? A GLU 2116 
1336 1 Y 1 A GLU 2117 ? A GLU 2117 
1337 1 Y 1 A ARG 2118 ? A ARG 2118 
1338 1 Y 1 A GLY 2119 ? A GLY 2119 
1339 1 Y 1 A GLU 2120 ? A GLU 2120 
1340 1 Y 1 A ALA 2121 ? A ALA 2121 
1341 1 Y 1 A VAL 2122 ? A VAL 2122 
1342 1 Y 1 A ASP 2123 ? A ASP 2123 
1343 1 Y 1 A GLU 2124 ? A GLU 2124 
1344 1 Y 1 A GLY 2125 ? A GLY 2125 
1345 1 Y 1 A GLU 2126 ? A GLU 2126 
1346 1 Y 1 A GLU 2389 ? A GLU 2389 
1347 1 Y 1 A GLY 2390 ? A GLY 2390 
1348 1 Y 1 A GLU 2391 ? A GLU 2391 
1349 1 Y 1 A ASP 2392 ? A ASP 2392 
1350 1 Y 1 A GLU 2393 ? A GLU 2393 
1351 1 Y 1 A ALA 2394 ? A ALA 2394 
1352 1 Y 1 A GLN 2395 ? A GLN 2395 
1353 1 Y 1 A ARG 2396 ? A ARG 2396 
1354 1 Y 1 A ARG 2397 ? A ARG 2397 
1355 1 Y 1 A ARG 2398 ? A ARG 2398 
1356 1 Y 1 A LYS 2399 ? A LYS 2399 
1357 1 Y 1 A GLY 2400 ? A GLY 2400 
1358 1 Y 1 A LYS 2401 ? A LYS 2401 
1359 1 Y 1 A GLU 2402 ? A GLU 2402 
1360 1 Y 1 A ASP 2403 ? A ASP 2403 
1361 1 Y 1 A GLU 2404 ? A GLU 2404 
1362 1 Y 1 A GLY 2405 ? A GLY 2405 
1363 1 Y 1 A GLU 2406 ? A GLU 2406 
1364 1 Y 1 A GLU 2407 ? A GLU 2407 
1365 1 Y 1 A ALA 2408 ? A ALA 2408 
1366 1 Y 1 A ALA 2409 ? A ALA 2409 
1367 1 Y 1 A SER 3071 ? A SER 3071 
1368 1 Y 1 A SER 3072 ? A SER 3072 
1369 1 Y 1 A GLU 3073 ? A GLU 3073 
1370 1 Y 1 A GLY 3074 ? A GLY 3074 
1371 1 Y 1 A LEU 3075 ? A LEU 3075 
1372 1 Y 1 A LYS 3076 ? A LYS 3076 
1373 1 Y 1 A ASP 3077 ? A ASP 3077 
1374 1 Y 1 A ARG 3078 ? A ARG 3078 
1375 1 Y 1 A ALA 3079 ? A ALA 3079 
1376 1 Y 1 A ALA 3080 ? A ALA 3080 
1377 1 Y 1 A THR 3081 ? A THR 3081 
1378 1 Y 1 A ASP 3221 ? A ASP 3221 
1379 1 Y 1 A LEU 3222 ? A LEU 3222 
1380 1 Y 1 A ARG 3223 ? A ARG 3223 
1381 1 Y 1 A ILE 3224 ? A ILE 3224 
1382 1 Y 1 A LYS 3225 ? A LYS 3225 
1383 1 Y 1 A SER 3226 ? A SER 3226 
1384 1 Y 1 A GLN 3227 ? A GLN 3227 
1385 1 Y 1 A GLU 3228 ? A GLU 3228 
1386 1 Y 1 A LEU 3229 ? A LEU 3229 
1387 1 Y 1 A GLU 3230 ? A GLU 3230 
1388 1 Y 1 A VAL 3231 ? A VAL 3231 
1389 1 Y 1 A LYS 3232 ? A LYS 3232 
1390 1 Y 1 A ASN 3233 ? A ASN 3233 
1391 1 Y 1 A ALA 3234 ? A ALA 3234 
1392 1 Y 1 A ALA 3235 ? A ALA 3235 
1393 1 Y 1 A ALA 3236 ? A ALA 3236 
1394 1 Y 1 A ASN 3237 ? A ASN 3237 
1395 1 Y 1 A ASP 3238 ? A ASP 3238 
1396 1 Y 1 A LYS 3239 ? A LYS 3239 
1397 1 Y 1 A LEU 3240 ? A LEU 3240 
1398 1 Y 1 A LYS 3241 ? A LYS 3241 
1399 1 Y 1 A LYS 3242 ? A LYS 3242 
1400 1 Y 1 A MET 3243 ? A MET 3243 
1401 1 Y 1 A VAL 3244 ? A VAL 3244 
1402 1 Y 1 A LYS 3245 ? A LYS 3245 
1403 1 Y 1 A ASP 3246 ? A ASP 3246 
1404 1 Y 1 A GLN 3247 ? A GLN 3247 
1405 1 Y 1 A GLN 3248 ? A GLN 3248 
1406 1 Y 1 A GLU 3249 ? A GLU 3249 
1407 1 Y 1 A ALA 3250 ? A ALA 3250 
1408 1 Y 1 A GLU 3251 ? A GLU 3251 
1409 1 Y 1 A LYS 3252 ? A LYS 3252 
1410 1 Y 1 A LYS 3253 ? A LYS 3253 
1411 1 Y 1 A LYS 3254 ? A LYS 3254 
1412 1 Y 1 A VAL 3255 ? A VAL 3255 
1413 1 Y 1 A MET 3256 ? A MET 3256 
1414 1 Y 1 A SER 3257 ? A SER 3257 
1415 1 Y 1 A GLN 3258 ? A GLN 3258 
1416 1 Y 1 A GLU 3259 ? A GLU 3259 
1417 1 Y 1 A ILE 3260 ? A ILE 3260 
1418 1 Y 1 A GLN 3261 ? A GLN 3261 
1419 1 Y 1 A GLU 3262 ? A GLU 3262 
1420 1 Y 1 A GLN 3263 ? A GLN 3263 
1421 1 Y 1 A LEU 3264 ? A LEU 3264 
1422 1 Y 1 A HIS 3265 ? A HIS 3265 
1423 1 Y 1 A LYS 3266 ? A LYS 3266 
1424 1 Y 1 A GLN 3267 ? A GLN 3267 
1425 1 Y 1 A GLN 3268 ? A GLN 3268 
1426 1 Y 1 A GLU 3269 ? A GLU 3269 
1427 1 Y 1 A VAL 3270 ? A VAL 3270 
1428 1 Y 1 A ILE 3271 ? A ILE 3271 
1429 1 Y 1 A ALA 3272 ? A ALA 3272 
1430 1 Y 1 A ASP 3273 ? A ASP 3273 
1431 1 Y 1 A LYS 3274 ? A LYS 3274 
1432 1 Y 1 A GLN 3275 ? A GLN 3275 
1433 1 Y 1 A MET 3276 ? A MET 3276 
1434 1 Y 1 A SER 3277 ? A SER 3277 
1435 1 Y 1 A VAL 3278 ? A VAL 3278 
1436 1 Y 1 A LYS 3279 ? A LYS 3279 
1437 1 Y 1 A GLU 3280 ? A GLU 3280 
1438 1 Y 1 A ASP 3281 ? A ASP 3281 
1439 1 Y 1 A LEU 3282 ? A LEU 3282 
1440 1 Y 1 A ASP 3283 ? A ASP 3283 
1441 1 Y 1 A LYS 3284 ? A LYS 3284 
1442 1 Y 1 A VAL 3285 ? A VAL 3285 
1443 1 Y 1 A GLU 3286 ? A GLU 3286 
1444 1 Y 1 A PRO 3287 ? A PRO 3287 
1445 1 Y 1 A ALA 3288 ? A ALA 3288 
1446 1 Y 1 A VAL 3289 ? A VAL 3289 
1447 1 Y 1 A ILE 3290 ? A ILE 3290 
1448 1 Y 1 A GLU 3291 ? A GLU 3291 
1449 1 Y 1 A ALA 3292 ? A ALA 3292 
1450 1 Y 1 A GLN 3293 ? A GLN 3293 
1451 1 Y 1 A ASN 3294 ? A ASN 3294 
1452 1 Y 1 A ALA 3295 ? A ALA 3295 
1453 1 Y 1 A VAL 3296 ? A VAL 3296 
1454 1 Y 1 A LYS 3297 ? A LYS 3297 
1455 1 Y 1 A SER 3298 ? A SER 3298 
1456 1 Y 1 A ILE 3299 ? A ILE 3299 
1457 1 Y 1 A LYS 3300 ? A LYS 3300 
1458 1 Y 1 A LYS 3301 ? A LYS 3301 
1459 1 Y 1 A GLN 3302 ? A GLN 3302 
1460 1 Y 1 A HIS 3303 ? A HIS 3303 
1461 1 Y 1 A LEU 3304 ? A LEU 3304 
1462 1 Y 1 A VAL 3305 ? A VAL 3305 
1463 1 Y 1 A GLU 3306 ? A GLU 3306 
1464 1 Y 1 A VAL 3307 ? A VAL 3307 
1465 1 Y 1 A ARG 3308 ? A ARG 3308 
1466 1 Y 1 A SER 3309 ? A SER 3309 
1467 1 Y 1 A MET 3310 ? A MET 3310 
1468 1 Y 1 A ALA 3311 ? A ALA 3311 
1469 1 Y 1 A ASN 3312 ? A ASN 3312 
1470 1 Y 1 A PRO 3313 ? A PRO 3313 
1471 1 Y 1 A PRO 3314 ? A PRO 3314 
1472 1 Y 1 A ALA 3315 ? A ALA 3315 
1473 1 Y 1 A ALA 3316 ? A ALA 3316 
1474 1 Y 1 A VAL 3317 ? A VAL 3317 
1475 1 Y 1 A LYS 3318 ? A LYS 3318 
1476 1 Y 1 A LEU 3319 ? A LEU 3319 
1477 1 Y 1 A ALA 3320 ? A ALA 3320 
1478 1 Y 1 A LEU 3321 ? A LEU 3321 
1479 1 Y 1 A GLU 3322 ? A GLU 3322 
1480 1 Y 1 A SER 3323 ? A SER 3323 
1481 1 Y 1 A ILE 3324 ? A ILE 3324 
1482 1 Y 1 A CYS 3325 ? A CYS 3325 
1483 1 Y 1 A LEU 3326 ? A LEU 3326 
1484 1 Y 1 A LEU 3327 ? A LEU 3327 
1485 1 Y 1 A LEU 3328 ? A LEU 3328 
1486 1 Y 1 A GLY 3329 ? A GLY 3329 
1487 1 Y 1 A GLU 3330 ? A GLU 3330 
1488 1 Y 1 A SER 3331 ? A SER 3331 
1489 1 Y 1 A THR 3332 ? A THR 3332 
1490 1 Y 1 A THR 3333 ? A THR 3333 
1491 1 Y 1 A ASP 3334 ? A ASP 3334 
1492 1 Y 1 A TRP 3335 ? A TRP 3335 
1493 1 Y 1 A LYS 3336 ? A LYS 3336 
1494 1 Y 1 A GLN 3337 ? A GLN 3337 
1495 1 Y 1 A ILE 3338 ? A ILE 3338 
1496 1 Y 1 A ARG 3339 ? A ARG 3339 
1497 1 Y 1 A SER 3340 ? A SER 3340 
1498 1 Y 1 A ILE 3341 ? A ILE 3341 
1499 1 Y 1 A ILE 3342 ? A ILE 3342 
1500 1 Y 1 A MET 3343 ? A MET 3343 
1501 1 Y 1 A ARG 3344 ? A ARG 3344 
1502 1 Y 1 A GLU 3345 ? A GLU 3345 
1503 1 Y 1 A ASN 3346 ? A ASN 3346 
1504 1 Y 1 A PHE 3347 ? A PHE 3347 
1505 1 Y 1 A ILE 3348 ? A ILE 3348 
1506 1 Y 1 A PRO 3349 ? A PRO 3349 
1507 1 Y 1 A THR 3350 ? A THR 3350 
1508 1 Y 1 A ILE 3351 ? A ILE 3351 
1509 1 Y 1 A VAL 3352 ? A VAL 3352 
1510 1 Y 1 A ASN 3353 ? A ASN 3353 
1511 1 Y 1 A PHE 3354 ? A PHE 3354 
1512 1 Y 1 A SER 3355 ? A SER 3355 
1513 1 Y 1 A ALA 3356 ? A ALA 3356 
1514 1 Y 1 A GLU 3357 ? A GLU 3357 
1515 1 Y 1 A GLU 3358 ? A GLU 3358 
1516 1 Y 1 A ILE 3359 ? A ILE 3359 
1517 1 Y 1 A SER 3360 ? A SER 3360 
1518 1 Y 1 A ASP 3361 ? A ASP 3361 
1519 1 Y 1 A ALA 3362 ? A ALA 3362 
1520 1 Y 1 A ILE 3363 ? A ILE 3363 
1521 1 Y 1 A ARG 3364 ? A ARG 3364 
1522 1 Y 1 A GLU 3365 ? A GLU 3365 
1523 1 Y 1 A LYS 3366 ? A LYS 3366 
1524 1 Y 1 A MET 3367 ? A MET 3367 
1525 1 Y 1 A LYS 3368 ? A LYS 3368 
1526 1 Y 1 A LYS 3369 ? A LYS 3369 
1527 1 Y 1 A ASN 3370 ? A ASN 3370 
1528 1 Y 1 A TYR 3371 ? A TYR 3371 
1529 1 Y 1 A MET 3372 ? A MET 3372 
1530 1 Y 1 A SER 3373 ? A SER 3373 
1531 1 Y 1 A ASN 3374 ? A ASN 3374 
1532 1 Y 1 A PRO 3375 ? A PRO 3375 
1533 1 Y 1 A SER 3376 ? A SER 3376 
1534 1 Y 1 A TYR 3377 ? A TYR 3377 
1535 1 Y 1 A ASN 3378 ? A ASN 3378 
1536 1 Y 1 A TYR 3379 ? A TYR 3379 
1537 1 Y 1 A GLU 3380 ? A GLU 3380 
1538 1 Y 1 A ILE 3381 ? A ILE 3381 
1539 1 Y 1 A VAL 3382 ? A VAL 3382 
1540 1 Y 1 A ASN 3383 ? A ASN 3383 
1541 1 Y 1 A ARG 3384 ? A ARG 3384 
1542 1 Y 1 A ALA 3385 ? A ALA 3385 
1543 1 Y 1 A SER 3386 ? A SER 3386 
1544 1 Y 1 A LEU 3387 ? A LEU 3387 
1545 1 Y 1 A ALA 3388 ? A ALA 3388 
1546 1 Y 1 A CYS 3389 ? A CYS 3389 
1547 1 Y 1 A GLY 3390 ? A GLY 3390 
1548 1 Y 1 A PRO 3391 ? A PRO 3391 
1549 1 Y 1 A MET 3392 ? A MET 3392 
1550 1 Y 1 A VAL 3393 ? A VAL 3393 
1551 1 Y 1 A LYS 3394 ? A LYS 3394 
1552 1 Y 1 A TRP 3395 ? A TRP 3395 
1553 1 Y 1 A ALA 3396 ? A ALA 3396 
1554 1 Y 1 A ILE 3397 ? A ILE 3397 
1555 1 Y 1 A ALA 3398 ? A ALA 3398 
1556 1 Y 1 A GLN 3399 ? A GLN 3399 
1557 1 Y 1 A LEU 3400 ? A LEU 3400 
1558 1 Y 1 A ASN 3401 ? A ASN 3401 
1559 1 Y 1 A TYR 3402 ? A TYR 3402 
1560 1 Y 1 A ALA 3403 ? A ALA 3403 
1561 1 Y 1 A ASP 3404 ? A ASP 3404 
1562 1 Y 1 A MET 3405 ? A MET 3405 
1563 1 Y 1 A LEU 3406 ? A LEU 3406 
1564 1 Y 1 A LYS 3407 ? A LYS 3407 
1565 1 Y 1 A ARG 3408 ? A ARG 3408 
1566 1 Y 1 A VAL 3409 ? A VAL 3409 
1567 1 Y 1 A GLU 3410 ? A GLU 3410 
1568 1 Y 1 A PRO 3411 ? A PRO 3411 
1569 1 Y 1 A LEU 3412 ? A LEU 3412 
1570 1 Y 1 A ARG 3413 ? A ARG 3413 
1571 1 Y 1 A ASN 3414 ? A ASN 3414 
1572 1 Y 1 A GLU 3415 ? A GLU 3415 
1573 1 Y 1 A LEU 3416 ? A LEU 3416 
1574 1 Y 1 A GLN 3417 ? A GLN 3417 
1575 1 Y 1 A LYS 3418 ? A LYS 3418 
1576 1 Y 1 A LEU 3419 ? A LEU 3419 
1577 1 Y 1 A GLU 3420 ? A GLU 3420 
1578 1 Y 1 A ASP 3421 ? A ASP 3421 
1579 1 Y 1 A ASP 3422 ? A ASP 3422 
1580 1 Y 1 A ALA 3423 ? A ALA 3423 
1581 1 Y 1 A LYS 3424 ? A LYS 3424 
1582 1 Y 1 A ASP 3425 ? A ASP 3425 
1583 1 Y 1 A ASN 3426 ? A ASN 3426 
1584 1 Y 1 A GLN 3427 ? A GLN 3427 
1585 1 Y 1 A GLN 3428 ? A GLN 3428 
1586 1 Y 1 A LYS 3429 ? A LYS 3429 
1587 1 Y 1 A ALA 3430 ? A ALA 3430 
1588 1 Y 1 A ASN 3431 ? A ASN 3431 
1589 1 Y 1 A GLU 3432 ? A GLU 3432 
1590 1 Y 1 A VAL 3433 ? A VAL 3433 
1591 1 Y 1 A GLU 3434 ? A GLU 3434 
1592 1 Y 1 A GLN 3435 ? A GLN 3435 
1593 1 Y 1 A MET 3436 ? A MET 3436 
1594 1 Y 1 A ILE 3437 ? A ILE 3437 
1595 1 Y 1 A ARG 3438 ? A ARG 3438 
1596 1 Y 1 A ASP 3439 ? A ASP 3439 
1597 1 Y 1 A LEU 3440 ? A LEU 3440 
1598 1 Y 1 A GLU 3441 ? A GLU 3441 
1599 1 Y 1 A ALA 3442 ? A ALA 3442 
1600 1 Y 1 A SER 3443 ? A SER 3443 
1601 1 Y 1 A ILE 3444 ? A ILE 3444 
1602 1 Y 1 A ALA 3445 ? A ALA 3445 
1603 1 Y 1 A ARG 3446 ? A ARG 3446 
1604 1 Y 1 A TYR 3447 ? A TYR 3447 
1605 1 Y 1 A LYS 3448 ? A LYS 3448 
1606 1 Y 1 A GLU 3449 ? A GLU 3449 
1607 1 Y 1 A GLU 3450 ? A GLU 3450 
1608 1 Y 1 A TYR 3451 ? A TYR 3451 
1609 1 Y 1 A ALA 3452 ? A ALA 3452 
1610 1 Y 1 A VAL 3453 ? A VAL 3453 
1611 1 Y 1 A LEU 3454 ? A LEU 3454 
1612 1 Y 1 A ILE 3455 ? A ILE 3455 
1613 1 Y 1 A SER 3456 ? A SER 3456 
1614 1 Y 1 A GLU 3457 ? A GLU 3457 
1615 1 Y 1 A ALA 3458 ? A ALA 3458 
1616 1 Y 1 A GLN 3459 ? A GLN 3459 
1617 1 Y 1 A ALA 3460 ? A ALA 3460 
1618 1 Y 1 A ILE 3461 ? A ILE 3461 
1619 1 Y 1 A LYS 3462 ? A LYS 3462 
1620 1 Y 1 A ALA 3463 ? A ALA 3463 
1621 1 Y 1 A ASP 3464 ? A ASP 3464 
1622 1 Y 1 A LEU 3465 ? A LEU 3465 
1623 1 Y 1 A ALA 3466 ? A ALA 3466 
1624 1 Y 1 A ALA 3467 ? A ALA 3467 
1625 1 Y 1 A VAL 3468 ? A VAL 3468 
1626 1 Y 1 A GLU 3469 ? A GLU 3469 
1627 1 Y 1 A ALA 3470 ? A ALA 3470 
1628 1 Y 1 A MET 4348 ? A MET 4348 
1629 1 Y 1 A LEU 4349 ? A LEU 4349 
1630 1 Y 1 A GLU 4350 ? A GLU 4350 
1631 1 Y 1 A ASP 4351 ? A ASP 4351 
1632 1 Y 1 A GLU 4352 ? A GLU 4352 
1633 1 Y 1 A ASP 4353 ? A ASP 4353 
1634 1 Y 1 A ASP 4354 ? A ASP 4354 
1635 1 Y 1 A LEU 4355 ? A LEU 4355 
1636 1 Y 1 A ALA 4356 ? A ALA 4356 
1637 1 Y 1 A TYR 4357 ? A TYR 4357 
1638 1 Y 1 A ALA 4358 ? A ALA 4358 
1639 1 Y 1 A GLU 4359 ? A GLU 4359 
1640 1 Y 1 A THR 4360 ? A THR 4360 
1641 1 Y 1 A GLU 4361 ? A GLU 4361 
1642 1 Y 1 A LYS 4362 ? A LYS 4362 
1643 1 Y 1 A LYS 4363 ? A LYS 4363 
1644 1 Y 1 A THR 4364 ? A THR 4364 
1645 1 Y 1 A ARG 4365 ? A ARG 4365 
1646 1 Y 1 A THR 4366 ? A THR 4366 
1647 1 Y 1 A ASP 4367 ? A ASP 4367 
1648 1 Y 1 A SER 4368 ? A SER 4368 
1649 1 Y 1 A THR 4369 ? A THR 4369 
1650 1 Y 1 A SER 4370 ? A SER 4370 
1651 1 Y 1 A ASP 4371 ? A ASP 4371 
1652 1 Y 1 A GLY 4372 ? A GLY 4372 
1653 1 Y 1 A ARG 4373 ? A ARG 4373 
1654 1 Y 1 A PRO 4374 ? A PRO 4374 
1655 1 Y 1 A GLU 4646 ? A GLU 4646 
# 
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 
PHE N      N N N 336 
PHE CA     C N S 337 
PHE C      C N N 338 
PHE O      O N N 339 
PHE CB     C N N 340 
PHE CG     C Y N 341 
PHE CD1    C Y N 342 
PHE CD2    C Y N 343 
PHE CE1    C Y N 344 
PHE CE2    C Y N 345 
PHE CZ     C Y N 346 
PHE OXT    O N N 347 
PHE H      H N N 348 
PHE H2     H N N 349 
PHE HA     H N N 350 
PHE HB2    H N N 351 
PHE HB3    H N N 352 
PHE HD1    H N N 353 
PHE HD2    H N N 354 
PHE HE1    H N N 355 
PHE HE2    H N N 356 
PHE HZ     H N N 357 
PHE HXT    H N N 358 
PRO N      N N N 359 
PRO CA     C N S 360 
PRO C      C N N 361 
PRO O      O N N 362 
PRO CB     C N N 363 
PRO CG     C N N 364 
PRO CD     C N N 365 
PRO OXT    O N N 366 
PRO H      H N N 367 
PRO HA     H N N 368 
PRO HB2    H N N 369 
PRO HB3    H N N 370 
PRO HG2    H N N 371 
PRO HG3    H N N 372 
PRO HD2    H N N 373 
PRO HD3    H N N 374 
PRO HXT    H N N 375 
SER N      N N N 376 
SER CA     C N S 377 
SER C      C N N 378 
SER O      O N N 379 
SER CB     C N N 380 
SER OG     O N N 381 
SER OXT    O N N 382 
SER H      H N N 383 
SER H2     H N N 384 
SER HA     H N N 385 
SER HB2    H N N 386 
SER HB3    H N N 387 
SER HG     H N N 388 
SER HXT    H N N 389 
THR N      N N N 390 
THR CA     C N S 391 
THR C      C N N 392 
THR O      O N N 393 
THR CB     C N R 394 
THR OG1    O N N 395 
THR CG2    C N N 396 
THR OXT    O N N 397 
THR H      H N N 398 
THR H2     H N N 399 
THR HA     H N N 400 
THR HB     H N N 401 
THR HG1    H N N 402 
THR HG21   H N N 403 
THR HG22   H N N 404 
THR HG23   H N N 405 
THR HXT    H N N 406 
TRP N      N N N 407 
TRP CA     C N S 408 
TRP C      C N N 409 
TRP O      O N N 410 
TRP CB     C N N 411 
TRP CG     C Y N 412 
TRP CD1    C Y N 413 
TRP CD2    C Y N 414 
TRP NE1    N Y N 415 
TRP CE2    C Y N 416 
TRP CE3    C Y N 417 
TRP CZ2    C Y N 418 
TRP CZ3    C Y N 419 
TRP CH2    C Y N 420 
TRP OXT    O N N 421 
TRP H      H N N 422 
TRP H2     H N N 423 
TRP HA     H N N 424 
TRP HB2    H N N 425 
TRP HB3    H N N 426 
TRP HD1    H N N 427 
TRP HE1    H N N 428 
TRP HE3    H N N 429 
TRP HZ2    H N N 430 
TRP HZ3    H N N 431 
TRP HH2    H N N 432 
TRP HXT    H N N 433 
TYR N      N N N 434 
TYR CA     C N S 435 
TYR C      C N N 436 
TYR O      O N N 437 
TYR CB     C N N 438 
TYR CG     C Y N 439 
TYR CD1    C Y N 440 
TYR CD2    C Y N 441 
TYR CE1    C Y N 442 
TYR CE2    C Y N 443 
TYR CZ     C Y N 444 
TYR OH     O N N 445 
TYR OXT    O N N 446 
TYR H      H N N 447 
TYR H2     H N N 448 
TYR HA     H N N 449 
TYR HB2    H N N 450 
TYR HB3    H N N 451 
TYR HD1    H N N 452 
TYR HD2    H N N 453 
TYR HE1    H N N 454 
TYR HE2    H N N 455 
TYR HH     H N N 456 
TYR HXT    H N N 457 
VAL N      N N N 458 
VAL CA     C N S 459 
VAL C      C N N 460 
VAL O      O N N 461 
VAL CB     C N N 462 
VAL CG1    C N N 463 
VAL CG2    C N N 464 
VAL OXT    O N N 465 
VAL H      H N N 466 
VAL H2     H N N 467 
VAL HA     H N N 468 
VAL HB     H N N 469 
VAL HG11   H N N 470 
VAL HG12   H N N 471 
VAL HG13   H N N 472 
VAL HG21   H N N 473 
VAL HG22   H N N 474 
VAL HG23   H N N 475 
VAL HXT    H N N 476 
# 
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    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BM8 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-7c of motor domain from full-length human dynein-1 in 5 mM ATP' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                1.5 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ?         ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 SerialEM  4 
MASKING                         ? 3  ? ? ? ?         ? 
'CTF CORRECTION'                ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ? 
'MODEL FITTING'                 ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ?         ? 
OTHER                           ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION                  ? 12 1 ? ? ?         ? 
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC 4 
'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           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM142959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM139483 2 
# 
_atom_sites.entry_id                    9BM8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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     . GLN A 1 1327 ? 81.392  153.241 118.175 1.00 91.28  ? 1327 GLN A N     1 
ATOM   2     C CA    . GLN A 1 1327 ? 81.438  152.525 119.444 1.00 91.28  ? 1327 GLN A CA    1 
ATOM   3     C C     . GLN A 1 1327 ? 82.700  152.879 120.224 1.00 91.28  ? 1327 GLN A C     1 
ATOM   4     O O     . GLN A 1 1327 ? 83.394  153.842 119.897 1.00 91.28  ? 1327 GLN A O     1 
ATOM   5     C CB    . GLN A 1 1327 ? 81.367  151.015 119.212 1.00 91.28  ? 1327 GLN A CB    1 
ATOM   6     C CG    . GLN A 1 1327 ? 80.081  150.548 118.549 1.00 91.28  ? 1327 GLN A CG    1 
ATOM   7     C CD    . GLN A 1 1327 ? 78.924  150.447 119.523 1.00 91.28  ? 1327 GLN A CD    1 
ATOM   8     O OE1   . GLN A 1 1327 ? 79.109  150.539 120.737 1.00 91.28  ? 1327 GLN A OE1   1 
ATOM   9     N NE2   . GLN A 1 1327 ? 77.720  150.256 118.995 1.00 91.28  ? 1327 GLN A NE2   1 
ATOM   10    N N     . ASP A 1 1328 ? 82.986  152.092 121.265 1.00 95.84  ? 1328 ASP A N     1 
ATOM   11    C CA    . ASP A 1 1328 ? 84.187  152.325 122.061 1.00 95.84  ? 1328 ASP A CA    1 
ATOM   12    C C     . ASP A 1 1328 ? 85.448  152.104 121.236 1.00 95.84  ? 1328 ASP A C     1 
ATOM   13    O O     . ASP A 1 1328 ? 86.437  152.833 121.388 1.00 95.84  ? 1328 ASP A O     1 
ATOM   14    C CB    . ASP A 1 1328 ? 84.184  151.421 123.293 1.00 95.84  ? 1328 ASP A CB    1 
ATOM   15    C CG    . ASP A 1 1328 ? 82.841  151.400 123.995 1.00 95.84  ? 1328 ASP A CG    1 
ATOM   16    O OD1   . ASP A 1 1328 ? 82.350  152.484 124.371 1.00 95.84  ? 1328 ASP A OD1   1 
ATOM   17    O OD2   . ASP A 1 1328 ? 82.279  150.299 124.172 1.00 95.84  ? 1328 ASP A OD2   1 
ATOM   18    N N     . LEU A 1 1329 ? 85.437  151.093 120.363 1.00 90.76  ? 1329 LEU A N     1 
ATOM   19    C CA    . LEU A 1 1329 ? 86.588  150.847 119.501 1.00 90.76  ? 1329 LEU A CA    1 
ATOM   20    C C     . LEU A 1 1329 ? 86.833  152.023 118.563 1.00 90.76  ? 1329 LEU A C     1 
ATOM   21    O O     . LEU A 1 1329 ? 87.980  152.430 118.356 1.00 90.76  ? 1329 LEU A O     1 
ATOM   22    C CB    . LEU A 1 1329 ? 86.394  149.554 118.705 1.00 90.76  ? 1329 LEU A CB    1 
ATOM   23    C CG    . LEU A 1 1329 ? 85.951  148.280 119.436 1.00 90.76  ? 1329 LEU A CG    1 
ATOM   24    C CD1   . LEU A 1 1329 ? 84.434  148.199 119.583 1.00 90.76  ? 1329 LEU A CD1   1 
ATOM   25    C CD2   . LEU A 1 1329 ? 86.490  147.044 118.731 1.00 90.76  ? 1329 LEU A CD2   1 
ATOM   26    N N     . LYS A 1 1330 ? 85.766  152.585 117.989 1.00 87.14  ? 1330 LYS A N     1 
ATOM   27    C CA    . LYS A 1 1330 ? 85.922  153.749 117.122 1.00 87.14  ? 1330 LYS A CA    1 
ATOM   28    C C     . LYS A 1 1330 ? 86.475  154.940 117.894 1.00 87.14  ? 1330 LYS A C     1 
ATOM   29    O O     . LYS A 1 1330 ? 87.334  155.675 117.391 1.00 87.14  ? 1330 LYS A O     1 
ATOM   30    C CB    . LYS A 1 1330 ? 84.585  154.101 116.471 1.00 87.14  ? 1330 LYS A CB    1 
ATOM   31    C CG    . LYS A 1 1330 ? 84.654  155.261 115.492 1.00 87.14  ? 1330 LYS A CG    1 
ATOM   32    C CD    . LYS A 1 1330 ? 83.317  155.483 114.806 1.00 87.14  ? 1330 LYS A CD    1 
ATOM   33    C CE    . LYS A 1 1330 ? 83.397  156.608 113.787 1.00 87.14  ? 1330 LYS A CE    1 
ATOM   34    N NZ    . LYS A 1 1330 ? 82.102  156.812 113.082 1.00 87.14  ? 1330 LYS A NZ    1 
ATOM   35    N N     . GLY A 1 1331 ? 85.996  155.147 119.122 1.00 85.58  ? 1331 GLY A N     1 
ATOM   36    C CA    . GLY A 1 1331 ? 86.508  156.242 119.930 1.00 85.58  ? 1331 GLY A CA    1 
ATOM   37    C C     . GLY A 1 1331 ? 87.974  156.080 120.278 1.00 85.58  ? 1331 GLY A C     1 
ATOM   38    O O     . GLY A 1 1331 ? 88.747  157.041 120.219 1.00 85.58  ? 1331 GLY A O     1 
ATOM   39    N N     . VAL A 1 1332 ? 88.381  154.862 120.646 1.00 89.72  ? 1332 VAL A N     1 
ATOM   40    C CA    . VAL A 1 1332 ? 89.787  154.640 120.965 1.00 89.72  ? 1332 VAL A CA    1 
ATOM   41    C C     . VAL A 1 1332 ? 90.647  154.746 119.710 1.00 89.72  ? 1332 VAL A C     1 
ATOM   42    O O     . VAL A 1 1332 ? 91.797  155.191 119.780 1.00 89.72  ? 1332 VAL A O     1 
ATOM   43    C CB    . VAL A 1 1332 ? 89.986  153.296 121.695 1.00 89.72  ? 1332 VAL A CB    1 
ATOM   44    C CG1   . VAL A 1 1332 ? 90.038  152.129 120.719 1.00 89.72  ? 1332 VAL A CG1   1 
ATOM   45    C CG2   . VAL A 1 1332 ? 91.247  153.342 122.546 1.00 89.72  ? 1332 VAL A CG2   1 
ATOM   46    N N     . TRP A 1 1333 ? 90.109  154.370 118.546 1.00 90.97  ? 1333 TRP A N     1 
ATOM   47    C CA    . TRP A 1 1333 ? 90.840  154.579 117.299 1.00 90.97  ? 1333 TRP A CA    1 
ATOM   48    C C     . TRP A 1 1333 ? 91.026  156.063 117.017 1.00 90.97  ? 1333 TRP A C     1 
ATOM   49    O O     . TRP A 1 1333 ? 92.100  156.486 116.576 1.00 90.97  ? 1333 TRP A O     1 
ATOM   50    C CB    . TRP A 1 1333 ? 90.115  153.898 116.136 1.00 90.97  ? 1333 TRP A CB    1 
ATOM   51    C CG    . TRP A 1 1333 ? 90.350  152.414 116.033 1.00 90.97  ? 1333 TRP A CG    1 
ATOM   52    C CD1   . TRP A 1 1333 ? 89.398  151.444 115.907 1.00 90.97  ? 1333 TRP A CD1   1 
ATOM   53    C CD2   . TRP A 1 1333 ? 91.614  151.733 116.024 1.00 90.97  ? 1333 TRP A CD2   1 
ATOM   54    N NE1   . TRP A 1 1333 ? 89.985  150.206 115.833 1.00 90.97  ? 1333 TRP A NE1   1 
ATOM   55    C CE2   . TRP A 1 1333 ? 91.345  150.355 115.902 1.00 90.97  ? 1333 TRP A CE2   1 
ATOM   56    C CE3   . TRP A 1 1333 ? 92.946  152.155 116.113 1.00 90.97  ? 1333 TRP A CE3   1 
ATOM   57    C CZ2   . TRP A 1 1333 ? 92.357  149.398 115.866 1.00 90.97  ? 1333 TRP A CZ2   1 
ATOM   58    C CZ3   . TRP A 1 1333 ? 93.948  151.202 116.078 1.00 90.97  ? 1333 TRP A CZ3   1 
ATOM   59    C CH2   . TRP A 1 1333 ? 93.648  149.840 115.956 1.00 90.97  ? 1333 TRP A CH2   1 
ATOM   60    N N     . SER A 1 1334 ? 89.988  156.868 117.261 1.00 91.79  ? 1334 SER A N     1 
ATOM   61    C CA    . SER A 1 1334 ? 90.111  158.311 117.074 1.00 91.79  ? 1334 SER A CA    1 
ATOM   62    C C     . SER A 1 1334 ? 91.138  158.907 118.031 1.00 91.79  ? 1334 SER A C     1 
ATOM   63    O O     . SER A 1 1334 ? 91.943  159.763 117.640 1.00 91.79  ? 1334 SER A O     1 
ATOM   64    C CB    . SER A 1 1334 ? 88.750  158.982 117.261 1.00 91.79  ? 1334 SER A CB    1 
ATOM   65    O OG    . SER A 1 1334 ? 88.862  160.392 117.189 1.00 91.79  ? 1334 SER A OG    1 
ATOM   66    N N     . GLU A 1 1335 ? 91.122  158.470 119.292 1.00 92.80  ? 1335 GLU A N     1 
ATOM   67    C CA    . GLU A 1 1335 ? 92.107  158.959 120.253 1.00 92.80  ? 1335 GLU A CA    1 
ATOM   68    C C     . GLU A 1 1335 ? 93.520  158.548 119.853 1.00 92.80  ? 1335 GLU A C     1 
ATOM   69    O O     . GLU A 1 1335 ? 94.464  159.338 119.977 1.00 92.80  ? 1335 GLU A O     1 
ATOM   70    C CB    . GLU A 1 1335 ? 91.775  158.450 121.657 1.00 92.80  ? 1335 GLU A CB    1 
ATOM   71    C CG    . GLU A 1 1335 ? 90.422  158.903 122.185 1.00 92.80  ? 1335 GLU A CG    1 
ATOM   72    C CD    . GLU A 1 1335 ? 90.427  160.343 122.662 1.00 92.80  ? 1335 GLU A CD    1 
ATOM   73    O OE1   . GLU A 1 1335 ? 91.515  160.953 122.719 1.00 92.80  ? 1335 GLU A OE1   1 
ATOM   74    O OE2   . GLU A 1 1335 ? 89.338  160.866 122.982 1.00 92.80  ? 1335 GLU A OE2   1 
ATOM   75    N N     . LEU A 1 1336 ? 93.683  157.313 119.373 1.00 93.58  ? 1336 LEU A N     1 
ATOM   76    C CA    . LEU A 1 1336 ? 94.989  156.863 118.906 1.00 93.58  ? 1336 LEU A CA    1 
ATOM   77    C C     . LEU A 1 1336 ? 95.454  157.676 117.708 1.00 93.58  ? 1336 LEU A C     1 
ATOM   78    O O     . LEU A 1 1336 ? 96.639  158.004 117.595 1.00 93.58  ? 1336 LEU A O     1 
ATOM   79    C CB    . LEU A 1 1336 ? 94.937  155.376 118.554 1.00 93.58  ? 1336 LEU A CB    1 
ATOM   80    C CG    . LEU A 1 1336 ? 96.292  154.675 118.450 1.00 93.58  ? 1336 LEU A CG    1 
ATOM   81    C CD1   . LEU A 1 1336 ? 96.683  154.068 119.788 1.00 93.58  ? 1336 LEU A CD1   1 
ATOM   82    C CD2   . LEU A 1 1336 ? 96.273  153.622 117.354 1.00 93.58  ? 1336 LEU A CD2   1 
ATOM   83    N N     . SER A 1 1337 ? 94.536  158.001 116.795 1.00 93.43  ? 1337 SER A N     1 
ATOM   84    C CA    . SER A 1 1337 ? 94.890  158.838 115.653 1.00 93.43  ? 1337 SER A CA    1 
ATOM   85    C C     . SER A 1 1337 ? 95.323  160.226 116.103 1.00 93.43  ? 1337 SER A C     1 
ATOM   86    O O     . SER A 1 1337 ? 96.285  160.788 115.568 1.00 93.43  ? 1337 SER A O     1 
ATOM   87    C CB    . SER A 1 1337 ? 93.712  158.929 114.683 1.00 93.43  ? 1337 SER A CB    1 
ATOM   88    O OG    . SER A 1 1337 ? 92.601  159.571 115.286 1.00 93.43  ? 1337 SER A OG    1 
ATOM   89    N N     . LYS A 1 1338 ? 94.621  160.798 117.086 1.00 93.80  ? 1338 LYS A N     1 
ATOM   90    C CA    . LYS A 1 1338 ? 95.013  162.106 117.608 1.00 93.80  ? 1338 LYS A CA    1 
ATOM   91    C C     . LYS A 1 1338 ? 96.397  162.055 118.247 1.00 93.80  ? 1338 LYS A C     1 
ATOM   92    O O     . LYS A 1 1338 ? 97.225  162.950 118.031 1.00 93.80  ? 1338 LYS A O     1 
ATOM   93    C CB    . LYS A 1 1338 ? 93.976  162.599 118.619 1.00 93.80  ? 1338 LYS A CB    1 
ATOM   94    C CG    . LYS A 1 1338 ? 93.035  163.664 118.083 1.00 93.80  ? 1338 LYS A CG    1 
ATOM   95    C CD    . LYS A 1 1338 ? 92.245  163.158 116.888 1.00 93.80  ? 1338 LYS A CD    1 
ATOM   96    C CE    . LYS A 1 1338 ? 91.243  164.196 116.410 1.00 93.80  ? 1338 LYS A CE    1 
ATOM   97    N NZ    . LYS A 1 1338 ? 90.403  163.686 115.292 1.00 93.80  ? 1338 LYS A NZ    1 
ATOM   98    N N     . VAL A 1 1339 ? 96.666  161.011 119.033 1.00 97.25  ? 1339 VAL A N     1 
ATOM   99    C CA    . VAL A 1 1339 ? 97.972  160.875 119.671 1.00 97.25  ? 1339 VAL A CA    1 
ATOM   100   C C     . VAL A 1 1339 ? 99.064  160.687 118.624 1.00 97.25  ? 1339 VAL A C     1 
ATOM   101   O O     . VAL A 1 1339 ? 100.157 161.253 118.738 1.00 97.25  ? 1339 VAL A O     1 
ATOM   102   C CB    . VAL A 1 1339 ? 97.951  159.720 120.689 1.00 97.25  ? 1339 VAL A CB    1 
ATOM   103   C CG1   . VAL A 1 1339 ? 99.347  159.460 121.234 1.00 97.25  ? 1339 VAL A CG1   1 
ATOM   104   C CG2   . VAL A 1 1339 ? 96.988  160.036 121.821 1.00 97.25  ? 1339 VAL A CG2   1 
ATOM   105   N N     . TRP A 1 1340 ? 98.786  159.890 117.591 1.00 102.90 ? 1340 TRP A N     1 
ATOM   106   C CA    . TRP A 1 1340 ? 99.752  159.691 116.515 1.00 102.90 ? 1340 TRP A CA    1 
ATOM   107   C C     . TRP A 1 1340 ? 100.030 160.993 115.777 1.00 102.90 ? 1340 TRP A C     1 
ATOM   108   O O     . TRP A 1 1340 ? 101.177 161.277 115.418 1.00 102.90 ? 1340 TRP A O     1 
ATOM   109   C CB    . TRP A 1 1340 ? 99.242  158.625 115.547 1.00 102.90 ? 1340 TRP A CB    1 
ATOM   110   C CG    . TRP A 1 1340 ? 99.625  157.231 115.928 1.00 102.90 ? 1340 TRP A CG    1 
ATOM   111   C CD1   . TRP A 1 1340 ? 98.784  156.226 116.309 1.00 102.90 ? 1340 TRP A CD1   1 
ATOM   112   C CD2   . TRP A 1 1340 ? 100.946 156.681 115.960 1.00 102.90 ? 1340 TRP A CD2   1 
ATOM   113   N NE1   . TRP A 1 1340 ? 99.500  155.086 116.579 1.00 102.90 ? 1340 TRP A NE1   1 
ATOM   114   C CE2   . TRP A 1 1340 ? 100.830 155.339 116.372 1.00 102.90 ? 1340 TRP A CE2   1 
ATOM   115   C CE3   . TRP A 1 1340 ? 102.218 157.193 115.682 1.00 102.90 ? 1340 TRP A CE3   1 
ATOM   116   C CZ2   . TRP A 1 1340 ? 101.935 154.503 116.512 1.00 102.90 ? 1340 TRP A CZ2   1 
ATOM   117   C CZ3   . TRP A 1 1340 ? 103.314 156.361 115.822 1.00 102.90 ? 1340 TRP A CZ3   1 
ATOM   118   C CH2   . TRP A 1 1340 ? 103.165 155.031 116.234 1.00 102.90 ? 1340 TRP A CH2   1 
ATOM   119   N N     . GLU A 1 1341 ? 98.988  161.792 115.532 1.00 102.21 ? 1341 GLU A N     1 
ATOM   120   C CA    . GLU A 1 1341 ? 99.186  163.089 114.894 1.00 102.21 ? 1341 GLU A CA    1 
ATOM   121   C C     . GLU A 1 1341 ? 100.045 164.001 115.760 1.00 102.21 ? 1341 GLU A C     1 
ATOM   122   O O     . GLU A 1 1341 ? 100.943 164.681 115.252 1.00 102.21 ? 1341 GLU A O     1 
ATOM   123   C CB    . GLU A 1 1341 ? 97.836  163.744 114.599 1.00 102.21 ? 1341 GLU A CB    1 
ATOM   124   C CG    . GLU A 1 1341 ? 97.079  163.118 113.439 1.00 102.21 ? 1341 GLU A CG    1 
ATOM   125   C CD    . GLU A 1 1341 ? 98.003  162.580 112.362 1.00 102.21 ? 1341 GLU A CD    1 
ATOM   126   O OE1   . GLU A 1 1341 ? 98.669  163.393 111.686 1.00 102.21 ? 1341 GLU A OE1   1 
ATOM   127   O OE2   . GLU A 1 1341 ? 98.063  161.344 112.194 1.00 102.21 ? 1341 GLU A OE2   1 
ATOM   128   N N     . GLN A 1 1342 ? 99.787  164.023 117.069 1.00 101.98 ? 1342 GLN A N     1 
ATOM   129   C CA    . GLN A 1 1342 ? 100.611 164.825 117.971 1.00 101.98 ? 1342 GLN A CA    1 
ATOM   130   C C     . GLN A 1 1342 ? 102.067 164.372 117.931 1.00 101.98 ? 1342 GLN A C     1 
ATOM   131   O O     . GLN A 1 1342 ? 102.989 165.196 117.857 1.00 101.98 ? 1342 GLN A O     1 
ATOM   132   C CB    . GLN A 1 1342 ? 100.065 164.740 119.397 1.00 101.98 ? 1342 GLN A CB    1 
ATOM   133   C CG    . GLN A 1 1342 ? 98.717  165.405 119.599 1.00 101.98 ? 1342 GLN A CG    1 
ATOM   134   C CD    . GLN A 1 1342 ? 98.844  166.886 119.892 1.00 101.98 ? 1342 GLN A CD    1 
ATOM   135   O OE1   . GLN A 1 1342 ? 99.942  167.392 120.125 1.00 101.98 ? 1342 GLN A OE1   1 
ATOM   136   N NE2   . GLN A 1 1342 ? 97.718  167.589 119.888 1.00 101.98 ? 1342 GLN A NE2   1 
ATOM   137   N N     . ILE A 1 1343 ? 102.289 163.057 117.966 1.00 103.04 ? 1343 ILE A N     1 
ATOM   138   C CA    . ILE A 1 1343 ? 103.649 162.524 117.975 1.00 103.04 ? 1343 ILE A CA    1 
ATOM   139   C C     . ILE A 1 1343 ? 104.365 162.851 116.671 1.00 103.04 ? 1343 ILE A C     1 
ATOM   140   O O     . ILE A 1 1343 ? 105.548 163.207 116.670 1.00 103.04 ? 1343 ILE A O     1 
ATOM   141   C CB    . ILE A 1 1343 ? 103.630 161.009 118.251 1.00 103.04 ? 1343 ILE A CB    1 
ATOM   142   C CG1   . ILE A 1 1343 ? 103.200 160.732 119.691 1.00 103.04 ? 1343 ILE A CG1   1 
ATOM   143   C CG2   . ILE A 1 1343 ? 104.993 160.394 117.982 1.00 103.04 ? 1343 ILE A CG2   1 
ATOM   144   C CD1   . ILE A 1 1343 ? 103.032 159.261 119.997 1.00 103.04 ? 1343 ILE A CD1   1 
ATOM   145   N N     . ASP A 1 1344 ? 103.665 162.725 115.540 1.00 104.05 ? 1344 ASP A N     1 
ATOM   146   C CA    . ASP A 1 1344 ? 104.279 163.043 114.255 1.00 104.05 ? 1344 ASP A CA    1 
ATOM   147   C C     . ASP A 1 1344 ? 104.601 164.529 114.151 1.00 104.05 ? 1344 ASP A C     1 
ATOM   148   O O     . ASP A 1 1344 ? 105.693 164.907 113.707 1.00 104.05 ? 1344 ASP A O     1 
ATOM   149   C CB    . ASP A 1 1344 ? 103.364 162.606 113.113 1.00 104.05 ? 1344 ASP A CB    1 
ATOM   150   C CG    . ASP A 1 1344 ? 103.166 161.103 113.071 1.00 104.05 ? 1344 ASP A CG    1 
ATOM   151   O OD1   . ASP A 1 1344 ? 103.835 160.392 113.853 1.00 104.05 ? 1344 ASP A OD1   1 
ATOM   152   O OD2   . ASP A 1 1344 ? 102.342 160.632 112.260 1.00 104.05 ? 1344 ASP A OD2   1 
ATOM   153   N N     . GLN A 1 1345 ? 103.668 165.390 114.571 1.00 102.06 ? 1345 GLN A N     1 
ATOM   154   C CA    . GLN A 1 1345 ? 103.927 166.826 114.552 1.00 102.06 ? 1345 GLN A CA    1 
ATOM   155   C C     . GLN A 1 1345 ? 105.119 167.186 115.425 1.00 102.06 ? 1345 GLN A C     1 
ATOM   156   O O     . GLN A 1 1345 ? 105.884 168.099 115.095 1.00 102.06 ? 1345 GLN A O     1 
ATOM   157   C CB    . GLN A 1 1345 ? 102.690 167.600 115.003 1.00 102.06 ? 1345 GLN A CB    1 
ATOM   158   C CG    . GLN A 1 1345 ? 101.507 167.505 114.060 1.00 102.06 ? 1345 GLN A CG    1 
ATOM   159   C CD    . GLN A 1 1345 ? 100.194 167.819 114.748 1.00 102.06 ? 1345 GLN A CD    1 
ATOM   160   O OE1   . GLN A 1 1345 ? 100.164 168.161 115.930 1.00 102.06 ? 1345 GLN A OE1   1 
ATOM   161   N NE2   . GLN A 1 1345 ? 99.099  167.720 114.003 1.00 102.06 ? 1345 GLN A NE2   1 
ATOM   162   N N     . MET A 1 1346 ? 105.284 166.494 116.552 1.00 102.23 ? 1346 MET A N     1 
ATOM   163   C CA    . MET A 1 1346 ? 106.423 166.794 117.409 1.00 102.23 ? 1346 MET A CA    1 
ATOM   164   C C     . MET A 1 1346 ? 107.709 166.282 116.766 1.00 102.23 ? 1346 MET A C     1 
ATOM   165   O O     . MET A 1 1346 ? 108.715 166.998 116.715 1.00 102.23 ? 1346 MET A O     1 
ATOM   166   C CB    . MET A 1 1346 ? 106.190 166.177 118.792 1.00 102.23 ? 1346 MET A CB    1 
ATOM   167   C CG    . MET A 1 1346 ? 107.408 165.923 119.670 1.00 102.23 ? 1346 MET A CG    1 
ATOM   168   S SD    . MET A 1 1346 ? 108.578 167.296 119.752 1.00 102.23 ? 1346 MET A SD    1 
ATOM   169   C CE    . MET A 1 1346 ? 110.114 166.445 119.473 1.00 102.23 ? 1346 MET A CE    1 
ATOM   170   N N     . LYS A 1 1347 ? 107.667 165.077 116.189 1.00 99.76  ? 1347 LYS A N     1 
ATOM   171   C CA    . LYS A 1 1347 ? 108.844 164.507 115.546 1.00 99.76  ? 1347 LYS A CA    1 
ATOM   172   C C     . LYS A 1 1347 ? 109.250 165.265 114.291 1.00 99.76  ? 1347 LYS A C     1 
ATOM   173   O O     . LYS A 1 1347 ? 110.377 165.084 113.814 1.00 99.76  ? 1347 LYS A O     1 
ATOM   174   C CB    . LYS A 1 1347 ? 108.594 163.043 115.194 1.00 99.76  ? 1347 LYS A CB    1 
ATOM   175   C CG    . LYS A 1 1347 ? 108.763 162.107 116.368 1.00 99.76  ? 1347 LYS A CG    1 
ATOM   176   C CD    . LYS A 1 1347 ? 108.096 160.777 116.109 1.00 99.76  ? 1347 LYS A CD    1 
ATOM   177   C CE    . LYS A 1 1347 ? 108.717 160.084 114.914 1.00 99.76  ? 1347 LYS A CE    1 
ATOM   178   N NZ    . LYS A 1 1347 ? 108.064 158.778 114.647 1.00 99.76  ? 1347 LYS A NZ    1 
ATOM   179   N N     . GLU A 1 1348 ? 108.368 166.105 113.743 1.00 97.65  ? 1348 GLU A N     1 
ATOM   180   C CA    . GLU A 1 1348 ? 108.771 166.961 112.631 1.00 97.65  ? 1348 GLU A CA    1 
ATOM   181   C C     . GLU A 1 1348 ? 109.848 167.963 113.030 1.00 97.65  ? 1348 GLU A C     1 
ATOM   182   O O     . GLU A 1 1348 ? 110.471 168.564 112.149 1.00 97.65  ? 1348 GLU A O     1 
ATOM   183   C CB    . GLU A 1 1348 ? 107.564 167.710 112.058 1.00 97.65  ? 1348 GLU A CB    1 
ATOM   184   C CG    . GLU A 1 1348 ? 106.556 166.831 111.343 1.00 97.65  ? 1348 GLU A CG    1 
ATOM   185   C CD    . GLU A 1 1348 ? 107.218 165.798 110.457 1.00 97.65  ? 1348 GLU A CD    1 
ATOM   186   O OE1   . GLU A 1 1348 ? 107.903 166.191 109.489 1.00 97.65  ? 1348 GLU A OE1   1 
ATOM   187   O OE2   . GLU A 1 1348 ? 107.050 164.591 110.727 1.00 97.65  ? 1348 GLU A OE2   1 
ATOM   188   N N     . GLN A 1 1349 ? 110.070 168.169 114.325 1.00 95.41  ? 1349 GLN A N     1 
ATOM   189   C CA    . GLN A 1 1349 ? 111.087 169.116 114.765 1.00 95.41  ? 1349 GLN A CA    1 
ATOM   190   C C     . GLN A 1 1349 ? 112.476 168.608 114.386 1.00 95.41  ? 1349 GLN A C     1 
ATOM   191   O O     . GLN A 1 1349 ? 112.821 167.462 114.707 1.00 95.41  ? 1349 GLN A O     1 
ATOM   192   C CB    . GLN A 1 1349 ? 111.001 169.328 116.276 1.00 95.41  ? 1349 GLN A CB    1 
ATOM   193   C CG    . GLN A 1 1349 ? 111.573 170.650 116.759 1.00 95.41  ? 1349 GLN A CG    1 
ATOM   194   C CD    . GLN A 1 1349 ? 111.628 170.742 118.272 1.00 95.41  ? 1349 GLN A CD    1 
ATOM   195   O OE1   . GLN A 1 1349 ? 111.420 169.752 118.974 1.00 95.41  ? 1349 GLN A OE1   1 
ATOM   196   N NE2   . GLN A 1 1349 ? 111.926 171.930 118.781 1.00 95.41  ? 1349 GLN A NE2   1 
ATOM   197   N N     . PRO A 1 1350 ? 113.291 169.413 113.708 1.00 95.65  ? 1350 PRO A N     1 
ATOM   198   C CA    . PRO A 1 1350 ? 114.649 168.970 113.373 1.00 95.65  ? 1350 PRO A CA    1 
ATOM   199   C C     . PRO A 1 1350 ? 115.501 168.786 114.618 1.00 95.65  ? 1350 PRO A C     1 
ATOM   200   O O     . PRO A 1 1350 ? 115.300 169.446 115.641 1.00 95.65  ? 1350 PRO A O     1 
ATOM   201   C CB    . PRO A 1 1350 ? 115.190 170.102 112.492 1.00 95.65  ? 1350 PRO A CB    1 
ATOM   202   C CG    . PRO A 1 1350 ? 114.357 171.298 112.847 1.00 95.65  ? 1350 PRO A CG    1 
ATOM   203   C CD    . PRO A 1 1350 ? 113.000 170.763 113.194 1.00 95.65  ? 1350 PRO A CD    1 
ATOM   204   N N     . TRP A 1 1351 ? 116.473 167.875 114.509 1.00 96.84  ? 1351 TRP A N     1 
ATOM   205   C CA    . TRP A 1 1351 ? 117.336 167.553 115.641 1.00 96.84  ? 1351 TRP A CA    1 
ATOM   206   C C     . TRP A 1 1351 ? 118.040 168.784 116.197 1.00 96.84  ? 1351 TRP A C     1 
ATOM   207   O O     . TRP A 1 1351 ? 118.300 168.855 117.403 1.00 96.84  ? 1351 TRP A O     1 
ATOM   208   C CB    . TRP A 1 1351 ? 118.376 166.517 115.223 1.00 96.84  ? 1351 TRP A CB    1 
ATOM   209   C CG    . TRP A 1 1351 ? 119.338 166.156 116.306 1.00 96.84  ? 1351 TRP A CG    1 
ATOM   210   C CD1   . TRP A 1 1351 ? 120.639 166.552 116.410 1.00 96.84  ? 1351 TRP A CD1   1 
ATOM   211   C CD2   . TRP A 1 1351 ? 119.086 165.303 117.428 1.00 96.84  ? 1351 TRP A CD2   1 
ATOM   212   N NE1   . TRP A 1 1351 ? 121.209 166.010 117.537 1.00 96.84  ? 1351 TRP A NE1   1 
ATOM   213   C CE2   . TRP A 1 1351 ? 120.278 165.238 118.177 1.00 96.84  ? 1351 TRP A CE2   1 
ATOM   214   C CE3   . TRP A 1 1351 ? 117.968 164.596 117.875 1.00 96.84  ? 1351 TRP A CE3   1 
ATOM   215   C CZ2   . TRP A 1 1351 ? 120.383 164.494 119.347 1.00 96.84  ? 1351 TRP A CZ2   1 
ATOM   216   C CZ3   . TRP A 1 1351 ? 118.078 163.854 119.030 1.00 96.84  ? 1351 TRP A CZ3   1 
ATOM   217   C CH2   . TRP A 1 1351 ? 119.277 163.808 119.754 1.00 96.84  ? 1351 TRP A CH2   1 
ATOM   218   N N     . VAL A 1 1352 ? 118.357 169.755 115.339 1.00 94.92  ? 1352 VAL A N     1 
ATOM   219   C CA    . VAL A 1 1352 ? 119.079 170.938 115.793 1.00 94.92  ? 1352 VAL A CA    1 
ATOM   220   C C     . VAL A 1 1352 ? 118.230 171.747 116.767 1.00 94.92  ? 1352 VAL A C     1 
ATOM   221   O O     . VAL A 1 1352 ? 118.741 172.294 117.752 1.00 94.92  ? 1352 VAL A O     1 
ATOM   222   C CB    . VAL A 1 1352 ? 119.524 171.786 114.587 1.00 94.92  ? 1352 VAL A CB    1 
ATOM   223   C CG1   . VAL A 1 1352 ? 120.460 172.900 115.034 1.00 94.92  ? 1352 VAL A CG1   1 
ATOM   224   C CG2   . VAL A 1 1352 ? 120.189 170.906 113.539 1.00 94.92  ? 1352 VAL A CG2   1 
ATOM   225   N N     . SER A 1 1353 ? 116.924 171.828 116.518 1.00 90.53  ? 1353 SER A N     1 
ATOM   226   C CA    . SER A 1 1353 ? 116.024 172.651 117.311 1.00 90.53  ? 1353 SER A CA    1 
ATOM   227   C C     . SER A 1 1353 ? 115.226 171.853 118.338 1.00 90.53  ? 1353 SER A C     1 
ATOM   228   O O     . SER A 1 1353 ? 114.296 172.398 118.939 1.00 90.53  ? 1353 SER A O     1 
ATOM   229   C CB    . SER A 1 1353 ? 115.071 173.416 116.392 1.00 90.53  ? 1353 SER A CB    1 
ATOM   230   O OG    . SER A 1 1353 ? 114.015 172.585 115.947 1.00 90.53  ? 1353 SER A OG    1 
ATOM   231   N N     . VAL A 1 1354 ? 115.560 170.583 118.552 1.00 91.51  ? 1354 VAL A N     1 
ATOM   232   C CA    . VAL A 1 1354 ? 114.882 169.775 119.563 1.00 91.51  ? 1354 VAL A CA    1 
ATOM   233   C C     . VAL A 1 1354 ? 115.533 170.065 120.912 1.00 91.51  ? 1354 VAL A C     1 
ATOM   234   O O     . VAL A 1 1354 ? 116.679 169.679 121.155 1.00 91.51  ? 1354 VAL A O     1 
ATOM   235   C CB    . VAL A 1 1354 ? 114.937 168.280 119.227 1.00 91.51  ? 1354 VAL A CB    1 
ATOM   236   C CG1   . VAL A 1 1354 ? 114.570 167.445 120.446 1.00 91.51  ? 1354 VAL A CG1   1 
ATOM   237   C CG2   . VAL A 1 1354 ? 113.999 167.959 118.076 1.00 91.51  ? 1354 VAL A CG2   1 
ATOM   238   N N     . GLN A 1 1355 ? 114.807 170.756 121.790 1.00 90.24  ? 1355 GLN A N     1 
ATOM   239   C CA    . GLN A 1 1355 ? 115.309 171.064 123.122 1.00 90.24  ? 1355 GLN A CA    1 
ATOM   240   C C     . GLN A 1 1355 ? 115.002 169.889 124.039 1.00 90.24  ? 1355 GLN A C     1 
ATOM   241   O O     . GLN A 1 1355 ? 113.820 169.576 124.249 1.00 90.24  ? 1355 GLN A O     1 
ATOM   242   C CB    . GLN A 1 1355 ? 114.673 172.341 123.654 1.00 90.24  ? 1355 GLN A CB    1 
ATOM   243   C CG    . GLN A 1 1355 ? 114.912 172.603 125.133 1.00 90.24  ? 1355 GLN A CG    1 
ATOM   244   C CD    . GLN A 1 1355 ? 116.377 172.543 125.516 1.00 90.24  ? 1355 GLN A CD    1 
ATOM   245   O OE1   . GLN A 1 1355 ? 116.761 171.819 126.435 1.00 90.24  ? 1355 GLN A OE1   1 
ATOM   246   N NE2   . GLN A 1 1355 ? 117.205 173.305 124.810 1.00 90.24  ? 1355 GLN A NE2   1 
ATOM   247   N N     . PRO A 1 1356 ? 116.009 169.211 124.594 1.00 96.53  ? 1356 PRO A N     1 
ATOM   248   C CA    . PRO A 1 1356 ? 115.730 168.018 125.412 1.00 96.53  ? 1356 PRO A CA    1 
ATOM   249   C C     . PRO A 1 1356 ? 114.844 168.281 126.617 1.00 96.53  ? 1356 PRO A C     1 
ATOM   250   O O     . PRO A 1 1356 ? 114.011 167.430 126.951 1.00 96.53  ? 1356 PRO A O     1 
ATOM   251   C CB    . PRO A 1 1356 ? 117.131 167.554 125.834 1.00 96.53  ? 1356 PRO A CB    1 
ATOM   252   C CG    . PRO A 1 1356 ? 118.046 168.114 124.797 1.00 96.53  ? 1356 PRO A CG    1 
ATOM   253   C CD    . PRO A 1 1356 ? 117.453 169.435 124.416 1.00 96.53  ? 1356 PRO A CD    1 
ATOM   254   N N     . ARG A 1 1357 ? 114.990 169.428 127.283 1.00 94.76  ? 1357 ARG A N     1 
ATOM   255   C CA    . ARG A 1 1357 ? 114.151 169.718 128.443 1.00 94.76  ? 1357 ARG A CA    1 
ATOM   256   C C     . ARG A 1 1357 ? 112.695 169.908 128.032 1.00 94.76  ? 1357 ARG A C     1 
ATOM   257   O O     . ARG A 1 1357 ? 111.786 169.303 128.615 1.00 94.76  ? 1357 ARG A O     1 
ATOM   258   C CB    . ARG A 1 1357 ? 114.677 170.956 129.172 1.00 94.76  ? 1357 ARG A CB    1 
ATOM   259   C CG    . ARG A 1 1357 ? 116.110 170.820 129.664 1.00 94.76  ? 1357 ARG A CG    1 
ATOM   260   C CD    . ARG A 1 1357 ? 116.572 172.076 130.387 1.00 94.76  ? 1357 ARG A CD    1 
ATOM   261   N NE    . ARG A 1 1357 ? 117.942 171.956 130.871 1.00 94.76  ? 1357 ARG A NE    1 
ATOM   262   C CZ    . ARG A 1 1357 ? 118.611 172.926 131.477 1.00 94.76  ? 1357 ARG A CZ    1 
ATOM   263   N NH1   . ARG A 1 1357 ? 118.067 174.112 131.693 1.00 94.76  ? 1357 ARG A NH1   1 
ATOM   264   N NH2   . ARG A 1 1357 ? 119.860 172.701 131.877 1.00 94.76  ? 1357 ARG A NH2   1 
ATOM   265   N N     . LYS A 1 1358 ? 112.457 170.746 127.018 1.00 91.46  ? 1358 LYS A N     1 
ATOM   266   C CA    . LYS A 1 1358 ? 111.103 170.920 126.509 1.00 91.46  ? 1358 LYS A CA    1 
ATOM   267   C C     . LYS A 1 1358 ? 110.569 169.636 125.893 1.00 91.46  ? 1358 LYS A C     1 
ATOM   268   O O     . LYS A 1 1358 ? 109.369 169.356 125.994 1.00 91.46  ? 1358 LYS A O     1 
ATOM   269   C CB    . LYS A 1 1358 ? 111.062 172.058 125.490 1.00 91.46  ? 1358 LYS A CB    1 
ATOM   270   C CG    . LYS A 1 1358 ? 111.545 173.394 126.030 1.00 91.46  ? 1358 LYS A CG    1 
ATOM   271   C CD    . LYS A 1 1358 ? 111.601 174.443 124.932 1.00 91.46  ? 1358 LYS A CD    1 
ATOM   272   C CE    . LYS A 1 1358 ? 112.132 175.766 125.458 1.00 91.46  ? 1358 LYS A CE    1 
ATOM   273   N NZ    . LYS A 1 1358 ? 112.174 176.807 124.394 1.00 91.46  ? 1358 LYS A NZ    1 
ATOM   274   N N     . LEU A 1 1359 ? 111.435 168.846 125.253 1.00 92.50  ? 1359 LEU A N     1 
ATOM   275   C CA    . LEU A 1 1359 ? 111.007 167.558 124.720 1.00 92.50  ? 1359 LEU A CA    1 
ATOM   276   C C     . LEU A 1 1359 ? 110.515 166.642 125.833 1.00 92.50  ? 1359 LEU A C     1 
ATOM   277   O O     . LEU A 1 1359 ? 109.473 165.992 125.702 1.00 92.50  ? 1359 LEU A O     1 
ATOM   278   C CB    . LEU A 1 1359 ? 112.149 166.902 123.944 1.00 92.50  ? 1359 LEU A CB    1 
ATOM   279   C CG    . LEU A 1 1359 ? 112.043 165.393 123.715 1.00 92.50  ? 1359 LEU A CG    1 
ATOM   280   C CD1   . LEU A 1 1359 ? 111.037 165.081 122.624 1.00 92.50  ? 1359 LEU A CD1   1 
ATOM   281   C CD2   . LEU A 1 1359 ? 113.404 164.804 123.371 1.00 92.50  ? 1359 LEU A CD2   1 
ATOM   282   N N     . ARG A 1 1360 ? 111.253 166.587 126.945 1.00 93.94  ? 1360 ARG A N     1 
ATOM   283   C CA    . ARG A 1 1360 ? 110.832 165.761 128.072 1.00 93.94  ? 1360 ARG A CA    1 
ATOM   284   C C     . ARG A 1 1360 ? 109.527 166.272 128.671 1.00 93.94  ? 1360 ARG A C     1 
ATOM   285   O O     . ARG A 1 1360 ? 108.642 165.480 129.016 1.00 93.94  ? 1360 ARG A O     1 
ATOM   286   C CB    . ARG A 1 1360 ? 111.933 165.715 129.134 1.00 93.94  ? 1360 ARG A CB    1 
ATOM   287   C CG    . ARG A 1 1360 ? 111.420 165.564 130.560 1.00 93.94  ? 1360 ARG A CG    1 
ATOM   288   C CD    . ARG A 1 1360 ? 112.559 165.380 131.552 1.00 93.94  ? 1360 ARG A CD    1 
ATOM   289   N NE    . ARG A 1 1360 ? 112.133 165.627 132.925 1.00 93.94  ? 1360 ARG A NE    1 
ATOM   290   C CZ    . ARG A 1 1360 ? 111.390 164.795 133.644 1.00 93.94  ? 1360 ARG A CZ    1 
ATOM   291   N NH1   . ARG A 1 1360 ? 110.977 163.637 133.155 1.00 93.94  ? 1360 ARG A NH1   1 
ATOM   292   N NH2   . ARG A 1 1360 ? 111.054 165.133 134.886 1.00 93.94  ? 1360 ARG A NH2   1 
ATOM   293   N N     . GLN A 1 1361 ? 109.389 167.594 128.801 1.00 87.31  ? 1361 GLN A N     1 
ATOM   294   C CA    . GLN A 1 1361 ? 108.155 168.157 129.346 1.00 87.31  ? 1361 GLN A CA    1 
ATOM   295   C C     . GLN A 1 1361 ? 106.957 167.825 128.460 1.00 87.31  ? 1361 GLN A C     1 
ATOM   296   O O     . GLN A 1 1361 ? 105.891 167.437 128.953 1.00 87.31  ? 1361 GLN A O     1 
ATOM   297   C CB    . GLN A 1 1361 ? 108.299 169.669 129.519 1.00 87.31  ? 1361 GLN A CB    1 
ATOM   298   C CG    . GLN A 1 1361 ? 109.331 170.080 130.557 1.00 87.31  ? 1361 GLN A CG    1 
ATOM   299   C CD    . GLN A 1 1361 ? 109.828 171.498 130.358 1.00 87.31  ? 1361 GLN A CD    1 
ATOM   300   O OE1   . GLN A 1 1361 ? 109.419 172.185 129.421 1.00 87.31  ? 1361 GLN A OE1   1 
ATOM   301   N NE2   . GLN A 1 1361 ? 110.713 171.946 131.240 1.00 87.31  ? 1361 GLN A NE2   1 
ATOM   302   N N     . ASN A 1 1362 ? 107.120 167.957 127.142 1.00 87.05  ? 1362 ASN A N     1 
ATOM   303   C CA    . ASN A 1 1362 ? 106.016 167.672 126.231 1.00 87.05  ? 1362 ASN A CA    1 
ATOM   304   C C     . ASN A 1 1362 ? 105.708 166.180 126.180 1.00 87.05  ? 1362 ASN A C     1 
ATOM   305   O O     . ASN A 1 1362 ? 104.545 165.785 126.044 1.00 87.05  ? 1362 ASN A O     1 
ATOM   306   C CB    . ASN A 1 1362 ? 106.332 168.211 124.836 1.00 87.05  ? 1362 ASN A CB    1 
ATOM   307   C CG    . ASN A 1 1362 ? 106.589 169.707 124.837 1.00 87.05  ? 1362 ASN A CG    1 
ATOM   308   O OD1   . ASN A 1 1362 ? 106.418 170.378 125.855 1.00 87.05  ? 1362 ASN A OD1   1 
ATOM   309   N ND2   . ASN A 1 1362 ? 107.005 170.237 123.692 1.00 87.05  ? 1362 ASN A ND2   1 
ATOM   310   N N     . LEU A 1 1363 ? 106.733 165.333 126.293 1.00 90.23  ? 1363 LEU A N     1 
ATOM   311   C CA    . LEU A 1 1363 ? 106.494 163.895 126.361 1.00 90.23  ? 1363 LEU A CA    1 
ATOM   312   C C     . LEU A 1 1363 ? 105.740 163.526 127.632 1.00 90.23  ? 1363 LEU A C     1 
ATOM   313   O O     . LEU A 1 1363 ? 104.857 162.661 127.608 1.00 90.23  ? 1363 LEU A O     1 
ATOM   314   C CB    . LEU A 1 1363 ? 107.817 163.137 126.276 1.00 90.23  ? 1363 LEU A CB    1 
ATOM   315   C CG    . LEU A 1 1363 ? 108.416 162.979 124.877 1.00 90.23  ? 1363 LEU A CG    1 
ATOM   316   C CD1   . LEU A 1 1363 ? 109.594 162.017 124.903 1.00 90.23  ? 1363 LEU A CD1   1 
ATOM   317   C CD2   . LEU A 1 1363 ? 107.360 162.512 123.886 1.00 90.23  ? 1363 LEU A CD2   1 
ATOM   318   N N     . ASP A 1 1364 ? 106.071 164.172 128.752 1.00 88.36  ? 1364 ASP A N     1 
ATOM   319   C CA    . ASP A 1 1364 ? 105.321 163.948 129.985 1.00 88.36  ? 1364 ASP A CA    1 
ATOM   320   C C     . ASP A 1 1364 ? 103.878 164.418 129.839 1.00 88.36  ? 1364 ASP A C     1 
ATOM   321   O O     . ASP A 1 1364 ? 102.953 163.773 130.346 1.00 88.36  ? 1364 ASP A O     1 
ATOM   322   C CB    . ASP A 1 1364 ? 106.003 164.658 131.154 1.00 88.36  ? 1364 ASP A CB    1 
ATOM   323   C CG    . ASP A 1 1364 ? 105.115 164.742 132.380 1.00 88.36  ? 1364 ASP A CG    1 
ATOM   324   O OD1   . ASP A 1 1364 ? 104.698 163.680 132.888 1.00 88.36  ? 1364 ASP A OD1   1 
ATOM   325   O OD2   . ASP A 1 1364 ? 104.834 165.870 132.836 1.00 88.36  ? 1364 ASP A OD2   1 
ATOM   326   N N     . ALA A 1 1365 ? 103.670 165.546 129.156 1.00 85.87  ? 1365 ALA A N     1 
ATOM   327   C CA    . ALA A 1 1365 ? 102.310 166.014 128.903 1.00 85.87  ? 1365 ALA A CA    1 
ATOM   328   C C     . ALA A 1 1365 ? 101.530 165.017 128.052 1.00 85.87  ? 1365 ALA A C     1 
ATOM   329   O O     . ALA A 1 1365 ? 100.354 164.744 128.319 1.00 85.87  ? 1365 ALA A O     1 
ATOM   330   C CB    . ALA A 1 1365 ? 102.343 167.386 128.230 1.00 85.87  ? 1365 ALA A CB    1 
ATOM   331   N N     . LEU A 1 1366 ? 102.172 164.464 127.019 1.00 90.83  ? 1366 LEU A N     1 
ATOM   332   C CA    . LEU A 1 1366 ? 101.523 163.452 126.191 1.00 90.83  ? 1366 LEU A CA    1 
ATOM   333   C C     . LEU A 1 1366 ? 101.204 162.198 126.998 1.00 90.83  ? 1366 LEU A C     1 
ATOM   334   O O     . LEU A 1 1366 ? 100.142 161.590 126.822 1.00 90.83  ? 1366 LEU A O     1 
ATOM   335   C CB    . LEU A 1 1366 ? 102.407 163.106 124.992 1.00 90.83  ? 1366 LEU A CB    1 
ATOM   336   C CG    . LEU A 1 1366 ? 102.607 164.196 123.937 1.00 90.83  ? 1366 LEU A CG    1 
ATOM   337   C CD1   . LEU A 1 1366 ? 103.330 163.634 122.723 1.00 90.83  ? 1366 LEU A CD1   1 
ATOM   338   C CD2   . LEU A 1 1366 ? 101.274 164.807 123.533 1.00 90.83  ? 1366 LEU A CD2   1 
ATOM   339   N N     . LEU A 1 1367 ? 102.121 161.789 127.879 1.00 94.32  ? 1367 LEU A N     1 
ATOM   340   C CA    . LEU A 1 1367 ? 101.867 160.631 128.730 1.00 94.32  ? 1367 LEU A CA    1 
ATOM   341   C C     . LEU A 1 1367 ? 100.689 160.883 129.664 1.00 94.32  ? 1367 LEU A C     1 
ATOM   342   O O     . LEU A 1 1367 ? 99.859  159.993 129.883 1.00 94.32  ? 1367 LEU A O     1 
ATOM   343   C CB    . LEU A 1 1367 ? 103.122 160.281 129.528 1.00 94.32  ? 1367 LEU A CB    1 
ATOM   344   C CG    . LEU A 1 1367 ? 104.214 159.515 128.779 1.00 94.32  ? 1367 LEU A CG    1 
ATOM   345   C CD1   . LEU A 1 1367 ? 105.445 159.336 129.654 1.00 94.32  ? 1367 LEU A CD1   1 
ATOM   346   C CD2   . LEU A 1 1367 ? 103.693 158.169 128.302 1.00 94.32  ? 1367 LEU A CD2   1 
ATOM   347   N N     . ASN A 1 1368 ? 100.605 162.088 130.230 1.00 94.15  ? 1368 ASN A N     1 
ATOM   348   C CA    . ASN A 1 1368 ? 99.473  162.430 131.086 1.00 94.15  ? 1368 ASN A CA    1 
ATOM   349   C C     . ASN A 1 1368 ? 98.169  162.442 130.298 1.00 94.15  ? 1368 ASN A C     1 
ATOM   350   O O     . ASN A 1 1368 ? 97.124  162.025 130.809 1.00 94.15  ? 1368 ASN A O     1 
ATOM   351   C CB    . ASN A 1 1368 ? 99.709  163.783 131.759 1.00 94.15  ? 1368 ASN A CB    1 
ATOM   352   C CG    . ASN A 1 1368 ? 100.864 163.752 132.740 1.00 94.15  ? 1368 ASN A CG    1 
ATOM   353   O OD1   . ASN A 1 1368 ? 101.005 162.809 133.520 1.00 94.15  ? 1368 ASN A OD1   1 
ATOM   354   N ND2   . ASN A 1 1368 ? 101.695 164.786 132.710 1.00 94.15  ? 1368 ASN A ND2   1 
ATOM   355   N N     . GLN A 1 1369 ? 98.211  162.930 129.055 1.00 97.25  ? 1369 GLN A N     1 
ATOM   356   C CA    . GLN A 1 1369 ? 97.032  162.872 128.196 1.00 97.25  ? 1369 GLN A CA    1 
ATOM   357   C C     . GLN A 1 1369 ? 96.612  161.430 127.939 1.00 97.25  ? 1369 GLN A C     1 
ATOM   358   O O     . GLN A 1 1369 ? 95.419  161.106 127.962 1.00 97.25  ? 1369 GLN A O     1 
ATOM   359   C CB    . GLN A 1 1369 ? 97.308  163.594 126.877 1.00 97.25  ? 1369 GLN A CB    1 
ATOM   360   C CG    . GLN A 1 1369 ? 96.312  163.277 125.772 1.00 97.25  ? 1369 GLN A CG    1 
ATOM   361   C CD    . GLN A 1 1369 ? 96.782  163.749 124.410 1.00 97.25  ? 1369 GLN A CD    1 
ATOM   362   O OE1   . GLN A 1 1369 ? 97.854  164.338 124.279 1.00 97.25  ? 1369 GLN A OE1   1 
ATOM   363   N NE2   . GLN A 1 1369 ? 95.980  163.486 123.384 1.00 97.25  ? 1369 GLN A NE2   1 
ATOM   364   N N     . LEU A 1 1370 ? 97.584  160.549 127.690 1.00 96.74  ? 1370 LEU A N     1 
ATOM   365   C CA    . LEU A 1 1370 ? 97.279  159.136 127.488 1.00 96.74  ? 1370 LEU A CA    1 
ATOM   366   C C     . LEU A 1 1370 ? 96.657  158.520 128.735 1.00 96.74  ? 1370 LEU A C     1 
ATOM   367   O O     . LEU A 1 1370 ? 95.696  157.747 128.644 1.00 96.74  ? 1370 LEU A O     1 
ATOM   368   C CB    . LEU A 1 1370 ? 98.543  158.374 127.093 1.00 96.74  ? 1370 LEU A CB    1 
ATOM   369   C CG    . LEU A 1 1370 ? 99.012  158.507 125.645 1.00 96.74  ? 1370 LEU A CG    1 
ATOM   370   C CD1   . LEU A 1 1370 ? 100.294 157.722 125.430 1.00 96.74  ? 1370 LEU A CD1   1 
ATOM   371   C CD2   . LEU A 1 1370 ? 97.928  158.033 124.693 1.00 96.74  ? 1370 LEU A CD2   1 
ATOM   372   N N     . LYS A 1 1371 ? 97.197  158.847 129.912 1.00 94.45  ? 1371 LYS A N     1 
ATOM   373   C CA    . LYS A 1 1371 ? 96.661  158.312 131.158 1.00 94.45  ? 1371 LYS A CA    1 
ATOM   374   C C     . LYS A 1 1371 ? 95.266  158.838 131.465 1.00 94.45  ? 1371 LYS A C     1 
ATOM   375   O O     . LYS A 1 1371 ? 94.539  158.213 132.244 1.00 94.45  ? 1371 LYS A O     1 
ATOM   376   C CB    . LYS A 1 1371 ? 97.605  158.632 132.317 1.00 94.45  ? 1371 LYS A CB    1 
ATOM   377   C CG    . LYS A 1 1371 ? 98.955  157.936 132.227 1.00 94.45  ? 1371 LYS A CG    1 
ATOM   378   C CD    . LYS A 1 1371 ? 100.019 158.694 133.005 1.00 94.45  ? 1371 LYS A CD    1 
ATOM   379   C CE    . LYS A 1 1371 ? 101.402 158.107 132.764 1.00 94.45  ? 1371 LYS A CE    1 
ATOM   380   N NZ    . LYS A 1 1371 ? 102.476 158.956 133.350 1.00 94.45  ? 1371 LYS A NZ    1 
ATOM   381   N N     . SER A 1 1372 ? 94.875  159.969 130.872 1.00 99.80  ? 1372 SER A N     1 
ATOM   382   C CA    . SER A 1 1372 ? 93.545  160.523 131.097 1.00 99.80  ? 1372 SER A CA    1 
ATOM   383   C C     . SER A 1 1372 ? 92.443  159.708 130.436 1.00 99.80  ? 1372 SER A C     1 
ATOM   384   O O     . SER A 1 1372 ? 91.264  159.958 130.709 1.00 99.80  ? 1372 SER A O     1 
ATOM   385   C CB    . SER A 1 1372 ? 93.489  161.968 130.594 1.00 99.80  ? 1372 SER A CB    1 
ATOM   386   O OG    . SER A 1 1372 ? 93.611  162.022 129.185 1.00 99.80  ? 1372 SER A OG    1 
ATOM   387   N N     . PHE A 1 1373 ? 92.791  158.753 129.577 1.00 101.23 ? 1373 PHE A N     1 
ATOM   388   C CA    . PHE A 1 1373 ? 91.785  157.936 128.921 1.00 101.23 ? 1373 PHE A CA    1 
ATOM   389   C C     . PHE A 1 1373 ? 91.126  156.993 129.928 1.00 101.23 ? 1373 PHE A C     1 
ATOM   390   O O     . PHE A 1 1373 ? 91.740  156.611 130.929 1.00 101.23 ? 1373 PHE A O     1 
ATOM   391   C CB    . PHE A 1 1373 ? 92.409  157.129 127.786 1.00 101.23 ? 1373 PHE A CB    1 
ATOM   392   C CG    . PHE A 1 1373 ? 92.875  157.966 126.628 1.00 101.23 ? 1373 PHE A CG    1 
ATOM   393   C CD1   . PHE A 1 1373 ? 92.455  159.278 126.487 1.00 101.23 ? 1373 PHE A CD1   1 
ATOM   394   C CD2   . PHE A 1 1373 ? 93.734  157.439 125.678 1.00 101.23 ? 1373 PHE A CD2   1 
ATOM   395   C CE1   . PHE A 1 1373 ? 92.885  160.049 125.424 1.00 101.23 ? 1373 PHE A CE1   1 
ATOM   396   C CE2   . PHE A 1 1373 ? 94.167  158.203 124.613 1.00 101.23 ? 1373 PHE A CE2   1 
ATOM   397   C CZ    . PHE A 1 1373 ? 93.742  159.510 124.485 1.00 101.23 ? 1373 PHE A CZ    1 
ATOM   398   N N     . PRO A 1 1374 ? 89.873  156.610 129.690 1.00 98.48  ? 1374 PRO A N     1 
ATOM   399   C CA    . PRO A 1 1374 ? 89.206  155.667 130.593 1.00 98.48  ? 1374 PRO A CA    1 
ATOM   400   C C     . PRO A 1 1374 ? 89.871  154.299 130.568 1.00 98.48  ? 1374 PRO A C     1 
ATOM   401   O O     . PRO A 1 1374 ? 90.604  153.945 129.643 1.00 98.48  ? 1374 PRO A O     1 
ATOM   402   C CB    . PRO A 1 1374 ? 87.774  155.597 130.047 1.00 98.48  ? 1374 PRO A CB    1 
ATOM   403   C CG    . PRO A 1 1374 ? 87.608  156.845 129.242 1.00 98.48  ? 1374 PRO A CG    1 
ATOM   404   C CD    . PRO A 1 1374 ? 88.958  157.131 128.662 1.00 98.48  ? 1374 PRO A CD    1 
ATOM   405   N N     . ALA A 1 1375 ? 89.601  153.526 131.624 1.00 97.94  ? 1375 ALA A N     1 
ATOM   406   C CA    . ALA A 1 1375 ? 90.226  152.215 131.768 1.00 97.94  ? 1375 ALA A CA    1 
ATOM   407   C C     . ALA A 1 1375 ? 89.831  151.278 130.633 1.00 97.94  ? 1375 ALA A C     1 
ATOM   408   O O     . ALA A 1 1375 ? 90.634  150.440 130.203 1.00 97.94  ? 1375 ALA A O     1 
ATOM   409   C CB    . ALA A 1 1375 ? 89.860  151.604 133.120 1.00 97.94  ? 1375 ALA A CB    1 
ATOM   410   N N     . ARG A 1 1376 ? 88.595  151.397 130.139 1.00 99.61  ? 1376 ARG A N     1 
ATOM   411   C CA    . ARG A 1 1376 ? 88.163  150.553 129.028 1.00 99.61  ? 1376 ARG A CA    1 
ATOM   412   C C     . ARG A 1 1376 ? 88.985  150.826 127.776 1.00 99.61  ? 1376 ARG A C     1 
ATOM   413   O O     . ARG A 1 1376 ? 89.357  149.895 127.052 1.00 99.61  ? 1376 ARG A O     1 
ATOM   414   C CB    . ARG A 1 1376 ? 86.674  150.766 128.752 1.00 99.61  ? 1376 ARG A CB    1 
ATOM   415   C CG    . ARG A 1 1376 ? 86.250  152.225 128.673 1.00 99.61  ? 1376 ARG A CG    1 
ATOM   416   C CD    . ARG A 1 1376 ? 84.848  152.361 128.101 1.00 99.61  ? 1376 ARG A CD    1 
ATOM   417   N NE    . ARG A 1 1376 ? 84.484  153.755 127.874 1.00 99.61  ? 1376 ARG A NE    1 
ATOM   418   C CZ    . ARG A 1 1376 ? 83.346  154.151 127.322 1.00 99.61  ? 1376 ARG A CZ    1 
ATOM   419   N NH1   . ARG A 1 1376 ? 82.431  153.284 126.924 1.00 99.61  ? 1376 ARG A NH1   1 
ATOM   420   N NH2   . ARG A 1 1376 ? 83.119  155.453 127.166 1.00 99.61  ? 1376 ARG A NH2   1 
ATOM   421   N N     . LEU A 1 1377 ? 89.280  152.099 127.502 1.00 98.38  ? 1377 LEU A N     1 
ATOM   422   C CA    . LEU A 1 1377 ? 90.094  152.433 126.338 1.00 98.38  ? 1377 LEU A CA    1 
ATOM   423   C C     . LEU A 1 1377 ? 91.561  152.086 126.558 1.00 98.38  ? 1377 LEU A C     1 
ATOM   424   O O     . LEU A 1 1377 ? 92.308  151.917 125.589 1.00 98.38  ? 1377 LEU A O     1 
ATOM   425   C CB    . LEU A 1 1377 ? 89.945  153.916 126.000 1.00 98.38  ? 1377 LEU A CB    1 
ATOM   426   C CG    . LEU A 1 1377 ? 88.527  154.412 125.705 1.00 98.38  ? 1377 LEU A CG    1 
ATOM   427   C CD1   . LEU A 1 1377 ? 88.553  155.852 125.217 1.00 98.38  ? 1377 LEU A CD1   1 
ATOM   428   C CD2   . LEU A 1 1377 ? 87.837  153.511 124.693 1.00 98.38  ? 1377 LEU A CD2   1 
ATOM   429   N N     . ARG A 1 1378 ? 91.991  151.976 127.818 1.00 98.84  ? 1378 ARG A N     1 
ATOM   430   C CA    . ARG A 1 1378 ? 93.394  151.697 128.105 1.00 98.84  ? 1378 ARG A CA    1 
ATOM   431   C C     . ARG A 1 1378 ? 93.760  150.236 127.878 1.00 98.84  ? 1378 ARG A C     1 
ATOM   432   O O     . ARG A 1 1378 ? 94.950  149.919 127.772 1.00 98.84  ? 1378 ARG A O     1 
ATOM   433   C CB    . ARG A 1 1378 ? 93.727  152.096 129.543 1.00 98.84  ? 1378 ARG A CB    1 
ATOM   434   C CG    . ARG A 1 1378 ? 93.824  153.598 129.764 1.00 98.84  ? 1378 ARG A CG    1 
ATOM   435   C CD    . ARG A 1 1378 ? 94.339  153.920 131.158 1.00 98.84  ? 1378 ARG A CD    1 
ATOM   436   N NE    . ARG A 1 1378 ? 93.271  153.927 132.150 1.00 98.84  ? 1378 ARG A NE    1 
ATOM   437   C CZ    . ARG A 1 1378 ? 93.442  154.220 133.432 1.00 98.84  ? 1378 ARG A CZ    1 
ATOM   438   N NH1   . ARG A 1 1378 ? 94.632  154.536 133.916 1.00 98.84  ? 1378 ARG A NH1   1 
ATOM   439   N NH2   . ARG A 1 1378 ? 92.393  154.192 134.249 1.00 98.84  ? 1378 ARG A NH2   1 
ATOM   440   N N     . GLN A 1 1379 ? 92.774  149.341 127.800 1.00 98.58  ? 1379 GLN A N     1 
ATOM   441   C CA    . GLN A 1 1379 ? 93.049  147.922 127.611 1.00 98.58  ? 1379 GLN A CA    1 
ATOM   442   C C     . GLN A 1 1379 ? 93.356  147.559 126.166 1.00 98.58  ? 1379 GLN A C     1 
ATOM   443   O O     . GLN A 1 1379 ? 93.790  146.430 125.909 1.00 98.58  ? 1379 GLN A O     1 
ATOM   444   C CB    . GLN A 1 1379 ? 91.862  147.088 128.103 1.00 98.58  ? 1379 GLN A CB    1 
ATOM   445   C CG    . GLN A 1 1379 ? 91.547  147.263 129.578 1.00 98.58  ? 1379 GLN A CG    1 
ATOM   446   C CD    . GLN A 1 1379 ? 90.117  146.889 129.914 1.00 98.58  ? 1379 GLN A CD    1 
ATOM   447   O OE1   . GLN A 1 1379 ? 89.362  146.440 129.052 1.00 98.58  ? 1379 GLN A OE1   1 
ATOM   448   N NE2   . GLN A 1 1379 ? 89.737  147.074 131.174 1.00 98.58  ? 1379 GLN A NE2   1 
ATOM   449   N N     . TYR A 1 1380 ? 93.144  148.472 125.223 1.00 96.53  ? 1380 TYR A N     1 
ATOM   450   C CA    . TYR A 1 1380 ? 93.366  148.166 123.818 1.00 96.53  ? 1380 TYR A CA    1 
ATOM   451   C C     . TYR A 1 1380 ? 94.854  148.017 123.522 1.00 96.53  ? 1380 TYR A C     1 
ATOM   452   O O     . TYR A 1 1380 ? 95.701  148.703 124.101 1.00 96.53  ? 1380 TYR A O     1 
ATOM   453   C CB    . TYR A 1 1380 ? 92.753  149.255 122.937 1.00 96.53  ? 1380 TYR A CB    1 
ATOM   454   C CG    . TYR A 1 1380 ? 91.243  149.183 122.864 1.00 96.53  ? 1380 TYR A CG    1 
ATOM   455   C CD1   . TYR A 1 1380 ? 90.611  148.227 122.081 1.00 96.53  ? 1380 TYR A CD1   1 
ATOM   456   C CD2   . TYR A 1 1380 ? 90.452  150.062 123.591 1.00 96.53  ? 1380 TYR A CD2   1 
ATOM   457   C CE1   . TYR A 1 1380 ? 89.232  148.157 122.016 1.00 96.53  ? 1380 TYR A CE1   1 
ATOM   458   C CE2   . TYR A 1 1380 ? 89.073  150.001 123.532 1.00 96.53  ? 1380 TYR A CE2   1 
ATOM   459   C CZ    . TYR A 1 1380 ? 88.469  149.045 122.744 1.00 96.53  ? 1380 TYR A CZ    1 
ATOM   460   O OH    . TYR A 1 1380 ? 87.095  148.979 122.683 1.00 96.53  ? 1380 TYR A OH    1 
ATOM   461   N N     . ALA A 1 1381 ? 95.166  147.100 122.603 1.00 92.76  ? 1381 ALA A N     1 
ATOM   462   C CA    . ALA A 1 1381 ? 96.560  146.793 122.294 1.00 92.76  ? 1381 ALA A CA    1 
ATOM   463   C C     . ALA A 1 1381 ? 97.275  147.987 121.671 1.00 92.76  ? 1381 ALA A C     1 
ATOM   464   O O     . ALA A 1 1381 ? 98.451  148.232 121.965 1.00 92.76  ? 1381 ALA A O     1 
ATOM   465   C CB    . ALA A 1 1381 ? 96.636  145.581 121.366 1.00 92.76  ? 1381 ALA A CB    1 
ATOM   466   N N     . SER A 1 1382 ? 96.590  148.729 120.797 1.00 94.58  ? 1382 SER A N     1 
ATOM   467   C CA    . SER A 1 1382 ? 97.217  149.878 120.151 1.00 94.58  ? 1382 SER A CA    1 
ATOM   468   C C     . SER A 1 1382 ? 97.588  150.952 121.167 1.00 94.58  ? 1382 SER A C     1 
ATOM   469   O O     . SER A 1 1382 ? 98.666  151.554 121.081 1.00 94.58  ? 1382 SER A O     1 
ATOM   470   C CB    . SER A 1 1382 ? 96.285  150.448 119.082 1.00 94.58  ? 1382 SER A CB    1 
ATOM   471   O OG    . SER A 1 1382 ? 96.085  149.517 118.032 1.00 94.58  ? 1382 SER A OG    1 
ATOM   472   N N     . TYR A 1 1383 ? 96.703  151.209 122.135 1.00 98.74  ? 1383 TYR A N     1 
ATOM   473   C CA    . TYR A 1 1383 ? 97.015  152.180 123.177 1.00 98.74  ? 1383 TYR A CA    1 
ATOM   474   C C     . TYR A 1 1383 ? 98.213  151.730 124.003 1.00 98.74  ? 1383 TYR A C     1 
ATOM   475   O O     . TYR A 1 1383 ? 99.073  152.545 124.356 1.00 98.74  ? 1383 TYR A O     1 
ATOM   476   C CB    . TYR A 1 1383 ? 95.798  152.403 124.075 1.00 98.74  ? 1383 TYR A CB    1 
ATOM   477   C CG    . TYR A 1 1383 ? 96.097  153.206 125.324 1.00 98.74  ? 1383 TYR A CG    1 
ATOM   478   C CD1   . TYR A 1 1383 ? 96.091  154.594 125.299 1.00 98.74  ? 1383 TYR A CD1   1 
ATOM   479   C CD2   . TYR A 1 1383 ? 96.384  152.574 126.530 1.00 98.74  ? 1383 TYR A CD2   1 
ATOM   480   C CE1   . TYR A 1 1383 ? 96.365  155.331 126.438 1.00 98.74  ? 1383 TYR A CE1   1 
ATOM   481   C CE2   . TYR A 1 1383 ? 96.658  153.302 127.671 1.00 98.74  ? 1383 TYR A CE2   1 
ATOM   482   C CZ    . TYR A 1 1383 ? 96.647  154.679 127.620 1.00 98.74  ? 1383 TYR A CZ    1 
ATOM   483   O OH    . TYR A 1 1383 ? 96.918  155.407 128.756 1.00 98.74  ? 1383 TYR A OH    1 
ATOM   484   N N     . GLU A 1 1384 ? 98.281  150.436 124.327 1.00 95.86  ? 1384 GLU A N     1 
ATOM   485   C CA    . GLU A 1 1384 ? 99.423  149.918 125.073 1.00 95.86  ? 1384 GLU A CA    1 
ATOM   486   C C     . GLU A 1 1384 ? 100.713 150.073 124.280 1.00 95.86  ? 1384 GLU A C     1 
ATOM   487   O O     . GLU A 1 1384 ? 101.755 150.434 124.839 1.00 95.86  ? 1384 GLU A O     1 
ATOM   488   C CB    . GLU A 1 1384 ? 99.190  148.452 125.438 1.00 95.86  ? 1384 GLU A CB    1 
ATOM   489   C CG    . GLU A 1 1384 ? 98.024  148.221 126.383 1.00 95.86  ? 1384 GLU A CG    1 
ATOM   490   C CD    . GLU A 1 1384 ? 97.792  146.751 126.669 1.00 95.86  ? 1384 GLU A CD    1 
ATOM   491   O OE1   . GLU A 1 1384 ? 98.703  145.941 126.398 1.00 95.86  ? 1384 GLU A OE1   1 
ATOM   492   O OE2   . GLU A 1 1384 ? 96.699  146.404 127.164 1.00 95.86  ? 1384 GLU A OE2   1 
ATOM   493   N N     . PHE A 1 1385 ? 100.664 149.798 122.975 1.00 100.22 ? 1385 PHE A N     1 
ATOM   494   C CA    . PHE A 1 1385 ? 101.850 149.951 122.138 1.00 100.22 ? 1385 PHE A CA    1 
ATOM   495   C C     . PHE A 1 1385 ? 102.303 151.404 122.082 1.00 100.22 ? 1385 PHE A C     1 
ATOM   496   O O     . PHE A 1 1385 ? 103.501 151.692 122.184 1.00 100.22 ? 1385 PHE A O     1 
ATOM   497   C CB    . PHE A 1 1385 ? 101.570 149.419 120.732 1.00 100.22 ? 1385 PHE A CB    1 
ATOM   498   C CG    . PHE A 1 1385 ? 102.467 149.997 119.675 1.00 100.22 ? 1385 PHE A CG    1 
ATOM   499   C CD1   . PHE A 1 1385 ? 103.812 149.666 119.629 1.00 100.22 ? 1385 PHE A CD1   1 
ATOM   500   C CD2   . PHE A 1 1385 ? 101.966 150.872 118.724 1.00 100.22 ? 1385 PHE A CD2   1 
ATOM   501   C CE1   . PHE A 1 1385 ? 104.638 150.196 118.657 1.00 100.22 ? 1385 PHE A CE1   1 
ATOM   502   C CE2   . PHE A 1 1385 ? 102.788 151.405 117.750 1.00 100.22 ? 1385 PHE A CE2   1 
ATOM   503   C CZ    . PHE A 1 1385 ? 104.126 151.067 117.716 1.00 100.22 ? 1385 PHE A CZ    1 
ATOM   504   N N     . VAL A 1 1386 ? 101.359 152.335 121.929 1.00 98.64  ? 1386 VAL A N     1 
ATOM   505   C CA    . VAL A 1 1386 ? 101.716 153.752 121.893 1.00 98.64  ? 1386 VAL A CA    1 
ATOM   506   C C     . VAL A 1 1386 ? 102.301 154.191 123.232 1.00 98.64  ? 1386 VAL A C     1 
ATOM   507   O O     . VAL A 1 1386 ? 103.303 154.918 123.283 1.00 98.64  ? 1386 VAL A O     1 
ATOM   508   C CB    . VAL A 1 1386 ? 100.494 154.599 121.493 1.00 98.64  ? 1386 VAL A CB    1 
ATOM   509   C CG1   . VAL A 1 1386 ? 100.626 156.021 122.019 1.00 98.64  ? 1386 VAL A CG1   1 
ATOM   510   C CG2   . VAL A 1 1386 ? 100.327 154.602 119.982 1.00 98.64  ? 1386 VAL A CG2   1 
ATOM   511   N N     . GLN A 1 1387 ? 101.687 153.752 124.335 1.00 97.80  ? 1387 GLN A N     1 
ATOM   512   C CA    . GLN A 1 1387 ? 102.178 154.123 125.657 1.00 97.80  ? 1387 GLN A CA    1 
ATOM   513   C C     . GLN A 1 1387 ? 103.578 153.577 125.904 1.00 97.80  ? 1387 GLN A C     1 
ATOM   514   O O     . GLN A 1 1387 ? 104.435 154.279 126.450 1.00 97.80  ? 1387 GLN A O     1 
ATOM   515   C CB    . GLN A 1 1387 ? 101.212 153.632 126.734 1.00 97.80  ? 1387 GLN A CB    1 
ATOM   516   C CG    . GLN A 1 1387 ? 101.310 154.396 128.046 1.00 97.80  ? 1387 GLN A CG    1 
ATOM   517   C CD    . GLN A 1 1387 ? 100.079 154.225 128.914 1.00 97.80  ? 1387 GLN A CD    1 
ATOM   518   O OE1   . GLN A 1 1387 ? 99.387  155.194 129.228 1.00 97.80  ? 1387 GLN A OE1   1 
ATOM   519   N NE2   . GLN A 1 1387 ? 99.801  152.988 129.309 1.00 97.80  ? 1387 GLN A NE2   1 
ATOM   520   N N     . ARG A 1 1388 ? 103.834 152.327 125.510 1.00 96.41  ? 1388 ARG A N     1 
ATOM   521   C CA    . ARG A 1 1388 ? 105.163 151.764 125.723 1.00 96.41  ? 1388 ARG A CA    1 
ATOM   522   C C     . ARG A 1 1388 ? 106.193 152.386 124.787 1.00 96.41  ? 1388 ARG A C     1 
ATOM   523   O O     . ARG A 1 1388 ? 107.363 152.514 125.160 1.00 96.41  ? 1388 ARG A O     1 
ATOM   524   C CB    . ARG A 1 1388 ? 105.136 150.241 125.570 1.00 96.41  ? 1388 ARG A CB    1 
ATOM   525   C CG    . ARG A 1 1388 ? 104.936 149.729 124.157 1.00 96.41  ? 1388 ARG A CG    1 
ATOM   526   C CD    . ARG A 1 1388 ? 104.854 148.210 124.140 1.00 96.41  ? 1388 ARG A CD    1 
ATOM   527   N NE    . ARG A 1 1388 ? 104.551 147.687 122.813 1.00 96.41  ? 1388 ARG A NE    1 
ATOM   528   C CZ    . ARG A 1 1388 ? 105.464 147.401 121.895 1.00 96.41  ? 1388 ARG A CZ    1 
ATOM   529   N NH1   . ARG A 1 1388 ? 106.754 147.585 122.122 1.00 96.41  ? 1388 ARG A NH1   1 
ATOM   530   N NH2   . ARG A 1 1388 ? 105.073 146.917 120.720 1.00 96.41  ? 1388 ARG A NH2   1 
ATOM   531   N N     . LEU A 1 1389 ? 105.783 152.800 123.585 1.00 93.46  ? 1389 LEU A N     1 
ATOM   532   C CA    . LEU A 1 1389 ? 106.696 153.531 122.712 1.00 93.46  ? 1389 LEU A CA    1 
ATOM   533   C C     . LEU A 1 1389 ? 107.071 154.878 123.319 1.00 93.46  ? 1389 LEU A C     1 
ATOM   534   O O     . LEU A 1 1389 ? 108.241 155.281 123.288 1.00 93.46  ? 1389 LEU A O     1 
ATOM   535   C CB    . LEU A 1 1389 ? 106.065 153.712 121.331 1.00 93.46  ? 1389 LEU A CB    1 
ATOM   536   C CG    . LEU A 1 1389 ? 106.952 154.316 120.243 1.00 93.46  ? 1389 LEU A CG    1 
ATOM   537   C CD1   . LEU A 1 1389 ? 107.842 153.247 119.629 1.00 93.46  ? 1389 LEU A CD1   1 
ATOM   538   C CD2   . LEU A 1 1389 ? 106.107 154.992 119.173 1.00 93.46  ? 1389 LEU A CD2   1 
ATOM   539   N N     . LEU A 1 1390 ? 106.092 155.585 123.888 1.00 93.94  ? 1390 LEU A N     1 
ATOM   540   C CA    . LEU A 1 1390 ? 106.392 156.850 124.555 1.00 93.94  ? 1390 LEU A CA    1 
ATOM   541   C C     . LEU A 1 1390 ? 107.246 156.630 125.800 1.00 93.94  ? 1390 LEU A C     1 
ATOM   542   O O     . LEU A 1 1390 ? 108.110 157.454 126.122 1.00 93.94  ? 1390 LEU A O     1 
ATOM   543   C CB    . LEU A 1 1390 ? 105.098 157.581 124.908 1.00 93.94  ? 1390 LEU A CB    1 
ATOM   544   C CG    . LEU A 1 1390 ? 104.476 158.410 123.782 1.00 93.94  ? 1390 LEU A CG    1 
ATOM   545   C CD1   . LEU A 1 1390 ? 103.381 159.318 124.321 1.00 93.94  ? 1390 LEU A CD1   1 
ATOM   546   C CD2   . LEU A 1 1390 ? 105.540 159.220 123.055 1.00 93.94  ? 1390 LEU A CD2   1 
ATOM   547   N N     . LYS A 1 1391 ? 107.018 155.526 126.513 1.00 92.83  ? 1391 LYS A N     1 
ATOM   548   C CA    . LYS A 1 1391 ? 107.855 155.194 127.661 1.00 92.83  ? 1391 LYS A CA    1 
ATOM   549   C C     . LYS A 1 1391 ? 109.292 154.921 127.234 1.00 92.83  ? 1391 LYS A C     1 
ATOM   550   O O     . LYS A 1 1391 ? 110.239 155.336 127.910 1.00 92.83  ? 1391 LYS A O     1 
ATOM   551   C CB    . LYS A 1 1391 ? 107.273 153.988 128.399 1.00 92.83  ? 1391 LYS A CB    1 
ATOM   552   C CG    . LYS A 1 1391 ? 108.215 153.355 129.410 1.00 92.83  ? 1391 LYS A CG    1 
ATOM   553   C CD    . LYS A 1 1391 ? 107.646 152.053 129.946 1.00 92.83  ? 1391 LYS A CD    1 
ATOM   554   C CE    . LYS A 1 1391 ? 107.228 151.130 128.812 1.00 92.83  ? 1391 LYS A CE    1 
ATOM   555   N NZ    . LYS A 1 1391 ? 106.565 149.896 129.313 1.00 92.83  ? 1391 LYS A NZ    1 
ATOM   556   N N     . GLY A 1 1392 ? 109.473 154.214 126.117 1.00 91.48  ? 1392 GLY A N     1 
ATOM   557   C CA    . GLY A 1 1392 ? 110.810 154.022 125.581 1.00 91.48  ? 1392 GLY A CA    1 
ATOM   558   C C     . GLY A 1 1392 ? 111.463 155.318 125.152 1.00 91.48  ? 1392 GLY A C     1 
ATOM   559   O O     . GLY A 1 1392 ? 112.670 155.500 125.332 1.00 91.48  ? 1392 GLY A O     1 
ATOM   560   N N     . TYR A 1 1393 ? 110.681 156.235 124.577 1.00 96.90  ? 1393 TYR A N     1 
ATOM   561   C CA    . TYR A 1 1393 ? 111.214 157.552 124.241 1.00 96.90  ? 1393 TYR A CA    1 
ATOM   562   C C     . TYR A 1 1393 ? 111.656 158.299 125.496 1.00 96.90  ? 1393 TYR A C     1 
ATOM   563   O O     . TYR A 1 1393 ? 112.718 158.932 125.512 1.00 96.90  ? 1393 TYR A O     1 
ATOM   564   C CB    . TYR A 1 1393 ? 110.172 158.359 123.466 1.00 96.90  ? 1393 TYR A CB    1 
ATOM   565   C CG    . TYR A 1 1393 ? 109.916 157.839 122.069 1.00 96.90  ? 1393 TYR A CG    1 
ATOM   566   C CD1   . TYR A 1 1393 ? 110.904 157.156 121.371 1.00 96.90  ? 1393 TYR A CD1   1 
ATOM   567   C CD2   . TYR A 1 1393 ? 108.686 158.026 121.451 1.00 96.90  ? 1393 TYR A CD2   1 
ATOM   568   C CE1   . TYR A 1 1393 ? 110.675 156.675 120.094 1.00 96.90  ? 1393 TYR A CE1   1 
ATOM   569   C CE2   . TYR A 1 1393 ? 108.448 157.549 120.174 1.00 96.90  ? 1393 TYR A CE2   1 
ATOM   570   C CZ    . TYR A 1 1393 ? 109.446 156.875 119.501 1.00 96.90  ? 1393 TYR A CZ    1 
ATOM   571   O OH    . TYR A 1 1393 ? 109.215 156.398 118.231 1.00 96.90  ? 1393 TYR A OH    1 
ATOM   572   N N     . MET A 1 1394 ? 110.860 158.222 126.564 1.00 97.65  ? 1394 MET A N     1 
ATOM   573   C CA    . MET A 1 1394 ? 111.256 158.834 127.830 1.00 97.65  ? 1394 MET A CA    1 
ATOM   574   C C     . MET A 1 1394 ? 112.524 158.195 128.384 1.00 97.65  ? 1394 MET A C     1 
ATOM   575   O O     . MET A 1 1394 ? 113.388 158.888 128.932 1.00 97.65  ? 1394 MET A O     1 
ATOM   576   C CB    . MET A 1 1394 ? 110.116 158.733 128.845 1.00 97.65  ? 1394 MET A CB    1 
ATOM   577   C CG    . MET A 1 1394 ? 110.294 159.565 130.125 1.00 97.65  ? 1394 MET A CG    1 
ATOM   578   S SD    . MET A 1 1394 ? 111.107 161.183 130.028 1.00 97.65  ? 1394 MET A SD    1 
ATOM   579   C CE    . MET A 1 1394 ? 110.275 161.977 128.650 1.00 97.65  ? 1394 MET A CE    1 
ATOM   580   N N     . LYS A 1 1395 ? 112.643 156.870 128.271 1.00 96.43  ? 1395 LYS A N     1 
ATOM   581   C CA    . LYS A 1 1395 ? 113.853 156.193 128.728 1.00 96.43  ? 1395 LYS A CA    1 
ATOM   582   C C     . LYS A 1 1395 ? 115.076 156.656 127.947 1.00 96.43  ? 1395 LYS A C     1 
ATOM   583   O O     . LYS A 1 1395 ? 116.123 156.950 128.535 1.00 96.43  ? 1395 LYS A O     1 
ATOM   584   C CB    . LYS A 1 1395 ? 113.694 154.678 128.597 1.00 96.43  ? 1395 LYS A CB    1 
ATOM   585   C CG    . LYS A 1 1395 ? 114.983 153.921 128.867 1.00 96.43  ? 1395 LYS A CG    1 
ATOM   586   C CD    . LYS A 1 1395 ? 114.892 152.463 128.457 1.00 96.43  ? 1395 LYS A CD    1 
ATOM   587   C CE    . LYS A 1 1395 ? 116.240 151.773 128.629 1.00 96.43  ? 1395 LYS A CE    1 
ATOM   588   N NZ    . LYS A 1 1395 ? 116.185 150.326 128.287 1.00 96.43  ? 1395 LYS A NZ    1 
ATOM   589   N N     . ILE A 1 1396 ? 114.958 156.738 126.617 1.00 96.09  ? 1396 ILE A N     1 
ATOM   590   C CA    . ILE A 1 1396 ? 116.075 157.158 125.779 1.00 96.09  ? 1396 ILE A CA    1 
ATOM   591   C C     . ILE A 1 1396 ? 116.246 158.667 125.754 1.00 96.09  ? 1396 ILE A C     1 
ATOM   592   O O     . ILE A 1 1396 ? 117.130 159.165 125.048 1.00 96.09  ? 1396 ILE A O     1 
ATOM   593   C CB    . ILE A 1 1396 ? 115.918 156.654 124.329 1.00 96.09  ? 1396 ILE A CB    1 
ATOM   594   C CG1   . ILE A 1 1396 ? 114.775 157.392 123.629 1.00 96.09  ? 1396 ILE A CG1   1 
ATOM   595   C CG2   . ILE A 1 1396 ? 115.693 155.150 124.305 1.00 96.09  ? 1396 ILE A CG2   1 
ATOM   596   C CD1   . ILE A 1 1396 ? 114.530 156.944 122.208 1.00 96.09  ? 1396 ILE A CD1   1 
ATOM   597   N N     . ASN A 1 1397 ? 115.404 159.411 126.475 1.00 96.23  ? 1397 ASN A N     1 
ATOM   598   C CA    . ASN A 1 1397 ? 115.579 160.858 126.548 1.00 96.23  ? 1397 ASN A CA    1 
ATOM   599   C C     . ASN A 1 1397 ? 116.946 161.231 127.108 1.00 96.23  ? 1397 ASN A C     1 
ATOM   600   O O     . ASN A 1 1397 ? 117.511 162.259 126.723 1.00 96.23  ? 1397 ASN A O     1 
ATOM   601   C CB    . ASN A 1 1397 ? 114.460 161.483 127.385 1.00 96.23  ? 1397 ASN A CB    1 
ATOM   602   C CG    . ASN A 1 1397 ? 114.653 162.973 127.598 1.00 96.23  ? 1397 ASN A CG    1 
ATOM   603   O OD1   . ASN A 1 1397 ? 114.804 163.733 126.641 1.00 96.23  ? 1397 ASN A OD1   1 
ATOM   604   N ND2   . ASN A 1 1397 ? 114.642 163.401 128.856 1.00 96.23  ? 1397 ASN A ND2   1 
ATOM   605   N N     . MET A 1 1398 ? 117.499 160.413 128.008 1.00 98.62  ? 1398 MET A N     1 
ATOM   606   C CA    . MET A 1 1398 ? 118.855 160.670 128.481 1.00 98.62  ? 1398 MET A CA    1 
ATOM   607   C C     . MET A 1 1398 ? 119.850 160.573 127.329 1.00 98.62  ? 1398 MET A C     1 
ATOM   608   O O     . MET A 1 1398 ? 120.765 161.398 127.212 1.00 98.62  ? 1398 MET A O     1 
ATOM   609   C CB    . MET A 1 1398 ? 119.213 159.686 129.601 1.00 98.62  ? 1398 MET A CB    1 
ATOM   610   C CG    . MET A 1 1398 ? 120.674 159.686 130.082 1.00 98.62  ? 1398 MET A CG    1 
ATOM   611   S SD    . MET A 1 1398 ? 121.581 161.257 130.144 1.00 98.62  ? 1398 MET A SD    1 
ATOM   612   C CE    . MET A 1 1398 ? 120.436 162.355 130.986 1.00 98.62  ? 1398 MET A CE    1 
ATOM   613   N N     . LEU A 1 1399 ? 119.672 159.581 126.452 1.00 99.49  ? 1399 LEU A N     1 
ATOM   614   C CA    . LEU A 1 1399 ? 120.520 159.472 125.271 1.00 99.49  ? 1399 LEU A CA    1 
ATOM   615   C C     . LEU A 1 1399 ? 120.313 160.649 124.324 1.00 99.49  ? 1399 LEU A C     1 
ATOM   616   O O     . LEU A 1 1399 ? 121.261 161.092 123.671 1.00 99.49  ? 1399 LEU A O     1 
ATOM   617   C CB    . LEU A 1 1399 ? 120.255 158.150 124.550 1.00 99.49  ? 1399 LEU A CB    1 
ATOM   618   C CG    . LEU A 1 1399 ? 121.045 156.936 125.048 1.00 99.49  ? 1399 LEU A CG    1 
ATOM   619   C CD1   . LEU A 1 1399 ? 122.516 157.276 125.165 1.00 99.49  ? 1399 LEU A CD1   1 
ATOM   620   C CD2   . LEU A 1 1399 ? 120.514 156.409 126.367 1.00 99.49  ? 1399 LEU A CD2   1 
ATOM   621   N N     . VAL A 1 1400 ? 119.083 161.156 124.226 1.00 96.66  ? 1400 VAL A N     1 
ATOM   622   C CA    . VAL A 1 1400 ? 118.835 162.383 123.463 1.00 96.66  ? 1400 VAL A CA    1 
ATOM   623   C C     . VAL A 1 1400 ? 119.615 163.556 124.046 1.00 96.66  ? 1400 VAL A C     1 
ATOM   624   O O     . VAL A 1 1400 ? 120.213 164.350 123.310 1.00 96.66  ? 1400 VAL A O     1 
ATOM   625   C CB    . VAL A 1 1400 ? 117.324 162.681 123.396 1.00 96.66  ? 1400 VAL A CB    1 
ATOM   626   C CG1   . VAL A 1 1400 ? 117.013 163.591 122.238 1.00 96.66  ? 1400 VAL A CG1   1 
ATOM   627   C CG2   . VAL A 1 1400 ? 116.557 161.400 123.188 1.00 96.66  ? 1400 VAL A CG2   1 
ATOM   628   N N     . ILE A 1 1401 ? 119.616 163.690 125.372 1.00 96.09  ? 1401 ILE A N     1 
ATOM   629   C CA    . ILE A 1 1401 ? 120.364 164.772 126.013 1.00 96.09  ? 1401 ILE A CA    1 
ATOM   630   C C     . ILE A 1 1401 ? 121.851 164.634 125.716 1.00 96.09  ? 1401 ILE A C     1 
ATOM   631   O O     . ILE A 1 1401 ? 122.536 165.611 125.386 1.00 96.09  ? 1401 ILE A O     1 
ATOM   632   C CB    . ILE A 1 1401 ? 120.102 164.782 127.527 1.00 96.09  ? 1401 ILE A CB    1 
ATOM   633   C CG1   . ILE A 1 1401 ? 118.623 165.043 127.805 1.00 96.09  ? 1401 ILE A CG1   1 
ATOM   634   C CG2   . ILE A 1 1401 ? 120.988 165.815 128.213 1.00 96.09  ? 1401 ILE A CG2   1 
ATOM   635   C CD1   . ILE A 1 1401 ? 118.305 165.205 129.263 1.00 96.09  ? 1401 ILE A CD1   1 
ATOM   636   N N     . GLU A 1 1402 ? 122.374 163.413 125.843 1.00 96.32  ? 1402 GLU A N     1 
ATOM   637   C CA    . GLU A 1 1402 ? 123.800 163.192 125.627 1.00 96.32  ? 1402 GLU A CA    1 
ATOM   638   C C     . GLU A 1 1402 ? 124.190 163.367 124.165 1.00 96.32  ? 1402 GLU A C     1 
ATOM   639   O O     . GLU A 1 1402 ? 125.312 163.793 123.873 1.00 96.32  ? 1402 GLU A O     1 
ATOM   640   C CB    . GLU A 1 1402 ? 124.202 161.804 126.125 1.00 96.32  ? 1402 GLU A CB    1 
ATOM   641   C CG    . GLU A 1 1402 ? 124.143 161.636 127.640 1.00 96.32  ? 1402 GLU A CG    1 
ATOM   642   C CD    . GLU A 1 1402 ? 124.271 160.187 128.081 1.00 96.32  ? 1402 GLU A CD    1 
ATOM   643   O OE1   . GLU A 1 1402 ? 124.286 159.294 127.209 1.00 96.32  ? 1402 GLU A OE1   1 
ATOM   644   O OE2   . GLU A 1 1402 ? 124.374 159.942 129.303 1.00 96.32  ? 1402 GLU A OE2   1 
ATOM   645   N N     . LEU A 1 1403 ? 123.289 163.042 123.235 1.00 95.78  ? 1403 LEU A N     1 
ATOM   646   C CA    . LEU A 1 1403 ? 123.612 163.174 121.819 1.00 95.78  ? 1403 LEU A CA    1 
ATOM   647   C C     . LEU A 1 1403 ? 123.664 164.636 121.396 1.00 95.78  ? 1403 LEU A C     1 
ATOM   648   O O     . LEU A 1 1403 ? 124.587 165.047 120.684 1.00 95.78  ? 1403 LEU A O     1 
ATOM   649   C CB    . LEU A 1 1403 ? 122.600 162.404 120.971 1.00 95.78  ? 1403 LEU A CB    1 
ATOM   650   C CG    . LEU A 1 1403 ? 122.832 160.902 120.794 1.00 95.78  ? 1403 LEU A CG    1 
ATOM   651   C CD1   . LEU A 1 1403 ? 121.722 160.286 119.958 1.00 95.78  ? 1403 LEU A CD1   1 
ATOM   652   C CD2   . LEU A 1 1403 ? 124.188 160.645 120.159 1.00 95.78  ? 1403 LEU A CD2   1 
ATOM   653   N N     . LYS A 1 1404 ? 122.689 165.438 121.826 1.00 92.55  ? 1404 LYS A N     1 
ATOM   654   C CA    . LYS A 1 1404 ? 122.625 166.846 121.436 1.00 92.55  ? 1404 LYS A CA    1 
ATOM   655   C C     . LYS A 1 1404 ? 123.502 167.704 122.353 1.00 92.55  ? 1404 LYS A C     1 
ATOM   656   O O     . LYS A 1 1404 ? 123.033 168.556 123.106 1.00 92.55  ? 1404 LYS A O     1 
ATOM   657   C CB    . LYS A 1 1404 ? 121.187 167.342 121.438 1.00 92.55  ? 1404 LYS A CB    1 
ATOM   658   C CG    . LYS A 1 1404 ? 120.968 168.523 120.511 1.00 92.55  ? 1404 LYS A CG    1 
ATOM   659   C CD    . LYS A 1 1404 ? 119.793 169.370 120.951 1.00 92.55  ? 1404 LYS A CD    1 
ATOM   660   C CE    . LYS A 1 1404 ? 120.143 170.189 122.183 1.00 92.55  ? 1404 LYS A CE    1 
ATOM   661   N NZ    . LYS A 1 1404 ? 121.089 171.296 121.873 1.00 92.55  ? 1404 LYS A NZ    1 
ATOM   662   N N     . SER A 1 1405 ? 124.802 167.458 122.271 1.00 91.89  ? 1405 SER A N     1 
ATOM   663   C CA    . SER A 1 1405 ? 125.800 168.231 122.992 1.00 91.89  ? 1405 SER A CA    1 
ATOM   664   C C     . SER A 1 1405 ? 126.861 168.735 122.023 1.00 91.89  ? 1405 SER A C     1 
ATOM   665   O O     . SER A 1 1405 ? 126.796 168.504 120.812 1.00 91.89  ? 1405 SER A O     1 
ATOM   666   C CB    . SER A 1 1405 ? 126.443 167.388 124.102 1.00 91.89  ? 1405 SER A CB    1 
ATOM   667   O OG    . SER A 1 1405 ? 127.542 168.064 124.688 1.00 91.89  ? 1405 SER A OG    1 
ATOM   668   N N     . GLU A 1 1406 ? 127.850 169.436 122.573 1.00 92.64  ? 1406 GLU A N     1 
ATOM   669   C CA    . GLU A 1 1406 ? 129.034 169.798 121.808 1.00 92.64  ? 1406 GLU A CA    1 
ATOM   670   C C     . GLU A 1 1406 ? 129.992 168.626 121.651 1.00 92.64  ? 1406 GLU A C     1 
ATOM   671   O O     . GLU A 1 1406 ? 131.161 168.833 121.309 1.00 92.64  ? 1406 GLU A O     1 
ATOM   672   C CB    . GLU A 1 1406 ? 129.747 170.981 122.469 1.00 92.64  ? 1406 GLU A CB    1 
ATOM   673   C CG    . GLU A 1 1406 ? 128.828 172.162 122.762 1.00 92.64  ? 1406 GLU A CG    1 
ATOM   674   C CD    . GLU A 1 1406 ? 129.526 173.285 123.507 1.00 92.64  ? 1406 GLU A CD    1 
ATOM   675   O OE1   . GLU A 1 1406 ? 130.718 173.128 123.844 1.00 92.64  ? 1406 GLU A OE1   1 
ATOM   676   O OE2   . GLU A 1 1406 ? 128.882 174.325 123.758 1.00 92.64  ? 1406 GLU A OE2   1 
ATOM   677   N N     . ALA A 1 1407 ? 129.515 167.403 121.901 1.00 91.12  ? 1407 ALA A N     1 
ATOM   678   C CA    . ALA A 1 1407 ? 130.364 166.223 121.819 1.00 91.12  ? 1407 ALA A CA    1 
ATOM   679   C C     . ALA A 1 1407 ? 130.456 165.699 120.396 1.00 91.12  ? 1407 ALA A C     1 
ATOM   680   O O     . ALA A 1 1407 ? 131.555 165.506 119.864 1.00 91.12  ? 1407 ALA A O     1 
ATOM   681   C CB    . ALA A 1 1407 ? 129.819 165.132 122.741 1.00 91.12  ? 1407 ALA A CB    1 
ATOM   682   N N     . LEU A 1 1408 ? 129.304 165.477 119.765 1.00 92.34  ? 1408 LEU A N     1 
ATOM   683   C CA    . LEU A 1 1408 ? 129.255 164.692 118.540 1.00 92.34  ? 1408 LEU A CA    1 
ATOM   684   C C     . LEU A 1 1408 ? 129.967 165.381 117.383 1.00 92.34  ? 1408 LEU A C     1 
ATOM   685   O O     . LEU A 1 1408 ? 130.631 164.707 116.585 1.00 92.34  ? 1408 LEU A O     1 
ATOM   686   C CB    . LEU A 1 1408 ? 127.798 164.405 118.186 1.00 92.34  ? 1408 LEU A CB    1 
ATOM   687   C CG    . LEU A 1 1408 ? 127.274 162.996 118.476 1.00 92.34  ? 1408 LEU A CG    1 
ATOM   688   C CD1   . LEU A 1 1408 ? 127.779 162.002 117.453 1.00 92.34  ? 1408 LEU A CD1   1 
ATOM   689   C CD2   . LEU A 1 1408 ? 127.665 162.561 119.879 1.00 92.34  ? 1408 LEU A CD2   1 
ATOM   690   N N     . LYS A 1 1409 ? 129.857 166.707 117.282 1.00 91.32  ? 1409 LYS A N     1 
ATOM   691   C CA    . LYS A 1 1409 ? 130.339 167.461 116.115 1.00 91.32  ? 1409 LYS A CA    1 
ATOM   692   C C     . LYS A 1 1409 ? 129.679 166.834 114.886 1.00 91.32  ? 1409 LYS A C     1 
ATOM   693   O O     . LYS A 1 1409 ? 128.444 166.764 114.831 1.00 91.32  ? 1409 LYS A O     1 
ATOM   694   C CB    . LYS A 1 1409 ? 131.863 167.500 116.092 1.00 91.32  ? 1409 LYS A CB    1 
ATOM   695   C CG    . LYS A 1 1409 ? 132.485 168.746 116.708 1.00 91.32  ? 1409 LYS A CG    1 
ATOM   696   C CD    . LYS A 1 1409 ? 132.499 168.708 118.226 1.00 91.32  ? 1409 LYS A CD    1 
ATOM   697   C CE    . LYS A 1 1409 ? 133.303 169.877 118.775 1.00 91.32  ? 1409 LYS A CE    1 
ATOM   698   N NZ    . LYS A 1 1409 ? 133.383 169.872 120.259 1.00 91.32  ? 1409 LYS A NZ    1 
ATOM   699   N N     . ASP A 1 1410 ? 130.441 166.377 113.895 1.00 91.77  ? 1410 ASP A N     1 
ATOM   700   C CA    . ASP A 1 1410 ? 129.882 165.627 112.778 1.00 91.77  ? 1410 ASP A CA    1 
ATOM   701   C C     . ASP A 1 1410 ? 130.658 164.367 112.430 1.00 91.77  ? 1410 ASP A C     1 
ATOM   702   O O     . ASP A 1 1410 ? 130.076 163.461 111.821 1.00 91.77  ? 1410 ASP A O     1 
ATOM   703   C CB    . ASP A 1 1410 ? 129.791 166.512 111.526 1.00 91.77  ? 1410 ASP A CB    1 
ATOM   704   C CG    . ASP A 1 1410 ? 128.740 166.026 110.549 1.00 91.77  ? 1410 ASP A CG    1 
ATOM   705   O OD1   . ASP A 1 1410 ? 127.541 166.070 110.894 1.00 91.77  ? 1410 ASP A OD1   1 
ATOM   706   O OD2   . ASP A 1 1410 ? 129.112 165.600 109.436 1.00 91.77  ? 1410 ASP A OD2   1 
ATOM   707   N N     . ARG A 1 1411 ? 131.941 164.273 112.789 1.00 93.82  ? 1411 ARG A N     1 
ATOM   708   C CA    . ARG A 1 1411 ? 132.702 163.058 112.521 1.00 93.82  ? 1411 ARG A CA    1 
ATOM   709   C C     . ARG A 1 1411 ? 132.189 161.888 113.354 1.00 93.82  ? 1411 ARG A C     1 
ATOM   710   O O     . ARG A 1 1411 ? 132.082 160.763 112.854 1.00 93.82  ? 1411 ARG A O     1 
ATOM   711   C CB    . ARG A 1 1411 ? 134.187 163.308 112.786 1.00 93.82  ? 1411 ARG A CB    1 
ATOM   712   C CG    . ARG A 1 1411 ? 134.982 162.068 113.155 1.00 93.82  ? 1411 ARG A CG    1 
ATOM   713   C CD    . ARG A 1 1411 ? 136.394 162.421 113.609 1.00 93.82  ? 1411 ARG A CD    1 
ATOM   714   N NE    . ARG A 1 1411 ? 136.405 163.255 114.805 1.00 93.82  ? 1411 ARG A NE    1 
ATOM   715   C CZ    . ARG A 1 1411 ? 136.572 164.571 114.802 1.00 93.82  ? 1411 ARG A CZ    1 
ATOM   716   N NH1   . ARG A 1 1411 ? 136.745 165.243 113.676 1.00 93.82  ? 1411 ARG A NH1   1 
ATOM   717   N NH2   . ARG A 1 1411 ? 136.566 165.228 115.959 1.00 93.82  ? 1411 ARG A NH2   1 
ATOM   718   N N     . HIS A 1 1412 ? 131.867 162.132 114.627 1.00 92.86  ? 1412 HIS A N     1 
ATOM   719   C CA    . HIS A 1 1412 ? 131.262 161.082 115.441 1.00 92.86  ? 1412 HIS A CA    1 
ATOM   720   C C     . HIS A 1 1412 ? 129.872 160.726 114.926 1.00 92.86  ? 1412 HIS A C     1 
ATOM   721   O O     . HIS A 1 1412 ? 129.465 159.558 114.981 1.00 92.86  ? 1412 HIS A O     1 
ATOM   722   C CB    . HIS A 1 1412 ? 131.206 161.514 116.905 1.00 92.86  ? 1412 HIS A CB    1 
ATOM   723   C CG    . HIS A 1 1412 ? 132.487 162.098 117.414 1.00 92.86  ? 1412 HIS A CG    1 
ATOM   724   N ND1   . HIS A 1 1412 ? 132.650 163.447 117.647 1.00 92.86  ? 1412 HIS A ND1   1 
ATOM   725   C CD2   . HIS A 1 1412 ? 133.664 161.515 117.740 1.00 92.86  ? 1412 HIS A CD2   1 
ATOM   726   C CE1   . HIS A 1 1412 ? 133.874 163.670 118.091 1.00 92.86  ? 1412 HIS A CE1   1 
ATOM   727   N NE2   . HIS A 1 1412 ? 134.509 162.514 118.158 1.00 92.86  ? 1412 HIS A NE2   1 
ATOM   728   N N     . TRP A 1 1413 ? 129.133 161.715 114.419 1.00 95.88  ? 1413 TRP A N     1 
ATOM   729   C CA    . TRP A 1 1413 ? 127.877 161.410 113.741 1.00 95.88  ? 1413 TRP A CA    1 
ATOM   730   C C     . TRP A 1 1413 ? 128.124 160.543 112.515 1.00 95.88  ? 1413 TRP A C     1 
ATOM   731   O O     . TRP A 1 1413 ? 127.322 159.658 112.197 1.00 95.88  ? 1413 TRP A O     1 
ATOM   732   C CB    . TRP A 1 1413 ? 127.152 162.695 113.342 1.00 95.88  ? 1413 TRP A CB    1 
ATOM   733   C CG    . TRP A 1 1413 ? 126.276 163.267 114.415 1.00 95.88  ? 1413 TRP A CG    1 
ATOM   734   C CD1   . TRP A 1 1413 ? 126.457 164.444 115.077 1.00 95.88  ? 1413 TRP A CD1   1 
ATOM   735   C CD2   . TRP A 1 1413 ? 125.092 162.676 114.966 1.00 95.88  ? 1413 TRP A CD2   1 
ATOM   736   N NE1   . TRP A 1 1413 ? 125.453 164.632 115.995 1.00 95.88  ? 1413 TRP A NE1   1 
ATOM   737   C CE2   . TRP A 1 1413 ? 124.604 163.558 115.950 1.00 95.88  ? 1413 TRP A CE2   1 
ATOM   738   C CE3   . TRP A 1 1413 ? 124.396 161.489 114.720 1.00 95.88  ? 1413 TRP A CE3   1 
ATOM   739   C CZ2   . TRP A 1 1413 ? 123.453 163.293 116.686 1.00 95.88  ? 1413 TRP A CZ2   1 
ATOM   740   C CZ3   . TRP A 1 1413 ? 123.252 161.227 115.452 1.00 95.88  ? 1413 TRP A CZ3   1 
ATOM   741   C CH2   . TRP A 1 1413 ? 122.793 162.124 116.423 1.00 95.88  ? 1413 TRP A CH2   1 
ATOM   742   N N     . LYS A 1 1414 ? 129.234 160.783 111.811 1.00 94.96  ? 1414 LYS A N     1 
ATOM   743   C CA    . LYS A 1 1414 ? 129.582 159.948 110.667 1.00 94.96  ? 1414 LYS A CA    1 
ATOM   744   C C     . LYS A 1 1414 ? 129.885 158.518 111.103 1.00 94.96  ? 1414 LYS A C     1 
ATOM   745   O O     . LYS A 1 1414 ? 129.498 157.561 110.423 1.00 94.96  ? 1414 LYS A O     1 
ATOM   746   C CB    . LYS A 1 1414 ? 130.771 160.551 109.922 1.00 94.96  ? 1414 LYS A CB    1 
ATOM   747   C CG    . LYS A 1 1414 ? 130.992 159.975 108.534 1.00 94.96  ? 1414 LYS A CG    1 
ATOM   748   C CD    . LYS A 1 1414 ? 129.845 160.334 107.603 1.00 94.96  ? 1414 LYS A CD    1 
ATOM   749   C CE    . LYS A 1 1414 ? 129.660 161.840 107.503 1.00 94.96  ? 1414 LYS A CE    1 
ATOM   750   N NZ    . LYS A 1 1414 ? 130.925 162.536 107.137 1.00 94.96  ? 1414 LYS A NZ    1 
ATOM   751   N N     . GLN A 1 1415 ? 130.582 158.356 112.231 1.00 96.00  ? 1415 GLN A N     1 
ATOM   752   C CA    . GLN A 1 1415 ? 130.829 157.015 112.757 1.00 96.00  ? 1415 GLN A CA    1 
ATOM   753   C C     . GLN A 1 1415 ? 129.523 156.324 113.128 1.00 96.00  ? 1415 GLN A C     1 
ATOM   754   O O     . GLN A 1 1415 ? 129.348 155.126 112.868 1.00 96.00  ? 1415 GLN A O     1 
ATOM   755   C CB    . GLN A 1 1415 ? 131.756 157.079 113.971 1.00 96.00  ? 1415 GLN A CB    1 
ATOM   756   C CG    . GLN A 1 1415 ? 133.033 157.873 113.761 1.00 96.00  ? 1415 GLN A CG    1 
ATOM   757   C CD    . GLN A 1 1415 ? 133.597 158.412 115.061 1.00 96.00  ? 1415 GLN A CD    1 
ATOM   758   O OE1   . GLN A 1 1415 ? 133.013 158.227 116.128 1.00 96.00  ? 1415 GLN A OE1   1 
ATOM   759   N NE2   . GLN A 1 1415 ? 134.742 159.081 114.978 1.00 96.00  ? 1415 GLN A NE2   1 
ATOM   760   N N     . LEU A 1 1416 ? 128.599 157.062 113.746 1.00 93.38  ? 1416 LEU A N     1 
ATOM   761   C CA    . LEU A 1 1416 ? 127.301 156.491 114.090 1.00 93.38  ? 1416 LEU A CA    1 
ATOM   762   C C     . LEU A 1 1416 ? 126.531 156.079 112.841 1.00 93.38  ? 1416 LEU A C     1 
ATOM   763   O O     . LEU A 1 1416 ? 125.892 155.022 112.818 1.00 93.38  ? 1416 LEU A O     1 
ATOM   764   C CB    . LEU A 1 1416 ? 126.488 157.484 114.918 1.00 93.38  ? 1416 LEU A CB    1 
ATOM   765   C CG    . LEU A 1 1416 ? 126.635 157.385 116.439 1.00 93.38  ? 1416 LEU A CG    1 
ATOM   766   C CD1   . LEU A 1 1416 ? 125.972 158.569 117.124 1.00 93.38  ? 1416 LEU A CD1   1 
ATOM   767   C CD2   . LEU A 1 1416 ? 126.059 156.076 116.950 1.00 93.38  ? 1416 LEU A CD2   1 
ATOM   768   N N     . MET A 1 1417 ? 126.575 156.907 111.795 1.00 95.38  ? 1417 MET A N     1 
ATOM   769   C CA    . MET A 1 1417 ? 125.919 156.558 110.538 1.00 95.38  ? 1417 MET A CA    1 
ATOM   770   C C     . MET A 1 1417 ? 126.541 155.311 109.921 1.00 95.38  ? 1417 MET A C     1 
ATOM   771   O O     . MET A 1 1417 ? 125.828 154.436 109.417 1.00 95.38  ? 1417 MET A O     1 
ATOM   772   C CB    . MET A 1 1417 ? 125.997 157.730 109.558 1.00 95.38  ? 1417 MET A CB    1 
ATOM   773   C CG    . MET A 1 1417 ? 125.169 158.976 109.903 1.00 95.38  ? 1417 MET A CG    1 
ATOM   774   S SD    . MET A 1 1417 ? 123.575 158.727 110.722 1.00 95.38  ? 1417 MET A SD    1 
ATOM   775   C CE    . MET A 1 1417 ? 124.013 158.706 112.462 1.00 95.38  ? 1417 MET A CE    1 
ATOM   776   N N     . LYS A 1 1418 ? 127.873 155.219 109.946 1.00 95.37  ? 1418 LYS A N     1 
ATOM   777   C CA    . LYS A 1 1418 ? 128.550 154.059 109.378 1.00 95.37  ? 1418 LYS A CA    1 
ATOM   778   C C     . LYS A 1 1418 ? 128.201 152.785 110.138 1.00 95.37  ? 1418 LYS A C     1 
ATOM   779   O O     . LYS A 1 1418 ? 127.961 151.737 109.529 1.00 95.37  ? 1418 LYS A O     1 
ATOM   780   C CB    . LYS A 1 1418 ? 130.062 154.289 109.374 1.00 95.37  ? 1418 LYS A CB    1 
ATOM   781   C CG    . LYS A 1 1418 ? 130.877 153.109 108.871 1.00 95.37  ? 1418 LYS A CG    1 
ATOM   782   C CD    . LYS A 1 1418 ? 131.669 152.464 109.998 1.00 95.37  ? 1418 LYS A CD    1 
ATOM   783   C CE    . LYS A 1 1418 ? 132.961 153.219 110.268 1.00 95.37  ? 1418 LYS A CE    1 
ATOM   784   N NZ    . LYS A 1 1418 ? 133.629 152.752 111.514 1.00 95.37  ? 1418 LYS A NZ    1 
ATOM   785   N N     . ARG A 1 1419 ? 128.164 152.857 111.470 1.00 100.12 ? 1419 ARG A N     1 
ATOM   786   C CA    . ARG A 1 1419 ? 127.880 151.662 112.258 1.00 100.12 ? 1419 ARG A CA    1 
ATOM   787   C C     . ARG A 1 1419 ? 126.409 151.265 112.179 1.00 100.12 ? 1419 ARG A C     1 
ATOM   788   O O     . ARG A 1 1419 ? 126.088 150.073 112.135 1.00 100.12 ? 1419 ARG A O     1 
ATOM   789   C CB    . ARG A 1 1419 ? 128.296 151.876 113.713 1.00 100.12 ? 1419 ARG A CB    1 
ATOM   790   C CG    . ARG A 1 1419 ? 128.245 150.611 114.554 1.00 100.12 ? 1419 ARG A CG    1 
ATOM   791   C CD    . ARG A 1 1419 ? 129.331 150.589 115.617 1.00 100.12 ? 1419 ARG A CD    1 
ATOM   792   N NE    . ARG A 1 1419 ? 129.795 151.926 115.964 1.00 100.12 ? 1419 ARG A NE    1 
ATOM   793   C CZ    . ARG A 1 1419 ? 130.867 152.178 116.703 1.00 100.12 ? 1419 ARG A CZ    1 
ATOM   794   N NH1   . ARG A 1 1419 ? 131.608 151.201 117.201 1.00 100.12 ? 1419 ARG A NH1   1 
ATOM   795   N NH2   . ARG A 1 1419 ? 131.201 153.441 116.954 1.00 100.12 ? 1419 ARG A NH2   1 
ATOM   796   N N     . LEU A 1 1420 ? 125.504 152.244 112.157 1.00 94.11  ? 1420 LEU A N     1 
ATOM   797   C CA    . LEU A 1 1420 ? 124.074 151.963 112.128 1.00 94.11  ? 1420 LEU A CA    1 
ATOM   798   C C     . LEU A 1 1420 ? 123.542 151.720 110.722 1.00 94.11  ? 1420 LEU A C     1 
ATOM   799   O O     . LEU A 1 1420 ? 122.393 151.285 110.583 1.00 94.11  ? 1420 LEU A O     1 
ATOM   800   C CB    . LEU A 1 1420 ? 123.304 153.115 112.781 1.00 94.11  ? 1420 LEU A CB    1 
ATOM   801   C CG    . LEU A 1 1420 ? 123.502 153.269 114.291 1.00 94.11  ? 1420 LEU A CG    1 
ATOM   802   C CD1   . LEU A 1 1420 ? 122.536 154.294 114.863 1.00 94.11  ? 1420 LEU A CD1   1 
ATOM   803   C CD2   . LEU A 1 1420 ? 123.345 151.930 114.995 1.00 94.11  ? 1420 LEU A CD2   1 
ATOM   804   N N     . HIS A 1 1421 ? 124.345 151.988 109.690 1.00 95.90  ? 1421 HIS A N     1 
ATOM   805   C CA    . HIS A 1 1421 ? 123.967 151.740 108.296 1.00 95.90  ? 1421 HIS A CA    1 
ATOM   806   C C     . HIS A 1 1421 ? 122.670 152.456 107.925 1.00 95.90  ? 1421 HIS A C     1 
ATOM   807   O O     . HIS A 1 1421 ? 121.779 151.883 107.293 1.00 95.90  ? 1421 HIS A O     1 
ATOM   808   C CB    . HIS A 1 1421 ? 123.863 150.239 108.013 1.00 95.90  ? 1421 HIS A CB    1 
ATOM   809   C CG    . HIS A 1 1421 ? 124.914 149.422 108.699 1.00 95.90  ? 1421 HIS A CG    1 
ATOM   810   N ND1   . HIS A 1 1421 ? 126.262 149.626 108.498 1.00 95.90  ? 1421 HIS A ND1   1 
ATOM   811   C CD2   . HIS A 1 1421 ? 124.815 148.402 109.583 1.00 95.90  ? 1421 HIS A CD2   1 
ATOM   812   C CE1   . HIS A 1 1421 ? 126.949 148.766 109.229 1.00 95.90  ? 1421 HIS A CE1   1 
ATOM   813   N NE2   . HIS A 1 1421 ? 126.095 148.011 109.897 1.00 95.90  ? 1421 HIS A NE2   1 
ATOM   814   N N     . VAL A 1 1422 ? 122.560 153.720 108.324 1.00 95.03  ? 1422 VAL A N     1 
ATOM   815   C CA    . VAL A 1 1422 ? 121.433 154.576 107.966 1.00 95.03  ? 1422 VAL A CA    1 
ATOM   816   C C     . VAL A 1 1422 ? 121.989 155.803 107.254 1.00 95.03  ? 1422 VAL A C     1 
ATOM   817   O O     . VAL A 1 1422 ? 123.065 156.301 107.610 1.00 95.03  ? 1422 VAL A O     1 
ATOM   818   C CB    . VAL A 1 1422 ? 120.588 154.964 109.191 1.00 95.03  ? 1422 VAL A CB    1 
ATOM   819   C CG1   . VAL A 1 1422 ? 120.201 153.723 109.982 1.00 95.03  ? 1422 VAL A CG1   1 
ATOM   820   C CG2   . VAL A 1 1422 ? 121.337 155.939 110.087 1.00 95.03  ? 1422 VAL A CG2   1 
ATOM   821   N N     . ASN A 1 1423 ? 121.277 156.266 106.226 1.00 96.01  ? 1423 ASN A N     1 
ATOM   822   C CA    . ASN A 1 1423 ? 121.736 157.388 105.407 1.00 96.01  ? 1423 ASN A CA    1 
ATOM   823   C C     . ASN A 1 1423 ? 120.816 158.583 105.640 1.00 96.01  ? 1423 ASN A C     1 
ATOM   824   O O     . ASN A 1 1423 ? 119.818 158.794 104.947 1.00 96.01  ? 1423 ASN A O     1 
ATOM   825   C CB    . ASN A 1 1423 ? 121.787 156.991 103.938 1.00 96.01  ? 1423 ASN A CB    1 
ATOM   826   C CG    . ASN A 1 1423 ? 122.711 155.815 103.684 1.00 96.01  ? 1423 ASN A CG    1 
ATOM   827   O OD1   . ASN A 1 1423 ? 123.416 155.360 104.583 1.00 96.01  ? 1423 ASN A OD1   1 
ATOM   828   N ND2   . ASN A 1 1423 ? 122.708 155.316 102.453 1.00 96.01  ? 1423 ASN A ND2   1 
ATOM   829   N N     . TRP A 1 1424 ? 121.171 159.381 106.642 1.00 95.13  ? 1424 TRP A N     1 
ATOM   830   C CA    . TRP A 1 1424 ? 120.447 160.604 106.943 1.00 95.13  ? 1424 TRP A CA    1 
ATOM   831   C C     . TRP A 1 1424 ? 121.146 161.807 106.314 1.00 95.13  ? 1424 TRP A C     1 
ATOM   832   O O     . TRP A 1 1424 ? 122.192 161.691 105.671 1.00 95.13  ? 1424 TRP A O     1 
ATOM   833   C CB    . TRP A 1 1424 ? 120.323 160.799 108.454 1.00 95.13  ? 1424 TRP A CB    1 
ATOM   834   C CG    . TRP A 1 1424 ? 119.598 159.693 109.154 1.00 95.13  ? 1424 TRP A CG    1 
ATOM   835   C CD1   . TRP A 1 1424 ? 118.708 158.818 108.603 1.00 95.13  ? 1424 TRP A CD1   1 
ATOM   836   C CD2   . TRP A 1 1424 ? 119.701 159.345 110.538 1.00 95.13  ? 1424 TRP A CD2   1 
ATOM   837   N NE1   . TRP A 1 1424 ? 118.251 157.945 109.560 1.00 95.13  ? 1424 TRP A NE1   1 
ATOM   838   C CE2   . TRP A 1 1424 ? 118.845 158.247 110.757 1.00 95.13  ? 1424 TRP A CE2   1 
ATOM   839   C CE3   . TRP A 1 1424 ? 120.433 159.854 111.615 1.00 95.13  ? 1424 TRP A CE3   1 
ATOM   840   C CZ2   . TRP A 1 1424 ? 118.704 157.650 112.008 1.00 95.13  ? 1424 TRP A CZ2   1 
ATOM   841   C CZ3   . TRP A 1 1424 ? 120.291 159.259 112.855 1.00 95.13  ? 1424 TRP A CZ3   1 
ATOM   842   C CH2   . TRP A 1 1424 ? 119.434 158.169 113.041 1.00 95.13  ? 1424 TRP A CH2   1 
ATOM   843   N N     . VAL A 1 1425 ? 120.551 162.979 106.511 1.00 85.42  ? 1425 VAL A N     1 
ATOM   844   C CA    . VAL A 1 1425 ? 121.128 164.250 106.090 1.00 85.42  ? 1425 VAL A CA    1 
ATOM   845   C C     . VAL A 1 1425 ? 121.293 165.117 107.329 1.00 85.42  ? 1425 VAL A C     1 
ATOM   846   O O     . VAL A 1 1425 ? 120.347 165.280 108.106 1.00 85.42  ? 1425 VAL A O     1 
ATOM   847   C CB    . VAL A 1 1425 ? 120.255 164.957 105.037 1.00 85.42  ? 1425 VAL A CB    1 
ATOM   848   C CG1   . VAL A 1 1425 ? 120.937 166.226 104.551 1.00 85.42  ? 1425 VAL A CG1   1 
ATOM   849   C CG2   . VAL A 1 1425 ? 119.964 164.022 103.874 1.00 85.42  ? 1425 VAL A CG2   1 
ATOM   850   N N     . VAL A 1 1426 ? 122.497 165.664 107.513 1.00 80.93  ? 1426 VAL A N     1 
ATOM   851   C CA    . VAL A 1 1426 ? 122.785 166.446 108.715 1.00 80.93  ? 1426 VAL A CA    1 
ATOM   852   C C     . VAL A 1 1426 ? 121.895 167.684 108.770 1.00 80.93  ? 1426 VAL A C     1 
ATOM   853   O O     . VAL A 1 1426 ? 121.320 168.013 109.814 1.00 80.93  ? 1426 VAL A O     1 
ATOM   854   C CB    . VAL A 1 1426 ? 124.277 166.819 108.766 1.00 80.93  ? 1426 VAL A CB    1 
ATOM   855   C CG1   . VAL A 1 1426 ? 124.567 167.695 109.976 1.00 80.93  ? 1426 VAL A CG1   1 
ATOM   856   C CG2   . VAL A 1 1426 ? 125.135 165.563 108.785 1.00 80.93  ? 1426 VAL A CG2   1 
ATOM   857   N N     . SER A 1 1427 ? 121.772 168.390 107.643 1.00 83.97  ? 1427 SER A N     1 
ATOM   858   C CA    . SER A 1 1427 ? 120.910 169.568 107.598 1.00 83.97  ? 1427 SER A CA    1 
ATOM   859   C C     . SER A 1 1427 ? 119.446 169.191 107.785 1.00 83.97  ? 1427 SER A C     1 
ATOM   860   O O     . SER A 1 1427 ? 118.699 169.898 108.473 1.00 83.97  ? 1427 SER A O     1 
ATOM   861   C CB    . SER A 1 1427 ? 121.107 170.312 106.279 1.00 83.97  ? 1427 SER A CB    1 
ATOM   862   O OG    . SER A 1 1427 ? 120.684 169.521 105.182 1.00 83.97  ? 1427 SER A OG    1 
ATOM   863   N N     . GLU A 1 1428 ? 119.020 168.083 107.187 1.00 88.16  ? 1428 GLU A N     1 
ATOM   864   C CA    . GLU A 1 1428 ? 117.640 167.625 107.259 1.00 88.16  ? 1428 GLU A CA    1 
ATOM   865   C C     . GLU A 1 1428 ? 117.392 166.682 108.430 1.00 88.16  ? 1428 GLU A C     1 
ATOM   866   O O     . GLU A 1 1428 ? 116.304 166.102 108.520 1.00 88.16  ? 1428 GLU A O     1 
ATOM   867   C CB    . GLU A 1 1428 ? 117.243 166.937 105.951 1.00 88.16  ? 1428 GLU A CB    1 
ATOM   868   C CG    . GLU A 1 1428 ? 117.572 167.741 104.706 1.00 88.16  ? 1428 GLU A CG    1 
ATOM   869   C CD    . GLU A 1 1428 ? 117.456 166.921 103.438 1.00 88.16  ? 1428 GLU A CD    1 
ATOM   870   O OE1   . GLU A 1 1428 ? 117.110 165.724 103.532 1.00 88.16  ? 1428 GLU A OE1   1 
ATOM   871   O OE2   . GLU A 1 1428 ? 117.718 167.470 102.348 1.00 88.16  ? 1428 GLU A OE2   1 
ATOM   872   N N     . LEU A 1 1429 ? 118.373 166.506 109.313 1.00 91.51  ? 1429 LEU A N     1 
ATOM   873   C CA    . LEU A 1 1429 ? 118.213 165.589 110.432 1.00 91.51  ? 1429 LEU A CA    1 
ATOM   874   C C     . LEU A 1 1429 ? 117.084 166.047 111.346 1.00 91.51  ? 1429 LEU A C     1 
ATOM   875   O O     . LEU A 1 1429 ? 116.986 167.224 111.705 1.00 91.51  ? 1429 LEU A O     1 
ATOM   876   C CB    . LEU A 1 1429 ? 119.521 165.479 111.219 1.00 91.51  ? 1429 LEU A CB    1 
ATOM   877   C CG    . LEU A 1 1429 ? 119.499 164.574 112.453 1.00 91.51  ? 1429 LEU A CG    1 
ATOM   878   C CD1   . LEU A 1 1429 ? 119.070 163.163 112.083 1.00 91.51  ? 1429 LEU A CD1   1 
ATOM   879   C CD2   . LEU A 1 1429 ? 120.858 164.567 113.134 1.00 91.51  ? 1429 LEU A CD2   1 
ATOM   880   N N     . THR A 1 1430 ? 116.227 165.100 111.718 1.00 91.97  ? 1430 THR A N     1 
ATOM   881   C CA    . THR A 1 1430 ? 115.098 165.359 112.597 1.00 91.97  ? 1430 THR A CA    1 
ATOM   882   C C     . THR A 1 1430 ? 115.039 164.262 113.647 1.00 91.97  ? 1430 THR A C     1 
ATOM   883   O O     . THR A 1 1430 ? 115.627 163.189 113.487 1.00 91.97  ? 1430 THR A O     1 
ATOM   884   C CB    . THR A 1 1430 ? 113.772 165.429 111.825 1.00 91.97  ? 1430 THR A CB    1 
ATOM   885   O OG1   . THR A 1 1430 ? 112.716 165.804 112.719 1.00 91.97  ? 1430 THR A OG1   1 
ATOM   886   C CG2   . THR A 1 1430 ? 113.445 164.082 111.201 1.00 91.97  ? 1430 THR A CG2   1 
ATOM   887   N N     . LEU A 1 1431 ? 114.330 164.554 114.741 1.00 91.67  ? 1431 LEU A N     1 
ATOM   888   C CA    . LEU A 1 1431 ? 114.222 163.583 115.825 1.00 91.67  ? 1431 LEU A CA    1 
ATOM   889   C C     . LEU A 1 1431 ? 113.492 162.327 115.373 1.00 91.67  ? 1431 LEU A C     1 
ATOM   890   O O     . LEU A 1 1431 ? 113.707 161.250 115.937 1.00 91.67  ? 1431 LEU A O     1 
ATOM   891   C CB    . LEU A 1 1431 ? 113.520 164.210 117.033 1.00 91.67  ? 1431 LEU A CB    1 
ATOM   892   C CG    . LEU A 1 1431 ? 113.220 163.257 118.197 1.00 91.67  ? 1431 LEU A CG    1 
ATOM   893   C CD1   . LEU A 1 1431 ? 114.500 162.844 118.900 1.00 91.67  ? 1431 LEU A CD1   1 
ATOM   894   C CD2   . LEU A 1 1431 ? 112.272 163.876 119.191 1.00 91.67  ? 1431 LEU A CD2   1 
ATOM   895   N N     . GLY A 1 1432 ? 112.639 162.440 114.353 1.00 86.17  ? 1432 GLY A N     1 
ATOM   896   C CA    . GLY A 1 1432 ? 111.927 161.270 113.867 1.00 86.17  ? 1432 GLY A CA    1 
ATOM   897   C C     . GLY A 1 1432 ? 112.855 160.201 113.324 1.00 86.17  ? 1432 GLY A C     1 
ATOM   898   O O     . GLY A 1 1432 ? 112.669 159.011 113.591 1.00 86.17  ? 1432 GLY A O     1 
ATOM   899   N N     . GLN A 1 1433 ? 113.870 160.612 112.560 1.00 89.33  ? 1433 GLN A N     1 
ATOM   900   C CA    . GLN A 1 1433 ? 114.826 159.652 112.016 1.00 89.33  ? 1433 GLN A CA    1 
ATOM   901   C C     . GLN A 1 1433 ? 115.603 158.950 113.124 1.00 89.33  ? 1433 GLN A C     1 
ATOM   902   O O     . GLN A 1 1433 ? 115.798 157.730 113.077 1.00 89.33  ? 1433 GLN A O     1 
ATOM   903   C CB    . GLN A 1 1433 ? 115.782 160.358 111.055 1.00 89.33  ? 1433 GLN A CB    1 
ATOM   904   C CG    . GLN A 1 1433 ? 115.108 160.953 109.831 1.00 89.33  ? 1433 GLN A CG    1 
ATOM   905   C CD    . GLN A 1 1433 ? 114.894 159.931 108.732 1.00 89.33  ? 1433 GLN A CD    1 
ATOM   906   O OE1   . GLN A 1 1433 ? 115.335 158.787 108.837 1.00 89.33  ? 1433 GLN A OE1   1 
ATOM   907   N NE2   . GLN A 1 1433 ? 114.214 160.342 107.668 1.00 89.33  ? 1433 GLN A NE2   1 
ATOM   908   N N     . ILE A 1 1434 ? 116.051 159.705 114.129 1.00 92.16  ? 1434 ILE A N     1 
ATOM   909   C CA    . ILE A 1 1434 ? 116.820 159.111 115.219 1.00 92.16  ? 1434 ILE A CA    1 
ATOM   910   C C     . ILE A 1 1434 ? 115.939 158.196 116.063 1.00 92.16  ? 1434 ILE A C     1 
ATOM   911   O O     . ILE A 1 1434 ? 116.389 157.149 116.543 1.00 92.16  ? 1434 ILE A O     1 
ATOM   912   C CB    . ILE A 1 1434 ? 117.482 160.211 116.066 1.00 92.16  ? 1434 ILE A CB    1 
ATOM   913   C CG1   . ILE A 1 1434 ? 118.211 161.207 115.159 1.00 92.16  ? 1434 ILE A CG1   1 
ATOM   914   C CG2   . ILE A 1 1434 ? 118.437 159.603 117.081 1.00 92.16  ? 1434 ILE A CG2   1 
ATOM   915   C CD1   . ILE A 1 1434 ? 119.207 162.085 115.880 1.00 92.16  ? 1434 ILE A CD1   1 
ATOM   916   N N     . TRP A 1 1435 ? 114.676 158.577 116.263 1.00 94.58  ? 1435 TRP A N     1 
ATOM   917   C CA    . TRP A 1 1435 ? 113.759 157.765 117.052 1.00 94.58  ? 1435 TRP A CA    1 
ATOM   918   C C     . TRP A 1 1435 ? 113.343 156.496 116.321 1.00 94.58  ? 1435 TRP A C     1 
ATOM   919   O O     . TRP A 1 1435 ? 113.042 155.488 116.968 1.00 94.58  ? 1435 TRP A O     1 
ATOM   920   C CB    . TRP A 1 1435 ? 112.525 158.585 117.430 1.00 94.58  ? 1435 TRP A CB    1 
ATOM   921   C CG    . TRP A 1 1435 ? 112.665 159.308 118.735 1.00 94.58  ? 1435 TRP A CG    1 
ATOM   922   C CD1   . TRP A 1 1435 ? 113.794 159.416 119.494 1.00 94.58  ? 1435 TRP A CD1   1 
ATOM   923   C CD2   . TRP A 1 1435 ? 111.642 160.030 119.431 1.00 94.58  ? 1435 TRP A CD2   1 
ATOM   924   N NE1   . TRP A 1 1435 ? 113.535 160.157 120.623 1.00 94.58  ? 1435 TRP A NE1   1 
ATOM   925   C CE2   . TRP A 1 1435 ? 112.222 160.546 120.607 1.00 94.58  ? 1435 TRP A CE2   1 
ATOM   926   C CE3   . TRP A 1 1435 ? 110.292 160.289 119.174 1.00 94.58  ? 1435 TRP A CE3   1 
ATOM   927   C CZ2   . TRP A 1 1435 ? 111.498 161.305 121.525 1.00 94.58  ? 1435 TRP A CZ2   1 
ATOM   928   C CZ3   . TRP A 1 1435 ? 109.576 161.043 120.086 1.00 94.58  ? 1435 TRP A CZ3   1 
ATOM   929   C CH2   . TRP A 1 1435 ? 110.180 161.542 121.247 1.00 94.58  ? 1435 TRP A CH2   1 
ATOM   930   N N     . ASP A 1 1436 ? 113.310 156.527 114.986 1.00 90.78  ? 1436 ASP A N     1 
ATOM   931   C CA    . ASP A 1 1436 ? 113.028 155.310 114.232 1.00 90.78  ? 1436 ASP A CA    1 
ATOM   932   C C     . ASP A 1 1436 ? 114.103 154.257 114.475 1.00 90.78  ? 1436 ASP A C     1 
ATOM   933   O O     . ASP A 1 1436 ? 113.795 153.073 114.652 1.00 90.78  ? 1436 ASP A O     1 
ATOM   934   C CB    . ASP A 1 1436 ? 112.910 155.628 112.742 1.00 90.78  ? 1436 ASP A CB    1 
ATOM   935   C CG    . ASP A 1 1436 ? 111.597 156.300 112.393 1.00 90.78  ? 1436 ASP A CG    1 
ATOM   936   O OD1   . ASP A 1 1436 ? 110.750 156.454 113.298 1.00 90.78  ? 1436 ASP A OD1   1 
ATOM   937   O OD2   . ASP A 1 1436 ? 111.412 156.672 111.216 1.00 90.78  ? 1436 ASP A OD2   1 
ATOM   938   N N     . VAL A 1 1437 ? 115.370 154.671 114.487 1.00 89.26  ? 1437 VAL A N     1 
ATOM   939   C CA    . VAL A 1 1437 ? 116.451 153.764 114.848 1.00 89.26  ? 1437 VAL A CA    1 
ATOM   940   C C     . VAL A 1 1437 ? 116.407 153.515 116.349 1.00 89.26  ? 1437 VAL A C     1 
ATOM   941   O O     . VAL A 1 1437 ? 116.314 154.456 117.148 1.00 89.26  ? 1437 VAL A O     1 
ATOM   942   C CB    . VAL A 1 1437 ? 117.807 154.340 114.414 1.00 89.26  ? 1437 VAL A CB    1 
ATOM   943   C CG1   . VAL A 1 1437 ? 118.944 153.586 115.081 1.00 89.26  ? 1437 VAL A CG1   1 
ATOM   944   C CG2   . VAL A 1 1437 ? 117.941 154.287 112.901 1.00 89.26  ? 1437 VAL A CG2   1 
ATOM   945   N N     . ASP A 1 1438 ? 116.466 152.246 116.741 1.00 91.25  ? 1438 ASP A N     1 
ATOM   946   C CA    . ASP A 1 1438 ? 116.321 151.870 118.145 1.00 91.25  ? 1438 ASP A CA    1 
ATOM   947   C C     . ASP A 1 1438 ? 117.554 152.322 118.917 1.00 91.25  ? 1438 ASP A C     1 
ATOM   948   O O     . ASP A 1 1438 ? 118.600 151.672 118.884 1.00 91.25  ? 1438 ASP A O     1 
ATOM   949   C CB    . ASP A 1 1438 ? 116.112 150.366 118.271 1.00 91.25  ? 1438 ASP A CB    1 
ATOM   950   C CG    . ASP A 1 1438 ? 115.371 149.986 119.538 1.00 91.25  ? 1438 ASP A CG    1 
ATOM   951   O OD1   . ASP A 1 1438 ? 115.838 150.355 120.636 1.00 91.25  ? 1438 ASP A OD1   1 
ATOM   952   O OD2   . ASP A 1 1438 ? 114.321 149.317 119.435 1.00 91.25  ? 1438 ASP A OD2   1 
ATOM   953   N N     . LEU A 1 1439 ? 117.431 153.454 119.616 1.00 90.85  ? 1439 LEU A N     1 
ATOM   954   C CA    . LEU A 1 1439 ? 118.523 153.924 120.462 1.00 90.85  ? 1439 LEU A CA    1 
ATOM   955   C C     . LEU A 1 1439 ? 118.723 153.006 121.661 1.00 90.85  ? 1439 LEU A C     1 
ATOM   956   O O     . LEU A 1 1439 ? 119.857 152.800 122.110 1.00 90.85  ? 1439 LEU A O     1 
ATOM   957   C CB    . LEU A 1 1439 ? 118.252 155.357 120.919 1.00 90.85  ? 1439 LEU A CB    1 
ATOM   958   C CG    . LEU A 1 1439 ? 118.142 156.419 119.823 1.00 90.85  ? 1439 LEU A CG    1 
ATOM   959   C CD1   . LEU A 1 1439 ? 118.089 157.814 120.429 1.00 90.85  ? 1439 LEU A CD1   1 
ATOM   960   C CD2   . LEU A 1 1439 ? 119.298 156.302 118.840 1.00 90.85  ? 1439 LEU A CD2   1 
ATOM   961   N N     . GLN A 1 1440 ? 117.630 152.456 122.198 1.00 92.36  ? 1440 GLN A N     1 
ATOM   962   C CA    . GLN A 1 1440 ? 117.737 151.532 123.322 1.00 92.36  ? 1440 GLN A CA    1 
ATOM   963   C C     . GLN A 1 1440 ? 118.479 150.261 122.926 1.00 92.36  ? 1440 GLN A C     1 
ATOM   964   O O     . GLN A 1 1440 ? 119.321 149.763 123.683 1.00 92.36  ? 1440 GLN A O     1 
ATOM   965   C CB    . GLN A 1 1440 ? 116.343 151.204 123.857 1.00 92.36  ? 1440 GLN A CB    1 
ATOM   966   C CG    . GLN A 1 1440 ? 116.300 150.053 124.848 1.00 92.36  ? 1440 GLN A CG    1 
ATOM   967   C CD    . GLN A 1 1440 ? 114.895 149.759 125.335 1.00 92.36  ? 1440 GLN A CD    1 
ATOM   968   O OE1   . GLN A 1 1440 ? 113.952 150.486 125.022 1.00 92.36  ? 1440 GLN A OE1   1 
ATOM   969   N NE2   . GLN A 1 1440 ? 114.747 148.688 126.105 1.00 92.36  ? 1440 GLN A NE2   1 
ATOM   970   N N     . LYS A 1 1441 ? 118.177 149.719 121.745 1.00 91.00  ? 1441 LYS A N     1 
ATOM   971   C CA    . LYS A 1 1441 ? 118.894 148.542 121.265 1.00 91.00  ? 1441 LYS A CA    1 
ATOM   972   C C     . LYS A 1 1441 ? 120.356 148.866 120.979 1.00 91.00  ? 1441 LYS A C     1 
ATOM   973   O O     . LYS A 1 1441 ? 121.247 148.057 121.266 1.00 91.00  ? 1441 LYS A O     1 
ATOM   974   C CB    . LYS A 1 1441 ? 118.208 147.983 120.018 1.00 91.00  ? 1441 LYS A CB    1 
ATOM   975   C CG    . LYS A 1 1441 ? 119.111 147.153 119.118 1.00 91.00  ? 1441 LYS A CG    1 
ATOM   976   C CD    . LYS A 1 1441 ? 118.483 146.933 117.751 1.00 91.00  ? 1441 LYS A CD    1 
ATOM   977   C CE    . LYS A 1 1441 ? 117.101 146.306 117.868 1.00 91.00  ? 1441 LYS A CE    1 
ATOM   978   N NZ    . LYS A 1 1441 ? 117.134 145.023 118.621 1.00 91.00  ? 1441 LYS A NZ    1 
ATOM   979   N N     . ASN A 1 1442 ? 120.623 150.052 120.427 1.00 90.70  ? 1442 ASN A N     1 
ATOM   980   C CA    . ASN A 1 1442 ? 121.971 150.482 120.079 1.00 90.70  ? 1442 ASN A CA    1 
ATOM   981   C C     . ASN A 1 1442 ? 122.627 151.303 121.182 1.00 90.70  ? 1442 ASN A C     1 
ATOM   982   O O     . ASN A 1 1442 ? 123.419 152.209 120.889 1.00 90.70  ? 1442 ASN A O     1 
ATOM   983   C CB    . ASN A 1 1442 ? 121.946 151.272 118.770 1.00 90.70  ? 1442 ASN A CB    1 
ATOM   984   C CG    . ASN A 1 1442 ? 121.462 150.441 117.599 1.00 90.70  ? 1442 ASN A CG    1 
ATOM   985   O OD1   . ASN A 1 1442 ? 121.881 149.297 117.418 1.00 90.70  ? 1442 ASN A OD1   1 
ATOM   986   N ND2   . ASN A 1 1442 ? 120.574 151.011 116.794 1.00 90.70  ? 1442 ASN A ND2   1 
ATOM   987   N N     . GLU A 1 1443 ? 122.309 151.012 122.447 1.00 91.59  ? 1443 GLU A N     1 
ATOM   988   C CA    . GLU A 1 1443 ? 122.852 151.795 123.554 1.00 91.59  ? 1443 GLU A CA    1 
ATOM   989   C C     . GLU A 1 1443 ? 124.370 151.686 123.628 1.00 91.59  ? 1443 GLU A C     1 
ATOM   990   O O     . GLU A 1 1443 ? 125.054 152.672 123.926 1.00 91.59  ? 1443 GLU A O     1 
ATOM   991   C CB    . GLU A 1 1443 ? 122.221 151.348 124.872 1.00 91.59  ? 1443 GLU A CB    1 
ATOM   992   C CG    . GLU A 1 1443 ? 120.941 152.084 125.232 1.00 91.59  ? 1443 GLU A CG    1 
ATOM   993   C CD    . GLU A 1 1443 ? 120.584 151.946 126.699 1.00 91.59  ? 1443 GLU A CD    1 
ATOM   994   O OE1   . GLU A 1 1443 ? 121.171 151.075 127.375 1.00 91.59  ? 1443 GLU A OE1   1 
ATOM   995   O OE2   . GLU A 1 1443 ? 119.718 152.708 127.177 1.00 91.59  ? 1443 GLU A OE2   1 
ATOM   996   N N     . ALA A 1 1444 ? 124.917 150.494 123.375 1.00 85.64  ? 1444 ALA A N     1 
ATOM   997   C CA    . ALA A 1 1444 ? 126.363 150.311 123.461 1.00 85.64  ? 1444 ALA A CA    1 
ATOM   998   C C     . ALA A 1 1444 ? 127.090 151.147 122.415 1.00 85.64  ? 1444 ALA A C     1 
ATOM   999   O O     . ALA A 1 1444 ? 128.082 151.822 122.721 1.00 85.64  ? 1444 ALA A O     1 
ATOM   1000  C CB    . ALA A 1 1444 ? 126.712 148.830 123.307 1.00 85.64  ? 1444 ALA A CB    1 
ATOM   1001  N N     . ILE A 1 1445 ? 126.607 151.115 121.171 1.00 91.23  ? 1445 ILE A N     1 
ATOM   1002  C CA    . ILE A 1 1445 ? 127.242 151.878 120.097 1.00 91.23  ? 1445 ILE A CA    1 
ATOM   1003  C C     . ILE A 1 1445 ? 127.165 153.370 120.392 1.00 91.23  ? 1445 ILE A C     1 
ATOM   1004  O O     . ILE A 1 1445 ? 128.151 154.108 120.248 1.00 91.23  ? 1445 ILE A O     1 
ATOM   1005  C CB    . ILE A 1 1445 ? 126.588 151.536 118.747 1.00 91.23  ? 1445 ILE A CB    1 
ATOM   1006  C CG1   . ILE A 1 1445 ? 126.906 150.092 118.349 1.00 91.23  ? 1445 ILE A CG1   1 
ATOM   1007  C CG2   . ILE A 1 1445 ? 127.028 152.516 117.671 1.00 91.23  ? 1445 ILE A CG2   1 
ATOM   1008  C CD1   . ILE A 1 1445 ? 126.010 149.549 117.259 1.00 91.23  ? 1445 ILE A CD1   1 
ATOM   1009  N N     . VAL A 1 1446 ? 125.987 153.834 120.815 1.00 89.13  ? 1446 VAL A N     1 
ATOM   1010  C CA    . VAL A 1 1446 ? 125.802 155.251 121.109 1.00 89.13  ? 1446 VAL A CA    1 
ATOM   1011  C C     . VAL A 1 1446 ? 126.725 155.680 122.242 1.00 89.13  ? 1446 VAL A C     1 
ATOM   1012  O O     . VAL A 1 1446 ? 127.372 156.730 122.172 1.00 89.13  ? 1446 VAL A O     1 
ATOM   1013  C CB    . VAL A 1 1446 ? 124.326 155.543 121.436 1.00 89.13  ? 1446 VAL A CB    1 
ATOM   1014  C CG1   . VAL A 1 1446 ? 124.175 156.942 122.007 1.00 89.13  ? 1446 VAL A CG1   1 
ATOM   1015  C CG2   . VAL A 1 1446 ? 123.464 155.376 120.195 1.00 89.13  ? 1446 VAL A CG2   1 
ATOM   1016  N N     . LYS A 1 1447 ? 126.805 154.868 123.300 1.00 90.26  ? 1447 LYS A N     1 
ATOM   1017  C CA    . LYS A 1 1447 ? 127.653 155.210 124.437 1.00 90.26  ? 1447 LYS A CA    1 
ATOM   1018  C C     . LYS A 1 1447 ? 129.126 155.236 124.049 1.00 90.26  ? 1447 LYS A C     1 
ATOM   1019  O O     . LYS A 1 1447 ? 129.876 156.108 124.503 1.00 90.26  ? 1447 LYS A O     1 
ATOM   1020  C CB    . LYS A 1 1447 ? 127.416 154.229 125.584 1.00 90.26  ? 1447 LYS A CB    1 
ATOM   1021  C CG    . LYS A 1 1447 ? 126.188 154.547 126.422 1.00 90.26  ? 1447 LYS A CG    1 
ATOM   1022  C CD    . LYS A 1 1447 ? 125.906 153.450 127.437 1.00 90.26  ? 1447 LYS A CD    1 
ATOM   1023  C CE    . LYS A 1 1447 ? 124.652 153.752 128.240 1.00 90.26  ? 1447 LYS A CE    1 
ATOM   1024  N NZ    . LYS A 1 1447 ? 124.345 152.676 129.222 1.00 90.26  ? 1447 LYS A NZ    1 
ATOM   1025  N N     . ASP A 1 1448 ? 129.564 154.285 123.219 1.00 92.51  ? 1448 ASP A N     1 
ATOM   1026  C CA    . ASP A 1 1448 ? 130.950 154.297 122.762 1.00 92.51  ? 1448 ASP A CA    1 
ATOM   1027  C C     . ASP A 1 1448 ? 131.252 155.553 121.954 1.00 92.51  ? 1448 ASP A C     1 
ATOM   1028  O O     . ASP A 1 1448 ? 132.302 156.184 122.139 1.00 92.51  ? 1448 ASP A O     1 
ATOM   1029  C CB    . ASP A 1 1448 ? 131.243 153.046 121.934 1.00 92.51  ? 1448 ASP A CB    1 
ATOM   1030  C CG    . ASP A 1 1448 ? 132.662 153.021 121.400 1.00 92.51  ? 1448 ASP A CG    1 
ATOM   1031  O OD1   . ASP A 1 1448 ? 133.600 152.816 122.200 1.00 92.51  ? 1448 ASP A OD1   1 
ATOM   1032  O OD2   . ASP A 1 1448 ? 132.841 153.207 120.178 1.00 92.51  ? 1448 ASP A OD2   1 
ATOM   1033  N N     . VAL A 1 1449 ? 130.336 155.937 121.060 1.00 89.91  ? 1449 VAL A N     1 
ATOM   1034  C CA    . VAL A 1 1449 ? 130.539 157.150 120.271 1.00 89.91  ? 1449 VAL A CA    1 
ATOM   1035  C C     . VAL A 1 1449 ? 130.582 158.375 121.178 1.00 89.91  ? 1449 VAL A C     1 
ATOM   1036  O O     . VAL A 1 1449 ? 131.409 159.276 120.990 1.00 89.91  ? 1449 VAL A O     1 
ATOM   1037  C CB    . VAL A 1 1449 ? 129.446 157.272 119.193 1.00 89.91  ? 1449 VAL A CB    1 
ATOM   1038  C CG1   . VAL A 1 1449 ? 129.508 158.634 118.522 1.00 89.91  ? 1449 VAL A CG1   1 
ATOM   1039  C CG2   . VAL A 1 1449 ? 129.599 156.162 118.164 1.00 89.91  ? 1449 VAL A CG2   1 
ATOM   1040  N N     . LEU A 1 1450 ? 129.699 158.423 122.179 1.00 88.79  ? 1450 LEU A N     1 
ATOM   1041  C CA    . LEU A 1 1450 ? 129.684 159.546 123.114 1.00 88.79  ? 1450 LEU A CA    1 
ATOM   1042  C C     . LEU A 1 1450 ? 130.985 159.635 123.902 1.00 88.79  ? 1450 LEU A C     1 
ATOM   1043  O O     . LEU A 1 1450 ? 131.507 160.731 124.124 1.00 88.79  ? 1450 LEU A O     1 
ATOM   1044  C CB    . LEU A 1 1450 ? 128.496 159.430 124.069 1.00 88.79  ? 1450 LEU A CB    1 
ATOM   1045  C CG    . LEU A 1 1450 ? 127.086 159.459 123.481 1.00 88.79  ? 1450 LEU A CG    1 
ATOM   1046  C CD1   . LEU A 1 1450 ? 126.069 159.113 124.548 1.00 88.79  ? 1450 LEU A CD1   1 
ATOM   1047  C CD2   . LEU A 1 1450 ? 126.787 160.822 122.890 1.00 88.79  ? 1450 LEU A CD2   1 
ATOM   1048  N N     . LEU A 1 1451 ? 131.514 158.495 124.349 1.00 88.05  ? 1451 LEU A N     1 
ATOM   1049  C CA    . LEU A 1 1451 ? 132.761 158.512 125.108 1.00 88.05  ? 1451 LEU A CA    1 
ATOM   1050  C C     . LEU A 1 1451 ? 133.939 158.938 124.236 1.00 88.05  ? 1451 LEU A C     1 
ATOM   1051  O O     . LEU A 1 1451 ? 134.813 159.696 124.685 1.00 88.05  ? 1451 LEU A O     1 
ATOM   1052  C CB    . LEU A 1 1451 ? 133.006 157.140 125.731 1.00 88.05  ? 1451 LEU A CB    1 
ATOM   1053  C CG    . LEU A 1 1451 ? 132.201 156.895 127.009 1.00 88.05  ? 1451 LEU A CG    1 
ATOM   1054  C CD1   . LEU A 1 1451 ? 131.761 155.444 127.120 1.00 88.05  ? 1451 LEU A CD1   1 
ATOM   1055  C CD2   . LEU A 1 1451 ? 133.005 157.309 128.232 1.00 88.05  ? 1451 LEU A CD2   1 
ATOM   1056  N N     . VAL A 1 1452 ? 133.979 158.459 122.989 1.00 87.84  ? 1452 VAL A N     1 
ATOM   1057  C CA    . VAL A 1 1452 ? 135.020 158.901 122.063 1.00 87.84  ? 1452 VAL A CA    1 
ATOM   1058  C C     . VAL A 1 1452 ? 134.930 160.405 121.847 1.00 87.84  ? 1452 VAL A C     1 
ATOM   1059  O O     . VAL A 1 1452 ? 135.942 161.117 121.879 1.00 87.84  ? 1452 VAL A O     1 
ATOM   1060  C CB    . VAL A 1 1452 ? 134.922 158.130 120.734 1.00 87.84  ? 1452 VAL A CB    1 
ATOM   1061  C CG1   . VAL A 1 1452 ? 135.838 158.751 119.692 1.00 87.84  ? 1452 VAL A CG1   1 
ATOM   1062  C CG2   . VAL A 1 1452 ? 135.268 156.666 120.944 1.00 87.84  ? 1452 VAL A CG2   1 
ATOM   1063  N N     . ALA A 1 1453 ? 133.713 160.916 121.649 1.00 87.53  ? 1453 ALA A N     1 
ATOM   1064  C CA    . ALA A 1 1453 ? 133.527 162.353 121.485 1.00 87.53  ? 1453 ALA A CA    1 
ATOM   1065  C C     . ALA A 1 1453 ? 133.925 163.120 122.740 1.00 87.53  ? 1453 ALA A C     1 
ATOM   1066  O O     . ALA A 1 1453 ? 134.433 164.242 122.640 1.00 87.53  ? 1453 ALA A O     1 
ATOM   1067  C CB    . ALA A 1 1453 ? 132.076 162.650 121.114 1.00 87.53  ? 1453 ALA A CB    1 
ATOM   1068  N N     . GLN A 1 1454 ? 133.691 162.541 123.921 1.00 88.31  ? 1454 GLN A N     1 
ATOM   1069  C CA    . GLN A 1 1454 ? 134.092 163.188 125.166 1.00 88.31  ? 1454 GLN A CA    1 
ATOM   1070  C C     . GLN A 1 1454 ? 135.603 163.333 125.246 1.00 88.31  ? 1454 GLN A C     1 
ATOM   1071  O O     . GLN A 1 1454 ? 136.121 164.428 125.524 1.00 88.31  ? 1454 GLN A O     1 
ATOM   1072  C CB    . GLN A 1 1454 ? 133.548 162.410 126.364 1.00 88.31  ? 1454 GLN A CB    1 
ATOM   1073  C CG    . GLN A 1 1454 ? 134.151 162.823 127.690 1.00 88.31  ? 1454 GLN A CG    1 
ATOM   1074  C CD    . GLN A 1 1454 ? 133.768 161.887 128.815 1.00 88.31  ? 1454 GLN A CD    1 
ATOM   1075  O OE1   . GLN A 1 1454 ? 132.593 161.768 129.165 1.00 88.31  ? 1454 GLN A OE1   1 
ATOM   1076  N NE2   . GLN A 1 1454 ? 134.755 161.199 129.377 1.00 88.31  ? 1454 GLN A NE2   1 
ATOM   1077  N N     . GLY A 1 1455 ? 136.316 162.222 125.035 1.00 89.38  ? 1455 GLY A N     1 
ATOM   1078  C CA    . GLY A 1 1455 ? 137.789 162.244 125.120 1.00 89.38  ? 1455 GLY A CA    1 
ATOM   1079  C C     . GLY A 1 1455 ? 138.373 163.270 124.169 1.00 89.38  ? 1455 GLY A C     1 
ATOM   1080  O O     . GLY A 1 1455 ? 139.250 164.050 124.601 1.00 89.38  ? 1455 GLY A O     1 
ATOM   1081  N N     . GLU A 1 1456 ? 137.898 163.279 122.920 1.00 87.52  ? 1456 GLU A N     1 
ATOM   1082  C CA    . GLU A 1 1456 ? 138.431 164.225 121.906 1.00 87.52  ? 1456 GLU A CA    1 
ATOM   1083  C C     . GLU A 1 1456 ? 138.234 165.663 122.412 1.00 87.52  ? 1456 GLU A C     1 
ATOM   1084  O O     . GLU A 1 1456 ? 139.205 166.446 122.373 1.00 87.52  ? 1456 GLU A O     1 
ATOM   1085  C CB    . GLU A 1 1456 ? 137.747 164.012 120.555 1.00 87.52  ? 1456 GLU A CB    1 
ATOM   1086  C CG    . GLU A 1 1456 ? 138.009 162.631 119.961 1.00 87.52  ? 1456 GLU A CG    1 
ATOM   1087  C CD    . GLU A 1 1456 ? 137.531 162.472 118.530 1.00 87.52  ? 1456 GLU A CD    1 
ATOM   1088  O OE1   . GLU A 1 1456 ? 137.010 163.458 117.968 1.00 87.52  ? 1456 GLU A OE1   1 
ATOM   1089  O OE2   . GLU A 1 1456 ? 137.677 161.361 117.977 1.00 87.52  ? 1456 GLU A OE2   1 
ATOM   1090  N N     . MET A 1 1457 ? 137.032 165.984 122.897 1.00 88.05  ? 1457 MET A N     1 
ATOM   1091  C CA    . MET A 1 1457 ? 136.754 167.368 123.356 1.00 88.05  ? 1457 MET A CA    1 
ATOM   1092  C C     . MET A 1 1457 ? 137.815 167.767 124.392 1.00 88.05  ? 1457 MET A C     1 
ATOM   1093  O O     . MET A 1 1457 ? 138.401 168.858 124.244 1.00 88.05  ? 1457 MET A O     1 
ATOM   1094  C CB    . MET A 1 1457 ? 135.366 167.476 123.996 1.00 88.05  ? 1457 MET A CB    1 
ATOM   1095  C CG    . MET A 1 1457 ? 134.219 167.357 123.014 1.00 88.05  ? 1457 MET A CG    1 
ATOM   1096  S SD    . MET A 1 1457 ? 132.632 167.676 123.809 1.00 88.05  ? 1457 MET A SD    1 
ATOM   1097  C CE    . MET A 1 1457 ? 132.634 166.393 125.068 1.00 88.05  ? 1457 MET A CE    1 
ATOM   1098  N N     . ALA A 1 1458 ? 138.074 166.899 125.375 1.00 83.35  ? 1458 ALA A N     1 
ATOM   1099  C CA    . ALA A 1 1458 ? 139.034 167.237 126.453 1.00 83.35  ? 1458 ALA A CA    1 
ATOM   1100  C C     . ALA A 1 1458 ? 140.395 167.594 125.851 1.00 83.35  ? 1458 ALA A C     1 
ATOM   1101  O O     . ALA A 1 1458 ? 140.939 168.667 126.192 1.00 83.35  ? 1458 ALA A O     1 
ATOM   1102  C CB    . ALA A 1 1458 ? 139.145 166.079 127.419 1.00 83.35  ? 1458 ALA A CB    1 
ATOM   1103  N N     . LEU A 1 1459 ? 140.923 166.731 124.978 1.00 83.76  ? 1459 LEU A N     1 
ATOM   1104  C CA    . LEU A 1 1459 ? 142.267 166.973 124.389 1.00 83.76  ? 1459 LEU A CA    1 
ATOM   1105  C C     . LEU A 1 1459 ? 142.223 168.238 123.517 1.00 83.76  ? 1459 LEU A C     1 
ATOM   1106  O O     . LEU A 1 1459 ? 143.142 169.076 123.642 1.00 83.76  ? 1459 LEU A O     1 
ATOM   1107  C CB    . LEU A 1 1459 ? 142.717 165.755 123.585 1.00 83.76  ? 1459 LEU A CB    1 
ATOM   1108  C CG    . LEU A 1 1459 ? 142.795 164.433 124.354 1.00 83.76  ? 1459 LEU A CG    1 
ATOM   1109  C CD1   . LEU A 1 1459 ? 143.418 163.352 123.490 1.00 83.76  ? 1459 LEU A CD1   1 
ATOM   1110  C CD2   . LEU A 1 1459 ? 143.579 164.605 125.643 1.00 83.76  ? 1459 LEU A CD2   1 
ATOM   1111  N N     . GLU A 1 1460 ? 141.191 168.369 122.679 1.00 105.28 ? 1460 GLU A N     1 
ATOM   1112  C CA    . GLU A 1 1460 ? 141.076 169.544 121.776 1.00 105.28 ? 1460 GLU A CA    1 
ATOM   1113  C C     . GLU A 1 1460 ? 141.043 170.824 122.626 1.00 105.28 ? 1460 GLU A C     1 
ATOM   1114  O O     . GLU A 1 1460 ? 141.776 171.782 122.294 1.00 105.28 ? 1460 GLU A O     1 
ATOM   1115  C CB    . GLU A 1 1460 ? 139.823 169.415 120.910 1.00 105.28 ? 1460 GLU A CB    1 
ATOM   1116  C CG    . GLU A 1 1460 ? 139.551 170.644 120.047 1.00 105.28 ? 1460 GLU A CG    1 
ATOM   1117  C CD    . GLU A 1 1460 ? 138.709 171.718 120.713 1.00 105.28 ? 1460 GLU A CD    1 
ATOM   1118  O OE1   . GLU A 1 1460 ? 138.282 171.510 121.868 1.00 105.28 ? 1460 GLU A OE1   1 
ATOM   1119  O OE2   . GLU A 1 1460 ? 138.481 172.765 120.073 1.00 105.28 ? 1460 GLU A OE2   1 
ATOM   1120  N N     . GLU A 1 1461 ? 140.229 170.821 123.685 1.00 107.11 ? 1461 GLU A N     1 
ATOM   1121  C CA    . GLU A 1 1461 ? 140.119 171.988 124.596 1.00 107.11 ? 1461 GLU A CA    1 
ATOM   1122  C C     . GLU A 1 1461 ? 141.495 172.261 125.221 1.00 107.11 ? 1461 GLU A C     1 
ATOM   1123  O O     . GLU A 1 1461 ? 141.869 173.446 125.328 1.00 107.11 ? 1461 GLU A O     1 
ATOM   1124  C CB    . GLU A 1 1461 ? 139.066 171.715 125.669 1.00 107.11 ? 1461 GLU A CB    1 
ATOM   1125  C CG    . GLU A 1 1461 ? 137.654 171.586 125.104 1.00 107.11 ? 1461 GLU A CG    1 
ATOM   1126  C CD    . GLU A 1 1461 ? 136.725 170.734 125.948 1.00 107.11 ? 1461 GLU A CD    1 
ATOM   1127  O OE1   . GLU A 1 1461 ? 137.175 170.230 126.998 1.00 107.11 ? 1461 GLU A OE1   1 
ATOM   1128  O OE2   . GLU A 1 1461 ? 135.552 170.567 125.551 1.00 107.11 ? 1461 GLU A OE2   1 
ATOM   1129  N N     . PHE A 1 1462 ? 142.213 171.202 125.607 1.00 110.94 ? 1462 PHE A N     1 
ATOM   1130  C CA    . PHE A 1 1462 ? 143.550 171.366 126.240 1.00 110.94 ? 1462 PHE A CA    1 
ATOM   1131  C C     . PHE A 1 1462 ? 144.492 172.040 125.243 1.00 110.94 ? 1462 PHE A C     1 
ATOM   1132  O O     . PHE A 1 1462 ? 145.218 172.981 125.633 1.00 110.94 ? 1462 PHE A O     1 
ATOM   1133  C CB    . PHE A 1 1462 ? 144.089 170.011 126.707 1.00 110.94 ? 1462 PHE A CB    1 
ATOM   1134  C CG    . PHE A 1 1462 ? 145.354 170.108 127.548 1.00 110.94 ? 1462 PHE A CG    1 
ATOM   1135  C CD1   . PHE A 1 1462 ? 145.283 170.245 128.930 1.00 110.94 ? 1462 PHE A CD1   1 
ATOM   1136  C CD2   . PHE A 1 1462 ? 146.611 170.067 126.956 1.00 110.94 ? 1462 PHE A CD2   1 
ATOM   1137  C CE1   . PHE A 1 1462 ? 146.436 170.336 129.693 1.00 110.94 ? 1462 PHE A CE1   1 
ATOM   1138  C CE2   . PHE A 1 1462 ? 147.760 170.157 127.725 1.00 110.94 ? 1462 PHE A CE2   1 
ATOM   1139  C CZ    . PHE A 1 1462 ? 147.670 170.292 129.090 1.00 110.94 ? 1462 PHE A CZ    1 
ATOM   1140  N N     . LEU A 1 1463 ? 144.482 171.576 123.989 1.00 109.81 ? 1463 LEU A N     1 
ATOM   1141  C CA    . LEU A 1 1463 ? 145.325 172.205 122.939 1.00 109.81 ? 1463 LEU A CA    1 
ATOM   1142  C C     . LEU A 1 1463 ? 144.892 173.669 122.785 1.00 109.81 ? 1463 LEU A C     1 
ATOM   1143  O O     . LEU A 1 1463 ? 145.779 174.542 122.664 1.00 109.81 ? 1463 LEU A O     1 
ATOM   1144  C CB    . LEU A 1 1463 ? 145.184 171.435 121.628 1.00 109.81 ? 1463 LEU A CB    1 
ATOM   1145  C CG    . LEU A 1 1463 ? 145.641 169.973 121.658 1.00 109.81 ? 1463 LEU A CG    1 
ATOM   1146  C CD1   . LEU A 1 1463 ? 145.359 169.295 120.329 1.00 109.81 ? 1463 LEU A CD1   1 
ATOM   1147  C CD2   . LEU A 1 1463 ? 147.117 169.882 122.002 1.00 109.81 ? 1463 LEU A CD2   1 
ATOM   1148  N N     . LYS A 1 1464 ? 143.579 173.920 122.801 1.00 107.49 ? 1464 LYS A N     1 
ATOM   1149  C CA    . LYS A 1 1464 ? 143.058 175.308 122.700 1.00 107.49 ? 1464 LYS A CA    1 
ATOM   1150  C C     . LYS A 1 1464 ? 143.608 176.130 123.874 1.00 107.49 ? 1464 LYS A C     1 
ATOM   1151  O O     . LYS A 1 1464 ? 144.080 177.262 123.634 1.00 107.49 ? 1464 LYS A O     1 
ATOM   1152  C CB    . LYS A 1 1464 ? 141.528 175.269 122.715 1.00 107.49 ? 1464 LYS A CB    1 
ATOM   1153  C CG    . LYS A 1 1464 ? 140.828 176.619 122.698 1.00 107.49 ? 1464 LYS A CG    1 
ATOM   1154  C CD    . LYS A 1 1464 ? 139.320 176.464 122.846 1.00 107.49 ? 1464 LYS A CD    1 
ATOM   1155  C CE    . LYS A 1 1464 ? 138.767 175.469 121.876 1.00 107.49 ? 1464 LYS A CE    1 
ATOM   1156  N NZ    . LYS A 1 1464 ? 137.330 175.260 122.067 1.00 107.49 ? 1464 LYS A NZ    1 
ATOM   1157  N N     . GLN A 1 1465 ? 143.551 175.578 125.089 1.00 109.61 ? 1465 GLN A N     1 
ATOM   1158  C CA    . GLN A 1 1465 ? 144.116 176.274 126.274 1.00 109.61 ? 1465 GLN A CA    1 
ATOM   1159  C C     . GLN A 1 1465 ? 145.578 176.622 125.974 1.00 109.61 ? 1465 GLN A C     1 
ATOM   1160  O O     . GLN A 1 1465 ? 145.906 177.828 125.933 1.00 109.61 ? 1465 GLN A O     1 
ATOM   1161  C CB    . GLN A 1 1465 ? 144.025 175.373 127.505 1.00 109.61 ? 1465 GLN A CB    1 
ATOM   1162  C CG    . GLN A 1 1465 ? 142.617 174.868 127.799 1.00 109.61 ? 1465 GLN A CG    1 
ATOM   1163  C CD    . GLN A 1 1465 ? 142.600 173.601 128.626 1.00 109.61 ? 1465 GLN A CD    1 
ATOM   1164  O OE1   . GLN A 1 1465 ? 143.646 173.073 129.021 1.00 109.61 ? 1465 GLN A OE1   1 
ATOM   1165  N NE2   . GLN A 1 1465 ? 141.405 173.097 128.895 1.00 109.61 ? 1465 GLN A NE2   1 
ATOM   1166  N N     . ILE A 1 1466 ? 146.417 175.602 125.772 1.00 113.18 ? 1466 ILE A N     1 
ATOM   1167  C CA    . ILE A 1 1466 ? 147.818 175.842 125.429 1.00 113.18 ? 1466 ILE A CA    1 
ATOM   1168  C C     . ILE A 1 1466 ? 147.922 176.930 124.367 1.00 113.18 ? 1466 ILE A C     1 
ATOM   1169  O O     . ILE A 1 1466 ? 148.749 177.848 124.465 1.00 113.18 ? 1466 ILE A O     1 
ATOM   1170  C CB    . ILE A 1 1466 ? 148.491 174.537 124.966 1.00 113.18 ? 1466 ILE A CB    1 
ATOM   1171  C CG1   . ILE A 1 1466 ? 148.955 173.711 126.166 1.00 113.18 ? 1466 ILE A CG1   1 
ATOM   1172  C CG2   . ILE A 1 1466 ? 149.664 174.828 124.037 1.00 113.18 ? 1466 ILE A CG2   1 
ATOM   1173  C CD1   . ILE A 1 1466 ? 149.426 172.324 125.797 1.00 113.18 ? 1466 ILE A CD1   1 
ATOM   1174  N N     . ARG A 1 1467 ? 147.078 176.841 123.336 1.00 111.60 ? 1467 ARG A N     1 
ATOM   1175  C CA    . ARG A 1 1467 ? 147.099 177.827 122.261 1.00 111.60 ? 1467 ARG A CA    1 
ATOM   1176  C C     . ARG A 1 1467 ? 146.791 179.222 122.789 1.00 111.60 ? 1467 ARG A C     1 
ATOM   1177  O O     . ARG A 1 1467 ? 147.491 180.189 122.468 1.00 111.60 ? 1467 ARG A O     1 
ATOM   1178  C CB    . ARG A 1 1467 ? 146.100 177.428 121.175 1.00 111.60 ? 1467 ARG A CB    1 
ATOM   1179  C CG    . ARG A 1 1467 ? 146.218 178.222 119.885 1.00 111.60 ? 1467 ARG A CG    1 
ATOM   1180  C CD    . ARG A 1 1467 ? 145.390 177.595 118.770 1.00 111.60 ? 1467 ARG A CD    1 
ATOM   1181  N NE    . ARG A 1 1467 ? 145.861 176.261 118.414 1.00 111.60 ? 1467 ARG A NE    1 
ATOM   1182  C CZ    . ARG A 1 1467 ? 145.272 175.133 118.789 1.00 111.60 ? 1467 ARG A CZ    1 
ATOM   1183  N NH1   . ARG A 1 1467 ? 144.179 175.138 119.535 1.00 111.60 ? 1467 ARG A NH1   1 
ATOM   1184  N NH2   . ARG A 1 1467 ? 145.793 173.971 118.405 1.00 111.60 ? 1467 ARG A NH2   1 
ATOM   1185  N N     . GLU A 1 1468 ? 145.749 179.343 123.614 1.00 110.86 ? 1468 GLU A N     1 
ATOM   1186  C CA    . GLU A 1 1468 ? 145.384 180.643 124.168 1.00 110.86 ? 1468 GLU A CA    1 
ATOM   1187  C C     . GLU A 1 1468 ? 146.485 181.192 125.067 1.00 110.86 ? 1468 GLU A C     1 
ATOM   1188  O O     . GLU A 1 1468 ? 146.817 182.382 124.998 1.00 110.86 ? 1468 GLU A O     1 
ATOM   1189  C CB    . GLU A 1 1468 ? 144.067 180.531 124.936 1.00 110.86 ? 1468 GLU A CB    1 
ATOM   1190  C CG    . GLU A 1 1468 ? 143.585 181.836 125.548 1.00 110.86 ? 1468 GLU A CG    1 
ATOM   1191  C CD    . GLU A 1 1468 ? 143.983 181.979 127.005 1.00 110.86 ? 1468 GLU A CD    1 
ATOM   1192  O OE1   . GLU A 1 1468 ? 143.993 180.957 127.723 1.00 110.86 ? 1468 GLU A OE1   1 
ATOM   1193  O OE2   . GLU A 1 1468 ? 144.288 183.113 127.431 1.00 110.86 ? 1468 GLU A OE2   1 
ATOM   1194  N N     . VAL A 1 1469 ? 147.067 180.338 125.912 1.00 111.79 ? 1469 VAL A N     1 
ATOM   1195  C CA    . VAL A 1 1469 ? 148.100 180.787 126.841 1.00 111.79 ? 1469 VAL A CA    1 
ATOM   1196  C C     . VAL A 1 1469 ? 149.318 181.288 126.077 1.00 111.79 ? 1469 VAL A C     1 
ATOM   1197  O O     . VAL A 1 1469 ? 149.869 182.352 126.382 1.00 111.79 ? 1469 VAL A O     1 
ATOM   1198  C CB    . VAL A 1 1469 ? 148.469 179.656 127.818 1.00 111.79 ? 1469 VAL A CB    1 
ATOM   1199  C CG1   . VAL A 1 1469 ? 149.831 179.912 128.446 1.00 111.79 ? 1469 VAL A CG1   1 
ATOM   1200  C CG2   . VAL A 1 1469 ? 147.402 179.516 128.893 1.00 111.79 ? 1469 VAL A CG2   1 
ATOM   1201  N N     . TRP A 1 1470 ? 149.747 180.541 125.059 1.00 114.97 ? 1470 TRP A N     1 
ATOM   1202  C CA    . TRP A 1 1470 ? 150.945 180.927 124.327 1.00 114.97 ? 1470 TRP A CA    1 
ATOM   1203  C C     . TRP A 1 1470 ? 150.681 181.983 123.262 1.00 114.97 ? 1470 TRP A C     1 
ATOM   1204  O O     . TRP A 1 1470 ? 151.641 182.528 122.707 1.00 114.97 ? 1470 TRP A O     1 
ATOM   1205  C CB    . TRP A 1 1470 ? 151.597 179.695 123.699 1.00 114.97 ? 1470 TRP A CB    1 
ATOM   1206  C CG    . TRP A 1 1470 ? 152.370 178.892 124.697 1.00 114.97 ? 1470 TRP A CG    1 
ATOM   1207  C CD1   . TRP A 1 1470 ? 152.177 177.582 125.020 1.00 114.97 ? 1470 TRP A CD1   1 
ATOM   1208  C CD2   . TRP A 1 1470 ? 153.449 179.354 125.522 1.00 114.97 ? 1470 TRP A CD2   1 
ATOM   1209  N NE1   . TRP A 1 1470 ? 153.072 177.197 125.988 1.00 114.97 ? 1470 TRP A NE1   1 
ATOM   1210  C CE2   . TRP A 1 1470 ? 153.865 178.266 126.312 1.00 114.97 ? 1470 TRP A CE2   1 
ATOM   1211  C CE3   . TRP A 1 1470 ? 154.107 180.581 125.663 1.00 114.97 ? 1470 TRP A CE3   1 
ATOM   1212  C CZ2   . TRP A 1 1470 ? 154.907 178.366 127.230 1.00 114.97 ? 1470 TRP A CZ2   1 
ATOM   1213  C CZ3   . TRP A 1 1470 ? 155.140 180.678 126.576 1.00 114.97 ? 1470 TRP A CZ3   1 
ATOM   1214  C CH2   . TRP A 1 1470 ? 155.530 179.578 127.347 1.00 114.97 ? 1470 TRP A CH2   1 
ATOM   1215  N N     . ASN A 1 1471 ? 149.418 182.285 122.962 1.00 110.16 ? 1471 ASN A N     1 
ATOM   1216  C CA    . ASN A 1 1471 ? 149.102 183.419 122.106 1.00 110.16 ? 1471 ASN A CA    1 
ATOM   1217  C C     . ASN A 1 1471 ? 148.834 184.693 122.893 1.00 110.16 ? 1471 ASN A C     1 
ATOM   1218  O O     . ASN A 1 1471 ? 148.883 185.784 122.314 1.00 110.16 ? 1471 ASN A O     1 
ATOM   1219  C CB    . ASN A 1 1471 ? 147.889 183.096 121.229 1.00 110.16 ? 1471 ASN A CB    1 
ATOM   1220  C CG    . ASN A 1 1471 ? 148.222 182.135 120.106 1.00 110.16 ? 1471 ASN A CG    1 
ATOM   1221  O OD1   . ASN A 1 1471 ? 149.384 181.979 119.731 1.00 110.16 ? 1471 ASN A OD1   1 
ATOM   1222  N ND2   . ASN A 1 1471 ? 147.201 181.482 119.563 1.00 110.16 ? 1471 ASN A ND2   1 
ATOM   1223  N N     . THR A 1 1472 ? 148.553 184.581 124.192 1.00 111.84 ? 1472 THR A N     1 
ATOM   1224  C CA    . THR A 1 1472 ? 148.320 185.740 125.044 1.00 111.84 ? 1472 THR A CA    1 
ATOM   1225  C C     . THR A 1 1472 ? 149.436 185.956 126.061 1.00 111.84 ? 1472 THR A C     1 
ATOM   1226  O O     . THR A 1 1472 ? 149.282 186.781 126.967 1.00 111.84 ? 1472 THR A O     1 
ATOM   1227  C CB    . THR A 1 1472 ? 146.977 185.605 125.766 1.00 111.84 ? 1472 THR A CB    1 
ATOM   1228  O OG1   . THR A 1 1472 ? 146.960 184.388 126.523 1.00 111.84 ? 1472 THR A OG1   1 
ATOM   1229  C CG2   . THR A 1 1472 ? 145.834 185.588 124.762 1.00 111.84 ? 1472 THR A CG2   1 
ATOM   1230  N N     . TYR A 1 1473 ? 150.551 185.241 125.934 1.00 116.35 ? 1473 TYR A N     1 
ATOM   1231  C CA    . TYR A 1 1473 ? 151.665 185.374 126.864 1.00 116.35 ? 1473 TYR A CA    1 
ATOM   1232  C C     . TYR A 1 1473 ? 152.559 186.531 126.440 1.00 116.35 ? 1473 TYR A C     1 
ATOM   1233  O O     . TYR A 1 1473 ? 152.940 186.635 125.270 1.00 116.35 ? 1473 TYR A O     1 
ATOM   1234  C CB    . TYR A 1 1473 ? 152.475 184.078 126.928 1.00 116.35 ? 1473 TYR A CB    1 
ATOM   1235  C CG    . TYR A 1 1473 ? 153.180 183.861 128.247 1.00 116.35 ? 1473 TYR A CG    1 
ATOM   1236  C CD1   . TYR A 1 1473 ? 154.334 184.565 128.564 1.00 116.35 ? 1473 TYR A CD1   1 
ATOM   1237  C CD2   . TYR A 1 1473 ? 152.692 182.950 129.175 1.00 116.35 ? 1473 TYR A CD2   1 
ATOM   1238  C CE1   . TYR A 1 1473 ? 154.982 184.369 129.769 1.00 116.35 ? 1473 TYR A CE1   1 
ATOM   1239  C CE2   . TYR A 1 1473 ? 153.333 182.747 130.383 1.00 116.35 ? 1473 TYR A CE2   1 
ATOM   1240  C CZ    . TYR A 1 1473 ? 154.478 183.459 130.674 1.00 116.35 ? 1473 TYR A CZ    1 
ATOM   1241  O OH    . TYR A 1 1473 ? 155.120 183.261 131.875 1.00 116.35 ? 1473 TYR A OH    1 
ATOM   1242  N N     . GLU A 1 1474 ? 152.897 187.393 127.396 1.00 115.86 ? 1474 GLU A N     1 
ATOM   1243  C CA    . GLU A 1 1474 ? 153.758 188.540 127.155 1.00 115.86 ? 1474 GLU A CA    1 
ATOM   1244  C C     . GLU A 1 1474 ? 154.962 188.484 128.085 1.00 115.86 ? 1474 GLU A C     1 
ATOM   1245  O O     . GLU A 1 1474 ? 154.823 188.209 129.281 1.00 115.86 ? 1474 GLU A O     1 
ATOM   1246  C CB    . GLU A 1 1474 ? 152.999 189.856 127.359 1.00 115.86 ? 1474 GLU A CB    1 
ATOM   1247  C CG    . GLU A 1 1474 ? 152.033 190.194 126.234 1.00 115.86 ? 1474 GLU A CG    1 
ATOM   1248  C CD    . GLU A 1 1474 ? 151.467 191.596 126.352 1.00 115.86 ? 1474 GLU A CD    1 
ATOM   1249  O OE1   . GLU A 1 1474 ? 151.915 192.347 127.244 1.00 115.86 ? 1474 GLU A OE1   1 
ATOM   1250  O OE2   . GLU A 1 1474 ? 150.574 191.947 125.553 1.00 115.86 ? 1474 GLU A OE2   1 
ATOM   1251  N N     . LEU A 1 1475 ? 156.143 188.743 127.528 1.00 116.56 ? 1475 LEU A N     1 
ATOM   1252  C CA    . LEU A 1 1475 ? 157.374 188.737 128.308 1.00 116.56 ? 1475 LEU A CA    1 
ATOM   1253  C C     . LEU A 1 1475 ? 157.491 190.043 129.084 1.00 116.56 ? 1475 LEU A C     1 
ATOM   1254  O O     . LEU A 1 1475 ? 157.532 191.125 128.487 1.00 116.56 ? 1475 LEU A O     1 
ATOM   1255  C CB    . LEU A 1 1475 ? 158.583 188.541 127.397 1.00 116.56 ? 1475 LEU A CB    1 
ATOM   1256  C CG    . LEU A 1 1475 ? 158.800 187.136 126.834 1.00 116.56 ? 1475 LEU A CG    1 
ATOM   1257  C CD1   . LEU A 1 1475 ? 160.056 187.091 125.979 1.00 116.56 ? 1475 LEU A CD1   1 
ATOM   1258  C CD2   . LEU A 1 1475 ? 158.876 186.115 127.956 1.00 116.56 ? 1475 LEU A CD2   1 
ATOM   1259  N N     . ASP A 1 1476 ? 157.543 189.942 130.409 1.00 117.40 ? 1476 ASP A N     1 
ATOM   1260  C CA    . ASP A 1 1476 ? 157.666 191.128 131.245 1.00 117.40 ? 1476 ASP A CA    1 
ATOM   1261  C C     . ASP A 1 1476 ? 159.039 191.765 131.070 1.00 117.40 ? 1476 ASP A C     1 
ATOM   1262  O O     . ASP A 1 1476 ? 160.049 191.074 130.914 1.00 117.40 ? 1476 ASP A O     1 
ATOM   1263  C CB    . ASP A 1 1476 ? 157.436 190.769 132.712 1.00 117.40 ? 1476 ASP A CB    1 
ATOM   1264  C CG    . ASP A 1 1476 ? 157.413 191.987 133.613 1.00 117.40 ? 1476 ASP A CG    1 
ATOM   1265  O OD1   . ASP A 1 1476 ? 156.457 192.784 133.513 1.00 117.40 ? 1476 ASP A OD1   1 
ATOM   1266  O OD2   . ASP A 1 1476 ? 158.353 192.150 134.418 1.00 117.40 ? 1476 ASP A OD2   1 
ATOM   1267  N N     . LEU A 1 1477 ? 159.071 193.096 131.095 1.00 114.19 ? 1477 LEU A N     1 
ATOM   1268  C CA    . LEU A 1 1477 ? 160.303 193.855 130.941 1.00 114.19 ? 1477 LEU A CA    1 
ATOM   1269  C C     . LEU A 1 1477 ? 160.406 194.888 132.054 1.00 114.19 ? 1477 LEU A C     1 
ATOM   1270  O O     . LEU A 1 1477 ? 159.432 195.582 132.360 1.00 114.19 ? 1477 LEU A O     1 
ATOM   1271  C CB    . LEU A 1 1477 ? 160.363 194.549 129.574 1.00 114.19 ? 1477 LEU A CB    1 
ATOM   1272  C CG    . LEU A 1 1477 ? 160.033 193.693 128.349 1.00 114.19 ? 1477 LEU A CG    1 
ATOM   1273  C CD1   . LEU A 1 1477 ? 159.724 194.573 127.147 1.00 114.19 ? 1477 LEU A CD1   1 
ATOM   1274  C CD2   . LEU A 1 1477 ? 161.169 192.731 128.038 1.00 114.19 ? 1477 LEU A CD2   1 
ATOM   1275  N N     . VAL A 1 1478 ? 161.590 194.987 132.654 1.00 108.92 ? 1478 VAL A N     1 
ATOM   1276  C CA    . VAL A 1 1478 ? 161.852 195.925 133.739 1.00 108.92 ? 1478 VAL A CA    1 
ATOM   1277  C C     . VAL A 1 1478 ? 163.107 196.721 133.409 1.00 108.92 ? 1478 VAL A C     1 
ATOM   1278  O O     . VAL A 1 1478 ? 164.122 196.155 132.990 1.00 108.92 ? 1478 VAL A O     1 
ATOM   1279  C CB    . VAL A 1 1478 ? 162.001 195.206 135.096 1.00 108.92 ? 1478 VAL A CB    1 
ATOM   1280  C CG1   . VAL A 1 1478 ? 160.641 194.762 135.605 1.00 108.92 ? 1478 VAL A CG1   1 
ATOM   1281  C CG2   . VAL A 1 1478 ? 162.939 194.015 134.972 1.00 108.92 ? 1478 VAL A CG2   1 
ATOM   1282  N N     . ASN A 1 1479 ? 163.033 198.037 133.602 1.00 103.99 ? 1479 ASN A N     1 
ATOM   1283  C CA    . ASN A 1 1479 ? 164.144 198.912 133.254 1.00 103.99 ? 1479 ASN A CA    1 
ATOM   1284  C C     . ASN A 1 1479 ? 165.373 198.590 134.095 1.00 103.99 ? 1479 ASN A C     1 
ATOM   1285  O O     . ASN A 1 1479 ? 165.267 198.228 135.270 1.00 103.99 ? 1479 ASN A O     1 
ATOM   1286  C CB    . ASN A 1 1479 ? 163.743 200.376 133.445 1.00 103.99 ? 1479 ASN A CB    1 
ATOM   1287  C CG    . ASN A 1 1479 ? 164.828 201.340 133.003 1.00 103.99 ? 1479 ASN A CG    1 
ATOM   1288  O OD1   . ASN A 1 1479 ? 165.404 201.193 131.925 1.00 103.99 ? 1479 ASN A OD1   1 
ATOM   1289  N ND2   . ASN A 1 1479 ? 165.112 202.333 133.836 1.00 103.99 ? 1479 ASN A ND2   1 
ATOM   1290  N N     . TYR A 1 1480 ? 166.546 198.722 133.480 1.00 100.83 ? 1480 TYR A N     1 
ATOM   1291  C CA    . TYR A 1 1480 ? 167.825 198.426 134.121 1.00 100.83 ? 1480 TYR A CA    1 
ATOM   1292  C C     . TYR A 1 1480 ? 168.743 199.632 133.948 1.00 100.83 ? 1480 TYR A C     1 
ATOM   1293  O O     . TYR A 1 1480 ? 169.377 199.790 132.899 1.00 100.83 ? 1480 TYR A O     1 
ATOM   1294  C CB    . TYR A 1 1480 ? 168.448 197.165 133.531 1.00 100.83 ? 1480 TYR A CB    1 
ATOM   1295  C CG    . TYR A 1 1480 ? 169.860 196.896 133.999 1.00 100.83 ? 1480 TYR A CG    1 
ATOM   1296  C CD1   . TYR A 1 1480 ? 170.108 196.418 135.278 1.00 100.83 ? 1480 TYR A CD1   1 
ATOM   1297  C CD2   . TYR A 1 1480 ? 170.944 197.110 133.158 1.00 100.83 ? 1480 TYR A CD2   1 
ATOM   1298  C CE1   . TYR A 1 1480 ? 171.397 196.168 135.709 1.00 100.83 ? 1480 TYR A CE1   1 
ATOM   1299  C CE2   . TYR A 1 1480 ? 172.237 196.862 133.581 1.00 100.83 ? 1480 TYR A CE2   1 
ATOM   1300  C CZ    . TYR A 1 1480 ? 172.457 196.391 134.858 1.00 100.83 ? 1480 TYR A CZ    1 
ATOM   1301  O OH    . TYR A 1 1480 ? 173.740 196.142 135.287 1.00 100.83 ? 1480 TYR A OH    1 
ATOM   1302  N N     . GLN A 1 1481 ? 168.804 200.480 134.976 1.00 100.00 ? 1481 GLN A N     1 
ATOM   1303  C CA    . GLN A 1 1481 ? 169.696 201.641 135.003 1.00 100.00 ? 1481 GLN A CA    1 
ATOM   1304  C C     . GLN A 1 1481 ? 169.464 202.569 133.814 1.00 100.00 ? 1481 GLN A C     1 
ATOM   1305  O O     . GLN A 1 1481 ? 170.400 203.207 133.324 1.00 100.00 ? 1481 GLN A O     1 
ATOM   1306  C CB    . GLN A 1 1481 ? 171.164 201.209 135.060 1.00 100.00 ? 1481 GLN A CB    1 
ATOM   1307  C CG    . GLN A 1 1481 ? 171.620 200.728 136.427 1.00 100.00 ? 1481 GLN A CG    1 
ATOM   1308  C CD    . GLN A 1 1481 ? 172.663 199.631 136.338 1.00 100.00 ? 1481 GLN A CD    1 
ATOM   1309  O OE1   . GLN A 1 1481 ? 173.464 199.594 135.405 1.00 100.00 ? 1481 GLN A OE1   1 
ATOM   1310  N NE2   . GLN A 1 1481 ? 172.658 198.731 137.313 1.00 100.00 ? 1481 GLN A NE2   1 
ATOM   1311  N N     . ASN A 1 1482 ? 168.216 202.647 133.345 1.00 104.02 ? 1482 ASN A N     1 
ATOM   1312  C CA    . ASN A 1 1482 ? 167.842 203.481 132.201 1.00 104.02 ? 1482 ASN A CA    1 
ATOM   1313  C C     . ASN A 1 1482 ? 168.658 203.139 130.957 1.00 104.02 ? 1482 ASN A C     1 
ATOM   1314  O O     . ASN A 1 1482 ? 168.941 204.007 130.127 1.00 104.02 ? 1482 ASN A O     1 
ATOM   1315  C CB    . ASN A 1 1482 ? 167.969 204.971 132.533 1.00 104.02 ? 1482 ASN A CB    1 
ATOM   1316  C CG    . ASN A 1 1482 ? 167.165 205.366 133.756 1.00 104.02 ? 1482 ASN A CG    1 
ATOM   1317  O OD1   . ASN A 1 1482 ? 166.103 204.803 134.022 1.00 104.02 ? 1482 ASN A OD1   1 
ATOM   1318  N ND2   . ASN A 1 1482 ? 167.669 206.337 134.508 1.00 104.02 ? 1482 ASN A ND2   1 
ATOM   1319  N N     . LYS A 1 1483 ? 169.041 201.873 130.820 1.00 97.93  ? 1483 LYS A N     1 
ATOM   1320  C CA    . LYS A 1 1483 ? 169.803 201.391 129.674 1.00 97.93  ? 1483 LYS A CA    1 
ATOM   1321  C C     . LYS A 1 1483 ? 169.008 200.454 128.782 1.00 97.93  ? 1483 LYS A C     1 
ATOM   1322  O O     . LYS A 1 1483 ? 169.074 200.571 127.557 1.00 97.93  ? 1483 LYS A O     1 
ATOM   1323  C CB    . LYS A 1 1483 ? 171.074 200.680 130.150 1.00 97.93  ? 1483 LYS A CB    1 
ATOM   1324  C CG    . LYS A 1 1483 ? 172.017 201.576 130.931 1.00 97.93  ? 1483 LYS A CG    1 
ATOM   1325  C CD    . LYS A 1 1483 ? 173.320 200.867 131.253 1.00 97.93  ? 1483 LYS A CD    1 
ATOM   1326  C CE    . LYS A 1 1483 ? 174.253 201.778 132.031 1.00 97.93  ? 1483 LYS A CE    1 
ATOM   1327  N NZ    . LYS A 1 1483 ? 175.328 201.016 132.720 1.00 97.93  ? 1483 LYS A NZ    1 
ATOM   1328  N N     . CYS A 1 1484 ? 168.257 199.529 129.370 1.00 99.99  ? 1484 CYS A N     1 
ATOM   1329  C CA    . CYS A 1 1484 ? 167.398 198.620 128.624 1.00 99.99  ? 1484 CYS A CA    1 
ATOM   1330  C C     . CYS A 1 1484 ? 166.322 198.111 129.576 1.00 99.99  ? 1484 CYS A C     1 
ATOM   1331  O O     . CYS A 1 1484 ? 166.243 198.535 130.734 1.00 99.99  ? 1484 CYS A O     1 
ATOM   1332  C CB    . CYS A 1 1484 ? 168.208 197.476 128.006 1.00 99.99  ? 1484 CYS A CB    1 
ATOM   1333  S SG    . CYS A 1 1484 ? 169.153 196.509 129.200 1.00 99.99  ? 1484 CYS A SG    1 
ATOM   1334  N N     . ARG A 1 1485 ? 165.490 197.194 129.088 1.00 106.41 ? 1485 ARG A N     1 
ATOM   1335  C CA    . ARG A 1 1485 ? 164.415 196.601 129.875 1.00 106.41 ? 1485 ARG A CA    1 
ATOM   1336  C C     . ARG A 1 1485 ? 164.608 195.091 129.892 1.00 106.41 ? 1485 ARG A C     1 
ATOM   1337  O O     . ARG A 1 1485 ? 164.144 194.393 128.984 1.00 106.41 ? 1485 ARG A O     1 
ATOM   1338  C CB    . ARG A 1 1485 ? 163.048 196.970 129.303 1.00 106.41 ? 1485 ARG A CB    1 
ATOM   1339  C CG    . ARG A 1 1485 ? 162.768 198.460 129.256 1.00 106.41 ? 1485 ARG A CG    1 
ATOM   1340  C CD    . ARG A 1 1485 ? 161.380 198.716 128.701 1.00 106.41 ? 1485 ARG A CD    1 
ATOM   1341  N NE    . ARG A 1 1485 ? 160.360 198.026 129.480 1.00 106.41 ? 1485 ARG A NE    1 
ATOM   1342  C CZ    . ARG A 1 1485 ? 159.058 198.255 129.382 1.00 106.41 ? 1485 ARG A CZ    1 
ATOM   1343  N NH1   . ARG A 1 1485 ? 158.575 199.152 128.539 1.00 106.41 ? 1485 ARG A NH1   1 
ATOM   1344  N NH2   . ARG A 1 1485 ? 158.219 197.564 130.149 1.00 106.41 ? 1485 ARG A NH2   1 
ATOM   1345  N N     . LEU A 1 1486 ? 165.274 194.588 130.925 1.00 104.29 ? 1486 LEU A N     1 
ATOM   1346  C CA    . LEU A 1 1486 ? 165.572 193.168 131.017 1.00 104.29 ? 1486 LEU A CA    1 
ATOM   1347  C C     . LEU A 1 1486 ? 164.306 192.377 131.335 1.00 104.29 ? 1486 LEU A C     1 
ATOM   1348  O O     . LEU A 1 1486 ? 163.336 192.902 131.886 1.00 104.29 ? 1486 LEU A O     1 
ATOM   1349  C CB    . LEU A 1 1486 ? 166.638 192.899 132.079 1.00 104.29 ? 1486 LEU A CB    1 
ATOM   1350  C CG    . LEU A 1 1486 ? 168.043 193.415 131.757 1.00 104.29 ? 1486 LEU A CG    1 
ATOM   1351  C CD1   . LEU A 1 1486 ? 168.820 193.695 133.035 1.00 104.29 ? 1486 LEU A CD1   1 
ATOM   1352  C CD2   . LEU A 1 1486 ? 168.803 192.476 130.840 1.00 104.29 ? 1486 LEU A CD2   1 
ATOM   1353  N N     . ILE A 1 1487 ? 164.330 191.098 130.978 1.00 112.13 ? 1487 ILE A N     1 
ATOM   1354  C CA    . ILE A 1 1487 ? 163.172 190.231 131.164 1.00 112.13 ? 1487 ILE A CA    1 
ATOM   1355  C C     . ILE A 1 1487 ? 163.096 189.793 132.620 1.00 112.13 ? 1487 ILE A C     1 
ATOM   1356  O O     . ILE A 1 1487 ? 164.068 189.267 133.177 1.00 112.13 ? 1487 ILE A O     1 
ATOM   1357  C CB    . ILE A 1 1487 ? 163.239 189.022 130.218 1.00 112.13 ? 1487 ILE A CB    1 
ATOM   1358  C CG1   . ILE A 1 1487 ? 162.858 189.441 128.796 1.00 112.13 ? 1487 ILE A CG1   1 
ATOM   1359  C CG2   . ILE A 1 1487 ? 162.332 187.903 130.710 1.00 112.13 ? 1487 ILE A CG2   1 
ATOM   1360  C CD1   . ILE A 1 1487 ? 163.399 188.528 127.722 1.00 112.13 ? 1487 ILE A CD1   1 
ATOM   1361  N N     . ARG A 1 1488 ? 161.939 190.009 133.239 1.00 114.91 ? 1488 ARG A N     1 
ATOM   1362  C CA    . ARG A 1 1488 ? 161.681 189.612 134.615 1.00 114.91 ? 1488 ARG A CA    1 
ATOM   1363  C C     . ARG A 1 1488 ? 160.588 188.552 134.644 1.00 114.91 ? 1488 ARG A C     1 
ATOM   1364  O O     . ARG A 1 1488 ? 159.611 188.632 133.893 1.00 114.91 ? 1488 ARG A O     1 
ATOM   1365  C CB    . ARG A 1 1488 ? 161.267 190.818 135.465 1.00 114.91 ? 1488 ARG A CB    1 
ATOM   1366  C CG    . ARG A 1 1488 ? 160.812 190.471 136.876 1.00 114.91 ? 1488 ARG A CG    1 
ATOM   1367  C CD    . ARG A 1 1488 ? 160.378 191.712 137.641 1.00 114.91 ? 1488 ARG A CD    1 
ATOM   1368  N NE    . ARG A 1 1488 ? 159.094 192.226 137.178 1.00 114.91 ? 1488 ARG A NE    1 
ATOM   1369  C CZ    . ARG A 1 1488 ? 157.918 191.689 137.472 1.00 114.91 ? 1488 ARG A CZ    1 
ATOM   1370  N NH1   . ARG A 1 1488 ? 157.820 190.618 138.243 1.00 114.91 ? 1488 ARG A NH1   1 
ATOM   1371  N NH2   . ARG A 1 1488 ? 156.812 192.241 136.982 1.00 114.91 ? 1488 ARG A NH2   1 
ATOM   1372  N N     . GLY A 1 1489 ? 160.758 187.558 135.512 1.00 111.45 ? 1489 GLY A N     1 
ATOM   1373  C CA    . GLY A 1 1489 ? 159.795 186.481 135.621 1.00 111.45 ? 1489 GLY A CA    1 
ATOM   1374  C C     . GLY A 1 1489 ? 160.276 185.200 134.974 1.00 111.45 ? 1489 GLY A C     1 
ATOM   1375  O O     . GLY A 1 1489 ? 159.500 184.490 134.327 1.00 111.45 ? 1489 GLY A O     1 
ATOM   1376  N N     . TRP A 1 1490 ? 161.567 184.901 135.138 1.00 114.43 ? 1490 TRP A N     1 
ATOM   1377  C CA    . TRP A 1 1490 ? 162.128 183.689 134.552 1.00 114.43 ? 1490 TRP A CA    1 
ATOM   1378  C C     . TRP A 1 1490 ? 161.514 182.437 135.162 1.00 114.43 ? 1490 TRP A C     1 
ATOM   1379  O O     . TRP A 1 1490 ? 161.230 181.467 134.449 1.00 114.43 ? 1490 TRP A O     1 
ATOM   1380  C CB    . TRP A 1 1490 ? 163.646 183.676 134.724 1.00 114.43 ? 1490 TRP A CB    1 
ATOM   1381  C CG    . TRP A 1 1490 ? 164.352 184.594 133.786 1.00 114.43 ? 1490 TRP A CG    1 
ATOM   1382  C CD1   . TRP A 1 1490 ? 165.088 185.694 134.110 1.00 114.43 ? 1490 TRP A CD1   1 
ATOM   1383  C CD2   . TRP A 1 1490 ? 164.388 184.492 132.359 1.00 114.43 ? 1490 TRP A CD2   1 
ATOM   1384  N NE1   . TRP A 1 1490 ? 165.580 186.285 132.973 1.00 114.43 ? 1490 TRP A NE1   1 
ATOM   1385  C CE2   . TRP A 1 1490 ? 165.165 185.565 131.884 1.00 114.43 ? 1490 TRP A CE2   1 
ATOM   1386  C CE3   . TRP A 1 1490 ? 163.838 183.596 131.438 1.00 114.43 ? 1490 TRP A CE3   1 
ATOM   1387  C CZ2   . TRP A 1 1490 ? 165.405 185.766 130.529 1.00 114.43 ? 1490 TRP A CZ2   1 
ATOM   1388  C CZ3   . TRP A 1 1490 ? 164.078 183.798 130.095 1.00 114.43 ? 1490 TRP A CZ3   1 
ATOM   1389  C CH2   . TRP A 1 1490 ? 164.853 184.873 129.652 1.00 114.43 ? 1490 TRP A CH2   1 
ATOM   1390  N N     . ASP A 1 1491 ? 161.309 182.435 136.480 1.00 118.58 ? 1491 ASP A N     1 
ATOM   1391  C CA    . ASP A 1 1491 ? 160.799 181.242 137.148 1.00 118.58 ? 1491 ASP A CA    1 
ATOM   1392  C C     . ASP A 1 1491 ? 159.405 180.881 136.648 1.00 118.58 ? 1491 ASP A C     1 
ATOM   1393  O O     . ASP A 1 1491 ? 159.116 179.710 136.380 1.00 118.58 ? 1491 ASP A O     1 
ATOM   1394  C CB    . ASP A 1 1491 ? 160.803 181.448 138.665 1.00 118.58 ? 1491 ASP A CB    1 
ATOM   1395  C CG    . ASP A 1 1491 ? 160.001 182.663 139.098 1.00 118.58 ? 1491 ASP A CG    1 
ATOM   1396  O OD1   . ASP A 1 1491 ? 159.510 183.404 138.221 1.00 118.58 ? 1491 ASP A OD1   1 
ATOM   1397  O OD2   . ASP A 1 1491 ? 159.859 182.874 140.321 1.00 118.58 ? 1491 ASP A OD2   1 
ATOM   1398  N N     . ASP A 1 1492 ? 158.530 181.880 136.500 1.00 117.62 ? 1492 ASP A N     1 
ATOM   1399  C CA    . ASP A 1 1492 ? 157.170 181.610 136.044 1.00 117.62 ? 1492 ASP A CA    1 
ATOM   1400  C C     . ASP A 1 1492 ? 157.161 181.063 134.622 1.00 117.62 ? 1492 ASP A C     1 
ATOM   1401  O O     . ASP A 1 1492 ? 156.471 180.078 134.331 1.00 117.62 ? 1492 ASP A O     1 
ATOM   1402  C CB    . ASP A 1 1492 ? 156.326 182.881 136.133 1.00 117.62 ? 1492 ASP A CB    1 
ATOM   1403  C CG    . ASP A 1 1492 ? 156.076 183.316 137.563 1.00 117.62 ? 1492 ASP A CG    1 
ATOM   1404  O OD1   . ASP A 1 1492 ? 155.997 182.439 138.448 1.00 117.62 ? 1492 ASP A OD1   1 
ATOM   1405  O OD2   . ASP A 1 1492 ? 155.959 184.537 137.802 1.00 117.62 ? 1492 ASP A OD2   1 
ATOM   1406  N N     . LEU A 1 1493 ? 157.927 181.688 133.724 1.00 115.59 ? 1493 LEU A N     1 
ATOM   1407  C CA    . LEU A 1 1493 ? 157.970 181.229 132.340 1.00 115.59 ? 1493 LEU A CA    1 
ATOM   1408  C C     . LEU A 1 1493 ? 158.547 179.824 132.240 1.00 115.59 ? 1493 LEU A C     1 
ATOM   1409  O O     . LEU A 1 1493 ? 158.021 178.980 131.504 1.00 115.59 ? 1493 LEU A O     1 
ATOM   1410  C CB    . LEU A 1 1493 ? 158.782 182.206 131.489 1.00 115.59 ? 1493 LEU A CB    1 
ATOM   1411  C CG    . LEU A 1 1493 ? 158.922 181.857 130.005 1.00 115.59 ? 1493 LEU A CG    1 
ATOM   1412  C CD1   . LEU A 1 1493 ? 157.568 181.888 129.314 1.00 115.59 ? 1493 LEU A CD1   1 
ATOM   1413  C CD2   . LEU A 1 1493 ? 159.899 182.800 129.321 1.00 115.59 ? 1493 LEU A CD2   1 
ATOM   1414  N N     . PHE A 1 1494 ? 159.628 179.550 132.975 1.00 115.10 ? 1494 PHE A N     1 
ATOM   1415  C CA    . PHE A 1 1494 ? 160.236 178.225 132.922 1.00 115.10 ? 1494 PHE A CA    1 
ATOM   1416  C C     . PHE A 1 1494 ? 159.312 177.165 133.509 1.00 115.10 ? 1494 PHE A C     1 
ATOM   1417  O O     . PHE A 1 1494 ? 159.222 176.053 132.976 1.00 115.10 ? 1494 PHE A O     1 
ATOM   1418  C CB    . PHE A 1 1494 ? 161.584 178.234 133.642 1.00 115.10 ? 1494 PHE A CB    1 
ATOM   1419  C CG    . PHE A 1 1494 ? 162.705 178.794 132.813 1.00 115.10 ? 1494 PHE A CG    1 
ATOM   1420  C CD1   . PHE A 1 1494 ? 162.885 178.383 131.503 1.00 115.10 ? 1494 PHE A CD1   1 
ATOM   1421  C CD2   . PHE A 1 1494 ? 163.580 179.728 133.342 1.00 115.10 ? 1494 PHE A CD2   1 
ATOM   1422  C CE1   . PHE A 1 1494 ? 163.913 178.894 130.735 1.00 115.10 ? 1494 PHE A CE1   1 
ATOM   1423  C CE2   . PHE A 1 1494 ? 164.611 180.243 132.579 1.00 115.10 ? 1494 PHE A CE2   1 
ATOM   1424  C CZ    . PHE A 1 1494 ? 164.778 179.825 131.273 1.00 115.10 ? 1494 PHE A CZ    1 
ATOM   1425  N N     . ASN A 1 1495 ? 158.616 177.487 134.604 1.00 115.71 ? 1495 ASN A N     1 
ATOM   1426  C CA    . ASN A 1 1495 ? 157.660 176.544 135.173 1.00 115.71 ? 1495 ASN A CA    1 
ATOM   1427  C C     . ASN A 1 1495 ? 156.523 176.261 134.200 1.00 115.71 ? 1495 ASN A C     1 
ATOM   1428  O O     . ASN A 1 1495 ? 156.115 175.105 134.031 1.00 115.71 ? 1495 ASN A O     1 
ATOM   1429  C CB    . ASN A 1 1495 ? 157.115 177.086 136.494 1.00 115.71 ? 1495 ASN A CB    1 
ATOM   1430  C CG    . ASN A 1 1495 ? 156.464 176.011 137.341 1.00 115.71 ? 1495 ASN A CG    1 
ATOM   1431  O OD1   . ASN A 1 1495 ? 155.309 175.645 137.122 1.00 115.71 ? 1495 ASN A OD1   1 
ATOM   1432  N ND2   . ASN A 1 1495 ? 157.204 175.498 138.318 1.00 115.71 ? 1495 ASN A ND2   1 
ATOM   1433  N N     . LYS A 1 1496 ? 156.004 177.304 133.545 1.00 113.39 ? 1496 LYS A N     1 
ATOM   1434  C CA    . LYS A 1 1496 ? 154.949 177.105 132.558 1.00 113.39 ? 1496 LYS A CA    1 
ATOM   1435  C C     . LYS A 1 1496 ? 155.432 176.237 131.403 1.00 113.39 ? 1496 LYS A C     1 
ATOM   1436  O O     . LYS A 1 1496 ? 154.720 175.327 130.961 1.00 113.39 ? 1496 LYS A O     1 
ATOM   1437  C CB    . LYS A 1 1496 ? 154.456 178.458 132.042 1.00 113.39 ? 1496 LYS A CB    1 
ATOM   1438  C CG    . LYS A 1 1496 ? 153.070 178.426 131.415 1.00 113.39 ? 1496 LYS A CG    1 
ATOM   1439  C CD    . LYS A 1 1496 ? 151.988 178.233 132.464 1.00 113.39 ? 1496 LYS A CD    1 
ATOM   1440  C CE    . LYS A 1 1496 ? 150.607 178.482 131.880 1.00 113.39 ? 1496 LYS A CE    1 
ATOM   1441  N NZ    . LYS A 1 1496 ? 149.543 177.772 132.641 1.00 113.39 ? 1496 LYS A NZ    1 
ATOM   1442  N N     . VAL A 1 1497 ? 156.646 176.495 130.912 1.00 110.93 ? 1497 VAL A N     1 
ATOM   1443  C CA    . VAL A 1 1497 ? 157.179 175.728 129.788 1.00 110.93 ? 1497 VAL A CA    1 
ATOM   1444  C C     . VAL A 1 1497 ? 157.365 174.267 130.181 1.00 110.93 ? 1497 VAL A C     1 
ATOM   1445  O O     . VAL A 1 1497 ? 157.020 173.354 129.422 1.00 110.93 ? 1497 VAL A O     1 
ATOM   1446  C CB    . VAL A 1 1497 ? 158.495 176.350 129.287 1.00 110.93 ? 1497 VAL A CB    1 
ATOM   1447  C CG1   . VAL A 1 1497 ? 159.211 175.392 128.353 1.00 110.93 ? 1497 VAL A CG1   1 
ATOM   1448  C CG2   . VAL A 1 1497 ? 158.227 177.670 128.587 1.00 110.93 ? 1497 VAL A CG2   1 
ATOM   1449  N N     . LYS A 1 1498 ? 157.919 174.024 131.373 1.00 111.84 ? 1498 LYS A N     1 
ATOM   1450  C CA    . LYS A 1 1498 ? 158.136 172.651 131.820 1.00 111.84 ? 1498 LYS A CA    1 
ATOM   1451  C C     . LYS A 1 1498 ? 156.816 171.914 132.011 1.00 111.84 ? 1498 LYS A C     1 
ATOM   1452  O O     . LYS A 1 1498 ? 156.681 170.752 131.603 1.00 111.84 ? 1498 LYS A O     1 
ATOM   1453  C CB    . LYS A 1 1498 ? 158.950 172.645 133.114 1.00 111.84 ? 1498 LYS A CB    1 
ATOM   1454  C CG    . LYS A 1 1498 ? 160.430 172.935 132.911 1.00 111.84 ? 1498 LYS A CG    1 
ATOM   1455  C CD    . LYS A 1 1498 ? 161.157 173.094 134.236 1.00 111.84 ? 1498 LYS A CD    1 
ATOM   1456  C CE    . LYS A 1 1498 ? 162.471 173.838 134.054 1.00 111.84 ? 1498 LYS A CE    1 
ATOM   1457  N NZ    . LYS A 1 1498 ? 163.390 173.116 133.131 1.00 111.84 ? 1498 LYS A NZ    1 
ATOM   1458  N N     . GLU A 1 1499 ? 155.827 172.574 132.622 1.00 114.77 ? 1499 GLU A N     1 
ATOM   1459  C CA    . GLU A 1 1499 ? 154.518 171.954 132.799 1.00 114.77 ? 1499 GLU A CA    1 
ATOM   1460  C C     . GLU A 1 1499 ? 153.886 171.623 131.454 1.00 114.77 ? 1499 GLU A C     1 
ATOM   1461  O O     . GLU A 1 1499 ? 153.333 170.533 131.264 1.00 114.77 ? 1499 GLU A O     1 
ATOM   1462  C CB    . GLU A 1 1499 ? 153.608 172.880 133.608 1.00 114.77 ? 1499 GLU A CB    1 
ATOM   1463  C CG    . GLU A 1 1499 ? 152.217 172.322 133.871 1.00 114.77 ? 1499 GLU A CG    1 
ATOM   1464  C CD    . GLU A 1 1499 ? 151.171 173.413 134.005 1.00 114.77 ? 1499 GLU A CD    1 
ATOM   1465  O OE1   . GLU A 1 1499 ? 151.407 174.374 134.767 1.00 114.77 ? 1499 GLU A OE1   1 
ATOM   1466  O OE2   . GLU A 1 1499 ? 150.112 173.309 133.351 1.00 114.77 ? 1499 GLU A OE2   1 
ATOM   1467  N N     . HIS A 1 1500 ? 153.969 172.556 130.500 1.00 111.59 ? 1500 HIS A N     1 
ATOM   1468  C CA    . HIS A 1 1500 ? 153.388 172.321 129.184 1.00 111.59 ? 1500 HIS A CA    1 
ATOM   1469  C C     . HIS A 1 1500 ? 154.097 171.191 128.453 1.00 111.59 ? 1500 HIS A C     1 
ATOM   1470  O O     . HIS A 1 1500 ? 153.449 170.387 127.780 1.00 111.59 ? 1500 HIS A O     1 
ATOM   1471  C CB    . HIS A 1 1500 ? 153.429 173.600 128.354 1.00 111.59 ? 1500 HIS A CB    1 
ATOM   1472  C CG    . HIS A 1 1500 ? 152.296 174.533 128.635 1.00 111.59 ? 1500 HIS A CG    1 
ATOM   1473  N ND1   . HIS A 1 1500 ? 151.643 175.232 127.643 1.00 111.59 ? 1500 HIS A ND1   1 
ATOM   1474  C CD2   . HIS A 1 1500 ? 151.698 174.883 129.799 1.00 111.59 ? 1500 HIS A CD2   1 
ATOM   1475  C CE1   . HIS A 1 1500 ? 150.691 175.972 128.183 1.00 111.59 ? 1500 HIS A CE1   1 
ATOM   1476  N NE2   . HIS A 1 1500 ? 150.703 175.779 129.489 1.00 111.59 ? 1500 HIS A NE2   1 
ATOM   1477  N N     . ILE A 1 1501 ? 155.423 171.116 128.561 1.00 106.79 ? 1501 ILE A N     1 
ATOM   1478  C CA    . ILE A 1 1501 ? 156.167 170.049 127.898 1.00 106.79 ? 1501 ILE A CA    1 
ATOM   1479  C C     . ILE A 1 1501 ? 155.797 168.694 128.492 1.00 106.79 ? 1501 ILE A C     1 
ATOM   1480  O O     . ILE A 1 1501 ? 155.574 167.713 127.767 1.00 106.79 ? 1501 ILE A O     1 
ATOM   1481  C CB    . ILE A 1 1501 ? 157.679 170.318 127.994 1.00 106.79 ? 1501 ILE A CB    1 
ATOM   1482  C CG1   . ILE A 1 1501 ? 158.109 171.323 126.924 1.00 106.79 ? 1501 ILE A CG1   1 
ATOM   1483  C CG2   . ILE A 1 1501 ? 158.470 169.023 127.874 1.00 106.79 ? 1501 ILE A CG2   1 
ATOM   1484  C CD1   . ILE A 1 1501 ? 159.516 171.845 127.110 1.00 106.79 ? 1501 ILE A CD1   1 
ATOM   1485  N N     . ASN A 1 1502 ? 155.725 168.621 129.825 1.00 105.70 ? 1502 ASN A N     1 
ATOM   1486  C CA    . ASN A 1 1502 ? 155.336 167.373 130.469 1.00 105.70 ? 1502 ASN A CA    1 
ATOM   1487  C C     . ASN A 1 1502 ? 153.924 166.966 130.069 1.00 105.70 ? 1502 ASN A C     1 
ATOM   1488  O O     . ASN A 1 1502 ? 153.667 165.790 129.799 1.00 105.70 ? 1502 ASN A O     1 
ATOM   1489  C CB    . ASN A 1 1502 ? 155.449 167.506 131.987 1.00 105.70 ? 1502 ASN A CB    1 
ATOM   1490  C CG    . ASN A 1 1502 ? 156.863 167.804 132.442 1.00 105.70 ? 1502 ASN A CG    1 
ATOM   1491  O OD1   . ASN A 1 1502 ? 157.823 167.598 131.699 1.00 105.70 ? 1502 ASN A OD1   1 
ATOM   1492  N ND2   . ASN A 1 1502 ? 156.999 168.297 133.667 1.00 105.70 ? 1502 ASN A ND2   1 
ATOM   1493  N N     . SER A 1 1503 ? 153.000 167.926 129.999 1.00 104.77 ? 1503 SER A N     1 
ATOM   1494  C CA    . SER A 1 1503 ? 151.632 167.596 129.608 1.00 104.77 ? 1503 SER A CA    1 
ATOM   1495  C C     . SER A 1 1503 ? 151.538 167.254 128.122 1.00 104.77 ? 1503 SER A C     1 
ATOM   1496  O O     . SER A 1 1503 ? 150.646 166.500 127.706 1.00 104.77 ? 1503 SER A O     1 
ATOM   1497  C CB    . SER A 1 1503 ? 150.694 168.747 129.963 1.00 104.77 ? 1503 SER A CB    1 
ATOM   1498  O OG    . SER A 1 1503 ? 150.776 169.066 131.342 1.00 104.77 ? 1503 SER A OG    1 
ATOM   1499  N N     . VAL A 1 1504 ? 152.442 167.793 127.302 1.00 104.01 ? 1504 VAL A N     1 
ATOM   1500  C CA    . VAL A 1 1504 ? 152.445 167.418 125.894 1.00 104.01 ? 1504 VAL A CA    1 
ATOM   1501  C C     . VAL A 1 1504 ? 152.898 165.976 125.736 1.00 104.01 ? 1504 VAL A C     1 
ATOM   1502  O O     . VAL A 1 1504 ? 152.273 165.184 125.014 1.00 104.01 ? 1504 VAL A O     1 
ATOM   1503  C CB    . VAL A 1 1504 ? 153.295 168.380 125.052 1.00 104.01 ? 1504 VAL A CB    1 
ATOM   1504  C CG1   . VAL A 1 1504 ? 153.550 167.768 123.692 1.00 104.01 ? 1504 VAL A CG1   1 
ATOM   1505  C CG2   . VAL A 1 1504 ? 152.568 169.698 124.875 1.00 104.01 ? 1504 VAL A CG2   1 
ATOM   1506  N N     . SER A 1 1505 ? 153.973 165.603 126.431 1.00 102.66 ? 1505 SER A N     1 
ATOM   1507  C CA    . SER A 1 1505 ? 154.317 164.189 126.514 1.00 102.66 ? 1505 SER A CA    1 
ATOM   1508  C C     . SER A 1 1505 ? 153.129 163.385 127.029 1.00 102.66 ? 1505 SER A C     1 
ATOM   1509  O O     . SER A 1 1505 ? 152.814 162.315 126.495 1.00 102.66 ? 1505 SER A O     1 
ATOM   1510  C CB    . SER A 1 1505 ? 155.544 164.001 127.403 1.00 102.66 ? 1505 SER A CB    1 
ATOM   1511  O OG    . SER A 1 1505 ? 156.676 164.651 126.844 1.00 102.66 ? 1505 SER A OG    1 
ATOM   1512  N N     . ALA A 1 1506 ? 152.416 163.929 128.020 1.00 101.79 ? 1506 ALA A N     1 
ATOM   1513  C CA    . ALA A 1 1506 ? 151.277 163.239 128.611 1.00 101.79 ? 1506 ALA A CA    1 
ATOM   1514  C C     . ALA A 1 1506 ? 150.194 162.914 127.588 1.00 101.79 ? 1506 ALA A C     1 
ATOM   1515  O O     . ALA A 1 1506 ? 149.688 161.786 127.585 1.00 101.79 ? 1506 ALA A O     1 
ATOM   1516  C CB    . ALA A 1 1506 ? 150.692 164.070 129.752 1.00 101.79 ? 1506 ALA A CB    1 
ATOM   1517  N N     . MET A 1 1507 ? 149.800 163.859 126.721 1.00 102.09 ? 1507 MET A N     1 
ATOM   1518  C CA    . MET A 1 1507 ? 148.776 163.456 125.757 1.00 102.09 ? 1507 MET A CA    1 
ATOM   1519  C C     . MET A 1 1507 ? 149.391 162.564 124.689 1.00 102.09 ? 1507 MET A C     1 
ATOM   1520  O O     . MET A 1 1507 ? 148.718 161.675 124.162 1.00 102.09 ? 1507 MET A O     1 
ATOM   1521  C CB    . MET A 1 1507 ? 148.014 164.604 125.071 1.00 102.09 ? 1507 MET A CB    1 
ATOM   1522  C CG    . MET A 1 1507 ? 148.718 165.445 124.020 1.00 102.09 ? 1507 MET A CG    1 
ATOM   1523  S SD    . MET A 1 1507 ? 149.692 166.841 124.524 1.00 102.09 ? 1507 MET A SD    1 
ATOM   1524  C CE    . MET A 1 1507 ? 148.413 167.986 125.004 1.00 102.09 ? 1507 MET A CE    1 
ATOM   1525  N N     . LYS A 1 1508 ? 150.681 162.754 124.378 1.00 102.30 ? 1508 LYS A N     1 
ATOM   1526  C CA    . LYS A 1 1508 ? 151.343 161.823 123.466 1.00 102.30 ? 1508 LYS A CA    1 
ATOM   1527  C C     . LYS A 1 1508 ? 151.225 160.393 123.975 1.00 102.30 ? 1508 LYS A C     1 
ATOM   1528  O O     . LYS A 1 1508 ? 151.278 159.435 123.194 1.00 102.30 ? 1508 LYS A O     1 
ATOM   1529  C CB    . LYS A 1 1508 ? 152.814 162.196 123.288 1.00 102.30 ? 1508 LYS A CB    1 
ATOM   1530  C CG    . LYS A 1 1508 ? 153.058 163.433 122.449 1.00 102.30 ? 1508 LYS A CG    1 
ATOM   1531  C CD    . LYS A 1 1508 ? 154.541 163.751 122.400 1.00 102.30 ? 1508 LYS A CD    1 
ATOM   1532  C CE    . LYS A 1 1508 ? 154.874 164.708 121.270 1.00 102.30 ? 1508 LYS A CE    1 
ATOM   1533  N NZ    . LYS A 1 1508 ? 156.341 164.935 121.168 1.00 102.30 ? 1508 LYS A NZ    1 
ATOM   1534  N N     . LEU A 1 1509 ? 151.078 160.235 125.287 1.00 99.49  ? 1509 LEU A N     1 
ATOM   1535  C CA    . LEU A 1 1509 ? 150.786 158.947 125.900 1.00 99.49  ? 1509 LEU A CA    1 
ATOM   1536  C C     . LEU A 1 1509 ? 149.307 158.578 125.848 1.00 99.49  ? 1509 LEU A C     1 
ATOM   1537  O O     . LEU A 1 1509 ? 148.971 157.411 126.075 1.00 99.49  ? 1509 LEU A O     1 
ATOM   1538  C CB    . LEU A 1 1509 ? 151.257 158.983 127.349 1.00 99.49  ? 1509 LEU A CB    1 
ATOM   1539  C CG    . LEU A 1 1509 ? 152.689 159.504 127.426 1.00 99.49  ? 1509 LEU A CG    1 
ATOM   1540  C CD1   . LEU A 1 1509 ? 153.002 159.992 128.818 1.00 99.49  ? 1509 LEU A CD1   1 
ATOM   1541  C CD2   . LEU A 1 1509 ? 153.689 158.449 126.969 1.00 99.49  ? 1509 LEU A CD2   1 
ATOM   1542  N N     . SER A 1 1510 ? 148.425 159.530 125.549 1.00 100.30 ? 1510 SER A N     1 
ATOM   1543  C CA    . SER A 1 1510 ? 146.992 159.283 125.606 1.00 100.30 ? 1510 SER A CA    1 
ATOM   1544  C C     . SER A 1 1510 ? 146.543 158.382 124.454 1.00 100.30 ? 1510 SER A C     1 
ATOM   1545  O O     . SER A 1 1510 ? 147.186 158.337 123.402 1.00 100.30 ? 1510 SER A O     1 
ATOM   1546  C CB    . SER A 1 1510 ? 146.227 160.606 125.560 1.00 100.30 ? 1510 SER A CB    1 
ATOM   1547  O OG    . SER A 1 1510 ? 144.826 160.408 125.507 1.00 100.30 ? 1510 SER A OG    1 
ATOM   1548  N N     . PRO A 1 1511 ? 145.448 157.637 124.638 1.00 103.10 ? 1511 PRO A N     1 
ATOM   1549  C CA    . PRO A 1 1511 ? 144.911 156.852 123.516 1.00 103.10 ? 1511 PRO A CA    1 
ATOM   1550  C C     . PRO A 1 1511 ? 144.150 157.688 122.502 1.00 103.10 ? 1511 PRO A C     1 
ATOM   1551  O O     . PRO A 1 1511 ? 144.220 157.394 121.302 1.00 103.10 ? 1511 PRO A O     1 
ATOM   1552  C CB    . PRO A 1 1511 ? 143.997 155.835 124.208 1.00 103.10 ? 1511 PRO A CB    1 
ATOM   1553  C CG    . PRO A 1 1511 ? 143.582 156.505 125.470 1.00 103.10 ? 1511 PRO A CG    1 
ATOM   1554  C CD    . PRO A 1 1511 ? 144.749 157.346 125.902 1.00 103.10 ? 1511 PRO A CD    1 
ATOM   1555  N N     . TYR A 1 1512 ? 143.424 158.719 122.939 1.00 108.26 ? 1512 TYR A N     1 
ATOM   1556  C CA    . TYR A 1 1512 ? 142.757 159.638 122.023 1.00 108.26 ? 1512 TYR A CA    1 
ATOM   1557  C C     . TYR A 1 1512 ? 143.733 160.562 121.308 1.00 108.26 ? 1512 TYR A C     1 
ATOM   1558  O O     . TYR A 1 1512 ? 143.300 161.462 120.580 1.00 108.26 ? 1512 TYR A O     1 
ATOM   1559  C CB    . TYR A 1 1512 ? 141.717 160.479 122.771 1.00 108.26 ? 1512 TYR A CB    1 
ATOM   1560  C CG    . TYR A 1 1512 ? 140.909 159.724 123.801 1.00 108.26 ? 1512 TYR A CG    1 
ATOM   1561  C CD1   . TYR A 1 1512 ? 139.884 158.868 123.418 1.00 108.26 ? 1512 TYR A CD1   1 
ATOM   1562  C CD2   . TYR A 1 1512 ? 141.158 159.882 125.158 1.00 108.26 ? 1512 TYR A CD2   1 
ATOM   1563  C CE1   . TYR A 1 1512 ? 139.138 158.182 124.358 1.00 108.26 ? 1512 TYR A CE1   1 
ATOM   1564  C CE2   . TYR A 1 1512 ? 140.417 159.201 126.105 1.00 108.26 ? 1512 TYR A CE2   1 
ATOM   1565  C CZ    . TYR A 1 1512 ? 139.409 158.353 125.700 1.00 108.26 ? 1512 TYR A CZ    1 
ATOM   1566  O OH    . TYR A 1 1512 ? 138.669 157.674 126.640 1.00 108.26 ? 1512 TYR A OH    1 
ATOM   1567  N N     . TYR A 1 1513 ? 145.035 160.354 121.503 1.00 108.98 ? 1513 TYR A N     1 
ATOM   1568  C CA    . TYR A 1 1513 ? 146.054 161.245 120.964 1.00 108.98 ? 1513 TYR A CA    1 
ATOM   1569  C C     . TYR A 1 1513 ? 146.224 161.092 119.460 1.00 108.98 ? 1513 TYR A C     1 
ATOM   1570  O O     . TYR A 1 1513 ? 146.743 162.002 118.807 1.00 108.98 ? 1513 TYR A O     1 
ATOM   1571  C CB    . TYR A 1 1513 ? 147.371 160.982 121.690 1.00 108.98 ? 1513 TYR A CB    1 
ATOM   1572  C CG    . TYR A 1 1513 ? 148.634 161.377 120.964 1.00 108.98 ? 1513 TYR A CG    1 
ATOM   1573  C CD1   . TYR A 1 1513 ? 149.035 162.704 120.900 1.00 108.98 ? 1513 TYR A CD1   1 
ATOM   1574  C CD2   . TYR A 1 1513 ? 149.449 160.417 120.381 1.00 108.98 ? 1513 TYR A CD2   1 
ATOM   1575  C CE1   . TYR A 1 1513 ? 150.197 163.066 120.250 1.00 108.98 ? 1513 TYR A CE1   1 
ATOM   1576  C CE2   . TYR A 1 1513 ? 150.614 160.769 119.731 1.00 108.98 ? 1513 TYR A CE2   1 
ATOM   1577  C CZ    . TYR A 1 1513 ? 150.984 162.096 119.669 1.00 108.98 ? 1513 TYR A CZ    1 
ATOM   1578  O OH    . TYR A 1 1513 ? 152.143 162.453 119.021 1.00 108.98 ? 1513 TYR A OH    1 
ATOM   1579  N N     . LYS A 1 1514 ? 145.798 159.960 118.896 1.00 104.51 ? 1514 LYS A N     1 
ATOM   1580  C CA    . LYS A 1 1514 ? 145.915 159.769 117.455 1.00 104.51 ? 1514 LYS A CA    1 
ATOM   1581  C C     . LYS A 1 1514 ? 145.070 160.779 116.688 1.00 104.51 ? 1514 LYS A C     1 
ATOM   1582  O O     . LYS A 1 1514 ? 145.395 161.122 115.545 1.00 104.51 ? 1514 LYS A O     1 
ATOM   1583  C CB    . LYS A 1 1514 ? 145.520 158.338 117.088 1.00 104.51 ? 1514 LYS A CB    1 
ATOM   1584  C CG    . LYS A 1 1514 ? 145.897 157.920 115.676 1.00 104.51 ? 1514 LYS A CG    1 
ATOM   1585  C CD    . LYS A 1 1514 ? 145.399 156.515 115.373 1.00 104.51 ? 1514 LYS A CD    1 
ATOM   1586  C CE    . LYS A 1 1514 ? 145.329 156.259 113.877 1.00 104.51 ? 1514 LYS A CE    1 
ATOM   1587  N NZ    . LYS A 1 1514 ? 144.250 155.291 113.533 1.00 104.51 ? 1514 LYS A NZ    1 
ATOM   1588  N N     . VAL A 1 1515 ? 143.987 161.266 117.297 1.00 106.81 ? 1515 VAL A N     1 
ATOM   1589  C CA    . VAL A 1 1515 ? 143.151 162.274 116.651 1.00 106.81 ? 1515 VAL A CA    1 
ATOM   1590  C C     . VAL A 1 1515 ? 143.890 163.606 116.558 1.00 106.81 ? 1515 VAL A C     1 
ATOM   1591  O O     . VAL A 1 1515 ? 143.908 164.252 115.504 1.00 106.81 ? 1515 VAL A O     1 
ATOM   1592  C CB    . VAL A 1 1515 ? 141.815 162.420 117.402 1.00 106.81 ? 1515 VAL A CB    1 
ATOM   1593  C CG1   . VAL A 1 1515 ? 140.963 163.510 116.770 1.00 106.81 ? 1515 VAL A CG1   1 
ATOM   1594  C CG2   . VAL A 1 1515 ? 141.070 161.094 117.422 1.00 106.81 ? 1515 VAL A CG2   1 
ATOM   1595  N N     . PHE A 1 1516 ? 144.511 164.033 117.657 1.00 109.36 ? 1516 PHE A N     1 
ATOM   1596  C CA    . PHE A 1 1516 ? 145.206 165.313 117.725 1.00 109.36 ? 1516 PHE A CA    1 
ATOM   1597  C C     . PHE A 1 1516 ? 146.716 165.175 117.583 1.00 109.36 ? 1516 PHE A C     1 
ATOM   1598  O O     . PHE A 1 1516 ? 147.455 166.021 118.102 1.00 109.36 ? 1516 PHE A O     1 
ATOM   1599  C CB    . PHE A 1 1516 ? 144.877 166.020 119.046 1.00 109.36 ? 1516 PHE A CB    1 
ATOM   1600  C CG    . PHE A 1 1516 ? 143.425 165.944 119.434 1.00 109.36 ? 1516 PHE A CG    1 
ATOM   1601  C CD1   . PHE A 1 1516 ? 142.509 166.853 118.928 1.00 109.36 ? 1516 PHE A CD1   1 
ATOM   1602  C CD2   . PHE A 1 1516 ? 142.979 164.969 120.312 1.00 109.36 ? 1516 PHE A CD2   1 
ATOM   1603  C CE1   . PHE A 1 1516 ? 141.175 166.786 119.287 1.00 109.36 ? 1516 PHE A CE1   1 
ATOM   1604  C CE2   . PHE A 1 1516 ? 141.646 164.898 120.674 1.00 109.36 ? 1516 PHE A CE2   1 
ATOM   1605  C CZ    . PHE A 1 1516 ? 140.743 165.808 120.161 1.00 109.36 ? 1516 PHE A CZ    1 
ATOM   1606  N N     . GLU A 1 1517 ? 147.184 164.124 116.907 1.00 111.00 ? 1517 GLU A N     1 
ATOM   1607  C CA    . GLU A 1 1517 ? 148.600 163.779 116.860 1.00 111.00 ? 1517 GLU A CA    1 
ATOM   1608  C C     . GLU A 1 1517 ? 149.456 164.875 116.230 1.00 111.00 ? 1517 GLU A C     1 
ATOM   1609  O O     . GLU A 1 1517 ? 150.474 165.291 116.797 1.00 111.00 ? 1517 GLU A O     1 
ATOM   1610  C CB    . GLU A 1 1517 ? 148.759 162.460 116.095 1.00 111.00 ? 1517 GLU A CB    1 
ATOM   1611  C CG    . GLU A 1 1517 ? 150.013 161.672 116.423 1.00 111.00 ? 1517 GLU A CG    1 
ATOM   1612  C CD    . GLU A 1 1517 ? 151.186 162.028 115.537 1.00 111.00 ? 1517 GLU A CD    1 
ATOM   1613  O OE1   . GLU A 1 1517 ? 150.959 162.547 114.424 1.00 111.00 ? 1517 GLU A OE1   1 
ATOM   1614  O OE2   . GLU A 1 1517 ? 152.335 161.774 115.952 1.00 111.00 ? 1517 GLU A OE2   1 
ATOM   1615  N N     . GLU A 1 1518 ? 149.057 165.346 115.047 1.00 111.40 ? 1518 GLU A N     1 
ATOM   1616  C CA    . GLU A 1 1518 ? 149.847 166.350 114.339 1.00 111.40 ? 1518 GLU A CA    1 
ATOM   1617  C C     . GLU A 1 1518 ? 149.881 167.672 115.101 1.00 111.40 ? 1518 GLU A C     1 
ATOM   1618  O O     . GLU A 1 1518 ? 150.927 168.328 115.190 1.00 111.40 ? 1518 GLU A O     1 
ATOM   1619  C CB    . GLU A 1 1518 ? 149.297 166.546 112.922 1.00 111.40 ? 1518 GLU A CB    1 
ATOM   1620  C CG    . GLU A 1 1518 ? 147.808 166.879 112.840 1.00 111.40 ? 1518 GLU A CG    1 
ATOM   1621  C CD    . GLU A 1 1518 ? 146.920 165.646 112.876 1.00 111.40 ? 1518 GLU A CD    1 
ATOM   1622  O OE1   . GLU A 1 1518 ? 147.062 164.831 113.812 1.00 111.40 ? 1518 GLU A OE1   1 
ATOM   1623  O OE2   . GLU A 1 1518 ? 146.078 165.493 111.967 1.00 111.40 ? 1518 GLU A OE2   1 
ATOM   1624  N N     . ASP A 1 1519 ? 148.738 168.078 115.659 1.00 110.51 ? 1519 ASP A N     1 
ATOM   1625  C CA    . ASP A 1 1519 ? 148.690 169.315 116.432 1.00 110.51 ? 1519 ASP A CA    1 
ATOM   1626  C C     . ASP A 1 1519 ? 149.571 169.214 117.671 1.00 110.51 ? 1519 ASP A C     1 
ATOM   1627  O O     . ASP A 1 1519 ? 150.292 170.160 118.017 1.00 110.51 ? 1519 ASP A O     1 
ATOM   1628  C CB    . ASP A 1 1519 ? 147.245 169.634 116.817 1.00 110.51 ? 1519 ASP A CB    1 
ATOM   1629  C CG    . ASP A 1 1519 ? 147.067 171.068 117.273 1.00 110.51 ? 1519 ASP A CG    1 
ATOM   1630  O OD1   . ASP A 1 1519 ? 148.018 171.864 117.124 1.00 110.51 ? 1519 ASP A OD1   1 
ATOM   1631  O OD2   . ASP A 1 1519 ? 145.976 171.401 117.780 1.00 110.51 ? 1519 ASP A OD2   1 
ATOM   1632  N N     . ALA A 1 1520 ? 149.533 168.063 118.348 1.00 112.65 ? 1520 ALA A N     1 
ATOM   1633  C CA    . ALA A 1 1520 ? 150.381 167.863 119.518 1.00 112.65 ? 1520 ALA A CA    1 
ATOM   1634  C C     . ALA A 1 1520 ? 151.855 167.900 119.138 1.00 112.65 ? 1520 ALA A C     1 
ATOM   1635  O O     . ALA A 1 1520 ? 152.679 168.468 119.861 1.00 112.65 ? 1520 ALA A O     1 
ATOM   1636  C CB    . ALA A 1 1520 ? 150.028 166.541 120.201 1.00 112.65 ? 1520 ALA A CB    1 
ATOM   1637  N N     . LEU A 1 1521 ? 152.206 167.293 118.001 1.00 109.68 ? 1521 LEU A N     1 
ATOM   1638  C CA    . LEU A 1 1521 ? 153.592 167.324 117.539 1.00 109.68 ? 1521 LEU A CA    1 
ATOM   1639  C C     . LEU A 1 1521 ? 154.050 168.751 117.263 1.00 109.68 ? 1521 LEU A C     1 
ATOM   1640  O O     . LEU A 1 1521 ? 155.154 169.152 117.651 1.00 109.68 ? 1521 LEU A O     1 
ATOM   1641  C CB    . LEU A 1 1521 ? 153.748 166.465 116.284 1.00 109.68 ? 1521 LEU A CB    1 
ATOM   1642  C CG    . LEU A 1 1521 ? 153.832 164.950 116.454 1.00 109.68 ? 1521 LEU A CG    1 
ATOM   1643  C CD1   . LEU A 1 1521 ? 154.030 164.291 115.100 1.00 109.68 ? 1521 LEU A CD1   1 
ATOM   1644  C CD2   . LEU A 1 1521 ? 154.954 164.574 117.408 1.00 109.68 ? 1521 LEU A CD2   1 
ATOM   1645  N N     . SER A 1 1522 ? 153.207 169.533 116.584 1.00 108.52 ? 1522 SER A N     1 
ATOM   1646  C CA    . SER A 1 1522 ? 153.563 170.913 116.273 1.00 108.52 ? 1522 SER A CA    1 
ATOM   1647  C C     . SER A 1 1522 ? 153.740 171.734 117.545 1.00 108.52 ? 1522 SER A C     1 
ATOM   1648  O O     . SER A 1 1522 ? 154.690 172.519 117.672 1.00 108.52 ? 1522 SER A O     1 
ATOM   1649  C CB    . SER A 1 1522 ? 152.497 171.536 115.370 1.00 108.52 ? 1522 SER A CB    1 
ATOM   1650  O OG    . SER A 1 1522 ? 152.873 172.839 114.960 1.00 108.52 ? 1522 SER A OG    1 
ATOM   1651  N N     . TRP A 1 1523 ? 152.835 171.553 118.510 1.00 111.07 ? 1523 TRP A N     1 
ATOM   1652  C CA    . TRP A 1 1523 ? 152.933 172.319 119.747 1.00 111.07 ? 1523 TRP A CA    1 
ATOM   1653  C C     . TRP A 1 1523 ? 154.145 171.888 120.566 1.00 111.07 ? 1523 TRP A C     1 
ATOM   1654  O O     . TRP A 1 1523 ? 154.785 172.718 121.221 1.00 111.07 ? 1523 TRP A O     1 
ATOM   1655  C CB    . TRP A 1 1523 ? 151.643 172.182 120.554 1.00 111.07 ? 1523 TRP A CB    1 
ATOM   1656  C CG    . TRP A 1 1523 ? 150.615 173.218 120.189 1.00 111.07 ? 1523 TRP A CG    1 
ATOM   1657  C CD1   . TRP A 1 1523 ? 149.342 172.989 119.756 1.00 111.07 ? 1523 TRP A CD1   1 
ATOM   1658  C CD2   . TRP A 1 1523 ? 150.782 174.644 120.203 1.00 111.07 ? 1523 TRP A CD2   1 
ATOM   1659  N NE1   . TRP A 1 1523 ? 148.702 174.180 119.510 1.00 111.07 ? 1523 TRP A NE1   1 
ATOM   1660  C CE2   . TRP A 1 1523 ? 149.565 175.211 119.776 1.00 111.07 ? 1523 TRP A CE2   1 
ATOM   1661  C CE3   . TRP A 1 1523 ? 151.840 175.495 120.542 1.00 111.07 ? 1523 TRP A CE3   1 
ATOM   1662  C CZ2   . TRP A 1 1523 ? 149.377 176.588 119.678 1.00 111.07 ? 1523 TRP A CZ2   1 
ATOM   1663  C CZ3   . TRP A 1 1523 ? 151.651 176.861 120.442 1.00 111.07 ? 1523 TRP A CZ3   1 
ATOM   1664  C CH2   . TRP A 1 1523 ? 150.429 177.394 120.014 1.00 111.07 ? 1523 TRP A CH2   1 
ATOM   1665  N N     . GLU A 1 1524 ? 154.486 170.597 120.530 1.00 109.94 ? 1524 GLU A N     1 
ATOM   1666  C CA    . GLU A 1 1524 ? 155.701 170.129 121.191 1.00 109.94 ? 1524 GLU A CA    1 
ATOM   1667  C C     . GLU A 1 1524 ? 156.943 170.742 120.561 1.00 109.94 ? 1524 GLU A C     1 
ATOM   1668  O O     . GLU A 1 1524 ? 157.885 171.122 121.263 1.00 109.94 ? 1524 GLU A O     1 
ATOM   1669  C CB    . GLU A 1 1524 ? 155.780 168.603 121.140 1.00 109.94 ? 1524 GLU A CB    1 
ATOM   1670  C CG    . GLU A 1 1524 ? 157.139 168.034 121.548 1.00 109.94 ? 1524 GLU A CG    1 
ATOM   1671  C CD    . GLU A 1 1524 ? 157.388 168.054 123.049 1.00 109.94 ? 1524 GLU A CD    1 
ATOM   1672  O OE1   . GLU A 1 1524 ? 156.579 168.644 123.796 1.00 109.94 ? 1524 GLU A OE1   1 
ATOM   1673  O OE2   . GLU A 1 1524 ? 158.404 167.474 123.485 1.00 109.94 ? 1524 GLU A OE2   1 
ATOM   1674  N N     . ASP A 1 1525 ? 156.969 170.827 119.230 1.00 109.22 ? 1525 ASP A N     1 
ATOM   1675  C CA    . ASP A 1 1525 ? 158.103 171.454 118.559 1.00 109.22 ? 1525 ASP A CA    1 
ATOM   1676  C C     . ASP A 1 1525 ? 158.222 172.921 118.955 1.00 109.22 ? 1525 ASP A C     1 
ATOM   1677  O O     . ASP A 1 1525 ? 159.322 173.422 119.225 1.00 109.22 ? 1525 ASP A O     1 
ATOM   1678  C CB    . ASP A 1 1525 ? 157.961 171.310 117.043 1.00 109.22 ? 1525 ASP A CB    1 
ATOM   1679  C CG    . ASP A 1 1525 ? 158.893 172.231 116.282 1.00 109.22 ? 1525 ASP A CG    1 
ATOM   1680  O OD1   . ASP A 1 1525 ? 160.122 172.128 116.478 1.00 109.22 ? 1525 ASP A OD1   1 
ATOM   1681  O OD2   . ASP A 1 1525 ? 158.397 173.058 115.488 1.00 109.22 ? 1525 ASP A OD2   1 
ATOM   1682  N N     . LYS A 1 1526 ? 157.087 173.622 119.008 1.00 106.49 ? 1526 LYS A N     1 
ATOM   1683  C CA    . LYS A 1 1526 ? 157.096 175.022 119.425 1.00 106.49 ? 1526 LYS A CA    1 
ATOM   1684  C C     . LYS A 1 1526 ? 157.609 175.167 120.855 1.00 106.49 ? 1526 LYS A C     1 
ATOM   1685  O O     . LYS A 1 1526 ? 158.415 176.057 121.156 1.00 106.49 ? 1526 LYS A O     1 
ATOM   1686  C CB    . LYS A 1 1526 ? 155.691 175.613 119.296 1.00 106.49 ? 1526 LYS A CB    1 
ATOM   1687  C CG    . LYS A 1 1526 ? 155.265 175.920 117.868 1.00 106.49 ? 1526 LYS A CG    1 
ATOM   1688  C CD    . LYS A 1 1526 ? 156.430 176.422 117.030 1.00 106.49 ? 1526 LYS A CD    1 
ATOM   1689  C CE    . LYS A 1 1526 ? 155.985 176.754 115.616 1.00 106.49 ? 1526 LYS A CE    1 
ATOM   1690  N NZ    . LYS A 1 1526 ? 155.007 177.877 115.594 1.00 106.49 ? 1526 LYS A NZ    1 
ATOM   1691  N N     . LEU A 1 1527 ? 157.152 174.290 121.753 1.00 104.68 ? 1527 LEU A N     1 
ATOM   1692  C CA    . LEU A 1 1527 ? 157.584 174.345 123.146 1.00 104.68 ? 1527 LEU A CA    1 
ATOM   1693  C C     . LEU A 1 1527 ? 159.072 174.048 123.280 1.00 104.68 ? 1527 LEU A C     1 
ATOM   1694  O O     . LEU A 1 1527 ? 159.770 174.670 124.087 1.00 104.68 ? 1527 LEU A O     1 
ATOM   1695  C CB    . LEU A 1 1527 ? 156.762 173.369 123.988 1.00 104.68 ? 1527 LEU A CB    1 
ATOM   1696  C CG    . LEU A 1 1527 ? 155.320 173.794 124.254 1.00 104.68 ? 1527 LEU A CG    1 
ATOM   1697  C CD1   . LEU A 1 1527 ? 154.544 172.677 124.921 1.00 104.68 ? 1527 LEU A CD1   1 
ATOM   1698  C CD2   . LEU A 1 1527 ? 155.308 175.042 125.112 1.00 104.68 ? 1527 LEU A CD2   1 
ATOM   1699  N N     . ASN A 1 1528 ? 159.570 173.081 122.508 1.00 105.03 ? 1528 ASN A N     1 
ATOM   1700  C CA    . ASN A 1 1528 ? 160.995 172.767 122.539 1.00 105.03 ? 1528 ASN A CA    1 
ATOM   1701  C C     . ASN A 1 1528 ? 161.821 173.951 122.054 1.00 105.03 ? 1528 ASN A C     1 
ATOM   1702  O O     . ASN A 1 1528 ? 162.869 174.271 122.629 1.00 105.03 ? 1528 ASN A O     1 
ATOM   1703  C CB    . ASN A 1 1528 ? 161.275 171.526 121.690 1.00 105.03 ? 1528 ASN A CB    1 
ATOM   1704  C CG    . ASN A 1 1528 ? 161.037 170.235 122.449 1.00 105.03 ? 1528 ASN A CG    1 
ATOM   1705  O OD1   . ASN A 1 1528 ? 161.584 170.028 123.532 1.00 105.03 ? 1528 ASN A OD1   1 
ATOM   1706  N ND2   . ASN A 1 1528 ? 160.215 169.359 121.883 1.00 105.03 ? 1528 ASN A ND2   1 
ATOM   1707  N N     . ARG A 1 1529 ? 161.358 174.617 120.993 1.00 107.97 ? 1529 ARG A N     1 
ATOM   1708  C CA    . ARG A 1 1529 ? 162.048 175.810 120.511 1.00 107.97 ? 1529 ARG A CA    1 
ATOM   1709  C C     . ARG A 1 1529 ? 162.060 176.902 121.575 1.00 107.97 ? 1529 ARG A C     1 
ATOM   1710  O O     . ARG A 1 1529 ? 163.087 177.553 121.805 1.00 107.97 ? 1529 ARG A O     1 
ATOM   1711  C CB    . ARG A 1 1529 ? 161.387 176.312 119.228 1.00 107.97 ? 1529 ARG A CB    1 
ATOM   1712  C CG    . ARG A 1 1529 ? 161.628 175.428 118.016 1.00 107.97 ? 1529 ARG A CG    1 
ATOM   1713  C CD    . ARG A 1 1529 ? 160.824 175.909 116.820 1.00 107.97 ? 1529 ARG A CD    1 
ATOM   1714  N NE    . ARG A 1 1529 ? 161.283 177.205 116.338 1.00 107.97 ? 1529 ARG A NE    1 
ATOM   1715  C CZ    . ARG A 1 1529 ? 160.541 178.046 115.632 1.00 107.97 ? 1529 ARG A CZ    1 
ATOM   1716  N NH1   . ARG A 1 1529 ? 159.292 177.759 115.305 1.00 107.97 ? 1529 ARG A NH1   1 
ATOM   1717  N NH2   . ARG A 1 1529 ? 161.065 179.206 115.245 1.00 107.97 ? 1529 ARG A NH2   1 
ATOM   1718  N N     . ILE A 1 1530 ? 160.922 177.108 122.243 1.00 106.85 ? 1530 ILE A N     1 
ATOM   1719  C CA    . ILE A 1 1530 ? 160.835 178.123 123.293 1.00 106.85 ? 1530 ILE A CA    1 
ATOM   1720  C C     . ILE A 1 1530 ? 161.800 177.799 124.429 1.00 106.85 ? 1530 ILE A C     1 
ATOM   1721  O O     . ILE A 1 1530 ? 162.520 178.674 124.932 1.00 106.85 ? 1530 ILE A O     1 
ATOM   1722  C CB    . ILE A 1 1530 ? 159.384 178.238 123.797 1.00 106.85 ? 1530 ILE A CB    1 
ATOM   1723  C CG1   . ILE A 1 1530 ? 158.517 178.974 122.773 1.00 106.85 ? 1530 ILE A CG1   1 
ATOM   1724  C CG2   . ILE A 1 1530 ? 159.328 178.919 125.154 1.00 106.85 ? 1530 ILE A CG2   1 
ATOM   1725  C CD1   . ILE A 1 1530 ? 157.033 178.749 122.960 1.00 106.85 ? 1530 ILE A CD1   1 
ATOM   1726  N N     . MET A 1 1531 ? 161.821 176.533 124.850 1.00 107.05 ? 1531 MET A N     1 
ATOM   1727  C CA    . MET A 1 1531 ? 162.694 176.104 125.938 1.00 107.05 ? 1531 MET A CA    1 
ATOM   1728  C C     . MET A 1 1531 ? 164.157 176.330 125.581 1.00 107.05 ? 1531 MET A C     1 
ATOM   1729  O O     . MET A 1 1531 ? 164.924 176.899 126.369 1.00 107.05 ? 1531 MET A O     1 
ATOM   1730  C CB    . MET A 1 1531 ? 162.431 174.627 126.242 1.00 107.05 ? 1531 MET A CB    1 
ATOM   1731  C CG    . MET A 1 1531 ? 163.144 174.049 127.458 1.00 107.05 ? 1531 MET A CG    1 
ATOM   1732  S SD    . MET A 1 1531 ? 162.596 174.763 129.020 1.00 107.05 ? 1531 MET A SD    1 
ATOM   1733  C CE    . MET A 1 1531 ? 164.013 174.452 130.066 1.00 107.05 ? 1531 MET A CE    1 
ATOM   1734  N N     . ALA A 1 1532 ? 164.557 175.899 124.380 1.00 104.80 ? 1532 ALA A N     1 
ATOM   1735  C CA    . ALA A 1 1532 ? 165.940 176.057 123.949 1.00 104.80 ? 1532 ALA A CA    1 
ATOM   1736  C C     . ALA A 1 1532 ? 166.329 177.519 123.790 1.00 104.80 ? 1532 ALA A C     1 
ATOM   1737  O O     . ALA A 1 1532 ? 167.486 177.870 124.048 1.00 104.80 ? 1532 ALA A O     1 
ATOM   1738  C CB    . ALA A 1 1532 ? 166.171 175.310 122.635 1.00 104.80 ? 1532 ALA A CB    1 
ATOM   1739  N N     . LEU A 1 1533 ? 165.398 178.377 123.371 1.00 108.66 ? 1533 LEU A N     1 
ATOM   1740  C CA    . LEU A 1 1533 ? 165.703 179.798 123.258 1.00 108.66 ? 1533 LEU A CA    1 
ATOM   1741  C C     . LEU A 1 1533 ? 165.907 180.429 124.631 1.00 108.66 ? 1533 LEU A C     1 
ATOM   1742  O O     . LEU A 1 1533 ? 166.910 181.111 124.874 1.00 108.66 ? 1533 LEU A O     1 
ATOM   1743  C CB    . LEU A 1 1533 ? 164.581 180.515 122.502 1.00 108.66 ? 1533 LEU A CB    1 
ATOM   1744  C CG    . LEU A 1 1533 ? 164.775 182.018 122.297 1.00 108.66 ? 1533 LEU A CG    1 
ATOM   1745  C CD1   . LEU A 1 1533 ? 165.896 182.275 121.304 1.00 108.66 ? 1533 LEU A CD1   1 
ATOM   1746  C CD2   . LEU A 1 1533 ? 163.484 182.687 121.847 1.00 108.66 ? 1533 LEU A CD2   1 
ATOM   1747  N N     . PHE A 1 1534 ? 164.975 180.188 125.556 1.00 111.30 ? 1534 PHE A N     1 
ATOM   1748  C CA    . PHE A 1 1534 ? 165.038 180.891 126.833 1.00 111.30 ? 1534 PHE A CA    1 
ATOM   1749  C C     . PHE A 1 1534 ? 166.139 180.348 127.735 1.00 111.30 ? 1534 PHE A C     1 
ATOM   1750  O O     . PHE A 1 1534 ? 166.678 181.098 128.561 1.00 111.30 ? 1534 PHE A O     1 
ATOM   1751  C CB    . PHE A 1 1534 ? 163.680 180.843 127.530 1.00 111.30 ? 1534 PHE A CB    1 
ATOM   1752  C CG    . PHE A 1 1534 ? 162.672 181.787 126.939 1.00 111.30 ? 1534 PHE A CG    1 
ATOM   1753  C CD1   . PHE A 1 1534 ? 162.875 183.156 126.994 1.00 111.30 ? 1534 PHE A CD1   1 
ATOM   1754  C CD2   . PHE A 1 1534 ? 161.529 181.311 126.324 1.00 111.30 ? 1534 PHE A CD2   1 
ATOM   1755  C CE1   . PHE A 1 1534 ? 161.956 184.031 126.450 1.00 111.30 ? 1534 PHE A CE1   1 
ATOM   1756  C CE2   . PHE A 1 1534 ? 160.604 182.182 125.778 1.00 111.30 ? 1534 PHE A CE2   1 
ATOM   1757  C CZ    . PHE A 1 1534 ? 160.819 183.544 125.841 1.00 111.30 ? 1534 PHE A CZ    1 
ATOM   1758  N N     . ASP A 1 1535 ? 166.512 179.071 127.581 1.00 106.45 ? 1535 ASP A N     1 
ATOM   1759  C CA    . ASP A 1 1535 ? 167.640 178.547 128.346 1.00 106.45 ? 1535 ASP A CA    1 
ATOM   1760  C C     . ASP A 1 1535 ? 168.917 179.316 128.041 1.00 106.45 ? 1535 ASP A C     1 
ATOM   1761  O O     . ASP A 1 1535 ? 169.693 179.634 128.949 1.00 106.45 ? 1535 ASP A O     1 
ATOM   1762  C CB    . ASP A 1 1535 ? 167.836 177.060 128.053 1.00 106.45 ? 1535 ASP A CB    1 
ATOM   1763  C CG    . ASP A 1 1535 ? 166.789 176.197 128.712 1.00 106.45 ? 1535 ASP A CG    1 
ATOM   1764  O OD1   . ASP A 1 1535 ? 166.287 176.597 129.783 1.00 106.45 ? 1535 ASP A OD1   1 
ATOM   1765  O OD2   . ASP A 1 1535 ? 166.471 175.122 128.162 1.00 106.45 ? 1535 ASP A OD2   1 
ATOM   1766  N N     . VAL A 1 1536 ? 169.159 179.614 126.765 1.00 104.11 ? 1536 VAL A N     1 
ATOM   1767  C CA    . VAL A 1 1536 ? 170.321 180.417 126.406 1.00 104.11 ? 1536 VAL A CA    1 
ATOM   1768  C C     . VAL A 1 1536 ? 170.105 181.874 126.799 1.00 104.11 ? 1536 VAL A C     1 
ATOM   1769  O O     . VAL A 1 1536 ? 171.047 182.563 127.214 1.00 104.11 ? 1536 VAL A O     1 
ATOM   1770  C CB    . VAL A 1 1536 ? 170.628 180.266 124.905 1.00 104.11 ? 1536 VAL A CB    1 
ATOM   1771  C CG1   . VAL A 1 1536 ? 171.942 180.949 124.560 1.00 104.11 ? 1536 VAL A CG1   1 
ATOM   1772  C CG2   . VAL A 1 1536 ? 170.667 178.795 124.519 1.00 104.11 ? 1536 VAL A CG2   1 
ATOM   1773  N N     . TRP A 1 1537 ? 168.870 182.370 126.666 1.00 109.93 ? 1537 TRP A N     1 
ATOM   1774  C CA    . TRP A 1 1537 ? 168.609 183.786 126.911 1.00 109.93 ? 1537 TRP A CA    1 
ATOM   1775  C C     . TRP A 1 1537 ? 168.886 184.162 128.362 1.00 109.93 ? 1537 TRP A C     1 
ATOM   1776  O O     . TRP A 1 1537 ? 169.448 185.227 128.640 1.00 109.93 ? 1537 TRP A O     1 
ATOM   1777  C CB    . TRP A 1 1537 ? 167.166 184.135 126.543 1.00 109.93 ? 1537 TRP A CB    1 
ATOM   1778  C CG    . TRP A 1 1537 ? 166.916 185.617 126.490 1.00 109.93 ? 1537 TRP A CG    1 
ATOM   1779  C CD1   . TRP A 1 1537 ? 166.734 186.457 127.550 1.00 109.93 ? 1537 TRP A CD1   1 
ATOM   1780  C CD2   . TRP A 1 1537 ? 166.794 186.427 125.315 1.00 109.93 ? 1537 TRP A CD2   1 
ATOM   1781  N NE1   . TRP A 1 1537 ? 166.525 187.740 127.110 1.00 109.93 ? 1537 TRP A NE1   1 
ATOM   1782  C CE2   . TRP A 1 1537 ? 166.553 187.749 125.741 1.00 109.93 ? 1537 TRP A CE2   1 
ATOM   1783  C CE3   . TRP A 1 1537 ? 166.870 186.165 123.944 1.00 109.93 ? 1537 TRP A CE3   1 
ATOM   1784  C CZ2   . TRP A 1 1537 ? 166.389 188.804 124.847 1.00 109.93 ? 1537 TRP A CZ2   1 
ATOM   1785  C CZ3   . TRP A 1 1537 ? 166.707 187.213 123.057 1.00 109.93 ? 1537 TRP A CZ3   1 
ATOM   1786  C CH2   . TRP A 1 1537 ? 166.468 188.516 123.513 1.00 109.93 ? 1537 TRP A CH2   1 
ATOM   1787  N N     . ILE A 1 1538 ? 168.479 183.308 129.305 1.00 106.13 ? 1538 ILE A N     1 
ATOM   1788  C CA    . ILE A 1 1538 ? 168.681 183.635 130.717 1.00 106.13 ? 1538 ILE A CA    1 
ATOM   1789  C C     . ILE A 1 1538 ? 170.170 183.680 131.050 1.00 106.13 ? 1538 ILE A C     1 
ATOM   1790  O O     . ILE A 1 1538 ? 170.632 184.563 131.787 1.00 106.13 ? 1538 ILE A O     1 
ATOM   1791  C CB    . ILE A 1 1538 ? 167.912 182.648 131.619 1.00 106.13 ? 1538 ILE A CB    1 
ATOM   1792  C CG1   . ILE A 1 1538 ? 168.084 183.026 133.092 1.00 106.13 ? 1538 ILE A CG1   1 
ATOM   1793  C CG2   . ILE A 1 1538 ? 168.341 181.209 131.368 1.00 106.13 ? 1538 ILE A CG2   1 
ATOM   1794  C CD1   . ILE A 1 1538 ? 167.135 182.304 134.022 1.00 106.13 ? 1538 ILE A CD1   1 
ATOM   1795  N N     . ASP A 1 1539 ? 170.944 182.737 130.508 1.00 100.66 ? 1539 ASP A N     1 
ATOM   1796  C CA    . ASP A 1 1539 ? 172.384 182.729 130.741 1.00 100.66 ? 1539 ASP A CA    1 
ATOM   1797  C C     . ASP A 1 1539 ? 173.037 183.969 130.142 1.00 100.66 ? 1539 ASP A C     1 
ATOM   1798  O O     . ASP A 1 1539 ? 173.921 184.579 130.757 1.00 100.66 ? 1539 ASP A O     1 
ATOM   1799  C CB    . ASP A 1 1539 ? 172.998 181.455 130.159 1.00 100.66 ? 1539 ASP A CB    1 
ATOM   1800  C CG    . ASP A 1 1539 ? 174.412 181.208 130.650 1.00 100.66 ? 1539 ASP A CG    1 
ATOM   1801  O OD1   . ASP A 1 1539 ? 174.906 181.998 131.483 1.00 100.66 ? 1539 ASP A OD1   1 
ATOM   1802  O OD2   . ASP A 1 1539 ? 175.032 180.220 130.203 1.00 100.66 ? 1539 ASP A OD2   1 
ATOM   1803  N N     . VAL A 1 1540 ? 172.613 184.356 128.935 1.00 101.38 ? 1540 VAL A N     1 
ATOM   1804  C CA    . VAL A 1 1540 ? 173.144 185.568 128.317 1.00 101.38 ? 1540 VAL A CA    1 
ATOM   1805  C C     . VAL A 1 1540 ? 172.814 186.789 129.161 1.00 101.38 ? 1540 VAL A C     1 
ATOM   1806  O O     . VAL A 1 1540 ? 173.661 187.671 129.351 1.00 101.38 ? 1540 VAL A O     1 
ATOM   1807  C CB    . VAL A 1 1540 ? 172.615 185.719 126.877 1.00 101.38 ? 1540 VAL A CB    1 
ATOM   1808  C CG1   . VAL A 1 1540 ? 173.052 187.049 126.288 1.00 101.38 ? 1540 VAL A CG1   1 
ATOM   1809  C CG2   . VAL A 1 1540 ? 173.117 184.580 126.011 1.00 101.38 ? 1540 VAL A CG2   1 
ATOM   1810  N N     . GLN A 1 1541 ? 171.590 186.861 129.686 1.00 103.45 ? 1541 GLN A N     1 
ATOM   1811  C CA    . GLN A 1 1541 ? 171.197 187.990 130.523 1.00 103.45 ? 1541 GLN A CA    1 
ATOM   1812  C C     . GLN A 1 1541 ? 172.051 188.066 131.784 1.00 103.45 ? 1541 GLN A C     1 
ATOM   1813  O O     . GLN A 1 1541 ? 172.532 189.142 132.161 1.00 103.45 ? 1541 GLN A O     1 
ATOM   1814  C CB    . GLN A 1 1541 ? 169.714 187.876 130.882 1.00 103.45 ? 1541 GLN A CB    1 
ATOM   1815  C CG    . GLN A 1 1541 ? 169.152 189.105 131.563 1.00 103.45 ? 1541 GLN A CG    1 
ATOM   1816  C CD    . GLN A 1 1541 ? 167.640 189.175 131.491 1.00 103.45 ? 1541 GLN A CD    1 
ATOM   1817  O OE1   . GLN A 1 1541 ? 166.945 188.899 132.469 1.00 103.45 ? 1541 GLN A OE1   1 
ATOM   1818  N NE2   . GLN A 1 1541 ? 167.122 189.534 130.324 1.00 103.45 ? 1541 GLN A NE2   1 
ATOM   1819  N N     . ARG A 1 1542 ? 172.252 186.927 132.451 1.00 101.32 ? 1542 ARG A N     1 
ATOM   1820  C CA    . ARG A 1 1542 ? 173.024 186.915 133.691 1.00 101.32 ? 1542 ARG A CA    1 
ATOM   1821  C C     . ARG A 1 1542 ? 174.481 187.287 133.437 1.00 101.32 ? 1542 ARG A C     1 
ATOM   1822  O O     . ARG A 1 1542 ? 175.065 188.116 134.148 1.00 101.32 ? 1542 ARG A O     1 
ATOM   1823  C CB    . ARG A 1 1542 ? 172.916 185.541 134.353 1.00 101.32 ? 1542 ARG A CB    1 
ATOM   1824  C CG    . ARG A 1 1542 ? 171.536 185.240 134.915 1.00 101.32 ? 1542 ARG A CG    1 
ATOM   1825  C CD    . ARG A 1 1542 ? 171.462 183.834 135.484 1.00 101.32 ? 1542 ARG A CD    1 
ATOM   1826  N NE    . ARG A 1 1542 ? 172.125 182.867 134.617 1.00 101.32 ? 1542 ARG A NE    1 
ATOM   1827  C CZ    . ARG A 1 1542 ? 172.014 181.551 134.737 1.00 101.32 ? 1542 ARG A CZ    1 
ATOM   1828  N NH1   . ARG A 1 1542 ? 171.269 181.004 135.684 1.00 101.32 ? 1542 ARG A NH1   1 
ATOM   1829  N NH2   . ARG A 1 1542 ? 172.663 180.765 133.884 1.00 101.32 ? 1542 ARG A NH2   1 
ATOM   1830  N N     . ARG A 1 1543 ? 175.086 186.688 132.411 1.00 93.37  ? 1543 ARG A N     1 
ATOM   1831  C CA    . ARG A 1 1543 ? 176.462 187.027 132.073 1.00 93.37  ? 1543 ARG A CA    1 
ATOM   1832  C C     . ARG A 1 1543 ? 176.568 188.487 131.653 1.00 93.37  ? 1543 ARG A C     1 
ATOM   1833  O O     . ARG A 1 1543 ? 177.534 189.178 131.999 1.00 93.37  ? 1543 ARG A O     1 
ATOM   1834  C CB    . ARG A 1 1543 ? 176.976 186.094 130.974 1.00 93.37  ? 1543 ARG A CB    1 
ATOM   1835  C CG    . ARG A 1 1543 ? 177.132 184.652 131.437 1.00 93.37  ? 1543 ARG A CG    1 
ATOM   1836  C CD    . ARG A 1 1543 ? 177.703 183.753 130.352 1.00 93.37  ? 1543 ARG A CD    1 
ATOM   1837  N NE    . ARG A 1 1543 ? 177.503 182.341 130.658 1.00 93.37  ? 1543 ARG A NE    1 
ATOM   1838  C CZ    . ARG A 1 1543 ? 177.948 181.341 129.909 1.00 93.37  ? 1543 ARG A CZ    1 
ATOM   1839  N NH1   . ARG A 1 1543 ? 178.627 181.562 128.795 1.00 93.37  ? 1543 ARG A NH1   1 
ATOM   1840  N NH2   . ARG A 1 1543 ? 177.712 180.089 130.290 1.00 93.37  ? 1543 ARG A NH2   1 
ATOM   1841  N N     . TRP A 1 1544 ? 175.572 188.979 130.912 1.00 93.39  ? 1544 TRP A N     1 
ATOM   1842  C CA    . TRP A 1 1544 ? 175.632 190.359 130.445 1.00 93.39  ? 1544 TRP A CA    1 
ATOM   1843  C C     . TRP A 1 1544 ? 175.551 191.338 131.608 1.00 93.39  ? 1544 TRP A C     1 
ATOM   1844  O O     . TRP A 1 1544 ? 176.274 192.335 131.635 1.00 93.39  ? 1544 TRP A O     1 
ATOM   1845  C CB    . TRP A 1 1544 ? 174.522 190.653 129.437 1.00 93.39  ? 1544 TRP A CB    1 
ATOM   1846  C CG    . TRP A 1 1544 ? 174.498 192.102 129.049 1.00 93.39  ? 1544 TRP A CG    1 
ATOM   1847  C CD1   . TRP A 1 1544 ? 175.310 192.716 128.141 1.00 93.39  ? 1544 TRP A CD1   1 
ATOM   1848  C CD2   . TRP A 1 1544 ? 173.641 193.124 129.574 1.00 93.39  ? 1544 TRP A CD2   1 
ATOM   1849  N NE1   . TRP A 1 1544 ? 175.005 194.052 128.059 1.00 93.39  ? 1544 TRP A NE1   1 
ATOM   1850  C CE2   . TRP A 1 1544 ? 173.984 194.328 128.929 1.00 93.39  ? 1544 TRP A CE2   1 
ATOM   1851  C CE3   . TRP A 1 1544 ? 172.613 193.137 130.520 1.00 93.39  ? 1544 TRP A CE3   1 
ATOM   1852  C CZ2   . TRP A 1 1544 ? 173.337 195.531 129.199 1.00 93.39  ? 1544 TRP A CZ2   1 
ATOM   1853  C CZ3   . TRP A 1 1544 ? 171.973 194.333 130.789 1.00 93.39  ? 1544 TRP A CZ3   1 
ATOM   1854  C CH2   . TRP A 1 1544 ? 172.337 195.513 130.131 1.00 93.39  ? 1544 TRP A CH2   1 
ATOM   1855  N N     . VAL A 1 1545 ? 174.667 191.082 132.576 1.00 90.47  ? 1545 VAL A N     1 
ATOM   1856  C CA    . VAL A 1 1545 ? 174.556 191.996 133.714 1.00 90.47  ? 1545 VAL A CA    1 
ATOM   1857  C C     . VAL A 1 1545 ? 175.813 191.927 134.576 1.00 90.47  ? 1545 VAL A C     1 
ATOM   1858  O O     . VAL A 1 1545 ? 176.276 192.945 135.105 1.00 90.47  ? 1545 VAL A O     1 
ATOM   1859  C CB    . VAL A 1 1545 ? 173.276 191.728 134.532 1.00 90.47  ? 1545 VAL A CB    1 
ATOM   1860  C CG1   . VAL A 1 1545 ? 172.036 191.956 133.681 1.00 90.47  ? 1545 VAL A CG1   1 
ATOM   1861  C CG2   . VAL A 1 1545 ? 173.266 190.337 135.136 1.00 90.47  ? 1545 VAL A CG2   1 
ATOM   1862  N N     . TYR A 1 1546 ? 176.392 190.730 134.725 1.00 83.26  ? 1546 TYR A N     1 
ATOM   1863  C CA    . TYR A 1 1546 ? 177.648 190.620 135.464 1.00 83.26  ? 1546 TYR A CA    1 
ATOM   1864  C C     . TYR A 1 1546 ? 178.750 191.448 134.806 1.00 83.26  ? 1546 TYR A C     1 
ATOM   1865  O O     . TYR A 1 1546 ? 179.442 192.234 135.469 1.00 83.26  ? 1546 TYR A O     1 
ATOM   1866  C CB    . TYR A 1 1546 ? 178.064 189.151 135.570 1.00 83.26  ? 1546 TYR A CB    1 
ATOM   1867  C CG    . TYR A 1 1546 ? 179.271 188.917 136.451 1.00 83.26  ? 1546 TYR A CG    1 
ATOM   1868  C CD1   . TYR A 1 1546 ? 179.442 189.630 137.631 1.00 83.26  ? 1546 TYR A CD1   1 
ATOM   1869  C CD2   . TYR A 1 1546 ? 180.241 187.986 136.103 1.00 83.26  ? 1546 TYR A CD2   1 
ATOM   1870  C CE1   . TYR A 1 1546 ? 180.547 189.421 138.439 1.00 83.26  ? 1546 TYR A CE1   1 
ATOM   1871  C CE2   . TYR A 1 1546 ? 181.348 187.770 136.905 1.00 83.26  ? 1546 TYR A CE2   1 
ATOM   1872  C CZ    . TYR A 1 1546 ? 181.496 188.489 138.071 1.00 83.26  ? 1546 TYR A CZ    1 
ATOM   1873  O OH    . TYR A 1 1546 ? 182.598 188.273 138.867 1.00 83.26  ? 1546 TYR A OH    1 
ATOM   1874  N N     . LEU A 1 1547 ? 178.909 191.303 133.489 1.00 85.04  ? 1547 LEU A N     1 
ATOM   1875  C CA    . LEU A 1 1547 ? 179.953 192.050 132.793 1.00 85.04  ? 1547 LEU A CA    1 
ATOM   1876  C C     . LEU A 1 1547 ? 179.638 193.540 132.742 1.00 85.04  ? 1547 LEU A C     1 
ATOM   1877  O O     . LEU A 1 1547 ? 180.550 194.370 132.694 1.00 85.04  ? 1547 LEU A O     1 
ATOM   1878  C CB    . LEU A 1 1547 ? 180.152 191.495 131.386 1.00 85.04  ? 1547 LEU A CB    1 
ATOM   1879  C CG    . LEU A 1 1547 ? 181.183 190.380 131.222 1.00 85.04  ? 1547 LEU A CG    1 
ATOM   1880  C CD1   . LEU A 1 1547 ? 180.714 189.073 131.839 1.00 85.04  ? 1547 LEU A CD1   1 
ATOM   1881  C CD2   . LEU A 1 1547 ? 181.482 190.205 129.752 1.00 85.04  ? 1547 LEU A CD2   1 
ATOM   1882  N N     . GLU A 1 1548 ? 178.354 193.898 132.735 1.00 87.70  ? 1548 GLU A N     1 
ATOM   1883  C CA    . GLU A 1 1548 ? 177.973 195.305 132.768 1.00 87.70  ? 1548 GLU A CA    1 
ATOM   1884  C C     . GLU A 1 1548 ? 178.355 195.936 134.099 1.00 87.70  ? 1548 GLU A C     1 
ATOM   1885  O O     . GLU A 1 1548 ? 178.871 197.058 134.145 1.00 87.70  ? 1548 GLU A O     1 
ATOM   1886  C CB    . GLU A 1 1548 ? 176.472 195.441 132.506 1.00 87.70  ? 1548 GLU A CB    1 
ATOM   1887  C CG    . GLU A 1 1548 ? 175.871 196.780 132.898 1.00 87.70  ? 1548 GLU A CG    1 
ATOM   1888  C CD    . GLU A 1 1548 ? 176.535 197.957 132.211 1.00 87.70  ? 1548 GLU A CD    1 
ATOM   1889  O OE1   . GLU A 1 1548 ? 177.053 197.786 131.087 1.00 87.70  ? 1548 GLU A OE1   1 
ATOM   1890  O OE2   . GLU A 1 1548 ? 176.536 199.057 132.799 1.00 87.70  ? 1548 GLU A OE2   1 
ATOM   1891  N N     . GLY A 1 1549 ? 178.109 195.223 135.198 1.00 83.32  ? 1549 GLY A N     1 
ATOM   1892  C CA    . GLY A 1 1549 ? 178.573 195.683 136.493 1.00 83.32  ? 1549 GLY A CA    1 
ATOM   1893  C C     . GLY A 1 1549 ? 180.080 195.764 136.611 1.00 83.32  ? 1549 GLY A C     1 
ATOM   1894  O O     . GLY A 1 1549 ? 180.586 196.690 137.256 1.00 83.32  ? 1549 GLY A O     1 
ATOM   1895  N N     . ILE A 1 1550 ? 180.806 194.825 136.006 1.00 80.06  ? 1550 ILE A N     1 
ATOM   1896  C CA    . ILE A 1 1550 ? 182.265 194.843 136.059 1.00 80.06  ? 1550 ILE A CA    1 
ATOM   1897  C C     . ILE A 1 1550 ? 182.831 195.995 135.235 1.00 80.06  ? 1550 ILE A C     1 
ATOM   1898  O O     . ILE A 1 1550 ? 183.735 196.708 135.686 1.00 80.06  ? 1550 ILE A O     1 
ATOM   1899  C CB    . ILE A 1 1550 ? 182.853 193.502 135.582 1.00 80.06  ? 1550 ILE A CB    1 
ATOM   1900  C CG1   . ILE A 1 1550 ? 182.420 192.364 136.506 1.00 80.06  ? 1550 ILE A CG1   1 
ATOM   1901  C CG2   . ILE A 1 1550 ? 184.370 193.577 135.507 1.00 80.06  ? 1550 ILE A CG2   1 
ATOM   1902  C CD1   . ILE A 1 1550 ? 182.615 190.995 135.902 1.00 80.06  ? 1550 ILE A CD1   1 
ATOM   1903  N N     . PHE A 1 1551 ? 182.298 196.195 134.030 1.00 85.77  ? 1551 PHE A N     1 
ATOM   1904  C CA    . PHE A 1 1551 ? 182.938 197.018 133.012 1.00 85.77  ? 1551 PHE A CA    1 
ATOM   1905  C C     . PHE A 1 1551 ? 182.479 198.471 133.007 1.00 85.77  ? 1551 PHE A C     1 
ATOM   1906  O O     . PHE A 1 1551 ? 183.045 199.276 132.263 1.00 85.77  ? 1551 PHE A O     1 
ATOM   1907  C CB    . PHE A 1 1551 ? 182.695 196.413 131.625 1.00 85.77  ? 1551 PHE A CB    1 
ATOM   1908  C CG    . PHE A 1 1551 ? 183.693 195.361 131.238 1.00 85.77  ? 1551 PHE A CG    1 
ATOM   1909  C CD1   . PHE A 1 1551 ? 184.994 195.706 130.917 1.00 85.77  ? 1551 PHE A CD1   1 
ATOM   1910  C CD2   . PHE A 1 1551 ? 183.325 194.028 131.183 1.00 85.77  ? 1551 PHE A CD2   1 
ATOM   1911  C CE1   . PHE A 1 1551 ? 185.913 194.739 130.558 1.00 85.77  ? 1551 PHE A CE1   1 
ATOM   1912  C CE2   . PHE A 1 1551 ? 184.238 193.057 130.823 1.00 85.77  ? 1551 PHE A CE2   1 
ATOM   1913  C CZ    . PHE A 1 1551 ? 185.534 193.413 130.511 1.00 85.77  ? 1551 PHE A CZ    1 
ATOM   1914  N N     . THR A 1 1552 ? 181.477 198.832 133.807 1.00 88.16  ? 1552 THR A N     1 
ATOM   1915  C CA    . THR A 1 1552 ? 180.967 200.199 133.808 1.00 88.16  ? 1552 THR A CA    1 
ATOM   1916  C C     . THR A 1 1552 ? 181.016 200.885 135.163 1.00 88.16  ? 1552 THR A C     1 
ATOM   1917  O O     . THR A 1 1552 ? 180.958 202.120 135.203 1.00 88.16  ? 1552 THR A O     1 
ATOM   1918  C CB    . THR A 1 1552 ? 179.522 200.240 133.290 1.00 88.16  ? 1552 THR A CB    1 
ATOM   1919  O OG1   . THR A 1 1552 ? 178.731 199.271 133.988 1.00 88.16  ? 1552 THR A OG1   1 
ATOM   1920  C CG2   . THR A 1 1552 ? 179.485 199.943 131.798 1.00 88.16  ? 1552 THR A CG2   1 
ATOM   1921  N N     . GLY A 1 1553 ? 181.120 200.144 136.268 1.00 85.38  ? 1553 GLY A N     1 
ATOM   1922  C CA    . GLY A 1 1553 ? 181.279 200.777 137.564 1.00 85.38  ? 1553 GLY A CA    1 
ATOM   1923  C C     . GLY A 1 1553 ? 182.669 201.325 137.804 1.00 85.38  ? 1553 GLY A C     1 
ATOM   1924  O O     . GLY A 1 1553 ? 182.890 202.011 138.807 1.00 85.38  ? 1553 GLY A O     1 
ATOM   1925  N N     . SER A 1 1554 ? 183.607 201.038 136.905 1.00 85.05  ? 1554 SER A N     1 
ATOM   1926  C CA    . SER A 1 1554 ? 184.985 201.484 137.022 1.00 85.05  ? 1554 SER A CA    1 
ATOM   1927  C C     . SER A 1 1554 ? 185.450 202.132 135.726 1.00 85.05  ? 1554 SER A C     1 
ATOM   1928  O O     . SER A 1 1554 ? 184.846 201.946 134.665 1.00 85.05  ? 1554 SER A O     1 
ATOM   1929  C CB    . SER A 1 1554 ? 185.918 200.326 137.366 1.00 85.05  ? 1554 SER A CB    1 
ATOM   1930  O OG    . SER A 1 1554 ? 187.259 200.772 137.374 1.00 85.05  ? 1554 SER A OG    1 
ATOM   1931  N N     . ALA A 1 1555 ? 186.539 202.898 135.827 1.00 87.07  ? 1555 ALA A N     1 
ATOM   1932  C CA    . ALA A 1 1555 ? 187.139 203.551 134.674 1.00 87.07  ? 1555 ALA A CA    1 
ATOM   1933  C C     . ALA A 1 1555 ? 188.482 202.966 134.266 1.00 87.07  ? 1555 ALA A C     1 
ATOM   1934  O O     . ALA A 1 1555 ? 188.851 203.076 133.093 1.00 87.07  ? 1555 ALA A O     1 
ATOM   1935  C CB    . ALA A 1 1555 ? 187.316 205.053 134.943 1.00 87.07  ? 1555 ALA A CB    1 
ATOM   1936  N N     . ASP A 1 1556 ? 189.215 202.348 135.189 1.00 81.50  ? 1556 ASP A N     1 
ATOM   1937  C CA    . ASP A 1 1556 ? 190.528 201.789 134.894 1.00 81.50  ? 1556 ASP A CA    1 
ATOM   1938  C C     . ASP A 1 1556 ? 190.453 200.404 134.263 1.00 81.50  ? 1556 ASP A C     1 
ATOM   1939  O O     . ASP A 1 1556 ? 191.487 199.865 133.856 1.00 81.50  ? 1556 ASP A O     1 
ATOM   1940  C CB    . ASP A 1 1556 ? 191.372 201.739 136.175 1.00 81.50  ? 1556 ASP A CB    1 
ATOM   1941  C CG    . ASP A 1 1556 ? 192.828 201.408 135.906 1.00 81.50  ? 1556 ASP A CG    1 
ATOM   1942  O OD1   . ASP A 1 1556 ? 193.538 202.263 135.335 1.00 81.50  ? 1556 ASP A OD1   1 
ATOM   1943  O OD2   . ASP A 1 1556 ? 193.264 200.294 136.265 1.00 81.50  ? 1556 ASP A OD2   1 
ATOM   1944  N N     . ILE A 1 1557 ? 189.257 199.821 134.163 1.00 81.43  ? 1557 ILE A N     1 
ATOM   1945  C CA    . ILE A 1 1557 ? 189.127 198.492 133.573 1.00 81.43  ? 1557 ILE A CA    1 
ATOM   1946  C C     . ILE A 1 1557 ? 189.469 198.517 132.087 1.00 81.43  ? 1557 ILE A C     1 
ATOM   1947  O O     . ILE A 1 1557 ? 189.884 197.497 131.523 1.00 81.43  ? 1557 ILE A O     1 
ATOM   1948  C CB    . ILE A 1 1557 ? 187.713 197.935 133.825 1.00 81.43  ? 1557 ILE A CB    1 
ATOM   1949  C CG1   . ILE A 1 1557 ? 187.670 196.429 133.558 1.00 81.43  ? 1557 ILE A CG1   1 
ATOM   1950  C CG2   . ILE A 1 1557 ? 186.681 198.666 132.977 1.00 81.43  ? 1557 ILE A CG2   1 
ATOM   1951  C CD1   . ILE A 1 1557 ? 188.486 195.614 134.536 1.00 81.43  ? 1557 ILE A CD1   1 
ATOM   1952  N N     . LYS A 1 1558 ? 189.312 199.668 131.429 1.00 82.54  ? 1558 LYS A N     1 
ATOM   1953  C CA    . LYS A 1 1558 ? 189.565 199.733 129.993 1.00 82.54  ? 1558 LYS A CA    1 
ATOM   1954  C C     . LYS A 1 1558 ? 191.054 199.631 129.683 1.00 82.54  ? 1558 LYS A C     1 
ATOM   1955  O O     . LYS A 1 1558 ? 191.442 199.093 128.640 1.00 82.54  ? 1558 LYS A O     1 
ATOM   1956  C CB    . LYS A 1 1558 ? 188.971 201.018 129.409 1.00 82.54  ? 1558 LYS A CB    1 
ATOM   1957  C CG    . LYS A 1 1558 ? 189.816 202.270 129.601 1.00 82.54  ? 1558 LYS A CG    1 
ATOM   1958  C CD    . LYS A 1 1558 ? 188.950 203.513 129.721 1.00 82.54  ? 1558 LYS A CD    1 
ATOM   1959  C CE    . LYS A 1 1558 ? 189.684 204.629 130.448 1.00 82.54  ? 1558 LYS A CE    1 
ATOM   1960  N NZ    . LYS A 1 1558 ? 188.833 205.839 130.615 1.00 82.54  ? 1558 LYS A NZ    1 
ATOM   1961  N N     . HIS A 1 1559 ? 191.907 200.146 130.572 1.00 82.51  ? 1559 HIS A N     1 
ATOM   1962  C CA    . HIS A 1 1559 ? 193.344 200.091 130.325 1.00 82.51  ? 1559 HIS A CA    1 
ATOM   1963  C C     . HIS A 1 1559 ? 193.904 198.702 130.602 1.00 82.51  ? 1559 HIS A C     1 
ATOM   1964  O O     . HIS A 1 1559 ? 194.830 198.251 129.918 1.00 82.51  ? 1559 HIS A O     1 
ATOM   1965  C CB    . HIS A 1 1559 ? 194.063 201.141 131.171 1.00 82.51  ? 1559 HIS A CB    1 
ATOM   1966  C CG    . HIS A 1 1559 ? 194.191 202.473 130.499 1.00 82.51  ? 1559 HIS A CG    1 
ATOM   1967  N ND1   . HIS A 1 1559 ? 195.307 203.270 130.632 1.00 82.51  ? 1559 HIS A ND1   1 
ATOM   1968  C CD2   . HIS A 1 1559 ? 193.343 203.146 129.685 1.00 82.51  ? 1559 HIS A CD2   1 
ATOM   1969  C CE1   . HIS A 1 1559 ? 195.141 204.377 129.931 1.00 82.51  ? 1559 HIS A CE1   1 
ATOM   1970  N NE2   . HIS A 1 1559 ? 193.957 204.327 129.347 1.00 82.51  ? 1559 HIS A NE2   1 
ATOM   1971  N N     . LEU A 1 1560 ? 193.356 198.009 131.602 1.00 76.54  ? 1560 LEU A N     1 
ATOM   1972  C CA    . LEU A 1 1560 ? 193.879 196.695 131.962 1.00 76.54  ? 1560 LEU A CA    1 
ATOM   1973  C C     . LEU A 1 1560 ? 193.480 195.636 130.943 1.00 76.54  ? 1560 LEU A C     1 
ATOM   1974  O O     . LEU A 1 1560 ? 194.291 194.775 130.584 1.00 76.54  ? 1560 LEU A O     1 
ATOM   1975  C CB    . LEU A 1 1560 ? 193.395 196.306 133.357 1.00 76.54  ? 1560 LEU A CB    1 
ATOM   1976  C CG    . LEU A 1 1560 ? 193.646 197.325 134.469 1.00 76.54  ? 1560 LEU A CG    1 
ATOM   1977  C CD1   . LEU A 1 1560 ? 192.919 196.917 135.742 1.00 76.54  ? 1560 LEU A CD1   1 
ATOM   1978  C CD2   . LEU A 1 1560 ? 195.139 197.481 134.724 1.00 76.54  ? 1560 LEU A CD2   1 
ATOM   1979  N N     . LEU A 1 1561 ? 192.239 195.680 130.464 1.00 83.76  ? 1561 LEU A N     1 
ATOM   1980  C CA    . LEU A 1 1561 ? 191.707 194.685 129.534 1.00 83.76  ? 1561 LEU A CA    1 
ATOM   1981  C C     . LEU A 1 1561 ? 191.093 195.405 128.341 1.00 83.76  ? 1561 LEU A C     1 
ATOM   1982  O O     . LEU A 1 1561 ? 189.867 195.446 128.189 1.00 83.76  ? 1561 LEU A O     1 
ATOM   1983  C CB    . LEU A 1 1561 ? 190.674 193.796 130.227 1.00 83.76  ? 1561 LEU A CB    1 
ATOM   1984  C CG    . LEU A 1 1561 ? 191.175 192.959 131.404 1.00 83.76  ? 1561 LEU A CG    1 
ATOM   1985  C CD1   . LEU A 1 1561 ? 190.073 192.775 132.436 1.00 83.76  ? 1561 LEU A CD1   1 
ATOM   1986  C CD2   . LEU A 1 1561 ? 191.693 191.614 130.930 1.00 83.76  ? 1561 LEU A CD2   1 
ATOM   1987  N N     . PRO A 1 1562 ? 191.922 195.981 127.466 1.00 87.64  ? 1562 PRO A N     1 
ATOM   1988  C CA    . PRO A 1 1562 ? 191.361 196.819 126.392 1.00 87.64  ? 1562 PRO A CA    1 
ATOM   1989  C C     . PRO A 1 1562 ? 190.677 196.029 125.290 1.00 87.64  ? 1562 PRO A C     1 
ATOM   1990  O O     . PRO A 1 1562 ? 189.588 196.413 124.845 1.00 87.64  ? 1562 PRO A O     1 
ATOM   1991  C CB    . PRO A 1 1562 ? 192.588 197.578 125.871 1.00 87.64  ? 1562 PRO A CB    1 
ATOM   1992  C CG    . PRO A 1 1562 ? 193.735 196.676 126.169 1.00 87.64  ? 1562 PRO A CG    1 
ATOM   1993  C CD    . PRO A 1 1562 ? 193.394 195.939 127.432 1.00 87.64  ? 1562 PRO A CD    1 
ATOM   1994  N N     . VAL A 1 1563 ? 191.285 194.940 124.819 1.00 92.29  ? 1563 VAL A N     1 
ATOM   1995  C CA    . VAL A 1 1563 ? 190.704 194.220 123.689 1.00 92.29  ? 1563 VAL A CA    1 
ATOM   1996  C C     . VAL A 1 1563 ? 189.440 193.484 124.129 1.00 92.29  ? 1563 VAL A C     1 
ATOM   1997  O O     . VAL A 1 1563 ? 188.445 193.420 123.394 1.00 92.29  ? 1563 VAL A O     1 
ATOM   1998  C CB    . VAL A 1 1563 ? 191.745 193.279 123.052 1.00 92.29  ? 1563 VAL A CB    1 
ATOM   1999  C CG1   . VAL A 1 1563 ? 192.184 192.179 124.012 1.00 92.29  ? 1563 VAL A CG1   1 
ATOM   2000  C CG2   . VAL A 1 1563 ? 191.243 192.734 121.728 1.00 92.29  ? 1563 VAL A CG2   1 
ATOM   2001  N N     . GLU A 1 1564 ? 189.453 192.935 125.350 1.00 91.92  ? 1564 GLU A N     1 
ATOM   2002  C CA    . GLU A 1 1564 ? 188.237 192.357 125.911 1.00 91.92  ? 1564 GLU A CA    1 
ATOM   2003  C C     . GLU A 1 1564 ? 187.183 193.425 126.161 1.00 91.92  ? 1564 GLU A C     1 
ATOM   2004  O O     . GLU A 1 1564 ? 185.987 193.157 126.020 1.00 91.92  ? 1564 GLU A O     1 
ATOM   2005  C CB    . GLU A 1 1564 ? 188.543 191.604 127.207 1.00 91.92  ? 1564 GLU A CB    1 
ATOM   2006  C CG    . GLU A 1 1564 ? 189.622 190.536 127.084 1.00 91.92  ? 1564 GLU A CG    1 
ATOM   2007  C CD    . GLU A 1 1564 ? 190.997 191.026 127.515 1.00 91.92  ? 1564 GLU A CD    1 
ATOM   2008  O OE1   . GLU A 1 1564 ? 191.294 192.226 127.336 1.00 91.92  ? 1564 GLU A OE1   1 
ATOM   2009  O OE2   . GLU A 1 1564 ? 191.790 190.205 128.021 1.00 91.92  ? 1564 GLU A OE2   1 
ATOM   2010  N N     . THR A 1 1565 ? 187.602 194.638 126.527 1.00 91.77  ? 1565 THR A N     1 
ATOM   2011  C CA    . THR A 1 1565 ? 186.646 195.734 126.647 1.00 91.77  ? 1565 THR A CA    1 
ATOM   2012  C C     . THR A 1 1565 ? 185.978 196.012 125.307 1.00 91.77  ? 1565 THR A C     1 
ATOM   2013  O O     . THR A 1 1565 ? 184.766 196.232 125.239 1.00 91.77  ? 1565 THR A O     1 
ATOM   2014  C CB    . THR A 1 1565 ? 187.341 196.991 127.175 1.00 91.77  ? 1565 THR A CB    1 
ATOM   2015  O OG1   . THR A 1 1565 ? 187.849 196.741 128.492 1.00 91.77  ? 1565 THR A OG1   1 
ATOM   2016  C CG2   . THR A 1 1565 ? 186.365 198.160 127.236 1.00 91.77  ? 1565 THR A CG2   1 
ATOM   2017  N N     . GLN A 1 1566 ? 186.759 195.997 124.224 1.00 97.32  ? 1566 GLN A N     1 
ATOM   2018  C CA    . GLN A 1 1566 ? 186.190 196.212 122.895 1.00 97.32  ? 1566 GLN A CA    1 
ATOM   2019  C C     . GLN A 1 1566 ? 185.224 195.095 122.510 1.00 97.32  ? 1566 GLN A C     1 
ATOM   2020  O O     . GLN A 1 1566 ? 184.142 195.357 121.960 1.00 97.32  ? 1566 GLN A O     1 
ATOM   2021  C CB    . GLN A 1 1566 ? 187.310 196.328 121.863 1.00 97.32  ? 1566 GLN A CB    1 
ATOM   2022  C CG    . GLN A 1 1566 ? 188.210 197.536 122.064 1.00 97.32  ? 1566 GLN A CG    1 
ATOM   2023  C CD    . GLN A 1 1566 ? 189.366 197.567 121.086 1.00 97.32  ? 1566 GLN A CD    1 
ATOM   2024  O OE1   . GLN A 1 1566 ? 189.547 196.645 120.292 1.00 97.32  ? 1566 GLN A OE1   1 
ATOM   2025  N NE2   . GLN A 1 1566 ? 190.155 198.634 121.137 1.00 97.32  ? 1566 GLN A NE2   1 
ATOM   2026  N N     . ARG A 1 1567 ? 185.600 193.840 122.782 1.00 92.57  ? 1567 ARG A N     1 
ATOM   2027  C CA    . ARG A 1 1567 ? 184.700 192.732 122.467 1.00 92.57  ? 1567 ARG A CA    1 
ATOM   2028  C C     . ARG A 1 1567 ? 183.409 192.836 123.267 1.00 92.57  ? 1567 ARG A C     1 
ATOM   2029  O O     . ARG A 1 1567 ? 182.320 192.592 122.737 1.00 92.57  ? 1567 ARG A O     1 
ATOM   2030  C CB    . ARG A 1 1567 ? 185.361 191.377 122.727 1.00 92.57  ? 1567 ARG A CB    1 
ATOM   2031  C CG    . ARG A 1 1567 ? 186.513 191.014 121.812 1.00 92.57  ? 1567 ARG A CG    1 
ATOM   2032  C CD    . ARG A 1 1567 ? 187.061 189.638 122.184 1.00 92.57  ? 1567 ARG A CD    1 
ATOM   2033  N NE    . ARG A 1 1567 ? 188.160 189.225 121.322 1.00 92.57  ? 1567 ARG A NE    1 
ATOM   2034  C CZ    . ARG A 1 1567 ? 189.439 189.468 121.576 1.00 92.57  ? 1567 ARG A CZ    1 
ATOM   2035  N NH1   . ARG A 1 1567 ? 189.826 190.022 122.714 1.00 92.57  ? 1567 ARG A NH1   1 
ATOM   2036  N NH2   . ARG A 1 1567 ? 190.356 189.134 120.671 1.00 92.57  ? 1567 ARG A NH2   1 
ATOM   2037  N N     . PHE A 1 1568 ? 183.509 193.203 124.547 1.00 93.46  ? 1568 PHE A N     1 
ATOM   2038  C CA    . PHE A 1 1568 ? 182.306 193.360 125.353 1.00 93.46  ? 1568 PHE A CA    1 
ATOM   2039  C C     . PHE A 1 1568 ? 181.465 194.531 124.871 1.00 93.46  ? 1568 PHE A C     1 
ATOM   2040  O O     . PHE A 1 1568 ? 180.237 194.489 124.962 1.00 93.46  ? 1568 PHE A O     1 
ATOM   2041  C CB    . PHE A 1 1568 ? 182.658 193.539 126.827 1.00 93.46  ? 1568 PHE A CB    1 
ATOM   2042  C CG    . PHE A 1 1568 ? 181.498 193.998 127.659 1.00 93.46  ? 1568 PHE A CG    1 
ATOM   2043  C CD1   . PHE A 1 1568 ? 180.443 193.143 127.926 1.00 93.46  ? 1568 PHE A CD1   1 
ATOM   2044  C CD2   . PHE A 1 1568 ? 181.454 195.287 128.165 1.00 93.46  ? 1568 PHE A CD2   1 
ATOM   2045  C CE1   . PHE A 1 1568 ? 179.365 193.561 128.680 1.00 93.46  ? 1568 PHE A CE1   1 
ATOM   2046  C CE2   . PHE A 1 1568 ? 180.380 195.711 128.925 1.00 93.46  ? 1568 PHE A CE2   1 
ATOM   2047  C CZ    . PHE A 1 1568 ? 179.334 194.847 129.184 1.00 93.46  ? 1568 PHE A CZ    1 
ATOM   2048  N N     . GLN A 1 1569 ? 182.101 195.595 124.379 1.00 92.05  ? 1569 GLN A N     1 
ATOM   2049  C CA    . GLN A 1 1569 ? 181.335 196.703 123.819 1.00 92.05  ? 1569 GLN A CA    1 
ATOM   2050  C C     . GLN A 1 1569 ? 180.553 196.258 122.591 1.00 92.05  ? 1569 GLN A C     1 
ATOM   2051  O O     . GLN A 1 1569 ? 179.383 196.622 122.427 1.00 92.05  ? 1569 GLN A O     1 
ATOM   2052  C CB    . GLN A 1 1569 ? 182.259 197.872 123.476 1.00 92.05  ? 1569 GLN A CB    1 
ATOM   2053  C CG    . GLN A 1 1569 ? 182.819 198.612 124.685 1.00 92.05  ? 1569 GLN A CG    1 
ATOM   2054  C CD    . GLN A 1 1569 ? 181.755 199.343 125.491 1.00 92.05  ? 1569 GLN A CD    1 
ATOM   2055  O OE1   . GLN A 1 1569 ? 180.600 199.451 125.076 1.00 92.05  ? 1569 GLN A OE1   1 
ATOM   2056  N NE2   . GLN A 1 1569 ? 182.144 199.843 126.657 1.00 92.05  ? 1569 GLN A NE2   1 
ATOM   2057  N N     . SER A 1 1570 ? 181.180 195.464 121.720 1.00 94.65  ? 1570 SER A N     1 
ATOM   2058  C CA    . SER A 1 1570 ? 180.458 194.933 120.564 1.00 94.65  ? 1570 SER A CA    1 
ATOM   2059  C C     . SER A 1 1570 ? 179.312 194.023 121.000 1.00 94.65  ? 1570 SER A C     1 
ATOM   2060  O O     . SER A 1 1570 ? 178.193 194.109 120.467 1.00 94.65  ? 1570 SER A O     1 
ATOM   2061  C CB    . SER A 1 1570 ? 181.422 194.182 119.645 1.00 94.65  ? 1570 SER A CB    1 
ATOM   2062  O OG    . SER A 1 1570 ? 182.310 195.076 118.996 1.00 94.65  ? 1570 SER A OG    1 
ATOM   2063  N N     . ILE A 1 1571 ? 179.574 193.150 121.976 1.00 93.80  ? 1571 ILE A N     1 
ATOM   2064  C CA    . ILE A 1 1571 ? 178.545 192.245 122.479 1.00 93.80  ? 1571 ILE A CA    1 
ATOM   2065  C C     . ILE A 1 1571 ? 177.390 193.035 123.077 1.00 93.80  ? 1571 ILE A C     1 
ATOM   2066  O O     . ILE A 1 1571 ? 176.219 192.706 122.865 1.00 93.80  ? 1571 ILE A O     1 
ATOM   2067  C CB    . ILE A 1 1571 ? 179.151 191.268 123.504 1.00 93.80  ? 1571 ILE A CB    1 
ATOM   2068  C CG1   . ILE A 1 1571 ? 180.152 190.332 122.826 1.00 93.80  ? 1571 ILE A CG1   1 
ATOM   2069  C CG2   . ILE A 1 1571 ? 178.058 190.468 124.196 1.00 93.80  ? 1571 ILE A CG2   1 
ATOM   2070  C CD1   . ILE A 1 1571 ? 181.084 189.643 123.795 1.00 93.80  ? 1571 ILE A CD1   1 
ATOM   2071  N N     . SER A 1 1572 ? 177.702 194.088 123.834 1.00 94.88  ? 1572 SER A N     1 
ATOM   2072  C CA    . SER A 1 1572 ? 176.676 194.921 124.443 1.00 94.88  ? 1572 SER A CA    1 
ATOM   2073  C C     . SER A 1 1572 ? 175.877 195.683 123.399 1.00 94.88  ? 1572 SER A C     1 
ATOM   2074  O O     . SER A 1 1572 ? 174.669 195.857 123.561 1.00 94.88  ? 1572 SER A O     1 
ATOM   2075  C CB    . SER A 1 1572 ? 177.311 195.893 125.437 1.00 94.88  ? 1572 SER A CB    1 
ATOM   2076  O OG    . SER A 1 1572 ? 176.329 196.499 126.260 1.00 94.88  ? 1572 SER A OG    1 
ATOM   2077  N N     . THR A 1 1573 ? 176.527 196.154 122.333 1.00 91.36  ? 1573 THR A N     1 
ATOM   2078  C CA    . THR A 1 1573 ? 175.790 196.813 121.259 1.00 91.36  ? 1573 THR A CA    1 
ATOM   2079  C C     . THR A 1 1573 ? 174.792 195.855 120.622 1.00 91.36  ? 1573 THR A C     1 
ATOM   2080  O O     . THR A 1 1573 ? 173.613 196.193 120.435 1.00 91.36  ? 1573 THR A O     1 
ATOM   2081  C CB    . THR A 1 1573 ? 176.763 197.355 120.211 1.00 91.36  ? 1573 THR A CB    1 
ATOM   2082  O OG1   . THR A 1 1573 ? 177.618 198.337 120.810 1.00 91.36  ? 1573 THR A OG1   1 
ATOM   2083  C CG2   . THR A 1 1573 ? 176.005 197.989 119.055 1.00 91.36  ? 1573 THR A CG2   1 
ATOM   2084  N N     . GLU A 1 1574 ? 175.243 194.637 120.302 1.00 95.18  ? 1574 GLU A N     1 
ATOM   2085  C CA    . GLU A 1 1574 ? 174.333 193.656 119.715 1.00 95.18  ? 1574 GLU A CA    1 
ATOM   2086  C C     . GLU A 1 1574 ? 173.213 193.294 120.686 1.00 95.18  ? 1574 GLU A C     1 
ATOM   2087  O O     . GLU A 1 1574 ? 172.046 193.173 120.288 1.00 95.18  ? 1574 GLU A O     1 
ATOM   2088  C CB    . GLU A 1 1574 ? 175.104 192.405 119.291 1.00 95.18  ? 1574 GLU A CB    1 
ATOM   2089  C CG    . GLU A 1 1574 ? 174.211 191.245 118.869 1.00 95.18  ? 1574 GLU A CG    1 
ATOM   2090  C CD    . GLU A 1 1574 ? 174.964 190.172 118.106 1.00 95.18  ? 1574 GLU A CD    1 
ATOM   2091  O OE1   . GLU A 1 1574 ? 175.651 190.514 117.121 1.00 95.18  ? 1574 GLU A OE1   1 
ATOM   2092  O OE2   . GLU A 1 1574 ? 174.863 188.987 118.485 1.00 95.18  ? 1574 GLU A OE2   1 
ATOM   2093  N N     . PHE A 1 1575 ? 173.549 193.130 121.968 1.00 95.74  ? 1575 PHE A N     1 
ATOM   2094  C CA    . PHE A 1 1575 ? 172.549 192.774 122.967 1.00 95.74  ? 1575 PHE A CA    1 
ATOM   2095  C C     . PHE A 1 1575 ? 171.520 193.880 123.143 1.00 95.74  ? 1575 PHE A C     1 
ATOM   2096  O O     . PHE A 1 1575 ? 170.326 193.604 123.278 1.00 95.74  ? 1575 PHE A O     1 
ATOM   2097  C CB    . PHE A 1 1575 ? 173.231 192.459 124.299 1.00 95.74  ? 1575 PHE A CB    1 
ATOM   2098  C CG    . PHE A 1 1575 ? 172.296 191.932 125.348 1.00 95.74  ? 1575 PHE A CG    1 
ATOM   2099  C CD1   . PHE A 1 1575 ? 171.783 190.649 125.256 1.00 95.74  ? 1575 PHE A CD1   1 
ATOM   2100  C CD2   . PHE A 1 1575 ? 171.928 192.720 126.425 1.00 95.74  ? 1575 PHE A CD2   1 
ATOM   2101  C CE1   . PHE A 1 1575 ? 170.922 190.161 126.219 1.00 95.74  ? 1575 PHE A CE1   1 
ATOM   2102  C CE2   . PHE A 1 1575 ? 171.066 192.238 127.391 1.00 95.74  ? 1575 PHE A CE2   1 
ATOM   2103  C CZ    . PHE A 1 1575 ? 170.563 190.957 127.288 1.00 95.74  ? 1575 PHE A CZ    1 
ATOM   2104  N N     . LEU A 1 1576 ? 171.962 195.139 123.155 1.00 97.47  ? 1576 LEU A N     1 
ATOM   2105  C CA    . LEU A 1 1576 ? 171.031 196.253 123.285 1.00 97.47  ? 1576 LEU A CA    1 
ATOM   2106  C C     . LEU A 1 1576 ? 170.130 196.360 122.064 1.00 97.47  ? 1576 LEU A C     1 
ATOM   2107  O O     . LEU A 1 1576 ? 168.935 196.650 122.194 1.00 97.47  ? 1576 LEU A O     1 
ATOM   2108  C CB    . LEU A 1 1576 ? 171.797 197.558 123.506 1.00 97.47  ? 1576 LEU A CB    1 
ATOM   2109  C CG    . LEU A 1 1576 ? 172.433 197.753 124.884 1.00 97.47  ? 1576 LEU A CG    1 
ATOM   2110  C CD1   . LEU A 1 1576 ? 172.830 199.207 125.091 1.00 97.47  ? 1576 LEU A CD1   1 
ATOM   2111  C CD2   . LEU A 1 1576 ? 171.495 197.287 125.987 1.00 97.47  ? 1576 LEU A CD2   1 
ATOM   2112  N N     . ALA A 1 1577 ? 170.679 196.129 120.868 1.00 97.69  ? 1577 ALA A N     1 
ATOM   2113  C CA    . ALA A 1 1577 ? 169.837 196.109 119.676 1.00 97.69  ? 1577 ALA A CA    1 
ATOM   2114  C C     . ALA A 1 1577 ? 168.786 195.008 119.768 1.00 97.69  ? 1577 ALA A C     1 
ATOM   2115  O O     . ALA A 1 1577 ? 167.610 195.228 119.448 1.00 97.69  ? 1577 ALA A O     1 
ATOM   2116  C CB    . ALA A 1 1577 ? 170.698 195.933 118.426 1.00 97.69  ? 1577 ALA A CB    1 
ATOM   2117  N N     . LEU A 1 1578 ? 169.190 193.819 120.224 1.00 98.03  ? 1578 LEU A N     1 
ATOM   2118  C CA    . LEU A 1 1578 ? 168.242 192.717 120.357 1.00 98.03  ? 1578 LEU A CA    1 
ATOM   2119  C C     . LEU A 1 1578 ? 167.184 193.016 121.413 1.00 98.03  ? 1578 LEU A C     1 
ATOM   2120  O O     . LEU A 1 1578 ? 166.006 192.689 121.232 1.00 98.03  ? 1578 LEU A O     1 
ATOM   2121  C CB    . LEU A 1 1578 ? 168.988 191.425 120.688 1.00 98.03  ? 1578 LEU A CB    1 
ATOM   2122  C CG    . LEU A 1 1578 ? 168.145 190.160 120.842 1.00 98.03  ? 1578 LEU A CG    1 
ATOM   2123  C CD1   . LEU A 1 1578 ? 167.252 189.958 119.631 1.00 98.03  ? 1578 LEU A CD1   1 
ATOM   2124  C CD2   . LEU A 1 1578 ? 169.046 188.954 121.048 1.00 98.03  ? 1578 LEU A CD2   1 
ATOM   2125  N N     . MET A 1 1579 ? 167.587 193.631 122.528 1.00 103.73 ? 1579 MET A N     1 
ATOM   2126  C CA    . MET A 1 1579 ? 166.631 193.986 123.573 1.00 103.73 ? 1579 MET A CA    1 
ATOM   2127  C C     . MET A 1 1579 ? 165.639 195.029 123.079 1.00 103.73 ? 1579 MET A C     1 
ATOM   2128  O O     . MET A 1 1579 ? 164.448 194.966 123.403 1.00 103.73 ? 1579 MET A O     1 
ATOM   2129  C CB    . MET A 1 1579 ? 167.368 194.492 124.814 1.00 103.73 ? 1579 MET A CB    1 
ATOM   2130  C CG    . MET A 1 1579 ? 168.225 193.442 125.504 1.00 103.73 ? 1579 MET A CG    1 
ATOM   2131  S SD    . MET A 1 1579 ? 167.295 192.021 126.106 1.00 103.73 ? 1579 MET A SD    1 
ATOM   2132  C CE    . MET A 1 1579 ? 166.369 192.767 127.440 1.00 103.73 ? 1579 MET A CE    1 
ATOM   2133  N N     . LYS A 1 1580 ? 166.114 196.007 122.304 1.00 102.74 ? 1580 LYS A N     1 
ATOM   2134  C CA    . LYS A 1 1580 ? 165.211 196.991 121.716 1.00 102.74 ? 1580 LYS A CA    1 
ATOM   2135  C C     . LYS A 1 1580 ? 164.234 196.329 120.753 1.00 102.74 ? 1580 LYS A C     1 
ATOM   2136  O O     . LYS A 1 1580 ? 163.049 196.680 120.721 1.00 102.74 ? 1580 LYS A O     1 
ATOM   2137  C CB    . LYS A 1 1580 ? 166.013 198.081 121.005 1.00 102.74 ? 1580 LYS A CB    1 
ATOM   2138  C CG    . LYS A 1 1580 ? 165.158 199.140 120.326 1.00 102.74 ? 1580 LYS A CG    1 
ATOM   2139  C CD    . LYS A 1 1580 ? 166.009 200.273 119.772 1.00 102.74 ? 1580 LYS A CD    1 
ATOM   2140  C CE    . LYS A 1 1580 ? 167.112 199.753 118.862 1.00 102.74 ? 1580 LYS A CE    1 
ATOM   2141  N NZ    . LYS A 1 1580 ? 166.597 198.804 117.836 1.00 102.74 ? 1580 LYS A NZ    1 
ATOM   2142  N N     . LYS A 1 1581 ? 164.715 195.371 119.956 1.00 103.38 ? 1581 LYS A N     1 
ATOM   2143  C CA    . LYS A 1 1581 ? 163.821 194.638 119.064 1.00 103.38 ? 1581 LYS A CA    1 
ATOM   2144  C C     . LYS A 1 1581 ? 162.776 193.854 119.849 1.00 103.38 ? 1581 LYS A C     1 
ATOM   2145  O O     . LYS A 1 1581 ? 161.606 193.792 119.453 1.00 103.38 ? 1581 LYS A O     1 
ATOM   2146  C CB    . LYS A 1 1581 ? 164.628 193.703 118.163 1.00 103.38 ? 1581 LYS A CB    1 
ATOM   2147  C CG    . LYS A 1 1581 ? 165.461 194.418 117.112 1.00 103.38 ? 1581 LYS A CG    1 
ATOM   2148  C CD    . LYS A 1 1581 ? 166.284 193.433 116.296 1.00 103.38 ? 1581 LYS A CD    1 
ATOM   2149  C CE    . LYS A 1 1581 ? 165.402 192.603 115.378 1.00 103.38 ? 1581 LYS A CE    1 
ATOM   2150  N NZ    . LYS A 1 1581 ? 164.798 193.426 114.294 1.00 103.38 ? 1581 LYS A NZ    1 
ATOM   2151  N N     . VAL A 1 1582 ? 163.184 193.240 120.962 1.00 104.81 ? 1582 VAL A N     1 
ATOM   2152  C CA    . VAL A 1 1582 ? 162.254 192.465 121.778 1.00 104.81 ? 1582 VAL A CA    1 
ATOM   2153  C C     . VAL A 1 1582 ? 161.221 193.376 122.433 1.00 104.81 ? 1582 VAL A C     1 
ATOM   2154  O O     . VAL A 1 1582 ? 160.041 193.020 122.545 1.00 104.81 ? 1582 VAL A O     1 
ATOM   2155  C CB    . VAL A 1 1582 ? 163.027 191.637 122.821 1.00 104.81 ? 1582 VAL A CB    1 
ATOM   2156  C CG1   . VAL A 1 1582 ? 162.079 191.056 123.860 1.00 104.81 ? 1582 VAL A CG1   1 
ATOM   2157  C CG2   . VAL A 1 1582 ? 163.810 190.527 122.138 1.00 104.81 ? 1582 VAL A CG2   1 
ATOM   2158  N N     . SER A 1 1583 ? 161.643 194.565 122.871 1.00 105.23 ? 1583 SER A N     1 
ATOM   2159  C CA    . SER A 1 1583 ? 160.732 195.471 123.565 1.00 105.23 ? 1583 SER A CA    1 
ATOM   2160  C C     . SER A 1 1583 ? 159.580 195.912 122.672 1.00 105.23 ? 1583 SER A C     1 
ATOM   2161  O O     . SER A 1 1583 ? 158.452 196.075 123.152 1.00 105.23 ? 1583 SER A O     1 
ATOM   2162  C CB    . SER A 1 1583 ? 161.499 196.690 124.081 1.00 105.23 ? 1583 SER A CB    1 
ATOM   2163  O OG    . SER A 1 1583 ? 160.629 197.608 124.719 1.00 105.23 ? 1583 SER A OG    1 
ATOM   2164  N N     . LYS A 1 1584 ? 159.839 196.111 121.378 1.00 106.75 ? 1584 LYS A N     1 
ATOM   2165  C CA    . LYS A 1 1584 ? 158.784 196.529 120.462 1.00 106.75 ? 1584 LYS A CA    1 
ATOM   2166  C C     . LYS A 1 1584 ? 157.744 195.440 120.235 1.00 106.75 ? 1584 LYS A C     1 
ATOM   2167  O O     . LYS A 1 1584 ? 156.659 195.734 119.723 1.00 106.75 ? 1584 LYS A O     1 
ATOM   2168  C CB    . LYS A 1 1584 ? 159.393 196.958 119.126 1.00 106.75 ? 1584 LYS A CB    1 
ATOM   2169  C CG    . LYS A 1 1584 ? 160.081 198.313 119.170 1.00 106.75 ? 1584 LYS A CG    1 
ATOM   2170  C CD    . LYS A 1 1584 ? 160.818 198.605 117.874 1.00 106.75 ? 1584 LYS A CD    1 
ATOM   2171  C CE    . LYS A 1 1584 ? 161.607 199.901 117.970 1.00 106.75 ? 1584 LYS A CE    1 
ATOM   2172  N NZ    . LYS A 1 1584 ? 162.460 200.124 116.771 1.00 106.75 ? 1584 LYS A NZ    1 
ATOM   2173  N N     . SER A 1 1585 ? 158.046 194.197 120.603 1.00 111.18 ? 1585 SER A N     1 
ATOM   2174  C CA    . SER A 1 1585 ? 157.101 193.087 120.468 1.00 111.18 ? 1585 SER A CA    1 
ATOM   2175  C C     . SER A 1 1585 ? 157.379 192.077 121.569 1.00 111.18 ? 1585 SER A C     1 
ATOM   2176  O O     . SER A 1 1585 ? 158.040 191.054 121.352 1.00 111.18 ? 1585 SER A O     1 
ATOM   2177  C CB    . SER A 1 1585 ? 157.202 192.436 119.088 1.00 111.18 ? 1585 SER A CB    1 
ATOM   2178  O OG    . SER A 1 1585 ? 158.546 192.111 118.776 1.00 111.18 ? 1585 SER A OG    1 
ATOM   2179  N N     . PRO A 1 1586 ? 156.882 192.334 122.783 1.00 112.52 ? 1586 PRO A N     1 
ATOM   2180  C CA    . PRO A 1 1586 ? 157.206 191.459 123.919 1.00 112.52 ? 1586 PRO A CA    1 
ATOM   2181  C C     . PRO A 1 1586 ? 156.482 190.122 123.907 1.00 112.52 ? 1586 PRO A C     1 
ATOM   2182  O O     . PRO A 1 1586 ? 156.684 189.326 124.831 1.00 112.52 ? 1586 PRO A O     1 
ATOM   2183  C CB    . PRO A 1 1586 ? 156.782 192.299 125.130 1.00 112.52 ? 1586 PRO A CB    1 
ATOM   2184  C CG    . PRO A 1 1586 ? 155.674 193.149 124.612 1.00 112.52 ? 1586 PRO A CG    1 
ATOM   2185  C CD    . PRO A 1 1586 ? 156.015 193.458 123.177 1.00 112.52 ? 1586 PRO A CD    1 
ATOM   2186  N N     . LEU A 1 1587 ? 155.647 189.849 122.908 1.00 111.59 ? 1587 LEU A N     1 
ATOM   2187  C CA    . LEU A 1 1587 ? 154.949 188.573 122.847 1.00 111.59 ? 1587 LEU A CA    1 
ATOM   2188  C C     . LEU A 1 1587 ? 155.941 187.437 122.623 1.00 111.59 ? 1587 LEU A C     1 
ATOM   2189  O O     . LEU A 1 1587 ? 156.917 187.580 121.882 1.00 111.59 ? 1587 LEU A O     1 
ATOM   2190  C CB    . LEU A 1 1587 ? 153.902 188.594 121.735 1.00 111.59 ? 1587 LEU A CB    1 
ATOM   2191  C CG    . LEU A 1 1587 ? 152.598 189.323 122.070 1.00 111.59 ? 1587 LEU A CG    1 
ATOM   2192  C CD1   . LEU A 1 1587 ? 151.900 189.796 120.806 1.00 111.59 ? 1587 LEU A CD1   1 
ATOM   2193  C CD2   . LEU A 1 1587 ? 151.677 188.431 122.887 1.00 111.59 ? 1587 LEU A CD2   1 
ATOM   2194  N N     . VAL A 1 1588 ? 155.686 186.302 123.279 1.00 111.38 ? 1588 VAL A N     1 
ATOM   2195  C CA    . VAL A 1 1588 ? 156.618 185.177 123.219 1.00 111.38 ? 1588 VAL A CA    1 
ATOM   2196  C C     . VAL A 1 1588 ? 156.714 184.639 121.797 1.00 111.38 ? 1588 VAL A C     1 
ATOM   2197  O O     . VAL A 1 1588 ? 157.810 184.386 121.281 1.00 111.38 ? 1588 VAL A O     1 
ATOM   2198  C CB    . VAL A 1 1588 ? 156.195 184.078 124.211 1.00 111.38 ? 1588 VAL A CB    1 
ATOM   2199  C CG1   . VAL A 1 1588 ? 156.984 182.801 123.962 1.00 111.38 ? 1588 VAL A CG1   1 
ATOM   2200  C CG2   . VAL A 1 1588 ? 156.385 184.556 125.640 1.00 111.38 ? 1588 VAL A CG2   1 
ATOM   2201  N N     . MET A 1 1589 ? 155.566 184.457 121.140 1.00 113.06 ? 1589 MET A N     1 
ATOM   2202  C CA    . MET A 1 1589 ? 155.574 183.963 119.767 1.00 113.06 ? 1589 MET A CA    1 
ATOM   2203  C C     . MET A 1 1589 ? 156.242 184.958 118.827 1.00 113.06 ? 1589 MET A C     1 
ATOM   2204  O O     . MET A 1 1589 ? 156.996 184.565 117.929 1.00 113.06 ? 1589 MET A O     1 
ATOM   2205  C CB    . MET A 1 1589 ? 154.146 183.661 119.308 1.00 113.06 ? 1589 MET A CB    1 
ATOM   2206  C CG    . MET A 1 1589 ? 153.458 182.466 119.989 1.00 113.06 ? 1589 MET A CG    1 
ATOM   2207  S SD    . MET A 1 1589 ? 154.447 181.121 120.701 1.00 113.06 ? 1589 MET A SD    1 
ATOM   2208  C CE    . MET A 1 1589 ? 155.522 180.625 119.349 1.00 113.06 ? 1589 MET A CE    1 
ATOM   2209  N N     . ASP A 1 1590 ? 155.973 186.252 119.016 1.00 109.51 ? 1590 ASP A N     1 
ATOM   2210  C CA    . ASP A 1 1590 ? 156.612 187.268 118.185 1.00 109.51 ? 1590 ASP A CA    1 
ATOM   2211  C C     . ASP A 1 1590 ? 158.122 187.279 118.388 1.00 109.51 ? 1590 ASP A C     1 
ATOM   2212  O O     . ASP A 1 1590 ? 158.884 187.418 117.425 1.00 109.51 ? 1590 ASP A O     1 
ATOM   2213  C CB    . ASP A 1 1590 ? 156.017 188.643 118.485 1.00 109.51 ? 1590 ASP A CB    1 
ATOM   2214  C CG    . ASP A 1 1590 ? 154.545 188.728 118.138 1.00 109.51 ? 1590 ASP A CG    1 
ATOM   2215  O OD1   . ASP A 1 1590 ? 153.975 187.706 117.702 1.00 109.51 ? 1590 ASP A OD1   1 
ATOM   2216  O OD2   . ASP A 1 1590 ? 153.958 189.819 118.295 1.00 109.51 ? 1590 ASP A OD2   1 
ATOM   2217  N N     . VAL A 1 1591 ? 158.572 187.137 119.637 1.00 108.07 ? 1591 VAL A N     1 
ATOM   2218  C CA    . VAL A 1 1591 ? 160.006 187.099 119.914 1.00 108.07 ? 1591 VAL A CA    1 
ATOM   2219  C C     . VAL A 1 1591 ? 160.642 185.873 119.270 1.00 108.07 ? 1591 VAL A C     1 
ATOM   2220  O O     . VAL A 1 1591 ? 161.717 185.957 118.664 1.00 108.07 ? 1591 VAL A O     1 
ATOM   2221  C CB    . VAL A 1 1591 ? 160.257 187.140 121.433 1.00 108.07 ? 1591 VAL A CB    1 
ATOM   2222  C CG1   . VAL A 1 1591 ? 161.637 186.591 121.768 1.00 108.07 ? 1591 VAL A CG1   1 
ATOM   2223  C CG2   . VAL A 1 1591 ? 160.104 188.559 121.957 1.00 108.07 ? 1591 VAL A CG2   1 
ATOM   2224  N N     . LEU A 1 1592 ? 159.984 184.717 119.384 1.00 106.20 ? 1592 LEU A N     1 
ATOM   2225  C CA    . LEU A 1 1592 ? 160.525 183.493 118.803 1.00 106.20 ? 1592 LEU A CA    1 
ATOM   2226  C C     . LEU A 1 1592 ? 160.576 183.558 117.281 1.00 106.20 ? 1592 LEU A C     1 
ATOM   2227  O O     . LEU A 1 1592 ? 161.458 182.947 116.666 1.00 106.20 ? 1592 LEU A O     1 
ATOM   2228  C CB    . LEU A 1 1592 ? 159.697 182.289 119.254 1.00 106.20 ? 1592 LEU A CB    1 
ATOM   2229  C CG    . LEU A 1 1592 ? 160.219 180.902 118.870 1.00 106.20 ? 1592 LEU A CG    1 
ATOM   2230  C CD1   . LEU A 1 1592 ? 161.493 180.572 119.629 1.00 106.20 ? 1592 LEU A CD1   1 
ATOM   2231  C CD2   . LEU A 1 1592 ? 159.158 179.843 119.119 1.00 106.20 ? 1592 LEU A CD2   1 
ATOM   2232  N N     . ASN A 1 1593 ? 159.656 184.291 116.658 1.00 105.89 ? 1593 ASN A N     1 
ATOM   2233  C CA    . ASN A 1 1593 ? 159.559 184.343 115.206 1.00 105.89 ? 1593 ASN A CA    1 
ATOM   2234  C C     . ASN A 1 1593 ? 160.500 185.362 114.573 1.00 105.89 ? 1593 ASN A C     1 
ATOM   2235  O O     . ASN A 1 1593 ? 160.548 185.451 113.341 1.00 105.89 ? 1593 ASN A O     1 
ATOM   2236  C CB    . ASN A 1 1593 ? 158.117 184.643 114.785 1.00 105.89 ? 1593 ASN A CB    1 
ATOM   2237  C CG    . ASN A 1 1593 ? 157.179 183.482 115.053 1.00 105.89 ? 1593 ASN A CG    1 
ATOM   2238  O OD1   . ASN A 1 1593 ? 157.581 182.320 115.001 1.00 105.89 ? 1593 ASN A OD1   1 
ATOM   2239  N ND2   . ASN A 1 1593 ? 155.921 183.792 115.343 1.00 105.89 ? 1593 ASN A ND2   1 
ATOM   2240  N N     . ILE A 1 1594 ? 161.241 186.131 115.372 1.00 102.39 ? 1594 ILE A N     1 
ATOM   2241  C CA    . ILE A 1 1594 ? 162.221 187.051 114.810 1.00 102.39 ? 1594 ILE A CA    1 
ATOM   2242  C C     . ILE A 1 1594 ? 163.369 186.253 114.197 1.00 102.39 ? 1594 ILE A C     1 
ATOM   2243  O O     . ILE A 1 1594 ? 163.753 185.185 114.693 1.00 102.39 ? 1594 ILE A O     1 
ATOM   2244  C CB    . ILE A 1 1594 ? 162.723 188.037 115.882 1.00 102.39 ? 1594 ILE A CB    1 
ATOM   2245  C CG1   . ILE A 1 1594 ? 161.555 188.833 116.465 1.00 102.39 ? 1594 ILE A CG1   1 
ATOM   2246  C CG2   . ILE A 1 1594 ? 163.763 188.992 115.311 1.00 102.39 ? 1594 ILE A CG2   1 
ATOM   2247  C CD1   . ILE A 1 1594 ? 161.868 189.489 117.792 1.00 102.39 ? 1594 ILE A CD1   1 
ATOM   2248  N N     . GLN A 1 1595 ? 163.911 186.768 113.092 1.00 102.40 ? 1595 GLN A N     1 
ATOM   2249  C CA    . GLN A 1 1595 ? 164.934 186.073 112.320 1.00 102.40 ? 1595 GLN A CA    1 
ATOM   2250  C C     . GLN A 1 1595 ? 166.189 185.776 113.133 1.00 102.40 ? 1595 GLN A C     1 
ATOM   2251  O O     . GLN A 1 1595 ? 166.898 186.695 113.556 1.00 102.40 ? 1595 GLN A O     1 
ATOM   2252  C CB    . GLN A 1 1595 ? 165.307 186.893 111.083 1.00 102.40 ? 1595 GLN A CB    1 
ATOM   2253  C CG    . GLN A 1 1595 ? 166.441 186.298 110.265 1.00 102.40 ? 1595 GLN A CG    1 
ATOM   2254  C CD    . GLN A 1 1595 ? 166.869 187.197 109.122 1.00 102.40 ? 1595 GLN A CD    1 
ATOM   2255  O OE1   . GLN A 1 1595 ? 166.321 188.283 108.933 1.00 102.40 ? 1595 GLN A OE1   1 
ATOM   2256  N NE2   . GLN A 1 1595 ? 167.853 186.747 108.352 1.00 102.40 ? 1595 GLN A NE2   1 
ATOM   2257  N N     . GLY A 1 1596 ? 166.466 184.493 113.350 1.00 97.16  ? 1596 GLY A N     1 
ATOM   2258  C CA    . GLY A 1 1596 ? 167.731 184.069 113.931 1.00 97.16  ? 1596 GLY A CA    1 
ATOM   2259  C C     . GLY A 1 1596 ? 167.998 184.562 115.336 1.00 97.16  ? 1596 GLY A C     1 
ATOM   2260  O O     . GLY A 1 1596 ? 169.123 184.979 115.639 1.00 97.16  ? 1596 GLY A O     1 
ATOM   2261  N N     . VAL A 1 1597 ? 166.987 184.531 116.206 1.00 101.39 ? 1597 VAL A N     1 
ATOM   2262  C CA    . VAL A 1 1597 ? 167.209 184.889 117.603 1.00 101.39 ? 1597 VAL A CA    1 
ATOM   2263  C C     . VAL A 1 1597 ? 168.128 183.874 118.270 1.00 101.39 ? 1597 VAL A C     1 
ATOM   2264  O O     . VAL A 1 1597 ? 169.034 184.237 119.027 1.00 101.39 ? 1597 VAL A O     1 
ATOM   2265  C CB    . VAL A 1 1597 ? 165.872 185.012 118.354 1.00 101.39 ? 1597 VAL A CB    1 
ATOM   2266  C CG1   . VAL A 1 1597 ? 166.100 185.574 119.747 1.00 101.39 ? 1597 VAL A CG1   1 
ATOM   2267  C CG2   . VAL A 1 1597 ? 164.919 185.891 117.585 1.00 101.39 ? 1597 VAL A CG2   1 
ATOM   2268  N N     . GLN A 1 1598 ? 167.904 182.585 118.001 1.00 102.48 ? 1598 GLN A N     1 
ATOM   2269  C CA    . GLN A 1 1598 ? 168.692 181.542 118.650 1.00 102.48 ? 1598 GLN A CA    1 
ATOM   2270  C C     . GLN A 1 1598 ? 170.155 181.592 118.223 1.00 102.48 ? 1598 GLN A C     1 
ATOM   2271  O O     . GLN A 1 1598 ? 171.052 181.399 119.049 1.00 102.48 ? 1598 GLN A O     1 
ATOM   2272  C CB    . GLN A 1 1598 ? 168.090 180.168 118.352 1.00 102.48 ? 1598 GLN A CB    1 
ATOM   2273  C CG    . GLN A 1 1598 ? 168.970 178.994 118.761 1.00 102.48 ? 1598 GLN A CG    1 
ATOM   2274  C CD    . GLN A 1 1598 ? 169.017 178.784 120.264 1.00 102.48 ? 1598 GLN A CD    1 
ATOM   2275  O OE1   . GLN A 1 1598 ? 168.291 179.431 121.019 1.00 102.48 ? 1598 GLN A OE1   1 
ATOM   2276  N NE2   . GLN A 1 1598 ? 169.878 177.874 120.705 1.00 102.48 ? 1598 GLN A NE2   1 
ATOM   2277  N N     . ARG A 1 1599 ? 170.417 181.847 116.939 1.00 102.33 ? 1599 ARG A N     1 
ATOM   2278  C CA    . ARG A 1 1599 ? 171.795 181.874 116.454 1.00 102.33 ? 1599 ARG A CA    1 
ATOM   2279  C C     . ARG A 1 1599 ? 172.582 183.011 117.097 1.00 102.33 ? 1599 ARG A C     1 
ATOM   2280  O O     . ARG A 1 1599 ? 173.672 182.801 117.646 1.00 102.33 ? 1599 ARG A O     1 
ATOM   2281  C CB    . ARG A 1 1599 ? 171.805 182.007 114.931 1.00 102.33 ? 1599 ARG A CB    1 
ATOM   2282  C CG    . ARG A 1 1599 ? 170.865 181.048 114.221 1.00 102.33 ? 1599 ARG A CG    1 
ATOM   2283  C CD    . ARG A 1 1599 ? 170.699 181.422 112.757 1.00 102.33 ? 1599 ARG A CD    1 
ATOM   2284  N NE    . ARG A 1 1599 ? 169.637 180.656 112.117 1.00 102.33 ? 1599 ARG A NE    1 
ATOM   2285  C CZ    . ARG A 1 1599 ? 169.227 180.841 110.869 1.00 102.33 ? 1599 ARG A CZ    1 
ATOM   2286  N NH1   . ARG A 1 1599 ? 169.771 181.763 110.092 1.00 102.33 ? 1599 ARG A NH1   1 
ATOM   2287  N NH2   . ARG A 1 1599 ? 168.245 180.082 110.390 1.00 102.33 ? 1599 ARG A NH2   1 
ATOM   2288  N N     . SER A 1 1600 ? 172.036 184.229 117.040 1.00 97.37  ? 1600 SER A N     1 
ATOM   2289  C CA    . SER A 1 1600 ? 172.701 185.369 117.659 1.00 97.37  ? 1600 SER A CA    1 
ATOM   2290  C C     . SER A 1 1600 ? 172.797 185.192 119.167 1.00 97.37  ? 1600 SER A C     1 
ATOM   2291  O O     . SER A 1 1600 ? 173.778 185.612 119.789 1.00 97.37  ? 1600 SER A O     1 
ATOM   2292  C CB    . SER A 1 1600 ? 171.958 186.660 117.316 1.00 97.37  ? 1600 SER A CB    1 
ATOM   2293  O OG    . SER A 1 1600 ? 172.597 187.785 117.894 1.00 97.37  ? 1600 SER A OG    1 
ATOM   2294  N N     . LEU A 1 1601 ? 171.785 184.569 119.772 1.00 99.29  ? 1601 LEU A N     1 
ATOM   2295  C CA    . LEU A 1 1601 ? 171.803 184.334 121.211 1.00 99.29  ? 1601 LEU A CA    1 
ATOM   2296  C C     . LEU A 1 1601 ? 172.923 183.379 121.603 1.00 99.29  ? 1601 LEU A C     1 
ATOM   2297  O O     . LEU A 1 1601 ? 173.627 183.610 122.591 1.00 99.29  ? 1601 LEU A O     1 
ATOM   2298  C CB    . LEU A 1 1601 ? 170.448 183.791 121.655 1.00 99.29  ? 1601 LEU A CB    1 
ATOM   2299  C CG    . LEU A 1 1601 ? 170.152 183.782 123.149 1.00 99.29  ? 1601 LEU A CG    1 
ATOM   2300  C CD1   . LEU A 1 1601 ? 170.251 185.185 123.721 1.00 99.29  ? 1601 LEU A CD1   1 
ATOM   2301  C CD2   . LEU A 1 1601 ? 168.775 183.201 123.374 1.00 99.29  ? 1601 LEU A CD2   1 
ATOM   2302  N N     . GLU A 1 1602 ? 173.106 182.301 120.838 1.00 95.66  ? 1602 GLU A N     1 
ATOM   2303  C CA    . GLU A 1 1602 ? 174.194 181.369 121.116 1.00 95.66  ? 1602 GLU A CA    1 
ATOM   2304  C C     . GLU A 1 1602 ? 175.548 182.020 120.870 1.00 95.66  ? 1602 GLU A C     1 
ATOM   2305  O O     . GLU A 1 1602 ? 176.513 181.759 121.601 1.00 95.66  ? 1602 GLU A O     1 
ATOM   2306  C CB    . GLU A 1 1602 ? 174.034 180.108 120.266 1.00 95.66  ? 1602 GLU A CB    1 
ATOM   2307  C CG    . GLU A 1 1602 ? 175.086 179.042 120.528 1.00 95.66  ? 1602 GLU A CG    1 
ATOM   2308  C CD    . GLU A 1 1602 ? 175.399 178.213 119.297 1.00 95.66  ? 1602 GLU A CD    1 
ATOM   2309  O OE1   . GLU A 1 1602 ? 176.457 177.550 119.279 1.00 95.66  ? 1602 GLU A OE1   1 
ATOM   2310  O OE2   . GLU A 1 1602 ? 174.587 178.224 118.348 1.00 95.66  ? 1602 GLU A OE2   1 
ATOM   2311  N N     . ARG A 1 1603 ? 175.641 182.868 119.842 1.00 95.02  ? 1603 ARG A N     1 
ATOM   2312  C CA    . ARG A 1 1603 ? 176.881 183.601 119.604 1.00 95.02  ? 1603 ARG A CA    1 
ATOM   2313  C C     . ARG A 1 1603 ? 177.208 184.515 120.780 1.00 95.02  ? 1603 ARG A C     1 
ATOM   2314  O O     . ARG A 1 1603 ? 178.351 184.561 121.252 1.00 95.02  ? 1603 ARG A O     1 
ATOM   2315  C CB    . ARG A 1 1603 ? 176.772 184.401 118.305 1.00 95.02  ? 1603 ARG A CB    1 
ATOM   2316  C CG    . ARG A 1 1603 ? 177.827 185.481 118.144 1.00 95.02  ? 1603 ARG A CG    1 
ATOM   2317  C CD    . ARG A 1 1603 ? 177.625 186.251 116.853 1.00 95.02  ? 1603 ARG A CD    1 
ATOM   2318  N NE    . ARG A 1 1603 ? 176.289 186.831 116.770 1.00 95.02  ? 1603 ARG A NE    1 
ATOM   2319  C CZ    . ARG A 1 1603 ? 175.838 187.527 115.736 1.00 95.02  ? 1603 ARG A CZ    1 
ATOM   2320  N NH1   . ARG A 1 1603 ? 176.589 187.746 114.670 1.00 95.02  ? 1603 ARG A NH1   1 
ATOM   2321  N NH2   . ARG A 1 1603 ? 174.601 188.015 115.773 1.00 95.02  ? 1603 ARG A NH2   1 
ATOM   2322  N N     . LEU A 1 1604 ? 176.206 185.241 121.281 1.00 91.16  ? 1604 LEU A N     1 
ATOM   2323  C CA    . LEU A 1 1604 ? 176.421 186.079 122.454 1.00 91.16  ? 1604 LEU A CA    1 
ATOM   2324  C C     . LEU A 1 1604 ? 176.809 185.239 123.662 1.00 91.16  ? 1604 LEU A C     1 
ATOM   2325  O O     . LEU A 1 1604 ? 177.686 185.627 124.439 1.00 91.16  ? 1604 LEU A O     1 
ATOM   2326  C CB    . LEU A 1 1604 ? 175.171 186.905 122.757 1.00 91.16  ? 1604 LEU A CB    1 
ATOM   2327  C CG    . LEU A 1 1604 ? 174.768 187.963 121.731 1.00 91.16  ? 1604 LEU A CG    1 
ATOM   2328  C CD1   . LEU A 1 1604 ? 173.437 188.594 122.108 1.00 91.16  ? 1604 LEU A CD1   1 
ATOM   2329  C CD2   . LEU A 1 1604 ? 175.851 189.023 121.604 1.00 91.16  ? 1604 LEU A CD2   1 
ATOM   2330  N N     . ALA A 1 1605 ? 176.170 184.080 123.831 1.00 90.20  ? 1605 ALA A N     1 
ATOM   2331  C CA    . ALA A 1 1605 ? 176.472 183.221 124.970 1.00 90.20  ? 1605 ALA A CA    1 
ATOM   2332  C C     . ALA A 1 1605 ? 177.922 182.759 124.944 1.00 90.20  ? 1605 ALA A C     1 
ATOM   2333  O O     . ALA A 1 1605 ? 178.634 182.853 125.951 1.00 90.20  ? 1605 ALA A O     1 
ATOM   2334  C CB    . ALA A 1 1605 ? 175.526 182.020 124.985 1.00 90.20  ? 1605 ALA A CB    1 
ATOM   2335  N N     . ASP A 1 1606 ? 178.388 182.265 123.793 1.00 90.65  ? 1606 ASP A N     1 
ATOM   2336  C CA    . ASP A 1 1606 ? 179.748 181.738 123.746 1.00 90.65  ? 1606 ASP A CA    1 
ATOM   2337  C C     . ASP A 1 1606 ? 180.776 182.862 123.816 1.00 90.65  ? 1606 ASP A C     1 
ATOM   2338  O O     . ASP A 1 1606 ? 181.845 182.695 124.413 1.00 90.65  ? 1606 ASP A O     1 
ATOM   2339  C CB    . ASP A 1 1606 ? 179.942 180.837 122.514 1.00 90.65  ? 1606 ASP A CB    1 
ATOM   2340  C CG    . ASP A 1 1606 ? 180.098 181.599 121.194 1.00 90.65  ? 1606 ASP A CG    1 
ATOM   2341  O OD1   . ASP A 1 1606 ? 180.253 182.834 121.171 1.00 90.65  ? 1606 ASP A OD1   1 
ATOM   2342  O OD2   . ASP A 1 1606 ? 180.063 180.927 120.142 1.00 90.65  ? 1606 ASP A OD2   1 
ATOM   2343  N N     . LEU A 1 1607 ? 180.463 184.026 123.235 1.00 89.53  ? 1607 LEU A N     1 
ATOM   2344  C CA    . LEU A 1 1607 ? 181.364 185.168 123.361 1.00 89.53  ? 1607 LEU A CA    1 
ATOM   2345  C C     . LEU A 1 1607 ? 181.473 185.629 124.810 1.00 89.53  ? 1607 LEU A C     1 
ATOM   2346  O O     . LEU A 1 1607 ? 182.574 185.926 125.295 1.00 89.53  ? 1607 LEU A O     1 
ATOM   2347  C CB    . LEU A 1 1607 ? 180.886 186.312 122.468 1.00 89.53  ? 1607 LEU A CB    1 
ATOM   2348  C CG    . LEU A 1 1607 ? 181.392 186.309 121.025 1.00 89.53  ? 1607 LEU A CG    1 
ATOM   2349  C CD1   . LEU A 1 1607 ? 180.477 187.136 120.135 1.00 89.53  ? 1607 LEU A CD1   1 
ATOM   2350  C CD2   . LEU A 1 1607 ? 182.822 186.821 120.956 1.00 89.53  ? 1607 LEU A CD2   1 
ATOM   2351  N N     . LEU A 1 1608 ? 180.341 185.697 125.518 1.00 84.45  ? 1608 LEU A N     1 
ATOM   2352  C CA    . LEU A 1 1608 ? 180.366 186.076 126.926 1.00 84.45  ? 1608 LEU A CA    1 
ATOM   2353  C C     . LEU A 1 1608 ? 181.131 185.053 127.751 1.00 84.45  ? 1608 LEU A C     1 
ATOM   2354  O O     . LEU A 1 1608 ? 181.884 185.416 128.660 1.00 84.45  ? 1608 LEU A O     1 
ATOM   2355  C CB    . LEU A 1 1608 ? 178.944 186.237 127.459 1.00 84.45  ? 1608 LEU A CB    1 
ATOM   2356  C CG    . LEU A 1 1608 ? 178.193 187.489 127.009 1.00 84.45  ? 1608 LEU A CG    1 
ATOM   2357  C CD1   . LEU A 1 1608 ? 176.695 187.272 127.121 1.00 84.45  ? 1608 LEU A CD1   1 
ATOM   2358  C CD2   . LEU A 1 1608 ? 178.633 188.697 127.817 1.00 84.45  ? 1608 LEU A CD2   1 
ATOM   2359  N N     . GLY A 1 1609 ? 180.958 183.768 127.443 1.00 81.76  ? 1609 GLY A N     1 
ATOM   2360  C CA    . GLY A 1 1609 ? 181.738 182.753 128.128 1.00 81.76  ? 1609 GLY A CA    1 
ATOM   2361  C C     . GLY A 1 1609 ? 183.230 182.920 127.907 1.00 81.76  ? 1609 GLY A C     1 
ATOM   2362  O O     . GLY A 1 1609 ? 184.015 182.874 128.858 1.00 81.76  ? 1609 GLY A O     1 
ATOM   2363  N N     . LYS A 1 1610 ? 183.640 183.120 126.652 1.00 81.00  ? 1610 LYS A N     1 
ATOM   2364  C CA    . LYS A 1 1610 ? 185.063 183.255 126.355 1.00 81.00  ? 1610 LYS A CA    1 
ATOM   2365  C C     . LYS A 1 1610 ? 185.658 184.477 127.039 1.00 81.00  ? 1610 LYS A C     1 
ATOM   2366  O O     . LYS A 1 1610 ? 186.753 184.405 127.611 1.00 81.00  ? 1610 LYS A O     1 
ATOM   2367  C CB    . LYS A 1 1610 ? 185.292 183.324 124.843 1.00 81.00  ? 1610 LYS A CB    1 
ATOM   2368  C CG    . LYS A 1 1610 ? 184.884 182.078 124.063 1.00 81.00  ? 1610 LYS A CG    1 
ATOM   2369  C CD    . LYS A 1 1610 ? 184.994 180.810 124.897 1.00 81.00  ? 1610 LYS A CD    1 
ATOM   2370  C CE    . LYS A 1 1610 ? 186.388 180.208 124.800 1.00 81.00  ? 1610 LYS A CE    1 
ATOM   2371  N NZ    . LYS A 1 1610 ? 186.532 178.994 125.649 1.00 81.00  ? 1610 LYS A NZ    1 
ATOM   2372  N N     . ILE A 1 1611 ? 184.948 185.607 127.006 1.00 79.54  ? 1611 ILE A N     1 
ATOM   2373  C CA    . ILE A 1 1611 ? 185.465 186.788 127.689 1.00 79.54  ? 1611 ILE A CA    1 
ATOM   2374  C C     . ILE A 1 1611 ? 185.458 186.583 129.201 1.00 79.54  ? 1611 ILE A C     1 
ATOM   2375  O O     . ILE A 1 1611 ? 186.291 187.155 129.912 1.00 79.54  ? 1611 ILE A O     1 
ATOM   2376  C CB    . ILE A 1 1611 ? 184.684 188.047 127.269 1.00 79.54  ? 1611 ILE A CB    1 
ATOM   2377  C CG1   . ILE A 1 1611 ? 185.356 189.304 127.820 1.00 79.54  ? 1611 ILE A CG1   1 
ATOM   2378  C CG2   . ILE A 1 1611 ? 183.255 187.981 127.726 1.00 79.54  ? 1611 ILE A CG2   1 
ATOM   2379  C CD1   . ILE A 1 1611 ? 184.817 190.570 127.227 1.00 79.54  ? 1611 ILE A CD1   1 
ATOM   2380  N N     . GLN A 1 1612 ? 184.549 185.751 129.720 1.00 76.95  ? 1612 GLN A N     1 
ATOM   2381  C CA    . GLN A 1 1612 ? 184.552 185.473 131.152 1.00 76.95  ? 1612 GLN A CA    1 
ATOM   2382  C C     . GLN A 1 1612 ? 185.769 184.647 131.556 1.00 76.95  ? 1612 GLN A C     1 
ATOM   2383  O O     . GLN A 1 1612 ? 186.414 184.942 132.569 1.00 76.95  ? 1612 GLN A O     1 
ATOM   2384  C CB    . GLN A 1 1612 ? 183.259 184.766 131.555 1.00 76.95  ? 1612 GLN A CB    1 
ATOM   2385  C CG    . GLN A 1 1612 ? 183.331 184.070 132.902 1.00 76.95  ? 1612 GLN A CG    1 
ATOM   2386  C CD    . GLN A 1 1612 ? 182.875 184.964 134.039 1.00 76.95  ? 1612 GLN A CD    1 
ATOM   2387  O OE1   . GLN A 1 1612 ? 181.804 185.569 133.977 1.00 76.95  ? 1612 GLN A OE1   1 
ATOM   2388  N NE2   . GLN A 1 1612 ? 183.688 185.054 135.085 1.00 76.95  ? 1612 GLN A NE2   1 
ATOM   2389  N N     . LYS A 1 1613 ? 186.101 183.607 130.782 1.00 73.45  ? 1613 LYS A N     1 
ATOM   2390  C CA    . LYS A 1 1613 ? 187.351 182.895 131.052 1.00 73.45  ? 1613 LYS A CA    1 
ATOM   2391  C C     . LYS A 1 1613 ? 188.563 183.802 130.868 1.00 73.45  ? 1613 LYS A C     1 
ATOM   2392  O O     . LYS A 1 1613 ? 189.554 183.669 131.593 1.00 73.45  ? 1613 LYS A O     1 
ATOM   2393  C CB    . LYS A 1 1613 ? 187.513 181.624 130.203 1.00 73.45  ? 1613 LYS A CB    1 
ATOM   2394  C CG    . LYS A 1 1613 ? 186.817 180.360 130.747 1.00 73.45  ? 1613 LYS A CG    1 
ATOM   2395  C CD    . LYS A 1 1613 ? 185.314 180.300 130.609 1.00 73.45  ? 1613 LYS A CD    1 
ATOM   2396  C CE    . LYS A 1 1613 ? 184.934 180.128 129.149 1.00 73.45  ? 1613 LYS A CE    1 
ATOM   2397  N NZ    . LYS A 1 1613 ? 183.462 179.999 128.968 1.00 73.45  ? 1613 LYS A NZ    1 
ATOM   2398  N N     . ALA A 1 1614 ? 188.516 184.728 129.906 1.00 72.09  ? 1614 ALA A N     1 
ATOM   2399  C CA    . ALA A 1 1614 ? 189.630 185.662 129.752 1.00 72.09  ? 1614 ALA A CA    1 
ATOM   2400  C C     . ALA A 1 1614 ? 189.790 186.537 130.991 1.00 72.09  ? 1614 ALA A C     1 
ATOM   2401  O O     . ALA A 1 1614 ? 190.910 186.752 131.473 1.00 72.09  ? 1614 ALA A O     1 
ATOM   2402  C CB    . ALA A 1 1614 ? 189.432 186.522 128.505 1.00 72.09  ? 1614 ALA A CB    1 
ATOM   2403  N N     . LEU A 1 1615 ? 188.677 187.043 131.525 1.00 67.48  ? 1615 LEU A N     1 
ATOM   2404  C CA    . LEU A 1 1615 ? 188.731 187.845 132.743 1.00 67.48  ? 1615 LEU A CA    1 
ATOM   2405  C C     . LEU A 1 1615 ? 189.224 187.018 133.924 1.00 67.48  ? 1615 LEU A C     1 
ATOM   2406  O O     . LEU A 1 1615 ? 189.992 187.510 134.759 1.00 67.48  ? 1615 LEU A O     1 
ATOM   2407  C CB    . LEU A 1 1615 ? 187.356 188.444 133.036 1.00 67.48  ? 1615 LEU A CB    1 
ATOM   2408  C CG    . LEU A 1 1615 ? 187.164 189.109 134.401 1.00 67.48  ? 1615 LEU A CG    1 
ATOM   2409  C CD1   . LEU A 1 1615 ? 187.887 190.446 134.460 1.00 67.48  ? 1615 LEU A CD1   1 
ATOM   2410  C CD2   . LEU A 1 1615 ? 185.686 189.287 134.698 1.00 67.48  ? 1615 LEU A CD2   1 
ATOM   2411  N N     . GLY A 1 1616 ? 188.786 185.761 134.015 1.00 65.91  ? 1616 GLY A N     1 
ATOM   2412  C CA    . GLY A 1 1616 ? 189.278 184.893 135.073 1.00 65.91  ? 1616 GLY A CA    1 
ATOM   2413  C C     . GLY A 1 1616 ? 190.771 184.644 134.974 1.00 65.91  ? 1616 GLY A C     1 
ATOM   2414  O O     . GLY A 1 1616 ? 191.474 184.612 135.986 1.00 65.91  ? 1616 GLY A O     1 
ATOM   2415  N N     . GLU A 1 1617 ? 191.276 184.467 133.751 1.00 67.80  ? 1617 GLU A N     1 
ATOM   2416  C CA    . GLU A 1 1617 ? 192.713 184.304 133.558 1.00 67.80  ? 1617 GLU A CA    1 
ATOM   2417  C C     . GLU A 1 1617 ? 193.467 185.569 133.949 1.00 67.80  ? 1617 GLU A C     1 
ATOM   2418  O O     . GLU A 1 1617 ? 194.553 185.498 134.536 1.00 67.80  ? 1617 GLU A O     1 
ATOM   2419  C CB    . GLU A 1 1617 ? 193.008 183.929 132.106 1.00 67.80  ? 1617 GLU A CB    1 
ATOM   2420  C CG    . GLU A 1 1617 ? 194.466 183.594 131.832 1.00 67.80  ? 1617 GLU A CG    1 
ATOM   2421  C CD    . GLU A 1 1617 ? 195.105 182.793 132.950 1.00 67.80  ? 1617 GLU A CD    1 
ATOM   2422  O OE1   . GLU A 1 1617 ? 194.612 181.685 133.249 1.00 67.80  ? 1617 GLU A OE1   1 
ATOM   2423  O OE2   . GLU A 1 1617 ? 196.102 183.272 133.530 1.00 67.80  ? 1617 GLU A OE2   1 
ATOM   2424  N N     . TYR A 1 1618 ? 192.910 186.738 133.623 1.00 61.75  ? 1618 TYR A N     1 
ATOM   2425  C CA    . TYR A 1 1618 ? 193.537 187.987 134.047 1.00 61.75  ? 1618 TYR A CA    1 
ATOM   2426  C C     . TYR A 1 1618 ? 193.571 188.094 135.567 1.00 61.75  ? 1618 TYR A C     1 
ATOM   2427  O O     . TYR A 1 1618 ? 194.576 188.524 136.148 1.00 61.75  ? 1618 TYR A O     1 
ATOM   2428  C CB    . TYR A 1 1618 ? 192.804 189.185 133.446 1.00 61.75  ? 1618 TYR A CB    1 
ATOM   2429  C CG    . TYR A 1 1618 ? 193.378 190.513 133.881 1.00 61.75  ? 1618 TYR A CG    1 
ATOM   2430  C CD1   . TYR A 1 1618 ? 194.581 190.973 133.365 1.00 61.75  ? 1618 TYR A CD1   1 
ATOM   2431  C CD2   . TYR A 1 1618 ? 192.722 191.305 134.813 1.00 61.75  ? 1618 TYR A CD2   1 
ATOM   2432  C CE1   . TYR A 1 1618 ? 195.114 192.183 133.762 1.00 61.75  ? 1618 TYR A CE1   1 
ATOM   2433  C CE2   . TYR A 1 1618 ? 193.247 192.518 135.215 1.00 61.75  ? 1618 TYR A CE2   1 
ATOM   2434  C CZ    . TYR A 1 1618 ? 194.443 192.952 134.686 1.00 61.75  ? 1618 TYR A CZ    1 
ATOM   2435  O OH    . TYR A 1 1618 ? 194.971 194.158 135.084 1.00 61.75  ? 1618 TYR A OH    1 
ATOM   2436  N N     . LEU A 1 1619 ? 192.481 187.705 136.229 1.00 58.32  ? 1619 LEU A N     1 
ATOM   2437  C CA    . LEU A 1 1619 ? 192.457 187.722 137.688 1.00 58.32  ? 1619 LEU A CA    1 
ATOM   2438  C C     . LEU A 1 1619 ? 193.489 186.759 138.261 1.00 58.32  ? 1619 LEU A C     1 
ATOM   2439  O O     . LEU A 1 1619 ? 194.157 187.068 139.255 1.00 58.32  ? 1619 LEU A O     1 
ATOM   2440  C CB    . LEU A 1 1619 ? 191.058 187.375 138.195 1.00 58.32  ? 1619 LEU A CB    1 
ATOM   2441  C CG    . LEU A 1 1619 ? 189.944 188.375 137.871 1.00 58.32  ? 1619 LEU A CG    1 
ATOM   2442  C CD1   . LEU A 1 1619 ? 188.591 187.839 138.312 1.00 58.32  ? 1619 LEU A CD1   1 
ATOM   2443  C CD2   . LEU A 1 1619 ? 190.218 189.734 138.490 1.00 58.32  ? 1619 LEU A CD2   1 
ATOM   2444  N N     . GLU A 1 1620 ? 193.630 185.582 137.646 1.00 56.55  ? 1620 GLU A N     1 
ATOM   2445  C CA    . GLU A 1 1620 ? 194.618 184.614 138.111 1.00 56.55  ? 1620 GLU A CA    1 
ATOM   2446  C C     . GLU A 1 1620 ? 196.038 185.143 137.946 1.00 56.55  ? 1620 GLU A C     1 
ATOM   2447  O O     . GLU A 1 1620 ? 196.887 184.941 138.822 1.00 56.55  ? 1620 GLU A O     1 
ATOM   2448  C CB    . GLU A 1 1620 ? 194.451 183.291 137.366 1.00 56.55  ? 1620 GLU A CB    1 
ATOM   2449  C CG    . GLU A 1 1620 ? 195.173 182.125 138.018 1.00 56.55  ? 1620 GLU A CG    1 
ATOM   2450  C CD    . GLU A 1 1620 ? 196.545 181.886 137.419 1.00 56.55  ? 1620 GLU A CD    1 
ATOM   2451  O OE1   . GLU A 1 1620 ? 196.915 182.606 136.468 1.00 56.55  ? 1620 GLU A OE1   1 
ATOM   2452  O OE2   . GLU A 1 1620 ? 197.256 180.980 137.900 1.00 56.55  ? 1620 GLU A OE2   1 
ATOM   2453  N N     . ARG A 1 1621 ? 196.322 185.810 136.825 1.00 55.54  ? 1621 ARG A N     1 
ATOM   2454  C CA    . ARG A 1 1621 ? 197.658 186.369 136.638 1.00 55.54  ? 1621 ARG A CA    1 
ATOM   2455  C C     . ARG A 1 1621 ? 197.909 187.515 137.611 1.00 55.54  ? 1621 ARG A C     1 
ATOM   2456  O O     . ARG A 1 1621 ? 199.042 187.716 138.067 1.00 55.54  ? 1621 ARG A O     1 
ATOM   2457  C CB    . ARG A 1 1621 ? 197.857 186.818 135.187 1.00 55.54  ? 1621 ARG A CB    1 
ATOM   2458  C CG    . ARG A 1 1621 ? 197.393 188.230 134.866 1.00 55.54  ? 1621 ARG A CG    1 
ATOM   2459  C CD    . ARG A 1 1621 ? 197.659 188.587 133.411 1.00 55.54  ? 1621 ARG A CD    1 
ATOM   2460  N NE    . ARG A 1 1621 ? 197.627 190.027 133.180 1.00 55.54  ? 1621 ARG A NE    1 
ATOM   2461  C CZ    . ARG A 1 1621 ? 198.561 190.878 133.582 1.00 55.54  ? 1621 ARG A CZ    1 
ATOM   2462  N NH1   . ARG A 1 1621 ? 199.639 190.468 134.231 1.00 55.54  ? 1621 ARG A NH1   1 
ATOM   2463  N NH2   . ARG A 1 1621 ? 198.412 192.174 133.322 1.00 55.54  ? 1621 ARG A NH2   1 
ATOM   2464  N N     . GLU A 1 1622 ? 196.861 188.272 137.951 1.00 50.65  ? 1622 GLU A N     1 
ATOM   2465  C CA    . GLU A 1 1622 ? 197.001 189.307 138.970 1.00 50.65  ? 1622 GLU A CA    1 
ATOM   2466  C C     . GLU A 1 1622 ? 197.300 188.696 140.334 1.00 50.65  ? 1622 GLU A C     1 
ATOM   2467  O O     . GLU A 1 1622 ? 198.108 189.233 141.100 1.00 50.65  ? 1622 GLU A O     1 
ATOM   2468  C CB    . GLU A 1 1622 ? 195.736 190.165 139.026 1.00 50.65  ? 1622 GLU A CB    1 
ATOM   2469  C CG    . GLU A 1 1622 ? 195.630 191.200 137.911 1.00 50.65  ? 1622 GLU A CG    1 
ATOM   2470  C CD    . GLU A 1 1622 ? 196.464 192.446 138.164 1.00 50.65  ? 1622 GLU A CD    1 
ATOM   2471  O OE1   . GLU A 1 1622 ? 197.372 192.406 139.022 1.00 50.65  ? 1622 GLU A OE1   1 
ATOM   2472  O OE2   . GLU A 1 1622 ? 196.211 193.472 137.499 1.00 50.65  ? 1622 GLU A OE2   1 
ATOM   2473  N N     . ARG A 1 1623 ? 196.649 187.575 140.656 1.00 39.11  ? 1623 ARG A N     1 
ATOM   2474  C CA    . ARG A 1 1623 ? 196.978 186.852 141.882 1.00 39.11  ? 1623 ARG A CA    1 
ATOM   2475  C C     . ARG A 1 1623 ? 198.423 186.373 141.870 1.00 39.11  ? 1623 ARG A C     1 
ATOM   2476  O O     . ARG A 1 1623 ? 199.138 186.502 142.869 1.00 39.11  ? 1623 ARG A O     1 
ATOM   2477  C CB    . ARG A 1 1623 ? 196.043 185.657 142.071 1.00 39.11  ? 1623 ARG A CB    1 
ATOM   2478  C CG    . ARG A 1 1623 ? 194.905 185.875 143.046 1.00 39.11  ? 1623 ARG A CG    1 
ATOM   2479  C CD    . ARG A 1 1623 ? 193.850 186.785 142.482 1.00 39.11  ? 1623 ARG A CD    1 
ATOM   2480  N NE    . ARG A 1 1623 ? 192.636 186.769 143.289 1.00 39.11  ? 1623 ARG A NE    1 
ATOM   2481  C CZ    . ARG A 1 1623 ? 191.616 185.947 143.087 1.00 39.11  ? 1623 ARG A CZ    1 
ATOM   2482  N NH1   . ARG A 1 1623 ? 191.633 185.049 142.116 1.00 39.11  ? 1623 ARG A NH1   1 
ATOM   2483  N NH2   . ARG A 1 1623 ? 190.551 186.028 143.879 1.00 39.11  ? 1623 ARG A NH2   1 
ATOM   2484  N N     . SER A 1 1624 ? 198.865 185.805 140.748 1.00 40.36  ? 1624 SER A N     1 
ATOM   2485  C CA    . SER A 1 1624 ? 200.209 185.240 140.684 1.00 40.36  ? 1624 SER A CA    1 
ATOM   2486  C C     . SER A 1 1624 ? 201.274 186.323 140.803 1.00 40.36  ? 1624 SER A C     1 
ATOM   2487  O O     . SER A 1 1624 ? 202.309 186.113 141.445 1.00 40.36  ? 1624 SER A O     1 
ATOM   2488  C CB    . SER A 1 1624 ? 200.386 184.452 139.388 1.00 40.36  ? 1624 SER A CB    1 
ATOM   2489  O OG    . SER A 1 1624 ? 201.476 183.552 139.487 1.00 40.36  ? 1624 SER A OG    1 
ATOM   2490  N N     . SER A 1 1625 ? 201.046 187.483 140.183 1.00 37.46  ? 1625 SER A N     1 
ATOM   2491  C CA    . SER A 1 1625 ? 202.032 188.557 140.254 1.00 37.46  ? 1625 SER A CA    1 
ATOM   2492  C C     . SER A 1 1625 ? 202.168 189.096 141.674 1.00 37.46  ? 1625 SER A C     1 
ATOM   2493  O O     . SER A 1 1625 ? 203.284 189.322 142.155 1.00 37.46  ? 1625 SER A O     1 
ATOM   2494  C CB    . SER A 1 1625 ? 201.656 189.676 139.286 1.00 37.46  ? 1625 SER A CB    1 
ATOM   2495  O OG    . SER A 1 1625 ? 202.598 190.732 139.340 1.00 37.46  ? 1625 SER A OG    1 
ATOM   2496  N N     . PHE A 1 1626 ? 201.047 189.309 142.358 1.00 31.30  ? 1626 PHE A N     1 
ATOM   2497  C CA    . PHE A 1 1626 ? 201.043 189.754 143.752 1.00 31.30  ? 1626 PHE A CA    1 
ATOM   2498  C C     . PHE A 1 1626 ? 200.378 188.682 144.601 1.00 31.30  ? 1626 PHE A C     1 
ATOM   2499  O O     . PHE A 1 1626 ? 199.137 188.609 144.652 1.00 31.30  ? 1626 PHE A O     1 
ATOM   2500  C CB    . PHE A 1 1626 ? 200.320 191.090 143.905 1.00 31.30  ? 1626 PHE A CB    1 
ATOM   2501  C CG    . PHE A 1 1626 ? 200.568 191.766 145.223 1.00 31.30  ? 1626 PHE A CG    1 
ATOM   2502  C CD1   . PHE A 1 1626 ? 201.855 192.068 145.628 1.00 31.30  ? 1626 PHE A CD1   1 
ATOM   2503  C CD2   . PHE A 1 1626 ? 199.514 192.103 146.053 1.00 31.30  ? 1626 PHE A CD2   1 
ATOM   2504  C CE1   . PHE A 1 1626 ? 202.087 192.691 146.838 1.00 31.30  ? 1626 PHE A CE1   1 
ATOM   2505  C CE2   . PHE A 1 1626 ? 199.740 192.726 147.264 1.00 31.30  ? 1626 PHE A CE2   1 
ATOM   2506  C CZ    . PHE A 1 1626 ? 201.028 193.020 147.656 1.00 31.30  ? 1626 PHE A CZ    1 
ATOM   2507  N N     . PRO A 1 1627 ? 201.151 187.835 145.285 1.00 27.07  ? 1627 PRO A N     1 
ATOM   2508  C CA    . PRO A 1 1627 ? 200.552 186.674 145.965 1.00 27.07  ? 1627 PRO A CA    1 
ATOM   2509  C C     . PRO A 1 1627 ? 199.533 187.035 147.030 1.00 27.07  ? 1627 PRO A C     1 
ATOM   2510  O O     . PRO A 1 1627 ? 198.628 186.236 147.299 1.00 27.07  ? 1627 PRO A O     1 
ATOM   2511  C CB    . PRO A 1 1627 ? 201.769 185.962 146.572 1.00 27.07  ? 1627 PRO A CB    1 
ATOM   2512  C CG    . PRO A 1 1627 ? 202.942 186.460 145.786 1.00 27.07  ? 1627 PRO A CG    1 
ATOM   2513  C CD    . PRO A 1 1627 ? 202.613 187.875 145.443 1.00 27.07  ? 1627 PRO A CD    1 
ATOM   2514  N N     . ARG A 1 1628 ? 199.645 188.214 147.646 1.00 23.61  ? 1628 ARG A N     1 
ATOM   2515  C CA    . ARG A 1 1628 ? 198.716 188.585 148.706 1.00 23.61  ? 1628 ARG A CA    1 
ATOM   2516  C C     . ARG A 1 1628 ? 197.298 188.792 148.192 1.00 23.61  ? 1628 ARG A C     1 
ATOM   2517  O O     . ARG A 1 1628 ? 196.362 188.844 148.996 1.00 23.61  ? 1628 ARG A O     1 
ATOM   2518  C CB    . ARG A 1 1628 ? 199.206 189.847 149.415 1.00 23.61  ? 1628 ARG A CB    1 
ATOM   2519  C CG    . ARG A 1 1628 ? 200.453 189.628 150.250 1.00 23.61  ? 1628 ARG A CG    1 
ATOM   2520  C CD    . ARG A 1 1628 ? 200.489 190.559 151.445 1.00 23.61  ? 1628 ARG A CD    1 
ATOM   2521  N NE    . ARG A 1 1628 ? 201.845 190.739 151.946 1.00 23.61  ? 1628 ARG A NE    1 
ATOM   2522  C CZ    . ARG A 1 1628 ? 202.271 190.304 153.124 1.00 23.61  ? 1628 ARG A CZ    1 
ATOM   2523  N NH1   . ARG A 1 1628 ? 201.469 189.655 153.951 1.00 23.61  ? 1628 ARG A NH1   1 
ATOM   2524  N NH2   . ARG A 1 1628 ? 203.533 190.524 153.479 1.00 23.61  ? 1628 ARG A NH2   1 
ATOM   2525  N N     . PHE A 1 1629 ? 197.117 188.914 146.876 1.00 30.67  ? 1629 PHE A N     1 
ATOM   2526  C CA    . PHE A 1 1629 ? 195.782 189.023 146.301 1.00 30.67  ? 1629 PHE A CA    1 
ATOM   2527  C C     . PHE A 1 1629 ? 194.956 187.756 146.471 1.00 30.67  ? 1629 PHE A C     1 
ATOM   2528  O O     . PHE A 1 1629 ? 193.740 187.801 146.267 1.00 30.67  ? 1629 PHE A O     1 
ATOM   2529  C CB    . PHE A 1 1629 ? 195.873 189.371 144.815 1.00 30.67  ? 1629 PHE A CB    1 
ATOM   2530  C CG    . PHE A 1 1629 ? 196.103 190.829 144.546 1.00 30.67  ? 1629 PHE A CG    1 
ATOM   2531  C CD1   . PHE A 1 1629 ? 195.825 191.778 145.513 1.00 30.67  ? 1629 PHE A CD1   1 
ATOM   2532  C CD2   . PHE A 1 1629 ? 196.583 191.251 143.319 1.00 30.67  ? 1629 PHE A CD2   1 
ATOM   2533  C CE1   . PHE A 1 1629 ? 196.029 193.119 145.263 1.00 30.67  ? 1629 PHE A CE1   1 
ATOM   2534  C CE2   . PHE A 1 1629 ? 196.789 192.590 143.065 1.00 30.67  ? 1629 PHE A CE2   1 
ATOM   2535  C CZ    . PHE A 1 1629 ? 196.512 193.525 144.037 1.00 30.67  ? 1629 PHE A CZ    1 
ATOM   2536  N N     . TYR A 1 1630 ? 195.580 186.631 146.824 1.00 28.03  ? 1630 TYR A N     1 
ATOM   2537  C CA    . TYR A 1 1630 ? 194.830 185.396 147.012 1.00 28.03  ? 1630 TYR A CA    1 
ATOM   2538  C C     . TYR A 1 1630 ? 193.905 185.455 148.220 1.00 28.03  ? 1630 TYR A C     1 
ATOM   2539  O O     . TYR A 1 1630 ? 192.945 184.682 148.285 1.00 28.03  ? 1630 TYR A O     1 
ATOM   2540  C CB    . TYR A 1 1630 ? 195.791 184.217 147.152 1.00 28.03  ? 1630 TYR A CB    1 
ATOM   2541  C CG    . TYR A 1 1630 ? 196.291 183.673 145.835 1.00 28.03  ? 1630 TYR A CG    1 
ATOM   2542  C CD1   . TYR A 1 1630 ? 195.437 183.007 144.968 1.00 28.03  ? 1630 TYR A CD1   1 
ATOM   2543  C CD2   . TYR A 1 1630 ? 197.618 183.826 145.457 1.00 28.03  ? 1630 TYR A CD2   1 
ATOM   2544  C CE1   . TYR A 1 1630 ? 195.889 182.509 143.762 1.00 28.03  ? 1630 TYR A CE1   1 
ATOM   2545  C CE2   . TYR A 1 1630 ? 198.079 183.331 144.253 1.00 28.03  ? 1630 TYR A CE2   1 
ATOM   2546  C CZ    . TYR A 1 1630 ? 197.210 182.674 143.410 1.00 28.03  ? 1630 TYR A CZ    1 
ATOM   2547  O OH    . TYR A 1 1630 ? 197.664 182.178 142.210 1.00 28.03  ? 1630 TYR A OH    1 
ATOM   2548  N N     . PHE A 1 1631 ? 194.170 186.348 149.174 1.00 22.52  ? 1631 PHE A N     1 
ATOM   2549  C CA    . PHE A 1 1631 ? 193.329 186.421 150.364 1.00 22.52  ? 1631 PHE A CA    1 
ATOM   2550  C C     . PHE A 1 1631 ? 192.006 187.118 150.073 1.00 22.52  ? 1631 PHE A C     1 
ATOM   2551  O O     . PHE A 1 1631 ? 190.973 186.763 150.652 1.00 22.52  ? 1631 PHE A O     1 
ATOM   2552  C CB    . PHE A 1 1631 ? 194.080 187.128 151.491 1.00 22.52  ? 1631 PHE A CB    1 
ATOM   2553  C CG    . PHE A 1 1631 ? 195.426 186.533 151.784 1.00 22.52  ? 1631 PHE A CG    1 
ATOM   2554  C CD1   . PHE A 1 1631 ? 195.570 185.168 151.953 1.00 22.52  ? 1631 PHE A CD1   1 
ATOM   2555  C CD2   . PHE A 1 1631 ? 196.546 187.336 151.886 1.00 22.52  ? 1631 PHE A CD2   1 
ATOM   2556  C CE1   . PHE A 1 1631 ? 196.805 184.616 152.220 1.00 22.52  ? 1631 PHE A CE1   1 
ATOM   2557  C CE2   . PHE A 1 1631 ? 197.784 186.789 152.154 1.00 22.52  ? 1631 PHE A CE2   1 
ATOM   2558  C CZ    . PHE A 1 1631 ? 197.913 185.428 152.321 1.00 22.52  ? 1631 PHE A CZ    1 
ATOM   2559  N N     . VAL A 1 1632 ? 192.012 188.110 149.183 1.00 29.71  ? 1632 VAL A N     1 
ATOM   2560  C CA    . VAL A 1 1632 ? 190.783 188.818 148.850 1.00 29.71  ? 1632 VAL A CA    1 
ATOM   2561  C C     . VAL A 1 1632 ? 190.006 188.040 147.792 1.00 29.71  ? 1632 VAL A C     1 
ATOM   2562  O O     . VAL A 1 1632 ? 190.559 187.245 147.028 1.00 29.71  ? 1632 VAL A O     1 
ATOM   2563  C CB    . VAL A 1 1632 ? 191.075 190.255 148.387 1.00 29.71  ? 1632 VAL A CB    1 
ATOM   2564  C CG1   . VAL A 1 1632 ? 191.742 191.041 149.501 1.00 29.71  ? 1632 VAL A CG1   1 
ATOM   2565  C CG2   . VAL A 1 1632 ? 191.941 190.249 147.146 1.00 29.71  ? 1632 VAL A CG2   1 
ATOM   2566  N N     . GLY A 1 1633 ? 188.696 188.282 147.749 1.00 38.55  ? 1633 GLY A N     1 
ATOM   2567  C CA    . GLY A 1 1633 ? 187.829 187.545 146.856 1.00 38.55  ? 1633 GLY A CA    1 
ATOM   2568  C C     . GLY A 1 1633 ? 187.901 188.028 145.421 1.00 38.55  ? 1633 GLY A C     1 
ATOM   2569  O O     . GLY A 1 1633 ? 188.546 189.025 145.097 1.00 38.55  ? 1633 GLY A O     1 
ATOM   2570  N N     . ASP A 1 1634 ? 187.222 187.283 144.545 1.00 44.48  ? 1634 ASP A N     1 
ATOM   2571  C CA    . ASP A 1 1634 ? 187.201 187.643 143.130 1.00 44.48  ? 1634 ASP A CA    1 
ATOM   2572  C C     . ASP A 1 1634 ? 186.528 188.993 142.914 1.00 44.48  ? 1634 ASP A C     1 
ATOM   2573  O O     . ASP A 1 1634 ? 187.036 189.833 142.163 1.00 44.48  ? 1634 ASP A O     1 
ATOM   2574  C CB    . ASP A 1 1634 ? 186.496 186.554 142.323 1.00 44.48  ? 1634 ASP A CB    1 
ATOM   2575  C CG    . ASP A 1 1634 ? 187.467 185.568 141.705 1.00 44.48  ? 1634 ASP A CG    1 
ATOM   2576  O OD1   . ASP A 1 1634 ? 188.645 185.552 142.120 1.00 44.48  ? 1634 ASP A OD1   1 
ATOM   2577  O OD2   . ASP A 1 1634 ? 187.054 184.811 140.802 1.00 44.48  ? 1634 ASP A OD2   1 
ATOM   2578  N N     . GLU A 1 1635 ? 185.384 189.220 143.563 1.00 50.40  ? 1635 GLU A N     1 
ATOM   2579  C CA    . GLU A 1 1635 ? 184.738 190.525 143.479 1.00 50.40  ? 1635 GLU A CA    1 
ATOM   2580  C C     . GLU A 1 1635 ? 185.603 191.602 144.121 1.00 50.40  ? 1635 GLU A C     1 
ATOM   2581  O O     . GLU A 1 1635 ? 185.700 192.724 143.608 1.00 50.40  ? 1635 GLU A O     1 
ATOM   2582  C CB    . GLU A 1 1635 ? 183.363 190.473 144.143 1.00 50.40  ? 1635 GLU A CB    1 
ATOM   2583  C CG    . GLU A 1 1635 ? 182.439 189.411 143.571 1.00 50.40  ? 1635 GLU A CG    1 
ATOM   2584  C CD    . GLU A 1 1635 ? 181.715 189.877 142.323 1.00 50.40  ? 1635 GLU A CD    1 
ATOM   2585  O OE1   . GLU A 1 1635 ? 182.160 189.525 141.210 1.00 50.40  ? 1635 GLU A OE1   1 
ATOM   2586  O OE2   . GLU A 1 1635 ? 180.701 190.593 142.455 1.00 50.40  ? 1635 GLU A OE2   1 
ATOM   2587  N N     . ASP A 1 1636 ? 186.242 191.273 145.245 1.00 46.31  ? 1636 ASP A N     1 
ATOM   2588  C CA    . ASP A 1 1636 ? 187.147 192.220 145.885 1.00 46.31  ? 1636 ASP A CA    1 
ATOM   2589  C C     . ASP A 1 1636 ? 188.319 192.557 144.974 1.00 46.31  ? 1636 ASP A C     1 
ATOM   2590  O O     . ASP A 1 1636 ? 188.724 193.720 144.880 1.00 46.31  ? 1636 ASP A O     1 
ATOM   2591  C CB    . ASP A 1 1636 ? 187.643 191.654 147.215 1.00 46.31  ? 1636 ASP A CB    1 
ATOM   2592  C CG    . ASP A 1 1636 ? 186.512 191.340 148.174 1.00 46.31  ? 1636 ASP A CG    1 
ATOM   2593  O OD1   . ASP A 1 1636 ? 185.406 191.890 147.991 1.00 46.31  ? 1636 ASP A OD1   1 
ATOM   2594  O OD2   . ASP A 1 1636 ? 186.727 190.542 149.110 1.00 46.31  ? 1636 ASP A OD2   1 
ATOM   2595  N N     . LEU A 1 1637 ? 188.872 191.556 144.286 1.00 45.34  ? 1637 LEU A N     1 
ATOM   2596  C CA    . LEU A 1 1637 ? 189.968 191.826 143.362 1.00 45.34  ? 1637 LEU A CA    1 
ATOM   2597  C C     . LEU A 1 1637 ? 189.504 192.653 142.171 1.00 45.34  ? 1637 LEU A C     1 
ATOM   2598  O O     . LEU A 1 1637 ? 190.248 193.509 141.678 1.00 45.34  ? 1637 LEU A O     1 
ATOM   2599  C CB    . LEU A 1 1637 ? 190.600 190.525 142.880 1.00 45.34  ? 1637 LEU A CB    1 
ATOM   2600  C CG    . LEU A 1 1637 ? 191.951 190.800 142.224 1.00 45.34  ? 1637 LEU A CG    1 
ATOM   2601  C CD1   . LEU A 1 1637 ? 193.002 191.058 143.281 1.00 45.34  ? 1637 LEU A CD1   1 
ATOM   2602  C CD2   . LEU A 1 1637 ? 192.364 189.673 141.305 1.00 45.34  ? 1637 LEU A CD2   1 
ATOM   2603  N N     . LEU A 1 1638 ? 188.293 192.393 141.674 1.00 50.74  ? 1638 LEU A N     1 
ATOM   2604  C CA    . LEU A 1 1638 ? 187.760 193.205 140.586 1.00 50.74  ? 1638 LEU A CA    1 
ATOM   2605  C C     . LEU A 1 1638 ? 187.624 194.659 141.013 1.00 50.74  ? 1638 LEU A C     1 
ATOM   2606  O O     . LEU A 1 1638 ? 187.985 195.572 140.262 1.00 50.74  ? 1638 LEU A O     1 
ATOM   2607  C CB    . LEU A 1 1638 ? 186.412 192.651 140.126 1.00 50.74  ? 1638 LEU A CB    1 
ATOM   2608  C CG    . LEU A 1 1638 ? 186.456 191.392 139.260 1.00 50.74  ? 1638 LEU A CG    1 
ATOM   2609  C CD1   . LEU A 1 1638 ? 185.053 190.857 139.027 1.00 50.74  ? 1638 LEU A CD1   1 
ATOM   2610  C CD2   . LEU A 1 1638 ? 187.149 191.682 137.941 1.00 50.74  ? 1638 LEU A CD2   1 
ATOM   2611  N N     . GLU A 1 1639 ? 187.119 194.890 142.227 1.00 52.11  ? 1639 GLU A N     1 
ATOM   2612  C CA    . GLU A 1 1639 ? 187.041 196.252 142.746 1.00 52.11  ? 1639 GLU A CA    1 
ATOM   2613  C C     . GLU A 1 1639 ? 188.428 196.862 142.904 1.00 52.11  ? 1639 GLU A C     1 
ATOM   2614  O O     . GLU A 1 1639 ? 188.629 198.047 142.618 1.00 52.11  ? 1639 GLU A O     1 
ATOM   2615  C CB    . GLU A 1 1639 ? 186.294 196.264 144.080 1.00 52.11  ? 1639 GLU A CB    1 
ATOM   2616  C CG    . GLU A 1 1639 ? 184.837 195.846 143.980 1.00 52.11  ? 1639 GLU A CG    1 
ATOM   2617  C CD    . GLU A 1 1639 ? 184.094 195.999 145.293 1.00 52.11  ? 1639 GLU A CD    1 
ATOM   2618  O OE1   . GLU A 1 1639 ? 184.126 195.056 146.110 1.00 52.11  ? 1639 GLU A OE1   1 
ATOM   2619  O OE2   . GLU A 1 1639 ? 183.476 197.063 145.506 1.00 52.11  ? 1639 GLU A OE2   1 
ATOM   2620  N N     . ILE A 1 1640 ? 189.397 196.067 143.360 1.00 48.82  ? 1640 ILE A N     1 
ATOM   2621  C CA    . ILE A 1 1640 ? 190.746 196.577 143.586 1.00 48.82  ? 1640 ILE A CA    1 
ATOM   2622  C C     . ILE A 1 1640 ? 191.382 197.019 142.273 1.00 48.82  ? 1640 ILE A C     1 
ATOM   2623  O O     . ILE A 1 1640 ? 191.904 198.134 142.162 1.00 48.82  ? 1640 ILE A O     1 
ATOM   2624  C CB    . ILE A 1 1640 ? 191.603 195.513 144.297 1.00 48.82  ? 1640 ILE A CB    1 
ATOM   2625  C CG1   . ILE A 1 1640 ? 191.291 195.488 145.795 1.00 48.82  ? 1640 ILE A CG1   1 
ATOM   2626  C CG2   . ILE A 1 1640 ? 193.085 195.749 144.045 1.00 48.82  ? 1640 ILE A CG2   1 
ATOM   2627  C CD1   . ILE A 1 1640 ? 191.852 194.282 146.511 1.00 48.82  ? 1640 ILE A CD1   1 
ATOM   2628  N N     . ILE A 1 1641 ? 191.348 196.152 141.260 1.00 55.28  ? 1641 ILE A N     1 
ATOM   2629  C CA    . ILE A 1 1641 ? 192.002 196.472 139.994 1.00 55.28  ? 1641 ILE A CA    1 
ATOM   2630  C C     . ILE A 1 1641 ? 191.239 197.566 139.255 1.00 55.28  ? 1641 ILE A C     1 
ATOM   2631  O O     . ILE A 1 1641 ? 191.843 198.459 138.649 1.00 55.28  ? 1641 ILE A O     1 
ATOM   2632  C CB    . ILE A 1 1641 ? 192.175 195.205 139.135 1.00 55.28  ? 1641 ILE A CB    1 
ATOM   2633  C CG1   . ILE A 1 1641 ? 190.824 194.579 138.788 1.00 55.28  ? 1641 ILE A CG1   1 
ATOM   2634  C CG2   . ILE A 1 1641 ? 193.062 194.196 139.848 1.00 55.28  ? 1641 ILE A CG2   1 
ATOM   2635  C CD1   . ILE A 1 1641 ? 190.918 193.437 137.805 1.00 55.28  ? 1641 ILE A CD1   1 
ATOM   2636  N N     . GLY A 1 1642 ? 189.906 197.518 139.291 1.00 62.55  ? 1642 GLY A N     1 
ATOM   2637  C CA    . GLY A 1 1642 ? 189.123 198.540 138.618 1.00 62.55  ? 1642 GLY A CA    1 
ATOM   2638  C C     . GLY A 1 1642 ? 189.263 199.907 139.260 1.00 62.55  ? 1642 GLY A C     1 
ATOM   2639  O O     . GLY A 1 1642 ? 189.340 200.922 138.564 1.00 62.55  ? 1642 GLY A O     1 
ATOM   2640  N N     . ASN A 1 1643 ? 189.295 199.955 140.589 1.00 64.02  ? 1643 ASN A N     1 
ATOM   2641  C CA    . ASN A 1 1643 ? 189.370 201.211 141.332 1.00 64.02  ? 1643 ASN A CA    1 
ATOM   2642  C C     . ASN A 1 1643 ? 190.798 201.528 141.753 1.00 64.02  ? 1643 ASN A C     1 
ATOM   2643  O O     . ASN A 1 1643 ? 191.035 202.062 142.840 1.00 64.02  ? 1643 ASN A O     1 
ATOM   2644  C CB    . ASN A 1 1643 ? 188.446 201.162 142.544 1.00 64.02  ? 1643 ASN A CB    1 
ATOM   2645  C CG    . ASN A 1 1643 ? 186.984 201.053 142.159 1.00 64.02  ? 1643 ASN A CG    1 
ATOM   2646  O OD1   . ASN A 1 1643 ? 186.637 200.394 141.179 1.00 64.02  ? 1643 ASN A OD1   1 
ATOM   2647  N ND2   . ASN A 1 1643 ? 186.117 201.696 142.933 1.00 64.02  ? 1643 ASN A ND2   1 
ATOM   2648  N N     . SER A 1 1644 ? 191.769 201.191 140.902 1.00 65.77  ? 1644 SER A N     1 
ATOM   2649  C CA    . SER A 1 1644 ? 193.170 201.416 141.239 1.00 65.77  ? 1644 SER A CA    1 
ATOM   2650  C C     . SER A 1 1644 ? 193.486 202.903 141.337 1.00 65.77  ? 1644 SER A C     1 
ATOM   2651  O O     . SER A 1 1644 ? 194.342 203.312 142.131 1.00 65.77  ? 1644 SER A O     1 
ATOM   2652  C CB    . SER A 1 1644 ? 194.068 200.747 140.199 1.00 65.77  ? 1644 SER A CB    1 
ATOM   2653  O OG    . SER A 1 1644 ? 193.858 199.347 140.170 1.00 65.77  ? 1644 SER A OG    1 
ATOM   2654  N N     . LYS A 1 1645 ? 192.810 203.728 140.534 1.00 67.59  ? 1645 LYS A N     1 
ATOM   2655  C CA    . LYS A 1 1645 ? 193.112 205.156 140.514 1.00 67.59  ? 1645 LYS A CA    1 
ATOM   2656  C C     . LYS A 1 1645 ? 192.732 205.825 141.830 1.00 67.59  ? 1645 LYS A C     1 
ATOM   2657  O O     . LYS A 1 1645 ? 193.501 206.624 142.376 1.00 67.59  ? 1645 LYS A O     1 
ATOM   2658  C CB    . LYS A 1 1645 ? 192.406 205.823 139.334 1.00 67.59  ? 1645 LYS A CB    1 
ATOM   2659  C CG    . LYS A 1 1645 ? 192.983 205.433 137.984 1.00 67.59  ? 1645 LYS A CG    1 
ATOM   2660  C CD    . LYS A 1 1645 ? 194.502 205.414 138.038 1.00 67.59  ? 1645 LYS A CD    1 
ATOM   2661  C CE    . LYS A 1 1645 ? 195.091 204.623 136.889 1.00 67.59  ? 1645 LYS A CE    1 
ATOM   2662  N NZ    . LYS A 1 1645 ? 196.568 204.508 137.020 1.00 67.59  ? 1645 LYS A NZ    1 
ATOM   2663  N N     . ASN A 1 1646 ? 191.552 205.513 142.359 1.00 63.37  ? 1646 ASN A N     1 
ATOM   2664  C CA    . ASN A 1 1646 ? 191.128 206.046 143.651 1.00 63.37  ? 1646 ASN A CA    1 
ATOM   2665  C C     . ASN A 1 1646 ? 191.481 205.071 144.776 1.00 63.37  ? 1646 ASN A C     1 
ATOM   2666  O O     . ASN A 1 1646 ? 190.889 203.998 144.909 1.00 63.37  ? 1646 ASN A O     1 
ATOM   2667  C CB    . ASN A 1 1646 ? 189.650 206.453 143.613 1.00 63.37  ? 1646 ASN A CB    1 
ATOM   2668  C CG    . ASN A 1 1646 ? 188.683 205.295 143.343 1.00 63.37  ? 1646 ASN A CG    1 
ATOM   2669  O OD1   . ASN A 1 1646 ? 189.056 204.130 143.281 1.00 63.37  ? 1646 ASN A OD1   1 
ATOM   2670  N ND2   . ASN A 1 1646 ? 187.409 205.641 143.191 1.00 63.37  ? 1646 ASN A ND2   1 
ATOM   2671  N N     . VAL A 1 1647 ? 192.470 205.449 145.588 1.00 51.71  ? 1647 VAL A N     1 
ATOM   2672  C CA    . VAL A 1 1647 ? 192.949 204.575 146.651 1.00 51.71  ? 1647 VAL A CA    1 
ATOM   2673  C C     . VAL A 1 1647 ? 191.987 204.482 147.824 1.00 51.71  ? 1647 VAL A C     1 
ATOM   2674  O O     . VAL A 1 1647 ? 192.185 203.635 148.701 1.00 51.71  ? 1647 VAL A O     1 
ATOM   2675  C CB    . VAL A 1 1647 ? 194.330 205.044 147.148 1.00 51.71  ? 1647 VAL A CB    1 
ATOM   2676  C CG1   . VAL A 1 1647 ? 195.395 204.728 146.110 1.00 51.71  ? 1647 VAL A CG1   1 
ATOM   2677  C CG2   . VAL A 1 1647 ? 194.291 206.525 147.448 1.00 51.71  ? 1647 VAL A CG2   1 
ATOM   2678  N N     . ALA A 1 1648 ? 190.949 205.323 147.863 1.00 51.63  ? 1648 ALA A N     1 
ATOM   2679  C CA    . ALA A 1 1648 ? 189.983 205.256 148.955 1.00 51.63  ? 1648 ALA A CA    1 
ATOM   2680  C C     . ALA A 1 1648 ? 189.263 203.917 148.986 1.00 51.63  ? 1648 ALA A C     1 
ATOM   2681  O O     . ALA A 1 1648 ? 189.029 203.363 150.066 1.00 51.63  ? 1648 ALA A O     1 
ATOM   2682  C CB    . ALA A 1 1648 ? 188.969 206.394 148.835 1.00 51.63  ? 1648 ALA A CB    1 
ATOM   2683  N N     . LYS A 1 1649 ? 188.893 203.386 147.820 1.00 51.84  ? 1649 LYS A N     1 
ATOM   2684  C CA    . LYS A 1 1649 ? 188.259 202.077 147.762 1.00 51.84  ? 1649 LYS A CA    1 
ATOM   2685  C C     . LYS A 1 1649 ? 189.252 200.943 147.966 1.00 51.84  ? 1649 LYS A C     1 
ATOM   2686  O O     . LYS A 1 1649 ? 188.834 199.808 148.220 1.00 51.84  ? 1649 LYS A O     1 
ATOM   2687  C CB    . LYS A 1 1649 ? 187.537 201.900 146.426 1.00 51.84  ? 1649 LYS A CB    1 
ATOM   2688  C CG    . LYS A 1 1649 ? 186.423 202.907 146.192 1.00 51.84  ? 1649 LYS A CG    1 
ATOM   2689  C CD    . LYS A 1 1649 ? 185.263 202.682 147.146 1.00 51.84  ? 1649 LYS A CD    1 
ATOM   2690  C CE    . LYS A 1 1649 ? 184.127 203.651 146.865 1.00 51.84  ? 1649 LYS A CE    1 
ATOM   2691  N NZ    . LYS A 1 1649 ? 182.989 203.462 147.804 1.00 51.84  ? 1649 LYS A NZ    1 
ATOM   2692  N N     . LEU A 1 1650 ? 190.552 201.223 147.855 1.00 44.49  ? 1650 LEU A N     1 
ATOM   2693  C CA    . LEU A 1 1650 ? 191.569 200.213 148.118 1.00 44.49  ? 1650 LEU A CA    1 
ATOM   2694  C C     . LEU A 1 1650 ? 191.762 199.966 149.607 1.00 44.49  ? 1650 LEU A C     1 
ATOM   2695  O O     . LEU A 1 1650 ? 192.022 198.828 150.013 1.00 44.49  ? 1650 LEU A O     1 
ATOM   2696  C CB    . LEU A 1 1650 ? 192.900 200.631 147.493 1.00 44.49  ? 1650 LEU A CB    1 
ATOM   2697  C CG    . LEU A 1 1650 ? 193.191 200.124 146.083 1.00 44.49  ? 1650 LEU A CG    1 
ATOM   2698  C CD1   . LEU A 1 1650 ? 194.449 200.770 145.532 1.00 44.49  ? 1650 LEU A CD1   1 
ATOM   2699  C CD2   . LEU A 1 1650 ? 193.334 198.619 146.107 1.00 44.49  ? 1650 LEU A CD2   1 
ATOM   2700  N N     . GLN A 1 1651 ? 191.638 201.010 150.428 1.00 38.90  ? 1651 GLN A N     1 
ATOM   2701  C CA    . GLN A 1 1651 ? 191.959 200.905 151.846 1.00 38.90  ? 1651 GLN A CA    1 
ATOM   2702  C C     . GLN A 1 1651 ? 191.014 199.983 152.604 1.00 38.90  ? 1651 GLN A C     1 
ATOM   2703  O O     . GLN A 1 1651 ? 191.333 199.585 153.729 1.00 38.90  ? 1651 GLN A O     1 
ATOM   2704  C CB    . GLN A 1 1651 ? 191.951 202.295 152.481 1.00 38.90  ? 1651 GLN A CB    1 
ATOM   2705  C CG    . GLN A 1 1651 ? 192.930 203.262 151.843 1.00 38.90  ? 1651 GLN A CG    1 
ATOM   2706  C CD    . GLN A 1 1651 ? 193.086 204.540 152.637 1.00 38.90  ? 1651 GLN A CD    1 
ATOM   2707  O OE1   . GLN A 1 1651 ? 194.162 205.137 152.669 1.00 38.90  ? 1651 GLN A OE1   1 
ATOM   2708  N NE2   . GLN A 1 1651 ? 192.008 204.972 153.281 1.00 38.90  ? 1651 GLN A NE2   1 
ATOM   2709  N N     . LYS A 1 1652 ? 189.864 199.632 152.026 1.00 40.89  ? 1652 LYS A N     1 
ATOM   2710  C CA    . LYS A 1 1652 ? 188.942 198.746 152.727 1.00 40.89  ? 1652 LYS A CA    1 
ATOM   2711  C C     . LYS A 1 1652 ? 189.349 197.287 152.565 1.00 40.89  ? 1652 LYS A C     1 
ATOM   2712  O O     . LYS A 1 1652 ? 188.748 196.395 153.174 1.00 40.89  ? 1652 LYS A O     1 
ATOM   2713  C CB    . LYS A 1 1652 ? 187.512 198.971 152.233 1.00 40.89  ? 1652 LYS A CB    1 
ATOM   2714  C CG    . LYS A 1 1652 ? 187.233 198.466 150.829 1.00 40.89  ? 1652 LYS A CG    1 
ATOM   2715  C CD    . LYS A 1 1652 ? 185.823 198.836 150.394 1.00 40.89  ? 1652 LYS A CD    1 
ATOM   2716  C CE    . LYS A 1 1652 ? 185.516 198.326 148.997 1.00 40.89  ? 1652 LYS A CE    1 
ATOM   2717  N NZ    . LYS A 1 1652 ? 185.342 196.848 148.978 1.00 40.89  ? 1652 LYS A NZ    1 
ATOM   2718  N N     . HIS A 1 1653 ? 190.369 197.023 151.747 1.00 36.61  ? 1653 HIS A N     1 
ATOM   2719  C CA    . HIS A 1 1653 ? 190.874 195.671 151.549 1.00 36.61  ? 1653 HIS A CA    1 
ATOM   2720  C C     . HIS A 1 1653 ? 192.203 195.416 152.244 1.00 36.61  ? 1653 HIS A C     1 
ATOM   2721  O O     . HIS A 1 1653 ? 192.563 194.251 152.443 1.00 36.61  ? 1653 HIS A O     1 
ATOM   2722  C CB    . HIS A 1 1653 ? 191.038 195.375 150.055 1.00 36.61  ? 1653 HIS A CB    1 
ATOM   2723  C CG    . HIS A 1 1653 ? 189.785 195.554 149.259 1.00 36.61  ? 1653 HIS A CG    1 
ATOM   2724  N ND1   . HIS A 1 1653 ? 188.887 194.531 149.045 1.00 36.61  ? 1653 HIS A ND1   1 
ATOM   2725  C CD2   . HIS A 1 1653 ? 189.283 196.635 148.617 1.00 36.61  ? 1653 HIS A CD2   1 
ATOM   2726  C CE1   . HIS A 1 1653 ? 187.884 194.975 148.309 1.00 36.61  ? 1653 HIS A CE1   1 
ATOM   2727  N NE2   . HIS A 1 1653 ? 188.100 196.249 148.036 1.00 36.61  ? 1653 HIS A NE2   1 
ATOM   2728  N N     . PHE A 1 1654 ? 192.937 196.466 152.619 1.00 29.04  ? 1654 PHE A N     1 
ATOM   2729  C CA    . PHE A 1 1654 ? 194.287 196.300 153.144 1.00 29.04  ? 1654 PHE A CA    1 
ATOM   2730  C C     . PHE A 1 1654 ? 194.332 195.522 154.451 1.00 29.04  ? 1654 PHE A C     1 
ATOM   2731  O O     . PHE A 1 1654 ? 195.391 194.982 154.788 1.00 29.04  ? 1654 PHE A O     1 
ATOM   2732  C CB    . PHE A 1 1654 ? 194.945 197.665 153.334 1.00 29.04  ? 1654 PHE A CB    1 
ATOM   2733  C CG    . PHE A 1 1654 ? 195.723 198.127 152.140 1.00 29.04  ? 1654 PHE A CG    1 
ATOM   2734  C CD1   . PHE A 1 1654 ? 196.777 197.376 151.653 1.00 29.04  ? 1654 PHE A CD1   1 
ATOM   2735  C CD2   . PHE A 1 1654 ? 195.399 199.310 151.502 1.00 29.04  ? 1654 PHE A CD2   1 
ATOM   2736  C CE1   . PHE A 1 1654 ? 197.494 197.798 150.552 1.00 29.04  ? 1654 PHE A CE1   1 
ATOM   2737  C CE2   . PHE A 1 1654 ? 196.113 199.736 150.401 1.00 29.04  ? 1654 PHE A CE2   1 
ATOM   2738  C CZ    . PHE A 1 1654 ? 197.162 198.980 149.926 1.00 29.04  ? 1654 PHE A CZ    1 
ATOM   2739  N N     . LYS A 1 1655 ? 193.229 195.442 155.187 1.00 26.79  ? 1655 LYS A N     1 
ATOM   2740  C CA    . LYS A 1 1655 ? 193.183 194.645 156.402 1.00 26.79  ? 1655 LYS A CA    1 
ATOM   2741  C C     . LYS A 1 1655 ? 193.029 193.158 156.120 1.00 26.79  ? 1655 LYS A C     1 
ATOM   2742  O O     . LYS A 1 1655 ? 193.114 192.352 157.052 1.00 26.79  ? 1655 LYS A O     1 
ATOM   2743  C CB    . LYS A 1 1655 ? 192.045 195.121 157.310 1.00 26.79  ? 1655 LYS A CB    1 
ATOM   2744  C CG    . LYS A 1 1655 ? 190.657 194.747 156.821 1.00 26.79  ? 1655 LYS A CG    1 
ATOM   2745  C CD    . LYS A 1 1655 ? 189.626 194.858 157.936 1.00 26.79  ? 1655 LYS A CD    1 
ATOM   2746  C CE    . LYS A 1 1655 ? 189.847 196.101 158.784 1.00 26.79  ? 1655 LYS A CE    1 
ATOM   2747  N NZ    . LYS A 1 1655 ? 189.679 197.352 157.995 1.00 26.79  ? 1655 LYS A NZ    1 
ATOM   2748  N N     . LYS A 1 1656 ? 192.805 192.777 154.862 1.00 26.20  ? 1656 LYS A N     1 
ATOM   2749  C CA    . LYS A 1 1656 ? 192.716 191.378 154.470 1.00 26.20  ? 1656 LYS A CA    1 
ATOM   2750  C C     . LYS A 1 1656 ? 194.006 190.830 153.884 1.00 26.20  ? 1656 LYS A C     1 
ATOM   2751  O O     . LYS A 1 1656 ? 194.297 189.647 154.070 1.00 26.20  ? 1656 LYS A O     1 
ATOM   2752  C CB    . LYS A 1 1656 ? 191.592 191.179 153.446 1.00 26.20  ? 1656 LYS A CB    1 
ATOM   2753  C CG    . LYS A 1 1656 ? 190.210 191.024 154.055 1.00 26.20  ? 1656 LYS A CG    1 
ATOM   2754  C CD    . LYS A 1 1656 ? 189.130 191.121 152.989 1.00 26.20  ? 1656 LYS A CD    1 
ATOM   2755  C CE    . LYS A 1 1656 ? 189.076 192.512 152.377 1.00 26.20  ? 1656 LYS A CE    1 
ATOM   2756  N NZ    . LYS A 1 1656 ? 188.127 193.404 153.099 1.00 26.20  ? 1656 LYS A NZ    1 
ATOM   2757  N N     . MET A 1 1657 ? 194.781 191.656 153.183 1.00 25.13  ? 1657 MET A N     1 
ATOM   2758  C CA    . MET A 1 1657 ? 196.024 191.184 152.575 1.00 25.13  ? 1657 MET A CA    1 
ATOM   2759  C C     . MET A 1 1657 ? 197.168 191.202 153.585 1.00 25.13  ? 1657 MET A C     1 
ATOM   2760  O O     . MET A 1 1657 ? 197.804 190.176 153.841 1.00 25.13  ? 1657 MET A O     1 
ATOM   2761  C CB    . MET A 1 1657 ? 196.362 192.035 151.346 1.00 25.13  ? 1657 MET A CB    1 
ATOM   2762  C CG    . MET A 1 1657 ? 195.205 192.214 150.379 1.00 25.13  ? 1657 MET A CG    1 
ATOM   2763  S SD    . MET A 1 1657 ? 195.601 193.337 149.027 1.00 25.13  ? 1657 MET A SD    1 
ATOM   2764  C CE    . MET A 1 1657 ? 194.711 194.805 149.534 1.00 25.13  ? 1657 MET A CE    1 
ATOM   2765  N N     . PHE A 1 1658 ? 197.443 192.366 154.165 1.00 22.86  ? 1658 PHE A N     1 
ATOM   2766  C CA    . PHE A 1 1658 ? 198.530 192.496 155.120 1.00 22.86  ? 1658 PHE A CA    1 
ATOM   2767  C C     . PHE A 1 1658 ? 198.058 192.129 156.525 1.00 22.86  ? 1658 PHE A C     1 
ATOM   2768  O O     . PHE A 1 1658 ? 196.870 191.916 156.780 1.00 22.86  ? 1658 PHE A O     1 
ATOM   2769  C CB    . PHE A 1 1658 ? 199.101 193.913 155.099 1.00 22.86  ? 1658 PHE A CB    1 
ATOM   2770  C CG    . PHE A 1 1658 ? 199.692 194.315 153.776 1.00 22.86  ? 1658 PHE A CG    1 
ATOM   2771  C CD1   . PHE A 1 1658 ? 198.879 194.629 152.699 1.00 22.86  ? 1658 PHE A CD1   1 
ATOM   2772  C CD2   . PHE A 1 1658 ? 201.064 194.374 153.609 1.00 22.86  ? 1658 PHE A CD2   1 
ATOM   2773  C CE1   . PHE A 1 1658 ? 199.425 194.996 151.485 1.00 22.86  ? 1658 PHE A CE1   1 
ATOM   2774  C CE2   . PHE A 1 1658 ? 201.614 194.740 152.397 1.00 22.86  ? 1658 PHE A CE2   1 
ATOM   2775  C CZ    . PHE A 1 1658 ? 200.793 195.051 151.334 1.00 22.86  ? 1658 PHE A CZ    1 
ATOM   2776  N N     . ALA A 1 1659 ? 199.015 192.057 157.450 1.00 18.50  ? 1659 ALA A N     1 
ATOM   2777  C CA    . ALA A 1 1659 ? 198.730 191.632 158.817 1.00 18.50  ? 1659 ALA A CA    1 
ATOM   2778  C C     . ALA A 1 1659 ? 198.222 192.785 159.676 1.00 18.50  ? 1659 ALA A C     1 
ATOM   2779  O O     . ALA A 1 1659 ? 197.104 192.734 160.199 1.00 18.50  ? 1659 ALA A O     1 
ATOM   2780  C CB    . ALA A 1 1659 ? 199.983 191.015 159.445 1.00 18.50  ? 1659 ALA A CB    1 
ATOM   2781  N N     . GLY A 1 1660 ? 199.032 193.828 159.828 1.00 18.25  ? 1660 GLY A N     1 
ATOM   2782  C CA    . GLY A 1 1660 ? 198.665 194.954 160.662 1.00 18.25  ? 1660 GLY A CA    1 
ATOM   2783  C C     . GLY A 1 1660 ? 198.271 196.180 159.868 1.00 18.25  ? 1660 GLY A C     1 
ATOM   2784  O O     . GLY A 1 1660 ? 197.612 197.081 160.393 1.00 18.25  ? 1660 GLY A O     1 
ATOM   2785  N N     . VAL A 1 1661 ? 198.677 196.227 158.601 1.00 19.76  ? 1661 VAL A N     1 
ATOM   2786  C CA    . VAL A 1 1661 ? 198.389 197.366 157.739 1.00 19.76  ? 1661 VAL A CA    1 
ATOM   2787  C C     . VAL A 1 1661 ? 196.890 197.459 157.501 1.00 19.76  ? 1661 VAL A C     1 
ATOM   2788  O O     . VAL A 1 1661 ? 196.257 196.494 157.060 1.00 19.76  ? 1661 VAL A O     1 
ATOM   2789  C CB    . VAL A 1 1661 ? 199.149 197.260 156.406 1.00 19.76  ? 1661 VAL A CB    1 
ATOM   2790  C CG1   . VAL A 1 1661 ? 198.810 198.436 155.508 1.00 19.76  ? 1661 VAL A CG1   1 
ATOM   2791  C CG2   . VAL A 1 1661 ? 200.641 197.180 156.654 1.00 19.76  ? 1661 VAL A CG2   1 
ATOM   2792  N N     . SER A 1 1662 ? 196.311 198.623 157.794 1.00 24.42  ? 1662 SER A N     1 
ATOM   2793  C CA    . SER A 1 1662 ? 194.907 198.879 157.521 1.00 24.42  ? 1662 SER A CA    1 
ATOM   2794  C C     . SER A 1 1662 ? 194.698 200.051 156.576 1.00 24.42  ? 1662 SER A C     1 
ATOM   2795  O O     . SER A 1 1662 ? 193.570 200.265 156.122 1.00 24.42  ? 1662 SER A O     1 
ATOM   2796  C CB    . SER A 1 1662 ? 194.141 199.138 158.825 1.00 24.42  ? 1662 SER A CB    1 
ATOM   2797  O OG    . SER A 1 1662 ? 194.396 200.444 159.310 1.00 24.42  ? 1662 SER A OG    1 
ATOM   2798  N N     . SER A 1 1663 ? 195.745 200.810 156.271 1.00 27.98  ? 1663 SER A N     1 
ATOM   2799  C CA    . SER A 1 1663 ? 195.667 201.925 155.338 1.00 27.98  ? 1663 SER A CA    1 
ATOM   2800  C C     . SER A 1 1663 ? 197.081 202.249 154.878 1.00 27.98  ? 1663 SER A C     1 
ATOM   2801  O O     . SER A 1 1663 ? 198.060 201.685 155.372 1.00 27.98  ? 1663 SER A O     1 
ATOM   2802  C CB    . SER A 1 1663 ? 194.992 203.141 155.977 1.00 27.98  ? 1663 SER A CB    1 
ATOM   2803  O OG    . SER A 1 1663 ? 195.256 204.316 155.231 1.00 27.98  ? 1663 SER A OG    1 
ATOM   2804  N N     . ILE A 1 1664 ? 197.183 203.170 153.925 1.00 30.82  ? 1664 ILE A N     1 
ATOM   2805  C CA    . ILE A 1 1664 ? 198.468 203.623 153.406 1.00 30.82  ? 1664 ILE A CA    1 
ATOM   2806  C C     . ILE A 1 1664 ? 198.462 205.143 153.384 1.00 30.82  ? 1664 ILE A C     1 
ATOM   2807  O O     . ILE A 1 1664 ? 197.442 205.760 153.060 1.00 30.82  ? 1664 ILE A O     1 
ATOM   2808  C CB    . ILE A 1 1664 ? 198.760 203.055 152.003 1.00 30.82  ? 1664 ILE A CB    1 
ATOM   2809  C CG1   . ILE A 1 1664 ? 197.542 203.212 151.093 1.00 30.82  ? 1664 ILE A CG1   1 
ATOM   2810  C CG2   . ILE A 1 1664 ? 199.169 201.595 152.095 1.00 30.82  ? 1664 ILE A CG2   1 
ATOM   2811  C CD1   . ILE A 1 1664 ? 197.813 202.848 149.652 1.00 30.82  ? 1664 ILE A CD1   1 
ATOM   2812  N N     . ILE A 1 1665 ? 199.591 205.747 153.748 1.00 34.18  ? 1665 ILE A N     1 
ATOM   2813  C CA    . ILE A 1 1665 ? 199.708 207.204 153.813 1.00 34.18  ? 1665 ILE A CA    1 
ATOM   2814  C C     . ILE A 1 1665 ? 200.304 207.649 152.481 1.00 34.18  ? 1665 ILE A C     1 
ATOM   2815  O O     . ILE A 1 1665 ? 201.452 207.348 152.154 1.00 34.18  ? 1665 ILE A O     1 
ATOM   2816  C CB    . ILE A 1 1665 ? 200.544 207.659 155.006 1.00 34.18  ? 1665 ILE A CB    1 
ATOM   2817  C CG1   . ILE A 1 1665 ? 200.024 207.022 156.296 1.00 34.18  ? 1665 ILE A CG1   1 
ATOM   2818  C CG2   . ILE A 1 1665 ? 200.530 209.174 155.115 1.00 34.18  ? 1665 ILE A CG2   1 
ATOM   2819  C CD1   . ILE A 1 1665 ? 198.547 207.247 156.542 1.00 34.18  ? 1665 ILE A CD1   1 
ATOM   2820  N N     . LEU A 1 1666 ? 199.510 208.382 151.704 1.00 42.07  ? 1666 LEU A N     1 
ATOM   2821  C CA    . LEU A 1 1666 ? 199.936 208.836 150.391 1.00 42.07  ? 1666 LEU A CA    1 
ATOM   2822  C C     . LEU A 1 1666 ? 200.318 210.315 150.426 1.00 42.07  ? 1666 LEU A C     1 
ATOM   2823  O O     . LEU A 1 1666 ? 200.368 210.952 151.481 1.00 42.07  ? 1666 LEU A O     1 
ATOM   2824  C CB    . LEU A 1 1666 ? 198.846 208.580 149.351 1.00 42.07  ? 1666 LEU A CB    1 
ATOM   2825  C CG    . LEU A 1 1666 ? 198.210 207.190 149.311 1.00 42.07  ? 1666 LEU A CG    1 
ATOM   2826  C CD1   . LEU A 1 1666 ? 196.950 207.138 150.163 1.00 42.07  ? 1666 LEU A CD1   1 
ATOM   2827  C CD2   . LEU A 1 1666 ? 197.918 206.781 147.878 1.00 42.07  ? 1666 LEU A CD2   1 
ATOM   2828  N N     . ASN A 1 1667 ? 200.590 210.867 149.247 1.00 53.30  ? 1667 ASN A N     1 
ATOM   2829  C CA    . ASN A 1 1667 ? 201.027 212.249 149.110 1.00 53.30  ? 1667 ASN A CA    1 
ATOM   2830  C C     . ASN A 1 1667 ? 199.792 213.152 149.094 1.00 53.30  ? 1667 ASN A C     1 
ATOM   2831  O O     . ASN A 1 1667 ? 198.673 212.710 149.369 1.00 53.30  ? 1667 ASN A O     1 
ATOM   2832  C CB    . ASN A 1 1667 ? 201.871 212.400 147.848 1.00 53.30  ? 1667 ASN A CB    1 
ATOM   2833  C CG    . ASN A 1 1667 ? 202.907 213.493 147.968 1.00 53.30  ? 1667 ASN A CG    1 
ATOM   2834  O OD1   . ASN A 1 1667 ? 203.040 214.121 149.015 1.00 53.30  ? 1667 ASN A OD1   1 
ATOM   2835  N ND2   . ASN A 1 1667 ? 203.647 213.729 146.891 1.00 53.30  ? 1667 ASN A ND2   1 
ATOM   2836  N N     . GLU A 1 1668 ? 199.971 214.439 148.774 1.00 62.97  ? 1668 GLU A N     1 
ATOM   2837  C CA    . GLU A 1 1668 ? 198.806 215.307 148.615 1.00 62.97  ? 1668 GLU A CA    1 
ATOM   2838  C C     . GLU A 1 1668 ? 197.980 214.903 147.400 1.00 62.97  ? 1668 GLU A C     1 
ATOM   2839  O O     . GLU A 1 1668 ? 196.744 214.944 147.441 1.00 62.97  ? 1668 GLU A O     1 
ATOM   2840  C CB    . GLU A 1 1668 ? 199.217 216.778 148.502 1.00 62.97  ? 1668 GLU A CB    1 
ATOM   2841  C CG    . GLU A 1 1668 ? 199.825 217.385 149.759 1.00 62.97  ? 1668 GLU A CG    1 
ATOM   2842  C CD    . GLU A 1 1668 ? 201.300 217.086 149.900 1.00 62.97  ? 1668 GLU A CD    1 
ATOM   2843  O OE1   . GLU A 1 1668 ? 201.864 216.461 148.983 1.00 62.97  ? 1668 GLU A OE1   1 
ATOM   2844  O OE2   . GLU A 1 1668 ? 201.895 217.479 150.926 1.00 62.97  ? 1668 GLU A OE2   1 
ATOM   2845  N N     . ASP A 1 1669 ? 198.640 214.514 146.312 1.00 61.00  ? 1669 ASP A N     1 
ATOM   2846  C CA    . ASP A 1 1669 ? 197.967 214.114 145.084 1.00 61.00  ? 1669 ASP A CA    1 
ATOM   2847  C C     . ASP A 1 1669 ? 197.818 212.604 144.961 1.00 61.00  ? 1669 ASP A C     1 
ATOM   2848  O O     . ASP A 1 1669 ? 197.495 212.113 143.874 1.00 61.00  ? 1669 ASP A O     1 
ATOM   2849  C CB    . ASP A 1 1669 ? 198.717 214.663 143.869 1.00 61.00  ? 1669 ASP A CB    1 
ATOM   2850  C CG    . ASP A 1 1669 ? 200.165 214.224 143.830 1.00 61.00  ? 1669 ASP A CG    1 
ATOM   2851  O OD1   . ASP A 1 1669 ? 200.688 213.801 144.883 1.00 61.00  ? 1669 ASP A OD1   1 
ATOM   2852  O OD2   . ASP A 1 1669 ? 200.781 214.300 142.747 1.00 61.00  ? 1669 ASP A OD2   1 
ATOM   2853  N N     . ASN A 1 1670 ? 198.047 211.862 146.047 1.00 55.10  ? 1670 ASN A N     1 
ATOM   2854  C CA    . ASN A 1 1670 ? 197.966 210.401 146.046 1.00 55.10  ? 1670 ASN A CA    1 
ATOM   2855  C C     . ASN A 1 1670 ? 198.905 209.797 145.005 1.00 55.10  ? 1670 ASN A C     1 
ATOM   2856  O O     . ASN A 1 1670 ? 198.559 208.841 144.308 1.00 55.10  ? 1670 ASN A O     1 
ATOM   2857  C CB    . ASN A 1 1670 ? 196.528 209.925 145.823 1.00 55.10  ? 1670 ASN A CB    1 
ATOM   2858  C CG    . ASN A 1 1670 ? 195.622 210.237 146.998 1.00 55.10  ? 1670 ASN A CG    1 
ATOM   2859  O OD1   . ASN A 1 1670 ? 196.014 210.091 148.155 1.00 55.10  ? 1670 ASN A OD1   1 
ATOM   2860  N ND2   . ASN A 1 1670 ? 194.401 210.669 146.704 1.00 55.10  ? 1670 ASN A ND2   1 
ATOM   2861  N N     . SER A 1 1671 ? 200.108 210.360 144.900 1.00 49.25  ? 1671 SER A N     1 
ATOM   2862  C CA    . SER A 1 1671 ? 201.082 209.923 143.910 1.00 49.25  ? 1671 SER A CA    1 
ATOM   2863  C C     . SER A 1 1671 ? 202.154 209.005 144.476 1.00 49.25  ? 1671 SER A C     1 
ATOM   2864  O O     . SER A 1 1671 ? 202.549 208.050 143.801 1.00 49.25  ? 1671 SER A O     1 
ATOM   2865  C CB    . SER A 1 1671 ? 201.759 211.135 143.262 1.00 49.25  ? 1671 SER A CB    1 
ATOM   2866  O OG    . SER A 1 1671 ? 202.655 211.758 144.165 1.00 49.25  ? 1671 SER A OG    1 
ATOM   2867  N N     . VAL A 1 1672 ? 202.639 209.266 145.687 1.00 43.28  ? 1672 VAL A N     1 
ATOM   2868  C CA    . VAL A 1 1672 ? 203.661 208.443 146.321 1.00 43.28  ? 1672 VAL A CA    1 
ATOM   2869  C C     . VAL A 1 1672 ? 203.114 207.915 147.638 1.00 43.28  ? 1672 VAL A C     1 
ATOM   2870  O O     . VAL A 1 1672 ? 202.382 208.616 148.346 1.00 43.28  ? 1672 VAL A O     1 
ATOM   2871  C CB    . VAL A 1 1672 ? 204.979 209.219 146.541 1.00 43.28  ? 1672 VAL A CB    1 
ATOM   2872  C CG1   . VAL A 1 1672 ? 205.508 209.748 145.219 1.00 43.28  ? 1672 VAL A CG1   1 
ATOM   2873  C CG2   . VAL A 1 1672 ? 204.790 210.354 147.531 1.00 43.28  ? 1672 VAL A CG2   1 
ATOM   2874  N N     . VAL A 1 1673 ? 203.447 206.666 147.952 1.00 34.15  ? 1673 VAL A N     1 
ATOM   2875  C CA    . VAL A 1 1673 ? 203.021 206.032 149.195 1.00 34.15  ? 1673 VAL A CA    1 
ATOM   2876  C C     . VAL A 1 1673 ? 204.074 206.364 150.247 1.00 34.15  ? 1673 VAL A C     1 
ATOM   2877  O O     . VAL A 1 1673 ? 205.119 205.717 150.326 1.00 34.15  ? 1673 VAL A O     1 
ATOM   2878  C CB    . VAL A 1 1673 ? 202.838 204.524 149.031 1.00 34.15  ? 1673 VAL A CB    1 
ATOM   2879  C CG1   . VAL A 1 1673 ? 202.183 203.933 150.267 1.00 34.15  ? 1673 VAL A CG1   1 
ATOM   2880  C CG2   . VAL A 1 1673 ? 202.012 204.230 147.794 1.00 34.15  ? 1673 VAL A CG2   1 
ATOM   2881  N N     . LEU A 1 1674 ? 203.797 207.389 151.056 1.00 33.97  ? 1674 LEU A N     1 
ATOM   2882  C CA    . LEU A 1 1674 ? 204.756 207.811 152.070 1.00 33.97  ? 1674 LEU A CA    1 
ATOM   2883  C C     . LEU A 1 1674 ? 204.986 206.718 153.106 1.00 33.97  ? 1674 LEU A C     1 
ATOM   2884  O O     . LEU A 1 1674 ? 206.125 206.481 153.525 1.00 33.97  ? 1674 LEU A O     1 
ATOM   2885  C CB    . LEU A 1 1674 ? 204.276 209.096 152.742 1.00 33.97  ? 1674 LEU A CB    1 
ATOM   2886  C CG    . LEU A 1 1674 ? 204.460 210.378 151.930 1.00 33.97  ? 1674 LEU A CG    1 
ATOM   2887  C CD1   . LEU A 1 1674 ? 203.992 211.587 152.722 1.00 33.97  ? 1674 LEU A CD1   1 
ATOM   2888  C CD2   . LEU A 1 1674 ? 205.911 210.537 151.507 1.00 33.97  ? 1674 LEU A CD2   1 
ATOM   2889  N N     . GLY A 1 1675 ? 203.926 206.043 153.527 1.00 28.45  ? 1675 GLY A N     1 
ATOM   2890  C CA    . GLY A 1 1675 ? 204.080 205.008 154.525 1.00 28.45  ? 1675 GLY A CA    1 
ATOM   2891  C C     . GLY A 1 1675 ? 202.790 204.255 154.753 1.00 28.45  ? 1675 GLY A C     1 
ATOM   2892  O O     . GLY A 1 1675 ? 201.819 204.400 154.008 1.00 28.45  ? 1675 GLY A O     1 
ATOM   2893  N N     . ILE A 1 1676 ? 202.799 203.445 155.806 1.00 25.41  ? 1676 ILE A N     1 
ATOM   2894  C CA    . ILE A 1 1676 ? 201.670 202.603 156.168 1.00 25.41  ? 1676 ILE A CA    1 
ATOM   2895  C C     . ILE A 1 1676 ? 201.191 202.981 157.563 1.00 25.41  ? 1676 ILE A C     1 
ATOM   2896  O O     . ILE A 1 1676 ? 201.927 203.549 158.375 1.00 25.41  ? 1676 ILE A O     1 
ATOM   2897  C CB    . ILE A 1 1676 ? 202.036 201.108 156.102 1.00 25.41  ? 1676 ILE A CB    1 
ATOM   2898  C CG1   . ILE A 1 1676 ? 203.152 200.806 157.102 1.00 25.41  ? 1676 ILE A CG1   1 
ATOM   2899  C CG2   . ILE A 1 1676 ? 202.434 200.716 154.694 1.00 25.41  ? 1676 ILE A CG2   1 
ATOM   2900  C CD1   . ILE A 1 1676 ? 203.432 199.345 157.286 1.00 25.41  ? 1676 ILE A CD1   1 
ATOM   2901  N N     . SER A 1 1677 ? 199.931 202.654 157.839 1.00 24.52  ? 1677 SER A N     1 
ATOM   2902  C CA    . SER A 1 1677 ? 199.319 202.945 159.126 1.00 24.52  ? 1677 SER A CA    1 
ATOM   2903  C C     . SER A 1 1677 ? 198.539 201.727 159.591 1.00 24.52  ? 1677 SER A C     1 
ATOM   2904  O O     . SER A 1 1677 ? 197.851 201.087 158.792 1.00 24.52  ? 1677 SER A O     1 
ATOM   2905  C CB    . SER A 1 1677 ? 198.396 204.165 159.040 1.00 24.52  ? 1677 SER A CB    1 
ATOM   2906  O OG    . SER A 1 1677 ? 197.269 203.894 158.226 1.00 24.52  ? 1677 SER A OG    1 
ATOM   2907  N N     . SER A 1 1678 ? 198.646 201.414 160.879 1.00 24.27  ? 1678 SER A N     1 
ATOM   2908  C CA    . SER A 1 1678 ? 197.948 200.270 161.439 1.00 24.27  ? 1678 SER A CA    1 
ATOM   2909  C C     . SER A 1 1678 ? 196.495 200.630 161.740 1.00 24.27  ? 1678 SER A C     1 
ATOM   2910  O O     . SER A 1 1678 ? 196.048 201.762 161.536 1.00 24.27  ? 1678 SER A O     1 
ATOM   2911  C CB    . SER A 1 1678 ? 198.661 199.777 162.695 1.00 24.27  ? 1678 SER A CB    1 
ATOM   2912  O OG    . SER A 1 1678 ? 197.908 198.765 163.340 1.00 24.27  ? 1678 SER A OG    1 
ATOM   2913  N N     . ARG A 1 1679 ? 195.744 199.644 162.236 1.00 29.67  ? 1679 ARG A N     1 
ATOM   2914  C CA    . ARG A 1 1679 ? 194.345 199.878 162.579 1.00 29.67  ? 1679 ARG A CA    1 
ATOM   2915  C C     . ARG A 1 1679 ? 194.210 200.801 163.783 1.00 29.67  ? 1679 ARG A C     1 
ATOM   2916  O O     . ARG A 1 1679 ? 193.246 201.570 163.868 1.00 29.67  ? 1679 ARG A O     1 
ATOM   2917  C CB    . ARG A 1 1679 ? 193.643 198.545 162.842 1.00 29.67  ? 1679 ARG A CB    1 
ATOM   2918  C CG    . ARG A 1 1679 ? 192.144 198.652 163.084 1.00 29.67  ? 1679 ARG A CG    1 
ATOM   2919  C CD    . ARG A 1 1679 ? 191.807 198.579 164.566 1.00 29.67  ? 1679 ARG A CD    1 
ATOM   2920  N NE    . ARG A 1 1679 ? 192.289 197.347 165.179 1.00 29.67  ? 1679 ARG A NE    1 
ATOM   2921  C CZ    . ARG A 1 1679 ? 191.581 196.230 165.271 1.00 29.67  ? 1679 ARG A CZ    1 
ATOM   2922  N NH1   . ARG A 1 1679 ? 190.347 196.152 164.800 1.00 29.67  ? 1679 ARG A NH1   1 
ATOM   2923  N NH2   . ARG A 1 1679 ? 192.123 195.164 165.853 1.00 29.67  ? 1679 ARG A NH2   1 
ATOM   2924  N N     . GLU A 1 1680 ? 195.158 200.745 164.715 1.00 28.18  ? 1680 GLU A N     1 
ATOM   2925  C CA    . GLU A 1 1680 ? 195.087 201.527 165.942 1.00 28.18  ? 1680 GLU A CA    1 
ATOM   2926  C C     . GLU A 1 1680 ? 195.620 202.943 165.781 1.00 28.18  ? 1680 GLU A C     1 
ATOM   2927  O O     . GLU A 1 1680 ? 195.628 203.698 166.759 1.00 28.18  ? 1680 GLU A O     1 
ATOM   2928  C CB    . GLU A 1 1680 ? 195.851 200.815 167.061 1.00 28.18  ? 1680 GLU A CB    1 
ATOM   2929  C CG    . GLU A 1 1680 ? 195.550 199.328 167.174 1.00 28.18  ? 1680 GLU A CG    1 
ATOM   2930  C CD    . GLU A 1 1680 ? 194.350 199.034 168.055 1.00 28.18  ? 1680 GLU A CD    1 
ATOM   2931  O OE1   . GLU A 1 1680 ? 194.374 198.006 168.764 1.00 28.18  ? 1680 GLU A OE1   1 
ATOM   2932  O OE2   . GLU A 1 1680 ? 193.384 199.826 168.042 1.00 28.18  ? 1680 GLU A OE2   1 
ATOM   2933  N N     . GLY A 1 1681 ? 196.066 203.322 164.586 1.00 25.15  ? 1681 GLY A N     1 
ATOM   2934  C CA    . GLY A 1 1681 ? 196.598 204.643 164.341 1.00 25.15  ? 1681 GLY A CA    1 
ATOM   2935  C C     . GLY A 1 1681 ? 198.108 204.720 164.283 1.00 25.15  ? 1681 GLY A C     1 
ATOM   2936  O O     . GLY A 1 1681 ? 198.642 205.770 163.904 1.00 25.15  ? 1681 GLY A O     1 
ATOM   2937  N N     . GLU A 1 1682 ? 198.809 203.651 164.648 1.00 23.76  ? 1682 GLU A N     1 
ATOM   2938  C CA    . GLU A 1 1682 ? 200.260 203.641 164.549 1.00 23.76  ? 1682 GLU A CA    1 
ATOM   2939  C C     . GLU A 1 1682 ? 200.688 203.698 163.089 1.00 23.76  ? 1682 GLU A C     1 
ATOM   2940  O O     . GLU A 1 1682 ? 200.143 202.991 162.238 1.00 23.76  ? 1682 GLU A O     1 
ATOM   2941  C CB    . GLU A 1 1682 ? 200.831 202.391 165.214 1.00 23.76  ? 1682 GLU A CB    1 
ATOM   2942  C CG    . GLU A 1 1682 ? 202.287 202.516 165.611 1.00 23.76  ? 1682 GLU A CG    1 
ATOM   2943  C CD    . GLU A 1 1682 ? 202.791 201.293 166.341 1.00 23.76  ? 1682 GLU A CD    1 
ATOM   2944  O OE1   . GLU A 1 1682 ? 202.570 200.170 165.843 1.00 23.76  ? 1682 GLU A OE1   1 
ATOM   2945  O OE2   . GLU A 1 1682 ? 203.402 201.453 167.417 1.00 23.76  ? 1682 GLU A OE2   1 
ATOM   2946  N N     . GLU A 1 1683 ? 201.674 204.542 162.802 1.00 26.44  ? 1683 GLU A N     1 
ATOM   2947  C CA    . GLU A 1 1683 ? 202.123 204.786 161.440 1.00 26.44  ? 1683 GLU A CA    1 
ATOM   2948  C C     . GLU A 1 1683 ? 203.603 204.461 161.306 1.00 26.44  ? 1683 GLU A C     1 
ATOM   2949  O O     . GLU A 1 1683 ? 204.405 204.789 162.185 1.00 26.44  ? 1683 GLU A O     1 
ATOM   2950  C CB    . GLU A 1 1683 ? 201.873 206.240 161.029 1.00 26.44  ? 1683 GLU A CB    1 
ATOM   2951  C CG    . GLU A 1 1683 ? 200.505 206.766 161.422 1.00 26.44  ? 1683 GLU A CG    1 
ATOM   2952  C CD    . GLU A 1 1683 ? 200.118 208.011 160.653 1.00 26.44  ? 1683 GLU A CD    1 
ATOM   2953  O OE1   . GLU A 1 1683 ? 200.824 208.355 159.682 1.00 26.44  ? 1683 GLU A OE1   1 
ATOM   2954  O OE2   . GLU A 1 1683 ? 199.106 208.646 161.018 1.00 26.44  ? 1683 GLU A OE2   1 
ATOM   2955  N N     . VAL A 1 1684 ? 203.954 203.812 160.199 1.00 23.81  ? 1684 VAL A N     1 
ATOM   2956  C CA    . VAL A 1 1684 ? 205.338 203.513 159.852 1.00 23.81  ? 1684 VAL A CA    1 
ATOM   2957  C C     . VAL A 1 1684 ? 205.667 204.280 158.581 1.00 23.81  ? 1684 VAL A C     1 
ATOM   2958  O O     . VAL A 1 1684 ? 205.014 204.092 157.547 1.00 23.81  ? 1684 VAL A O     1 
ATOM   2959  C CB    . VAL A 1 1684 ? 205.564 202.006 159.661 1.00 23.81  ? 1684 VAL A CB    1 
ATOM   2960  C CG1   . VAL A 1 1684 ? 206.889 201.752 158.963 1.00 23.81  ? 1684 VAL A CG1   1 
ATOM   2961  C CG2   . VAL A 1 1684 ? 205.521 201.293 161.000 1.00 23.81  ? 1684 VAL A CG2   1 
ATOM   2962  N N     . MET A 1 1685 ? 206.675 205.144 158.655 1.00 24.97  ? 1685 MET A N     1 
ATOM   2963  C CA    . MET A 1 1685 ? 207.080 205.954 157.517 1.00 24.97  ? 1685 MET A CA    1 
ATOM   2964  C C     . MET A 1 1685 ? 208.230 205.277 156.786 1.00 24.97  ? 1685 MET A C     1 
ATOM   2965  O O     . MET A 1 1685 ? 209.249 204.938 157.395 1.00 24.97  ? 1685 MET A O     1 
ATOM   2966  C CB    . MET A 1 1685 ? 207.490 207.356 157.969 1.00 24.97  ? 1685 MET A CB    1 
ATOM   2967  C CG    . MET A 1 1685 ? 206.337 208.202 158.475 1.00 24.97  ? 1685 MET A CG    1 
ATOM   2968  S SD    . MET A 1 1685 ? 205.138 208.569 157.181 1.00 24.97  ? 1685 MET A SD    1 
ATOM   2969  C CE    . MET A 1 1685 ? 203.619 208.039 157.966 1.00 24.97  ? 1685 MET A CE    1 
ATOM   2970  N N     . PHE A 1 1686 ? 208.061 205.081 155.482 1.00 24.42  ? 1686 PHE A N     1 
ATOM   2971  C CA    . PHE A 1 1686 ? 209.085 204.428 154.682 1.00 24.42  ? 1686 PHE A CA    1 
ATOM   2972  C C     . PHE A 1 1686 ? 210.346 205.279 154.625 1.00 24.42  ? 1686 PHE A C     1 
ATOM   2973  O O     . PHE A 1 1686 ? 210.284 206.505 154.499 1.00 24.42  ? 1686 PHE A O     1 
ATOM   2974  C CB    . PHE A 1 1686 ? 208.567 204.171 153.269 1.00 24.42  ? 1686 PHE A CB    1 
ATOM   2975  C CG    . PHE A 1 1686 ? 207.468 203.154 153.202 1.00 24.42  ? 1686 PHE A CG    1 
ATOM   2976  C CD1   . PHE A 1 1686 ? 207.364 202.162 154.159 1.00 24.42  ? 1686 PHE A CD1   1 
ATOM   2977  C CD2   . PHE A 1 1686 ? 206.542 203.185 152.174 1.00 24.42  ? 1686 PHE A CD2   1 
ATOM   2978  C CE1   . PHE A 1 1686 ? 206.354 201.224 154.095 1.00 24.42  ? 1686 PHE A CE1   1 
ATOM   2979  C CE2   . PHE A 1 1686 ? 205.532 202.250 152.106 1.00 24.42  ? 1686 PHE A CE2   1 
ATOM   2980  C CZ    . PHE A 1 1686 ? 205.439 201.268 153.066 1.00 24.42  ? 1686 PHE A CZ    1 
ATOM   2981  N N     . LYS A 1 1687 ? 211.502 204.618 154.728 1.00 23.38  ? 1687 LYS A N     1 
ATOM   2982  C CA    . LYS A 1 1687 ? 212.768 205.331 154.603 1.00 23.38  ? 1687 LYS A CA    1 
ATOM   2983  C C     . LYS A 1 1687 ? 212.935 205.909 153.203 1.00 23.38  ? 1687 LYS A C     1 
ATOM   2984  O O     . LYS A 1 1687 ? 213.362 207.058 153.042 1.00 23.38  ? 1687 LYS A O     1 
ATOM   2985  C CB    . LYS A 1 1687 ? 213.929 204.400 154.947 1.00 23.38  ? 1687 LYS A CB    1 
ATOM   2986  C CG    . LYS A 1 1687 ? 213.611 203.401 156.046 1.00 23.38  ? 1687 LYS A CG    1 
ATOM   2987  C CD    . LYS A 1 1687 ? 213.624 204.056 157.416 1.00 23.38  ? 1687 LYS A CD    1 
ATOM   2988  C CE    . LYS A 1 1687 ? 214.973 204.682 157.717 1.00 23.38  ? 1687 LYS A CE    1 
ATOM   2989  N NZ    . LYS A 1 1687 ? 214.988 205.344 159.050 1.00 23.38  ? 1687 LYS A NZ    1 
ATOM   2990  N N     . THR A 1 1688 ? 212.603 205.127 152.179 1.00 25.65  ? 1688 THR A N     1 
ATOM   2991  C CA    . THR A 1 1688 ? 212.594 205.596 150.793 1.00 25.65  ? 1688 THR A CA    1 
ATOM   2992  C C     . THR A 1 1688 ? 211.189 205.416 150.237 1.00 25.65  ? 1688 THR A C     1 
ATOM   2993  O O     . THR A 1 1688 ? 210.827 204.304 149.811 1.00 25.65  ? 1688 THR A O     1 
ATOM   2994  C CB    . THR A 1 1688 ? 213.610 204.838 149.940 1.00 25.65  ? 1688 THR A CB    1 
ATOM   2995  O OG1   . THR A 1 1688 ? 213.240 203.456 149.868 1.00 25.65  ? 1688 THR A OG1   1 
ATOM   2996  C CG2   . THR A 1 1688 ? 215.003 204.954 150.540 1.00 25.65  ? 1688 THR A CG2   1 
ATOM   2997  N N     . PRO A 1 1689 ? 210.364 206.462 150.227 1.00 29.14  ? 1689 PRO A N     1 
ATOM   2998  C CA    . PRO A 1 1689 ? 208.977 206.303 149.776 1.00 29.14  ? 1689 PRO A CA    1 
ATOM   2999  C C     . PRO A 1 1689 ? 208.905 205.841 148.329 1.00 29.14  ? 1689 PRO A C     1 
ATOM   3000  O O     . PRO A 1 1689 ? 209.712 206.240 147.488 1.00 29.14  ? 1689 PRO A O     1 
ATOM   3001  C CB    . PRO A 1 1689 ? 208.384 207.707 149.947 1.00 29.14  ? 1689 PRO A CB    1 
ATOM   3002  C CG    . PRO A 1 1689 ? 209.301 208.406 150.901 1.00 29.14  ? 1689 PRO A CG    1 
ATOM   3003  C CD    . PRO A 1 1689 ? 210.659 207.842 150.644 1.00 29.14  ? 1689 PRO A CD    1 
ATOM   3004  N N     . VAL A 1 1690 ? 207.926 204.988 148.046 1.00 33.40  ? 1690 VAL A N     1 
ATOM   3005  C CA    . VAL A 1 1690 ? 207.690 204.472 146.703 1.00 33.40  ? 1690 VAL A CA    1 
ATOM   3006  C C     . VAL A 1 1690 ? 206.686 205.376 146.006 1.00 33.40  ? 1690 VAL A C     1 
ATOM   3007  O O     . VAL A 1 1690 ? 205.882 206.053 146.659 1.00 33.40  ? 1690 VAL A O     1 
ATOM   3008  C CB    . VAL A 1 1690 ? 207.195 203.015 146.740 1.00 33.40  ? 1690 VAL A CB    1 
ATOM   3009  C CG1   . VAL A 1 1690 ? 208.138 202.158 147.566 1.00 33.40  ? 1690 VAL A CG1   1 
ATOM   3010  C CG2   . VAL A 1 1690 ? 205.784 202.947 147.294 1.00 33.40  ? 1690 VAL A CG2   1 
ATOM   3011  N N     . SER A 1 1691 ? 206.737 205.396 144.678 1.00 40.46  ? 1691 SER A N     1 
ATOM   3012  C CA    . SER A 1 1691 ? 205.891 206.260 143.870 1.00 40.46  ? 1691 SER A CA    1 
ATOM   3013  C C     . SER A 1 1691 ? 204.952 205.423 143.014 1.00 40.46  ? 1691 SER A C     1 
ATOM   3014  O O     . SER A 1 1691 ? 205.371 204.445 142.389 1.00 40.46  ? 1691 SER A O     1 
ATOM   3015  C CB    . SER A 1 1691 ? 206.736 207.169 142.976 1.00 40.46  ? 1691 SER A CB    1 
ATOM   3016  O OG    . SER A 1 1691 ? 207.802 206.446 142.385 1.00 40.46  ? 1691 SER A OG    1 
ATOM   3017  N N     . ILE A 1 1692 ? 203.678 205.814 142.991 1.00 42.88  ? 1692 ILE A N     1 
ATOM   3018  C CA    . ILE A 1 1692 ? 202.713 205.119 142.148 1.00 42.88  ? 1692 ILE A CA    1 
ATOM   3019  C C     . ILE A 1 1692 ? 202.825 205.584 140.700 1.00 42.88  ? 1692 ILE A C     1 
ATOM   3020  O O     . ILE A 1 1692 ? 202.567 204.808 139.773 1.00 42.88  ? 1692 ILE A O     1 
ATOM   3021  C CB    . ILE A 1 1692 ? 201.290 205.316 142.699 1.00 42.88  ? 1692 ILE A CB    1 
ATOM   3022  C CG1   . ILE A 1 1692 ? 201.195 204.773 144.125 1.00 42.88  ? 1692 ILE A CG1   1 
ATOM   3023  C CG2   . ILE A 1 1692 ? 200.262 204.626 141.817 1.00 42.88  ? 1692 ILE A CG2   1 
ATOM   3024  C CD1   . ILE A 1 1692 ? 199.898 205.115 144.819 1.00 42.88  ? 1692 ILE A CD1   1 
ATOM   3025  N N     . THR A 1 1693 ? 203.224 206.838 140.474 1.00 47.20  ? 1693 THR A N     1 
ATOM   3026  C CA    . THR A 1 1693 ? 203.322 207.344 139.108 1.00 47.20  ? 1693 THR A CA    1 
ATOM   3027  C C     . THR A 1 1693 ? 204.438 206.650 138.333 1.00 47.20  ? 1693 THR A C     1 
ATOM   3028  O O     . THR A 1 1693 ? 204.332 206.462 137.116 1.00 47.20  ? 1693 THR A O     1 
ATOM   3029  C CB    . THR A 1 1693 ? 203.524 208.862 139.118 1.00 47.20  ? 1693 THR A CB    1 
ATOM   3030  O OG1   . THR A 1 1693 ? 203.497 209.360 137.775 1.00 47.20  ? 1693 THR A OG1   1 
ATOM   3031  C CG2   . THR A 1 1693 ? 204.842 209.243 139.782 1.00 47.20  ? 1693 THR A CG2   1 
ATOM   3032  N N     . GLU A 1 1694 ? 205.517 206.262 139.018 1.00 46.62  ? 1694 GLU A N     1 
ATOM   3033  C CA    . GLU A 1 1694 ? 206.599 205.554 138.343 1.00 46.62  ? 1694 GLU A CA    1 
ATOM   3034  C C     . GLU A 1 1694 ? 206.246 204.094 138.091 1.00 46.62  ? 1694 GLU A C     1 
ATOM   3035  O O     . GLU A 1 1694 ? 206.739 203.496 137.128 1.00 46.62  ? 1694 GLU A O     1 
ATOM   3036  C CB    . GLU A 1 1694 ? 207.887 205.661 139.159 1.00 46.62  ? 1694 GLU A CB    1 
ATOM   3037  C CG    . GLU A 1 1694 ? 208.447 207.071 139.234 1.00 46.62  ? 1694 GLU A CG    1 
ATOM   3038  C CD    . GLU A 1 1694 ? 209.930 207.095 139.543 1.00 46.62  ? 1694 GLU A CD    1 
ATOM   3039  O OE1   . GLU A 1 1694 ? 210.628 206.121 139.190 1.00 46.62  ? 1694 GLU A OE1   1 
ATOM   3040  O OE2   . GLU A 1 1694 ? 210.398 208.089 140.136 1.00 46.62  ? 1694 GLU A OE2   1 
ATOM   3041  N N     . HIS A 1 1695 ? 205.403 203.506 138.938 1.00 44.22  ? 1695 HIS A N     1 
ATOM   3042  C CA    . HIS A 1 1695 ? 204.951 202.123 138.785 1.00 44.22  ? 1695 HIS A CA    1 
ATOM   3043  C C     . HIS A 1 1695 ? 203.430 202.127 138.837 1.00 44.22  ? 1695 HIS A C     1 
ATOM   3044  O O     . HIS A 1 1695 ? 202.831 201.820 139.877 1.00 44.22  ? 1695 HIS A O     1 
ATOM   3045  C CB    . HIS A 1 1695 ? 205.545 201.223 139.865 1.00 44.22  ? 1695 HIS A CB    1 
ATOM   3046  C CG    . HIS A 1 1695 ? 207.042 201.201 139.878 1.00 44.22  ? 1695 HIS A CG    1 
ATOM   3047  N ND1   . HIS A 1 1695 ? 207.797 202.249 140.356 1.00 44.22  ? 1695 HIS A ND1   1 
ATOM   3048  C CD2   . HIS A 1 1695 ? 207.923 200.257 139.472 1.00 44.22  ? 1695 HIS A CD2   1 
ATOM   3049  C CE1   . HIS A 1 1695 ? 209.079 201.953 140.244 1.00 44.22  ? 1695 HIS A CE1   1 
ATOM   3050  N NE2   . HIS A 1 1695 ? 209.183 200.749 139.710 1.00 44.22  ? 1695 HIS A NE2   1 
ATOM   3051  N N     . PRO A 1 1696 ? 202.770 202.474 137.732 1.00 45.00  ? 1696 PRO A N     1 
ATOM   3052  C CA    . PRO A 1 1696 ? 201.310 202.639 137.763 1.00 45.00  ? 1696 PRO A CA    1 
ATOM   3053  C C     . PRO A 1 1696 ? 200.551 201.331 137.920 1.00 45.00  ? 1696 PRO A C     1 
ATOM   3054  O O     . PRO A 1 1696 ? 199.415 201.327 138.406 1.00 45.00  ? 1696 PRO A O     1 
ATOM   3055  C CB    . PRO A 1 1696 ? 201.006 203.304 136.415 1.00 45.00  ? 1696 PRO A CB    1 
ATOM   3056  C CG    . PRO A 1 1696 ? 202.114 202.876 135.520 1.00 45.00  ? 1696 PRO A CG    1 
ATOM   3057  C CD    . PRO A 1 1696 ? 203.327 202.629 136.377 1.00 45.00  ? 1696 PRO A CD    1 
ATOM   3058  N N     . LYS A 1 1697 ? 201.156 200.220 137.513 1.00 39.97  ? 1697 LYS A N     1 
ATOM   3059  C CA    . LYS A 1 1697 ? 200.479 198.934 137.605 1.00 39.97  ? 1697 LYS A CA    1 
ATOM   3060  C C     . LYS A 1 1697 ? 200.332 198.529 139.067 1.00 39.97  ? 1697 LYS A C     1 
ATOM   3061  O O     . LYS A 1 1697 ? 201.259 198.686 139.865 1.00 39.97  ? 1697 LYS A O     1 
ATOM   3062  C CB    . LYS A 1 1697 ? 201.252 197.873 136.824 1.00 39.97  ? 1697 LYS A CB    1 
ATOM   3063  C CG    . LYS A 1 1697 ? 200.443 196.634 136.485 1.00 39.97  ? 1697 LYS A CG    1 
ATOM   3064  C CD    . LYS A 1 1697 ? 201.221 195.714 135.560 1.00 39.97  ? 1697 LYS A CD    1 
ATOM   3065  C CE    . LYS A 1 1697 ? 200.328 194.632 134.977 1.00 39.97  ? 1697 LYS A CE    1 
ATOM   3066  N NZ    . LYS A 1 1697 ? 199.826 193.689 136.008 1.00 39.97  ? 1697 LYS A NZ    1 
ATOM   3067  N N     . ILE A 1 1698 ? 199.155 198.003 139.414 1.00 36.22  ? 1698 ILE A N     1 
ATOM   3068  C CA    . ILE A 1 1698 ? 198.814 197.782 140.819 1.00 36.22  ? 1698 ILE A CA    1 
ATOM   3069  C C     . ILE A 1 1698 ? 199.782 196.799 141.473 1.00 36.22  ? 1698 ILE A C     1 
ATOM   3070  O O     . ILE A 1 1698 ? 200.290 197.047 142.577 1.00 36.22  ? 1698 ILE A O     1 
ATOM   3071  C CB    . ILE A 1 1698 ? 197.345 197.321 140.941 1.00 36.22  ? 1698 ILE A CB    1 
ATOM   3072  C CG1   . ILE A 1 1698 ? 196.925 197.194 142.408 1.00 36.22  ? 1698 ILE A CG1   1 
ATOM   3073  C CG2   . ILE A 1 1698 ? 197.086 196.033 140.160 1.00 36.22  ? 1698 ILE A CG2   1 
ATOM   3074  C CD1   . ILE A 1 1698 ? 196.807 198.512 143.127 1.00 36.22  ? 1698 ILE A CD1   1 
ATOM   3075  N N     . ASN A 1 1699 ? 200.078 195.689 140.794 1.00 38.45  ? 1699 ASN A N     1 
ATOM   3076  C CA    . ASN A 1 1699 ? 200.861 194.624 141.411 1.00 38.45  ? 1699 ASN A CA    1 
ATOM   3077  C C     . ASN A 1 1699 ? 202.287 195.073 141.703 1.00 38.45  ? 1699 ASN A C     1 
ATOM   3078  O O     . ASN A 1 1699 ? 202.826 194.796 142.781 1.00 38.45  ? 1699 ASN A O     1 
ATOM   3079  C CB    . ASN A 1 1699 ? 200.851 193.384 140.516 1.00 38.45  ? 1699 ASN A CB    1 
ATOM   3080  C CG    . ASN A 1 1699 ? 201.414 193.653 139.131 1.00 38.45  ? 1699 ASN A CG    1 
ATOM   3081  O OD1   . ASN A 1 1699 ? 201.940 194.730 138.854 1.00 38.45  ? 1699 ASN A OD1   1 
ATOM   3082  N ND2   . ASN A 1 1699 ? 201.310 192.665 138.253 1.00 38.45  ? 1699 ASN A ND2   1 
ATOM   3083  N N     . GLU A 1 1700 ? 202.915 195.772 140.756 1.00 38.78  ? 1700 GLU A N     1 
ATOM   3084  C CA    . GLU A 1 1700 ? 204.316 196.140 140.927 1.00 38.78  ? 1700 GLU A CA    1 
ATOM   3085  C C     . GLU A 1 1700 ? 204.492 197.146 142.059 1.00 38.78  ? 1700 GLU A C     1 
ATOM   3086  O O     . GLU A 1 1700 ? 205.398 197.005 142.888 1.00 38.78  ? 1700 GLU A O     1 
ATOM   3087  C CB    . GLU A 1 1700 ? 204.888 196.672 139.610 1.00 38.78  ? 1700 GLU A CB    1 
ATOM   3088  C CG    . GLU A 1 1700 ? 204.169 197.875 139.030 1.00 38.78  ? 1700 GLU A CG    1 
ATOM   3089  C CD    . GLU A 1 1700 ? 204.731 198.298 137.687 1.00 38.78  ? 1700 GLU A CD    1 
ATOM   3090  O OE1   . GLU A 1 1700 ? 205.702 197.665 137.222 1.00 38.78  ? 1700 GLU A OE1   1 
ATOM   3091  O OE2   . GLU A 1 1700 ? 204.202 199.263 137.096 1.00 38.78  ? 1700 GLU A OE2   1 
ATOM   3092  N N     . TRP A 1 1701 ? 203.620 198.155 142.137 1.00 35.82  ? 1701 TRP A N     1 
ATOM   3093  C CA    . TRP A 1 1701 ? 203.788 199.135 143.204 1.00 35.82  ? 1701 TRP A CA    1 
ATOM   3094  C C     . TRP A 1 1701 ? 203.347 198.578 144.552 1.00 35.82  ? 1701 TRP A C     1 
ATOM   3095  O O     . TRP A 1 1701 ? 203.906 198.963 145.582 1.00 35.82  ? 1701 TRP A O     1 
ATOM   3096  C CB    . TRP A 1 1701 ? 203.067 200.446 142.869 1.00 35.82  ? 1701 TRP A CB    1 
ATOM   3097  C CG    . TRP A 1 1701 ? 201.592 200.492 143.115 1.00 35.82  ? 1701 TRP A CG    1 
ATOM   3098  C CD1   . TRP A 1 1701 ? 200.609 200.294 142.197 1.00 35.82  ? 1701 TRP A CD1   1 
ATOM   3099  C CD2   . TRP A 1 1701 ? 200.930 200.799 144.349 1.00 35.82  ? 1701 TRP A CD2   1 
ATOM   3100  N NE1   . TRP A 1 1701 ? 199.376 200.438 142.779 1.00 35.82  ? 1701 TRP A NE1   1 
ATOM   3101  C CE2   . TRP A 1 1701 ? 199.545 200.747 144.102 1.00 35.82  ? 1701 TRP A CE2   1 
ATOM   3102  C CE3   . TRP A 1 1701 ? 201.373 201.100 145.638 1.00 35.82  ? 1701 TRP A CE3   1 
ATOM   3103  C CZ2   . TRP A 1 1701 ? 198.599 200.984 145.096 1.00 35.82  ? 1701 TRP A CZ2   1 
ATOM   3104  C CZ3   . TRP A 1 1701 ? 200.432 201.335 146.624 1.00 35.82  ? 1701 TRP A CZ3   1 
ATOM   3105  C CH2   . TRP A 1 1701 ? 199.062 201.277 146.347 1.00 35.82  ? 1701 TRP A CH2   1 
ATOM   3106  N N     . LEU A 1 1702 ? 202.393 197.641 144.577 1.00 31.01  ? 1702 LEU A N     1 
ATOM   3107  C CA    . LEU A 1 1702 ? 202.092 196.972 145.841 1.00 31.01  ? 1702 LEU A CA    1 
ATOM   3108  C C     . LEU A 1 1702 ? 203.265 196.114 146.311 1.00 31.01  ? 1702 LEU A C     1 
ATOM   3109  O O     . LEU A 1 1702 ? 203.568 196.067 147.510 1.00 31.01  ? 1702 LEU A O     1 
ATOM   3110  C CB    . LEU A 1 1702 ? 200.822 196.134 145.714 1.00 31.01  ? 1702 LEU A CB    1 
ATOM   3111  C CG    . LEU A 1 1702 ? 199.521 196.919 145.886 1.00 31.01  ? 1702 LEU A CG    1 
ATOM   3112  C CD1   . LEU A 1 1702 ? 198.315 196.015 145.729 1.00 31.01  ? 1702 LEU A CD1   1 
ATOM   3113  C CD2   . LEU A 1 1702 ? 199.497 197.612 147.236 1.00 31.01  ? 1702 LEU A CD2   1 
ATOM   3114  N N     . THR A 1 1703 ? 203.938 195.428 145.383 1.00 29.68  ? 1703 THR A N     1 
ATOM   3115  C CA    . THR A 1 1703 ? 205.117 194.650 145.753 1.00 29.68  ? 1703 THR A CA    1 
ATOM   3116  C C     . THR A 1 1703 ? 206.235 195.554 146.257 1.00 29.68  ? 1703 THR A C     1 
ATOM   3117  O O     . THR A 1 1703 ? 206.929 195.219 147.226 1.00 29.68  ? 1703 THR A O     1 
ATOM   3118  C CB    . THR A 1 1703 ? 205.594 193.820 144.563 1.00 29.68  ? 1703 THR A CB    1 
ATOM   3119  O OG1   . THR A 1 1703 ? 204.529 192.976 144.111 1.00 29.68  ? 1703 THR A OG1   1 
ATOM   3120  C CG2   . THR A 1 1703 ? 206.780 192.955 144.957 1.00 29.68  ? 1703 THR A CG2   1 
ATOM   3121  N N     . LEU A 1 1704 ? 206.429 196.703 145.606 1.00 29.14  ? 1704 LEU A N     1 
ATOM   3122  C CA    . LEU A 1 1704 ? 207.395 197.677 146.105 1.00 29.14  ? 1704 LEU A CA    1 
ATOM   3123  C C     . LEU A 1 1704 ? 207.014 198.166 147.496 1.00 29.14  ? 1704 LEU A C     1 
ATOM   3124  O O     . LEU A 1 1704 ? 207.885 198.350 148.353 1.00 29.14  ? 1704 LEU A O     1 
ATOM   3125  C CB    . LEU A 1 1704 ? 207.521 198.852 145.134 1.00 29.14  ? 1704 LEU A CB    1 
ATOM   3126  C CG    . LEU A 1 1704 ? 208.597 198.777 144.045 1.00 29.14  ? 1704 LEU A CG    1 
ATOM   3127  C CD1   . LEU A 1 1704 ? 209.979 198.817 144.677 1.00 29.14  ? 1704 LEU A CD1   1 
ATOM   3128  C CD2   . LEU A 1 1704 ? 208.455 197.541 143.176 1.00 29.14  ? 1704 LEU A CD2   1 
ATOM   3129  N N     . VAL A 1 1705 ? 205.718 198.376 147.742 1.00 28.97  ? 1705 VAL A N     1 
ATOM   3130  C CA    . VAL A 1 1705 ? 205.265 198.786 149.069 1.00 28.97  ? 1705 VAL A CA    1 
ATOM   3131  C C     . VAL A 1 1705 ? 205.632 197.733 150.105 1.00 28.97  ? 1705 VAL A C     1 
ATOM   3132  O O     . VAL A 1 1705 ? 206.139 198.051 151.185 1.00 28.97  ? 1705 VAL A O     1 
ATOM   3133  C CB    . VAL A 1 1705 ? 203.750 199.058 149.062 1.00 28.97  ? 1705 VAL A CB    1 
ATOM   3134  C CG1   . VAL A 1 1705 ? 203.204 199.048 150.479 1.00 28.97  ? 1705 VAL A CG1   1 
ATOM   3135  C CG2   . VAL A 1 1705 ? 203.457 200.390 148.404 1.00 28.97  ? 1705 VAL A CG2   1 
ATOM   3136  N N     . GLU A 1 1706 ? 205.385 196.462 149.789 1.00 25.61  ? 1706 GLU A N     1 
ATOM   3137  C CA    . GLU A 1 1706 ? 205.680 195.392 150.742 1.00 25.61  ? 1706 GLU A CA    1 
ATOM   3138  C C     . GLU A 1 1706 ? 207.180 195.287 151.012 1.00 25.61  ? 1706 GLU A C     1 
ATOM   3139  O O     . GLU A 1 1706 ? 207.614 195.160 152.168 1.00 25.61  ? 1706 GLU A O     1 
ATOM   3140  C CB    . GLU A 1 1706 ? 205.125 194.068 150.219 1.00 25.61  ? 1706 GLU A CB    1 
ATOM   3141  C CG    . GLU A 1 1706 ? 205.774 192.837 150.819 1.00 25.61  ? 1706 GLU A CG    1 
ATOM   3142  C CD    . GLU A 1 1706 ? 205.151 191.550 150.316 1.00 25.61  ? 1706 GLU A CD    1 
ATOM   3143  O OE1   . GLU A 1 1706 ? 205.003 191.402 149.085 1.00 25.61  ? 1706 GLU A OE1   1 
ATOM   3144  O OE2   . GLU A 1 1706 ? 204.812 190.685 151.150 1.00 25.61  ? 1706 GLU A OE2   1 
ATOM   3145  N N     . LYS A 1 1707 ? 207.991 195.341 149.953 1.00 23.77  ? 1707 LYS A N     1 
ATOM   3146  C CA    . LYS A 1 1707 ? 209.437 195.233 150.128 1.00 23.77  ? 1707 LYS A CA    1 
ATOM   3147  C C     . LYS A 1 1707 ? 209.987 196.411 150.922 1.00 23.77  ? 1707 LYS A C     1 
ATOM   3148  O O     . LYS A 1 1707 ? 210.837 196.235 151.806 1.00 23.77  ? 1707 LYS A O     1 
ATOM   3149  C CB    . LYS A 1 1707 ? 210.124 195.132 148.767 1.00 23.77  ? 1707 LYS A CB    1 
ATOM   3150  C CG    . LYS A 1 1707 ? 211.638 195.217 148.831 1.00 23.77  ? 1707 LYS A CG    1 
ATOM   3151  C CD    . LYS A 1 1707 ? 212.247 195.266 147.440 1.00 23.77  ? 1707 LYS A CD    1 
ATOM   3152  C CE    . LYS A 1 1707 ? 212.484 196.697 146.989 1.00 23.77  ? 1707 LYS A CE    1 
ATOM   3153  N NZ    . LYS A 1 1707 ? 213.597 197.336 147.744 1.00 23.77  ? 1707 LYS A NZ    1 
ATOM   3154  N N     . GLU A 1 1708 ? 209.508 197.623 150.629 1.00 23.80  ? 1708 GLU A N     1 
ATOM   3155  C CA    . GLU A 1 1708 ? 209.954 198.788 151.378 1.00 23.80  ? 1708 GLU A CA    1 
ATOM   3156  C C     . GLU A 1 1708 ? 209.473 198.737 152.819 1.00 23.80  ? 1708 GLU A C     1 
ATOM   3157  O O     . GLU A 1 1708 ? 210.175 199.206 153.717 1.00 23.80  ? 1708 GLU A O     1 
ATOM   3158  C CB    . GLU A 1 1708 ? 209.479 200.069 150.692 1.00 23.80  ? 1708 GLU A CB    1 
ATOM   3159  C CG    . GLU A 1 1708 ? 209.830 201.346 151.439 1.00 23.80  ? 1708 GLU A CG    1 
ATOM   3160  C CD    . GLU A 1 1708 ? 211.309 201.682 151.375 1.00 23.80  ? 1708 GLU A CD    1 
ATOM   3161  O OE1   . GLU A 1 1708 ? 212.058 200.970 150.676 1.00 23.80  ? 1708 GLU A OE1   1 
ATOM   3162  O OE2   . GLU A 1 1708 ? 211.725 202.666 152.022 1.00 23.80  ? 1708 GLU A OE2   1 
ATOM   3163  N N     . MET A 1 1709 ? 208.294 198.161 153.060 1.00 22.78  ? 1709 MET A N     1 
ATOM   3164  C CA    . MET A 1 1709 ? 207.851 197.918 154.428 1.00 22.78  ? 1709 MET A CA    1 
ATOM   3165  C C     . MET A 1 1709 ? 208.848 197.047 155.175 1.00 22.78  ? 1709 MET A C     1 
ATOM   3166  O O     . MET A 1 1709 ? 209.283 197.387 156.279 1.00 22.78  ? 1709 MET A O     1 
ATOM   3167  C CB    . MET A 1 1709 ? 206.475 197.255 154.420 1.00 22.78  ? 1709 MET A CB    1 
ATOM   3168  C CG    . MET A 1 1709 ? 205.904 197.002 155.799 1.00 22.78  ? 1709 MET A CG    1 
ATOM   3169  S SD    . MET A 1 1709 ? 204.272 196.241 155.731 1.00 22.78  ? 1709 MET A SD    1 
ATOM   3170  C CE    . MET A 1 1709 ? 204.686 194.587 155.183 1.00 22.78  ? 1709 MET A CE    1 
ATOM   3171  N N     . ARG A 1 1710 ? 209.228 195.916 154.581 1.00 19.78  ? 1710 ARG A N     1 
ATOM   3172  C CA    . ARG A 1 1710 ? 210.168 195.024 155.256 1.00 19.78  ? 1710 ARG A CA    1 
ATOM   3173  C C     . ARG A 1 1710 ? 211.507 195.713 155.500 1.00 19.78  ? 1710 ARG A C     1 
ATOM   3174  O O     . ARG A 1 1710 ? 212.091 195.591 156.586 1.00 19.78  ? 1710 ARG A O     1 
ATOM   3175  C CB    . ARG A 1 1710 ? 210.354 193.745 154.442 1.00 19.78  ? 1710 ARG A CB    1 
ATOM   3176  C CG    . ARG A 1 1710 ? 209.083 192.931 154.293 1.00 19.78  ? 1710 ARG A CG    1 
ATOM   3177  C CD    . ARG A 1 1710 ? 209.357 191.441 154.390 1.00 19.78  ? 1710 ARG A CD    1 
ATOM   3178  N NE    . ARG A 1 1710 ? 208.259 190.652 153.845 1.00 19.78  ? 1710 ARG A NE    1 
ATOM   3179  C CZ    . ARG A 1 1710 ? 208.124 190.335 152.564 1.00 19.78  ? 1710 ARG A CZ    1 
ATOM   3180  N NH1   . ARG A 1 1710 ? 209.010 190.721 151.660 1.00 19.78  ? 1710 ARG A NH1   1 
ATOM   3181  N NH2   . ARG A 1 1710 ? 207.074 189.615 152.181 1.00 19.78  ? 1710 ARG A NH2   1 
ATOM   3182  N N     . VAL A 1 1711 ? 212.001 196.459 154.509 1.00 20.06  ? 1711 VAL A N     1 
ATOM   3183  C CA    . VAL A 1 1711 ? 213.279 197.151 154.669 1.00 20.06  ? 1711 VAL A CA    1 
ATOM   3184  C C     . VAL A 1 1711 ? 213.193 198.200 155.774 1.00 20.06  ? 1711 VAL A C     1 
ATOM   3185  O O     . VAL A 1 1711 ? 214.121 198.352 156.582 1.00 20.06  ? 1711 VAL A O     1 
ATOM   3186  C CB    . VAL A 1 1711 ? 213.720 197.769 153.330 1.00 20.06  ? 1711 VAL A CB    1 
ATOM   3187  C CG1   . VAL A 1 1711 ? 214.897 198.709 153.535 1.00 20.06  ? 1711 VAL A CG1   1 
ATOM   3188  C CG2   . VAL A 1 1711 ? 214.074 196.676 152.335 1.00 20.06  ? 1711 VAL A CG2   1 
ATOM   3189  N N     . THR A 1 1712 ? 212.091 198.953 155.818 1.00 20.83  ? 1712 THR A N     1 
ATOM   3190  C CA    . THR A 1 1712 ? 211.928 199.982 156.839 1.00 20.83  ? 1712 THR A CA    1 
ATOM   3191  C C     . THR A 1 1712 ? 211.848 199.373 158.232 1.00 20.83  ? 1712 THR A C     1 
ATOM   3192  O O     . THR A 1 1712 ? 212.440 199.901 159.181 1.00 20.83  ? 1712 THR A O     1 
ATOM   3193  C CB    . THR A 1 1712 ? 210.682 200.815 156.542 1.00 20.83  ? 1712 THR A CB    1 
ATOM   3194  O OG1   . THR A 1 1712 ? 210.869 201.522 155.311 1.00 20.83  ? 1712 THR A OG1   1 
ATOM   3195  C CG2   . THR A 1 1712 ? 210.427 201.815 157.656 1.00 20.83  ? 1712 THR A CG2   1 
ATOM   3196  N N     . LEU A 1 1713 ? 211.118 198.264 158.376 1.00 16.14  ? 1713 LEU A N     1 
ATOM   3197  C CA    . LEU A 1 1713 ? 211.097 197.561 159.655 1.00 16.14  ? 1713 LEU A CA    1 
ATOM   3198  C C     . LEU A 1 1713 ? 212.493 197.102 160.054 1.00 16.14  ? 1713 LEU A C     1 
ATOM   3199  O O     . LEU A 1 1713 ? 212.876 197.210 161.224 1.00 16.14  ? 1713 LEU A O     1 
ATOM   3200  C CB    . LEU A 1 1713 ? 210.130 196.374 159.599 1.00 16.14  ? 1713 LEU A CB    1 
ATOM   3201  C CG    . LEU A 1 1713 ? 208.621 196.547 159.834 1.00 16.14  ? 1713 LEU A CG    1 
ATOM   3202  C CD1   . LEU A 1 1713 ? 208.391 197.008 161.235 1.00 16.14  ? 1713 LEU A CD1   1 
ATOM   3203  C CD2   . LEU A 1 1713 ? 207.951 197.524 158.896 1.00 16.14  ? 1713 LEU A CD2   1 
ATOM   3204  N N     . ALA A 1 1714 ? 213.274 196.596 159.096 1.00 16.27  ? 1714 ALA A N     1 
ATOM   3205  C CA    . ALA A 1 1714 ? 214.630 196.155 159.415 1.00 16.27  ? 1714 ALA A CA    1 
ATOM   3206  C C     . ALA A 1 1714 ? 215.496 197.318 159.895 1.00 16.27  ? 1714 ALA A C     1 
ATOM   3207  O O     . ALA A 1 1714 ? 216.216 197.202 160.895 1.00 16.27  ? 1714 ALA A O     1 
ATOM   3208  C CB    . ALA A 1 1714 ? 215.257 195.478 158.196 1.00 16.27  ? 1714 ALA A CB    1 
ATOM   3209  N N     . LYS A 1 1715 ? 215.432 198.454 159.196 1.00 16.80  ? 1715 LYS A N     1 
ATOM   3210  C CA    . LYS A 1 1715 ? 216.241 199.607 159.587 1.00 16.80  ? 1715 LYS A CA    1 
ATOM   3211  C C     . LYS A 1 1715 ? 215.817 200.148 160.949 1.00 16.80  ? 1715 LYS A C     1 
ATOM   3212  O O     . LYS A 1 1715 ? 216.666 200.509 161.779 1.00 16.80  ? 1715 LYS A O     1 
ATOM   3213  C CB    . LYS A 1 1715 ? 216.146 200.700 158.524 1.00 16.80  ? 1715 LYS A CB    1 
ATOM   3214  C CG    . LYS A 1 1715 ? 217.151 200.554 157.394 1.00 16.80  ? 1715 LYS A CG    1 
ATOM   3215  C CD    . LYS A 1 1715 ? 218.575 200.510 157.923 1.00 16.80  ? 1715 LYS A CD    1 
ATOM   3216  C CE    . LYS A 1 1715 ? 219.480 199.703 157.006 1.00 16.80  ? 1715 LYS A CE    1 
ATOM   3217  N NZ    . LYS A 1 1715 ? 220.920 199.963 157.279 1.00 16.80  ? 1715 LYS A NZ    1 
ATOM   3218  N N     . LEU A 1 1716 ? 214.506 200.216 161.193 1.00 16.16  ? 1716 LEU A N     1 
ATOM   3219  C CA    . LEU A 1 1716 ? 214.019 200.680 162.485 1.00 16.16  ? 1716 LEU A CA    1 
ATOM   3220  C C     . LEU A 1 1716 ? 214.450 199.739 163.601 1.00 16.16  ? 1716 LEU A C     1 
ATOM   3221  O O     . LEU A 1 1716 ? 214.801 200.188 164.697 1.00 16.16  ? 1716 LEU A O     1 
ATOM   3222  C CB    . LEU A 1 1716 ? 212.498 200.819 162.452 1.00 16.16  ? 1716 LEU A CB    1 
ATOM   3223  C CG    . LEU A 1 1716 ? 211.962 202.026 161.681 1.00 16.16  ? 1716 LEU A CG    1 
ATOM   3224  C CD1   . LEU A 1 1716 ? 210.467 202.176 161.896 1.00 16.16  ? 1716 LEU A CD1   1 
ATOM   3225  C CD2   . LEU A 1 1716 ? 212.695 203.291 162.089 1.00 16.16  ? 1716 LEU A CD2   1 
ATOM   3226  N N     . LEU A 1 1717 ? 214.429 198.429 163.342 1.00 13.67  ? 1717 LEU A N     1 
ATOM   3227  C CA    . LEU A 1 1717 ? 214.911 197.478 164.336 1.00 13.67  ? 1717 LEU A CA    1 
ATOM   3228  C C     . LEU A 1 1717 ? 216.391 197.684 164.617 1.00 13.67  ? 1717 LEU A C     1 
ATOM   3229  O O     . LEU A 1 1717 ? 216.824 197.610 165.770 1.00 13.67  ? 1717 LEU A O     1 
ATOM   3230  C CB    . LEU A 1 1717 ? 214.654 196.046 163.872 1.00 13.67  ? 1717 LEU A CB    1 
ATOM   3231  C CG    . LEU A 1 1717 ? 215.124 194.963 164.844 1.00 13.67  ? 1717 LEU A CG    1 
ATOM   3232  C CD1   . LEU A 1 1717 ? 214.505 195.172 166.213 1.00 13.67  ? 1717 LEU A CD1   1 
ATOM   3233  C CD2   . LEU A 1 1717 ? 214.802 193.580 164.315 1.00 13.67  ? 1717 LEU A CD2   1 
ATOM   3234  N N     . ALA A 1 1718 ? 217.184 197.939 163.575 1.00 15.72  ? 1718 ALA A N     1 
ATOM   3235  C CA    . ALA A 1 1718 ? 218.607 198.184 163.784 1.00 15.72  ? 1718 ALA A CA    1 
ATOM   3236  C C     . ALA A 1 1718 ? 218.828 199.402 164.675 1.00 15.72  ? 1718 ALA A C     1 
ATOM   3237  O O     . ALA A 1 1718 ? 219.607 199.354 165.636 1.00 15.72  ? 1718 ALA A O     1 
ATOM   3238  C CB    . ALA A 1 1718 ? 219.313 198.362 162.440 1.00 15.72  ? 1718 ALA A CB    1 
ATOM   3239  N N     . GLU A 1 1719 ? 218.128 200.501 164.382 1.00 18.37  ? 1719 GLU A N     1 
ATOM   3240  C CA    . GLU A 1 1719 ? 218.289 201.707 165.194 1.00 18.37  ? 1719 GLU A CA    1 
ATOM   3241  C C     . GLU A 1 1719 ? 217.812 201.486 166.628 1.00 18.37  ? 1719 GLU A C     1 
ATOM   3242  O O     . GLU A 1 1719 ? 218.467 201.923 167.587 1.00 18.37  ? 1719 GLU A O     1 
ATOM   3243  C CB    . GLU A 1 1719 ? 217.543 202.877 164.555 1.00 18.37  ? 1719 GLU A CB    1 
ATOM   3244  C CG    . GLU A 1 1719 ? 218.173 203.390 163.272 1.00 18.37  ? 1719 GLU A CG    1 
ATOM   3245  C CD    . GLU A 1 1719 ? 217.203 204.191 162.426 1.00 18.37  ? 1719 GLU A CD    1 
ATOM   3246  O OE1   . GLU A 1 1719 ? 216.266 204.785 162.998 1.00 18.37  ? 1719 GLU A OE1   1 
ATOM   3247  O OE2   . GLU A 1 1719 ? 217.379 204.228 161.191 1.00 18.37  ? 1719 GLU A OE2   1 
ATOM   3248  N N     . SER A 1 1720 ? 216.674 200.811 166.795 1.00 17.78  ? 1720 SER A N     1 
ATOM   3249  C CA    . SER A 1 1720 ? 216.142 200.576 168.131 1.00 17.78  ? 1720 SER A CA    1 
ATOM   3250  C C     . SER A 1 1720 ? 217.059 199.670 168.941 1.00 17.78  ? 1720 SER A C     1 
ATOM   3251  O O     . SER A 1 1720 ? 217.207 199.858 170.151 1.00 17.78  ? 1720 SER A O     1 
ATOM   3252  C CB    . SER A 1 1720 ? 214.738 199.985 168.038 1.00 17.78  ? 1720 SER A CB    1 
ATOM   3253  O OG    . SER A 1 1720 ? 214.074 200.058 169.285 1.00 17.78  ? 1720 SER A OG    1 
ATOM   3254  N N     . VAL A 1 1721 ? 217.681 198.681 168.296 1.00 17.77  ? 1721 VAL A N     1 
ATOM   3255  C CA    . VAL A 1 1721 ? 218.654 197.842 168.991 1.00 17.77  ? 1721 VAL A CA    1 
ATOM   3256  C C     . VAL A 1 1721 ? 219.879 198.660 169.374 1.00 17.77  ? 1721 VAL A C     1 
ATOM   3257  O O     . VAL A 1 1721 ? 220.441 198.492 170.464 1.00 17.77  ? 1721 VAL A O     1 
ATOM   3258  C CB    . VAL A 1 1721 ? 219.026 196.622 168.130 1.00 17.77  ? 1721 VAL A CB    1 
ATOM   3259  C CG1   . VAL A 1 1721 ? 220.240 195.916 168.703 1.00 17.77  ? 1721 VAL A CG1   1 
ATOM   3260  C CG2   . VAL A 1 1721 ? 217.855 195.661 168.057 1.00 17.77  ? 1721 VAL A CG2   1 
ATOM   3261  N N     . THR A 1 1722 ? 220.307 199.566 168.490 1.00 21.75  ? 1722 THR A N     1 
ATOM   3262  C CA    . THR A 1 1722 ? 221.430 200.439 168.819 1.00 21.75  ? 1722 THR A CA    1 
ATOM   3263  C C     . THR A 1 1722 ? 221.133 201.280 170.057 1.00 21.75  ? 1722 THR A C     1 
ATOM   3264  O O     . THR A 1 1722 ? 222.026 201.538 170.870 1.00 21.75  ? 1722 THR A O     1 
ATOM   3265  C CB    . THR A 1 1722 ? 221.763 201.338 167.628 1.00 21.75  ? 1722 THR A CB    1 
ATOM   3266  O OG1   . THR A 1 1722 ? 221.851 200.545 166.438 1.00 21.75  ? 1722 THR A OG1   1 
ATOM   3267  C CG2   . THR A 1 1722 ? 223.087 202.052 167.852 1.00 21.75  ? 1722 THR A CG2   1 
ATOM   3268  N N     . GLU A 1 1723 ? 219.887 201.730 170.207 1.00 23.87  ? 1723 GLU A N     1 
ATOM   3269  C CA    . GLU A 1 1723 ? 219.534 202.502 171.400 1.00 23.87  ? 1723 GLU A CA    1 
ATOM   3270  C C     . GLU A 1 1723 ? 219.384 201.610 172.634 1.00 23.87  ? 1723 GLU A C     1 
ATOM   3271  O O     . GLU A 1 1723 ? 219.811 201.978 173.740 1.00 23.87  ? 1723 GLU A O     1 
ATOM   3272  C CB    . GLU A 1 1723 ? 218.253 203.298 171.154 1.00 23.87  ? 1723 GLU A CB    1 
ATOM   3273  C CG    . GLU A 1 1723 ? 218.280 204.136 169.888 1.00 23.87  ? 1723 GLU A CG    1 
ATOM   3274  C CD    . GLU A 1 1723 ? 217.442 205.392 170.005 1.00 23.87  ? 1723 GLU A CD    1 
ATOM   3275  O OE1   . GLU A 1 1723 ? 216.812 205.591 171.064 1.00 23.87  ? 1723 GLU A OE1   1 
ATOM   3276  O OE2   . GLU A 1 1723 ? 217.412 206.181 169.037 1.00 23.87  ? 1723 GLU A OE2   1 
ATOM   3277  N N     . VAL A 1 1724 ? 218.776 200.432 172.472 1.00 23.82  ? 1724 VAL A N     1 
ATOM   3278  C CA    . VAL A 1 1724 ? 218.468 199.613 173.635 1.00 23.82  ? 1724 VAL A CA    1 
ATOM   3279  C C     . VAL A 1 1724 ? 219.707 198.898 174.156 1.00 23.82  ? 1724 VAL A C     1 
ATOM   3280  O O     . VAL A 1 1724 ? 219.720 198.465 175.310 1.00 23.82  ? 1724 VAL A O     1 
ATOM   3281  C CB    . VAL A 1 1724 ? 217.344 198.607 173.316 1.00 23.82  ? 1724 VAL A CB    1 
ATOM   3282  C CG1   . VAL A 1 1724 ? 217.838 197.525 172.382 1.00 23.82  ? 1724 VAL A CG1   1 
ATOM   3283  C CG2   . VAL A 1 1724 ? 216.760 198.015 174.592 1.00 23.82  ? 1724 VAL A CG2   1 
ATOM   3284  N N     . GLU A 1 1725 ? 220.761 198.763 173.347 1.00 27.51  ? 1725 GLU A N     1 
ATOM   3285  C CA    . GLU A 1 1725 ? 222.013 198.257 173.900 1.00 27.51  ? 1725 GLU A CA    1 
ATOM   3286  C C     . GLU A 1 1725 ? 222.642 199.284 174.834 1.00 27.51  ? 1725 GLU A C     1 
ATOM   3287  O O     . GLU A 1 1725 ? 223.256 198.920 175.843 1.00 27.51  ? 1725 GLU A O     1 
ATOM   3288  C CB    . GLU A 1 1725 ? 222.986 197.866 172.786 1.00 27.51  ? 1725 GLU A CB    1 
ATOM   3289  C CG    . GLU A 1 1725 ? 223.479 199.018 171.931 1.00 27.51  ? 1725 GLU A CG    1 
ATOM   3290  C CD    . GLU A 1 1725 ? 224.389 198.568 170.806 1.00 27.51  ? 1725 GLU A CD    1 
ATOM   3291  O OE1   . GLU A 1 1725 ? 224.620 197.348 170.678 1.00 27.51  ? 1725 GLU A OE1   1 
ATOM   3292  O OE2   . GLU A 1 1725 ? 224.878 199.436 170.054 1.00 27.51  ? 1725 GLU A OE2   1 
ATOM   3293  N N     . ILE A 1 1726 ? 222.503 200.572 174.510 1.00 31.12  ? 1726 ILE A N     1 
ATOM   3294  C CA    . ILE A 1 1726 ? 222.947 201.622 175.421 1.00 31.12  ? 1726 ILE A CA    1 
ATOM   3295  C C     . ILE A 1 1726 ? 222.106 201.613 176.688 1.00 31.12  ? 1726 ILE A C     1 
ATOM   3296  O O     . ILE A 1 1726 ? 222.630 201.739 177.801 1.00 31.12  ? 1726 ILE A O     1 
ATOM   3297  C CB    . ILE A 1 1726 ? 222.900 202.995 174.726 1.00 31.12  ? 1726 ILE A CB    1 
ATOM   3298  C CG1   . ILE A 1 1726 ? 223.593 202.933 173.363 1.00 31.12  ? 1726 ILE A CG1   1 
ATOM   3299  C CG2   . ILE A 1 1726 ? 223.531 204.061 175.607 1.00 31.12  ? 1726 ILE A CG2   1 
ATOM   3300  C CD1   . ILE A 1 1726 ? 225.059 202.577 173.442 1.00 31.12  ? 1726 ILE A CD1   1 
ATOM   3301  N N     . PHE A 1 1727 ? 220.786 201.474 176.540 1.00 32.95  ? 1727 PHE A N     1 
ATOM   3302  C CA    . PHE A 1 1727 ? 219.919 201.430 177.718 1.00 32.95  ? 1727 PHE A CA    1 
ATOM   3303  C C     . PHE A 1 1727 ? 220.242 200.233 178.607 1.00 32.95  ? 1727 PHE A C     1 
ATOM   3304  O O     . PHE A 1 1727 ? 220.294 200.355 179.836 1.00 32.95  ? 1727 PHE A O     1 
ATOM   3305  C CB    . PHE A 1 1727 ? 218.449 201.405 177.306 1.00 32.95  ? 1727 PHE A CB    1 
ATOM   3306  C CG    . PHE A 1 1727 ? 217.972 202.680 176.686 1.00 32.95  ? 1727 PHE A CG    1 
ATOM   3307  C CD1   . PHE A 1 1727 ? 218.717 203.841 176.795 1.00 32.95  ? 1727 PHE A CD1   1 
ATOM   3308  C CD2   . PHE A 1 1727 ? 216.770 202.723 176.009 1.00 32.95  ? 1727 PHE A CD2   1 
ATOM   3309  C CE1   . PHE A 1 1727 ? 218.277 205.017 176.229 1.00 32.95  ? 1727 PHE A CE1   1 
ATOM   3310  C CE2   . PHE A 1 1727 ? 216.327 203.893 175.443 1.00 32.95  ? 1727 PHE A CE2   1 
ATOM   3311  C CZ    . PHE A 1 1727 ? 217.079 205.043 175.552 1.00 32.95  ? 1727 PHE A CZ    1 
ATOM   3312  N N     . GLY A 1 1728 ? 220.453 199.064 178.001 1.00 37.50  ? 1728 GLY A N     1 
ATOM   3313  C CA    . GLY A 1 1728 ? 220.673 197.860 178.785 1.00 37.50  ? 1728 GLY A CA    1 
ATOM   3314  C C     . GLY A 1 1728 ? 221.973 197.883 179.566 1.00 37.50  ? 1728 GLY A C     1 
ATOM   3315  O O     . GLY A 1 1728 ? 222.010 197.492 180.736 1.00 37.50  ? 1728 GLY A O     1 
ATOM   3316  N N     . LYS A 1 1729 ? 223.054 198.341 178.938 1.00 43.35  ? 1729 LYS A N     1 
ATOM   3317  C CA    . LYS A 1 1729 ? 224.353 198.353 179.598 1.00 43.35  ? 1729 LYS A CA    1 
ATOM   3318  C C     . LYS A 1 1729 ? 224.498 199.586 180.481 1.00 43.35  ? 1729 LYS A C     1 
ATOM   3319  O O     . LYS A 1 1729 ? 225.467 200.341 180.352 1.00 43.35  ? 1729 LYS A O     1 
ATOM   3320  C CB    . LYS A 1 1729 ? 225.480 198.298 178.566 1.00 43.35  ? 1729 LYS A CB    1 
ATOM   3321  C CG    . LYS A 1 1729 ? 225.829 196.889 178.116 1.00 43.35  ? 1729 LYS A CG    1 
ATOM   3322  C CD    . LYS A 1 1729 ? 226.178 196.003 179.300 1.00 43.35  ? 1729 LYS A CD    1 
ATOM   3323  C CE    . LYS A 1 1729 ? 226.736 194.665 178.844 1.00 43.35  ? 1729 LYS A CE    1 
ATOM   3324  N NZ    . LYS A 1 1729 ? 226.348 193.561 179.766 1.00 43.35  ? 1729 LYS A NZ    1 
ATOM   3325  N N     . ALA A 1 1730 ? 223.540 199.793 181.380 1.00 50.95  ? 1730 ALA A N     1 
ATOM   3326  C CA    . ALA A 1 1730 ? 223.566 200.926 182.292 1.00 50.95  ? 1730 ALA A CA    1 
ATOM   3327  C C     . ALA A 1 1730 ? 222.642 200.630 183.463 1.00 50.95  ? 1730 ALA A C     1 
ATOM   3328  O O     . ALA A 1 1730 ? 221.819 199.712 183.412 1.00 50.95  ? 1730 ALA A O     1 
ATOM   3329  C CB    . ALA A 1 1730 ? 223.152 202.226 181.592 1.00 50.95  ? 1730 ALA A CB    1 
ATOM   3330  N N     . THR A 1 1731 ? 222.793 201.420 184.521 1.00 57.69  ? 1731 THR A N     1 
ATOM   3331  C CA    . THR A 1 1731 ? 221.969 201.307 185.713 1.00 57.69  ? 1731 THR A CA    1 
ATOM   3332  C C     . THR A 1 1731 ? 221.301 202.644 186.003 1.00 57.69  ? 1731 THR A C     1 
ATOM   3333  O O     . THR A 1 1731 ? 221.787 203.701 185.588 1.00 57.69  ? 1731 THR A O     1 
ATOM   3334  C CB    . THR A 1 1731 ? 222.795 200.859 186.927 1.00 57.69  ? 1731 THR A CB    1 
ATOM   3335  O OG1   . THR A 1 1731 ? 221.931 200.680 188.056 1.00 57.69  ? 1731 THR A OG1   1 
ATOM   3336  C CG2   . THR A 1 1731 ? 223.860 201.891 187.263 1.00 57.69  ? 1731 THR A CG2   1 
ATOM   3337  N N     . SER A 1 1732 ? 220.172 202.584 186.712 1.00 52.14  ? 1732 SER A N     1 
ATOM   3338  C CA    . SER A 1 1732 ? 219.374 203.764 187.048 1.00 52.14  ? 1732 SER A CA    1 
ATOM   3339  C C     . SER A 1 1732 ? 218.958 204.514 185.781 1.00 52.14  ? 1732 SER A C     1 
ATOM   3340  O O     . SER A 1 1732 ? 219.352 205.657 185.538 1.00 52.14  ? 1732 SER A O     1 
ATOM   3341  C CB    . SER A 1 1732 ? 220.127 204.681 188.020 1.00 52.14  ? 1732 SER A CB    1 
ATOM   3342  O OG    . SER A 1 1732 ? 221.188 205.357 187.369 1.00 52.14  ? 1732 SER A OG    1 
ATOM   3343  N N     . ILE A 1 1733 ? 218.148 203.834 184.966 1.00 40.96  ? 1733 ILE A N     1 
ATOM   3344  C CA    . ILE A 1 1733 ? 217.720 204.395 183.690 1.00 40.96  ? 1733 ILE A CA    1 
ATOM   3345  C C     . ILE A 1 1733 ? 216.873 205.634 183.928 1.00 40.96  ? 1733 ILE A C     1 
ATOM   3346  O O     . ILE A 1 1733 ? 215.979 205.646 184.784 1.00 40.96  ? 1733 ILE A O     1 
ATOM   3347  C CB    . ILE A 1 1733 ? 216.952 203.342 182.879 1.00 40.96  ? 1733 ILE A CB    1 
ATOM   3348  C CG1   . ILE A 1 1733 ? 217.754 202.044 182.797 1.00 40.96  ? 1733 ILE A CG1   1 
ATOM   3349  C CG2   . ILE A 1 1733 ? 216.636 203.864 181.488 1.00 40.96  ? 1733 ILE A CG2   1 
ATOM   3350  C CD1   . ILE A 1 1733 ? 217.002 200.907 182.151 1.00 40.96  ? 1733 ILE A CD1   1 
ATOM   3351  N N     . ASP A 1 1734 ? 217.154 206.687 183.171 1.00 36.88  ? 1734 ASP A N     1 
ATOM   3352  C CA    . ASP A 1 1734 ? 216.360 207.904 183.265 1.00 36.88  ? 1734 ASP A CA    1 
ATOM   3353  C C     . ASP A 1 1734 ? 214.996 207.677 182.624 1.00 36.88  ? 1734 ASP A C     1 
ATOM   3354  O O     . ASP A 1 1734 ? 214.925 207.261 181.462 1.00 36.88  ? 1734 ASP A O     1 
ATOM   3355  C CB    . ASP A 1 1734 ? 217.080 209.065 182.585 1.00 36.88  ? 1734 ASP A CB    1 
ATOM   3356  C CG    . ASP A 1 1734 ? 216.375 210.390 182.792 1.00 36.88  ? 1734 ASP A CG    1 
ATOM   3357  O OD1   . ASP A 1 1734 ? 216.432 210.926 183.919 1.00 36.88  ? 1734 ASP A OD1   1 
ATOM   3358  O OD2   . ASP A 1 1734 ? 215.766 210.896 181.827 1.00 36.88  ? 1734 ASP A OD2   1 
ATOM   3359  N N     . PRO A 1 1735 ? 213.898 207.920 183.342 1.00 34.98  ? 1735 PRO A N     1 
ATOM   3360  C CA    . PRO A 1 1735 ? 212.571 207.669 182.757 1.00 34.98  ? 1735 PRO A CA    1 
ATOM   3361  C C     . PRO A 1 1735 ? 212.287 208.482 181.506 1.00 34.98  ? 1735 PRO A C     1 
ATOM   3362  O O     . PRO A 1 1735 ? 211.590 207.991 180.609 1.00 34.98  ? 1735 PRO A O     1 
ATOM   3363  C CB    . PRO A 1 1735 ? 211.612 208.040 183.897 1.00 34.98  ? 1735 PRO A CB    1 
ATOM   3364  C CG    . PRO A 1 1735 ? 212.429 207.899 185.141 1.00 34.98  ? 1735 PRO A CG    1 
ATOM   3365  C CD    . PRO A 1 1735 ? 213.814 208.321 184.756 1.00 34.98  ? 1735 PRO A CD    1 
ATOM   3366  N N     . ASN A 1 1736 ? 212.805 209.708 181.414 1.00 34.82  ? 1736 ASN A N     1 
ATOM   3367  C CA    . ASN A 1 1736 ? 212.476 210.569 180.281 1.00 34.82  ? 1736 ASN A CA    1 
ATOM   3368  C C     . ASN A 1 1736 ? 213.006 209.993 178.973 1.00 34.82  ? 1736 ASN A C     1 
ATOM   3369  O O     . ASN A 1 1736 ? 212.267 209.880 177.987 1.00 34.82  ? 1736 ASN A O     1 
ATOM   3370  C CB    . ASN A 1 1736 ? 213.029 211.975 180.515 1.00 34.82  ? 1736 ASN A CB    1 
ATOM   3371  C CG    . ASN A 1 1736 ? 212.444 212.997 179.560 1.00 34.82  ? 1736 ASN A CG    1 
ATOM   3372  O OD1   . ASN A 1 1736 ? 211.521 212.699 178.802 1.00 34.82  ? 1736 ASN A OD1   1 
ATOM   3373  N ND2   . ASN A 1 1736 ? 212.980 214.211 179.592 1.00 34.82  ? 1736 ASN A ND2   1 
ATOM   3374  N N     . THR A 1 1737 ? 214.289 209.623 178.944 1.00 28.47  ? 1737 THR A N     1 
ATOM   3375  C CA    . THR A 1 1737 ? 214.868 209.093 177.713 1.00 28.47  ? 1737 THR A CA    1 
ATOM   3376  C C     . THR A 1 1737 ? 214.254 207.745 177.349 1.00 28.47  ? 1737 THR A C     1 
ATOM   3377  O O     . THR A 1 1737 ? 214.036 207.456 176.166 1.00 28.47  ? 1737 THR A O     1 
ATOM   3378  C CB    . THR A 1 1737 ? 216.391 208.995 177.836 1.00 28.47  ? 1737 THR A CB    1 
ATOM   3379  O OG1   . THR A 1 1737 ? 216.946 208.535 176.597 1.00 28.47  ? 1737 THR A OG1   1 
ATOM   3380  C CG2   . THR A 1 1737 ? 216.803 208.056 178.961 1.00 28.47  ? 1737 THR A CG2   1 
ATOM   3381  N N     . TYR A 1 1738 ? 213.950 206.916 178.350 1.00 22.42  ? 1738 TYR A N     1 
ATOM   3382  C CA    . TYR A 1 1738 ? 213.302 205.638 178.079 1.00 22.42  ? 1738 TYR A CA    1 
ATOM   3383  C C     . TYR A 1 1738 ? 211.921 205.841 177.470 1.00 22.42  ? 1738 TYR A C     1 
ATOM   3384  O O     . TYR A 1 1738 ? 211.548 205.151 176.515 1.00 22.42  ? 1738 TYR A O     1 
ATOM   3385  C CB    . TYR A 1 1738 ? 213.209 204.818 179.365 1.00 22.42  ? 1738 TYR A CB    1 
ATOM   3386  C CG    . TYR A 1 1738 ? 213.058 203.333 179.138 1.00 22.42  ? 1738 TYR A CG    1 
ATOM   3387  C CD1   . TYR A 1 1738 ? 214.116 202.574 178.660 1.00 22.42  ? 1738 TYR A CD1   1 
ATOM   3388  C CD2   . TYR A 1 1738 ? 211.860 202.689 179.407 1.00 22.42  ? 1738 TYR A CD2   1 
ATOM   3389  C CE1   . TYR A 1 1738 ? 213.984 201.216 178.452 1.00 22.42  ? 1738 TYR A CE1   1 
ATOM   3390  C CE2   . TYR A 1 1738 ? 211.719 201.332 179.202 1.00 22.42  ? 1738 TYR A CE2   1 
ATOM   3391  C CZ    . TYR A 1 1738 ? 212.783 200.601 178.725 1.00 22.42  ? 1738 TYR A CZ    1 
ATOM   3392  O OH    . TYR A 1 1738 ? 212.647 199.248 178.519 1.00 22.42  ? 1738 TYR A OH    1 
ATOM   3393  N N     . ILE A 1 1739 ? 211.151 206.792 178.002 1.00 21.57  ? 1739 ILE A N     1 
ATOM   3394  C CA    . ILE A 1 1739 ? 209.817 207.047 177.470 1.00 21.57  ? 1739 ILE A CA    1 
ATOM   3395  C C     . ILE A 1 1739 ? 209.903 207.624 176.062 1.00 21.57  ? 1739 ILE A C     1 
ATOM   3396  O O     . ILE A 1 1739 ? 209.093 207.286 175.189 1.00 21.57  ? 1739 ILE A O     1 
ATOM   3397  C CB    . ILE A 1 1739 ? 209.030 207.966 178.421 1.00 21.57  ? 1739 ILE A CB    1 
ATOM   3398  C CG1   . ILE A 1 1739 ? 208.623 207.197 179.679 1.00 21.57  ? 1739 ILE A CG1   1 
ATOM   3399  C CG2   . ILE A 1 1739 ? 207.798 208.529 177.734 1.00 21.57  ? 1739 ILE A CG2   1 
ATOM   3400  C CD1   . ILE A 1 1739 ? 207.813 205.953 179.398 1.00 21.57  ? 1739 ILE A CD1   1 
ATOM   3401  N N     . THR A 1 1740 ? 210.880 208.500 175.812 1.00 21.07  ? 1740 THR A N     1 
ATOM   3402  C CA    . THR A 1 1740 ? 211.056 209.024 174.460 1.00 21.07  ? 1740 THR A CA    1 
ATOM   3403  C C     . THR A 1 1740 ? 211.409 207.911 173.483 1.00 21.07  ? 1740 THR A C     1 
ATOM   3404  O O     . THR A 1 1740 ? 210.915 207.891 172.350 1.00 21.07  ? 1740 THR A O     1 
ATOM   3405  C CB    . THR A 1 1740 ? 212.131 210.111 174.435 1.00 21.07  ? 1740 THR A CB    1 
ATOM   3406  O OG1   . THR A 1 1740 ? 213.352 209.593 174.974 1.00 21.07  ? 1740 THR A OG1   1 
ATOM   3407  C CG2   . THR A 1 1740 ? 211.689 211.325 175.237 1.00 21.07  ? 1740 THR A CG2   1 
ATOM   3408  N N     . TRP A 1 1741 ? 212.266 206.977 173.902 1.00 19.87  ? 1741 TRP A N     1 
ATOM   3409  C CA    . TRP A 1 1741 ? 212.593 205.841 173.047 1.00 19.87  ? 1741 TRP A CA    1 
ATOM   3410  C C     . TRP A 1 1741 ? 211.369 204.974 172.785 1.00 19.87  ? 1741 TRP A C     1 
ATOM   3411  O O     . TRP A 1 1741 ? 211.167 204.495 171.664 1.00 19.87  ? 1741 TRP A O     1 
ATOM   3412  C CB    . TRP A 1 1741 ? 213.704 205.011 173.681 1.00 19.87  ? 1741 TRP A CB    1 
ATOM   3413  C CG    . TRP A 1 1741 ? 213.923 203.691 173.016 1.00 19.87  ? 1741 TRP A CG    1 
ATOM   3414  C CD1   . TRP A 1 1741 ? 214.574 203.467 171.841 1.00 19.87  ? 1741 TRP A CD1   1 
ATOM   3415  C CD2   . TRP A 1 1741 ? 213.496 202.408 173.489 1.00 19.87  ? 1741 TRP A CD2   1 
ATOM   3416  N NE1   . TRP A 1 1741 ? 214.578 202.125 171.550 1.00 19.87  ? 1741 TRP A NE1   1 
ATOM   3417  C CE2   . TRP A 1 1741 ? 213.922 201.453 172.547 1.00 19.87  ? 1741 TRP A CE2   1 
ATOM   3418  C CE3   . TRP A 1 1741 ? 212.794 201.975 174.617 1.00 19.87  ? 1741 TRP A CE3   1 
ATOM   3419  C CZ2   . TRP A 1 1741 ? 213.670 200.093 172.698 1.00 19.87  ? 1741 TRP A CZ2   1 
ATOM   3420  C CZ3   . TRP A 1 1741 ? 212.545 200.624 174.764 1.00 19.87  ? 1741 TRP A CZ3   1 
ATOM   3421  C CH2   . TRP A 1 1741 ? 212.983 199.700 173.811 1.00 19.87  ? 1741 TRP A CH2   1 
ATOM   3422  N N     . ILE A 1 1742 ? 210.546 204.752 173.812 1.00 16.63  ? 1742 ILE A N     1 
ATOM   3423  C CA    . ILE A 1 1742 ? 209.334 203.956 173.637 1.00 16.63  ? 1742 ILE A CA    1 
ATOM   3424  C C     . ILE A 1 1742 ? 208.396 204.628 172.643 1.00 16.63  ? 1742 ILE A C     1 
ATOM   3425  O O     . ILE A 1 1742 ? 207.820 203.971 171.767 1.00 16.63  ? 1742 ILE A O     1 
ATOM   3426  C CB    . ILE A 1 1742 ? 208.647 203.725 174.994 1.00 16.63  ? 1742 ILE A CB    1 
ATOM   3427  C CG1   . ILE A 1 1742 ? 209.507 202.829 175.880 1.00 16.63  ? 1742 ILE A CG1   1 
ATOM   3428  C CG2   . ILE A 1 1742 ? 207.276 203.104 174.800 1.00 16.63  ? 1742 ILE A CG2   1 
ATOM   3429  C CD1   . ILE A 1 1742 ? 208.979 202.693 177.279 1.00 16.63  ? 1742 ILE A CD1   1 
ATOM   3430  N N     . ASP A 1 1743 ? 208.229 205.946 172.761 1.00 17.67  ? 1743 ASP A N     1 
ATOM   3431  C CA    . ASP A 1 1743 ? 207.376 206.673 171.827 1.00 17.67  ? 1743 ASP A CA    1 
ATOM   3432  C C     . ASP A 1 1743 ? 207.956 206.683 170.419 1.00 17.67  ? 1743 ASP A C     1 
ATOM   3433  O O     . ASP A 1 1743 ? 207.202 206.712 169.440 1.00 17.67  ? 1743 ASP A O     1 
ATOM   3434  C CB    . ASP A 1 1743 ? 207.163 208.106 172.312 1.00 17.67  ? 1743 ASP A CB    1 
ATOM   3435  C CG    . ASP A 1 1743 ? 206.221 208.188 173.492 1.00 17.67  ? 1743 ASP A CG    1 
ATOM   3436  O OD1   . ASP A 1 1743 ? 205.299 207.351 173.578 1.00 17.67  ? 1743 ASP A OD1   1 
ATOM   3437  O OD2   . ASP A 1 1743 ? 206.401 209.092 174.334 1.00 17.67  ? 1743 ASP A OD2   1 
ATOM   3438  N N     . LYS A 1 1744 ? 209.285 206.667 170.298 1.00 19.28  ? 1744 LYS A N     1 
ATOM   3439  C CA    . LYS A 1 1744 ? 209.915 206.785 168.988 1.00 19.28  ? 1744 LYS A CA    1 
ATOM   3440  C C     . LYS A 1 1744 ? 209.598 205.589 168.098 1.00 19.28  ? 1744 LYS A C     1 
ATOM   3441  O O     . LYS A 1 1744 ? 209.307 205.753 166.908 1.00 19.28  ? 1744 LYS A O     1 
ATOM   3442  C CB    . LYS A 1 1744 ? 211.426 206.941 169.152 1.00 19.28  ? 1744 LYS A CB    1 
ATOM   3443  C CG    . LYS A 1 1744 ? 212.131 207.502 167.932 1.00 19.28  ? 1744 LYS A CG    1 
ATOM   3444  C CD    . LYS A 1 1744 ? 213.564 207.885 168.257 1.00 19.28  ? 1744 LYS A CD    1 
ATOM   3445  C CE    . LYS A 1 1744 ? 214.381 208.087 166.993 1.00 19.28  ? 1744 LYS A CE    1 
ATOM   3446  N NZ    . LYS A 1 1744 ? 215.835 208.210 167.286 1.00 19.28  ? 1744 LYS A NZ    1 
ATOM   3447  N N     . TYR A 1 1745 ? 209.644 204.382 168.652 1.00 16.94  ? 1745 TYR A N     1 
ATOM   3448  C CA    . TYR A 1 1745 ? 209.534 203.163 167.868 1.00 16.94  ? 1745 TYR A CA    1 
ATOM   3449  C C     . TYR A 1 1745 ? 208.207 202.462 168.123 1.00 16.94  ? 1745 TYR A C     1 
ATOM   3450  O O     . TYR A 1 1745 ? 207.544 202.680 169.141 1.00 16.94  ? 1745 TYR A O     1 
ATOM   3451  C CB    . TYR A 1 1745 ? 210.698 202.216 168.174 1.00 16.94  ? 1745 TYR A CB    1 
ATOM   3452  C CG    . TYR A 1 1745 ? 212.042 202.798 167.814 1.00 16.94  ? 1745 TYR A CG    1 
ATOM   3453  C CD1   . TYR A 1 1745 ? 212.421 202.945 166.489 1.00 16.94  ? 1745 TYR A CD1   1 
ATOM   3454  C CD2   . TYR A 1 1745 ? 212.925 203.213 168.797 1.00 16.94  ? 1745 TYR A CD2   1 
ATOM   3455  C CE1   . TYR A 1 1745 ? 213.646 203.482 166.153 1.00 16.94  ? 1745 TYR A CE1   1 
ATOM   3456  C CE2   . TYR A 1 1745 ? 214.153 203.752 168.471 1.00 16.94  ? 1745 TYR A CE2   1 
ATOM   3457  C CZ    . TYR A 1 1745 ? 214.508 203.883 167.148 1.00 16.94  ? 1745 TYR A CZ    1 
ATOM   3458  O OH    . TYR A 1 1745 ? 215.730 204.419 166.820 1.00 16.94  ? 1745 TYR A OH    1 
ATOM   3459  N N     . GLN A 1 1746 ? 207.830 201.610 167.174 1.00 16.32  ? 1746 GLN A N     1 
ATOM   3460  C CA    . GLN A 1 1746 ? 206.569 200.891 167.247 1.00 16.32  ? 1746 GLN A CA    1 
ATOM   3461  C C     . GLN A 1 1746 ? 206.607 199.848 168.360 1.00 16.32  ? 1746 GLN A C     1 
ATOM   3462  O O     . GLN A 1 1746 ? 207.672 199.423 168.815 1.00 16.32  ? 1746 GLN A O     1 
ATOM   3463  C CB    . GLN A 1 1746 ? 206.259 200.219 165.909 1.00 16.32  ? 1746 GLN A CB    1 
ATOM   3464  C CG    . GLN A 1 1746 ? 205.966 201.189 164.777 1.00 16.32  ? 1746 GLN A CG    1 
ATOM   3465  C CD    . GLN A 1 1746 ? 207.224 201.806 164.200 1.00 16.32  ? 1746 GLN A CD    1 
ATOM   3466  O OE1   . GLN A 1 1746 ? 208.326 201.302 164.409 1.00 16.32  ? 1746 GLN A OE1   1 
ATOM   3467  N NE2   . GLN A 1 1746 ? 207.066 202.906 163.475 1.00 16.32  ? 1746 GLN A NE2   1 
ATOM   3468  N N     . ALA A 1 1747 ? 205.415 199.434 168.797 1.00 15.85  ? 1747 ALA A N     1 
ATOM   3469  C CA    . ALA A 1 1747 ? 205.315 198.468 169.888 1.00 15.85  ? 1747 ALA A CA    1 
ATOM   3470  C C     . ALA A 1 1747 ? 206.023 197.168 169.533 1.00 15.85  ? 1747 ALA A C     1 
ATOM   3471  O O     . ALA A 1 1747 ? 206.784 196.617 170.341 1.00 15.85  ? 1747 ALA A O     1 
ATOM   3472  C CB    . ALA A 1 1747 ? 203.847 198.207 170.221 1.00 15.85  ? 1747 ALA A CB    1 
ATOM   3473  N N     . GLN A 1 1748 ? 205.792 196.670 168.317 1.00 14.36  ? 1748 GLN A N     1 
ATOM   3474  C CA    . GLN A 1 1748 ? 206.490 195.480 167.845 1.00 14.36  ? 1748 GLN A CA    1 
ATOM   3475  C C     . GLN A 1 1748 ? 207.998 195.678 167.902 1.00 14.36  ? 1748 GLN A C     1 
ATOM   3476  O O     . GLN A 1 1748 ? 208.735 194.818 168.398 1.00 14.36  ? 1748 GLN A O     1 
ATOM   3477  C CB    . GLN A 1 1748 ? 206.046 195.161 166.417 1.00 14.36  ? 1748 GLN A CB    1 
ATOM   3478  C CG    . GLN A 1 1748 ? 206.768 193.994 165.777 1.00 14.36  ? 1748 GLN A CG    1 
ATOM   3479  C CD    . GLN A 1 1748 ? 206.359 193.789 164.333 1.00 14.36  ? 1748 GLN A CD    1 
ATOM   3480  O OE1   . GLN A 1 1748 ? 205.547 194.539 163.795 1.00 14.36  ? 1748 GLN A OE1   1 
ATOM   3481  N NE2   . GLN A 1 1748 ? 206.920 192.769 163.698 1.00 14.36  ? 1748 GLN A NE2   1 
ATOM   3482  N N     . LEU A 1 1749 ? 208.468 196.826 167.413 1.00 12.80  ? 1749 LEU A N     1 
ATOM   3483  C CA    . LEU A 1 1749 ? 209.903 197.079 167.358 1.00 12.80  ? 1749 LEU A CA    1 
ATOM   3484  C C     . LEU A 1 1749 ? 210.484 197.222 168.754 1.00 12.80  ? 1749 LEU A C     1 
ATOM   3485  O O     . LEU A 1 1749 ? 211.586 196.738 169.025 1.00 12.80  ? 1749 LEU A O     1 
ATOM   3486  C CB    . LEU A 1 1749 ? 210.192 198.337 166.545 1.00 12.80  ? 1749 LEU A CB    1 
ATOM   3487  C CG    . LEU A 1 1749 ? 210.238 198.185 165.027 1.00 12.80  ? 1749 LEU A CG    1 
ATOM   3488  C CD1   . LEU A 1 1749 ? 211.367 197.273 164.611 1.00 12.80  ? 1749 LEU A CD1   1 
ATOM   3489  C CD2   . LEU A 1 1749 ? 208.915 197.688 164.506 1.00 12.80  ? 1749 LEU A CD2   1 
ATOM   3490  N N     . VAL A 1 1750 ? 209.757 197.891 169.649 1.00 15.00  ? 1750 VAL A N     1 
ATOM   3491  C CA    . VAL A 1 1750 ? 210.238 198.080 171.014 1.00 15.00  ? 1750 VAL A CA    1 
ATOM   3492  C C     . VAL A 1 1750 ? 210.372 196.737 171.722 1.00 15.00  ? 1750 VAL A C     1 
ATOM   3493  O O     . VAL A 1 1750 ? 211.394 196.446 172.359 1.00 15.00  ? 1750 VAL A O     1 
ATOM   3494  C CB    . VAL A 1 1750 ? 209.302 199.032 171.778 1.00 15.00  ? 1750 VAL A CB    1 
ATOM   3495  C CG1   . VAL A 1 1750 ? 209.619 199.004 173.244 1.00 15.00  ? 1750 VAL A CG1   1 
ATOM   3496  C CG2   . VAL A 1 1750 ? 209.438 200.444 171.240 1.00 15.00  ? 1750 VAL A CG2   1 
ATOM   3497  N N     . VAL A 1 1751 ? 209.343 195.893 171.612 1.00 12.20  ? 1751 VAL A N     1 
ATOM   3498  C CA    . VAL A 1 1751 ? 209.395 194.584 172.258 1.00 12.20  ? 1751 VAL A CA    1 
ATOM   3499  C C     . VAL A 1 1751 ? 210.514 193.739 171.667 1.00 12.20  ? 1751 VAL A C     1 
ATOM   3500  O O     . VAL A 1 1751 ? 211.273 193.088 172.399 1.00 12.20  ? 1751 VAL A O     1 
ATOM   3501  C CB    . VAL A 1 1751 ? 208.032 193.878 172.150 1.00 12.20  ? 1751 VAL A CB    1 
ATOM   3502  C CG1   . VAL A 1 1751 ? 208.125 192.478 172.713 1.00 12.20  ? 1751 VAL A CG1   1 
ATOM   3503  C CG2   . VAL A 1 1751 ? 206.970 194.673 172.885 1.00 12.20  ? 1751 VAL A CG2   1 
ATOM   3504  N N     . LEU A 1 1752 ? 210.643 193.739 170.338 1.00 11.91  ? 1752 LEU A N     1 
ATOM   3505  C CA    . LEU A 1 1752 ? 211.688 192.947 169.698 1.00 11.91  ? 1752 LEU A CA    1 
ATOM   3506  C C     . LEU A 1 1752 ? 213.074 193.425 170.107 1.00 11.91  ? 1752 LEU A C     1 
ATOM   3507  O O     . LEU A 1 1752 ? 213.978 192.613 170.330 1.00 11.91  ? 1752 LEU A O     1 
ATOM   3508  C CB    . LEU A 1 1752 ? 211.525 193.006 168.182 1.00 11.91  ? 1752 LEU A CB    1 
ATOM   3509  C CG    . LEU A 1 1752 ? 212.251 191.933 167.376 1.00 11.91  ? 1752 LEU A CG    1 
ATOM   3510  C CD1   . LEU A 1 1752 ? 211.931 190.555 167.919 1.00 11.91  ? 1752 LEU A CD1   1 
ATOM   3511  C CD2   . LEU A 1 1752 ? 211.858 192.041 165.920 1.00 11.91  ? 1752 LEU A CD2   1 
ATOM   3512  N N     . SER A 1 1753 ? 213.263 194.742 170.203 1.00 12.73  ? 1753 SER A N     1 
ATOM   3513  C CA    . SER A 1 1753 ? 214.552 195.282 170.615 1.00 12.73  ? 1753 SER A CA    1 
ATOM   3514  C C     . SER A 1 1753 ? 214.871 194.907 172.053 1.00 12.73  ? 1753 SER A C     1 
ATOM   3515  O O     . SER A 1 1753 ? 216.020 194.584 172.377 1.00 12.73  ? 1753 SER A O     1 
ATOM   3516  C CB    . SER A 1 1753 ? 214.556 196.797 170.440 1.00 12.73  ? 1753 SER A CB    1 
ATOM   3517  O OG    . SER A 1 1753 ? 214.282 197.135 169.094 1.00 12.73  ? 1753 SER A OG    1 
ATOM   3518  N N     . ALA A 1 1754 ? 213.870 194.952 172.936 1.00 12.30  ? 1754 ALA A N     1 
ATOM   3519  C CA    . ALA A 1 1754 ? 214.095 194.523 174.312 1.00 12.30  ? 1754 ALA A CA    1 
ATOM   3520  C C     . ALA A 1 1754 ? 214.502 193.056 174.368 1.00 12.30  ? 1754 ALA A C     1 
ATOM   3521  O O     . ALA A 1 1754 ? 215.441 192.689 175.088 1.00 12.30  ? 1754 ALA A O     1 
ATOM   3522  C CB    . ALA A 1 1754 ? 212.842 194.767 175.152 1.00 12.30  ? 1754 ALA A CB    1 
ATOM   3523  N N     . GLN A 1 1755 ? 213.816 192.204 173.599 1.00 10.54  ? 1755 GLN A N     1 
ATOM   3524  C CA    . GLN A 1 1755 ? 214.167 190.786 173.575 1.00 10.54  ? 1755 GLN A CA    1 
ATOM   3525  C C     . GLN A 1 1755 ? 215.580 190.576 173.051 1.00 10.54  ? 1755 GLN A C     1 
ATOM   3526  O O     . GLN A 1 1755 ? 216.345 189.780 173.609 1.00 10.54  ? 1755 GLN A O     1 
ATOM   3527  C CB    . GLN A 1 1755 ? 213.168 190.007 172.721 1.00 10.54  ? 1755 GLN A CB    1 
ATOM   3528  C CG    . GLN A 1 1755 ? 211.726 190.154 173.152 1.00 10.54  ? 1755 GLN A CG    1 
ATOM   3529  C CD    . GLN A 1 1755 ? 210.797 189.216 172.413 1.00 10.54  ? 1755 GLN A CD    1 
ATOM   3530  O OE1   . GLN A 1 1755 ? 210.169 189.596 171.427 1.00 10.54  ? 1755 GLN A OE1   1 
ATOM   3531  N NE2   . GLN A 1 1755 ? 210.701 187.982 172.891 1.00 10.54  ? 1755 GLN A NE2   1 
ATOM   3532  N N     . ILE A 1 1756 ? 215.944 191.280 171.978 1.00 11.30  ? 1756 ILE A N     1 
ATOM   3533  C CA    . ILE A 1 1756 ? 217.274 191.125 171.394 1.00 11.30  ? 1756 ILE A CA    1 
ATOM   3534  C C     . ILE A 1 1756 ? 218.341 191.561 172.388 1.00 11.30  ? 1756 ILE A C     1 
ATOM   3535  O O     . ILE A 1 1756 ? 219.356 190.878 172.578 1.00 11.30  ? 1756 ILE A O     1 
ATOM   3536  C CB    . ILE A 1 1756 ? 217.376 191.914 170.076 1.00 11.30  ? 1756 ILE A CB    1 
ATOM   3537  C CG1   . ILE A 1 1756 ? 216.610 191.200 168.966 1.00 11.30  ? 1756 ILE A CG1   1 
ATOM   3538  C CG2   . ILE A 1 1756 ? 218.826 192.097 169.673 1.00 11.30  ? 1756 ILE A CG2   1 
ATOM   3539  C CD1   . ILE A 1 1756 ? 216.537 191.989 167.686 1.00 11.30  ? 1756 ILE A CD1   1 
ATOM   3540  N N     . ALA A 1 1757 ? 218.128 192.707 173.038 1.00 12.50  ? 1757 ALA A N     1 
ATOM   3541  C CA    . ALA A 1 1757 ? 219.101 193.204 174.002 1.00 12.50  ? 1757 ALA A CA    1 
ATOM   3542  C C     . ALA A 1 1757 ? 219.272 192.228 175.156 1.00 12.50  ? 1757 ALA A C     1 
ATOM   3543  O O     . ALA A 1 1757 ? 220.399 191.932 175.571 1.00 12.50  ? 1757 ALA A O     1 
ATOM   3544  C CB    . ALA A 1 1757 ? 218.676 194.579 174.514 1.00 12.50  ? 1757 ALA A CB    1 
ATOM   3545  N N     . TRP A 1 1758 ? 218.161 191.702 175.681 1.00 11.15  ? 1758 TRP A N     1 
ATOM   3546  C CA    . TRP A 1 1758 ? 218.260 190.749 176.782 1.00 11.15  ? 1758 TRP A CA    1 
ATOM   3547  C C     . TRP A 1 1758 ? 218.982 189.480 176.351 1.00 11.15  ? 1758 TRP A C     1 
ATOM   3548  O O     . TRP A 1 1758 ? 219.812 188.947 177.098 1.00 11.15  ? 1758 TRP A O     1 
ATOM   3549  C CB    . TRP A 1 1758 ? 216.874 190.412 177.322 1.00 11.15  ? 1758 TRP A CB    1 
ATOM   3550  C CG    . TRP A 1 1758 ? 216.878 189.242 178.257 1.00 11.15  ? 1758 TRP A CG    1 
ATOM   3551  C CD1   . TRP A 1 1758 ? 217.280 189.238 179.559 1.00 11.15  ? 1758 TRP A CD1   1 
ATOM   3552  C CD2   . TRP A 1 1758 ? 216.466 187.903 177.961 1.00 11.15  ? 1758 TRP A CD2   1 
ATOM   3553  N NE1   . TRP A 1 1758 ? 217.142 187.982 180.095 1.00 11.15  ? 1758 TRP A NE1   1 
ATOM   3554  C CE2   . TRP A 1 1758 ? 216.644 187.143 179.133 1.00 11.15  ? 1758 TRP A CE2   1 
ATOM   3555  C CE3   . TRP A 1 1758 ? 215.962 187.272 176.820 1.00 11.15  ? 1758 TRP A CE3   1 
ATOM   3556  C CZ2   . TRP A 1 1758 ? 216.337 185.787 179.197 1.00 11.15  ? 1758 TRP A CZ2   1 
ATOM   3557  C CZ3   . TRP A 1 1758 ? 215.657 185.926 176.886 1.00 11.15  ? 1758 TRP A CZ3   1 
ATOM   3558  C CH2   . TRP A 1 1758 ? 215.846 185.198 178.066 1.00 11.15  ? 1758 TRP A CH2   1 
ATOM   3559  N N     . SER A 1 1759 ? 218.677 188.975 175.152 1.00 12.25  ? 1759 SER A N     1 
ATOM   3560  C CA    . SER A 1 1759 ? 219.313 187.746 174.691 1.00 12.25  ? 1759 SER A CA    1 
ATOM   3561  C C     . SER A 1 1759 ? 220.814 187.931 174.515 1.00 12.25  ? 1759 SER A C     1 
ATOM   3562  O O     . SER A 1 1759 ? 221.604 187.080 174.940 1.00 12.25  ? 1759 SER A O     1 
ATOM   3563  C CB    . SER A 1 1759 ? 218.673 187.278 173.386 1.00 12.25  ? 1759 SER A CB    1 
ATOM   3564  O OG    . SER A 1 1759 ? 218.963 188.173 172.329 1.00 12.25  ? 1759 SER A OG    1 
ATOM   3565  N N     . GLU A 1 1760 ? 221.230 189.041 173.897 1.00 17.56  ? 1760 GLU A N     1 
ATOM   3566  C CA    . GLU A 1 1760 ? 222.661 189.286 173.738 1.00 17.56  ? 1760 GLU A CA    1 
ATOM   3567  C C     . GLU A 1 1760 ? 223.344 189.484 175.085 1.00 17.56  ? 1760 GLU A C     1 
ATOM   3568  O O     . GLU A 1 1760 ? 224.468 189.009 175.289 1.00 17.56  ? 1760 GLU A O     1 
ATOM   3569  C CB    . GLU A 1 1760 ? 222.909 190.490 172.827 1.00 17.56  ? 1760 GLU A CB    1 
ATOM   3570  C CG    . GLU A 1 1760 ? 222.153 190.452 171.510 1.00 17.56  ? 1760 GLU A CG    1 
ATOM   3571  C CD    . GLU A 1 1760 ? 222.873 189.658 170.438 1.00 17.56  ? 1760 GLU A CD    1 
ATOM   3572  O OE1   . GLU A 1 1760 ? 223.871 188.981 170.762 1.00 17.56  ? 1760 GLU A OE1   1 
ATOM   3573  O OE2   . GLU A 1 1760 ? 222.438 189.707 169.269 1.00 17.56  ? 1760 GLU A OE2   1 
ATOM   3574  N N     . ASN A 1 1761 ? 222.687 190.180 176.019 1.00 19.89  ? 1761 ASN A N     1 
ATOM   3575  C CA    . ASN A 1 1761 ? 223.281 190.376 177.337 1.00 19.89  ? 1761 ASN A CA    1 
ATOM   3576  C C     . ASN A 1 1761 ? 223.476 189.049 178.057 1.00 19.89  ? 1761 ASN A C     1 
ATOM   3577  O O     . ASN A 1 1761 ? 224.535 188.804 178.647 1.00 19.89  ? 1761 ASN A O     1 
ATOM   3578  C CB    . ASN A 1 1761 ? 222.408 191.313 178.170 1.00 19.89  ? 1761 ASN A CB    1 
ATOM   3579  C CG    . ASN A 1 1761 ? 222.657 192.773 177.857 1.00 19.89  ? 1761 ASN A CG    1 
ATOM   3580  O OD1   . ASN A 1 1761 ? 223.394 193.104 176.928 1.00 19.89  ? 1761 ASN A OD1   1 
ATOM   3581  N ND2   . ASN A 1 1761 ? 222.044 193.657 178.634 1.00 19.89  ? 1761 ASN A ND2   1 
ATOM   3582  N N     . VAL A 1 1762 ? 222.470 188.174 178.008 1.00 20.05  ? 1762 VAL A N     1 
ATOM   3583  C CA    . VAL A 1 1762 ? 222.583 186.883 178.680 1.00 20.05  ? 1762 VAL A CA    1 
ATOM   3584  C C     . VAL A 1 1762 ? 223.641 186.018 178.007 1.00 20.05  ? 1762 VAL A C     1 
ATOM   3585  O O     . VAL A 1 1762 ? 224.397 185.308 178.679 1.00 20.05  ? 1762 VAL A O     1 
ATOM   3586  C CB    . VAL A 1 1762 ? 221.214 186.181 178.727 1.00 20.05  ? 1762 VAL A CB    1 
ATOM   3587  C CG1   . VAL A 1 1762 ? 221.364 184.761 179.237 1.00 20.05  ? 1762 VAL A CG1   1 
ATOM   3588  C CG2   . VAL A 1 1762 ? 220.260 186.955 179.612 1.00 20.05  ? 1762 VAL A CG2   1 
ATOM   3589  N N     . GLU A 1 1763 ? 223.715 186.060 176.673 1.00 23.52  ? 1763 GLU A N     1 
ATOM   3590  C CA    . GLU A 1 1763 ? 224.740 185.292 175.975 1.00 23.52  ? 1763 GLU A CA    1 
ATOM   3591  C C     . GLU A 1 1763 ? 226.138 185.769 176.348 1.00 23.52  ? 1763 GLU A C     1 
ATOM   3592  O O     . GLU A 1 1763 ? 227.038 184.954 176.579 1.00 23.52  ? 1763 GLU A O     1 
ATOM   3593  C CB    . GLU A 1 1763 ? 224.528 185.380 174.465 1.00 23.52  ? 1763 GLU A CB    1 
ATOM   3594  C CG    . GLU A 1 1763 ? 223.560 184.347 173.920 1.00 23.52  ? 1763 GLU A CG    1 
ATOM   3595  C CD    . GLU A 1 1763 ? 224.262 183.099 173.426 1.00 23.52  ? 1763 GLU A CD    1 
ATOM   3596  O OE1   . GLU A 1 1763 ? 225.509 183.104 173.361 1.00 23.52  ? 1763 GLU A OE1   1 
ATOM   3597  O OE2   . GLU A 1 1763 ? 223.569 182.111 173.106 1.00 23.52  ? 1763 GLU A OE2   1 
ATOM   3598  N N     . THR A 1 1764 ? 226.338 187.088 176.416 1.00 25.39  ? 1764 THR A N     1 
ATOM   3599  C CA    . THR A 1 1764 ? 227.635 187.618 176.824 1.00 25.39  ? 1764 THR A CA    1 
ATOM   3600  C C     . THR A 1 1764 ? 227.964 187.223 178.258 1.00 25.39  ? 1764 THR A C     1 
ATOM   3601  O O     . THR A 1 1764 ? 229.108 186.864 178.565 1.00 25.39  ? 1764 THR A O     1 
ATOM   3602  C CB    . THR A 1 1764 ? 227.654 189.138 176.671 1.00 25.39  ? 1764 THR A CB    1 
ATOM   3603  O OG1   . THR A 1 1764 ? 227.203 189.493 175.358 1.00 25.39  ? 1764 THR A OG1   1 
ATOM   3604  C CG2   . THR A 1 1764 ? 229.061 189.675 176.879 1.00 25.39  ? 1764 THR A CG2   1 
ATOM   3605  N N     . ALA A 1 1765 ? 226.972 187.283 179.150 1.00 30.03  ? 1765 ALA A N     1 
ATOM   3606  C CA    . ALA A 1 1765 ? 227.202 186.900 180.538 1.00 30.03  ? 1765 ALA A CA    1 
ATOM   3607  C C     . ALA A 1 1765 ? 227.591 185.431 180.649 1.00 30.03  ? 1765 ALA A C     1 
ATOM   3608  O O     . ALA A 1 1765 ? 228.500 185.078 181.409 1.00 30.03  ? 1765 ALA A O     1 
ATOM   3609  C CB    . ALA A 1 1765 ? 225.957 187.190 181.374 1.00 30.03  ? 1765 ALA A CB    1 
ATOM   3610  N N     . LEU A 1 1766 ? 226.909 184.561 179.903 1.00 30.97  ? 1766 LEU A N     1 
ATOM   3611  C CA    . LEU A 1 1766 ? 227.246 183.141 179.925 1.00 30.97  ? 1766 LEU A CA    1 
ATOM   3612  C C     . LEU A 1 1766 ? 228.631 182.892 179.340 1.00 30.97  ? 1766 LEU A C     1 
ATOM   3613  O O     . LEU A 1 1766 ? 229.390 182.067 179.862 1.00 30.97  ? 1766 LEU A O     1 
ATOM   3614  C CB    . LEU A 1 1766 ? 226.189 182.337 179.170 1.00 30.97  ? 1766 LEU A CB    1 
ATOM   3615  C CG    . LEU A 1 1766 ? 224.830 182.212 179.858 1.00 30.97  ? 1766 LEU A CG    1 
ATOM   3616  C CD1   . LEU A 1 1766 ? 223.905 181.315 179.058 1.00 30.97  ? 1766 LEU A CD1   1 
ATOM   3617  C CD2   . LEU A 1 1766 ? 224.993 181.693 181.274 1.00 30.97  ? 1766 LEU A CD2   1 
ATOM   3618  N N     . SER A 1 1767 ? 228.975 183.589 178.254 1.00 33.04  ? 1767 SER A N     1 
ATOM   3619  C CA    . SER A 1 1767 ? 230.294 183.416 177.655 1.00 33.04  ? 1767 SER A CA    1 
ATOM   3620  C C     . SER A 1 1767 ? 231.395 183.846 178.615 1.00 33.04  ? 1767 SER A C     1 
ATOM   3621  O O     . SER A 1 1767 ? 232.429 183.176 178.725 1.00 33.04  ? 1767 SER A O     1 
ATOM   3622  C CB    . SER A 1 1767 ? 230.385 184.203 176.348 1.00 33.04  ? 1767 SER A CB    1 
ATOM   3623  O OG    . SER A 1 1767 ? 230.325 185.597 176.590 1.00 33.04  ? 1767 SER A OG    1 
ATOM   3624  N N     . SER A 1 1768 ? 231.192 184.959 179.321 1.00 39.62  ? 1768 SER A N     1 
ATOM   3625  C CA    . SER A 1 1768 ? 232.176 185.409 180.299 1.00 39.62  ? 1768 SER A CA    1 
ATOM   3626  C C     . SER A 1 1768 ? 232.206 184.538 181.548 1.00 39.62  ? 1768 SER A C     1 
ATOM   3627  O O     . SER A 1 1768 ? 233.126 184.684 182.360 1.00 39.62  ? 1768 SER A O     1 
ATOM   3628  C CB    . SER A 1 1768 ? 231.905 186.863 180.688 1.00 39.62  ? 1768 SER A CB    1 
ATOM   3629  O OG    . SER A 1 1768 ? 231.753 187.678 179.540 1.00 39.62  ? 1768 SER A OG    1 
ATOM   3630  N N     . MET A 1 1769 ? 231.231 183.645 181.722 1.00 50.19  ? 1769 MET A N     1 
ATOM   3631  C CA    . MET A 1 1769 ? 231.174 182.744 182.866 1.00 50.19  ? 1769 MET A CA    1 
ATOM   3632  C C     . MET A 1 1769 ? 231.619 181.330 182.510 1.00 50.19  ? 1769 MET A C     1 
ATOM   3633  O O     . MET A 1 1769 ? 231.104 180.358 183.072 1.00 50.19  ? 1769 MET A O     1 
ATOM   3634  C CB    . MET A 1 1769 ? 229.761 182.718 183.448 1.00 50.19  ? 1769 MET A CB    1 
ATOM   3635  C CG    . MET A 1 1769 ? 229.567 183.604 184.662 1.00 50.19  ? 1769 MET A CG    1 
ATOM   3636  S SD    . MET A 1 1769 ? 227.823 183.860 185.034 1.00 50.19  ? 1769 MET A SD    1 
ATOM   3637  C CE    . MET A 1 1769 ? 227.343 182.213 185.544 1.00 50.19  ? 1769 MET A CE    1 
ATOM   3638  N N     . GLY A 1 1770 ? 232.567 181.198 181.580 1.00 60.41  ? 1770 GLY A N     1 
ATOM   3639  C CA    . GLY A 1 1770 ? 232.986 179.874 181.147 1.00 60.41  ? 1770 GLY A CA    1 
ATOM   3640  C C     . GLY A 1 1770 ? 233.613 179.059 182.262 1.00 60.41  ? 1770 GLY A C     1 
ATOM   3641  O O     . GLY A 1 1770 ? 233.393 177.849 182.357 1.00 60.41  ? 1770 GLY A O     1 
ATOM   3642  N N     . GLY A 1 1771 ? 234.405 179.708 183.117 1.00 69.68  ? 1771 GLY A N     1 
ATOM   3643  C CA    . GLY A 1 1771 ? 235.040 178.990 184.210 1.00 69.68  ? 1771 GLY A CA    1 
ATOM   3644  C C     . GLY A 1 1771 ? 234.043 178.433 185.207 1.00 69.68  ? 1771 GLY A C     1 
ATOM   3645  O O     . GLY A 1 1771 ? 234.199 177.312 185.697 1.00 69.68  ? 1771 GLY A O     1 
ATOM   3646  N N     . GLY A 1 1772 ? 233.013 179.197 185.515 1.00 70.32  ? 1772 GLY A N     1 
ATOM   3647  C CA    . GLY A 1 1772 ? 232.018 178.786 186.480 1.00 70.32  ? 1772 GLY A CA    1 
ATOM   3648  C C     . GLY A 1 1772 ? 231.292 180.005 187.036 1.00 70.32  ? 1772 GLY A C     1 
ATOM   3649  O O     . GLY A 1 1772 ? 231.113 181.003 186.336 1.00 70.32  ? 1772 GLY A O     1 
ATOM   3650  N N     . GLY A 1 1773 ? 230.884 179.898 188.301 1.00 75.03  ? 1773 GLY A N     1 
ATOM   3651  C CA    . GLY A 1 1773 ? 230.182 180.983 188.960 1.00 75.03  ? 1773 GLY A CA    1 
ATOM   3652  C C     . GLY A 1 1773 ? 231.044 182.162 189.351 1.00 75.03  ? 1773 GLY A C     1 
ATOM   3653  O O     . GLY A 1 1773 ? 230.507 183.186 189.784 1.00 75.03  ? 1773 GLY A O     1 
ATOM   3654  N N     . ASP A 1 1774 ? 232.362 182.039 189.216 1.00 77.24  ? 1774 ASP A N     1 
ATOM   3655  C CA    . ASP A 1 1774 ? 233.260 183.138 189.545 1.00 77.24  ? 1774 ASP A CA    1 
ATOM   3656  C C     . ASP A 1 1774 ? 233.023 184.315 188.607 1.00 77.24  ? 1774 ASP A C     1 
ATOM   3657  O O     . ASP A 1 1774 ? 232.908 184.137 187.390 1.00 77.24  ? 1774 ASP A O     1 
ATOM   3658  C CB    . ASP A 1 1774 ? 234.713 182.674 189.458 1.00 77.24  ? 1774 ASP A CB    1 
ATOM   3659  C CG    . ASP A 1 1774 ? 235.064 182.114 188.093 1.00 77.24  ? 1774 ASP A CG    1 
ATOM   3660  O OD1   . ASP A 1 1774 ? 234.401 181.151 187.656 1.00 77.24  ? 1774 ASP A OD1   1 
ATOM   3661  O OD2   . ASP A 1 1774 ? 236.001 182.639 187.456 1.00 77.24  ? 1774 ASP A OD2   1 
ATOM   3662  N N     . ALA A 1 1775 ? 232.956 185.516 189.179 1.00 72.81  ? 1775 ALA A N     1 
ATOM   3663  C CA    . ALA A 1 1775 ? 232.738 186.752 188.429 1.00 72.81  ? 1775 ALA A CA    1 
ATOM   3664  C C     . ALA A 1 1775 ? 231.504 186.633 187.535 1.00 72.81  ? 1775 ALA A C     1 
ATOM   3665  O O     . ALA A 1 1775 ? 231.581 186.684 186.307 1.00 72.81  ? 1775 ALA A O     1 
ATOM   3666  C CB    . ALA A 1 1775 ? 233.979 187.125 187.615 1.00 72.81  ? 1775 ALA A CB    1 
ATOM   3667  N N     . ALA A 1 1776 ? 230.353 186.462 188.183 1.00 53.66  ? 1776 ALA A N     1 
ATOM   3668  C CA    . ALA A 1 1776 ? 229.107 186.212 187.472 1.00 53.66  ? 1776 ALA A CA    1 
ATOM   3669  C C     . ALA A 1 1776 ? 228.417 187.528 187.141 1.00 53.66  ? 1776 ALA A C     1 
ATOM   3670  O O     . ALA A 1 1776 ? 227.988 188.236 188.062 1.00 53.66  ? 1776 ALA A O     1 
ATOM   3671  C CB    . ALA A 1 1776 ? 228.183 185.339 188.305 1.00 53.66  ? 1776 ALA A CB    1 
ATOM   3672  N N     . PRO A 1 1777 ? 228.288 187.893 185.867 1.00 38.42  ? 1777 PRO A N     1 
ATOM   3673  C CA    . PRO A 1 1777 ? 227.496 189.071 185.495 1.00 38.42  ? 1777 PRO A CA    1 
ATOM   3674  C C     . PRO A 1 1777 ? 226.020 188.786 185.262 1.00 38.42  ? 1777 PRO A C     1 
ATOM   3675  O O     . PRO A 1 1777 ? 225.289 189.704 184.873 1.00 38.42  ? 1777 PRO A O     1 
ATOM   3676  C CB    . PRO A 1 1777 ? 228.171 189.519 184.193 1.00 38.42  ? 1777 PRO A CB    1 
ATOM   3677  C CG    . PRO A 1 1777 ? 228.639 188.251 183.581 1.00 38.42  ? 1777 PRO A CG    1 
ATOM   3678  C CD    . PRO A 1 1777 ? 228.999 187.322 184.711 1.00 38.42  ? 1777 PRO A CD    1 
ATOM   3679  N N     . LEU A 1 1778 ? 225.572 187.547 185.476 1.00 31.32  ? 1778 LEU A N     1 
ATOM   3680  C CA    . LEU A 1 1778 ? 224.148 187.246 185.368 1.00 31.32  ? 1778 LEU A CA    1 
ATOM   3681  C C     . LEU A 1 1778 ? 223.350 188.017 186.410 1.00 31.32  ? 1778 LEU A C     1 
ATOM   3682  O O     . LEU A 1 1778 ? 222.217 188.443 186.151 1.00 31.32  ? 1778 LEU A O     1 
ATOM   3683  C CB    . LEU A 1 1778 ? 223.920 185.743 185.519 1.00 31.32  ? 1778 LEU A CB    1 
ATOM   3684  C CG    . LEU A 1 1778 ? 223.745 184.948 184.227 1.00 31.32  ? 1778 LEU A CG    1 
ATOM   3685  C CD1   . LEU A 1 1778 ? 223.486 183.487 184.540 1.00 31.32  ? 1778 LEU A CD1   1 
ATOM   3686  C CD2   . LEU A 1 1778 ? 222.618 185.528 183.394 1.00 31.32  ? 1778 LEU A CD2   1 
ATOM   3687  N N     . HIS A 1 1779 ? 223.928 188.206 187.597 1.00 30.29  ? 1779 HIS A N     1 
ATOM   3688  C CA    . HIS A 1 1779 ? 223.288 189.042 188.604 1.00 30.29  ? 1779 HIS A CA    1 
ATOM   3689  C C     . HIS A 1 1779 ? 223.146 190.475 188.109 1.00 30.29  ? 1779 HIS A C     1 
ATOM   3690  O O     . HIS A 1 1779 ? 222.149 191.143 188.400 1.00 30.29  ? 1779 HIS A O     1 
ATOM   3691  C CB    . HIS A 1 1779 ? 224.085 188.999 189.906 1.00 30.29  ? 1779 HIS A CB    1 
ATOM   3692  C CG    . HIS A 1 1779 ? 223.977 187.697 190.636 1.00 30.29  ? 1779 HIS A CG    1 
ATOM   3693  N ND1   . HIS A 1 1779 ? 224.797 186.623 190.367 1.00 30.29  ? 1779 HIS A ND1   1 
ATOM   3694  C CD2   . HIS A 1 1779 ? 223.143 187.296 191.625 1.00 30.29  ? 1779 HIS A CD2   1 
ATOM   3695  C CE1   . HIS A 1 1779 ? 224.475 185.616 191.160 1.00 30.29  ? 1779 HIS A CE1   1 
ATOM   3696  N NE2   . HIS A 1 1779 ? 223.474 185.998 191.932 1.00 30.29  ? 1779 HIS A NE2   1 
ATOM   3697  N N     . SER A 1 1780 ? 224.133 190.963 187.354 1.00 27.32  ? 1780 SER A N     1 
ATOM   3698  C CA    . SER A 1 1780 ? 224.024 192.295 186.769 1.00 27.32  ? 1780 SER A CA    1 
ATOM   3699  C C     . SER A 1 1780 ? 222.882 192.361 185.762 1.00 27.32  ? 1780 SER A C     1 
ATOM   3700  O O     . SER A 1 1780 ? 222.153 193.358 185.705 1.00 27.32  ? 1780 SER A O     1 
ATOM   3701  C CB    . SER A 1 1780 ? 225.344 192.695 186.111 1.00 27.32  ? 1780 SER A CB    1 
ATOM   3702  O OG    . SER A 1 1780 ? 225.593 191.915 184.955 1.00 27.32  ? 1780 SER A OG    1 
ATOM   3703  N N     . VAL A 1 1781 ? 222.714 191.310 184.956 1.00 24.85  ? 1781 VAL A N     1 
ATOM   3704  C CA    . VAL A 1 1781 ? 221.607 191.274 184.003 1.00 24.85  ? 1781 VAL A CA    1 
ATOM   3705  C C     . VAL A 1 1781 ? 220.273 191.287 184.736 1.00 24.85  ? 1781 VAL A C     1 
ATOM   3706  O O     . VAL A 1 1781 ? 219.338 192.004 184.350 1.00 24.85  ? 1781 VAL A O     1 
ATOM   3707  C CB    . VAL A 1 1781 ? 221.734 190.044 183.085 1.00 24.85  ? 1781 VAL A CB    1 
ATOM   3708  C CG1   . VAL A 1 1781 ? 220.530 189.943 182.164 1.00 24.85  ? 1781 VAL A CG1   1 
ATOM   3709  C CG2   . VAL A 1 1781 ? 223.021 190.113 182.283 1.00 24.85  ? 1781 VAL A CG2   1 
ATOM   3710  N N     . LEU A 1 1782 ? 220.161 190.497 185.806 1.00 21.46  ? 1782 LEU A N     1 
ATOM   3711  C CA    . LEU A 1 1782 ? 218.922 190.479 186.576 1.00 21.46  ? 1782 LEU A CA    1 
ATOM   3712  C C     . LEU A 1 1782 ? 218.651 191.834 187.219 1.00 21.46  ? 1782 LEU A C     1 
ATOM   3713  O O     . LEU A 1 1782 ? 217.506 192.295 187.248 1.00 21.46  ? 1782 LEU A O     1 
ATOM   3714  C CB    . LEU A 1 1782 ? 218.974 189.382 187.637 1.00 21.46  ? 1782 LEU A CB    1 
ATOM   3715  C CG    . LEU A 1 1782 ? 217.670 189.179 188.408 1.00 21.46  ? 1782 LEU A CG    1 
ATOM   3716  C CD1   . LEU A 1 1782 ? 216.549 188.811 187.454 1.00 21.46  ? 1782 LEU A CD1   1 
ATOM   3717  C CD2   . LEU A 1 1782 ? 217.837 188.115 189.478 1.00 21.46  ? 1782 LEU A CD2   1 
ATOM   3718  N N     . SER A 1 1783 ? 219.692 192.486 187.742 1.00 22.92  ? 1783 SER A N     1 
ATOM   3719  C CA    . SER A 1 1783 ? 219.521 193.812 188.327 1.00 22.92  ? 1783 SER A CA    1 
ATOM   3720  C C     . SER A 1 1783 ? 219.077 194.825 187.280 1.00 22.92  ? 1783 SER A C     1 
ATOM   3721  O O     . SER A 1 1783 ? 218.231 195.683 187.554 1.00 22.92  ? 1783 SER A O     1 
ATOM   3722  C CB    . SER A 1 1783 ? 220.820 194.264 188.992 1.00 22.92  ? 1783 SER A CB    1 
ATOM   3723  O OG    . SER A 1 1783 ? 220.861 195.674 189.122 1.00 22.92  ? 1783 SER A OG    1 
ATOM   3724  N N     . ASN A 1 1784 ? 219.646 194.745 186.076 1.00 22.32  ? 1784 ASN A N     1 
ATOM   3725  C CA    . ASN A 1 1784 ? 219.218 195.622 184.991 1.00 22.32  ? 1784 ASN A CA    1 
ATOM   3726  C C     . ASN A 1 1784 ? 217.751 195.398 184.651 1.00 22.32  ? 1784 ASN A C     1 
ATOM   3727  O O     . ASN A 1 1784 ? 216.997 196.358 184.444 1.00 22.32  ? 1784 ASN A O     1 
ATOM   3728  C CB    . ASN A 1 1784 ? 220.092 195.383 183.762 1.00 22.32  ? 1784 ASN A CB    1 
ATOM   3729  C CG    . ASN A 1 1784 ? 219.788 196.341 182.632 1.00 22.32  ? 1784 ASN A CG    1 
ATOM   3730  O OD1   . ASN A 1 1784 ? 219.082 197.332 182.810 1.00 22.32  ? 1784 ASN A OD1   1 
ATOM   3731  N ND2   . ASN A 1 1784 ? 220.309 196.037 181.452 1.00 22.32  ? 1784 ASN A ND2   1 
ATOM   3732  N N     . VAL A 1 1785 ? 217.330 194.134 184.588 1.00 17.99  ? 1785 VAL A N     1 
ATOM   3733  C CA    . VAL A 1 1785 ? 215.934 193.835 184.281 1.00 17.99  ? 1785 VAL A CA    1 
ATOM   3734  C C     . VAL A 1 1785 ? 215.023 194.365 185.382 1.00 17.99  ? 1785 VAL A C     1 
ATOM   3735  O O     . VAL A 1 1785 ? 213.948 194.911 185.108 1.00 17.99  ? 1785 VAL A O     1 
ATOM   3736  C CB    . VAL A 1 1785 ? 215.747 192.323 184.060 1.00 17.99  ? 1785 VAL A CB    1 
ATOM   3737  C CG1   . VAL A 1 1785 ? 214.275 191.975 184.000 1.00 17.99  ? 1785 VAL A CG1   1 
ATOM   3738  C CG2   . VAL A 1 1785 ? 216.444 191.890 182.783 1.00 17.99  ? 1785 VAL A CG2   1 
ATOM   3739  N N     . GLU A 1 1786 ? 215.439 194.217 186.642 1.00 18.79  ? 1786 GLU A N     1 
ATOM   3740  C CA    . GLU A 1 1786 ? 214.648 194.745 187.751 1.00 18.79  ? 1786 GLU A CA    1 
ATOM   3741  C C     . GLU A 1 1786 ? 214.538 196.263 187.682 1.00 18.79  ? 1786 GLU A C     1 
ATOM   3742  O O     . GLU A 1 1786 ? 213.472 196.827 187.951 1.00 18.79  ? 1786 GLU A O     1 
ATOM   3743  C CB    . GLU A 1 1786 ? 215.255 194.318 189.087 1.00 18.79  ? 1786 GLU A CB    1 
ATOM   3744  C CG    . GLU A 1 1786 ? 215.288 192.817 189.322 1.00 18.79  ? 1786 GLU A CG    1 
ATOM   3745  C CD    . GLU A 1 1786 ? 214.001 192.287 189.917 1.00 18.79  ? 1786 GLU A CD    1 
ATOM   3746  O OE1   . GLU A 1 1786 ? 213.027 193.061 190.019 1.00 18.79  ? 1786 GLU A OE1   1 
ATOM   3747  O OE2   . GLU A 1 1786 ? 213.967 191.096 190.290 1.00 18.79  ? 1786 GLU A OE2   1 
ATOM   3748  N N     . VAL A 1 1787 ? 215.633 196.943 187.337 1.00 20.18  ? 1787 VAL A N     1 
ATOM   3749  C CA    . VAL A 1 1787 ? 215.602 198.400 187.223 1.00 20.18  ? 1787 VAL A CA    1 
ATOM   3750  C C     . VAL A 1 1787 ? 214.658 198.829 186.107 1.00 20.18  ? 1787 VAL A C     1 
ATOM   3751  O O     . VAL A 1 1787 ? 213.859 199.763 186.269 1.00 20.18  ? 1787 VAL A O     1 
ATOM   3752  C CB    . VAL A 1 1787 ? 217.026 198.946 187.005 1.00 20.18  ? 1787 VAL A CB    1 
ATOM   3753  C CG1   . VAL A 1 1787 ? 216.977 200.362 186.458 1.00 20.18  ? 1787 VAL A CG1   1 
ATOM   3754  C CG2   . VAL A 1 1787 ? 217.812 198.900 188.303 1.00 20.18  ? 1787 VAL A CG2   1 
ATOM   3755  N N     . THR A 1 1788 ? 214.733 198.154 184.958 1.00 17.07  ? 1788 THR A N     1 
ATOM   3756  C CA    . THR A 1 1788 ? 213.838 198.481 183.852 1.00 17.07  ? 1788 THR A CA    1 
ATOM   3757  C C     . THR A 1 1788 ? 212.383 198.234 184.232 1.00 17.07  ? 1788 THR A C     1 
ATOM   3758  O O     . THR A 1 1788 ? 211.500 199.032 183.896 1.00 17.07  ? 1788 THR A O     1 
ATOM   3759  C CB    . THR A 1 1788 ? 214.215 197.669 182.614 1.00 17.07  ? 1788 THR A CB    1 
ATOM   3760  O OG1   . THR A 1 1788 ? 215.549 198.001 182.213 1.00 17.07  ? 1788 THR A OG1   1 
ATOM   3761  C CG2   . THR A 1 1788 ? 213.265 197.972 181.470 1.00 17.07  ? 1788 THR A CG2   1 
ATOM   3762  N N     . LEU A 1 1789 ? 212.115 197.133 184.938 1.00 14.90  ? 1789 LEU A N     1 
ATOM   3763  C CA    . LEU A 1 1789 ? 210.753 196.843 185.373 1.00 14.90  ? 1789 LEU A CA    1 
ATOM   3764  C C     . LEU A 1 1789 ? 210.255 197.888 186.362 1.00 14.90  ? 1789 LEU A C     1 
ATOM   3765  O O     . LEU A 1 1789 ? 209.083 198.273 186.326 1.00 14.90  ? 1789 LEU A O     1 
ATOM   3766  C CB    . LEU A 1 1789 ? 210.684 195.447 185.987 1.00 14.90  ? 1789 LEU A CB    1 
ATOM   3767  C CG    . LEU A 1 1789 ? 210.187 194.344 185.055 1.00 14.90  ? 1789 LEU A CG    1 
ATOM   3768  C CD1   . LEU A 1 1789 ? 210.316 192.986 185.719 1.00 14.90  ? 1789 LEU A CD1   1 
ATOM   3769  C CD2   . LEU A 1 1789 ? 208.752 194.611 184.648 1.00 14.90  ? 1789 LEU A CD2   1 
ATOM   3770  N N     . ASN A 1 1790 ? 211.126 198.347 187.263 1.00 15.98  ? 1790 ASN A N     1 
ATOM   3771  C CA    . ASN A 1 1790 ? 210.739 199.406 188.189 1.00 15.98  ? 1790 ASN A CA    1 
ATOM   3772  C C     . ASN A 1 1790 ? 210.404 200.690 187.442 1.00 15.98  ? 1790 ASN A C     1 
ATOM   3773  O O     . ASN A 1 1790 ? 209.417 201.365 187.761 1.00 15.98  ? 1790 ASN A O     1 
ATOM   3774  C CB    . ASN A 1 1790 ? 211.856 199.654 189.202 1.00 15.98  ? 1790 ASN A CB    1 
ATOM   3775  C CG    . ASN A 1 1790 ? 211.850 198.648 190.333 1.00 15.98  ? 1790 ASN A CG    1 
ATOM   3776  O OD1   . ASN A 1 1790 ? 211.027 197.733 190.362 1.00 15.98  ? 1790 ASN A OD1   1 
ATOM   3777  N ND2   . ASN A 1 1790 ? 212.772 198.811 191.275 1.00 15.98  ? 1790 ASN A ND2   1 
ATOM   3778  N N     . VAL A 1 1791 ? 211.213 201.038 186.440 1.00 16.64  ? 1791 VAL A N     1 
ATOM   3779  C CA    . VAL A 1 1791 ? 210.944 202.236 185.647 1.00 16.64  ? 1791 VAL A CA    1 
ATOM   3780  C C     . VAL A 1 1791 ? 209.602 202.109 184.934 1.00 16.64  ? 1791 VAL A C     1 
ATOM   3781  O O     . VAL A 1 1791 ? 208.791 203.043 184.924 1.00 16.64  ? 1791 VAL A O     1 
ATOM   3782  C CB    . VAL A 1 1791 ? 212.091 202.491 184.653 1.00 16.64  ? 1791 VAL A CB    1 
ATOM   3783  C CG1   . VAL A 1 1791 ? 211.666 203.496 183.595 1.00 16.64  ? 1791 VAL A CG1   1 
ATOM   3784  C CG2   . VAL A 1 1791 ? 213.328 202.976 185.388 1.00 16.64  ? 1791 VAL A CG2   1 
ATOM   3785  N N     . LEU A 1 1792 ? 209.346 200.945 184.334 1.00 14.53  ? 1792 LEU A N     1 
ATOM   3786  C CA    . LEU A 1 1792 ? 208.087 200.737 183.623 1.00 14.53  ? 1792 LEU A CA    1 
ATOM   3787  C C     . LEU A 1 1792 ? 206.894 200.786 184.572 1.00 14.53  ? 1792 LEU A C     1 
ATOM   3788  O O     . LEU A 1 1792 ? 205.853 201.365 184.238 1.00 14.53  ? 1792 LEU A O     1 
ATOM   3789  C CB    . LEU A 1 1792 ? 208.123 199.405 182.878 1.00 14.53  ? 1792 LEU A CB    1 
ATOM   3790  C CG    . LEU A 1 1792 ? 209.115 199.290 181.722 1.00 14.53  ? 1792 LEU A CG    1 
ATOM   3791  C CD1   . LEU A 1 1792 ? 209.287 197.840 181.313 1.00 14.53  ? 1792 LEU A CD1   1 
ATOM   3792  C CD2   . LEU A 1 1792 ? 208.660 200.124 180.545 1.00 14.53  ? 1792 LEU A CD2   1 
ATOM   3793  N N     . ALA A 1 1793 ? 207.023 200.177 185.753 1.00 14.75  ? 1793 ALA A N     1 
ATOM   3794  C CA    . ALA A 1 1793 ? 205.932 200.183 186.721 1.00 14.75  ? 1793 ALA A CA    1 
ATOM   3795  C C     . ALA A 1 1793 ? 205.655 201.589 187.232 1.00 14.75  ? 1793 ALA A C     1 
ATOM   3796  O O     . ALA A 1 1793 ? 204.498 201.950 187.476 1.00 14.75  ? 1793 ALA A O     1 
ATOM   3797  C CB    . ALA A 1 1793 ? 206.254 199.243 187.881 1.00 14.75  ? 1793 ALA A CB    1 
ATOM   3798  N N     . ASP A 1 1794 ? 206.703 202.393 187.418 1.00 15.66  ? 1794 ASP A N     1 
ATOM   3799  C CA    . ASP A 1 1794 ? 206.492 203.793 187.766 1.00 15.66  ? 1794 ASP A CA    1 
ATOM   3800  C C     . ASP A 1 1794 ? 205.807 204.543 186.630 1.00 15.66  ? 1794 ASP A C     1 
ATOM   3801  O O     . ASP A 1 1794 ? 204.940 205.390 186.872 1.00 15.66  ? 1794 ASP A O     1 
ATOM   3802  C CB    . ASP A 1 1794 ? 207.824 204.453 188.121 1.00 15.66  ? 1794 ASP A CB    1 
ATOM   3803  C CG    . ASP A 1 1794 ? 208.273 204.135 189.533 1.00 15.66  ? 1794 ASP A CG    1 
ATOM   3804  O OD1   . ASP A 1 1794 ? 207.536 203.421 190.245 1.00 15.66  ? 1794 ASP A OD1   1 
ATOM   3805  O OD2   . ASP A 1 1794 ? 209.361 204.600 189.931 1.00 15.66  ? 1794 ASP A OD2   1 
ATOM   3806  N N     . SER A 1 1795 ? 206.185 204.245 185.385 1.00 16.64  ? 1795 SER A N     1 
ATOM   3807  C CA    . SER A 1 1795 ? 205.610 204.951 184.245 1.00 16.64  ? 1795 SER A CA    1 
ATOM   3808  C C     . SER A 1 1795 ? 204.131 204.637 184.056 1.00 16.64  ? 1795 SER A C     1 
ATOM   3809  O O     . SER A 1 1795 ? 203.345 205.544 183.764 1.00 16.64  ? 1795 SER A O     1 
ATOM   3810  C CB    . SER A 1 1795 ? 206.386 204.613 182.974 1.00 16.64  ? 1795 SER A CB    1 
ATOM   3811  O OG    . SER A 1 1795 ? 207.722 205.072 183.058 1.00 16.64  ? 1795 SER A OG    1 
ATOM   3812  N N     . VAL A 1 1796 ? 203.729 203.371 184.210 1.00 16.01  ? 1796 VAL A N     1 
ATOM   3813  C CA    . VAL A 1 1796 ? 202.335 203.006 183.953 1.00 16.01  ? 1796 VAL A CA    1 
ATOM   3814  C C     . VAL A 1 1796 ? 201.374 203.555 184.993 1.00 16.01  ? 1796 VAL A C     1 
ATOM   3815  O O     . VAL A 1 1796 ? 200.164 203.594 184.740 1.00 16.01  ? 1796 VAL A O     1 
ATOM   3816  C CB    . VAL A 1 1796 ? 202.125 201.482 183.881 1.00 16.01  ? 1796 VAL A CB    1 
ATOM   3817  C CG1   . VAL A 1 1796 ? 202.696 200.930 182.591 1.00 16.01  ? 1796 VAL A CG1   1 
ATOM   3818  C CG2   . VAL A 1 1796 ? 202.738 200.798 185.083 1.00 16.01  ? 1796 VAL A CG2   1 
ATOM   3819  N N     . LEU A 1 1797 ? 201.871 203.979 186.155 1.00 18.64  ? 1797 LEU A N     1 
ATOM   3820  C CA    . LEU A 1 1797 ? 201.001 204.540 187.179 1.00 18.64  ? 1797 LEU A CA    1 
ATOM   3821  C C     . LEU A 1 1797 ? 200.511 205.939 186.832 1.00 18.64  ? 1797 LEU A C     1 
ATOM   3822  O O     . LEU A 1 1797 ? 199.492 206.376 187.376 1.00 18.64  ? 1797 LEU A O     1 
ATOM   3823  C CB    . LEU A 1 1797 ? 201.725 204.569 188.525 1.00 18.64  ? 1797 LEU A CB    1 
ATOM   3824  C CG    . LEU A 1 1797 ? 201.569 203.317 189.388 1.00 18.64  ? 1797 LEU A CG    1 
ATOM   3825  C CD1   . LEU A 1 1797 ? 202.251 203.499 190.733 1.00 18.64  ? 1797 LEU A CD1   1 
ATOM   3826  C CD2   . LEU A 1 1797 ? 200.100 202.984 189.569 1.00 18.64  ? 1797 LEU A CD2   1 
ATOM   3827  N N     . MET A 1 1798 ? 201.204 206.643 185.943 1.00 21.30  ? 1798 MET A N     1 
ATOM   3828  C CA    . MET A 1 1798 ? 200.839 208.001 185.575 1.00 21.30  ? 1798 MET A CA    1 
ATOM   3829  C C     . MET A 1 1798 ? 199.842 207.972 184.417 1.00 21.30  ? 1798 MET A C     1 
ATOM   3830  O O     . MET A 1 1798 ? 199.318 206.920 184.044 1.00 21.30  ? 1798 MET A O     1 
ATOM   3831  C CB    . MET A 1 1798 ? 202.089 208.806 185.230 1.00 21.30  ? 1798 MET A CB    1 
ATOM   3832  C CG    . MET A 1 1798 ? 203.111 208.871 186.351 1.00 21.30  ? 1798 MET A CG    1 
ATOM   3833  S SD    . MET A 1 1798 ? 204.807 208.889 185.743 1.00 21.30  ? 1798 MET A SD    1 
ATOM   3834  C CE    . MET A 1 1798 ? 204.636 209.931 184.297 1.00 21.30  ? 1798 MET A CE    1 
ATOM   3835  N N     . GLU A 1 1799 ? 199.570 209.137 183.836 1.00 25.52  ? 1799 GLU A N     1 
ATOM   3836  C CA    . GLU A 1 1799 ? 198.640 209.254 182.721 1.00 25.52  ? 1799 GLU A CA    1 
ATOM   3837  C C     . GLU A 1 1799 ? 199.422 209.204 181.415 1.00 25.52  ? 1799 GLU A C     1 
ATOM   3838  O O     . GLU A 1 1799 ? 200.286 210.053 181.170 1.00 25.52  ? 1799 GLU A O     1 
ATOM   3839  C CB    . GLU A 1 1799 ? 197.836 210.549 182.824 1.00 25.52  ? 1799 GLU A CB    1 
ATOM   3840  C CG    . GLU A 1 1799 ? 196.784 210.714 181.743 1.00 25.52  ? 1799 GLU A CG    1 
ATOM   3841  C CD    . GLU A 1 1799 ? 195.976 211.986 181.910 1.00 25.52  ? 1799 GLU A CD    1 
ATOM   3842  O OE1   . GLU A 1 1799 ? 196.254 212.748 182.859 1.00 25.52  ? 1799 GLU A OE1   1 
ATOM   3843  O OE2   . GLU A 1 1799 ? 195.060 212.221 181.094 1.00 25.52  ? 1799 GLU A OE2   1 
ATOM   3844  N N     . GLN A 1 1800 ? 199.116 208.218 180.579 1.00 19.22  ? 1800 GLN A N     1 
ATOM   3845  C CA    . GLN A 1 1800 ? 199.846 207.987 179.345 1.00 19.22  ? 1800 GLN A CA    1 
ATOM   3846  C C     . GLN A 1 1800 ? 198.878 207.905 178.175 1.00 19.22  ? 1800 GLN A C     1 
ATOM   3847  O O     . GLN A 1 1800 ? 197.703 207.571 178.359 1.00 19.22  ? 1800 GLN A O     1 
ATOM   3848  C CB    . GLN A 1 1800 ? 200.661 206.687 179.421 1.00 19.22  ? 1800 GLN A CB    1 
ATOM   3849  C CG    . GLN A 1 1800 ? 201.633 206.612 180.588 1.00 19.22  ? 1800 GLN A CG    1 
ATOM   3850  C CD    . GLN A 1 1800 ? 202.703 207.682 180.536 1.00 19.22  ? 1800 GLN A CD    1 
ATOM   3851  O OE1   . GLN A 1 1800 ? 203.166 208.063 179.463 1.00 19.22  ? 1800 GLN A OE1   1 
ATOM   3852  N NE2   . GLN A 1 1800 ? 203.107 208.169 181.702 1.00 19.22  ? 1800 GLN A NE2   1 
ATOM   3853  N N     . PRO A 1 1801 ? 199.339 208.213 176.965 1.00 17.08  ? 1801 PRO A N     1 
ATOM   3854  C CA    . PRO A 1 1801 ? 198.500 207.995 175.793 1.00 17.08  ? 1801 PRO A CA    1 
ATOM   3855  C C     . PRO A 1 1801 ? 198.210 206.516 175.619 1.00 17.08  ? 1801 PRO A C     1 
ATOM   3856  O O     . PRO A 1 1801 ? 199.009 205.658 176.037 1.00 17.08  ? 1801 PRO A O     1 
ATOM   3857  C CB    . PRO A 1 1801 ? 199.351 208.543 174.640 1.00 17.08  ? 1801 PRO A CB    1 
ATOM   3858  C CG    . PRO A 1 1801 ? 200.321 209.470 175.283 1.00 17.08  ? 1801 PRO A CG    1 
ATOM   3859  C CD    . PRO A 1 1801 ? 200.607 208.878 176.623 1.00 17.08  ? 1801 PRO A CD    1 
ATOM   3860  N N     . PRO A 1 1802 ? 197.065 206.173 175.023 1.00 15.49  ? 1802 PRO A N     1 
ATOM   3861  C CA    . PRO A 1 1802 ? 196.715 204.745 174.892 1.00 15.49  ? 1802 PRO A CA    1 
ATOM   3862  C C     . PRO A 1 1802 ? 197.752 203.926 174.141 1.00 15.49  ? 1802 PRO A C     1 
ATOM   3863  O O     . PRO A 1 1802 ? 198.016 202.777 174.518 1.00 15.49  ? 1802 PRO A O     1 
ATOM   3864  C CB    . PRO A 1 1802 ? 195.370 204.783 174.150 1.00 15.49  ? 1802 PRO A CB    1 
ATOM   3865  C CG    . PRO A 1 1802 ? 195.315 206.132 173.506 1.00 15.49  ? 1802 PRO A CG    1 
ATOM   3866  C CD    . PRO A 1 1802 ? 196.047 207.051 174.427 1.00 15.49  ? 1802 PRO A CD    1 
ATOM   3867  N N     . LEU A 1 1803 ? 198.355 204.486 173.091 1.00 14.96  ? 1803 LEU A N     1 
ATOM   3868  C CA    . LEU A 1 1803 ? 199.380 203.755 172.352 1.00 14.96  ? 1803 LEU A CA    1 
ATOM   3869  C C     . LEU A 1 1803 ? 200.607 203.506 173.221 1.00 14.96  ? 1803 LEU A C     1 
ATOM   3870  O O     . LEU A 1 1803 ? 201.132 202.385 173.277 1.00 14.96  ? 1803 LEU A O     1 
ATOM   3871  C CB    . LEU A 1 1803 ? 199.761 204.525 171.089 1.00 14.96  ? 1803 LEU A CB    1 
ATOM   3872  C CG    . LEU A 1 1803 ? 200.611 203.761 170.076 1.00 14.96  ? 1803 LEU A CG    1 
ATOM   3873  C CD1   . LEU A 1 1803 ? 199.922 202.467 169.695 1.00 14.96  ? 1803 LEU A CD1   1 
ATOM   3874  C CD2   . LEU A 1 1803 ? 200.882 204.612 168.846 1.00 14.96  ? 1803 LEU A CD2   1 
ATOM   3875  N N     . ARG A 1 1804 ? 201.079 204.546 173.910 1.00 15.84  ? 1804 ARG A N     1 
ATOM   3876  C CA    . ARG A 1 1804 ? 202.207 204.364 174.814 1.00 15.84  ? 1804 ARG A CA    1 
ATOM   3877  C C     . ARG A 1 1804 ? 201.835 203.464 175.981 1.00 15.84  ? 1804 ARG A C     1 
ATOM   3878  O O     . ARG A 1 1804 ? 202.689 202.745 176.500 1.00 15.84  ? 1804 ARG A O     1 
ATOM   3879  C CB    . ARG A 1 1804 ? 202.715 205.713 175.320 1.00 15.84  ? 1804 ARG A CB    1 
ATOM   3880  C CG    . ARG A 1 1804 ? 204.053 205.623 176.031 1.00 15.84  ? 1804 ARG A CG    1 
ATOM   3881  C CD    . ARG A 1 1804 ? 204.373 206.895 176.787 1.00 15.84  ? 1804 ARG A CD    1 
ATOM   3882  N NE    . ARG A 1 1804 ? 204.149 208.086 175.978 1.00 15.84  ? 1804 ARG A NE    1 
ATOM   3883  C CZ    . ARG A 1 1804 ? 204.223 209.327 176.439 1.00 15.84  ? 1804 ARG A CZ    1 
ATOM   3884  N NH1   . ARG A 1 1804 ? 204.514 209.577 177.704 1.00 15.84  ? 1804 ARG A NH1   1 
ATOM   3885  N NH2   . ARG A 1 1804 ? 204.000 210.341 175.609 1.00 15.84  ? 1804 ARG A NH2   1 
ATOM   3886  N N     . ARG A 1 1805 ? 200.569 203.479 176.399 1.00 15.84  ? 1805 ARG A N     1 
ATOM   3887  C CA    . ARG A 1 1805 ? 200.121 202.545 177.428 1.00 15.84  ? 1805 ARG A CA    1 
ATOM   3888  C C     . ARG A 1 1805 ? 200.237 201.102 176.955 1.00 15.84  ? 1805 ARG A C     1 
ATOM   3889  O O     . ARG A 1 1805 ? 200.706 200.232 177.701 1.00 15.84  ? 1805 ARG A O     1 
ATOM   3890  C CB    . ARG A 1 1805 ? 198.682 202.863 177.825 1.00 15.84  ? 1805 ARG A CB    1 
ATOM   3891  C CG    . ARG A 1 1805 ? 198.045 201.841 178.743 1.00 15.84  ? 1805 ARG A CG    1 
ATOM   3892  C CD    . ARG A 1 1805 ? 198.738 201.792 180.092 1.00 15.84  ? 1805 ARG A CD    1 
ATOM   3893  N NE    . ARG A 1 1805 ? 198.932 203.120 180.662 1.00 15.84  ? 1805 ARG A NE    1 
ATOM   3894  C CZ    . ARG A 1 1805 ? 197.957 203.892 181.118 1.00 15.84  ? 1805 ARG A CZ    1 
ATOM   3895  N NH1   . ARG A 1 1805 ? 196.690 203.521 181.045 1.00 15.84  ? 1805 ARG A NH1   1 
ATOM   3896  N NH2   . ARG A 1 1805 ? 198.259 205.072 181.651 1.00 15.84  ? 1805 ARG A NH2   1 
ATOM   3897  N N     . ARG A 1 1806 ? 199.809 200.827 175.721 1.00 14.80  ? 1806 ARG A N     1 
ATOM   3898  C CA    . ARG A 1 1806 ? 199.933 199.478 175.182 1.00 14.80  ? 1806 ARG A CA    1 
ATOM   3899  C C     . ARG A 1 1806 ? 201.394 199.066 175.074 1.00 14.80  ? 1806 ARG A C     1 
ATOM   3900  O O     . ARG A 1 1806 ? 201.759 197.937 175.429 1.00 14.80  ? 1806 ARG A O     1 
ATOM   3901  C CB    . ARG A 1 1806 ? 199.248 199.392 173.819 1.00 14.80  ? 1806 ARG A CB    1 
ATOM   3902  C CG    . ARG A 1 1806 ? 197.751 199.639 173.863 1.00 14.80  ? 1806 ARG A CG    1 
ATOM   3903  C CD    . ARG A 1 1806 ? 196.982 198.374 174.201 1.00 14.80  ? 1806 ARG A CD    1 
ATOM   3904  N NE    . ARG A 1 1806 ? 197.028 197.397 173.120 1.00 14.80  ? 1806 ARG A NE    1 
ATOM   3905  C CZ    . ARG A 1 1806 ? 196.317 197.481 172.004 1.00 14.80  ? 1806 ARG A CZ    1 
ATOM   3906  N NH1   . ARG A 1 1806 ? 195.497 198.495 171.781 1.00 14.80  ? 1806 ARG A NH1   1 
ATOM   3907  N NH2   . ARG A 1 1806 ? 196.431 196.524 171.089 1.00 14.80  ? 1806 ARG A NH2   1 
ATOM   3908  N N     . LYS A 1 1807 ? 202.247 199.972 174.594 1.00 10.46  ? 1807 LYS A N     1 
ATOM   3909  C CA    . LYS A 1 1807 ? 203.671 199.661 174.513 1.00 10.46  ? 1807 LYS A CA    1 
ATOM   3910  C C     . LYS A 1 1807 ? 204.252 199.393 175.896 1.00 10.46  ? 1807 LYS A C     1 
ATOM   3911  O O     . LYS A 1 1807 ? 205.052 198.467 176.076 1.00 10.46  ? 1807 LYS A O     1 
ATOM   3912  C CB    . LYS A 1 1807 ? 204.420 200.798 173.820 1.00 10.46  ? 1807 LYS A CB    1 
ATOM   3913  C CG    . LYS A 1 1807 ? 203.947 201.065 172.404 1.00 10.46  ? 1807 LYS A CG    1 
ATOM   3914  C CD    . LYS A 1 1807 ? 204.996 201.799 171.591 1.00 10.46  ? 1807 LYS A CD    1 
ATOM   3915  C CE    . LYS A 1 1807 ? 204.649 203.267 171.444 1.00 10.46  ? 1807 LYS A CE    1 
ATOM   3916  N NZ    . LYS A 1 1807 ? 205.231 203.846 170.204 1.00 10.46  ? 1807 LYS A NZ    1 
ATOM   3917  N N     . LEU A 1 1808 ? 203.846 200.187 176.889 1.00 11.78  ? 1808 LEU A N     1 
ATOM   3918  C CA    . LEU A 1 1808 ? 204.340 200.011 178.249 1.00 11.78  ? 1808 LEU A CA    1 
ATOM   3919  C C     . LEU A 1 1808 ? 203.934 198.659 178.816 1.00 11.78  ? 1808 LEU A C     1 
ATOM   3920  O O     . LEU A 1 1808 ? 204.745 197.980 179.453 1.00 11.78  ? 1808 LEU A O     1 
ATOM   3921  C CB    . LEU A 1 1808 ? 203.818 201.138 179.140 1.00 11.78  ? 1808 LEU A CB    1 
ATOM   3922  C CG    . LEU A 1 1808 ? 204.568 202.469 179.121 1.00 11.78  ? 1808 LEU A CG    1 
ATOM   3923  C CD1   . LEU A 1 1808 ? 204.035 203.393 180.199 1.00 11.78  ? 1808 LEU A CD1   1 
ATOM   3924  C CD2   . LEU A 1 1808 ? 206.047 202.242 179.308 1.00 11.78  ? 1808 LEU A CD2   1 
ATOM   3925  N N     . GLU A 1 1809 ? 202.684 198.247 178.599 1.00 15.30  ? 1809 GLU A N     1 
ATOM   3926  C CA    . GLU A 1 1809 ? 202.260 196.968 179.163 1.00 15.30  ? 1809 GLU A CA    1 
ATOM   3927  C C     . GLU A 1 1809 ? 202.874 195.788 178.415 1.00 15.30  ? 1809 GLU A C     1 
ATOM   3928  O O     . GLU A 1 1809 ? 203.187 194.766 179.039 1.00 15.30  ? 1809 GLU A O     1 
ATOM   3929  C CB    . GLU A 1 1809 ? 200.735 196.865 179.200 1.00 15.30  ? 1809 GLU A CB    1 
ATOM   3930  C CG    . GLU A 1 1809 ? 200.029 197.049 177.880 1.00 15.30  ? 1809 GLU A CG    1 
ATOM   3931  C CD    . GLU A 1 1809 ? 198.567 197.408 178.061 1.00 15.30  ? 1809 GLU A CD    1 
ATOM   3932  O OE1   . GLU A 1 1809 ? 198.208 197.903 179.150 1.00 15.30  ? 1809 GLU A OE1   1 
ATOM   3933  O OE2   . GLU A 1 1809 ? 197.776 197.192 177.119 1.00 15.30  ? 1809 GLU A OE2   1 
ATOM   3934  N N     . HIS A 1 1810 ? 203.083 195.905 177.099 1.00 11.70  ? 1810 HIS A N     1 
ATOM   3935  C CA    . HIS A 1 1810 ? 203.819 194.856 176.396 1.00 11.70  ? 1810 HIS A CA    1 
ATOM   3936  C C     . HIS A 1 1810 ? 205.242 194.740 176.927 1.00 11.70  ? 1810 HIS A C     1 
ATOM   3937  O O     . HIS A 1 1810 ? 205.752 193.630 177.138 1.00 11.70  ? 1810 HIS A O     1 
ATOM   3938  C CB    . HIS A 1 1810 ? 203.844 195.119 174.889 1.00 11.70  ? 1810 HIS A CB    1 
ATOM   3939  C CG    . HIS A 1 1810 ? 202.497 195.088 174.240 1.00 11.70  ? 1810 HIS A CG    1 
ATOM   3940  N ND1   . HIS A 1 1810 ? 201.588 194.076 174.461 1.00 11.70  ? 1810 HIS A ND1   1 
ATOM   3941  C CD2   . HIS A 1 1810 ? 201.924 195.916 173.336 1.00 11.70  ? 1810 HIS A CD2   1 
ATOM   3942  C CE1   . HIS A 1 1810 ? 200.500 194.301 173.747 1.00 11.70  ? 1810 HIS A CE1   1 
ATOM   3943  N NE2   . HIS A 1 1810 ? 200.679 195.411 173.054 1.00 11.70  ? 1810 HIS A NE2   1 
ATOM   3944  N N     . LEU A 1 1811 ? 205.899 195.881 177.153 1.00 10.34  ? 1811 LEU A N     1 
ATOM   3945  C CA    . LEU A 1 1811 ? 207.243 195.858 177.714 1.00 10.34  ? 1811 LEU A CA    1 
ATOM   3946  C C     . LEU A 1 1811 ? 207.249 195.247 179.105 1.00 10.34  ? 1811 LEU A C     1 
ATOM   3947  O O     . LEU A 1 1811 ? 208.163 194.496 179.452 1.00 10.34  ? 1811 LEU A O     1 
ATOM   3948  C CB    . LEU A 1 1811 ? 207.824 197.267 177.759 1.00 10.34  ? 1811 LEU A CB    1 
ATOM   3949  C CG    . LEU A 1 1811 ? 208.626 197.712 176.544 1.00 10.34  ? 1811 LEU A CG    1 
ATOM   3950  C CD1   . LEU A 1 1811 ? 208.916 199.187 176.667 1.00 10.34  ? 1811 LEU A CD1   1 
ATOM   3951  C CD2   . LEU A 1 1811 ? 209.909 196.912 176.429 1.00 10.34  ? 1811 LEU A CD2   1 
ATOM   3952  N N     . ILE A 1 1812 ? 206.249 195.573 179.925 1.00 10.53  ? 1812 ILE A N     1 
ATOM   3953  C CA    . ILE A 1 1812 ? 206.184 195.005 181.267 1.00 10.53  ? 1812 ILE A CA    1 
ATOM   3954  C C     . ILE A 1 1812 ? 206.029 193.494 181.197 1.00 10.53  ? 1812 ILE A C     1 
ATOM   3955  O O     . ILE A 1 1812 ? 206.698 192.757 181.926 1.00 10.53  ? 1812 ILE A O     1 
ATOM   3956  C CB    . ILE A 1 1812 ? 205.049 195.653 182.079 1.00 10.53  ? 1812 ILE A CB    1 
ATOM   3957  C CG1   . ILE A 1 1812 ? 205.444 197.062 182.511 1.00 10.53  ? 1812 ILE A CG1   1 
ATOM   3958  C CG2   . ILE A 1 1812 ? 204.718 194.811 183.296 1.00 10.53  ? 1812 ILE A CG2   1 
ATOM   3959  C CD1   . ILE A 1 1812 ? 204.352 197.795 183.239 1.00 10.53  ? 1812 ILE A CD1   1 
ATOM   3960  N N     . THR A 1 1813 ? 205.151 193.008 180.317 1.00 10.09  ? 1813 THR A N     1 
ATOM   3961  C CA    . THR A 1 1813 ? 204.973 191.565 180.177 1.00 10.09  ? 1813 THR A CA    1 
ATOM   3962  C C     . THR A 1 1813 ? 206.276 190.886 179.770 1.00 10.09  ? 1813 THR A C     1 
ATOM   3963  O O     . THR A 1 1813 ? 206.696 189.893 180.382 1.00 10.09  ? 1813 THR A O     1 
ATOM   3964  C CB    . THR A 1 1813 ? 203.874 191.270 179.156 1.00 10.09  ? 1813 THR A CB    1 
ATOM   3965  O OG1   . THR A 1 1813 ? 202.607 191.685 179.680 1.00 10.09  ? 1813 THR A OG1   1 
ATOM   3966  C CG2   . THR A 1 1813 ? 203.826 189.787 178.843 1.00 10.09  ? 1813 THR A CG2   1 
ATOM   3967  N N     . GLU A 1 1814 ? 206.944 191.422 178.745 1.00 12.85  ? 1814 GLU A N     1 
ATOM   3968  C CA    . GLU A 1 1814 ? 208.159 190.769 178.267 1.00 12.85  ? 1814 GLU A CA    1 
ATOM   3969  C C     . GLU A 1 1814 ? 209.282 190.856 179.294 1.00 12.85  ? 1814 GLU A C     1 
ATOM   3970  O O     . GLU A 1 1814 ? 210.039 189.896 179.475 1.00 12.85  ? 1814 GLU A O     1 
ATOM   3971  C CB    . GLU A 1 1814 ? 208.604 191.365 176.933 1.00 12.85  ? 1814 GLU A CB    1 
ATOM   3972  C CG    . GLU A 1 1814 ? 209.912 190.776 176.440 1.00 12.85  ? 1814 GLU A CG    1 
ATOM   3973  C CD    . GLU A 1 1814 ? 209.767 189.335 175.973 1.00 12.85  ? 1814 GLU A CD    1 
ATOM   3974  O OE1   . GLU A 1 1814 ? 208.624 188.837 175.893 1.00 12.85  ? 1814 GLU A OE1   1 
ATOM   3975  O OE2   . GLU A 1 1814 ? 210.802 188.686 175.715 1.00 12.85  ? 1814 GLU A OE2   1 
ATOM   3976  N N     . LEU A 1 1815 ? 209.407 191.993 179.981 1.00 12.35  ? 1815 LEU A N     1 
ATOM   3977  C CA    . LEU A 1 1815 ? 210.436 192.128 181.004 1.00 12.35  ? 1815 LEU A CA    1 
ATOM   3978  C C     . LEU A 1 1815 ? 210.163 191.225 182.197 1.00 12.35  ? 1815 LEU A C     1 
ATOM   3979  O O     . LEU A 1 1815 ? 211.104 190.712 182.803 1.00 12.35  ? 1815 LEU A O     1 
ATOM   3980  C CB    . LEU A 1 1815 ? 210.550 193.585 181.450 1.00 12.35  ? 1815 LEU A CB    1 
ATOM   3981  C CG    . LEU A 1 1815 ? 211.610 194.445 180.758 1.00 12.35  ? 1815 LEU A CG    1 
ATOM   3982  C CD1   . LEU A 1 1815 ? 213.000 193.921 181.065 1.00 12.35  ? 1815 LEU A CD1   1 
ATOM   3983  C CD2   . LEU A 1 1815 ? 211.385 194.510 179.260 1.00 12.35  ? 1815 LEU A CD2   1 
ATOM   3984  N N     . VAL A 1 1816 ? 208.893 191.018 182.551 1.00 12.30  ? 1816 VAL A N     1 
ATOM   3985  C CA    . VAL A 1 1816 ? 208.566 190.071 183.613 1.00 12.30  ? 1816 VAL A CA    1 
ATOM   3986  C C     . VAL A 1 1816 ? 208.960 188.661 183.202 1.00 12.30  ? 1816 VAL A C     1 
ATOM   3987  O O     . VAL A 1 1816 ? 209.519 187.898 184.000 1.00 12.30  ? 1816 VAL A O     1 
ATOM   3988  C CB    . VAL A 1 1816 ? 207.073 190.163 183.975 1.00 12.30  ? 1816 VAL A CB    1 
ATOM   3989  C CG1   . VAL A 1 1816 ? 206.645 188.944 184.767 1.00 12.30  ? 1816 VAL A CG1   1 
ATOM   3990  C CG2   . VAL A 1 1816 ? 206.804 191.421 184.776 1.00 12.30  ? 1816 VAL A CG2   1 
ATOM   3991  N N     . HIS A 1 1817 ? 208.678 188.290 181.950 1.00 13.11  ? 1817 HIS A N     1 
ATOM   3992  C CA    . HIS A 1 1817 ? 209.099 186.972 181.481 1.00 13.11  ? 1817 HIS A CA    1 
ATOM   3993  C C     . HIS A 1 1817 ? 210.616 186.830 181.526 1.00 13.11  ? 1817 HIS A C     1 
ATOM   3994  O O     . HIS A 1 1817 ? 211.138 185.794 181.954 1.00 13.11  ? 1817 HIS A O     1 
ATOM   3995  C CB    . HIS A 1 1817 ? 208.587 186.716 180.066 1.00 13.11  ? 1817 HIS A CB    1 
ATOM   3996  C CG    . HIS A 1 1817 ? 209.222 185.533 179.407 1.00 13.11  ? 1817 HIS A CG    1 
ATOM   3997  N ND1   . HIS A 1 1817 ? 210.002 185.640 178.275 1.00 13.11  ? 1817 HIS A ND1   1 
ATOM   3998  C CD2   . HIS A 1 1817 ? 209.200 184.218 179.725 1.00 13.11  ? 1817 HIS A CD2   1 
ATOM   3999  C CE1   . HIS A 1 1817 ? 210.429 184.441 177.923 1.00 13.11  ? 1817 HIS A CE1   1 
ATOM   4000  N NE2   . HIS A 1 1817 ? 209.956 183.560 178.785 1.00 13.11  ? 1817 HIS A NE2   1 
ATOM   4001  N N     . GLN A 1 1818 ? 211.338 187.864 181.091 1.00 11.71  ? 1818 GLN A N     1 
ATOM   4002  C CA    . GLN A 1 1818 ? 212.797 187.812 181.107 1.00 11.71  ? 1818 GLN A CA    1 
ATOM   4003  C C     . GLN A 1 1818 ? 213.335 187.728 182.530 1.00 11.71  ? 1818 GLN A C     1 
ATOM   4004  O O     . GLN A 1 1818 ? 214.309 187.015 182.793 1.00 11.71  ? 1818 GLN A O     1 
ATOM   4005  C CB    . GLN A 1 1818 ? 213.370 189.033 180.389 1.00 11.71  ? 1818 GLN A CB    1 
ATOM   4006  C CG    . GLN A 1 1818 ? 213.161 189.019 178.887 1.00 11.71  ? 1818 GLN A CG    1 
ATOM   4007  C CD    . GLN A 1 1818 ? 213.550 190.328 178.236 1.00 11.71  ? 1818 GLN A CD    1 
ATOM   4008  O OE1   . GLN A 1 1818 ? 214.141 191.199 178.872 1.00 11.71  ? 1818 GLN A OE1   1 
ATOM   4009  N NE2   . GLN A 1 1818 ? 213.221 190.474 176.960 1.00 11.71  ? 1818 GLN A NE2   1 
ATOM   4010  N N     . ARG A 1 1819 ? 212.721 188.465 183.458 1.00 14.37  ? 1819 ARG A N     1 
ATOM   4011  C CA    . ARG A 1 1819 ? 213.127 188.401 184.856 1.00 14.37  ? 1819 ARG A CA    1 
ATOM   4012  C C     . ARG A 1 1819 ? 212.904 187.011 185.429 1.00 14.37  ? 1819 ARG A C     1 
ATOM   4013  O O     . ARG A 1 1819 ? 213.759 186.483 186.147 1.00 14.37  ? 1819 ARG A O     1 
ATOM   4014  C CB    . ARG A 1 1819 ? 212.358 189.441 185.668 1.00 14.37  ? 1819 ARG A CB    1 
ATOM   4015  C CG    . ARG A 1 1819 ? 212.932 189.710 187.042 1.00 14.37  ? 1819 ARG A CG    1 
ATOM   4016  C CD    . ARG A 1 1819 ? 211.877 190.294 187.961 1.00 14.37  ? 1819 ARG A CD    1 
ATOM   4017  N NE    . ARG A 1 1819 ? 210.634 189.534 187.915 1.00 14.37  ? 1819 ARG A NE    1 
ATOM   4018  C CZ    . ARG A 1 1819 ? 209.475 189.967 188.391 1.00 14.37  ? 1819 ARG A CZ    1 
ATOM   4019  N NH1   . ARG A 1 1819 ? 209.361 191.157 188.956 1.00 14.37  ? 1819 ARG A NH1   1 
ATOM   4020  N NH2   . ARG A 1 1819 ? 208.403 189.185 188.297 1.00 14.37  ? 1819 ARG A NH2   1 
ATOM   4021  N N     . ASP A 1 1820 ? 211.756 186.402 185.125 1.00 14.42  ? 1820 ASP A N     1 
ATOM   4022  C CA    . ASP A 1 1820 ? 211.495 185.048 185.602 1.00 14.42  ? 1820 ASP A CA    1 
ATOM   4023  C C     . ASP A 1 1820 ? 212.486 184.056 185.010 1.00 14.42  ? 1820 ASP A C     1 
ATOM   4024  O O     . ASP A 1 1820 ? 212.930 183.129 185.697 1.00 14.42  ? 1820 ASP A O     1 
ATOM   4025  C CB    . ASP A 1 1820 ? 210.061 184.640 185.266 1.00 14.42  ? 1820 ASP A CB    1 
ATOM   4026  C CG    . ASP A 1 1820 ? 209.036 185.366 186.113 1.00 14.42  ? 1820 ASP A CG    1 
ATOM   4027  O OD1   . ASP A 1 1820 ? 209.422 185.943 187.151 1.00 14.42  ? 1820 ASP A OD1   1 
ATOM   4028  O OD2   . ASP A 1 1820 ? 207.844 185.361 185.740 1.00 14.42  ? 1820 ASP A OD2   1 
ATOM   4029  N N     . VAL A 1 1821 ? 212.840 184.232 183.737 1.00 14.11  ? 1821 VAL A N     1 
ATOM   4030  C CA    . VAL A 1 1821 ? 213.755 183.301 183.084 1.00 14.11  ? 1821 VAL A CA    1 
ATOM   4031  C C     . VAL A 1 1821 ? 215.156 183.422 183.673 1.00 14.11  ? 1821 VAL A C     1 
ATOM   4032  O O     . VAL A 1 1821 ? 215.786 182.420 184.029 1.00 14.11  ? 1821 VAL A O     1 
ATOM   4033  C CB    . VAL A 1 1821 ? 213.760 183.540 181.566 1.00 14.11  ? 1821 VAL A CB    1 
ATOM   4034  C CG1   . VAL A 1 1821 ? 214.979 182.896 180.925 1.00 14.11  ? 1821 VAL A CG1   1 
ATOM   4035  C CG2   . VAL A 1 1821 ? 212.476 183.025 180.954 1.00 14.11  ? 1821 VAL A CG2   1 
ATOM   4036  N N     . THR A 1 1822 ? 215.661 184.651 183.794 1.00 16.87  ? 1822 THR A N     1 
ATOM   4037  C CA    . THR A 1 1822 ? 217.026 184.845 184.270 1.00 16.87  ? 1822 THR A CA    1 
ATOM   4038  C C     . THR A 1 1822 ? 217.153 184.562 185.761 1.00 16.87  ? 1822 THR A C     1 
ATOM   4039  O O     . THR A 1 1822 ? 218.186 184.053 186.208 1.00 16.87  ? 1822 THR A O     1 
ATOM   4040  C CB    . THR A 1 1822 ? 217.493 186.268 183.966 1.00 16.87  ? 1822 THR A CB    1 
ATOM   4041  O OG1   . THR A 1 1822 ? 217.169 186.599 182.611 1.00 16.87  ? 1822 THR A OG1   1 
ATOM   4042  C CG2   . THR A 1 1822 ? 218.992 186.387 184.161 1.00 16.87  ? 1822 THR A CG2   1 
ATOM   4043  N N     . ARG A 1 1823 ? 216.121 184.886 186.542 1.00 21.78  ? 1823 ARG A N     1 
ATOM   4044  C CA    . ARG A 1 1823 ? 216.202 184.741 187.990 1.00 21.78  ? 1823 ARG A CA    1 
ATOM   4045  C C     . ARG A 1 1823 ? 216.325 183.281 188.404 1.00 21.78  ? 1823 ARG A C     1 
ATOM   4046  O O     . ARG A 1 1823 ? 217.101 182.951 189.308 1.00 21.78  ? 1823 ARG A O     1 
ATOM   4047  C CB    . ARG A 1 1823 ? 214.978 185.384 188.641 1.00 21.78  ? 1823 ARG A CB    1 
ATOM   4048  C CG    . ARG A 1 1823 ? 214.915 185.237 190.146 1.00 21.78  ? 1823 ARG A CG    1 
ATOM   4049  C CD    . ARG A 1 1823 ? 213.477 185.091 190.614 1.00 21.78  ? 1823 ARG A CD    1 
ATOM   4050  N NE    . ARG A 1 1823 ? 212.690 186.289 190.348 1.00 21.78  ? 1823 ARG A NE    1 
ATOM   4051  C CZ    . ARG A 1 1823 ? 212.765 187.410 191.053 1.00 21.78  ? 1823 ARG A CZ    1 
ATOM   4052  N NH1   . ARG A 1 1823 ? 213.591 187.528 192.079 1.00 21.78  ? 1823 ARG A NH1   1 
ATOM   4053  N NH2   . ARG A 1 1823 ? 211.989 188.438 190.721 1.00 21.78  ? 1823 ARG A NH2   1 
ATOM   4054  N N     . SER A 1 1824 ? 215.570 182.392 187.762 1.00 22.10  ? 1824 SER A N     1 
ATOM   4055  C CA    . SER A 1 1824 ? 215.547 180.988 188.151 1.00 22.10  ? 1824 SER A CA    1 
ATOM   4056  C C     . SER A 1 1824 ? 216.064 180.060 187.064 1.00 22.10  ? 1824 SER A C     1 
ATOM   4057  O O     . SER A 1 1824 ? 216.977 179.266 187.319 1.00 22.10  ? 1824 SER A O     1 
ATOM   4058  C CB    . SER A 1 1824 ? 214.121 180.578 188.551 1.00 22.10  ? 1824 SER A CB    1 
ATOM   4059  O OG    . SER A 1 1824 ? 213.220 180.743 187.470 1.00 22.10  ? 1824 SER A OG    1 
ATOM   4060  N N     . LEU A 1 1825 ? 215.513 180.139 185.853 1.00 22.56  ? 1825 LEU A N     1 
ATOM   4061  C CA    . LEU A 1 1825 ? 215.864 179.185 184.808 1.00 22.56  ? 1825 LEU A CA    1 
ATOM   4062  C C     . LEU A 1 1825 ? 217.297 179.332 184.316 1.00 22.56  ? 1825 LEU A C     1 
ATOM   4063  O O     . LEU A 1 1825 ? 217.776 178.446 183.601 1.00 22.56  ? 1825 LEU A O     1 
ATOM   4064  C CB    . LEU A 1 1825 ? 214.902 179.313 183.624 1.00 22.56  ? 1825 LEU A CB    1 
ATOM   4065  C CG    . LEU A 1 1825 ? 213.572 178.558 183.706 1.00 22.56  ? 1825 LEU A CG    1 
ATOM   4066  C CD1   . LEU A 1 1825 ? 212.590 179.256 184.634 1.00 22.56  ? 1825 LEU A CD1   1 
ATOM   4067  C CD2   . LEU A 1 1825 ? 212.970 178.382 182.319 1.00 22.56  ? 1825 LEU A CD2   1 
ATOM   4068  N N     . ILE A 1 1826 ? 217.986 180.417 184.661 1.00 23.83  ? 1826 ILE A N     1 
ATOM   4069  C CA    . ILE A 1 1826 ? 219.365 180.626 184.232 1.00 23.83  ? 1826 ILE A CA    1 
ATOM   4070  C C     . ILE A 1 1826 ? 220.329 180.775 185.399 1.00 23.83  ? 1826 ILE A C     1 
ATOM   4071  O O     . ILE A 1 1826 ? 221.532 180.529 185.222 1.00 23.83  ? 1826 ILE A O     1 
ATOM   4072  C CB    . ILE A 1 1826 ? 219.481 181.844 183.287 1.00 23.83  ? 1826 ILE A CB    1 
ATOM   4073  C CG1   . ILE A 1 1826 ? 218.401 181.788 182.209 1.00 23.83  ? 1826 ILE A CG1   1 
ATOM   4074  C CG2   . ILE A 1 1826 ? 220.832 181.875 182.598 1.00 23.83  ? 1826 ILE A CG2   1 
ATOM   4075  C CD1   . ILE A 1 1826 ? 218.535 180.606 181.283 1.00 23.83  ? 1826 ILE A CD1   1 
ATOM   4076  N N     . LYS A 1 1827 ? 219.853 181.134 186.589 1.00 25.06  ? 1827 LYS A N     1 
ATOM   4077  C CA    . LYS A 1 1827 ? 220.717 181.343 187.742 1.00 25.06  ? 1827 LYS A CA    1 
ATOM   4078  C C     . LYS A 1 1827 ? 220.842 180.103 188.619 1.00 25.06  ? 1827 LYS A C     1 
ATOM   4079  O O     . LYS A 1 1827 ? 221.366 180.196 189.734 1.00 25.06  ? 1827 LYS A O     1 
ATOM   4080  C CB    . LYS A 1 1827 ? 220.212 182.522 188.572 1.00 25.06  ? 1827 LYS A CB    1 
ATOM   4081  C CG    . LYS A 1 1827 ? 221.315 183.330 189.229 1.00 25.06  ? 1827 LYS A CG    1 
ATOM   4082  C CD    . LYS A 1 1827 ? 220.799 184.674 189.702 1.00 25.06  ? 1827 LYS A CD    1 
ATOM   4083  C CE    . LYS A 1 1827 ? 220.221 185.470 188.547 1.00 25.06  ? 1827 LYS A CE    1 
ATOM   4084  N NZ    . LYS A 1 1827 ? 221.179 185.576 187.414 1.00 25.06  ? 1827 LYS A NZ    1 
ATOM   4085  N N     . SER A 1 1828 ? 220.371 178.950 188.149 1.00 23.14  ? 1828 SER A N     1 
ATOM   4086  C CA    . SER A 1 1828 ? 220.510 177.698 188.892 1.00 23.14  ? 1828 SER A CA    1 
ATOM   4087  C C     . SER A 1 1828 ? 221.830 177.010 188.539 1.00 23.14  ? 1828 SER A C     1 
ATOM   4088  O O     . SER A 1 1828 ? 221.871 175.918 187.974 1.00 23.14  ? 1828 SER A O     1 
ATOM   4089  C CB    . SER A 1 1828 ? 219.318 176.787 188.621 1.00 23.14  ? 1828 SER A CB    1 
ATOM   4090  O OG    . SER A 1 1828 ? 218.133 177.320 189.186 1.00 23.14  ? 1828 SER A OG    1 
ATOM   4091  N N     . LYS A 1 1829 ? 222.925 177.688 188.895 1.00 27.46  ? 1829 LYS A N     1 
ATOM   4092  C CA    . LYS A 1 1829 ? 224.283 177.182 188.687 1.00 27.46  ? 1829 LYS A CA    1 
ATOM   4093  C C     . LYS A 1 1829 ? 224.526 176.821 187.222 1.00 27.46  ? 1829 LYS A C     1 
ATOM   4094  O O     . LYS A 1 1829 ? 225.009 175.735 186.896 1.00 27.46  ? 1829 LYS A O     1 
ATOM   4095  C CB    . LYS A 1 1829 ? 224.569 175.987 189.601 1.00 27.46  ? 1829 LYS A CB    1 
ATOM   4096  C CG    . LYS A 1 1829 ? 224.401 176.281 191.084 1.00 27.46  ? 1829 LYS A CG    1 
ATOM   4097  C CD    . LYS A 1 1829 ? 225.153 177.538 191.488 1.00 27.46  ? 1829 LYS A CD    1 
ATOM   4098  C CE    . LYS A 1 1829 ? 224.883 177.897 192.939 1.00 27.46  ? 1829 LYS A CE    1 
ATOM   4099  N NZ    . LYS A 1 1829 ? 223.426 178.012 193.219 1.00 27.46  ? 1829 LYS A NZ    1 
ATOM   4100  N N     . ILE A 1 1830 ? 224.182 177.748 186.334 1.00 30.92  ? 1830 ILE A N     1 
ATOM   4101  C CA    . ILE A 1 1830 ? 224.343 177.568 184.896 1.00 30.92  ? 1830 ILE A CA    1 
ATOM   4102  C C     . ILE A 1 1830 ? 225.422 178.529 184.422 1.00 30.92  ? 1830 ILE A C     1 
ATOM   4103  O O     . ILE A 1 1830 ? 225.333 179.740 184.657 1.00 30.92  ? 1830 ILE A O     1 
ATOM   4104  C CB    . ILE A 1 1830 ? 223.022 177.796 184.149 1.00 30.92  ? 1830 ILE A CB    1 
ATOM   4105  C CG1   . ILE A 1 1830 ? 221.988 176.771 184.613 1.00 30.92  ? 1830 ILE A CG1   1 
ATOM   4106  C CG2   . ILE A 1 1830 ? 223.236 177.706 182.649 1.00 30.92  ? 1830 ILE A CG2   1 
ATOM   4107  C CD1   . ILE A 1 1830 ? 220.578 177.134 184.266 1.00 30.92  ? 1830 ILE A CD1   1 
ATOM   4108  N N     . ASP A 1 1831 ? 226.441 177.989 183.753 1.00 41.60  ? 1831 ASP A N     1 
ATOM   4109  C CA    . ASP A 1 1831 ? 227.610 178.765 183.374 1.00 41.60  ? 1831 ASP A CA    1 
ATOM   4110  C C     . ASP A 1 1831 ? 228.058 178.553 181.935 1.00 41.60  ? 1831 ASP A C     1 
ATOM   4111  O O     . ASP A 1 1831 ? 229.014 179.206 181.503 1.00 41.60  ? 1831 ASP A O     1 
ATOM   4112  C CB    . ASP A 1 1831 ? 228.780 178.447 184.317 1.00 41.60  ? 1831 ASP A CB    1 
ATOM   4113  C CG    . ASP A 1 1831 ? 229.088 176.963 184.382 1.00 41.60  ? 1831 ASP A CG    1 
ATOM   4114  O OD1   . ASP A 1 1831 ? 228.337 176.171 183.775 1.00 41.60  ? 1831 ASP A OD1   1 
ATOM   4115  O OD2   . ASP A 1 1831 ? 230.078 176.587 185.042 1.00 41.60  ? 1831 ASP A OD2   1 
ATOM   4116  N N     . ASN A 1 1832 ? 227.407 177.672 181.183 1.00 32.59  ? 1832 ASN A N     1 
ATOM   4117  C CA    . ASN A 1 1832 ? 227.801 177.365 179.817 1.00 32.59  ? 1832 ASN A CA    1 
ATOM   4118  C C     . ASN A 1 1832 ? 226.744 177.865 178.844 1.00 32.59  ? 1832 ASN A C     1 
ATOM   4119  O O     . ASN A 1 1832 ? 225.544 177.670 179.062 1.00 32.59  ? 1832 ASN A O     1 
ATOM   4120  C CB    . ASN A 1 1832 ? 228.014 175.861 179.630 1.00 32.59  ? 1832 ASN A CB    1 
ATOM   4121  C CG    . ASN A 1 1832 ? 228.798 175.537 178.376 1.00 32.59  ? 1832 ASN A CG    1 
ATOM   4122  O OD1   . ASN A 1 1832 ? 229.264 176.433 177.672 1.00 32.59  ? 1832 ASN A OD1   1 
ATOM   4123  N ND2   . ASN A 1 1832 ? 228.952 174.249 178.091 1.00 32.59  ? 1832 ASN A ND2   1 
ATOM   4124  N N     . ALA A 1 1833 ? 227.196 178.512 177.769 1.00 29.04  ? 1833 ALA A N     1 
ATOM   4125  C CA    . ALA A 1 1833 ? 226.280 179.042 176.768 1.00 29.04  ? 1833 ALA A CA    1 
ATOM   4126  C C     . ALA A 1 1833 ? 225.638 177.956 175.918 1.00 29.04  ? 1833 ALA A C     1 
ATOM   4127  O O     . ALA A 1 1833 ? 224.641 178.234 175.243 1.00 29.04  ? 1833 ALA A O     1 
ATOM   4128  C CB    . ALA A 1 1833 ? 227.011 180.036 175.865 1.00 29.04  ? 1833 ALA A CB    1 
ATOM   4129  N N     . LYS A 1 1834 ? 226.177 176.740 175.929 1.00 26.12  ? 1834 LYS A N     1 
ATOM   4130  C CA    . LYS A 1 1834 ? 225.637 175.638 175.146 1.00 26.12  ? 1834 LYS A CA    1 
ATOM   4131  C C     . LYS A 1 1834 ? 224.756 174.702 175.962 1.00 26.12  ? 1834 LYS A C     1 
ATOM   4132  O O     . LYS A 1 1834 ? 224.255 173.716 175.414 1.00 26.12  ? 1834 LYS A O     1 
ATOM   4133  C CB    . LYS A 1 1834 ? 226.776 174.842 174.502 1.00 26.12  ? 1834 LYS A CB    1 
ATOM   4134  C CG    . LYS A 1 1834 ? 227.584 175.630 173.486 1.00 26.12  ? 1834 LYS A CG    1 
ATOM   4135  C CD    . LYS A 1 1834 ? 226.705 176.129 172.352 1.00 26.12  ? 1834 LYS A CD    1 
ATOM   4136  C CE    . LYS A 1 1834 ? 227.521 176.867 171.304 1.00 26.12  ? 1834 LYS A CE    1 
ATOM   4137  N NZ    . LYS A 1 1834 ? 228.233 178.041 171.879 1.00 26.12  ? 1834 LYS A NZ    1 
ATOM   4138  N N     . SER A 1 1835 ? 224.560 174.977 177.248 1.00 21.50  ? 1835 SER A N     1 
ATOM   4139  C CA    . SER A 1 1835 ? 223.704 174.132 178.068 1.00 21.50  ? 1835 SER A CA    1 
ATOM   4140  C C     . SER A 1 1835 ? 222.255 174.250 177.614 1.00 21.50  ? 1835 SER A C     1 
ATOM   4141  O O     . SER A 1 1835 ? 221.793 175.330 177.240 1.00 21.50  ? 1835 SER A O     1 
ATOM   4142  C CB    . SER A 1 1835 ? 223.825 174.519 179.539 1.00 21.50  ? 1835 SER A CB    1 
ATOM   4143  O OG    . SER A 1 1835 ? 223.366 175.841 179.754 1.00 21.50  ? 1835 SER A OG    1 
ATOM   4144  N N     . PHE A 1 1836 ? 221.535 173.126 177.649 1.00 13.34  ? 1836 PHE A N     1 
ATOM   4145  C CA    . PHE A 1 1836 ? 220.154 173.124 177.181 1.00 13.34  ? 1836 PHE A CA    1 
ATOM   4146  C C     . PHE A 1 1836 ? 219.238 173.974 178.049 1.00 13.34  ? 1836 PHE A C     1 
ATOM   4147  O O     . PHE A 1 1836 ? 218.158 174.359 177.591 1.00 13.34  ? 1836 PHE A O     1 
ATOM   4148  C CB    . PHE A 1 1836 ? 219.609 171.700 177.108 1.00 13.34  ? 1836 PHE A CB    1 
ATOM   4149  C CG    . PHE A 1 1836 ? 218.299 171.598 176.384 1.00 13.34  ? 1836 PHE A CG    1 
ATOM   4150  C CD1   . PHE A 1 1836 ? 218.249 171.675 175.004 1.00 13.34  ? 1836 PHE A CD1   1 
ATOM   4151  C CD2   . PHE A 1 1836 ? 217.117 171.442 177.082 1.00 13.34  ? 1836 PHE A CD2   1 
ATOM   4152  C CE1   . PHE A 1 1836 ? 217.046 171.587 174.336 1.00 13.34  ? 1836 PHE A CE1   1 
ATOM   4153  C CE2   . PHE A 1 1836 ? 215.913 171.357 176.418 1.00 13.34  ? 1836 PHE A CE2   1 
ATOM   4154  C CZ    . PHE A 1 1836 ? 215.877 171.427 175.044 1.00 13.34  ? 1836 PHE A CZ    1 
ATOM   4155  N N     . GLU A 1 1837 ? 219.637 174.274 179.287 1.00 18.93  ? 1837 GLU A N     1 
ATOM   4156  C CA    . GLU A 1 1837 ? 218.824 175.153 180.118 1.00 18.93  ? 1837 GLU A CA    1 
ATOM   4157  C C     . GLU A 1 1837 ? 218.707 176.542 179.506 1.00 18.93  ? 1837 GLU A C     1 
ATOM   4158  O O     . GLU A 1 1837 ? 217.706 177.234 179.723 1.00 18.93  ? 1837 GLU A O     1 
ATOM   4159  C CB    . GLU A 1 1837 ? 219.411 175.237 181.526 1.00 18.93  ? 1837 GLU A CB    1 
ATOM   4160  C CG    . GLU A 1 1837 ? 218.718 174.348 182.550 1.00 18.93  ? 1837 GLU A CG    1 
ATOM   4161  C CD    . GLU A 1 1837 ? 217.343 174.856 182.948 1.00 18.93  ? 1837 GLU A CD    1 
ATOM   4162  O OE1   . GLU A 1 1837 ? 216.655 174.157 183.722 1.00 18.93  ? 1837 GLU A OE1   1 
ATOM   4163  O OE2   . GLU A 1 1837 ? 216.951 175.953 182.499 1.00 18.93  ? 1837 GLU A OE2   1 
ATOM   4164  N N     . TRP A 1 1838 ? 219.714 176.965 178.745 1.00 12.94  ? 1838 TRP A N     1 
ATOM   4165  C CA    . TRP A 1 1838 ? 219.658 178.214 177.999 1.00 12.94  ? 1838 TRP A CA    1 
ATOM   4166  C C     . TRP A 1 1838 ? 219.255 178.022 176.546 1.00 12.94  ? 1838 TRP A C     1 
ATOM   4167  O O     . TRP A 1 1838 ? 218.609 178.905 175.973 1.00 12.94  ? 1838 TRP A O     1 
ATOM   4168  C CB    . TRP A 1 1838 ? 221.013 178.925 178.053 1.00 12.94  ? 1838 TRP A CB    1 
ATOM   4169  C CG    . TRP A 1 1838 ? 221.110 180.119 177.154 1.00 12.94  ? 1838 TRP A CG    1 
ATOM   4170  C CD1   . TRP A 1 1838 ? 222.007 180.310 176.145 1.00 12.94  ? 1838 TRP A CD1   1 
ATOM   4171  C CD2   . TRP A 1 1838 ? 220.284 181.288 177.183 1.00 12.94  ? 1838 TRP A CD2   1 
ATOM   4172  N NE1   . TRP A 1 1838 ? 221.790 181.525 175.543 1.00 12.94  ? 1838 TRP A NE1   1 
ATOM   4173  C CE2   . TRP A 1 1838 ? 220.738 182.145 176.163 1.00 12.94  ? 1838 TRP A CE2   1 
ATOM   4174  C CE3   . TRP A 1 1838 ? 219.205 181.695 177.973 1.00 12.94  ? 1838 TRP A CE3   1 
ATOM   4175  C CZ2   . TRP A 1 1838 ? 220.152 183.381 175.912 1.00 12.94  ? 1838 TRP A CZ2   1 
ATOM   4176  C CZ3   . TRP A 1 1838 ? 218.624 182.921 177.721 1.00 12.94  ? 1838 TRP A CZ3   1 
ATOM   4177  C CH2   . TRP A 1 1838 ? 219.097 183.749 176.699 1.00 12.94  ? 1838 TRP A CH2   1 
ATOM   4178  N N     . LEU A 1 1839 ? 219.616 176.889 175.938 1.00 12.56  ? 1839 LEU A N     1 
ATOM   4179  C CA    . LEU A 1 1839 ? 219.240 176.642 174.551 1.00 12.56  ? 1839 LEU A CA    1 
ATOM   4180  C C     . LEU A 1 1839 ? 217.737 176.461 174.397 1.00 12.56  ? 1839 LEU A C     1 
ATOM   4181  O O     . LEU A 1 1839 ? 217.186 176.755 173.331 1.00 12.56  ? 1839 LEU A O     1 
ATOM   4182  C CB    . LEU A 1 1839 ? 219.976 175.414 174.017 1.00 12.56  ? 1839 LEU A CB    1 
ATOM   4183  C CG    . LEU A 1 1839 ? 221.470 175.577 173.746 1.00 12.56  ? 1839 LEU A CG    1 
ATOM   4184  C CD1   . LEU A 1 1839 ? 222.000 174.392 172.962 1.00 12.56  ? 1839 LEU A CD1   1 
ATOM   4185  C CD2   . LEU A 1 1839 ? 221.738 176.872 173.004 1.00 12.56  ? 1839 LEU A CD2   1 
ATOM   4186  N N     . SER A 1 1840 ? 217.061 175.978 175.441 1.00 15.44  ? 1840 SER A N     1 
ATOM   4187  C CA    . SER A 1 1840 ? 215.616 175.797 175.365 1.00 15.44  ? 1840 SER A CA    1 
ATOM   4188  C C     . SER A 1 1840 ? 214.887 177.125 175.232 1.00 15.44  ? 1840 SER A C     1 
ATOM   4189  O O     . SER A 1 1840 ? 213.802 177.178 174.644 1.00 15.44  ? 1840 SER A O     1 
ATOM   4190  C CB    . SER A 1 1840 ? 215.115 175.043 176.595 1.00 15.44  ? 1840 SER A CB    1 
ATOM   4191  O OG    . SER A 1 1840 ? 213.706 175.131 176.703 1.00 15.44  ? 1840 SER A OG    1 
ATOM   4192  N N     . GLN A 1 1841 ? 215.455 178.198 175.773 1.00 15.80  ? 1841 GLN A N     1 
ATOM   4193  C CA    . GLN A 1 1841 ? 214.797 179.493 175.750 1.00 15.80  ? 1841 GLN A CA    1 
ATOM   4194  C C     . GLN A 1 1841 ? 214.894 180.126 174.368 1.00 15.80  ? 1841 GLN A C     1 
ATOM   4195  O O     . GLN A 1 1841 ? 215.867 179.930 173.636 1.00 15.80  ? 1841 GLN A O     1 
ATOM   4196  C CB    . GLN A 1 1841 ? 215.411 180.423 176.793 1.00 15.80  ? 1841 GLN A CB    1 
ATOM   4197  C CG    . GLN A 1 1841 ? 215.208 179.946 178.213 1.00 15.80  ? 1841 GLN A CG    1 
ATOM   4198  C CD    . GLN A 1 1841 ? 213.746 179.845 178.572 1.00 15.80  ? 1841 GLN A CD    1 
ATOM   4199  O OE1   . GLN A 1 1841 ? 213.211 178.751 178.745 1.00 15.80  ? 1841 GLN A OE1   1 
ATOM   4200  N NE2   . GLN A 1 1841 ? 213.077 180.985 178.644 1.00 15.80  ? 1841 GLN A NE2   1 
ATOM   4201  N N     . MET A 1 1842 ? 213.866 180.894 174.017 1.00 14.04  ? 1842 MET A N     1 
ATOM   4202  C CA    . MET A 1 1842 ? 213.824 181.573 172.726 1.00 14.04  ? 1842 MET A CA    1 
ATOM   4203  C C     . MET A 1 1842 ? 214.877 182.672 172.700 1.00 14.04  ? 1842 MET A C     1 
ATOM   4204  O O     . MET A 1 1842 ? 214.722 183.708 173.353 1.00 14.04  ? 1842 MET A O     1 
ATOM   4205  C CB    . MET A 1 1842 ? 212.432 182.143 172.476 1.00 14.04  ? 1842 MET A CB    1 
ATOM   4206  C CG    . MET A 1 1842 ? 212.288 182.865 171.151 1.00 14.04  ? 1842 MET A CG    1 
ATOM   4207  S SD    . MET A 1 1842 ? 210.589 182.868 170.560 1.00 14.04  ? 1842 MET A SD    1 
ATOM   4208  C CE    . MET A 1 1842 ? 210.532 181.309 169.684 1.00 14.04  ? 1842 MET A CE    1 
ATOM   4209  N N     . ARG A 1 1843 ? 215.948 182.450 171.947 1.00 12.85  ? 1843 ARG A N     1 
ATOM   4210  C CA    . ARG A 1 1843 ? 217.054 183.390 171.859 1.00 12.85  ? 1843 ARG A CA    1 
ATOM   4211  C C     . ARG A 1 1843 ? 216.988 184.160 170.548 1.00 12.85  ? 1843 ARG A C     1 
ATOM   4212  O O     . ARG A 1 1843 ? 216.660 183.597 169.500 1.00 12.85  ? 1843 ARG A O     1 
ATOM   4213  C CB    . ARG A 1 1843 ? 218.395 182.664 171.973 1.00 12.85  ? 1843 ARG A CB    1 
ATOM   4214  C CG    . ARG A 1 1843 ? 218.530 181.825 173.227 1.00 12.85  ? 1843 ARG A CG    1 
ATOM   4215  C CD    . ARG A 1 1843 ? 219.466 180.651 173.014 1.00 12.85  ? 1843 ARG A CD    1 
ATOM   4216  N NE    . ARG A 1 1843 ? 218.820 179.557 172.302 1.00 12.85  ? 1843 ARG A NE    1 
ATOM   4217  C CZ    . ARG A 1 1843 ? 219.321 178.968 171.225 1.00 12.85  ? 1843 ARG A CZ    1 
ATOM   4218  N NH1   . ARG A 1 1843 ? 220.479 179.343 170.708 1.00 12.85  ? 1843 ARG A NH1   1 
ATOM   4219  N NH2   . ARG A 1 1843 ? 218.643 177.977 170.653 1.00 12.85  ? 1843 ARG A NH2   1 
ATOM   4220  N N     . PHE A 1 1844 ? 217.301 185.450 170.616 1.00 11.17  ? 1844 PHE A N     1 
ATOM   4221  C CA    . PHE A 1 1844 ? 217.307 186.330 169.457 1.00 11.17  ? 1844 PHE A CA    1 
ATOM   4222  C C     . PHE A 1 1844 ? 218.737 186.750 169.154 1.00 11.17  ? 1844 PHE A C     1 
ATOM   4223  O O     . PHE A 1 1844 ? 219.467 187.173 170.056 1.00 11.17  ? 1844 PHE A O     1 
ATOM   4224  C CB    . PHE A 1 1844 ? 216.438 187.565 169.698 1.00 11.17  ? 1844 PHE A CB    1 
ATOM   4225  C CG    . PHE A 1 1844 ? 214.989 187.254 169.925 1.00 11.17  ? 1844 PHE A CG    1 
ATOM   4226  C CD1   . PHE A 1 1844 ? 214.545 186.817 171.160 1.00 11.17  ? 1844 PHE A CD1   1 
ATOM   4227  C CD2   . PHE A 1 1844 ? 214.069 187.407 168.905 1.00 11.17  ? 1844 PHE A CD2   1 
ATOM   4228  C CE1   . PHE A 1 1844 ? 213.214 186.533 171.369 1.00 11.17  ? 1844 PHE A CE1   1 
ATOM   4229  C CE2   . PHE A 1 1844 ? 212.736 187.125 169.109 1.00 11.17  ? 1844 PHE A CE2   1 
ATOM   4230  C CZ    . PHE A 1 1844 ? 212.308 186.687 170.343 1.00 11.17  ? 1844 PHE A CZ    1 
ATOM   4231  N N     . TYR A 1 1845 ? 219.132 186.632 167.890 1.00 16.38  ? 1845 TYR A N     1 
ATOM   4232  C CA    . TYR A 1 1845 ? 220.473 186.991 167.448 1.00 16.38  ? 1845 TYR A CA    1 
ATOM   4233  C C     . TYR A 1 1845 ? 220.358 187.999 166.315 1.00 16.38  ? 1845 TYR A C     1 
ATOM   4234  O O     . TYR A 1 1845 ? 219.721 187.721 165.295 1.00 16.38  ? 1845 TYR A O     1 
ATOM   4235  C CB    . TYR A 1 1845 ? 221.249 185.752 167.002 1.00 16.38  ? 1845 TYR A CB    1 
ATOM   4236  C CG    . TYR A 1 1845 ? 221.474 184.760 168.119 1.00 16.38  ? 1845 TYR A CG    1 
ATOM   4237  C CD1   . TYR A 1 1845 ? 222.060 185.155 169.314 1.00 16.38  ? 1845 TYR A CD1   1 
ATOM   4238  C CD2   . TYR A 1 1845 ? 221.090 183.435 167.985 1.00 16.38  ? 1845 TYR A CD2   1 
ATOM   4239  C CE1   . TYR A 1 1845 ? 222.264 184.256 170.340 1.00 16.38  ? 1845 TYR A CE1   1 
ATOM   4240  C CE2   . TYR A 1 1845 ? 221.289 182.529 169.006 1.00 16.38  ? 1845 TYR A CE2   1 
ATOM   4241  C CZ    . TYR A 1 1845 ? 221.877 182.945 170.181 1.00 16.38  ? 1845 TYR A CZ    1 
ATOM   4242  O OH    . TYR A 1 1845 ? 222.078 182.047 171.202 1.00 16.38  ? 1845 TYR A OH    1 
ATOM   4243  N N     . PHE A 1 1846 ? 220.980 189.160 166.493 1.00 23.27  ? 1846 PHE A N     1 
ATOM   4244  C CA    . PHE A 1 1846 ? 220.896 190.257 165.539 1.00 23.27  ? 1846 PHE A CA    1 
ATOM   4245  C C     . PHE A 1 1846 ? 222.238 190.438 164.848 1.00 23.27  ? 1846 PHE A C     1 
ATOM   4246  O O     . PHE A 1 1846 ? 223.266 190.607 165.512 1.00 23.27  ? 1846 PHE A O     1 
ATOM   4247  C CB    . PHE A 1 1846 ? 220.482 191.554 166.236 1.00 23.27  ? 1846 PHE A CB    1 
ATOM   4248  C CG    . PHE A 1 1846 ? 219.974 192.609 165.298 1.00 23.27  ? 1846 PHE A CG    1 
ATOM   4249  C CD1   . PHE A 1 1846 ? 218.888 192.360 164.479 1.00 23.27  ? 1846 PHE A CD1   1 
ATOM   4250  C CD2   . PHE A 1 1846 ? 220.582 193.849 165.236 1.00 23.27  ? 1846 PHE A CD2   1 
ATOM   4251  C CE1   . PHE A 1 1846 ? 218.418 193.327 163.616 1.00 23.27  ? 1846 PHE A CE1   1 
ATOM   4252  C CE2   . PHE A 1 1846 ? 220.117 194.821 164.374 1.00 23.27  ? 1846 PHE A CE2   1 
ATOM   4253  C CZ    . PHE A 1 1846 ? 219.033 194.558 163.563 1.00 23.27  ? 1846 PHE A CZ    1 
ATOM   4254  N N     . ASP A 1 1847 ? 222.223 190.406 163.517 1.00 37.11  ? 1847 ASP A N     1 
ATOM   4255  C CA    . ASP A 1 1847 ? 223.418 190.607 162.700 1.00 37.11  ? 1847 ASP A CA    1 
ATOM   4256  C C     . ASP A 1 1847 ? 223.104 191.694 161.682 1.00 37.11  ? 1847 ASP A C     1 
ATOM   4257  O O     . ASP A 1 1847 ? 222.730 191.401 160.538 1.00 37.11  ? 1847 ASP A O     1 
ATOM   4258  C CB    . ASP A 1 1847 ? 223.852 189.311 162.020 1.00 37.11  ? 1847 ASP A CB    1 
ATOM   4259  C CG    . ASP A 1 1847 ? 225.281 189.367 161.519 1.00 37.11  ? 1847 ASP A CG    1 
ATOM   4260  O OD1   . ASP A 1 1847 ? 225.915 190.436 161.640 1.00 37.11  ? 1847 ASP A OD1   1 
ATOM   4261  O OD2   . ASP A 1 1847 ? 225.772 188.341 161.003 1.00 37.11  ? 1847 ASP A OD2   1 
ATOM   4262  N N     . PRO A 1 1848 ? 223.235 192.965 162.066 1.00 40.18  ? 1848 PRO A N     1 
ATOM   4263  C CA    . PRO A 1 1848 ? 222.891 194.053 161.136 1.00 40.18  ? 1848 PRO A CA    1 
ATOM   4264  C C     . PRO A 1 1848 ? 223.786 194.120 159.911 1.00 40.18  ? 1848 PRO A C     1 
ATOM   4265  O O     . PRO A 1 1848 ? 223.400 194.748 158.918 1.00 40.18  ? 1848 PRO A O     1 
ATOM   4266  C CB    . PRO A 1 1848 ? 223.033 195.311 162.003 1.00 40.18  ? 1848 PRO A CB    1 
ATOM   4267  C CG    . PRO A 1 1848 ? 223.999 194.923 163.072 1.00 40.18  ? 1848 PRO A CG    1 
ATOM   4268  C CD    . PRO A 1 1848 ? 223.752 193.469 163.350 1.00 40.18  ? 1848 PRO A CD    1 
ATOM   4269  N N     . LYS A 1 1849 ? 224.967 193.499 159.949 1.00 46.22  ? 1849 LYS A N     1 
ATOM   4270  C CA    . LYS A 1 1849 ? 225.885 193.557 158.817 1.00 46.22  ? 1849 LYS A CA    1 
ATOM   4271  C C     . LYS A 1 1849 ? 225.352 192.829 157.591 1.00 46.22  ? 1849 LYS A C     1 
ATOM   4272  O O     . LYS A 1 1849 ? 225.807 193.108 156.477 1.00 46.22  ? 1849 LYS A O     1 
ATOM   4273  C CB    . LYS A 1 1849 ? 227.244 192.974 159.210 1.00 46.22  ? 1849 LYS A CB    1 
ATOM   4274  C CG    . LYS A 1 1849 ? 228.200 193.976 159.841 1.00 46.22  ? 1849 LYS A CG    1 
ATOM   4275  C CD    . LYS A 1 1849 ? 227.817 194.290 161.277 1.00 46.22  ? 1849 LYS A CD    1 
ATOM   4276  C CE    . LYS A 1 1849 ? 228.030 193.088 162.180 1.00 46.22  ? 1849 LYS A CE    1 
ATOM   4277  N NZ    . LYS A 1 1849 ? 227.697 193.397 163.597 1.00 46.22  ? 1849 LYS A NZ    1 
ATOM   4278  N N     . GLN A 1 1850 ? 224.410 191.905 157.765 1.00 47.47  ? 1850 GLN A N     1 
ATOM   4279  C CA    . GLN A 1 1850 ? 223.889 191.149 156.635 1.00 47.47  ? 1850 GLN A CA    1 
ATOM   4280  C C     . GLN A 1 1850 ? 223.068 192.052 155.721 1.00 47.47  ? 1850 GLN A C     1 
ATOM   4281  O O     . GLN A 1 1850 ? 222.275 192.874 156.188 1.00 47.47  ? 1850 GLN A O     1 
ATOM   4282  C CB    . GLN A 1 1850 ? 223.041 189.979 157.130 1.00 47.47  ? 1850 GLN A CB    1 
ATOM   4283  C CG    . GLN A 1 1850 ? 222.326 189.228 156.025 1.00 47.47  ? 1850 GLN A CG    1 
ATOM   4284  C CD    . GLN A 1 1850 ? 223.123 188.042 155.523 1.00 47.47  ? 1850 GLN A CD    1 
ATOM   4285  O OE1   . GLN A 1 1850 ? 224.295 187.881 155.862 1.00 47.47  ? 1850 GLN A OE1   1 
ATOM   4286  N NE2   . GLN A 1 1850 ? 222.493 187.206 154.706 1.00 47.47  ? 1850 GLN A NE2   1 
ATOM   4287  N N     . THR A 1 1851 ? 223.265 191.896 154.410 1.00 50.67  ? 1851 THR A N     1 
ATOM   4288  C CA    . THR A 1 1851 ? 222.576 192.754 153.452 1.00 50.67  ? 1851 THR A CA    1 
ATOM   4289  C C     . THR A 1 1851 ? 221.086 192.439 153.385 1.00 50.67  ? 1851 THR A C     1 
ATOM   4290  O O     . THR A 1 1851 ? 220.253 193.351 153.420 1.00 50.67  ? 1851 THR A O     1 
ATOM   4291  C CB    . THR A 1 1851 ? 223.211 192.612 152.069 1.00 50.67  ? 1851 THR A CB    1 
ATOM   4292  O OG1   . THR A 1 1851 ? 223.060 191.264 151.608 1.00 50.67  ? 1851 THR A OG1   1 
ATOM   4293  C CG2   . THR A 1 1851 ? 224.690 192.958 152.126 1.00 50.67  ? 1851 THR A CG2   1 
ATOM   4294  N N     . ASP A 1 1852 ? 220.731 191.160 153.288 1.00 45.63  ? 1852 ASP A N     1 
ATOM   4295  C CA    . ASP A 1 1852 ? 219.332 190.783 153.137 1.00 45.63  ? 1852 ASP A CA    1 
ATOM   4296  C C     . ASP A 1 1852 ? 218.560 191.060 154.420 1.00 45.63  ? 1852 ASP A C     1 
ATOM   4297  O O     . ASP A 1 1852 ? 219.016 190.740 155.520 1.00 45.63  ? 1852 ASP A O     1 
ATOM   4298  C CB    . ASP A 1 1852 ? 219.215 189.308 152.761 1.00 45.63  ? 1852 ASP A CB    1 
ATOM   4299  C CG    . ASP A 1 1852 ? 218.091 189.047 151.780 1.00 45.63  ? 1852 ASP A CG    1 
ATOM   4300  O OD1   . ASP A 1 1852 ? 217.153 189.869 151.719 1.00 45.63  ? 1852 ASP A OD1   1 
ATOM   4301  O OD2   . ASP A 1 1852 ? 218.143 188.021 151.070 1.00 45.63  ? 1852 ASP A OD2   1 
ATOM   4302  N N     . VAL A 1 1853 ? 217.375 191.656 154.270 1.00 35.70  ? 1853 VAL A N     1 
ATOM   4303  C CA    . VAL A 1 1853 ? 216.591 192.060 155.433 1.00 35.70  ? 1853 VAL A CA    1 
ATOM   4304  C C     . VAL A 1 1853 ? 216.056 190.844 156.179 1.00 35.70  ? 1853 VAL A C     1 
ATOM   4305  O O     . VAL A 1 1853 ? 216.029 190.823 157.415 1.00 35.70  ? 1853 VAL A O     1 
ATOM   4306  C CB    . VAL A 1 1853 ? 215.459 193.013 155.009 1.00 35.70  ? 1853 VAL A CB    1 
ATOM   4307  C CG1   . VAL A 1 1853 ? 216.021 194.389 154.701 1.00 35.70  ? 1853 VAL A CG1   1 
ATOM   4308  C CG2   . VAL A 1 1853 ? 214.722 192.460 153.802 1.00 35.70  ? 1853 VAL A CG2   1 
ATOM   4309  N N     . LEU A 1 1854 ? 215.619 189.815 155.451 1.00 33.93  ? 1854 LEU A N     1 
ATOM   4310  C CA    . LEU A 1 1854 ? 215.076 188.630 156.103 1.00 33.93  ? 1854 LEU A CA    1 
ATOM   4311  C C     . LEU A 1 1854 ? 216.140 187.837 156.851 1.00 33.93  ? 1854 LEU A C     1 
ATOM   4312  O O     . LEU A 1 1854 ? 215.794 187.027 157.717 1.00 33.93  ? 1854 LEU A O     1 
ATOM   4313  C CB    . LEU A 1 1854 ? 214.385 187.725 155.080 1.00 33.93  ? 1854 LEU A CB    1 
ATOM   4314  C CG    . LEU A 1 1854 ? 212.950 188.074 154.671 1.00 33.93  ? 1854 LEU A CG    1 
ATOM   4315  C CD1   . LEU A 1 1854 ? 212.906 189.277 153.742 1.00 33.93  ? 1854 LEU A CD1   1 
ATOM   4316  C CD2   . LEU A 1 1854 ? 212.270 186.875 154.029 1.00 33.93  ? 1854 LEU A CD2   1 
ATOM   4317  N N     . GLN A 1 1855 ? 217.416 188.047 156.542 1.00 35.55  ? 1855 GLN A N     1 
ATOM   4318  C CA    . GLN A 1 1855 ? 218.503 187.317 157.177 1.00 35.55  ? 1855 GLN A CA    1 
ATOM   4319  C C     . GLN A 1 1855 ? 219.150 188.080 158.327 1.00 35.55  ? 1855 GLN A C     1 
ATOM   4320  O O     . GLN A 1 1855 ? 220.083 187.560 158.946 1.00 35.55  ? 1855 GLN A O     1 
ATOM   4321  C CB    . GLN A 1 1855 ? 219.569 186.958 156.138 1.00 35.55  ? 1855 GLN A CB    1 
ATOM   4322  C CG    . GLN A 1 1855 ? 219.095 186.017 155.043 1.00 35.55  ? 1855 GLN A CG    1 
ATOM   4323  C CD    . GLN A 1 1855 ? 218.751 184.637 155.564 1.00 35.55  ? 1855 GLN A CD    1 
ATOM   4324  O OE1   . GLN A 1 1855 ? 219.430 184.106 156.443 1.00 35.55  ? 1855 GLN A OE1   1 
ATOM   4325  N NE2   . GLN A 1 1855 ? 217.693 184.047 155.022 1.00 35.55  ? 1855 GLN A NE2   1 
ATOM   4326  N N     . GLN A 1 1856 ? 218.689 189.297 158.626 1.00 31.93  ? 1856 GLN A N     1 
ATOM   4327  C CA    . GLN A 1 1856 ? 219.325 190.088 159.675 1.00 31.93  ? 1856 GLN A CA    1 
ATOM   4328  C C     . GLN A 1 1856 ? 219.090 189.479 161.052 1.00 31.93  ? 1856 GLN A C     1 
ATOM   4329  O O     . GLN A 1 1856 ? 220.031 189.316 161.837 1.00 31.93  ? 1856 GLN A O     1 
ATOM   4330  C CB    . GLN A 1 1856 ? 218.815 191.529 159.639 1.00 31.93  ? 1856 GLN A CB    1 
ATOM   4331  C CG    . GLN A 1 1856 ? 218.851 192.172 158.269 1.00 31.93  ? 1856 GLN A CG    1 
ATOM   4332  C CD    . GLN A 1 1856 ? 219.119 193.661 158.330 1.00 31.93  ? 1856 GLN A CD    1 
ATOM   4333  O OE1   . GLN A 1 1856 ? 219.789 194.146 159.241 1.00 31.93  ? 1856 GLN A OE1   1 
ATOM   4334  N NE2   . GLN A 1 1856 ? 218.595 194.396 157.356 1.00 31.93  ? 1856 GLN A NE2   1 
ATOM   4335  N N     . LEU A 1 1857 ? 217.845 189.136 161.362 1.00 17.94  ? 1857 LEU A N     1 
ATOM   4336  C CA    . LEU A 1 1857 ? 217.469 188.649 162.681 1.00 17.94  ? 1857 LEU A CA    1 
ATOM   4337  C C     . LEU A 1 1857 ? 217.154 187.163 162.610 1.00 17.94  ? 1857 LEU A C     1 
ATOM   4338  O O     . LEU A 1 1857 ? 216.392 186.726 161.742 1.00 17.94  ? 1857 LEU A O     1 
ATOM   4339  C CB    . LEU A 1 1857 ? 216.265 189.418 163.227 1.00 17.94  ? 1857 LEU A CB    1 
ATOM   4340  C CG    . LEU A 1 1857 ? 215.682 188.893 164.538 1.00 17.94  ? 1857 LEU A CG    1 
ATOM   4341  C CD1   . LEU A 1 1857 ? 216.726 188.936 165.633 1.00 17.94  ? 1857 LEU A CD1   1 
ATOM   4342  C CD2   . LEU A 1 1857 ? 214.464 189.696 164.937 1.00 17.94  ? 1857 LEU A CD2   1 
ATOM   4343  N N     . SER A 1 1858 ? 217.741 186.394 163.522 1.00 14.04  ? 1858 SER A N     1 
ATOM   4344  C CA    . SER A 1 1858 ? 217.514 184.960 163.617 1.00 14.04  ? 1858 SER A CA    1 
ATOM   4345  C C     . SER A 1 1858 ? 216.942 184.636 164.988 1.00 14.04  ? 1858 SER A C     1 
ATOM   4346  O O     . SER A 1 1858 ? 217.503 185.043 166.010 1.00 14.04  ? 1858 SER A O     1 
ATOM   4347  C CB    . SER A 1 1858 ? 218.810 184.181 163.386 1.00 14.04  ? 1858 SER A CB    1 
ATOM   4348  O OG    . SER A 1 1858 ? 218.703 182.861 163.886 1.00 14.04  ? 1858 SER A OG    1 
ATOM   4349  N N     . ILE A 1 1859 ? 215.830 183.908 165.007 1.00 11.61  ? 1859 ILE A N     1 
ATOM   4350  C CA    . ILE A 1 1859 ? 215.166 183.497 166.237 1.00 11.61  ? 1859 ILE A CA    1 
ATOM   4351  C C     . ILE A 1 1859 ? 215.364 181.997 166.388 1.00 11.61  ? 1859 ILE A C     1 
ATOM   4352  O O     . ILE A 1 1859 ? 214.992 181.223 165.498 1.00 11.61  ? 1859 ILE A O     1 
ATOM   4353  C CB    . ILE A 1 1859 ? 213.674 183.858 166.222 1.00 11.61  ? 1859 ILE A CB    1 
ATOM   4354  C CG1   . ILE A 1 1859 ? 213.496 185.360 166.008 1.00 11.61  ? 1859 ILE A CG1   1 
ATOM   4355  C CG2   . ILE A 1 1859 ? 213.008 183.415 167.512 1.00 11.61  ? 1859 ILE A CG2   1 
ATOM   4356  C CD1   . ILE A 1 1859 ? 212.059 185.780 165.849 1.00 11.61  ? 1859 ILE A CD1   1 
ATOM   4357  N N     . GLN A 1 1860 ? 215.946 181.584 167.510 1.00 13.17  ? 1860 GLN A N     1 
ATOM   4358  C CA    . GLN A 1 1860 ? 216.309 180.192 167.733 1.00 13.17  ? 1860 GLN A CA    1 
ATOM   4359  C C     . GLN A 1 1860 ? 215.684 179.689 169.025 1.00 13.17  ? 1860 GLN A C     1 
ATOM   4360  O O     . GLN A 1 1860 ? 215.749 180.366 170.056 1.00 13.17  ? 1860 GLN A O     1 
ATOM   4361  C CB    . GLN A 1 1860 ? 217.828 180.024 167.785 1.00 13.17  ? 1860 GLN A CB    1 
ATOM   4362  C CG    . GLN A 1 1860 ? 218.564 180.720 166.658 1.00 13.17  ? 1860 GLN A CG    1 
ATOM   4363  C CD    . GLN A 1 1860 ? 220.043 180.407 166.652 1.00 13.17  ? 1860 GLN A CD    1 
ATOM   4364  O OE1   . GLN A 1 1860 ? 220.545 179.714 167.535 1.00 13.17  ? 1860 GLN A OE1   1 
ATOM   4365  N NE2   . GLN A 1 1860 ? 220.751 180.916 165.652 1.00 13.17  ? 1860 GLN A NE2   1 
ATOM   4366  N N     . MET A 1 1861 ? 215.081 178.506 168.962 1.00 13.07  ? 1861 MET A N     1 
ATOM   4367  C CA    . MET A 1 1861 ? 214.588 177.800 170.138 1.00 13.07  ? 1861 MET A CA    1 
ATOM   4368  C C     . MET A 1 1861 ? 215.009 176.345 170.021 1.00 13.07  ? 1861 MET A C     1 
ATOM   4369  O O     . MET A 1 1861 ? 214.594 175.653 169.085 1.00 13.07  ? 1861 MET A O     1 
ATOM   4370  C CB    . MET A 1 1861 ? 213.068 177.915 170.265 1.00 13.07  ? 1861 MET A CB    1 
ATOM   4371  C CG    . MET A 1 1861 ? 212.574 177.875 171.699 1.00 13.07  ? 1861 MET A CG    1 
ATOM   4372  S SD    . MET A 1 1861 ? 210.795 178.107 171.843 1.00 13.07  ? 1861 MET A SD    1 
ATOM   4373  C CE    . MET A 1 1861 ? 210.596 178.048 173.620 1.00 13.07  ? 1861 MET A CE    1 
ATOM   4374  N N     . ALA A 1 1862 ? 215.829 175.886 170.968 1.00 12.83  ? 1862 ALA A N     1 
ATOM   4375  C CA    . ALA A 1 1862 ? 216.413 174.541 170.956 1.00 12.83  ? 1862 ALA A CA    1 
ATOM   4376  C C     . ALA A 1 1862 ? 217.210 174.396 169.665 1.00 12.83  ? 1862 ALA A C     1 
ATOM   4377  O O     . ALA A 1 1862 ? 218.115 175.214 169.428 1.00 12.83  ? 1862 ALA A O     1 
ATOM   4378  C CB    . ALA A 1 1862 ? 215.310 173.505 171.183 1.00 12.83  ? 1862 ALA A CB    1 
ATOM   4379  N N     . ASN A 1 1863 ? 216.929 173.410 168.816 1.00 12.95  ? 1863 ASN A N     1 
ATOM   4380  C CA    . ASN A 1 1863 ? 217.676 173.210 167.583 1.00 12.95  ? 1863 ASN A CA    1 
ATOM   4381  C C     . ASN A 1 1863 ? 217.001 173.829 166.368 1.00 12.95  ? 1863 ASN A C     1 
ATOM   4382  O O     . ASN A 1 1863 ? 217.486 173.646 165.248 1.00 12.95  ? 1863 ASN A O     1 
ATOM   4383  C CB    . ASN A 1 1863 ? 217.901 171.714 167.340 1.00 12.95  ? 1863 ASN A CB    1 
ATOM   4384  C CG    . ASN A 1 1863 ? 216.629 170.990 166.954 1.00 12.95  ? 1863 ASN A CG    1 
ATOM   4385  O OD1   . ASN A 1 1863 ? 215.733 170.803 167.776 1.00 12.95  ? 1863 ASN A OD1   1 
ATOM   4386  N ND2   . ASN A 1 1863 ? 216.543 170.577 165.696 1.00 12.95  ? 1863 ASN A ND2   1 
ATOM   4387  N N     . ALA A 1 1864 ? 215.902 174.552 166.556 1.00 12.25  ? 1864 ALA A N     1 
ATOM   4388  C CA    . ALA A 1 1864 ? 215.168 175.165 165.458 1.00 12.25  ? 1864 ALA A CA    1 
ATOM   4389  C C     . ALA A 1 1864 ? 215.587 176.620 165.309 1.00 12.25  ? 1864 ALA A C     1 
ATOM   4390  O O     . ALA A 1 1864 ? 215.578 177.375 166.286 1.00 12.25  ? 1864 ALA A O     1 
ATOM   4391  C CB    . ALA A 1 1864 ? 213.660 175.071 165.690 1.00 12.25  ? 1864 ALA A CB    1 
ATOM   4392  N N     . LYS A 1 1865 ? 215.947 177.009 164.090 1.00 10.57  ? 1865 LYS A N     1 
ATOM   4393  C CA    . LYS A 1 1865 ? 216.362 178.370 163.783 1.00 10.57  ? 1865 LYS A CA    1 
ATOM   4394  C C     . LYS A 1 1865 ? 215.401 178.969 162.767 1.00 10.57  ? 1865 LYS A C     1 
ATOM   4395  O O     . LYS A 1 1865 ? 215.108 178.345 161.742 1.00 10.57  ? 1865 LYS A O     1 
ATOM   4396  C CB    . LYS A 1 1865 ? 217.793 178.403 163.243 1.00 10.57  ? 1865 LYS A CB    1 
ATOM   4397  C CG    . LYS A 1 1865 ? 218.837 177.928 164.239 1.00 10.57  ? 1865 LYS A CG    1 
ATOM   4398  C CD    . LYS A 1 1865 ? 219.933 177.129 163.557 1.00 10.57  ? 1865 LYS A CD    1 
ATOM   4399  C CE    . LYS A 1 1865 ? 221.131 176.947 164.474 1.00 10.57  ? 1865 LYS A CE    1 
ATOM   4400  N NZ    . LYS A 1 1865 ? 221.931 178.195 164.601 1.00 10.57  ? 1865 LYS A NZ    1 
ATOM   4401  N N     . PHE A 1 1866 ? 214.917 180.175 163.053 1.00 10.98  ? 1866 PHE A N     1 
ATOM   4402  C CA    . PHE A 1 1866 ? 213.968 180.862 162.193 1.00 10.98  ? 1866 PHE A CA    1 
ATOM   4403  C C     . PHE A 1 1866 ? 214.487 182.253 161.863 1.00 10.98  ? 1866 PHE A C     1 
ATOM   4404  O O     . PHE A 1 1866 ? 215.223 182.867 162.638 1.00 10.98  ? 1866 PHE A O     1 
ATOM   4405  C CB    . PHE A 1 1866 ? 212.587 180.974 162.847 1.00 10.98  ? 1866 PHE A CB    1 
ATOM   4406  C CG    . PHE A 1 1866 ? 211.995 179.658 163.242 1.00 10.98  ? 1866 PHE A CG    1 
ATOM   4407  C CD1   . PHE A 1 1866 ? 211.328 178.878 162.315 1.00 10.98  ? 1866 PHE A CD1   1 
ATOM   4408  C CD2   . PHE A 1 1866 ? 212.102 179.199 164.541 1.00 10.98  ? 1866 PHE A CD2   1 
ATOM   4409  C CE1   . PHE A 1 1866 ? 210.781 177.667 162.675 1.00 10.98  ? 1866 PHE A CE1   1 
ATOM   4410  C CE2   . PHE A 1 1866 ? 211.557 177.989 164.907 1.00 10.98  ? 1866 PHE A CE2   1 
ATOM   4411  C CZ    . PHE A 1 1866 ? 210.895 177.221 163.973 1.00 10.98  ? 1866 PHE A CZ    1 
ATOM   4412  N N     . ASN A 1 1867 ? 214.089 182.745 160.695 1.00 12.73  ? 1867 ASN A N     1 
ATOM   4413  C CA    . ASN A 1 1867 ? 214.394 184.102 160.268 1.00 12.73  ? 1867 ASN A CA    1 
ATOM   4414  C C     . ASN A 1 1867 ? 213.156 184.967 160.448 1.00 12.73  ? 1867 ASN A C     1 
ATOM   4415  O O     . ASN A 1 1867 ? 212.052 184.565 160.066 1.00 12.73  ? 1867 ASN A O     1 
ATOM   4416  C CB    . ASN A 1 1867 ? 214.855 184.131 158.810 1.00 12.73  ? 1867 ASN A CB    1 
ATOM   4417  C CG    . ASN A 1 1867 ? 216.235 183.538 158.623 1.00 12.73  ? 1867 ASN A CG    1 
ATOM   4418  O OD1   . ASN A 1 1867 ? 217.138 183.771 159.424 1.00 12.73  ? 1867 ASN A OD1   1 
ATOM   4419  N ND2   . ASN A 1 1867 ? 216.406 182.766 157.557 1.00 12.73  ? 1867 ASN A ND2   1 
ATOM   4420  N N     . TYR A 1 1868 ? 213.339 186.144 161.037 1.00 11.48  ? 1868 TYR A N     1 
ATOM   4421  C CA    . TYR A 1 1868 ? 212.221 187.046 161.279 1.00 11.48  ? 1868 TYR A CA    1 
ATOM   4422  C C     . TYR A 1 1868 ? 211.649 187.520 159.949 1.00 11.48  ? 1868 TYR A C     1 
ATOM   4423  O O     . TYR A 1 1868 ? 212.388 187.995 159.082 1.00 11.48  ? 1868 TYR A O     1 
ATOM   4424  C CB    . TYR A 1 1868 ? 212.680 188.230 162.125 1.00 11.48  ? 1868 TYR A CB    1 
ATOM   4425  C CG    . TYR A 1 1868 ? 211.556 189.020 162.750 1.00 11.48  ? 1868 TYR A CG    1 
ATOM   4426  C CD1   . TYR A 1 1868 ? 210.754 188.464 163.734 1.00 11.48  ? 1868 TYR A CD1   1 
ATOM   4427  C CD2   . TYR A 1 1868 ? 211.301 190.327 162.362 1.00 11.48  ? 1868 TYR A CD2   1 
ATOM   4428  C CE1   . TYR A 1 1868 ? 209.728 189.184 164.309 1.00 11.48  ? 1868 TYR A CE1   1 
ATOM   4429  C CE2   . TYR A 1 1868 ? 210.276 191.054 162.931 1.00 11.48  ? 1868 TYR A CE2   1 
ATOM   4430  C CZ    . TYR A 1 1868 ? 209.494 190.478 163.903 1.00 11.48  ? 1868 TYR A CZ    1 
ATOM   4431  O OH    . TYR A 1 1868 ? 208.472 191.200 164.473 1.00 11.48  ? 1868 TYR A OH    1 
ATOM   4432  N N     . GLY A 1 1869 ? 210.333 187.390 159.787 1.00 11.46  ? 1869 GLY A N     1 
ATOM   4433  C CA    . GLY A 1 1869 ? 209.691 187.791 158.548 1.00 11.46  ? 1869 GLY A CA    1 
ATOM   4434  C C     . GLY A 1 1869 ? 209.502 189.283 158.391 1.00 11.46  ? 1869 GLY A C     1 
ATOM   4435  O O     . GLY A 1 1869 ? 209.235 189.740 157.274 1.00 11.46  ? 1869 GLY A O     1 
ATOM   4436  N N     . PHE A 1 1870 ? 209.623 190.044 159.478 1.00 12.24  ? 1870 PHE A N     1 
ATOM   4437  C CA    . PHE A 1 1870 ? 209.536 191.502 159.472 1.00 12.24  ? 1870 PHE A CA    1 
ATOM   4438  C C     . PHE A 1 1870 ? 208.194 192.010 158.962 1.00 12.24  ? 1870 PHE A C     1 
ATOM   4439  O O     . PHE A 1 1870 ? 208.092 193.156 158.515 1.00 12.24  ? 1870 PHE A O     1 
ATOM   4440  C CB    . PHE A 1 1870 ? 210.680 192.121 158.663 1.00 12.24  ? 1870 PHE A CB    1 
ATOM   4441  C CG    . PHE A 1 1870 ? 211.956 192.252 159.435 1.00 12.24  ? 1870 PHE A CG    1 
ATOM   4442  C CD1   . PHE A 1 1870 ? 212.075 193.190 160.442 1.00 12.24  ? 1870 PHE A CD1   1 
ATOM   4443  C CD2   . PHE A 1 1870 ? 213.034 191.432 159.160 1.00 12.24  ? 1870 PHE A CD2   1 
ATOM   4444  C CE1   . PHE A 1 1870 ? 213.245 193.311 161.156 1.00 12.24  ? 1870 PHE A CE1   1 
ATOM   4445  C CE2   . PHE A 1 1870 ? 214.207 191.549 159.872 1.00 12.24  ? 1870 PHE A CE2   1 
ATOM   4446  C CZ    . PHE A 1 1870 ? 214.313 192.490 160.871 1.00 12.24  ? 1870 PHE A CZ    1 
ATOM   4447  N N     . GLU A 1 1871 ? 207.158 191.181 159.020 1.00 16.96  ? 1871 GLU A N     1 
ATOM   4448  C CA    . GLU A 1 1871 ? 205.821 191.639 158.676 1.00 16.96  ? 1871 GLU A CA    1 
ATOM   4449  C C     . GLU A 1 1871 ? 205.334 192.646 159.708 1.00 16.96  ? 1871 GLU A C     1 
ATOM   4450  O O     . GLU A 1 1871 ? 205.499 192.451 160.914 1.00 16.96  ? 1871 GLU A O     1 
ATOM   4451  C CB    . GLU A 1 1871 ? 204.858 190.456 158.602 1.00 16.96  ? 1871 GLU A CB    1 
ATOM   4452  C CG    . GLU A 1 1871 ? 203.461 190.819 158.139 1.00 16.96  ? 1871 GLU A CG    1 
ATOM   4453  C CD    . GLU A 1 1871 ? 203.242 190.529 156.670 1.00 16.96  ? 1871 GLU A CD    1 
ATOM   4454  O OE1   . GLU A 1 1871 ? 204.238 190.288 155.957 1.00 16.96  ? 1871 GLU A OE1   1 
ATOM   4455  O OE2   . GLU A 1 1871 ? 202.075 190.540 156.228 1.00 16.96  ? 1871 GLU A OE2   1 
ATOM   4456  N N     . TYR A 1 1872 ? 204.734 193.733 159.231 1.00 18.15  ? 1872 TYR A N     1 
ATOM   4457  C CA    . TYR A 1 1872 ? 204.186 194.737 160.131 1.00 18.15  ? 1872 TYR A CA    1 
ATOM   4458  C C     . TYR A 1 1872 ? 202.949 194.170 160.813 1.00 18.15  ? 1872 TYR A C     1 
ATOM   4459  O O     . TYR A 1 1872 ? 202.039 193.669 160.146 1.00 18.15  ? 1872 TYR A O     1 
ATOM   4460  C CB    . TYR A 1 1872 ? 203.844 196.021 159.381 1.00 18.15  ? 1872 TYR A CB    1 
ATOM   4461  C CG    . TYR A 1 1872 ? 203.350 197.120 160.293 1.00 18.15  ? 1872 TYR A CG    1 
ATOM   4462  C CD1   . TYR A 1 1872 ? 204.106 197.535 161.379 1.00 18.15  ? 1872 TYR A CD1   1 
ATOM   4463  C CD2   . TYR A 1 1872 ? 202.126 197.734 160.075 1.00 18.15  ? 1872 TYR A CD2   1 
ATOM   4464  C CE1   . TYR A 1 1872 ? 203.661 198.533 162.219 1.00 18.15  ? 1872 TYR A CE1   1 
ATOM   4465  C CE2   . TYR A 1 1872 ? 201.674 198.735 160.909 1.00 18.15  ? 1872 TYR A CE2   1 
ATOM   4466  C CZ    . TYR A 1 1872 ? 202.446 199.130 161.979 1.00 18.15  ? 1872 TYR A CZ    1 
ATOM   4467  O OH    . TYR A 1 1872 ? 202.000 200.126 162.815 1.00 18.15  ? 1872 TYR A OH    1 
ATOM   4468  N N     . LEU A 1 1873 ? 202.918 194.250 162.141 1.00 16.26  ? 1873 LEU A N     1 
ATOM   4469  C CA    . LEU A 1 1873 ? 201.837 193.677 162.926 1.00 16.26  ? 1873 LEU A CA    1 
ATOM   4470  C C     . LEU A 1 1873 ? 201.001 194.723 163.647 1.00 16.26  ? 1873 LEU A C     1 
ATOM   4471  O O     . LEU A 1 1873 ? 199.978 194.370 164.242 1.00 16.26  ? 1873 LEU A O     1 
ATOM   4472  C CB    . LEU A 1 1873 ? 202.405 192.687 163.948 1.00 16.26  ? 1873 LEU A CB    1 
ATOM   4473  C CG    . LEU A 1 1873 ? 203.123 191.481 163.343 1.00 16.26  ? 1873 LEU A CG    1 
ATOM   4474  C CD1   . LEU A 1 1873 ? 203.842 190.697 164.422 1.00 16.26  ? 1873 LEU A CD1   1 
ATOM   4475  C CD2   . LEU A 1 1873 ? 202.145 190.593 162.594 1.00 16.26  ? 1873 LEU A CD2   1 
ATOM   4476  N N     . GLY A 1 1874 ? 201.398 195.992 163.602 1.00 17.04  ? 1874 GLY A N     1 
ATOM   4477  C CA    . GLY A 1 1874 ? 200.676 197.001 164.354 1.00 17.04  ? 1874 GLY A CA    1 
ATOM   4478  C C     . GLY A 1 1874 ? 200.859 196.788 165.843 1.00 17.04  ? 1874 GLY A C     1 
ATOM   4479  O O     . GLY A 1 1874 ? 201.956 196.483 166.324 1.00 17.04  ? 1874 GLY A O     1 
ATOM   4480  N N     . VAL A 1 1875 ? 199.770 196.949 166.590 1.00 18.21  ? 1875 VAL A N     1 
ATOM   4481  C CA    . VAL A 1 1875 ? 199.799 196.721 168.029 1.00 18.21  ? 1875 VAL A CA    1 
ATOM   4482  C C     . VAL A 1 1875 ? 198.888 195.548 168.361 1.00 18.21  ? 1875 VAL A C     1 
ATOM   4483  O O     . VAL A 1 1875 ? 197.676 195.715 168.538 1.00 18.21  ? 1875 VAL A O     1 
ATOM   4484  C CB    . VAL A 1 1875 ? 199.389 197.986 168.803 1.00 18.21  ? 1875 VAL A CB    1 
ATOM   4485  C CG1   . VAL A 1 1875 ? 199.459 197.740 170.300 1.00 18.21  ? 1875 VAL A CG1   1 
ATOM   4486  C CG2   . VAL A 1 1875 ? 200.280 199.145 168.411 1.00 18.21  ? 1875 VAL A CG2   1 
ATOM   4487  N N     . GLN A 1 1876 ? 199.465 194.355 168.440 1.00 18.38  ? 1876 GLN A N     1 
ATOM   4488  C CA    . GLN A 1 1876 ? 198.732 193.143 168.767 1.00 18.38  ? 1876 GLN A CA    1 
ATOM   4489  C C     . GLN A 1 1876 ? 198.819 192.859 170.261 1.00 18.38  ? 1876 GLN A C     1 
ATOM   4490  O O     . GLN A 1 1876 ? 199.775 193.246 170.937 1.00 18.38  ? 1876 GLN A O     1 
ATOM   4491  C CB    . GLN A 1 1876 ? 199.274 191.949 167.977 1.00 18.38  ? 1876 GLN A CB    1 
ATOM   4492  C CG    . GLN A 1 1876 ? 199.304 192.153 166.474 1.00 18.38  ? 1876 GLN A CG    1 
ATOM   4493  C CD    . GLN A 1 1876 ? 197.968 191.868 165.819 1.00 18.38  ? 1876 GLN A CD    1 
ATOM   4494  O OE1   . GLN A 1 1876 ? 197.003 191.497 166.486 1.00 18.38  ? 1876 GLN A OE1   1 
ATOM   4495  N NE2   . GLN A 1 1876 ? 197.905 192.039 164.504 1.00 18.38  ? 1876 GLN A NE2   1 
ATOM   4496  N N     . ASP A 1 1877 ? 197.800 192.176 170.771 1.00 16.54  ? 1877 ASP A N     1 
ATOM   4497  C CA    . ASP A 1 1877 ? 197.801 191.780 172.171 1.00 16.54  ? 1877 ASP A CA    1 
ATOM   4498  C C     . ASP A 1 1877 ? 198.865 190.718 172.414 1.00 16.54  ? 1877 ASP A C     1 
ATOM   4499  O O     . ASP A 1 1877 ? 198.933 189.710 171.706 1.00 16.54  ? 1877 ASP A O     1 
ATOM   4500  C CB    . ASP A 1 1877 ? 196.426 191.252 172.576 1.00 16.54  ? 1877 ASP A CB    1 
ATOM   4501  C CG    . ASP A 1 1877 ? 195.340 192.300 172.445 1.00 16.54  ? 1877 ASP A CG    1 
ATOM   4502  O OD1   . ASP A 1 1877 ? 195.660 193.442 172.052 1.00 16.54  ? 1877 ASP A OD1   1 
ATOM   4503  O OD2   . ASP A 1 1877 ? 194.167 191.984 172.734 1.00 16.54  ? 1877 ASP A OD2   1 
ATOM   4504  N N     . LYS A 1 1878 ? 199.697 190.947 173.425 1.00 16.24  ? 1878 LYS A N     1 
ATOM   4505  C CA    . LYS A 1 1878 ? 200.799 190.051 173.753 1.00 16.24  ? 1878 LYS A CA    1 
ATOM   4506  C C     . LYS A 1 1878 ? 200.364 189.139 174.891 1.00 16.24  ? 1878 LYS A C     1 
ATOM   4507  O O     . LYS A 1 1878 ? 199.971 189.614 175.961 1.00 16.24  ? 1878 LYS A O     1 
ATOM   4508  C CB    . LYS A 1 1878 ? 202.052 190.835 174.132 1.00 16.24  ? 1878 LYS A CB    1 
ATOM   4509  C CG    . LYS A 1 1878 ? 203.334 190.040 173.980 1.00 16.24  ? 1878 LYS A CG    1 
ATOM   4510  C CD    . LYS A 1 1878 ? 204.558 190.932 174.024 1.00 16.24  ? 1878 LYS A CD    1 
ATOM   4511  C CE    . LYS A 1 1878 ? 205.826 190.102 174.106 1.00 16.24  ? 1878 LYS A CE    1 
ATOM   4512  N NZ    . LYS A 1 1878 ? 205.639 188.883 174.938 1.00 16.24  ? 1878 LYS A NZ    1 
ATOM   4513  N N     . LEU A 1 1879 ? 200.433 187.832 174.658 1.00 21.75  ? 1879 LEU A N     1 
ATOM   4514  C CA    . LEU A 1 1879 ? 200.073 186.866 175.685 1.00 21.75  ? 1879 LEU A CA    1 
ATOM   4515  C C     . LEU A 1 1879 ? 201.126 186.842 176.783 1.00 21.75  ? 1879 LEU A C     1 
ATOM   4516  O O     . LEU A 1 1879 ? 202.317 187.038 176.522 1.00 21.75  ? 1879 LEU A O     1 
ATOM   4517  C CB    . LEU A 1 1879 ? 199.923 185.473 175.080 1.00 21.75  ? 1879 LEU A CB    1 
ATOM   4518  C CG    . LEU A 1 1879 ? 199.031 185.306 173.853 1.00 21.75  ? 1879 LEU A CG    1 
ATOM   4519  C CD1   . LEU A 1 1879 ? 198.762 183.834 173.631 1.00 21.75  ? 1879 LEU A CD1   1 
ATOM   4520  C CD2   . LEU A 1 1879 ? 197.728 186.068 174.019 1.00 21.75  ? 1879 LEU A CD2   1 
ATOM   4521  N N     . VAL A 1 1880 ? 200.685 186.604 178.018 1.00 16.27  ? 1880 VAL A N     1 
ATOM   4522  C CA    . VAL A 1 1880 ? 201.627 186.367 179.101 1.00 16.27  ? 1880 VAL A CA    1 
ATOM   4523  C C     . VAL A 1 1880 ? 202.277 185.011 178.890 1.00 16.27  ? 1880 VAL A C     1 
ATOM   4524  O O     . VAL A 1 1880 ? 201.592 183.992 178.742 1.00 16.27  ? 1880 VAL A O     1 
ATOM   4525  C CB    . VAL A 1 1880 ? 200.917 186.446 180.458 1.00 16.27  ? 1880 VAL A CB    1 
ATOM   4526  C CG1   . VAL A 1 1880 ? 201.877 186.085 181.572 1.00 16.27  ? 1880 VAL A CG1   1 
ATOM   4527  C CG2   . VAL A 1 1880 ? 200.338 187.833 180.670 1.00 16.27  ? 1880 VAL A CG2   1 
ATOM   4528  N N     . GLN A 1 1881 ? 203.609 184.988 178.875 1.00 15.29  ? 1881 GLN A N     1 
ATOM   4529  C CA    . GLN A 1 1881 ? 204.347 183.777 178.522 1.00 15.29  ? 1881 GLN A CA    1 
ATOM   4530  C C     . GLN A 1 1881 ? 204.415 182.861 179.741 1.00 15.29  ? 1881 GLN A C     1 
ATOM   4531  O O     . GLN A 1 1881 ? 205.406 182.801 180.473 1.00 15.29  ? 1881 GLN A O     1 
ATOM   4532  C CB    . GLN A 1 1881 ? 205.731 184.126 177.995 1.00 15.29  ? 1881 GLN A CB    1 
ATOM   4533  C CG    . GLN A 1 1881 ? 206.340 183.037 177.139 1.00 15.29  ? 1881 GLN A CG    1 
ATOM   4534  C CD    . GLN A 1 1881 ? 207.451 183.546 176.247 1.00 15.29  ? 1881 GLN A CD    1 
ATOM   4535  O OE1   . GLN A 1 1881 ? 207.718 184.746 176.192 1.00 15.29  ? 1881 GLN A OE1   1 
ATOM   4536  N NE2   . GLN A 1 1881 ? 208.109 182.633 175.543 1.00 15.29  ? 1881 GLN A NE2   1 
ATOM   4537  N N     . THR A 1 1882 ? 203.325 182.133 179.953 1.00 14.85  ? 1882 THR A N     1 
ATOM   4538  C CA    . THR A 1 1882 ? 203.236 181.137 181.008 1.00 14.85  ? 1882 THR A CA    1 
ATOM   4539  C C     . THR A 1 1882 ? 204.057 179.910 180.634 1.00 14.85  ? 1882 THR A C     1 
ATOM   4540  O O     . THR A 1 1882 ? 204.433 179.731 179.475 1.00 14.85  ? 1882 THR A O     1 
ATOM   4541  C CB    . THR A 1 1882 ? 201.773 180.770 181.241 1.00 14.85  ? 1882 THR A CB    1 
ATOM   4542  O OG1   . THR A 1 1882 ? 201.178 180.363 180.004 1.00 14.85  ? 1882 THR A OG1   1 
ATOM   4543  C CG2   . THR A 1 1882 ? 201.016 181.960 181.787 1.00 14.85  ? 1882 THR A CG2   1 
ATOM   4544  N N     . PRO A 1 1883 ? 204.374 179.046 181.606 1.00 15.93  ? 1883 PRO A N     1 
ATOM   4545  C CA    . PRO A 1 1883 ? 205.098 177.810 181.260 1.00 15.93  ? 1883 PRO A CA    1 
ATOM   4546  C C     . PRO A 1 1883 ? 204.377 176.959 180.230 1.00 15.93  ? 1883 PRO A C     1 
ATOM   4547  O O     . PRO A 1 1883 ? 205.030 176.285 179.424 1.00 15.93  ? 1883 PRO A O     1 
ATOM   4548  C CB    . PRO A 1 1883 ? 205.230 177.090 182.612 1.00 15.93  ? 1883 PRO A CB    1 
ATOM   4549  C CG    . PRO A 1 1883 ? 204.265 177.780 183.529 1.00 15.93  ? 1883 PRO A CG    1 
ATOM   4550  C CD    . PRO A 1 1883 ? 204.228 179.193 183.062 1.00 15.93  ? 1883 PRO A CD    1 
ATOM   4551  N N     . LEU A 1 1884 ? 203.042 176.968 180.232 1.00 14.05  ? 1884 LEU A N     1 
ATOM   4552  C CA    . LEU A 1 1884 ? 202.307 176.289 179.170 1.00 14.05  ? 1884 LEU A CA    1 
ATOM   4553  C C     . LEU A 1 1884 ? 202.594 176.924 177.817 1.00 14.05  ? 1884 LEU A C     1 
ATOM   4554  O O     . LEU A 1 1884 ? 202.727 176.222 176.809 1.00 14.05  ? 1884 LEU A O     1 
ATOM   4555  C CB    . LEU A 1 1884 ? 200.809 176.306 179.467 1.00 14.05  ? 1884 LEU A CB    1 
ATOM   4556  C CG    . LEU A 1 1884 ? 199.922 175.593 178.444 1.00 14.05  ? 1884 LEU A CG    1 
ATOM   4557  C CD1   . LEU A 1 1884 ? 200.335 174.140 178.299 1.00 14.05  ? 1884 LEU A CD1   1 
ATOM   4558  C CD2   . LEU A 1 1884 ? 198.461 175.697 178.840 1.00 14.05  ? 1884 LEU A CD2   1 
ATOM   4559  N N     . THR A 1 1885 ? 202.698 178.254 177.773 1.00 13.01  ? 1885 THR A N     1 
ATOM   4560  C CA    . THR A 1 1885 ? 203.048 178.923 176.525 1.00 13.01  ? 1885 THR A CA    1 
ATOM   4561  C C     . THR A 1 1885 ? 204.474 178.589 176.101 1.00 13.01  ? 1885 THR A C     1 
ATOM   4562  O O     . THR A 1 1885 ? 204.754 178.443 174.907 1.00 13.01  ? 1885 THR A O     1 
ATOM   4563  C CB    . THR A 1 1885 ? 202.864 180.433 176.668 1.00 13.01  ? 1885 THR A CB    1 
ATOM   4564  O OG1   . THR A 1 1885 ? 201.505 180.714 177.024 1.00 13.01  ? 1885 THR A OG1   1 
ATOM   4565  C CG2   . THR A 1 1885 ? 203.185 181.138 175.364 1.00 13.01  ? 1885 THR A CG2   1 
ATOM   4566  N N     . ASP A 1 1886 ? 205.391 178.466 177.063 1.00 15.93  ? 1886 ASP A N     1 
ATOM   4567  C CA    . ASP A 1 1886 ? 206.753 178.047 176.743 1.00 15.93  ? 1886 ASP A CA    1 
ATOM   4568  C C     . ASP A 1 1886 ? 206.767 176.649 176.140 1.00 15.93  ? 1886 ASP A C     1 
ATOM   4569  O O     . ASP A 1 1886 ? 207.460 176.386 175.149 1.00 15.93  ? 1886 ASP A O     1 
ATOM   4570  C CB    . ASP A 1 1886 ? 207.626 178.100 177.997 1.00 15.93  ? 1886 ASP A CB    1 
ATOM   4571  C CG    . ASP A 1 1886 ? 208.142 179.490 178.287 1.00 15.93  ? 1886 ASP A CG    1 
ATOM   4572  O OD1   . ASP A 1 1886 ? 207.958 180.379 177.433 1.00 15.93  ? 1886 ASP A OD1   1 
ATOM   4573  O OD2   . ASP A 1 1886 ? 208.730 179.694 179.370 1.00 15.93  ? 1886 ASP A OD2   1 
ATOM   4574  N N     . ARG A 1 1887 ? 206.003 175.731 176.736 1.00 15.08  ? 1887 ARG A N     1 
ATOM   4575  C CA    . ARG A 1 1887 ? 205.907 174.381 176.193 1.00 15.08  ? 1887 ARG A CA    1 
ATOM   4576  C C     . ARG A 1 1887 ? 205.291 174.394 174.802 1.00 15.08  ? 1887 ARG A C     1 
ATOM   4577  O O     . ARG A 1 1887 ? 205.715 173.641 173.918 1.00 15.08  ? 1887 ARG A O     1 
ATOM   4578  C CB    . ARG A 1 1887 ? 205.091 173.497 177.134 1.00 15.08  ? 1887 ARG A CB    1 
ATOM   4579  C CG    . ARG A 1 1887 ? 204.805 172.114 176.590 1.00 15.08  ? 1887 ARG A CG    1 
ATOM   4580  C CD    . ARG A 1 1887 ? 204.328 171.187 177.688 1.00 15.08  ? 1887 ARG A CD    1 
ATOM   4581  N NE    . ARG A 1 1887 ? 203.754 169.961 177.150 1.00 15.08  ? 1887 ARG A NE    1 
ATOM   4582  C CZ    . ARG A 1 1887 ? 203.308 168.957 177.892 1.00 15.08  ? 1887 ARG A CZ    1 
ATOM   4583  N NH1   . ARG A 1 1887 ? 203.359 168.999 179.213 1.00 15.08  ? 1887 ARG A NH1   1 
ATOM   4584  N NH2   . ARG A 1 1887 ? 202.797 167.886 177.294 1.00 15.08  ? 1887 ARG A NH2   1 
ATOM   4585  N N     . CYS A 1 1888 ? 204.282 175.241 174.593 1.00 12.47  ? 1888 CYS A N     1 
ATOM   4586  C CA    . CYS A 1 1888 ? 203.668 175.352 173.275 1.00 12.47  ? 1888 CYS A CA    1 
ATOM   4587  C C     . CYS A 1 1888 ? 204.672 175.849 172.246 1.00 12.47  ? 1888 CYS A C     1 
ATOM   4588  O O     . CYS A 1 1888 ? 204.755 175.314 171.136 1.00 12.47  ? 1888 CYS A O     1 
ATOM   4589  C CB    . CYS A 1 1888 ? 202.454 176.278 173.335 1.00 12.47  ? 1888 CYS A CB    1 
ATOM   4590  S SG    . CYS A 1 1888 ? 201.643 176.532 171.742 1.00 12.47  ? 1888 CYS A SG    1 
ATOM   4591  N N     . TYR A 1 1889 ? 205.450 176.873 172.599 1.00 12.43  ? 1889 TYR A N     1 
ATOM   4592  C CA    . TYR A 1 1889 ? 206.464 177.379 171.681 1.00 12.43  ? 1889 TYR A CA    1 
ATOM   4593  C C     . TYR A 1 1889 ? 207.484 176.299 171.354 1.00 12.43  ? 1889 TYR A C     1 
ATOM   4594  O O     . TYR A 1 1889 ? 207.839 176.099 170.188 1.00 12.43  ? 1889 TYR A O     1 
ATOM   4595  C CB    . TYR A 1 1889 ? 207.162 178.604 172.272 1.00 12.43  ? 1889 TYR A CB    1 
ATOM   4596  C CG    . TYR A 1 1889 ? 206.340 179.871 172.262 1.00 12.43  ? 1889 TYR A CG    1 
ATOM   4597  C CD1   . TYR A 1 1889 ? 205.018 179.867 171.847 1.00 12.43  ? 1889 TYR A CD1   1 
ATOM   4598  C CD2   . TYR A 1 1889 ? 206.896 181.077 172.661 1.00 12.43  ? 1889 TYR A CD2   1 
ATOM   4599  C CE1   . TYR A 1 1889 ? 204.271 181.025 171.838 1.00 12.43  ? 1889 TYR A CE1   1 
ATOM   4600  C CE2   . TYR A 1 1889 ? 206.158 182.239 172.654 1.00 12.43  ? 1889 TYR A CE2   1 
ATOM   4601  C CZ    . TYR A 1 1889 ? 204.847 182.208 172.242 1.00 12.43  ? 1889 TYR A CZ    1 
ATOM   4602  O OH    . TYR A 1 1889 ? 204.109 183.368 172.235 1.00 12.43  ? 1889 TYR A OH    1 
ATOM   4603  N N     . LEU A 1 1890 ? 207.955 175.579 172.374 1.00 6.16   ? 1890 LEU A N     1 
ATOM   4604  C CA    . LEU A 1 1890 ? 208.950 174.537 172.143 1.00 6.16   ? 1890 LEU A CA    1 
ATOM   4605  C C     . LEU A 1 1890 ? 208.404 173.450 171.227 1.00 6.16   ? 1890 LEU A C     1 
ATOM   4606  O O     . LEU A 1 1890 ? 209.052 173.065 170.247 1.00 6.16   ? 1890 LEU A O     1 
ATOM   4607  C CB    . LEU A 1 1890 ? 209.404 173.939 173.474 1.00 6.16   ? 1890 LEU A CB    1 
ATOM   4608  C CG    . LEU A 1 1890 ? 210.418 172.799 173.383 1.00 6.16   ? 1890 LEU A CG    1 
ATOM   4609  C CD1   . LEU A 1 1890 ? 211.787 173.332 173.010 1.00 6.16   ? 1890 LEU A CD1   1 
ATOM   4610  C CD2   . LEU A 1 1890 ? 210.481 172.034 174.690 1.00 6.16   ? 1890 LEU A CD2   1 
ATOM   4611  N N     . THR A 1 1891 ? 207.200 172.954 171.522 1.00 14.23  ? 1891 THR A N     1 
ATOM   4612  C CA    . THR A 1 1891 ? 206.628 171.874 170.725 1.00 14.23  ? 1891 THR A CA    1 
ATOM   4613  C C     . THR A 1 1891 ? 206.355 172.320 169.295 1.00 14.23  ? 1891 THR A C     1 
ATOM   4614  O O     . THR A 1 1891 ? 206.657 171.592 168.342 1.00 14.23  ? 1891 THR A O     1 
ATOM   4615  C CB    . THR A 1 1891 ? 205.346 171.363 171.379 1.00 14.23  ? 1891 THR A CB    1 
ATOM   4616  O OG1   . THR A 1 1891 ? 205.645 170.851 172.682 1.00 14.23  ? 1891 THR A OG1   1 
ATOM   4617  C CG2   . THR A 1 1891 ? 204.727 170.259 170.543 1.00 14.23  ? 1891 THR A CG2   1 
ATOM   4618  N N     . MET A 1 1892 ? 205.792 173.518 169.120 1.00 13.71  ? 1892 MET A N     1 
ATOM   4619  C CA    . MET A 1 1892 ? 205.472 173.984 167.777 1.00 13.71  ? 1892 MET A CA    1 
ATOM   4620  C C     . MET A 1 1892 ? 206.734 174.250 166.968 1.00 13.71  ? 1892 MET A C     1 
ATOM   4621  O O     . MET A 1 1892 ? 206.779 173.948 165.771 1.00 13.71  ? 1892 MET A O     1 
ATOM   4622  C CB    . MET A 1 1892 ? 204.602 175.237 167.847 1.00 13.71  ? 1892 MET A CB    1 
ATOM   4623  C CG    . MET A 1 1892 ? 203.222 175.021 168.457 1.00 13.71  ? 1892 MET A CG    1 
ATOM   4624  S SD    . MET A 1 1892 ? 202.176 173.864 167.560 1.00 13.71  ? 1892 MET A SD    1 
ATOM   4625  C CE    . MET A 1 1892 ? 202.321 172.401 168.582 1.00 13.71  ? 1892 MET A CE    1 
ATOM   4626  N N     . THR A 1 1893 ? 207.771 174.810 167.596 1.00 10.98  ? 1893 THR A N     1 
ATOM   4627  C CA    . THR A 1 1893 ? 209.023 175.033 166.882 1.00 10.98  ? 1893 THR A CA    1 
ATOM   4628  C C     . THR A 1 1893 ? 209.695 173.716 166.520 1.00 10.98  ? 1893 THR A C     1 
ATOM   4629  O O     . THR A 1 1893 ? 210.289 173.595 165.443 1.00 10.98  ? 1893 THR A O     1 
ATOM   4630  C CB    . THR A 1 1893 ? 209.959 175.903 167.717 1.00 10.98  ? 1893 THR A CB    1 
ATOM   4631  O OG1   . THR A 1 1893 ? 209.985 175.421 169.066 1.00 10.98  ? 1893 THR A OG1   1 
ATOM   4632  C CG2   . THR A 1 1893 ? 209.489 177.347 167.710 1.00 10.98  ? 1893 THR A CG2   1 
ATOM   4633  N N     . GLN A 1 1894 ? 209.620 172.717 167.405 1.00 16.58  ? 1894 GLN A N     1 
ATOM   4634  C CA    . GLN A 1 1894 ? 210.150 171.401 167.067 1.00 16.58  ? 1894 GLN A CA    1 
ATOM   4635  C C     . GLN A 1 1894 ? 209.392 170.791 165.895 1.00 16.58  ? 1894 GLN A C     1 
ATOM   4636  O O     . GLN A 1 1894 ? 209.994 170.172 165.011 1.00 16.58  ? 1894 GLN A O     1 
ATOM   4637  C CB    . GLN A 1 1894 ? 210.089 170.477 168.282 1.00 16.58  ? 1894 GLN A CB    1 
ATOM   4638  C CG    . GLN A 1 1894 ? 211.128 170.780 169.344 1.00 16.58  ? 1894 GLN A CG    1 
ATOM   4639  C CD    . GLN A 1 1894 ? 212.511 170.974 168.766 1.00 16.58  ? 1894 GLN A CD    1 
ATOM   4640  O OE1   . GLN A 1 1894 ? 213.121 172.029 168.930 1.00 16.58  ? 1894 GLN A OE1   1 
ATOM   4641  N NE2   . GLN A 1 1894 ? 213.018 169.952 168.087 1.00 16.58  ? 1894 GLN A NE2   1 
ATOM   4642  N N     . ALA A 1 1895 ? 208.067 170.951 165.877 1.00 15.85  ? 1895 ALA A N     1 
ATOM   4643  C CA    . ALA A 1 1895 ? 207.278 170.439 164.762 1.00 15.85  ? 1895 ALA A CA    1 
ATOM   4644  C C     . ALA A 1 1895 ? 207.630 171.151 163.461 1.00 15.85  ? 1895 ALA A C     1 
ATOM   4645  O O     . ALA A 1 1895 ? 207.734 170.516 162.406 1.00 15.85  ? 1895 ALA A O     1 
ATOM   4646  C CB    . ALA A 1 1895 ? 205.788 170.580 165.066 1.00 15.85  ? 1895 ALA A CB    1 
ATOM   4647  N N     . LEU A 1 1896 ? 207.811 172.472 163.517 1.00 15.00  ? 1896 LEU A N     1 
ATOM   4648  C CA    . LEU A 1 1896 ? 208.155 173.226 162.315 1.00 15.00  ? 1896 LEU A CA    1 
ATOM   4649  C C     . LEU A 1 1896 ? 209.543 172.859 161.806 1.00 15.00  ? 1896 LEU A C     1 
ATOM   4650  O O     . LEU A 1 1896 ? 209.764 172.785 160.593 1.00 15.00  ? 1896 LEU A O     1 
ATOM   4651  C CB    . LEU A 1 1896 ? 208.066 174.725 162.589 1.00 15.00  ? 1896 LEU A CB    1 
ATOM   4652  C CG    . LEU A 1 1896 ? 206.682 175.291 162.904 1.00 15.00  ? 1896 LEU A CG    1 
ATOM   4653  C CD1   . LEU A 1 1896 ? 206.691 176.799 162.779 1.00 15.00  ? 1896 LEU A CD1   1 
ATOM   4654  C CD2   . LEU A 1 1896 ? 205.630 174.682 161.999 1.00 15.00  ? 1896 LEU A CD2   1 
ATOM   4655  N N     . GLU A 1 1897 ? 210.494 172.640 162.718 1.00 18.51  ? 1897 GLU A N     1 
ATOM   4656  C CA    . GLU A 1 1897 ? 211.843 172.270 162.304 1.00 18.51  ? 1897 GLU A CA    1 
ATOM   4657  C C     . GLU A 1 1897 ? 211.844 170.941 161.561 1.00 18.51  ? 1897 GLU A C     1 
ATOM   4658  O O     . GLU A 1 1897 ? 212.527 170.791 160.541 1.00 18.51  ? 1897 GLU A O     1 
ATOM   4659  C CB    . GLU A 1 1897 ? 212.766 172.209 163.521 1.00 18.51  ? 1897 GLU A CB    1 
ATOM   4660  C CG    . GLU A 1 1897 ? 214.032 171.394 163.311 1.00 18.51  ? 1897 GLU A CG    1 
ATOM   4661  C CD    . GLU A 1 1897 ? 215.105 172.149 162.548 1.00 18.51  ? 1897 GLU A CD    1 
ATOM   4662  O OE1   . GLU A 1 1897 ? 216.238 171.632 162.451 1.00 18.51  ? 1897 GLU A OE1   1 
ATOM   4663  O OE2   . GLU A 1 1897 ? 214.823 173.260 162.050 1.00 18.51  ? 1897 GLU A OE2   1 
ATOM   4664  N N     . ALA A 1 1898 ? 211.080 169.969 162.050 1.00 19.36  ? 1898 ALA A N     1 
ATOM   4665  C CA    . ALA A 1 1898 ? 210.907 168.699 161.359 1.00 19.36  ? 1898 ALA A CA    1 
ATOM   4666  C C     . ALA A 1 1898 ? 209.915 168.791 160.208 1.00 19.36  ? 1898 ALA A C     1 
ATOM   4667  O O     . ALA A 1 1898 ? 209.560 167.757 159.633 1.00 19.36  ? 1898 ALA A O     1 
ATOM   4668  C CB    . ALA A 1 1898 ? 210.461 167.618 162.345 1.00 19.36  ? 1898 ALA A CB    1 
ATOM   4669  N N     . ARG A 1 1899 ? 209.458 170.001 159.880 1.00 18.92  ? 1899 ARG A N     1 
ATOM   4670  C CA    . ARG A 1 1899 ? 208.533 170.244 158.774 1.00 18.92  ? 1899 ARG A CA    1 
ATOM   4671  C C     . ARG A 1 1899 ? 207.197 169.540 158.979 1.00 18.92  ? 1899 ARG A C     1 
ATOM   4672  O O     . ARG A 1 1899 ? 206.504 169.210 158.015 1.00 18.92  ? 1899 ARG A O     1 
ATOM   4673  C CB    . ARG A 1 1899 ? 209.148 169.844 157.431 1.00 18.92  ? 1899 ARG A CB    1 
ATOM   4674  C CG    . ARG A 1 1899 ? 210.461 170.536 157.138 1.00 18.92  ? 1899 ARG A CG    1 
ATOM   4675  C CD    . ARG A 1 1899 ? 210.244 171.851 156.417 1.00 18.92  ? 1899 ARG A CD    1 
ATOM   4676  N NE    . ARG A 1 1899 ? 211.415 172.714 156.507 1.00 18.92  ? 1899 ARG A NE    1 
ATOM   4677  C CZ    . ARG A 1 1899 ? 211.371 174.039 156.512 1.00 18.92  ? 1899 ARG A CZ    1 
ATOM   4678  N NH1   . ARG A 1 1899 ? 210.223 174.692 156.433 1.00 18.92  ? 1899 ARG A NH1   1 
ATOM   4679  N NH2   . ARG A 1 1899 ? 212.506 174.726 156.600 1.00 18.92  ? 1899 ARG A NH2   1 
ATOM   4680  N N     . LEU A 1 1900 ? 206.822 169.306 160.231 1.00 17.80  ? 1900 LEU A N     1 
ATOM   4681  C CA    . LEU A 1 1900 ? 205.500 168.797 160.545 1.00 17.80  ? 1900 LEU A CA    1 
ATOM   4682  C C     . LEU A 1 1900 ? 204.560 169.965 160.832 1.00 17.80  ? 1900 LEU A C     1 
ATOM   4683  O O     . LEU A 1 1900 ? 204.930 171.136 160.735 1.00 17.80  ? 1900 LEU A O     1 
ATOM   4684  C CB    . LEU A 1 1900 ? 205.559 167.835 161.730 1.00 17.80  ? 1900 LEU A CB    1 
ATOM   4685  C CG    . LEU A 1 1900 ? 206.408 166.577 161.563 1.00 17.80  ? 1900 LEU A CG    1 
ATOM   4686  C CD1   . LEU A 1 1900 ? 207.060 166.202 162.881 1.00 17.80  ? 1900 LEU A CD1   1 
ATOM   4687  C CD2   . LEU A 1 1900 ? 205.562 165.432 161.041 1.00 17.80  ? 1900 LEU A CD2   1 
ATOM   4688  N N     . GLY A 1 1901 ? 203.318 169.642 161.188 1.00 17.55  ? 1901 GLY A N     1 
ATOM   4689  C CA    . GLY A 1 1901 ? 202.345 170.629 161.589 1.00 17.55  ? 1901 GLY A CA    1 
ATOM   4690  C C     . GLY A 1 1901 ? 202.175 170.646 163.099 1.00 17.55  ? 1901 GLY A C     1 
ATOM   4691  O O     . GLY A 1 1901 ? 202.748 169.843 163.831 1.00 17.55  ? 1901 GLY A O     1 
ATOM   4692  N N     . GLY A 1 1902 ? 201.365 171.594 163.558 1.00 16.31  ? 1902 GLY A N     1 
ATOM   4693  C CA    . GLY A 1 1902 ? 201.038 171.728 164.964 1.00 16.31  ? 1902 GLY A CA    1 
ATOM   4694  C C     . GLY A 1 1902 ? 199.547 171.527 165.180 1.00 16.31  ? 1902 GLY A C     1 
ATOM   4695  O O     . GLY A 1 1902 ? 198.725 172.148 164.506 1.00 16.31  ? 1902 GLY A O     1 
ATOM   4696  N N     . SER A 1 1903 ? 199.218 170.655 166.127 1.00 21.84  ? 1903 SER A N     1 
ATOM   4697  C CA    . SER A 1 1903 ? 197.831 170.350 166.472 1.00 21.84  ? 1903 SER A CA    1 
ATOM   4698  C C     . SER A 1 1903 ? 197.658 170.489 167.977 1.00 21.84  ? 1903 SER A C     1 
ATOM   4699  O O     . SER A 1 1903 ? 197.546 169.488 168.697 1.00 21.84  ? 1903 SER A O     1 
ATOM   4700  C CB    . SER A 1 1903 ? 197.437 168.951 165.998 1.00 21.84  ? 1903 SER A CB    1 
ATOM   4701  O OG    . SER A 1 1903 ? 196.154 168.596 166.479 1.00 21.84  ? 1903 SER A OG    1 
ATOM   4702  N N     . PRO A 1 1904 ? 197.624 171.719 168.489 1.00 34.96  ? 1904 PRO A N     1 
ATOM   4703  C CA    . PRO A 1 1904 ? 197.417 171.904 169.929 1.00 34.96  ? 1904 PRO A CA    1 
ATOM   4704  C C     . PRO A 1 1904 ? 195.978 171.641 170.336 1.00 34.96  ? 1904 PRO A C     1 
ATOM   4705  O O     . PRO A 1 1904 ? 195.161 172.562 170.362 1.00 34.96  ? 1904 PRO A O     1 
ATOM   4706  C CB    . PRO A 1 1904 ? 197.813 173.367 170.153 1.00 34.96  ? 1904 PRO A CB    1 
ATOM   4707  C CG    . PRO A 1 1904 ? 197.549 174.023 168.851 1.00 34.96  ? 1904 PRO A CG    1 
ATOM   4708  C CD    . PRO A 1 1904 ? 197.844 172.999 167.795 1.00 34.96  ? 1904 PRO A CD    1 
ATOM   4709  N N     . PHE A 1 1905 ? 195.648 170.385 170.621 1.00 14.67  ? 1905 PHE A N     1 
ATOM   4710  C CA    . PHE A 1 1905 ? 194.300 170.046 171.055 1.00 14.67  ? 1905 PHE A CA    1 
ATOM   4711  C C     . PHE A 1 1905 ? 194.089 170.417 172.518 1.00 14.67  ? 1905 PHE A C     1 
ATOM   4712  O O     . PHE A 1 1905 ? 195.037 170.534 173.298 1.00 14.67  ? 1905 PHE A O     1 
ATOM   4713  C CB    . PHE A 1 1905 ? 194.031 168.556 170.840 1.00 14.67  ? 1905 PHE A CB    1 
ATOM   4714  C CG    . PHE A 1 1905 ? 194.778 167.656 171.783 1.00 14.67  ? 1905 PHE A CG    1 
ATOM   4715  C CD1   . PHE A 1 1905 ? 194.205 167.237 172.971 1.00 14.67  ? 1905 PHE A CD1   1 
ATOM   4716  C CD2   . PHE A 1 1905 ? 196.054 167.222 171.474 1.00 14.67  ? 1905 PHE A CD2   1 
ATOM   4717  C CE1   . PHE A 1 1905 ? 194.893 166.408 173.833 1.00 14.67  ? 1905 PHE A CE1   1 
ATOM   4718  C CE2   . PHE A 1 1905 ? 196.745 166.393 172.333 1.00 14.67  ? 1905 PHE A CE2   1 
ATOM   4719  C CZ    . PHE A 1 1905 ? 196.164 165.986 173.513 1.00 14.67  ? 1905 PHE A CZ    1 
ATOM   4720  N N     . GLY A 1 1906 ? 192.824 170.602 172.887 1.00 18.32  ? 1906 GLY A N     1 
ATOM   4721  C CA    . GLY A 1 1906 ? 192.464 170.915 174.250 1.00 18.32  ? 1906 GLY A CA    1 
ATOM   4722  C C     . GLY A 1 1906 ? 191.081 171.525 174.355 1.00 18.32  ? 1906 GLY A C     1 
ATOM   4723  O O     . GLY A 1 1906 ? 190.457 171.880 173.351 1.00 18.32  ? 1906 GLY A O     1 
ATOM   4724  N N     . PRO A 1 1907 ? 190.574 171.658 175.581 1.00 18.13  ? 1907 PRO A N     1 
ATOM   4725  C CA    . PRO A 1 1907 ? 189.251 172.264 175.768 1.00 18.13  ? 1907 PRO A CA    1 
ATOM   4726  C C     . PRO A 1 1907 ? 189.237 173.711 175.303 1.00 18.13  ? 1907 PRO A C     1 
ATOM   4727  O O     . PRO A 1 1907 ? 190.252 174.408 175.340 1.00 18.13  ? 1907 PRO A O     1 
ATOM   4728  C CB    . PRO A 1 1907 ? 189.022 172.162 177.280 1.00 18.13  ? 1907 PRO A CB    1 
ATOM   4729  C CG    . PRO A 1 1907 ? 189.929 171.069 177.730 1.00 18.13  ? 1907 PRO A CG    1 
ATOM   4730  C CD    . PRO A 1 1907 ? 191.132 171.151 176.843 1.00 18.13  ? 1907 PRO A CD    1 
ATOM   4731  N N     . ALA A 1 1908 ? 188.067 174.157 174.854 1.00 17.93  ? 1908 ALA A N     1 
ATOM   4732  C CA    . ALA A 1 1908 ? 187.945 175.502 174.310 1.00 17.93  ? 1908 ALA A CA    1 
ATOM   4733  C C     . ALA A 1 1908 ? 188.184 176.547 175.392 1.00 17.93  ? 1908 ALA A C     1 
ATOM   4734  O O     . ALA A 1 1908 ? 187.722 176.410 176.527 1.00 17.93  ? 1908 ALA A O     1 
ATOM   4735  C CB    . ALA A 1 1908 ? 186.564 175.696 173.684 1.00 17.93  ? 1908 ALA A CB    1 
ATOM   4736  N N     . GLY A 1 1909 ? 188.913 177.599 175.030 1.00 21.61  ? 1909 GLY A N     1 
ATOM   4737  C CA    . GLY A 1 1909 ? 189.188 178.687 175.943 1.00 21.61  ? 1909 GLY A CA    1 
ATOM   4738  C C     . GLY A 1 1909 ? 190.514 178.624 176.665 1.00 21.61  ? 1909 GLY A C     1 
ATOM   4739  O O     . GLY A 1 1909 ? 190.723 179.402 177.603 1.00 21.61  ? 1909 GLY A O     1 
ATOM   4740  N N     . THR A 1 1910 ? 191.416 177.730 176.268 1.00 18.92  ? 1910 THR A N     1 
ATOM   4741  C CA    . THR A 1 1910 ? 192.725 177.626 176.896 1.00 18.92  ? 1910 THR A CA    1 
ATOM   4742  C C     . THR A 1 1910 ? 193.813 178.348 176.115 1.00 18.92  ? 1910 THR A C     1 
ATOM   4743  O O     . THR A 1 1910 ? 194.988 178.247 176.478 1.00 18.92  ? 1910 THR A O     1 
ATOM   4744  C CB    . THR A 1 1910 ? 193.115 176.159 177.077 1.00 18.92  ? 1910 THR A CB    1 
ATOM   4745  O OG1   . THR A 1 1910 ? 193.265 175.544 175.795 1.00 18.92  ? 1910 THR A OG1   1 
ATOM   4746  C CG2   . THR A 1 1910 ? 192.033 175.426 177.844 1.00 18.92  ? 1910 THR A CG2   1 
ATOM   4747  N N     . GLY A 1 1911 ? 193.456 179.064 175.053 1.00 23.09  ? 1911 GLY A N     1 
ATOM   4748  C CA    . GLY A 1 1911 ? 194.416 179.869 174.327 1.00 23.09  ? 1911 GLY A CA    1 
ATOM   4749  C C     . GLY A 1 1911 ? 195.227 179.149 173.278 1.00 23.09  ? 1911 GLY A C     1 
ATOM   4750  O O     . GLY A 1 1911 ? 196.351 179.574 172.995 1.00 23.09  ? 1911 GLY A O     1 
ATOM   4751  N N     . LYS A 1 1912 ? 194.703 178.068 172.695 1.00 15.48  ? 1912 LYS A N     1 
ATOM   4752  C CA    . LYS A 1 1912 ? 195.444 177.357 171.657 1.00 15.48  ? 1912 LYS A CA    1 
ATOM   4753  C C     . LYS A 1 1912 ? 195.650 178.241 170.433 1.00 15.48  ? 1912 LYS A C     1 
ATOM   4754  O O     . LYS A 1 1912 ? 196.779 178.423 169.960 1.00 15.48  ? 1912 LYS A O     1 
ATOM   4755  C CB    . LYS A 1 1912 ? 194.695 176.084 171.266 1.00 15.48  ? 1912 LYS A CB    1 
ATOM   4756  C CG    . LYS A 1 1912 ? 194.597 175.048 172.363 1.00 15.48  ? 1912 LYS A CG    1 
ATOM   4757  C CD    . LYS A 1 1912 ? 193.355 174.199 172.169 1.00 15.48  ? 1912 LYS A CD    1 
ATOM   4758  C CE    . LYS A 1 1912 ? 192.154 174.799 172.853 1.00 15.48  ? 1912 LYS A CE    1 
ATOM   4759  N NZ    . LYS A 1 1912 ? 190.897 174.389 172.172 1.00 15.48  ? 1912 LYS A NZ    1 
ATOM   4760  N N     . THR A 1 1913 ? 194.559 178.808 169.914 1.00 15.51  ? 1913 THR A N     1 
ATOM   4761  C CA    . THR A 1 1913 ? 194.648 179.691 168.757 1.00 15.51  ? 1913 THR A CA    1 
ATOM   4762  C C     . THR A 1 1913 ? 195.441 180.947 169.088 1.00 15.51  ? 1913 THR A C     1 
ATOM   4763  O O     . THR A 1 1913 ? 196.242 181.420 168.273 1.00 15.51  ? 1913 THR A O     1 
ATOM   4764  C CB    . THR A 1 1913 ? 193.246 180.057 168.271 1.00 15.51  ? 1913 THR A CB    1 
ATOM   4765  O OG1   . THR A 1 1913 ? 192.521 178.861 167.960 1.00 15.51  ? 1913 THR A OG1   1 
ATOM   4766  C CG2   . THR A 1 1913 ? 193.318 180.932 167.035 1.00 15.51  ? 1913 THR A CG2   1 
ATOM   4767  N N     . GLU A 1 1914 ? 195.229 181.502 170.282 1.00 18.21  ? 1914 GLU A N     1 
ATOM   4768  C CA    . GLU A 1 1914 ? 195.986 182.677 170.692 1.00 18.21  ? 1914 GLU A CA    1 
ATOM   4769  C C     . GLU A 1 1914 ? 197.469 182.361 170.822 1.00 18.21  ? 1914 GLU A C     1 
ATOM   4770  O O     . GLU A 1 1914 ? 198.312 183.181 170.451 1.00 18.21  ? 1914 GLU A O     1 
ATOM   4771  C CB    . GLU A 1 1914 ? 195.435 183.227 172.004 1.00 18.21  ? 1914 GLU A CB    1 
ATOM   4772  C CG    . GLU A 1 1914 ? 194.200 184.091 171.834 1.00 18.21  ? 1914 GLU A CG    1 
ATOM   4773  C CD    . GLU A 1 1914 ? 194.447 185.291 170.945 1.00 18.21  ? 1914 GLU A CD    1 
ATOM   4774  O OE1   . GLU A 1 1914 ? 195.270 186.151 171.321 1.00 18.21  ? 1914 GLU A OE1   1 
ATOM   4775  O OE2   . GLU A 1 1914 ? 193.816 185.376 169.871 1.00 18.21  ? 1914 GLU A OE2   1 
ATOM   4776  N N     . SER A 1 1915 ? 197.810 181.184 171.353 1.00 14.10  ? 1915 SER A N     1 
ATOM   4777  C CA    . SER A 1 1915 ? 199.217 180.805 171.450 1.00 14.10  ? 1915 SER A CA    1 
ATOM   4778  C C     . SER A 1 1915 ? 199.839 180.641 170.070 1.00 14.10  ? 1915 SER A C     1 
ATOM   4779  O O     . SER A 1 1915 ? 200.983 181.056 169.843 1.00 14.10  ? 1915 SER A O     1 
ATOM   4780  C CB    . SER A 1 1915 ? 199.366 179.518 172.258 1.00 14.10  ? 1915 SER A CB    1 
ATOM   4781  O OG    . SER A 1 1915 ? 198.922 179.703 173.590 1.00 14.10  ? 1915 SER A OG    1 
ATOM   4782  N N     . VAL A 1 1916 ? 199.103 180.035 169.135 1.00 11.92  ? 1916 VAL A N     1 
ATOM   4783  C CA    . VAL A 1 1916 ? 199.615 179.887 167.775 1.00 11.92  ? 1916 VAL A CA    1 
ATOM   4784  C C     . VAL A 1 1916 ? 199.838 181.253 167.139 1.00 11.92  ? 1916 VAL A C     1 
ATOM   4785  O O     . VAL A 1 1916 ? 200.874 181.501 166.507 1.00 11.92  ? 1916 VAL A O     1 
ATOM   4786  C CB    . VAL A 1 1916 ? 198.658 179.019 166.938 1.00 11.92  ? 1916 VAL A CB    1 
ATOM   4787  C CG1   . VAL A 1 1916 ? 198.936 179.196 165.457 1.00 11.92  ? 1916 VAL A CG1   1 
ATOM   4788  C CG2   . VAL A 1 1916 ? 198.787 177.560 167.338 1.00 11.92  ? 1916 VAL A CG2   1 
ATOM   4789  N N     . LYS A 1 1917 ? 198.876 182.165 167.302 1.00 13.34  ? 1917 LYS A N     1 
ATOM   4790  C CA    . LYS A 1 1917 ? 199.027 183.511 166.758 1.00 13.34  ? 1917 LYS A CA    1 
ATOM   4791  C C     . LYS A 1 1917 ? 200.199 184.241 167.397 1.00 13.34  ? 1917 LYS A C     1 
ATOM   4792  O O     . LYS A 1 1917 ? 200.929 184.969 166.718 1.00 13.34  ? 1917 LYS A O     1 
ATOM   4793  C CB    . LYS A 1 1917 ? 197.744 184.314 166.955 1.00 13.34  ? 1917 LYS A CB    1 
ATOM   4794  C CG    . LYS A 1 1917 ? 196.605 183.926 166.040 1.00 13.34  ? 1917 LYS A CG    1 
ATOM   4795  C CD    . LYS A 1 1917 ? 195.355 184.703 166.405 1.00 13.34  ? 1917 LYS A CD    1 
ATOM   4796  C CE    . LYS A 1 1917 ? 195.508 186.173 166.060 1.00 13.34  ? 1917 LYS A CE    1 
ATOM   4797  N NZ    . LYS A 1 1917 ? 194.259 186.934 166.327 1.00 13.34  ? 1917 LYS A NZ    1 
ATOM   4798  N N     . ALA A 1 1918 ? 200.379 184.083 168.710 1.00 12.55  ? 1918 ALA A N     1 
ATOM   4799  C CA    . ALA A 1 1918 ? 201.484 184.746 169.392 1.00 12.55  ? 1918 ALA A CA    1 
ATOM   4800  C C     . ALA A 1 1918 ? 202.825 184.221 168.904 1.00 12.55  ? 1918 ALA A C     1 
ATOM   4801  O O     . ALA A 1 1918 ? 203.767 184.997 168.712 1.00 12.55  ? 1918 ALA A O     1 
ATOM   4802  C CB    . ALA A 1 1918 ? 201.352 184.568 170.902 1.00 12.55  ? 1918 ALA A CB    1 
ATOM   4803  N N     . LEU A 1 1919 ? 202.934 182.907 168.701 1.00 9.95   ? 1919 LEU A N     1 
ATOM   4804  C CA    . LEU A 1 1919 ? 204.165 182.357 168.144 1.00 9.95   ? 1919 LEU A CA    1 
ATOM   4805  C C     . LEU A 1 1919 ? 204.407 182.878 166.734 1.00 9.95   ? 1919 LEU A C     1 
ATOM   4806  O O     . LEU A 1 1919 ? 205.538 183.230 166.381 1.00 9.95   ? 1919 LEU A O     1 
ATOM   4807  C CB    . LEU A 1 1919 ? 204.115 180.831 168.146 1.00 9.95   ? 1919 LEU A CB    1 
ATOM   4808  C CG    . LEU A 1 1919 ? 205.231 180.162 167.343 1.00 9.95   ? 1919 LEU A CG    1 
ATOM   4809  C CD1   . LEU A 1 1919 ? 206.576 180.367 168.017 1.00 9.95   ? 1919 LEU A CD1   1 
ATOM   4810  C CD2   . LEU A 1 1919 ? 204.942 178.690 167.157 1.00 9.95   ? 1919 LEU A CD2   1 
ATOM   4811  N N     . GLY A 1 1920 ? 203.355 182.937 165.914 1.00 9.53   ? 1920 GLY A N     1 
ATOM   4812  C CA    . GLY A 1 1920 ? 203.515 183.450 164.563 1.00 9.53   ? 1920 GLY A CA    1 
ATOM   4813  C C     . GLY A 1 1920 ? 203.941 184.905 164.537 1.00 9.53   ? 1920 GLY A C     1 
ATOM   4814  O O     . GLY A 1 1920 ? 204.769 185.305 163.717 1.00 9.53   ? 1920 GLY A O     1 
ATOM   4815  N N     . HIS A 1 1921 ? 203.379 185.715 165.435 1.00 11.02  ? 1921 HIS A N     1 
ATOM   4816  C CA    . HIS A 1 1921 ? 203.765 187.117 165.522 1.00 11.02  ? 1921 HIS A CA    1 
ATOM   4817  C C     . HIS A 1 1921 ? 205.166 187.276 166.093 1.00 11.02  ? 1921 HIS A C     1 
ATOM   4818  O O     . HIS A 1 1921 ? 205.849 188.261 165.792 1.00 11.02  ? 1921 HIS A O     1 
ATOM   4819  C CB    . HIS A 1 1921 ? 202.756 187.886 166.373 1.00 11.02  ? 1921 HIS A CB    1 
ATOM   4820  C CG    . HIS A 1 1921 ? 201.387 187.951 165.773 1.00 11.02  ? 1921 HIS A CG    1 
ATOM   4821  N ND1   . HIS A 1 1921 ? 201.160 187.817 164.421 1.00 11.02  ? 1921 HIS A ND1   1 
ATOM   4822  C CD2   . HIS A 1 1921 ? 200.173 188.136 166.341 1.00 11.02  ? 1921 HIS A CD2   1 
ATOM   4823  C CE1   . HIS A 1 1921 ? 199.865 187.916 164.181 1.00 11.02  ? 1921 HIS A CE1   1 
ATOM   4824  N NE2   . HIS A 1 1921 ? 199.243 188.110 165.330 1.00 11.02  ? 1921 HIS A NE2   1 
ATOM   4825  N N     . GLN A 1 1922 ? 205.606 186.328 166.921 1.00 10.64  ? 1922 GLN A N     1 
ATOM   4826  C CA    . GLN A 1 1922 ? 206.953 186.394 167.475 1.00 10.64  ? 1922 GLN A CA    1 
ATOM   4827  C C     . GLN A 1 1922 ? 208.003 186.264 166.381 1.00 10.64  ? 1922 GLN A C     1 
ATOM   4828  O O     . GLN A 1 1922 ? 209.044 186.927 166.429 1.00 10.64  ? 1922 GLN A O     1 
ATOM   4829  C CB    . GLN A 1 1922 ? 207.137 185.308 168.531 1.00 10.64  ? 1922 GLN A CB    1 
ATOM   4830  C CG    . GLN A 1 1922 ? 208.474 185.362 169.231 1.00 10.64  ? 1922 GLN A CG    1 
ATOM   4831  C CD    . GLN A 1 1922 ? 208.648 186.628 170.037 1.00 10.64  ? 1922 GLN A CD    1 
ATOM   4832  O OE1   . GLN A 1 1922 ? 209.348 187.550 169.621 1.00 10.64  ? 1922 GLN A OE1   1 
ATOM   4833  N NE2   . GLN A 1 1922 ? 208.005 186.683 171.196 1.00 10.64  ? 1922 GLN A NE2   1 
ATOM   4834  N N     . LEU A 1 1923 ? 207.748 185.416 165.389 1.00 10.95  ? 1923 LEU A N     1 
ATOM   4835  C CA    . LEU A 1 1923 ? 208.636 185.257 164.248 1.00 10.95  ? 1923 LEU A CA    1 
ATOM   4836  C C     . LEU A 1 1923 ? 208.319 186.226 163.118 1.00 10.95  ? 1923 LEU A C     1 
ATOM   4837  O O     . LEU A 1 1923 ? 208.952 186.151 162.061 1.00 10.95  ? 1923 LEU A O     1 
ATOM   4838  C CB    . LEU A 1 1923 ? 208.574 183.819 163.725 1.00 10.95  ? 1923 LEU A CB    1 
ATOM   4839  C CG    . LEU A 1 1923 ? 208.622 182.718 164.784 1.00 10.95  ? 1923 LEU A CG    1 
ATOM   4840  C CD1   . LEU A 1 1923 ? 208.300 181.372 164.164 1.00 10.95  ? 1923 LEU A CD1   1 
ATOM   4841  C CD2   . LEU A 1 1923 ? 209.977 182.686 165.463 1.00 10.95  ? 1923 LEU A CD2   1 
ATOM   4842  N N     . GLY A 1 1924 ? 207.361 187.126 163.315 1.00 11.33  ? 1924 GLY A N     1 
ATOM   4843  C CA    . GLY A 1 1924 ? 207.013 188.099 162.295 1.00 11.33  ? 1924 GLY A CA    1 
ATOM   4844  C C     . GLY A 1 1924 ? 206.395 187.505 161.050 1.00 11.33  ? 1924 GLY A C     1 
ATOM   4845  O O     . GLY A 1 1924 ? 206.736 187.921 159.936 1.00 11.33  ? 1924 GLY A O     1 
ATOM   4846  N N     . ARG A 1 1925 ? 205.492 186.544 161.208 1.00 11.33  ? 1925 ARG A N     1 
ATOM   4847  C CA    . ARG A 1 1925 ? 204.804 185.916 160.092 1.00 11.33  ? 1925 ARG A CA    1 
ATOM   4848  C C     . ARG A 1 1925 ? 203.336 186.313 160.105 1.00 11.33  ? 1925 ARG A C     1 
ATOM   4849  O O     . ARG A 1 1925 ? 202.722 186.419 161.170 1.00 11.33  ? 1925 ARG A O     1 
ATOM   4850  C CB    . ARG A 1 1925 ? 204.921 184.392 160.152 1.00 11.33  ? 1925 ARG A CB    1 
ATOM   4851  C CG    . ARG A 1 1925 ? 206.340 183.862 160.197 1.00 11.33  ? 1925 ARG A CG    1 
ATOM   4852  C CD    . ARG A 1 1925 ? 207.049 184.038 158.864 1.00 11.33  ? 1925 ARG A CD    1 
ATOM   4853  N NE    . ARG A 1 1925 ? 208.149 183.096 158.691 1.00 11.33  ? 1925 ARG A NE    1 
ATOM   4854  C CZ    . ARG A 1 1925 ? 209.246 183.061 159.436 1.00 11.33  ? 1925 ARG A CZ    1 
ATOM   4855  N NH1   . ARG A 1 1925 ? 209.456 183.937 160.406 1.00 11.33  ? 1925 ARG A NH1   1 
ATOM   4856  N NH2   . ARG A 1 1925 ? 210.163 182.128 159.197 1.00 11.33  ? 1925 ARG A NH2   1 
ATOM   4857  N N     . PHE A 1 1926 ? 202.781 186.537 158.918 1.00 14.46  ? 1926 PHE A N     1 
ATOM   4858  C CA    . PHE A 1 1926 ? 201.350 186.775 158.803 1.00 14.46  ? 1926 PHE A CA    1 
ATOM   4859  C C     . PHE A 1 1926 ? 200.591 185.522 159.219 1.00 14.46  ? 1926 PHE A C     1 
ATOM   4860  O O     . PHE A 1 1926 ? 200.836 184.432 158.697 1.00 14.46  ? 1926 PHE A O     1 
ATOM   4861  C CB    . PHE A 1 1926 ? 201.002 187.171 157.367 1.00 14.46  ? 1926 PHE A CB    1 
ATOM   4862  C CG    . PHE A 1 1926 ? 199.549 187.491 157.153 1.00 14.46  ? 1926 PHE A CG    1 
ATOM   4863  C CD1   . PHE A 1 1926 ? 198.779 188.020 158.172 1.00 14.46  ? 1926 PHE A CD1   1 
ATOM   4864  C CD2   . PHE A 1 1926 ? 198.957 187.267 155.923 1.00 14.46  ? 1926 PHE A CD2   1 
ATOM   4865  C CE1   . PHE A 1 1926 ? 197.446 188.315 157.971 1.00 14.46  ? 1926 PHE A CE1   1 
ATOM   4866  C CE2   . PHE A 1 1926 ? 197.626 187.560 155.716 1.00 14.46  ? 1926 PHE A CE2   1 
ATOM   4867  C CZ    . PHE A 1 1926 ? 196.870 188.084 156.741 1.00 14.46  ? 1926 PHE A CZ    1 
ATOM   4868  N N     . VAL A 1 1927 ? 199.674 185.676 160.170 1.00 12.78  ? 1927 VAL A N     1 
ATOM   4869  C CA    . VAL A 1 1927 ? 198.910 184.563 160.716 1.00 12.78  ? 1927 VAL A CA    1 
ATOM   4870  C C     . VAL A 1 1927 ? 197.443 184.772 160.378 1.00 12.78  ? 1927 VAL A C     1 
ATOM   4871  O O     . VAL A 1 1927 ? 196.878 185.832 160.668 1.00 12.78  ? 1927 VAL A O     1 
ATOM   4872  C CB    . VAL A 1 1927 ? 199.104 184.428 162.236 1.00 12.78  ? 1927 VAL A CB    1 
ATOM   4873  C CG1   . VAL A 1 1927 ? 198.400 183.186 162.749 1.00 12.78  ? 1927 VAL A CG1   1 
ATOM   4874  C CG2   . VAL A 1 1927 ? 200.579 184.382 162.575 1.00 12.78  ? 1927 VAL A CG2   1 
ATOM   4875  N N     . LEU A 1 1928 ? 196.832 183.763 159.767 1.00 15.93  ? 1928 LEU A N     1 
ATOM   4876  C CA    . LEU A 1 1928 ? 195.420 183.781 159.418 1.00 15.93  ? 1928 LEU A CA    1 
ATOM   4877  C C     . LEU A 1 1928 ? 194.691 182.733 160.244 1.00 15.93  ? 1928 LEU A C     1 
ATOM   4878  O O     . LEU A 1 1928 ? 195.155 181.593 160.355 1.00 15.93  ? 1928 LEU A O     1 
ATOM   4879  C CB    . LEU A 1 1928 ? 195.219 183.514 157.926 1.00 15.93  ? 1928 LEU A CB    1 
ATOM   4880  C CG    . LEU A 1 1928 ? 195.386 184.709 156.991 1.00 15.93  ? 1928 LEU A CG    1 
ATOM   4881  C CD1   . LEU A 1 1928 ? 195.854 184.248 155.626 1.00 15.93  ? 1928 LEU A CD1   1 
ATOM   4882  C CD2   . LEU A 1 1928 ? 194.083 185.480 156.880 1.00 15.93  ? 1928 LEU A CD2   1 
ATOM   4883  N N     . VAL A 1 1929 ? 193.557 183.117 160.819 1.00 16.91  ? 1929 VAL A N     1 
ATOM   4884  C CA    . VAL A 1 1929 ? 192.741 182.226 161.634 1.00 16.91  ? 1929 VAL A CA    1 
ATOM   4885  C C     . VAL A 1 1929 ? 191.455 181.942 160.874 1.00 16.91  ? 1929 VAL A C     1 
ATOM   4886  O O     . VAL A 1 1929 ? 190.726 182.871 160.504 1.00 16.91  ? 1929 VAL A O     1 
ATOM   4887  C CB    . VAL A 1 1929 ? 192.448 182.829 163.015 1.00 16.91  ? 1929 VAL A CB    1 
ATOM   4888  C CG1   . VAL A 1 1929 ? 191.350 182.048 163.711 1.00 16.91  ? 1929 VAL A CG1   1 
ATOM   4889  C CG2   . VAL A 1 1929 ? 193.707 182.838 163.855 1.00 16.91  ? 1929 VAL A CG2   1 
ATOM   4890  N N     . PHE A 1 1930 ? 191.176 180.664 160.641 1.00 22.32  ? 1930 PHE A N     1 
ATOM   4891  C CA    . PHE A 1 1930 ? 189.988 180.231 159.913 1.00 22.32  ? 1930 PHE A CA    1 
ATOM   4892  C C     . PHE A 1 1930 ? 188.986 179.682 160.921 1.00 22.32  ? 1930 PHE A C     1 
ATOM   4893  O O     . PHE A 1 1930 ? 189.090 178.528 161.346 1.00 22.32  ? 1930 PHE A O     1 
ATOM   4894  C CB    . PHE A 1 1930 ? 190.341 179.184 158.861 1.00 22.32  ? 1930 PHE A CB    1 
ATOM   4895  C CG    . PHE A 1 1930 ? 191.584 179.498 158.084 1.00 22.32  ? 1930 PHE A CG    1 
ATOM   4896  C CD1   . PHE A 1 1930 ? 191.752 180.733 157.487 1.00 22.32  ? 1930 PHE A CD1   1 
ATOM   4897  C CD2   . PHE A 1 1930 ? 192.582 178.551 157.943 1.00 22.32  ? 1930 PHE A CD2   1 
ATOM   4898  C CE1   . PHE A 1 1930 ? 192.894 181.019 156.770 1.00 22.32  ? 1930 PHE A CE1   1 
ATOM   4899  C CE2   . PHE A 1 1930 ? 193.726 178.832 157.227 1.00 22.32  ? 1930 PHE A CE2   1 
ATOM   4900  C CZ    . PHE A 1 1930 ? 193.882 180.067 156.641 1.00 22.32  ? 1930 PHE A CZ    1 
ATOM   4901  N N     . ASN A 1 1931 ? 188.017 180.509 161.301 1.00 32.64  ? 1931 ASN A N     1 
ATOM   4902  C CA    . ASN A 1 1931 ? 186.954 180.048 162.181 1.00 32.64  ? 1931 ASN A CA    1 
ATOM   4903  C C     . ASN A 1 1931 ? 186.091 179.022 161.460 1.00 32.64  ? 1931 ASN A C     1 
ATOM   4904  O O     . ASN A 1 1931 ? 185.723 179.204 160.296 1.00 32.64  ? 1931 ASN A O     1 
ATOM   4905  C CB    . ASN A 1 1931 ? 186.098 181.225 162.646 1.00 32.64  ? 1931 ASN A CB    1 
ATOM   4906  C CG    . ASN A 1 1931 ? 186.835 182.138 163.605 1.00 32.64  ? 1931 ASN A CG    1 
ATOM   4907  O OD1   . ASN A 1 1931 ? 187.549 181.678 164.493 1.00 32.64  ? 1931 ASN A OD1   1 
ATOM   4908  N ND2   . ASN A 1 1931 ? 186.666 183.443 163.427 1.00 32.64  ? 1931 ASN A ND2   1 
ATOM   4909  N N     . CYS A 1 1932 ? 185.768 177.935 162.159 1.00 39.93  ? 1932 CYS A N     1 
ATOM   4910  C CA    . CYS A 1 1932 ? 184.992 176.843 161.587 1.00 39.93  ? 1932 CYS A CA    1 
ATOM   4911  C C     . CYS A 1 1932 ? 183.548 176.839 162.076 1.00 39.93  ? 1932 CYS A C     1 
ATOM   4912  O O     . CYS A 1 1932 ? 182.819 175.871 161.840 1.00 39.93  ? 1932 CYS A O     1 
ATOM   4913  C CB    . CYS A 1 1932 ? 185.663 175.505 161.892 1.00 39.93  ? 1932 CYS A CB    1 
ATOM   4914  S SG    . CYS A 1 1932 ? 187.315 175.329 161.180 1.00 39.93  ? 1932 CYS A SG    1 
ATOM   4915  N N     . ASP A 1 1933 ? 183.118 177.906 162.746 1.00 54.46  ? 1933 ASP A N     1 
ATOM   4916  C CA    . ASP A 1 1933 ? 181.746 178.013 163.239 1.00 54.46  ? 1933 ASP A CA    1 
ATOM   4917  C C     . ASP A 1 1933 ? 180.819 178.494 162.121 1.00 54.46  ? 1933 ASP A C     1 
ATOM   4918  O O     . ASP A 1 1933 ? 180.356 179.634 162.096 1.00 54.46  ? 1933 ASP A O     1 
ATOM   4919  C CB    . ASP A 1 1933 ? 181.692 178.938 164.449 1.00 54.46  ? 1933 ASP A CB    1 
ATOM   4920  C CG    . ASP A 1 1933 ? 182.760 178.613 165.478 1.00 54.46  ? 1933 ASP A CG    1 
ATOM   4921  O OD1   . ASP A 1 1933 ? 183.090 179.498 166.296 1.00 54.46  ? 1933 ASP A OD1   1 
ATOM   4922  O OD2   . ASP A 1 1933 ? 183.277 177.477 165.460 1.00 54.46  ? 1933 ASP A OD2   1 
ATOM   4923  N N     . GLU A 1 1934 ? 180.609 177.598 161.155 1.00 62.57  ? 1934 GLU A N     1 
ATOM   4924  C CA    . GLU A 1 1934 ? 179.747 177.715 159.976 1.00 62.57  ? 1934 GLU A CA    1 
ATOM   4925  C C     . GLU A 1 1934 ? 180.036 178.955 159.138 1.00 62.57  ? 1934 GLU A C     1 
ATOM   4926  O O     . GLU A 1 1934 ? 179.286 179.234 158.195 1.00 62.57  ? 1934 GLU A O     1 
ATOM   4927  C CB    . GLU A 1 1934 ? 178.244 177.674 160.311 1.00 62.57  ? 1934 GLU A CB    1 
ATOM   4928  C CG    . GLU A 1 1934 ? 177.654 178.900 160.997 1.00 62.57  ? 1934 GLU A CG    1 
ATOM   4929  C CD    . GLU A 1 1934 ? 177.498 178.714 162.495 1.00 62.57  ? 1934 GLU A CD    1 
ATOM   4930  O OE1   . GLU A 1 1934 ? 178.077 177.753 163.043 1.00 62.57  ? 1934 GLU A OE1   1 
ATOM   4931  O OE2   . GLU A 1 1934 ? 176.794 179.531 163.126 1.00 62.57  ? 1934 GLU A OE2   1 
ATOM   4932  N N     . THR A 1 1935 ? 181.089 179.711 159.445 1.00 62.40  ? 1935 THR A N     1 
ATOM   4933  C CA    . THR A 1 1935 ? 181.559 180.788 158.575 1.00 62.40  ? 1935 THR A CA    1 
ATOM   4934  C C     . THR A 1 1935 ? 182.735 180.300 157.726 1.00 62.40  ? 1935 THR A C     1 
ATOM   4935  O O     . THR A 1 1935 ? 183.838 180.843 157.763 1.00 62.40  ? 1935 THR A O     1 
ATOM   4936  C CB    . THR A 1 1935 ? 181.937 182.011 159.403 1.00 62.40  ? 1935 THR A CB    1 
ATOM   4937  O OG1   . THR A 1 1935 ? 183.027 181.683 160.273 1.00 62.40  ? 1935 THR A OG1   1 
ATOM   4938  C CG2   . THR A 1 1935 ? 180.753 182.473 160.240 1.00 62.40  ? 1935 THR A CG2   1 
ATOM   4939  N N     . PHE A 1 1936 ? 182.481 179.248 156.952 1.00 49.99  ? 1936 PHE A N     1 
ATOM   4940  C CA    . PHE A 1 1936 ? 183.533 178.552 156.227 1.00 49.99  ? 1936 PHE A CA    1 
ATOM   4941  C C     . PHE A 1 1936 ? 183.067 178.261 154.804 1.00 49.99  ? 1936 PHE A C     1 
ATOM   4942  O O     . PHE A 1 1936 ? 181.865 178.159 154.541 1.00 49.99  ? 1936 PHE A O     1 
ATOM   4943  C CB    . PHE A 1 1936 ? 183.909 177.255 156.954 1.00 49.99  ? 1936 PHE A CB    1 
ATOM   4944  C CG    . PHE A 1 1936 ? 185.322 176.817 156.723 1.00 49.99  ? 1936 PHE A CG    1 
ATOM   4945  C CD1   . PHE A 1 1936 ? 186.370 177.536 157.269 1.00 49.99  ? 1936 PHE A CD1   1 
ATOM   4946  C CD2   . PHE A 1 1936 ? 185.609 175.685 155.986 1.00 49.99  ? 1936 PHE A CD2   1 
ATOM   4947  C CE1   . PHE A 1 1936 ? 187.675 177.145 157.073 1.00 49.99  ? 1936 PHE A CE1   1 
ATOM   4948  C CE2   . PHE A 1 1936 ? 186.918 175.289 155.789 1.00 49.99  ? 1936 PHE A CE2   1 
ATOM   4949  C CZ    . PHE A 1 1936 ? 187.949 176.021 156.332 1.00 49.99  ? 1936 PHE A CZ    1 
ATOM   4950  N N     . ASP A 1 1937 ? 184.024 178.120 153.885 1.00 54.96  ? 1937 ASP A N     1 
ATOM   4951  C CA    . ASP A 1 1937 ? 183.691 178.010 152.464 1.00 54.96  ? 1937 ASP A CA    1 
ATOM   4952  C C     . ASP A 1 1937 ? 184.877 177.455 151.690 1.00 54.96  ? 1937 ASP A C     1 
ATOM   4953  O O     . ASP A 1 1937 ? 186.027 177.746 152.033 1.00 54.96  ? 1937 ASP A O     1 
ATOM   4954  C CB    . ASP A 1 1937 ? 183.282 179.375 151.910 1.00 54.96  ? 1937 ASP A CB    1 
ATOM   4955  C CG    . ASP A 1 1937 ? 184.194 180.491 152.386 1.00 54.96  ? 1937 ASP A CG    1 
ATOM   4956  O OD1   . ASP A 1 1937 ? 185.021 180.239 153.288 1.00 54.96  ? 1937 ASP A OD1   1 
ATOM   4957  O OD2   . ASP A 1 1937 ? 184.081 181.619 151.862 1.00 54.96  ? 1937 ASP A OD2   1 
ATOM   4958  N N     . PHE A 1 1938 ? 184.598 176.661 150.649 1.00 55.78  ? 1938 PHE A N     1 
ATOM   4959  C CA    . PHE A 1 1938 ? 185.657 176.191 149.757 1.00 55.78  ? 1938 PHE A CA    1 
ATOM   4960  C C     . PHE A 1 1938 ? 186.282 177.334 148.970 1.00 55.78  ? 1938 PHE A C     1 
ATOM   4961  O O     . PHE A 1 1938 ? 187.513 177.464 148.915 1.00 55.78  ? 1938 PHE A O     1 
ATOM   4962  C CB    . PHE A 1 1938 ? 185.114 175.169 148.757 1.00 55.78  ? 1938 PHE A CB    1 
ATOM   4963  C CG    . PHE A 1 1938 ? 185.126 173.755 149.241 1.00 55.78  ? 1938 PHE A CG    1 
ATOM   4964  C CD1   . PHE A 1 1938 ? 186.317 173.061 149.353 1.00 55.78  ? 1938 PHE A CD1   1 
ATOM   4965  C CD2   . PHE A 1 1938 ? 183.940 173.090 149.492 1.00 55.78  ? 1938 PHE A CD2   1 
ATOM   4966  C CE1   . PHE A 1 1938 ? 186.327 171.751 149.771 1.00 55.78  ? 1938 PHE A CE1   1 
ATOM   4967  C CE2   . PHE A 1 1938 ? 183.944 171.775 149.898 1.00 55.78  ? 1938 PHE A CE2   1 
ATOM   4968  C CZ    . PHE A 1 1938 ? 185.137 171.106 150.042 1.00 55.78  ? 1938 PHE A CZ    1 
ATOM   4969  N N     . GLN A 1 1939 ? 185.444 178.155 148.330 1.00 55.62  ? 1939 GLN A N     1 
ATOM   4970  C CA    . GLN A 1 1939 ? 185.920 179.065 147.293 1.00 55.62  ? 1939 GLN A CA    1 
ATOM   4971  C C     . GLN A 1 1939 ? 186.934 180.062 147.830 1.00 55.62  ? 1939 GLN A C     1 
ATOM   4972  O O     . GLN A 1 1939 ? 187.821 180.502 147.091 1.00 55.62  ? 1939 GLN A O     1 
ATOM   4973  C CB    . GLN A 1 1939 ? 184.736 179.792 146.653 1.00 55.62  ? 1939 GLN A CB    1 
ATOM   4974  C CG    . GLN A 1 1939 ? 183.987 180.732 147.587 1.00 55.62  ? 1939 GLN A CG    1 
ATOM   4975  C CD    . GLN A 1 1939 ? 182.901 180.028 148.380 1.00 55.62  ? 1939 GLN A CD    1 
ATOM   4976  O OE1   . GLN A 1 1939 ? 182.890 178.801 148.487 1.00 55.62  ? 1939 GLN A OE1   1 
ATOM   4977  N NE2   . GLN A 1 1939 ? 181.981 180.804 148.940 1.00 55.62  ? 1939 GLN A NE2   1 
ATOM   4978  N N     . ALA A 1 1940 ? 186.827 180.427 149.104 1.00 43.84  ? 1940 ALA A N     1 
ATOM   4979  C CA    . ALA A 1 1940 ? 187.838 181.270 149.721 1.00 43.84  ? 1940 ALA A CA    1 
ATOM   4980  C C     . ALA A 1 1940 ? 189.016 180.468 150.249 1.00 43.84  ? 1940 ALA A C     1 
ATOM   4981  O O     . ALA A 1 1940 ? 190.162 180.910 150.119 1.00 43.84  ? 1940 ALA A O     1 
ATOM   4982  C CB    . ALA A 1 1940 ? 187.225 182.091 150.859 1.00 43.84  ? 1940 ALA A CB    1 
ATOM   4983  N N     . MET A 1 1941 ? 188.763 179.286 150.815 1.00 35.58  ? 1941 MET A N     1 
ATOM   4984  C CA    . MET A 1 1941 ? 189.817 178.522 151.468 1.00 35.58  ? 1941 MET A CA    1 
ATOM   4985  C C     . MET A 1 1941 ? 190.841 177.956 150.495 1.00 35.58  ? 1941 MET A C     1 
ATOM   4986  O O     . MET A 1 1941 ? 192.027 177.910 150.833 1.00 35.58  ? 1941 MET A O     1 
ATOM   4987  C CB    . MET A 1 1941 ? 189.215 177.383 152.296 1.00 35.58  ? 1941 MET A CB    1 
ATOM   4988  C CG    . MET A 1 1941 ? 190.194 176.679 153.242 1.00 35.58  ? 1941 MET A CG    1 
ATOM   4989  S SD    . MET A 1 1941 ? 191.110 177.660 154.464 1.00 35.58  ? 1941 MET A SD    1 
ATOM   4990  C CE    . MET A 1 1941 ? 190.029 179.055 154.789 1.00 35.58  ? 1941 MET A CE    1 
ATOM   4991  N N     . GLY A 1 1942 ? 190.425 177.518 149.306 1.00 31.88  ? 1942 GLY A N     1 
ATOM   4992  C CA    . GLY A 1 1942 ? 191.400 177.014 148.347 1.00 31.88  ? 1942 GLY A CA    1 
ATOM   4993  C C     . GLY A 1 1942 ? 192.399 178.076 147.924 1.00 31.88  ? 1942 GLY A C     1 
ATOM   4994  O O     . GLY A 1 1942 ? 193.617 177.863 147.961 1.00 31.88  ? 1942 GLY A O     1 
ATOM   4995  N N     . ARG A 1 1943 ? 191.897 179.251 147.543 1.00 31.65  ? 1943 ARG A N     1 
ATOM   4996  C CA    . ARG A 1 1943 ? 192.797 180.332 147.163 1.00 31.65  ? 1943 ARG A CA    1 
ATOM   4997  C C     . ARG A 1 1943 ? 193.561 180.869 148.366 1.00 31.65  ? 1943 ARG A C     1 
ATOM   4998  O O     . ARG A 1 1943 ? 194.679 181.369 148.210 1.00 31.65  ? 1943 ARG A O     1 
ATOM   4999  C CB    . ARG A 1 1943 ? 192.020 181.445 146.460 1.00 31.65  ? 1943 ARG A CB    1 
ATOM   5000  C CG    . ARG A 1 1943 ? 191.085 182.224 147.356 1.00 31.65  ? 1943 ARG A CG    1 
ATOM   5001  C CD    . ARG A 1 1943 ? 190.482 183.404 146.620 1.00 31.65  ? 1943 ARG A CD    1 
ATOM   5002  N NE    . ARG A 1 1943 ? 189.152 183.725 147.122 1.00 31.65  ? 1943 ARG A NE    1 
ATOM   5003  C CZ    . ARG A 1 1943 ? 188.918 184.433 148.217 1.00 31.65  ? 1943 ARG A CZ    1 
ATOM   5004  N NH1   . ARG A 1 1943 ? 189.906 184.920 148.949 1.00 31.65  ? 1943 ARG A NH1   1 
ATOM   5005  N NH2   . ARG A 1 1943 ? 187.661 184.659 148.587 1.00 31.65  ? 1943 ARG A NH2   1 
ATOM   5006  N N     . ILE A 1 1944 ? 193.001 180.751 149.573 1.00 27.80  ? 1944 ILE A N     1 
ATOM   5007  C CA    . ILE A 1 1944 ? 193.744 181.143 150.766 1.00 27.80  ? 1944 ILE A CA    1 
ATOM   5008  C C     . ILE A 1 1944 ? 194.926 180.208 150.987 1.00 27.80  ? 1944 ILE A C     1 
ATOM   5009  O O     . ILE A 1 1944 ? 196.022 180.648 151.349 1.00 27.80  ? 1944 ILE A O     1 
ATOM   5010  C CB    . ILE A 1 1944 ? 192.808 181.190 151.987 1.00 27.80  ? 1944 ILE A CB    1 
ATOM   5011  C CG1   . ILE A 1 1944 ? 192.099 182.543 152.057 1.00 27.80  ? 1944 ILE A CG1   1 
ATOM   5012  C CG2   . ILE A 1 1944 ? 193.577 180.943 153.268 1.00 27.80  ? 1944 ILE A CG2   1 
ATOM   5013  C CD1   . ILE A 1 1944 ? 190.941 182.574 153.023 1.00 27.80  ? 1944 ILE A CD1   1 
ATOM   5014  N N     . PHE A 1 1945 ? 194.724 178.906 150.775 1.00 24.39  ? 1945 PHE A N     1 
ATOM   5015  C CA    . PHE A 1 1945 ? 195.839 177.964 150.836 1.00 24.39  ? 1945 PHE A CA    1 
ATOM   5016  C C     . PHE A 1 1945 ? 196.888 178.286 149.782 1.00 24.39  ? 1945 PHE A C     1 
ATOM   5017  O O     . PHE A 1 1945 ? 198.094 178.221 150.052 1.00 24.39  ? 1945 PHE A O     1 
ATOM   5018  C CB    . PHE A 1 1945 ? 195.342 176.531 150.657 1.00 24.39  ? 1945 PHE A CB    1 
ATOM   5019  C CG    . PHE A 1 1945 ? 194.774 175.924 151.902 1.00 24.39  ? 1945 PHE A CG    1 
ATOM   5020  C CD1   . PHE A 1 1945 ? 195.032 176.481 153.140 1.00 24.39  ? 1945 PHE A CD1   1 
ATOM   5021  C CD2   . PHE A 1 1945 ? 193.992 174.786 151.834 1.00 24.39  ? 1945 PHE A CD2   1 
ATOM   5022  C CE1   . PHE A 1 1945 ? 194.515 175.918 154.287 1.00 24.39  ? 1945 PHE A CE1   1 
ATOM   5023  C CE2   . PHE A 1 1945 ? 193.471 174.219 152.977 1.00 24.39  ? 1945 PHE A CE2   1 
ATOM   5024  C CZ    . PHE A 1 1945 ? 193.733 174.785 154.203 1.00 24.39  ? 1945 PHE A CZ    1 
ATOM   5025  N N     . VAL A 1 1946 ? 196.446 178.625 148.569 1.00 25.90  ? 1946 VAL A N     1 
ATOM   5026  C CA    . VAL A 1 1946 ? 197.397 178.990 147.520 1.00 25.90  ? 1946 VAL A CA    1 
ATOM   5027  C C     . VAL A 1 1946 ? 198.205 180.213 147.942 1.00 25.90  ? 1946 VAL A C     1 
ATOM   5028  O O     . VAL A 1 1946 ? 199.427 180.270 147.759 1.00 25.90  ? 1946 VAL A O     1 
ATOM   5029  C CB    . VAL A 1 1946 ? 196.668 179.225 146.186 1.00 25.90  ? 1946 VAL A CB    1 
ATOM   5030  C CG1   . VAL A 1 1946 ? 197.648 179.696 145.131 1.00 25.90  ? 1946 VAL A CG1   1 
ATOM   5031  C CG2   . VAL A 1 1946 ? 195.973 177.954 145.734 1.00 25.90  ? 1946 VAL A CG2   1 
ATOM   5032  N N     . GLY A 1 1947 ? 197.533 181.206 148.526 1.00 22.37  ? 1947 GLY A N     1 
ATOM   5033  C CA    . GLY A 1 1947 ? 198.234 182.390 148.994 1.00 22.37  ? 1947 GLY A CA    1 
ATOM   5034  C C     . GLY A 1 1947 ? 199.209 182.094 150.117 1.00 22.37  ? 1947 GLY A C     1 
ATOM   5035  O O     . GLY A 1 1947 ? 200.313 182.639 150.152 1.00 22.37  ? 1947 GLY A O     1 
ATOM   5036  N N     . LEU A 1 1948 ? 198.811 181.230 151.054 1.00 18.05  ? 1948 LEU A N     1 
ATOM   5037  C CA    . LEU A 1 1948 ? 199.712 180.838 152.134 1.00 18.05  ? 1948 LEU A CA    1 
ATOM   5038  C C     . LEU A 1 1948 ? 200.954 180.157 151.582 1.00 18.05  ? 1948 LEU A C     1 
ATOM   5039  O O     . LEU A 1 1948 ? 202.069 180.400 152.056 1.00 18.05  ? 1948 LEU A O     1 
ATOM   5040  C CB    . LEU A 1 1948 ? 198.994 179.911 153.114 1.00 18.05  ? 1948 LEU A CB    1 
ATOM   5041  C CG    . LEU A 1 1948 ? 197.864 180.494 153.959 1.00 18.05  ? 1948 LEU A CG    1 
ATOM   5042  C CD1   . LEU A 1 1948 ? 197.273 179.422 154.855 1.00 18.05  ? 1948 LEU A CD1   1 
ATOM   5043  C CD2   . LEU A 1 1948 ? 198.360 181.666 154.780 1.00 18.05  ? 1948 LEU A CD2   1 
ATOM   5044  N N     . CYS A 1 1949 ? 200.777 179.294 150.581 1.00 23.62  ? 1949 CYS A N     1 
ATOM   5045  C CA    . CYS A 1 1949 ? 201.927 178.670 149.938 1.00 23.62  ? 1949 CYS A CA    1 
ATOM   5046  C C     . CYS A 1 1949 ? 202.802 179.697 149.231 1.00 23.62  ? 1949 CYS A C     1 
ATOM   5047  O O     . CYS A 1 1949 ? 204.032 179.585 149.260 1.00 23.62  ? 1949 CYS A O     1 
ATOM   5048  C CB    . CYS A 1 1949 ? 201.462 177.601 148.950 1.00 23.62  ? 1949 CYS A CB    1 
ATOM   5049  S SG    . CYS A 1 1949 ? 200.584 176.217 149.707 1.00 23.62  ? 1949 CYS A SG    1 
ATOM   5050  N N     . GLN A 1 1950 ? 202.193 180.700 148.597 1.00 24.30  ? 1950 GLN A N     1 
ATOM   5051  C CA    . GLN A 1 1950 ? 202.965 181.643 147.793 1.00 24.30  ? 1950 GLN A CA    1 
ATOM   5052  C C     . GLN A 1 1950 ? 203.718 182.652 148.656 1.00 24.30  ? 1950 GLN A C     1 
ATOM   5053  O O     . GLN A 1 1950 ? 204.952 182.710 148.623 1.00 24.30  ? 1950 GLN A O     1 
ATOM   5054  C CB    . GLN A 1 1950 ? 202.044 182.363 146.805 1.00 24.30  ? 1950 GLN A CB    1 
ATOM   5055  C CG    . GLN A 1 1950 ? 201.571 181.493 145.656 1.00 24.30  ? 1950 GLN A CG    1 
ATOM   5056  C CD    . GLN A 1 1950 ? 202.419 181.665 144.415 1.00 24.30  ? 1950 GLN A CD    1 
ATOM   5057  O OE1   . GLN A 1 1950 ? 202.909 182.757 144.130 1.00 24.30  ? 1950 GLN A OE1   1 
ATOM   5058  N NE2   . GLN A 1 1950 ? 202.601 180.582 143.668 1.00 24.30  ? 1950 GLN A NE2   1 
ATOM   5059  N N     . VAL A 1 1951 ? 202.993 183.464 149.429 1.00 20.31  ? 1951 VAL A N     1 
ATOM   5060  C CA    . VAL A 1 1951 ? 203.643 184.538 150.177 1.00 20.31  ? 1951 VAL A CA    1 
ATOM   5061  C C     . VAL A 1 1951 ? 204.479 183.973 151.321 1.00 20.31  ? 1951 VAL A C     1 
ATOM   5062  O O     . VAL A 1 1951 ? 205.544 184.508 151.650 1.00 20.31  ? 1951 VAL A O     1 
ATOM   5063  C CB    . VAL A 1 1951 ? 202.608 185.566 150.674 1.00 20.31  ? 1951 VAL A CB    1 
ATOM   5064  C CG1   . VAL A 1 1951 ? 201.653 184.954 151.682 1.00 20.31  ? 1951 VAL A CG1   1 
ATOM   5065  C CG2   . VAL A 1 1951 ? 203.308 186.775 151.271 1.00 20.31  ? 1951 VAL A CG2   1 
ATOM   5066  N N     . GLY A 1 1952 ? 204.020 182.890 151.942 1.00 17.98  ? 1952 GLY A N     1 
ATOM   5067  C CA    . GLY A 1 1952 ? 204.740 182.305 153.055 1.00 17.98  ? 1952 GLY A CA    1 
ATOM   5068  C C     . GLY A 1 1952 ? 204.206 182.740 154.402 1.00 17.98  ? 1952 GLY A C     1 
ATOM   5069  O O     . GLY A 1 1952 ? 204.975 183.098 155.299 1.00 17.98  ? 1952 GLY A O     1 
ATOM   5070  N N     . ALA A 1 1953 ? 202.887 182.716 154.555 1.00 12.46  ? 1953 ALA A N     1 
ATOM   5071  C CA    . ALA A 1 1953 ? 202.234 183.095 155.794 1.00 12.46  ? 1953 ALA A CA    1 
ATOM   5072  C C     . ALA A 1 1953 ? 201.805 181.845 156.557 1.00 12.46  ? 1953 ALA A C     1 
ATOM   5073  O O     . ALA A 1 1953 ? 201.990 180.713 156.106 1.00 12.46  ? 1953 ALA A O     1 
ATOM   5074  C CB    . ALA A 1 1953 ? 201.043 184.010 155.510 1.00 12.46  ? 1953 ALA A CB    1 
ATOM   5075  N N     . TRP A 1 1954 ? 201.224 182.055 157.732 1.00 11.36  ? 1954 TRP A N     1 
ATOM   5076  C CA    . TRP A 1 1954 ? 200.775 180.966 158.584 1.00 11.36  ? 1954 TRP A CA    1 
ATOM   5077  C C     . TRP A 1 1954 ? 199.259 180.838 158.530 1.00 11.36  ? 1954 TRP A C     1 
ATOM   5078  O O     . TRP A 1 1954 ? 198.541 181.819 158.325 1.00 11.36  ? 1954 TRP A O     1 
ATOM   5079  C CB    . TRP A 1 1954 ? 201.221 181.181 160.031 1.00 11.36  ? 1954 TRP A CB    1 
ATOM   5080  C CG    . TRP A 1 1954 ? 202.669 180.909 160.263 1.00 11.36  ? 1954 TRP A CG    1 
ATOM   5081  C CD1   . TRP A 1 1954 ? 203.665 180.921 159.334 1.00 11.36  ? 1954 TRP A CD1   1 
ATOM   5082  C CD2   . TRP A 1 1954 ? 203.287 180.577 161.510 1.00 11.36  ? 1954 TRP A CD2   1 
ATOM   5083  N NE1   . TRP A 1 1954 ? 204.867 180.621 159.925 1.00 11.36  ? 1954 TRP A NE1   1 
ATOM   5084  C CE2   . TRP A 1 1954 ? 204.661 180.405 161.261 1.00 11.36  ? 1954 TRP A CE2   1 
ATOM   5085  C CE3   . TRP A 1 1954 ? 202.812 180.413 162.813 1.00 11.36  ? 1954 TRP A CE3   1 
ATOM   5086  C CZ2   . TRP A 1 1954 ? 205.564 180.076 162.265 1.00 11.36  ? 1954 TRP A CZ2   1 
ATOM   5087  C CZ3   . TRP A 1 1954 ? 203.709 180.082 163.807 1.00 11.36  ? 1954 TRP A CZ3   1 
ATOM   5088  C CH2   . TRP A 1 1954 ? 205.069 179.919 163.529 1.00 11.36  ? 1954 TRP A CH2   1 
ATOM   5089  N N     . GLY A 1 1955 ? 198.779 179.613 158.719 1.00 34.96  ? 1955 GLY A N     1 
ATOM   5090  C CA    . GLY A 1 1955 ? 197.354 179.358 158.731 1.00 34.96  ? 1955 GLY A CA    1 
ATOM   5091  C C     . GLY A 1 1955 ? 196.931 178.482 159.889 1.00 34.96  ? 1955 GLY A C     1 
ATOM   5092  O O     . GLY A 1 1955 ? 197.385 177.341 160.009 1.00 34.96  ? 1955 GLY A O     1 
ATOM   5093  N N     . CYS A 1 1956 ? 196.061 179.002 160.749 1.00 22.53  ? 1956 CYS A N     1 
ATOM   5094  C CA    . CYS A 1 1956 ? 195.596 178.290 161.930 1.00 22.53  ? 1956 CYS A CA    1 
ATOM   5095  C C     . CYS A 1 1956 ? 194.088 178.111 161.853 1.00 22.53  ? 1956 CYS A C     1 
ATOM   5096  O O     . CYS A 1 1956 ? 193.362 179.061 161.548 1.00 22.53  ? 1956 CYS A O     1 
ATOM   5097  C CB    . CYS A 1 1956 ? 195.973 179.042 163.208 1.00 22.53  ? 1956 CYS A CB    1 
ATOM   5098  S SG    . CYS A 1 1956 ? 195.261 178.349 164.715 1.00 22.53  ? 1956 CYS A SG    1 
ATOM   5099  N N     . PHE A 1 1957 ? 193.624 176.896 162.127 1.00 19.21  ? 1957 PHE A N     1 
ATOM   5100  C CA    . PHE A 1 1957 ? 192.201 176.593 162.183 1.00 19.21  ? 1957 PHE A CA    1 
ATOM   5101  C C     . PHE A 1 1957 ? 191.746 176.647 163.633 1.00 19.21  ? 1957 PHE A C     1 
ATOM   5102  O O     . PHE A 1 1957 ? 192.366 176.027 164.501 1.00 19.21  ? 1957 PHE A O     1 
ATOM   5103  C CB    . PHE A 1 1957 ? 191.907 175.218 161.585 1.00 19.21  ? 1957 PHE A CB    1 
ATOM   5104  C CG    . PHE A 1 1957 ? 192.160 175.131 160.109 1.00 19.21  ? 1957 PHE A CG    1 
ATOM   5105  C CD1   . PHE A 1 1957 ? 193.447 174.997 159.619 1.00 19.21  ? 1957 PHE A CD1   1 
ATOM   5106  C CD2   . PHE A 1 1957 ? 191.110 175.184 159.211 1.00 19.21  ? 1957 PHE A CD2   1 
ATOM   5107  C CE1   . PHE A 1 1957 ? 193.681 174.917 158.262 1.00 19.21  ? 1957 PHE A CE1   1 
ATOM   5108  C CE2   . PHE A 1 1957 ? 191.339 175.105 157.854 1.00 19.21  ? 1957 PHE A CE2   1 
ATOM   5109  C CZ    . PHE A 1 1957 ? 192.625 174.971 157.380 1.00 19.21  ? 1957 PHE A CZ    1 
ATOM   5110  N N     . ASP A 1 1958 ? 190.670 177.392 163.894 1.00 23.47  ? 1958 ASP A N     1 
ATOM   5111  C CA    . ASP A 1 1958 ? 190.219 177.575 165.270 1.00 23.47  ? 1958 ASP A CA    1 
ATOM   5112  C C     . ASP A 1 1958 ? 189.803 176.250 165.896 1.00 23.47  ? 1958 ASP A C     1 
ATOM   5113  O O     . ASP A 1 1958 ? 190.248 175.903 166.995 1.00 23.47  ? 1958 ASP A O     1 
ATOM   5114  C CB    . ASP A 1 1958 ? 189.070 178.580 165.323 1.00 23.47  ? 1958 ASP A CB    1 
ATOM   5115  C CG    . ASP A 1 1958 ? 189.041 179.357 166.623 1.00 23.47  ? 1958 ASP A CG    1 
ATOM   5116  O OD1   . ASP A 1 1958 ? 189.902 179.097 167.489 1.00 23.47  ? 1958 ASP A OD1   1 
ATOM   5117  O OD2   . ASP A 1 1958 ? 188.156 180.223 166.786 1.00 23.47  ? 1958 ASP A OD2   1 
ATOM   5118  N N     . GLU A 1 1959 ? 188.951 175.493 165.209 1.00 26.77  ? 1959 GLU A N     1 
ATOM   5119  C CA    . GLU A 1 1959 ? 188.522 174.184 165.696 1.00 26.77  ? 1959 GLU A CA    1 
ATOM   5120  C C     . GLU A 1 1959 ? 188.192 173.326 164.485 1.00 26.77  ? 1959 GLU A C     1 
ATOM   5121  O O     . GLU A 1 1959 ? 187.124 173.481 163.887 1.00 26.77  ? 1959 GLU A O     1 
ATOM   5122  C CB    . GLU A 1 1959 ? 187.322 174.304 166.631 1.00 26.77  ? 1959 GLU A CB    1 
ATOM   5123  C CG    . GLU A 1 1959 ? 187.690 174.463 168.095 1.00 26.77  ? 1959 GLU A CG    1 
ATOM   5124  C CD    . GLU A 1 1959 ? 186.517 174.225 169.023 1.00 26.77  ? 1959 GLU A CD    1 
ATOM   5125  O OE1   . GLU A 1 1959 ? 185.951 173.113 168.995 1.00 26.77  ? 1959 GLU A OE1   1 
ATOM   5126  O OE2   . GLU A 1 1959 ? 186.163 175.150 169.783 1.00 26.77  ? 1959 GLU A OE2   1 
ATOM   5127  N N     . PHE A 1 1960 ? 189.105 172.421 164.131 1.00 26.53  ? 1960 PHE A N     1 
ATOM   5128  C CA    . PHE A 1 1960 ? 188.920 171.614 162.931 1.00 26.53  ? 1960 PHE A CA    1 
ATOM   5129  C C     . PHE A 1 1960 ? 187.766 170.632 163.077 1.00 26.53  ? 1960 PHE A C     1 
ATOM   5130  O O     . PHE A 1 1960 ? 187.103 170.310 162.085 1.00 26.53  ? 1960 PHE A O     1 
ATOM   5131  C CB    . PHE A 1 1960 ? 190.209 170.868 162.606 1.00 26.53  ? 1960 PHE A CB    1 
ATOM   5132  C CG    . PHE A 1 1960 ? 190.403 170.598 161.146 1.00 26.53  ? 1960 PHE A CG    1 
ATOM   5133  C CD1   . PHE A 1 1960 ? 190.395 171.634 160.231 1.00 26.53  ? 1960 PHE A CD1   1 
ATOM   5134  C CD2   . PHE A 1 1960 ? 190.608 169.309 160.689 1.00 26.53  ? 1960 PHE A CD2   1 
ATOM   5135  C CE1   . PHE A 1 1960 ? 190.578 171.389 158.887 1.00 26.53  ? 1960 PHE A CE1   1 
ATOM   5136  C CE2   . PHE A 1 1960 ? 190.793 169.058 159.346 1.00 26.53  ? 1960 PHE A CE2   1 
ATOM   5137  C CZ    . PHE A 1 1960 ? 190.778 170.100 158.444 1.00 26.53  ? 1960 PHE A CZ    1 
ATOM   5138  N N     . ASN A 1 1961 ? 187.509 170.146 164.292 1.00 27.61  ? 1961 ASN A N     1 
ATOM   5139  C CA    . ASN A 1 1961 ? 186.441 169.172 164.485 1.00 27.61  ? 1961 ASN A CA    1 
ATOM   5140  C C     . ASN A 1 1961 ? 185.058 169.773 164.268 1.00 27.61  ? 1961 ASN A C     1 
ATOM   5141  O O     . ASN A 1 1961 ? 184.091 169.022 164.102 1.00 27.61  ? 1961 ASN A O     1 
ATOM   5142  C CB    . ASN A 1 1961 ? 186.536 168.555 165.881 1.00 27.61  ? 1961 ASN A CB    1 
ATOM   5143  C CG    . ASN A 1 1961 ? 186.512 169.594 166.981 1.00 27.61  ? 1961 ASN A CG    1 
ATOM   5144  O OD1   . ASN A 1 1961 ? 187.536 170.193 167.306 1.00 27.61  ? 1961 ASN A OD1   1 
ATOM   5145  N ND2   . ASN A 1 1961 ? 185.340 169.811 167.565 1.00 27.61  ? 1961 ASN A ND2   1 
ATOM   5146  N N     . ARG A 1 1962 ? 184.939 171.102 164.262 1.00 33.42  ? 1962 ARG A N     1 
ATOM   5147  C CA    . ARG A 1 1962 ? 183.662 171.741 163.977 1.00 33.42  ? 1962 ARG A CA    1 
ATOM   5148  C C     . ARG A 1 1962 ? 183.268 171.642 162.510 1.00 33.42  ? 1962 ARG A C     1 
ATOM   5149  O O     . ARG A 1 1962 ? 182.105 171.897 162.181 1.00 33.42  ? 1962 ARG A O     1 
ATOM   5150  C CB    . ARG A 1 1962 ? 183.703 173.211 164.393 1.00 33.42  ? 1962 ARG A CB    1 
ATOM   5151  C CG    . ARG A 1 1962 ? 183.859 173.431 165.885 1.00 33.42  ? 1962 ARG A CG    1 
ATOM   5152  C CD    . ARG A 1 1962 ? 182.578 173.083 166.630 1.00 33.42  ? 1962 ARG A CD    1 
ATOM   5153  N NE    . ARG A 1 1962 ? 181.512 174.057 166.420 1.00 33.42  ? 1962 ARG A NE    1 
ATOM   5154  C CZ    . ARG A 1 1962 ? 181.555 175.329 166.797 1.00 33.42  ? 1962 ARG A CZ    1 
ATOM   5155  N NH1   . ARG A 1 1962 ? 182.589 175.822 167.461 1.00 33.42  ? 1962 ARG A NH1   1 
ATOM   5156  N NH2   . ARG A 1 1962 ? 180.529 176.125 166.510 1.00 33.42  ? 1962 ARG A NH2   1 
ATOM   5157  N N     . LEU A 1 1963 ? 184.199 171.291 161.629 1.00 35.87  ? 1963 LEU A N     1 
ATOM   5158  C CA    . LEU A 1 1963 ? 183.895 171.189 160.211 1.00 35.87  ? 1963 LEU A CA    1 
ATOM   5159  C C     . LEU A 1 1963 ? 182.987 169.994 159.942 1.00 35.87  ? 1963 LEU A C     1 
ATOM   5160  O O     . LEU A 1 1963 ? 183.087 168.951 160.593 1.00 35.87  ? 1963 LEU A O     1 
ATOM   5161  C CB    . LEU A 1 1963 ? 185.186 171.051 159.406 1.00 35.87  ? 1963 LEU A CB    1 
ATOM   5162  C CG    . LEU A 1 1963 ? 185.991 172.323 159.141 1.00 35.87  ? 1963 LEU A CG    1 
ATOM   5163  C CD1   . LEU A 1 1963 ? 187.011 172.084 158.043 1.00 35.87  ? 1963 LEU A CD1   1 
ATOM   5164  C CD2   . LEU A 1 1963 ? 185.074 173.474 158.779 1.00 35.87  ? 1963 LEU A CD2   1 
ATOM   5165  N N     . GLU A 1 1964 ? 182.092 170.149 158.969 1.00 44.71  ? 1964 GLU A N     1 
ATOM   5166  C CA    . GLU A 1 1964 ? 181.240 169.037 158.574 1.00 44.71  ? 1964 GLU A CA    1 
ATOM   5167  C C     . GLU A 1 1964 ? 182.059 167.981 157.839 1.00 44.71  ? 1964 GLU A C     1 
ATOM   5168  O O     . GLU A 1 1964 ? 183.142 168.256 157.317 1.00 44.71  ? 1964 GLU A O     1 
ATOM   5169  C CB    . GLU A 1 1964 ? 180.065 169.510 157.711 1.00 44.71  ? 1964 GLU A CB    1 
ATOM   5170  C CG    . GLU A 1 1964 ? 180.412 170.387 156.514 1.00 44.71  ? 1964 GLU A CG    1 
ATOM   5171  C CD    . GLU A 1 1964 ? 180.781 171.811 156.897 1.00 44.71  ? 1964 GLU A CD    1 
ATOM   5172  O OE1   . GLU A 1 1964 ? 180.763 172.131 158.105 1.00 44.71  ? 1964 GLU A OE1   1 
ATOM   5173  O OE2   . GLU A 1 1964 ? 181.086 172.611 155.989 1.00 44.71  ? 1964 GLU A OE2   1 
ATOM   5174  N N     . GLU A 1 1965 ? 181.520 166.760 157.805 1.00 48.56  ? 1965 GLU A N     1 
ATOM   5175  C CA    . GLU A 1 1965 ? 182.321 165.583 157.474 1.00 48.56  ? 1965 GLU A CA    1 
ATOM   5176  C C     . GLU A 1 1965 ? 182.986 165.701 156.106 1.00 48.56  ? 1965 GLU A C     1 
ATOM   5177  O O     . GLU A 1 1965 ? 184.201 165.520 155.978 1.00 48.56  ? 1965 GLU A O     1 
ATOM   5178  C CB    . GLU A 1 1965 ? 181.443 164.331 157.541 1.00 48.56  ? 1965 GLU A CB    1 
ATOM   5179  C CG    . GLU A 1 1965 ? 182.220 163.031 157.670 1.00 48.56  ? 1965 GLU A CG    1 
ATOM   5180  C CD    . GLU A 1 1965 ? 183.107 162.991 158.902 1.00 48.56  ? 1965 GLU A CD    1 
ATOM   5181  O OE1   . GLU A 1 1965 ? 184.141 162.292 158.866 1.00 48.56  ? 1965 GLU A OE1   1 
ATOM   5182  O OE2   . GLU A 1 1965 ? 182.770 163.649 159.910 1.00 48.56  ? 1965 GLU A OE2   1 
ATOM   5183  N N     . ARG A 1 1966 ? 182.201 166.000 155.068 1.00 49.70  ? 1966 ARG A N     1 
ATOM   5184  C CA    . ARG A 1 1966 ? 182.762 166.114 153.723 1.00 49.70  ? 1966 ARG A CA    1 
ATOM   5185  C C     . ARG A 1 1966 ? 183.708 167.305 153.609 1.00 49.70  ? 1966 ARG A C     1 
ATOM   5186  O O     . ARG A 1 1966 ? 184.781 167.203 152.993 1.00 49.70  ? 1966 ARG A O     1 
ATOM   5187  C CB    . ARG A 1 1966 ? 181.629 166.210 152.700 1.00 49.70  ? 1966 ARG A CB    1 
ATOM   5188  C CG    . ARG A 1 1966 ? 180.480 167.112 153.134 1.00 49.70  ? 1966 ARG A CG    1 
ATOM   5189  C CD    . ARG A 1 1966 ? 179.915 167.931 151.981 1.00 49.70  ? 1966 ARG A CD    1 
ATOM   5190  N NE    . ARG A 1 1966 ? 180.570 169.226 151.836 1.00 49.70  ? 1966 ARG A NE    1 
ATOM   5191  C CZ    . ARG A 1 1966 ? 180.382 170.048 150.812 1.00 49.70  ? 1966 ARG A CZ    1 
ATOM   5192  N NH1   . ARG A 1 1966 ? 179.576 169.733 149.812 1.00 49.70  ? 1966 ARG A NH1   1 
ATOM   5193  N NH2   . ARG A 1 1966 ? 181.013 171.218 150.796 1.00 49.70  ? 1966 ARG A NH2   1 
ATOM   5194  N N     . MET A 1 1967 ? 183.331 168.440 154.205 1.00 42.92  ? 1967 MET A N     1 
ATOM   5195  C CA    . MET A 1 1967 ? 184.207 169.606 154.202 1.00 42.92  ? 1967 MET A CA    1 
ATOM   5196  C C     . MET A 1 1967 ? 185.504 169.289 154.931 1.00 42.92  ? 1967 MET A C     1 
ATOM   5197  O O     . MET A 1 1967 ? 186.595 169.668 154.488 1.00 42.92  ? 1967 MET A O     1 
ATOM   5198  C CB    . MET A 1 1967 ? 183.503 170.787 154.867 1.00 42.92  ? 1967 MET A CB    1 
ATOM   5199  C CG    . MET A 1 1967 ? 184.236 172.111 154.782 1.00 42.92  ? 1967 MET A CG    1 
ATOM   5200  S SD    . MET A 1 1967 ? 184.297 172.639 153.062 1.00 42.92  ? 1967 MET A SD    1 
ATOM   5201  C CE    . MET A 1 1967 ? 185.712 173.724 153.039 1.00 42.92  ? 1967 MET A CE    1 
ATOM   5202  N N     . LEU A 1 1968 ? 185.395 168.591 156.063 1.00 36.00  ? 1968 LEU A N     1 
ATOM   5203  C CA    . LEU A 1 1968 ? 186.577 168.207 156.825 1.00 36.00  ? 1968 LEU A CA    1 
ATOM   5204  C C     . LEU A 1 1968 ? 187.479 167.297 156.005 1.00 36.00  ? 1968 LEU A C     1 
ATOM   5205  O O     . LEU A 1 1968 ? 188.703 167.455 156.010 1.00 36.00  ? 1968 LEU A O     1 
ATOM   5206  C CB    . LEU A 1 1968 ? 186.152 167.532 158.131 1.00 36.00  ? 1968 LEU A CB    1 
ATOM   5207  C CG    . LEU A 1 1968 ? 187.197 167.182 159.191 1.00 36.00  ? 1968 LEU A CG    1 
ATOM   5208  C CD1   . LEU A 1 1968 ? 186.547 167.181 160.561 1.00 36.00  ? 1968 LEU A CD1   1 
ATOM   5209  C CD2   . LEU A 1 1968 ? 187.822 165.824 158.922 1.00 36.00  ? 1968 LEU A CD2   1 
ATOM   5210  N N     . SER A 1 1969 ? 186.891 166.336 155.289 1.00 35.52  ? 1969 SER A N     1 
ATOM   5211  C CA    . SER A 1 1969 ? 187.693 165.426 154.478 1.00 35.52  ? 1969 SER A CA    1 
ATOM   5212  C C     . SER A 1 1969 ? 188.418 166.168 153.362 1.00 35.52  ? 1969 SER A C     1 
ATOM   5213  O O     . SER A 1 1969 ? 189.601 165.914 153.102 1.00 35.52  ? 1969 SER A O     1 
ATOM   5214  C CB    . SER A 1 1969 ? 186.810 164.321 153.900 1.00 35.52  ? 1969 SER A CB    1 
ATOM   5215  O OG    . SER A 1 1969 ? 187.481 163.617 152.869 1.00 35.52  ? 1969 SER A OG    1 
ATOM   5216  N N     . ALA A 1 1970 ? 187.730 167.094 152.694 1.00 33.27  ? 1970 ALA A N     1 
ATOM   5217  C CA    . ALA A 1 1970 ? 188.362 167.820 151.595 1.00 33.27  ? 1970 ALA A CA    1 
ATOM   5218  C C     . ALA A 1 1970 ? 189.469 168.744 152.100 1.00 33.27  ? 1970 ALA A C     1 
ATOM   5219  O O     . ALA A 1 1970 ? 190.553 168.820 151.502 1.00 33.27  ? 1970 ALA A O     1 
ATOM   5220  C CB    . ALA A 1 1970 ? 187.312 168.604 150.817 1.00 33.27  ? 1970 ALA A CB    1 
ATOM   5221  N N     . VAL A 1 1971 ? 189.216 169.458 153.200 1.00 30.47  ? 1971 VAL A N     1 
ATOM   5222  C CA    . VAL A 1 1971 ? 190.258 170.313 153.757 1.00 30.47  ? 1971 VAL A CA    1 
ATOM   5223  C C     . VAL A 1 1971 ? 191.424 169.476 154.257 1.00 30.47  ? 1971 VAL A C     1 
ATOM   5224  O O     . VAL A 1 1971 ? 192.582 169.890 154.145 1.00 30.47  ? 1971 VAL A O     1 
ATOM   5225  C CB    . VAL A 1 1971 ? 189.694 171.217 154.867 1.00 30.47  ? 1971 VAL A CB    1 
ATOM   5226  C CG1   . VAL A 1 1971 ? 190.790 172.099 155.434 1.00 30.47  ? 1971 VAL A CG1   1 
ATOM   5227  C CG2   . VAL A 1 1971 ? 188.586 172.081 154.321 1.00 30.47  ? 1971 VAL A CG2   1 
ATOM   5228  N N     . SER A 1 1972 ? 191.153 168.290 154.805 1.00 28.73  ? 1972 SER A N     1 
ATOM   5229  C CA    . SER A 1 1972 ? 192.233 167.403 155.216 1.00 28.73  ? 1972 SER A CA    1 
ATOM   5230  C C     . SER A 1 1972 ? 193.054 166.949 154.020 1.00 28.73  ? 1972 SER A C     1 
ATOM   5231  O O     . SER A 1 1972 ? 194.277 166.835 154.113 1.00 28.73  ? 1972 SER A O     1 
ATOM   5232  C CB    . SER A 1 1972 ? 191.668 166.200 155.970 1.00 28.73  ? 1972 SER A CB    1 
ATOM   5233  O OG    . SER A 1 1972 ? 190.739 166.610 156.957 1.00 28.73  ? 1972 SER A OG    1 
ATOM   5234  N N     . GLN A 1 1973 ? 192.401 166.682 152.888 1.00 27.28  ? 1973 GLN A N     1 
ATOM   5235  C CA    . GLN A 1 1973 ? 193.135 166.316 151.679 1.00 27.28  ? 1973 GLN A CA    1 
ATOM   5236  C C     . GLN A 1 1973 ? 194.044 167.454 151.223 1.00 27.28  ? 1973 GLN A C     1 
ATOM   5237  O O     . GLN A 1 1973 ? 195.220 167.238 150.894 1.00 27.28  ? 1973 GLN A O     1 
ATOM   5238  C CB    . GLN A 1 1973 ? 192.151 165.933 150.574 1.00 27.28  ? 1973 GLN A CB    1 
ATOM   5239  C CG    . GLN A 1 1973 ? 192.799 165.462 149.284 1.00 27.28  ? 1973 GLN A CG    1 
ATOM   5240  C CD    . GLN A 1 1973 ? 193.622 164.204 149.471 1.00 27.28  ? 1973 GLN A CD    1 
ATOM   5241  O OE1   . GLN A 1 1973 ? 194.852 164.251 149.494 1.00 27.28  ? 1973 GLN A OE1   1 
ATOM   5242  N NE2   . GLN A 1 1973 ? 192.945 163.071 149.609 1.00 27.28  ? 1973 GLN A NE2   1 
ATOM   5243  N N     . GLN A 1 1974 ? 193.515 168.680 151.206 1.00 26.72  ? 1974 GLN A N     1 
ATOM   5244  C CA    . GLN A 1 1974 ? 194.328 169.825 150.797 1.00 26.72  ? 1974 GLN A CA    1 
ATOM   5245  C C     . GLN A 1 1974 ? 195.494 170.050 151.755 1.00 26.72  ? 1974 GLN A C     1 
ATOM   5246  O O     . GLN A 1 1974 ? 196.629 170.305 151.326 1.00 26.72  ? 1974 GLN A O     1 
ATOM   5247  C CB    . GLN A 1 1974 ? 193.461 171.079 150.708 1.00 26.72  ? 1974 GLN A CB    1 
ATOM   5248  C CG    . GLN A 1 1974 ? 192.508 171.093 149.529 1.00 26.72  ? 1974 GLN A CG    1 
ATOM   5249  C CD    . GLN A 1 1974 ? 191.871 172.448 149.316 1.00 26.72  ? 1974 GLN A CD    1 
ATOM   5250  O OE1   . GLN A 1 1974 ? 191.531 173.144 150.272 1.00 26.72  ? 1974 GLN A OE1   1 
ATOM   5251  N NE2   . GLN A 1 1974 ? 191.702 172.831 148.057 1.00 26.72  ? 1974 GLN A NE2   1 
ATOM   5252  N N     . VAL A 1 1975 ? 195.229 169.955 153.060 1.00 23.78  ? 1975 VAL A N     1 
ATOM   5253  C CA    . VAL A 1 1975 ? 196.273 170.142 154.061 1.00 23.78  ? 1975 VAL A CA    1 
ATOM   5254  C C     . VAL A 1 1975 ? 197.316 169.041 153.947 1.00 23.78  ? 1975 VAL A C     1 
ATOM   5255  O O     . VAL A 1 1975 ? 198.512 169.280 154.133 1.00 23.78  ? 1975 VAL A O     1 
ATOM   5256  C CB    . VAL A 1 1975 ? 195.650 170.201 155.469 1.00 23.78  ? 1975 VAL A CB    1 
ATOM   5257  C CG1   . VAL A 1 1975 ? 196.707 170.000 156.537 1.00 23.78  ? 1975 VAL A CG1   1 
ATOM   5258  C CG2   . VAL A 1 1975 ? 194.936 171.524 155.673 1.00 23.78  ? 1975 VAL A CG2   1 
ATOM   5259  N N     . GLN A 1 1976 ? 196.883 167.819 153.633 1.00 26.01  ? 1976 GLN A N     1 
ATOM   5260  C CA    . GLN A 1 1976 ? 197.822 166.723 153.433 1.00 26.01  ? 1976 GLN A CA    1 
ATOM   5261  C C     . GLN A 1 1976 ? 198.724 166.987 152.239 1.00 26.01  ? 1976 GLN A C     1 
ATOM   5262  O O     . GLN A 1 1976 ? 199.930 166.730 152.300 1.00 26.01  ? 1976 GLN A O     1 
ATOM   5263  C CB    . GLN A 1 1976 ? 197.062 165.411 153.249 1.00 26.01  ? 1976 GLN A CB    1 
ATOM   5264  C CG    . GLN A 1 1976 ? 197.952 164.212 152.994 1.00 26.01  ? 1976 GLN A CG    1 
ATOM   5265  C CD    . GLN A 1 1976 ? 197.190 163.039 152.414 1.00 26.01  ? 1976 GLN A CD    1 
ATOM   5266  O OE1   . GLN A 1 1976 ? 196.060 162.761 152.813 1.00 26.01  ? 1976 GLN A OE1   1 
ATOM   5267  N NE2   . GLN A 1 1976 ? 197.805 162.346 151.464 1.00 26.01  ? 1976 GLN A NE2   1 
ATOM   5268  N N     . CYS A 1 1977 ? 198.161 167.500 151.144 1.00 27.36  ? 1977 CYS A N     1 
ATOM   5269  C CA    . CYS A 1 1977 ? 198.989 167.843 149.989 1.00 27.36  ? 1977 CYS A CA    1 
ATOM   5270  C C     . CYS A 1 1977 ? 200.022 168.905 150.355 1.00 27.36  ? 1977 CYS A C     1 
ATOM   5271  O O     . CYS A 1 1977 ? 201.219 168.762 150.061 1.00 27.36  ? 1977 CYS A O     1 
ATOM   5272  C CB    . CYS A 1 1977 ? 198.109 168.323 148.836 1.00 27.36  ? 1977 CYS A CB    1 
ATOM   5273  S SG    . CYS A 1 1977 ? 197.000 167.064 148.165 1.00 27.36  ? 1977 CYS A SG    1 
ATOM   5274  N N     . ILE A 1 1978 ? 199.575 169.970 151.024 1.00 24.99  ? 1978 ILE A N     1 
ATOM   5275  C CA    . ILE A 1 1978 ? 200.484 171.056 151.389 1.00 24.99  ? 1978 ILE A CA    1 
ATOM   5276  C C     . ILE A 1 1978 ? 201.569 170.553 152.334 1.00 24.99  ? 1978 ILE A C     1 
ATOM   5277  O O     . ILE A 1 1978 ? 202.753 170.885 152.185 1.00 24.99  ? 1978 ILE A O     1 
ATOM   5278  C CB    . ILE A 1 1978 ? 199.695 172.224 152.008 1.00 24.99  ? 1978 ILE A CB    1 
ATOM   5279  C CG1   . ILE A 1 1978 ? 198.757 172.842 150.971 1.00 24.99  ? 1978 ILE A CG1   1 
ATOM   5280  C CG2   . ILE A 1 1978 ? 200.643 173.270 152.555 1.00 24.99  ? 1978 ILE A CG2   1 
ATOM   5281  C CD1   . ILE A 1 1978 ? 198.137 174.146 151.412 1.00 24.99  ? 1978 ILE A CD1   1 
ATOM   5282  N N     . GLN A 1 1979 ? 201.187 169.736 153.316 1.00 22.99  ? 1979 GLN A N     1 
ATOM   5283  C CA    . GLN A 1 1979 ? 202.142 169.275 154.312 1.00 22.99  ? 1979 GLN A CA    1 
ATOM   5284  C C     . GLN A 1 1979 ? 203.104 168.251 153.730 1.00 22.99  ? 1979 GLN A C     1 
ATOM   5285  O O     . GLN A 1 1979 ? 204.263 168.191 154.147 1.00 22.99  ? 1979 GLN A O     1 
ATOM   5286  C CB    . GLN A 1 1979 ? 201.401 168.697 155.515 1.00 22.99  ? 1979 GLN A CB    1 
ATOM   5287  C CG    . GLN A 1 1979 ? 202.289 168.459 156.709 1.00 22.99  ? 1979 GLN A CG    1 
ATOM   5288  C CD    . GLN A 1 1979 ? 202.908 169.744 157.208 1.00 22.99  ? 1979 GLN A CD    1 
ATOM   5289  O OE1   . GLN A 1 1979 ? 204.079 170.021 156.957 1.00 22.99  ? 1979 GLN A OE1   1 
ATOM   5290  N NE2   . GLN A 1 1979 ? 202.119 170.547 157.909 1.00 22.99  ? 1979 GLN A NE2   1 
ATOM   5291  N N     . GLU A 1 1980 ? 202.653 167.441 152.771 1.00 27.04  ? 1980 GLU A N     1 
ATOM   5292  C CA    . GLU A 1 1980 ? 203.574 166.565 152.057 1.00 27.04  ? 1980 GLU A CA    1 
ATOM   5293  C C     . GLU A 1 1980 ? 204.584 167.378 151.263 1.00 27.04  ? 1980 GLU A C     1 
ATOM   5294  O O     . GLU A 1 1980 ? 205.767 167.022 151.201 1.00 27.04  ? 1980 GLU A O     1 
ATOM   5295  C CB    . GLU A 1 1980 ? 202.799 165.621 151.139 1.00 27.04  ? 1980 GLU A CB    1 
ATOM   5296  C CG    . GLU A 1 1980 ? 202.477 164.275 151.763 1.00 27.04  ? 1980 GLU A CG    1 
ATOM   5297  C CD    . GLU A 1 1980 ? 201.284 163.603 151.113 1.00 27.04  ? 1980 GLU A CD    1 
ATOM   5298  O OE1   . GLU A 1 1980 ? 200.997 163.906 149.936 1.00 27.04  ? 1980 GLU A OE1   1 
ATOM   5299  O OE2   . GLU A 1 1980 ? 200.635 162.768 151.778 1.00 27.04  ? 1980 GLU A OE2   1 
ATOM   5300  N N     . ALA A 1 1981 ? 204.137 168.476 150.646 1.00 28.23  ? 1981 ALA A N     1 
ATOM   5301  C CA    . ALA A 1 1981 ? 205.085 169.366 149.981 1.00 28.23  ? 1981 ALA A CA    1 
ATOM   5302  C C     . ALA A 1 1981 ? 206.102 169.919 150.973 1.00 28.23  ? 1981 ALA A C     1 
ATOM   5303  O O     . ALA A 1 1981 ? 207.306 169.955 150.691 1.00 28.23  ? 1981 ALA A O     1 
ATOM   5304  C CB    . ALA A 1 1981 ? 204.340 170.503 149.283 1.00 28.23  ? 1981 ALA A CB    1 
ATOM   5305  N N     . LEU A 1 1982 ? 205.636 170.331 152.154 1.00 27.58  ? 1982 LEU A N     1 
ATOM   5306  C CA    . LEU A 1 1982 ? 206.552 170.833 153.175 1.00 27.58  ? 1982 LEU A CA    1 
ATOM   5307  C C     . LEU A 1 1982 ? 207.537 169.756 153.620 1.00 27.58  ? 1982 LEU A C     1 
ATOM   5308  O O     . LEU A 1 1982 ? 208.715 170.045 153.862 1.00 27.58  ? 1982 LEU A O     1 
ATOM   5309  C CB    . LEU A 1 1982 ? 205.768 171.367 154.374 1.00 27.58  ? 1982 LEU A CB    1 
ATOM   5310  C CG    . LEU A 1 1982 ? 205.005 172.674 154.166 1.00 27.58  ? 1982 LEU A CG    1 
ATOM   5311  C CD1   . LEU A 1 1982 ? 204.127 172.973 155.366 1.00 27.58  ? 1982 LEU A CD1   1 
ATOM   5312  C CD2   . LEU A 1 1982 ? 205.976 173.811 153.920 1.00 27.58  ? 1982 LEU A CD2   1 
ATOM   5313  N N     . ARG A 1 1983 ? 207.071 168.513 153.750 1.00 30.17  ? 1983 ARG A N     1 
ATOM   5314  C CA    . ARG A 1 1983 ? 207.961 167.422 154.138 1.00 30.17  ? 1983 ARG A CA    1 
ATOM   5315  C C     . ARG A 1 1983 ? 209.028 167.174 153.080 1.00 30.17  ? 1983 ARG A C     1 
ATOM   5316  O O     . ARG A 1 1983 ? 210.211 167.031 153.409 1.00 30.17  ? 1983 ARG A O     1 
ATOM   5317  C CB    . ARG A 1 1983 ? 207.159 166.146 154.393 1.00 30.17  ? 1983 ARG A CB    1 
ATOM   5318  C CG    . ARG A 1 1983 ? 206.255 166.208 155.607 1.00 30.17  ? 1983 ARG A CG    1 
ATOM   5319  C CD    . ARG A 1 1983 ? 207.063 166.313 156.885 1.00 30.17  ? 1983 ARG A CD    1 
ATOM   5320  N NE    . ARG A 1 1983 ? 207.949 165.171 157.072 1.00 30.17  ? 1983 ARG A NE    1 
ATOM   5321  C CZ    . ARG A 1 1983 ? 207.587 164.030 157.641 1.00 30.17  ? 1983 ARG A CZ    1 
ATOM   5322  N NH1   . ARG A 1 1983 ? 206.355 163.838 158.082 1.00 30.17  ? 1983 ARG A NH1   1 
ATOM   5323  N NH2   . ARG A 1 1983 ? 208.483 163.057 157.771 1.00 30.17  ? 1983 ARG A NH2   1 
ATOM   5324  N N     . GLU A 1 1984 ? 208.633 167.118 151.806 1.00 40.16  ? 1984 GLU A N     1 
ATOM   5325  C CA    . GLU A 1 1984 ? 209.621 166.959 150.743 1.00 40.16  ? 1984 GLU A CA    1 
ATOM   5326  C C     . GLU A 1 1984 ? 210.546 168.162 150.632 1.00 40.16  ? 1984 GLU A C     1 
ATOM   5327  O O     . GLU A 1 1984 ? 211.637 168.037 150.068 1.00 40.16  ? 1984 GLU A O     1 
ATOM   5328  C CB    . GLU A 1 1984 ? 208.940 166.703 149.396 1.00 40.16  ? 1984 GLU A CB    1 
ATOM   5329  C CG    . GLU A 1 1984 ? 207.840 165.655 149.426 1.00 40.16  ? 1984 GLU A CG    1 
ATOM   5330  C CD    . GLU A 1 1984 ? 208.369 164.241 149.275 1.00 40.16  ? 1984 GLU A CD    1 
ATOM   5331  O OE1   . GLU A 1 1984 ? 209.603 164.053 149.319 1.00 40.16  ? 1984 GLU A OE1   1 
ATOM   5332  O OE2   . GLU A 1 1984 ? 207.547 163.315 149.110 1.00 40.16  ? 1984 GLU A OE2   1 
ATOM   5333  N N     . HIS A 1 1985 ? 210.135 169.321 151.152 1.00 41.51  ? 1985 HIS A N     1 
ATOM   5334  C CA    . HIS A 1 1985 ? 211.014 170.486 151.146 1.00 41.51  ? 1985 HIS A CA    1 
ATOM   5335  C C     . HIS A 1 1985 ? 212.277 170.274 151.972 1.00 41.51  ? 1985 HIS A C     1 
ATOM   5336  O O     . HIS A 1 1985 ? 213.253 171.007 151.784 1.00 41.51  ? 1985 HIS A O     1 
ATOM   5337  C CB    . HIS A 1 1985 ? 210.267 171.716 151.664 1.00 41.51  ? 1985 HIS A CB    1 
ATOM   5338  C CG    . HIS A 1 1985 ? 210.748 173.005 151.076 1.00 41.51  ? 1985 HIS A CG    1 
ATOM   5339  N ND1   . HIS A 1 1985 ? 210.251 173.517 149.897 1.00 41.51  ? 1985 HIS A ND1   1 
ATOM   5340  C CD2   . HIS A 1 1985 ? 211.686 173.883 151.502 1.00 41.51  ? 1985 HIS A CD2   1 
ATOM   5341  C CE1   . HIS A 1 1985 ? 210.860 174.656 149.623 1.00 41.51  ? 1985 HIS A CE1   1 
ATOM   5342  N NE2   . HIS A 1 1985 ? 211.736 174.901 150.581 1.00 41.51  ? 1985 HIS A NE2   1 
ATOM   5343  N N     . SER A 1 1986 ? 212.287 169.301 152.879 1.00 49.91  ? 1986 SER A N     1 
ATOM   5344  C CA    . SER A 1 1986 ? 213.438 169.029 153.732 1.00 49.91  ? 1986 SER A CA    1 
ATOM   5345  C C     . SER A 1 1986 ? 213.934 167.600 153.557 1.00 49.91  ? 1986 SER A C     1 
ATOM   5346  O O     . SER A 1 1986 ? 214.235 166.904 154.530 1.00 49.91  ? 1986 SER A O     1 
ATOM   5347  C CB    . SER A 1 1986 ? 213.109 169.300 155.197 1.00 49.91  ? 1986 SER A CB    1 
ATOM   5348  O OG    . SER A 1 1986 ? 212.547 168.152 155.810 1.00 49.91  ? 1986 SER A OG    1 
ATOM   5349  N N     . ASN A 1 1987 ? 214.018 167.143 152.316 1.00 70.75  ? 1987 ASN A N     1 
ATOM   5350  C CA    . ASN A 1 1987 ? 214.563 165.818 152.051 1.00 70.75  ? 1987 ASN A CA    1 
ATOM   5351  C C     . ASN A 1 1987 ? 216.057 165.810 152.355 1.00 70.75  ? 1987 ASN A C     1 
ATOM   5352  O O     . ASN A 1 1987 ? 216.782 166.697 151.891 1.00 70.75  ? 1987 ASN A O     1 
ATOM   5353  C CB    . ASN A 1 1987 ? 214.316 165.419 150.599 1.00 70.75  ? 1987 ASN A CB    1 
ATOM   5354  C CG    . ASN A 1 1987 ? 212.911 164.901 150.369 1.00 70.75  ? 1987 ASN A CG    1 
ATOM   5355  O OD1   . ASN A 1 1987 ? 212.197 164.572 151.316 1.00 70.75  ? 1987 ASN A OD1   1 
ATOM   5356  N ND2   . ASN A 1 1987 ? 212.506 164.828 149.107 1.00 70.75  ? 1987 ASN A ND2   1 
ATOM   5357  N N     . PRO A 1 1988 ? 216.551 164.848 153.141 1.00 85.92  ? 1988 PRO A N     1 
ATOM   5358  C CA    . PRO A 1 1988 ? 217.997 164.820 153.427 1.00 85.92  ? 1988 PRO A CA    1 
ATOM   5359  C C     . PRO A 1 1988 ? 218.851 164.700 152.178 1.00 85.92  ? 1988 PRO A C     1 
ATOM   5360  O O     . PRO A 1 1988 ? 219.922 165.316 152.101 1.00 85.92  ? 1988 PRO A O     1 
ATOM   5361  C CB    . PRO A 1 1988 ? 218.147 163.597 154.345 1.00 85.92  ? 1988 PRO A CB    1 
ATOM   5362  C CG    . PRO A 1 1988 ? 216.937 162.759 154.077 1.00 85.92  ? 1988 PRO A CG    1 
ATOM   5363  C CD    . PRO A 1 1988 ? 215.836 163.724 153.767 1.00 85.92  ? 1988 PRO A CD    1 
ATOM   5364  N N     . ASN A 1 1989 ? 218.404 163.923 151.190 1.00 89.36  ? 1989 ASN A N     1 
ATOM   5365  C CA    . ASN A 1 1989 ? 219.129 163.831 149.928 1.00 89.36  ? 1989 ASN A CA    1 
ATOM   5366  C C     . ASN A 1 1989 ? 218.899 165.053 149.050 1.00 89.36  ? 1989 ASN A C     1 
ATOM   5367  O O     . ASN A 1 1989 ? 219.759 165.392 148.229 1.00 89.36  ? 1989 ASN A O     1 
ATOM   5368  C CB    . ASN A 1 1989 ? 218.721 162.564 149.176 1.00 89.36  ? 1989 ASN A CB    1 
ATOM   5369  C CG    . ASN A 1 1989 ? 217.218 162.384 149.113 1.00 89.36  ? 1989 ASN A CG    1 
ATOM   5370  O OD1   . ASN A 1 1989 ? 216.553 162.246 150.140 1.00 89.36  ? 1989 ASN A OD1   1 
ATOM   5371  N ND2   . ASN A 1 1989 ? 216.672 162.387 147.902 1.00 89.36  ? 1989 ASN A ND2   1 
ATOM   5372  N N     . TYR A 1 1990 ? 217.759 165.720 149.206 1.00 88.79  ? 1990 TYR A N     1 
ATOM   5373  C CA    . TYR A 1 1990 ? 217.385 166.871 148.396 1.00 88.79  ? 1990 TYR A CA    1 
ATOM   5374  C C     . TYR A 1 1990 ? 217.277 168.123 149.262 1.00 88.79  ? 1990 TYR A C     1 
ATOM   5375  O O     . TYR A 1 1990 ? 216.351 168.925 149.125 1.00 88.79  ? 1990 TYR A O     1 
ATOM   5376  C CB    . TYR A 1 1990 ? 216.082 166.594 147.644 1.00 88.79  ? 1990 TYR A CB    1 
ATOM   5377  C CG    . TYR A 1 1990 ? 215.709 167.637 146.614 1.00 88.79  ? 1990 TYR A CG    1 
ATOM   5378  C CD1   . TYR A 1 1990 ? 216.503 167.851 145.495 1.00 88.79  ? 1990 TYR A CD1   1 
ATOM   5379  C CD2   . TYR A 1 1990 ? 214.552 168.393 146.750 1.00 88.79  ? 1990 TYR A CD2   1 
ATOM   5380  C CE1   . TYR A 1 1990 ? 216.165 168.800 144.551 1.00 88.79  ? 1990 TYR A CE1   1 
ATOM   5381  C CE2   . TYR A 1 1990 ? 214.205 169.343 145.812 1.00 88.79  ? 1990 TYR A CE2   1 
ATOM   5382  C CZ    . TYR A 1 1990 ? 215.014 169.542 144.714 1.00 88.79  ? 1990 TYR A CZ    1 
ATOM   5383  O OH    . TYR A 1 1990 ? 214.671 170.486 143.777 1.00 88.79  ? 1990 TYR A OH    1 
ATOM   5384  N N     . ASP A 1 1991 ? 218.227 168.293 150.186 1.00 98.09  ? 1991 ASP A N     1 
ATOM   5385  C CA    . ASP A 1 1991 ? 218.237 169.493 151.016 1.00 98.09  ? 1991 ASP A CA    1 
ATOM   5386  C C     . ASP A 1 1991 ? 218.480 170.738 150.172 1.00 98.09  ? 1991 ASP A C     1 
ATOM   5387  O O     . ASP A 1 1991 ? 217.831 171.771 150.374 1.00 98.09  ? 1991 ASP A O     1 
ATOM   5388  C CB    . ASP A 1 1991 ? 219.296 169.366 152.112 1.00 98.09  ? 1991 ASP A CB    1 
ATOM   5389  C CG    . ASP A 1 1991 ? 219.081 170.349 153.248 1.00 98.09  ? 1991 ASP A CG    1 
ATOM   5390  O OD1   . ASP A 1 1991 ? 218.091 171.108 153.202 1.00 98.09  ? 1991 ASP A OD1   1 
ATOM   5391  O OD2   . ASP A 1 1991 ? 219.901 170.360 154.189 1.00 98.09  ? 1991 ASP A OD2   1 
ATOM   5392  N N     . LYS A 1 1992 ? 219.409 170.658 149.222 1.00 90.22  ? 1992 LYS A N     1 
ATOM   5393  C CA    . LYS A 1 1992 ? 219.642 171.740 148.267 1.00 90.22  ? 1992 LYS A CA    1 
ATOM   5394  C C     . LYS A 1 1992 ? 218.538 171.672 147.220 1.00 90.22  ? 1992 LYS A C     1 
ATOM   5395  O O     . LYS A 1 1992 ? 218.655 170.999 146.195 1.00 90.22  ? 1992 LYS A O     1 
ATOM   5396  C CB    . LYS A 1 1992 ? 221.026 171.625 147.641 1.00 90.22  ? 1992 LYS A CB    1 
ATOM   5397  C CG    . LYS A 1 1992 ? 221.338 172.698 146.607 1.00 90.22  ? 1992 LYS A CG    1 
ATOM   5398  C CD    . LYS A 1 1992 ? 221.031 174.090 147.138 1.00 90.22  ? 1992 LYS A CD    1 
ATOM   5399  C CE    . LYS A 1 1992 ? 220.871 175.090 146.003 1.00 90.22  ? 1992 LYS A CE    1 
ATOM   5400  N NZ    . LYS A 1 1992 ? 219.747 174.729 145.095 1.00 90.22  ? 1992 LYS A NZ    1 
ATOM   5401  N N     . THR A 1 1993 ? 217.442 172.375 147.492 1.00 87.64  ? 1993 THR A N     1 
ATOM   5402  C CA    . THR A 1 1993 ? 216.264 172.350 146.629 1.00 87.64  ? 1993 THR A CA    1 
ATOM   5403  C C     . THR A 1 1993 ? 216.564 173.129 145.355 1.00 87.64  ? 1993 THR A C     1 
ATOM   5404  O O     . THR A 1 1993 ? 216.595 174.361 145.356 1.00 87.64  ? 1993 THR A O     1 
ATOM   5405  C CB    . THR A 1 1993 ? 215.061 172.931 147.363 1.00 87.64  ? 1993 THR A CB    1 
ATOM   5406  O OG1   . THR A 1 1993 ? 214.770 172.131 148.515 1.00 87.64  ? 1993 THR A OG1   1 
ATOM   5407  C CG2   . THR A 1 1993 ? 213.843 172.958 146.456 1.00 87.64  ? 1993 THR A CG2   1 
ATOM   5408  N N     . SER A 1 1994 ? 216.790 172.408 144.256 1.00 83.24  ? 1994 SER A N     1 
ATOM   5409  C CA    . SER A 1 1994 ? 217.035 173.042 142.964 1.00 83.24  ? 1994 SER A CA    1 
ATOM   5410  C C     . SER A 1 1994 ? 215.730 173.249 142.200 1.00 83.24  ? 1994 SER A C     1 
ATOM   5411  O O     . SER A 1 1994 ? 215.354 174.385 141.895 1.00 83.24  ? 1994 SER A O     1 
ATOM   5412  C CB    . SER A 1 1994 ? 218.018 172.199 142.144 1.00 83.24  ? 1994 SER A CB    1 
ATOM   5413  O OG    . SER A 1 1994 ? 218.137 172.694 140.822 1.00 83.24  ? 1994 SER A OG    1 
ATOM   5414  N N     . ALA A 1 1995 ? 215.032 172.161 141.890 1.00 82.86  ? 1995 ALA A N     1 
ATOM   5415  C CA    . ALA A 1 1995 ? 213.693 172.279 141.336 1.00 82.86  ? 1995 ALA A CA    1 
ATOM   5416  C C     . ALA A 1 1995 ? 212.724 172.701 142.439 1.00 82.86  ? 1995 ALA A C     1 
ATOM   5417  O O     . ALA A 1 1995 ? 212.781 172.168 143.551 1.00 82.86  ? 1995 ALA A O     1 
ATOM   5418  C CB    . ALA A 1 1995 ? 213.245 170.956 140.717 1.00 82.86  ? 1995 ALA A CB    1 
ATOM   5419  N N     . PRO A 1 1996 ? 211.828 173.647 142.166 1.00 70.58  ? 1996 PRO A N     1 
ATOM   5420  C CA    . PRO A 1 1996 ? 210.970 174.167 143.237 1.00 70.58  ? 1996 PRO A CA    1 
ATOM   5421  C C     . PRO A 1 1996 ? 209.994 173.113 143.736 1.00 70.58  ? 1996 PRO A C     1 
ATOM   5422  O O     . PRO A 1 1996 ? 209.432 172.339 142.958 1.00 70.58  ? 1996 PRO A O     1 
ATOM   5423  C CB    . PRO A 1 1996 ? 210.238 175.344 142.580 1.00 70.58  ? 1996 PRO A CB    1 
ATOM   5424  C CG    . PRO A 1 1996 ? 210.455 175.212 141.109 1.00 70.58  ? 1996 PRO A CG    1 
ATOM   5425  C CD    . PRO A 1 1996 ? 211.410 174.096 140.829 1.00 70.58  ? 1996 PRO A CD    1 
ATOM   5426  N N     . ILE A 1 1997 ? 209.800 173.091 145.051 1.00 57.73  ? 1997 ILE A N     1 
ATOM   5427  C CA    . ILE A 1 1997 ? 208.873 172.155 145.676 1.00 57.73  ? 1997 ILE A CA    1 
ATOM   5428  C C     . ILE A 1 1997 ? 207.463 172.710 145.534 1.00 57.73  ? 1997 ILE A C     1 
ATOM   5429  O O     . ILE A 1 1997 ? 207.165 173.807 146.018 1.00 57.73  ? 1997 ILE A O     1 
ATOM   5430  C CB    . ILE A 1 1997 ? 209.231 171.920 147.149 1.00 57.73  ? 1997 ILE A CB    1 
ATOM   5431  C CG1   . ILE A 1 1997 ? 210.539 171.133 147.266 1.00 57.73  ? 1997 ILE A CG1   1 
ATOM   5432  C CG2   . ILE A 1 1997 ? 208.104 171.193 147.855 1.00 57.73  ? 1997 ILE A CG2   1 
ATOM   5433  C CD1   . ILE A 1 1997 ? 210.652 169.973 146.300 1.00 57.73  ? 1997 ILE A CD1   1 
ATOM   5434  N N     . THR A 1 1998 ? 206.593 171.955 144.868 1.00 54.24  ? 1998 THR A N     1 
ATOM   5435  C CA    . THR A 1 1998 ? 205.254 172.413 144.534 1.00 54.24  ? 1998 THR A CA    1 
ATOM   5436  C C     . THR A 1 1998 ? 204.220 171.389 144.983 1.00 54.24  ? 1998 THR A C     1 
ATOM   5437  O O     . THR A 1 1998 ? 204.530 170.219 145.218 1.00 54.24  ? 1998 THR A O     1 
ATOM   5438  C CB    . THR A 1 1998 ? 205.107 172.670 143.028 1.00 54.24  ? 1998 THR A CB    1 
ATOM   5439  O OG1   . THR A 1 1998 ? 205.188 171.425 142.324 1.00 54.24  ? 1998 THR A OG1   1 
ATOM   5440  C CG2   . THR A 1 1998 ? 206.201 173.606 142.528 1.00 54.24  ? 1998 THR A CG2   1 
ATOM   5441  N N     . CYS A 1 1999 ? 202.979 171.852 145.096 1.00 57.42  ? 1999 CYS A N     1 
ATOM   5442  C CA    . CYS A 1 1999 ? 201.843 171.036 145.498 1.00 57.42  ? 1999 CYS A CA    1 
ATOM   5443  C C     . CYS A 1 1999 ? 200.673 171.279 144.550 1.00 57.42  ? 1999 CYS A C     1 
ATOM   5444  O O     . CYS A 1 1999 ? 200.608 172.292 143.850 1.00 57.42  ? 1999 CYS A O     1 
ATOM   5445  C CB    . CYS A 1 1999 ? 201.431 171.340 146.943 1.00 57.42  ? 1999 CYS A CB    1 
ATOM   5446  S SG    . CYS A 1 1999 ? 200.774 173.004 147.183 1.00 57.42  ? 1999 CYS A SG    1 
ATOM   5447  N N     . GLU A 1 2000 ? 199.736 170.332 144.540 1.00 61.18  ? 2000 GLU A N     1 
ATOM   5448  C CA    . GLU A 1 2000 ? 198.582 170.370 143.639 1.00 61.18  ? 2000 GLU A CA    1 
ATOM   5449  C C     . GLU A 1 2000 ? 197.423 171.044 144.366 1.00 61.18  ? 2000 GLU A C     1 
ATOM   5450  O O     . GLU A 1 2000 ? 196.667 170.403 145.097 1.00 61.18  ? 2000 GLU A O     1 
ATOM   5451  C CB    . GLU A 1 2000 ? 198.195 168.968 143.175 1.00 61.18  ? 2000 GLU A CB    1 
ATOM   5452  C CG    . GLU A 1 2000 ? 199.060 168.364 142.074 1.00 61.18  ? 2000 GLU A CG    1 
ATOM   5453  C CD    . GLU A 1 2000 ? 200.539 168.364 142.402 1.00 61.18  ? 2000 GLU A CD    1 
ATOM   5454  O OE1   . GLU A 1 2000 ? 200.904 167.922 143.511 1.00 61.18  ? 2000 GLU A OE1   1 
ATOM   5455  O OE2   . GLU A 1 2000 ? 201.336 168.796 141.545 1.00 61.18  ? 2000 GLU A OE2   1 
ATOM   5456  N N     . LEU A 1 2001 ? 197.280 172.349 144.155 1.00 50.42  ? 2001 LEU A N     1 
ATOM   5457  C CA    . LEU A 1 2001 ? 196.158 173.121 144.670 1.00 50.42  ? 2001 LEU A CA    1 
ATOM   5458  C C     . LEU A 1 2001 ? 195.425 173.786 143.514 1.00 50.42  ? 2001 LEU A C     1 
ATOM   5459  O O     . LEU A 1 2001 ? 196.054 174.303 142.586 1.00 50.42  ? 2001 LEU A O     1 
ATOM   5460  C CB    . LEU A 1 2001 ? 196.616 174.181 145.680 1.00 50.42  ? 2001 LEU A CB    1 
ATOM   5461  C CG    . LEU A 1 2001 ? 196.546 173.824 147.167 1.00 50.42  ? 2001 LEU A CG    1 
ATOM   5462  C CD1   . LEU A 1 2001 ? 195.096 173.728 147.609 1.00 50.42  ? 2001 LEU A CD1   1 
ATOM   5463  C CD2   . LEU A 1 2001 ? 197.280 172.532 147.474 1.00 50.42  ? 2001 LEU A CD2   1 
ATOM   5464  N N     . LEU A 1 2002 ? 194.092 173.764 143.578 1.00 53.27  ? 2002 LEU A N     1 
ATOM   5465  C CA    . LEU A 1 2002 ? 193.232 174.319 142.530 1.00 53.27  ? 2002 LEU A CA    1 
ATOM   5466  C C     . LEU A 1 2002 ? 193.525 173.698 141.167 1.00 53.27  ? 2002 LEU A C     1 
ATOM   5467  O O     . LEU A 1 2002 ? 193.413 174.364 140.135 1.00 53.27  ? 2002 LEU A O     1 
ATOM   5468  C CB    . LEU A 1 2002 ? 193.350 175.845 142.455 1.00 53.27  ? 2002 LEU A CB    1 
ATOM   5469  C CG    . LEU A 1 2002 ? 192.666 176.649 143.562 1.00 53.27  ? 2002 LEU A CG    1 
ATOM   5470  C CD1   . LEU A 1 2002 ? 192.601 178.121 143.186 1.00 53.27  ? 2002 LEU A CD1   1 
ATOM   5471  C CD2   . LEU A 1 2002 ? 191.277 176.102 143.847 1.00 53.27  ? 2002 LEU A CD2   1 
ATOM   5472  N N     . ASN A 1 2003 ? 193.897 172.416 141.163 1.00 57.59  ? 2003 ASN A N     1 
ATOM   5473  C CA    . ASN A 1 2003 ? 194.214 171.679 139.937 1.00 57.59  ? 2003 ASN A CA    1 
ATOM   5474  C C     . ASN A 1 2003 ? 195.326 172.362 139.143 1.00 57.59  ? 2003 ASN A C     1 
ATOM   5475  O O     . ASN A 1 2003 ? 195.297 172.407 137.911 1.00 57.59  ? 2003 ASN A O     1 
ATOM   5476  C CB    . ASN A 1 2003 ? 192.969 171.485 139.069 1.00 57.59  ? 2003 ASN A CB    1 
ATOM   5477  C CG    . ASN A 1 2003 ? 191.977 170.518 139.680 1.00 57.59  ? 2003 ASN A CG    1 
ATOM   5478  O OD1   . ASN A 1 2003 ? 192.358 169.479 140.221 1.00 57.59  ? 2003 ASN A OD1   1 
ATOM   5479  N ND2   . ASN A 1 2003 ? 190.695 170.850 139.592 1.00 57.59  ? 2003 ASN A ND2   1 
ATOM   5480  N N     . LYS A 1 2004 ? 196.317 172.898 139.853 1.00 52.78  ? 2004 LYS A N     1 
ATOM   5481  C CA    . LYS A 1 2004 ? 197.458 173.535 139.212 1.00 52.78  ? 2004 LYS A CA    1 
ATOM   5482  C C     . LYS A 1 2004 ? 198.647 173.491 140.160 1.00 52.78  ? 2004 LYS A C     1 
ATOM   5483  O O     . LYS A 1 2004 ? 198.494 173.316 141.371 1.00 52.78  ? 2004 LYS A O     1 
ATOM   5484  C CB    . LYS A 1 2004 ? 197.148 174.982 138.810 1.00 52.78  ? 2004 LYS A CB    1 
ATOM   5485  C CG    . LYS A 1 2004 ? 196.928 175.919 139.982 1.00 52.78  ? 2004 LYS A CG    1 
ATOM   5486  C CD    . LYS A 1 2004 ? 196.613 177.324 139.507 1.00 52.78  ? 2004 LYS A CD    1 
ATOM   5487  C CE    . LYS A 1 2004 ? 197.845 177.980 138.912 1.00 52.78  ? 2004 LYS A CE    1 
ATOM   5488  N NZ    . LYS A 1 2004 ? 198.890 178.234 139.942 1.00 52.78  ? 2004 LYS A NZ    1 
ATOM   5489  N N     . GLN A 1 2005 ? 199.839 173.648 139.590 1.00 50.63  ? 2005 GLN A N     1 
ATOM   5490  C CA    . GLN A 1 2005 ? 201.068 173.656 140.374 1.00 50.63  ? 2005 GLN A CA    1 
ATOM   5491  C C     . GLN A 1 2005 ? 201.178 174.967 141.142 1.00 50.63  ? 2005 GLN A C     1 
ATOM   5492  O O     . GLN A 1 2005 ? 200.983 176.045 140.571 1.00 50.63  ? 2005 GLN A O     1 
ATOM   5493  C CB    . GLN A 1 2005 ? 202.278 173.459 139.466 1.00 50.63  ? 2005 GLN A CB    1 
ATOM   5494  C CG    . GLN A 1 2005 ? 202.486 172.024 139.013 1.00 50.63  ? 2005 GLN A CG    1 
ATOM   5495  C CD    . GLN A 1 2005 ? 203.294 171.213 140.005 1.00 50.63  ? 2005 GLN A CD    1 
ATOM   5496  O OE1   . GLN A 1 2005 ? 202.904 171.056 141.160 1.00 50.63  ? 2005 GLN A OE1   1 
ATOM   5497  N NE2   . GLN A 1 2005 ? 204.427 170.687 139.555 1.00 50.63  ? 2005 GLN A NE2   1 
ATOM   5498  N N     . VAL A 1 2006 ? 201.490 174.876 142.433 1.00 44.89  ? 2006 VAL A N     1 
ATOM   5499  C CA    . VAL A 1 2006 ? 201.656 176.042 143.292 1.00 44.89  ? 2006 VAL A CA    1 
ATOM   5500  C C     . VAL A 1 2006 ? 202.973 175.905 144.040 1.00 44.89  ? 2006 VAL A C     1 
ATOM   5501  O O     . VAL A 1 2006 ? 203.211 174.891 144.705 1.00 44.89  ? 2006 VAL A O     1 
ATOM   5502  C CB    . VAL A 1 2006 ? 200.490 176.196 144.287 1.00 44.89  ? 2006 VAL A CB    1 
ATOM   5503  C CG1   . VAL A 1 2006 ? 200.704 177.418 145.162 1.00 44.89  ? 2006 VAL A CG1   1 
ATOM   5504  C CG2   . VAL A 1 2006 ? 199.165 176.292 143.550 1.00 44.89  ? 2006 VAL A CG2   1 
ATOM   5505  N N     . LYS A 1 2007 ? 203.822 176.924 143.936 1.00 41.53  ? 2007 LYS A N     1 
ATOM   5506  C CA    . LYS A 1 2007 ? 205.071 176.935 144.685 1.00 41.53  ? 2007 LYS A CA    1 
ATOM   5507  C C     . LYS A 1 2007 ? 204.788 177.096 146.173 1.00 41.53  ? 2007 LYS A C     1 
ATOM   5508  O O     . LYS A 1 2007 ? 203.946 177.902 146.577 1.00 41.53  ? 2007 LYS A O     1 
ATOM   5509  C CB    . LYS A 1 2007 ? 205.975 178.064 144.192 1.00 41.53  ? 2007 LYS A CB    1 
ATOM   5510  C CG    . LYS A 1 2007 ? 207.187 178.330 145.069 1.00 41.53  ? 2007 LYS A CG    1 
ATOM   5511  C CD    . LYS A 1 2007 ? 208.206 177.209 144.957 1.00 41.53  ? 2007 LYS A CD    1 
ATOM   5512  C CE    . LYS A 1 2007 ? 209.170 177.219 146.131 1.00 41.53  ? 2007 LYS A CE    1 
ATOM   5513  N NZ    . LYS A 1 2007 ? 209.714 178.581 146.391 1.00 41.53  ? 2007 LYS A NZ    1 
ATOM   5514  N N     . VAL A 1 2008 ? 205.496 176.323 146.991 1.00 32.62  ? 2008 VAL A N     1 
ATOM   5515  C CA    . VAL A 1 2008 ? 205.298 176.313 148.435 1.00 32.62  ? 2008 VAL A CA    1 
ATOM   5516  C C     . VAL A 1 2008 ? 206.488 177.010 149.076 1.00 32.62  ? 2008 VAL A C     1 
ATOM   5517  O O     . VAL A 1 2008 ? 207.635 176.573 148.921 1.00 32.62  ? 2008 VAL A O     1 
ATOM   5518  C CB    . VAL A 1 2008 ? 205.134 174.889 148.979 1.00 32.62  ? 2008 VAL A CB    1 
ATOM   5519  C CG1   . VAL A 1 2008 ? 205.267 174.885 150.489 1.00 32.62  ? 2008 VAL A CG1   1 
ATOM   5520  C CG2   . VAL A 1 2008 ? 203.794 174.318 148.560 1.00 32.62  ? 2008 VAL A CG2   1 
ATOM   5521  N N     . SER A 1 2009 ? 206.219 178.093 149.797 1.00 24.47  ? 2009 SER A N     1 
ATOM   5522  C CA    . SER A 1 2009 ? 207.279 178.793 150.505 1.00 24.47  ? 2009 SER A CA    1 
ATOM   5523  C C     . SER A 1 2009 ? 207.756 177.957 151.691 1.00 24.47  ? 2009 SER A C     1 
ATOM   5524  O O     . SER A 1 2009 ? 206.942 177.338 152.382 1.00 24.47  ? 2009 SER A O     1 
ATOM   5525  C CB    . SER A 1 2009 ? 206.790 180.156 150.988 1.00 24.47  ? 2009 SER A CB    1 
ATOM   5526  O OG    . SER A 1 2009 ? 207.863 180.941 151.473 1.00 24.47  ? 2009 SER A OG    1 
ATOM   5527  N N     . PRO A 1 2010 ? 209.065 177.914 151.949 1.00 22.85  ? 2010 PRO A N     1 
ATOM   5528  C CA    . PRO A 1 2010 ? 209.561 177.112 153.078 1.00 22.85  ? 2010 PRO A CA    1 
ATOM   5529  C C     . PRO A 1 2010 ? 209.135 177.634 154.437 1.00 22.85  ? 2010 PRO A C     1 
ATOM   5530  O O     . PRO A 1 2010 ? 209.118 176.857 155.399 1.00 22.85  ? 2010 PRO A O     1 
ATOM   5531  C CB    . PRO A 1 2010 ? 211.084 177.177 152.911 1.00 22.85  ? 2010 PRO A CB    1 
ATOM   5532  C CG    . PRO A 1 2010 ? 211.322 178.456 152.186 1.00 22.85  ? 2010 PRO A CG    1 
ATOM   5533  C CD    . PRO A 1 2010 ? 210.149 178.637 151.262 1.00 22.85  ? 2010 PRO A CD    1 
ATOM   5534  N N     . ASP A 1 2011 ? 208.789 178.915 154.552 1.00 20.25  ? 2011 ASP A N     1 
ATOM   5535  C CA    . ASP A 1 2011 ? 208.479 179.518 155.841 1.00 20.25  ? 2011 ASP A CA    1 
ATOM   5536  C C     . ASP A 1 2011 ? 207.019 179.374 156.243 1.00 20.25  ? 2011 ASP A C     1 
ATOM   5537  O O     . ASP A 1 2011 ? 206.662 179.766 157.359 1.00 20.25  ? 2011 ASP A O     1 
ATOM   5538  C CB    . ASP A 1 2011 ? 208.856 181.002 155.830 1.00 20.25  ? 2011 ASP A CB    1 
ATOM   5539  C CG    . ASP A 1 2011 ? 210.343 181.224 155.647 1.00 20.25  ? 2011 ASP A CG    1 
ATOM   5540  O OD1   . ASP A 1 2011 ? 210.730 181.890 154.664 1.00 20.25  ? 2011 ASP A OD1   1 
ATOM   5541  O OD2   . ASP A 1 2011 ? 211.126 180.732 156.487 1.00 20.25  ? 2011 ASP A OD2   1 
ATOM   5542  N N     . MET A 1 2012 ? 206.170 178.830 155.378 1.00 20.05  ? 2012 MET A N     1 
ATOM   5543  C CA    . MET A 1 2012 ? 204.763 178.688 155.715 1.00 20.05  ? 2012 MET A CA    1 
ATOM   5544  C C     . MET A 1 2012 ? 204.556 177.515 156.668 1.00 20.05  ? 2012 MET A C     1 
ATOM   5545  O O     . MET A 1 2012 ? 205.430 176.665 156.853 1.00 20.05  ? 2012 MET A O     1 
ATOM   5546  C CB    . MET A 1 2012 ? 203.925 178.491 154.455 1.00 20.05  ? 2012 MET A CB    1 
ATOM   5547  C CG    . MET A 1 2012 ? 203.890 177.061 153.958 1.00 20.05  ? 2012 MET A CG    1 
ATOM   5548  S SD    . MET A 1 2012 ? 202.428 176.739 152.962 1.00 20.05  ? 2012 MET A SD    1 
ATOM   5549  C CE    . MET A 1 2012 ? 201.226 176.424 154.247 1.00 20.05  ? 2012 MET A CE    1 
ATOM   5550  N N     . ALA A 1 2013 ? 203.375 177.481 157.282 1.00 14.62  ? 2013 ALA A N     1 
ATOM   5551  C CA    . ALA A 1 2013 ? 203.026 176.412 158.204 1.00 14.62  ? 2013 ALA A CA    1 
ATOM   5552  C C     . ALA A 1 2013 ? 201.513 176.324 158.323 1.00 14.62  ? 2013 ALA A C     1 
ATOM   5553  O O     . ALA A 1 2013 ? 200.799 177.296 158.066 1.00 14.62  ? 2013 ALA A O     1 
ATOM   5554  C CB    . ALA A 1 2013 ? 203.652 176.630 159.584 1.00 14.62  ? 2013 ALA A CB    1 
ATOM   5555  N N     . ILE A 1 2014 ? 201.033 175.148 158.716 1.00 7.47   ? 2014 ILE A N     1 
ATOM   5556  C CA    . ILE A 1 2014 ? 199.613 174.900 158.931 1.00 7.47   ? 2014 ILE A CA    1 
ATOM   5557  C C     . ILE A 1 2014 ? 199.439 174.374 160.346 1.00 7.47   ? 2014 ILE A C     1 
ATOM   5558  O O     . ILE A 1 2014 ? 200.078 173.386 160.726 1.00 7.47   ? 2014 ILE A O     1 
ATOM   5559  C CB    . ILE A 1 2014 ? 199.036 173.902 157.913 1.00 7.47   ? 2014 ILE A CB    1 
ATOM   5560  C CG1   . ILE A 1 2014 ? 199.114 174.473 156.498 1.00 7.47   ? 2014 ILE A CG1   1 
ATOM   5561  C CG2   . ILE A 1 2014 ? 197.600 173.562 158.262 1.00 7.47   ? 2014 ILE A CG2   1 
ATOM   5562  C CD1   . ILE A 1 2014 ? 198.274 175.712 156.297 1.00 7.47   ? 2014 ILE A CD1   1 
ATOM   5563  N N     . PHE A 1 2015 ? 198.583 175.028 161.123 1.00 11.62  ? 2015 PHE A N     1 
ATOM   5564  C CA    . PHE A 1 2015 ? 198.292 174.627 162.492 1.00 11.62  ? 2015 PHE A CA    1 
ATOM   5565  C C     . PHE A 1 2015 ? 196.819 174.268 162.608 1.00 11.62  ? 2015 PHE A C     1 
ATOM   5566  O O     . PHE A 1 2015 ? 195.953 175.033 162.172 1.00 11.62  ? 2015 PHE A O     1 
ATOM   5567  C CB    . PHE A 1 2015 ? 198.656 175.738 163.476 1.00 11.62  ? 2015 PHE A CB    1 
ATOM   5568  C CG    . PHE A 1 2015 ? 200.129 175.996 163.569 1.00 11.62  ? 2015 PHE A CG    1 
ATOM   5569  C CD1   . PHE A 1 2015 ? 200.905 175.323 164.493 1.00 11.62  ? 2015 PHE A CD1   1 
ATOM   5570  C CD2   . PHE A 1 2015 ? 200.741 176.899 162.723 1.00 11.62  ? 2015 PHE A CD2   1 
ATOM   5571  C CE1   . PHE A 1 2015 ? 202.260 175.554 164.576 1.00 11.62  ? 2015 PHE A CE1   1 
ATOM   5572  C CE2   . PHE A 1 2015 ? 202.095 177.131 162.802 1.00 11.62  ? 2015 PHE A CE2   1 
ATOM   5573  C CZ    . PHE A 1 2015 ? 202.856 176.458 163.730 1.00 11.62  ? 2015 PHE A CZ    1 
ATOM   5574  N N     . ILE A 1 2016 ? 196.540 173.106 163.191 1.00 25.57  ? 2016 ILE A N     1 
ATOM   5575  C CA    . ILE A 1 2016 ? 195.179 172.589 163.264 1.00 25.57  ? 2016 ILE A CA    1 
ATOM   5576  C C     . ILE A 1 2016 ? 194.779 172.406 164.721 1.00 25.57  ? 2016 ILE A C     1 
ATOM   5577  O O     . ILE A 1 2016 ? 195.059 171.368 165.330 1.00 25.57  ? 2016 ILE A O     1 
ATOM   5578  C CB    . ILE A 1 2016 ? 195.056 171.272 162.478 1.00 25.57  ? 2016 ILE A CB    1 
ATOM   5579  C CG1   . ILE A 1 2016 ? 195.338 171.514 160.996 1.00 25.57  ? 2016 ILE A CG1   1 
ATOM   5580  C CG2   . ILE A 1 2016 ? 193.682 170.671 162.646 1.00 25.57  ? 2016 ILE A CG2   1 
ATOM   5581  C CD1   . ILE A 1 2016 ? 195.096 170.306 160.128 1.00 25.57  ? 2016 ILE A CD1   1 
ATOM   5582  N N     . THR A 1 2017 ? 194.126 173.414 165.292 1.00 20.23  ? 2017 THR A N     1 
ATOM   5583  C CA    . THR A 1 2017 ? 193.686 173.331 166.677 1.00 20.23  ? 2017 THR A CA    1 
ATOM   5584  C C     . THR A 1 2017 ? 192.475 172.413 166.787 1.00 20.23  ? 2017 THR A C     1 
ATOM   5585  O O     . THR A 1 2017 ? 191.516 172.542 166.022 1.00 20.23  ? 2017 THR A O     1 
ATOM   5586  C CB    . THR A 1 2017 ? 193.348 174.722 167.207 1.00 20.23  ? 2017 THR A CB    1 
ATOM   5587  O OG1   . THR A 1 2017 ? 194.540 175.513 167.267 1.00 20.23  ? 2017 THR A OG1   1 
ATOM   5588  C CG2   . THR A 1 2017 ? 192.738 174.632 168.592 1.00 20.23  ? 2017 THR A CG2   1 
ATOM   5589  N N     . MET A 1 2018 ? 192.517 171.491 167.740 1.00 21.35  ? 2018 MET A N     1 
ATOM   5590  C CA    . MET A 1 2018 ? 191.474 170.492 167.927 1.00 21.35  ? 2018 MET A CA    1 
ATOM   5591  C C     . MET A 1 2018 ? 190.811 170.681 169.287 1.00 21.35  ? 2018 MET A C     1 
ATOM   5592  O O     . MET A 1 2018 ? 191.061 171.656 169.998 1.00 21.35  ? 2018 MET A O     1 
ATOM   5593  C CB    . MET A 1 2018 ? 192.046 169.078 167.797 1.00 21.35  ? 2018 MET A CB    1 
ATOM   5594  C CG    . MET A 1 2018 ? 192.513 168.721 166.401 1.00 21.35  ? 2018 MET A CG    1 
ATOM   5595  S SD    . MET A 1 2018 ? 191.161 168.717 165.216 1.00 21.35  ? 2018 MET A SD    1 
ATOM   5596  C CE    . MET A 1 2018 ? 190.180 167.352 165.827 1.00 21.35  ? 2018 MET A CE    1 
ATOM   5597  N N     . ASN A 1 2019 ? 189.951 169.732 169.641 1.00 19.21  ? 2019 ASN A N     1 
ATOM   5598  C CA    . ASN A 1 2019 ? 189.266 169.755 170.928 1.00 19.21  ? 2019 ASN A CA    1 
ATOM   5599  C C     . ASN A 1 2019 ? 189.060 168.336 171.454 1.00 19.21  ? 2019 ASN A C     1 
ATOM   5600  O O     . ASN A 1 2019 ? 188.803 167.408 170.689 0.00 19.21  ? 2019 ASN A O     1 
ATOM   5601  C CB    . ASN A 1 2019 ? 187.923 170.478 170.808 1.00 19.21  ? 2019 ASN A CB    1 
ATOM   5602  C CG    . ASN A 1 2019 ? 187.322 170.824 172.157 1.00 19.21  ? 2019 ASN A CG    1 
ATOM   5603  O OD1   . ASN A 1 2019 ? 187.887 170.507 173.203 1.00 19.21  ? 2019 ASN A OD1   1 
ATOM   5604  N ND2   . ASN A 1 2019 ? 186.171 171.483 172.138 1.00 19.21  ? 2019 ASN A ND2   1 
ATOM   5605  N N     . ASN A 1 2027 ? 189.309 163.850 167.186 1.00 24.74  ? 2027 ASN A N     1 
ATOM   5606  C CA    . ASN A 1 2027 ? 190.739 163.688 166.960 1.00 24.74  ? 2027 ASN A CA    1 
ATOM   5607  C C     . ASN A 1 2027 ? 191.098 164.029 165.518 1.00 24.74  ? 2027 ASN A C     1 
ATOM   5608  O O     . ASN A 1 2027 ? 190.218 164.276 164.695 1.00 24.74  ? 2027 ASN A O     1 
ATOM   5609  C CB    . ASN A 1 2027 ? 191.179 162.262 167.294 1.00 24.74  ? 2027 ASN A CB    1 
ATOM   5610  C CG    . ASN A 1 2027 ? 192.616 162.192 167.767 1.00 24.74  ? 2027 ASN A CG    1 
ATOM   5611  O OD1   . ASN A 1 2027 ? 193.315 163.204 167.817 1.00 24.74  ? 2027 ASN A OD1   1 
ATOM   5612  N ND2   . ASN A 1 2027 ? 193.064 160.994 168.121 1.00 24.74  ? 2027 ASN A ND2   1 
ATOM   5613  N N     . LEU A 1 2028 ? 192.394 164.039 165.220 1.00 25.04  ? 2028 LEU A N     1 
ATOM   5614  C CA    . LEU A 1 2028 ? 192.852 164.409 163.893 1.00 25.04  ? 2028 LEU A CA    1 
ATOM   5615  C C     . LEU A 1 2028 ? 192.401 163.375 162.862 1.00 25.04  ? 2028 LEU A C     1 
ATOM   5616  O O     . LEU A 1 2028 ? 192.246 162.193 163.181 1.00 25.04  ? 2028 LEU A O     1 
ATOM   5617  C CB    . LEU A 1 2028 ? 194.372 164.530 163.864 1.00 25.04  ? 2028 LEU A CB    1 
ATOM   5618  C CG    . LEU A 1 2028 ? 194.977 165.896 164.183 1.00 25.04  ? 2028 LEU A CG    1 
ATOM   5619  C CD1   . LEU A 1 2028 ? 196.484 165.782 164.328 1.00 25.04  ? 2028 LEU A CD1   1 
ATOM   5620  C CD2   . LEU A 1 2028 ? 194.616 166.909 163.113 1.00 25.04  ? 2028 LEU A CD2   1 
ATOM   5621  N N     . PRO A 1 2029 ? 192.175 163.798 161.619 1.00 25.02  ? 2029 PRO A N     1 
ATOM   5622  C CA    . PRO A 1 2029 ? 191.840 162.835 160.566 1.00 25.02  ? 2029 PRO A CA    1 
ATOM   5623  C C     . PRO A 1 2029 ? 192.993 161.876 160.317 1.00 25.02  ? 2029 PRO A C     1 
ATOM   5624  O O     . PRO A 1 2029 ? 194.160 162.196 160.553 1.00 25.02  ? 2029 PRO A O     1 
ATOM   5625  C CB    . PRO A 1 2029 ? 191.572 163.720 159.343 1.00 25.02  ? 2029 PRO A CB    1 
ATOM   5626  C CG    . PRO A 1 2029 ? 191.279 165.070 159.902 1.00 25.02  ? 2029 PRO A CG    1 
ATOM   5627  C CD    . PRO A 1 2029 ? 192.108 165.187 161.139 1.00 25.02  ? 2029 PRO A CD    1 
ATOM   5628  N N     . ASP A 1 2030 ? 192.647 160.677 159.842 1.00 26.84  ? 2030 ASP A N     1 
ATOM   5629  C CA    . ASP A 1 2030 ? 193.652 159.647 159.611 1.00 26.84  ? 2030 ASP A CA    1 
ATOM   5630  C C     . ASP A 1 2030 ? 194.693 160.071 158.584 1.00 26.84  ? 2030 ASP A C     1 
ATOM   5631  O O     . ASP A 1 2030 ? 195.806 159.536 158.590 1.00 26.84  ? 2030 ASP A O     1 
ATOM   5632  C CB    . ASP A 1 2030 ? 192.977 158.351 159.165 1.00 26.84  ? 2030 ASP A CB    1 
ATOM   5633  C CG    . ASP A 1 2030 ? 191.995 157.824 160.191 1.00 26.84  ? 2030 ASP A CG    1 
ATOM   5634  O OD1   . ASP A 1 2030 ? 190.991 158.515 160.463 1.00 26.84  ? 2030 ASP A OD1   1 
ATOM   5635  O OD2   . ASP A 1 2030 ? 192.226 156.719 160.725 1.00 26.84  ? 2030 ASP A OD2   1 
ATOM   5636  N N     . ASN A 1 2031 ? 194.356 161.011 157.698 1.00 24.88  ? 2031 ASN A N     1 
ATOM   5637  C CA    . ASN A 1 2031 ? 195.336 161.504 156.737 1.00 24.88  ? 2031 ASN A CA    1 
ATOM   5638  C C     . ASN A 1 2031 ? 196.476 162.239 157.432 1.00 24.88  ? 2031 ASN A C     1 
ATOM   5639  O O     . ASN A 1 2031 ? 197.646 162.059 157.077 1.00 24.88  ? 2031 ASN A O     1 
ATOM   5640  C CB    . ASN A 1 2031 ? 194.659 162.424 155.721 1.00 24.88  ? 2031 ASN A CB    1 
ATOM   5641  C CG    . ASN A 1 2031 ? 193.352 161.863 155.205 1.00 24.88  ? 2031 ASN A CG    1 
ATOM   5642  O OD1   . ASN A 1 2031 ? 193.336 160.943 154.389 1.00 24.88  ? 2031 ASN A OD1   1 
ATOM   5643  N ND2   . ASN A 1 2031 ? 192.243 162.419 155.678 1.00 24.88  ? 2031 ASN A ND2   1 
ATOM   5644  N N     . LEU A 1 2032 ? 196.155 163.063 158.427 1.00 23.74  ? 2032 LEU A N     1 
ATOM   5645  C CA    . LEU A 1 2032 ? 197.109 163.980 159.034 1.00 23.74  ? 2032 LEU A CA    1 
ATOM   5646  C C     . LEU A 1 2032 ? 197.667 163.479 160.360 1.00 23.74  ? 2032 LEU A C     1 
ATOM   5647  O O     . LEU A 1 2032 ? 198.349 164.238 161.055 1.00 23.74  ? 2032 LEU A O     1 
ATOM   5648  C CB    . LEU A 1 2032 ? 196.457 165.348 159.234 1.00 23.74  ? 2032 LEU A CB    1 
ATOM   5649  C CG    . LEU A 1 2032 ? 195.608 165.846 158.066 1.00 23.74  ? 2032 LEU A CG    1 
ATOM   5650  C CD1   . LEU A 1 2032 ? 194.774 167.040 158.485 1.00 23.74  ? 2032 LEU A CD1   1 
ATOM   5651  C CD2   . LEU A 1 2032 ? 196.493 166.197 156.887 1.00 23.74  ? 2032 LEU A CD2   1 
ATOM   5652  N N     . LYS A 1 2033 ? 197.390 162.229 160.733 1.00 23.09  ? 2033 LYS A N     1 
ATOM   5653  C CA    . LYS A 1 2033 ? 197.899 161.715 162.001 1.00 23.09  ? 2033 LYS A CA    1 
ATOM   5654  C C     . LYS A 1 2033 ? 199.421 161.637 161.997 1.00 23.09  ? 2033 LYS A C     1 
ATOM   5655  O O     . LYS A 1 2033 ? 200.068 161.944 163.004 1.00 23.09  ? 2033 LYS A O     1 
ATOM   5656  C CB    . LYS A 1 2033 ? 197.291 160.345 162.297 1.00 23.09  ? 2033 LYS A CB    1 
ATOM   5657  C CG    . LYS A 1 2033 ? 195.896 160.403 162.894 1.00 23.09  ? 2033 LYS A CG    1 
ATOM   5658  C CD    . LYS A 1 2033 ? 195.444 159.034 163.370 1.00 23.09  ? 2033 LYS A CD    1 
ATOM   5659  C CE    . LYS A 1 2033 ? 194.039 159.083 163.945 1.00 23.09  ? 2033 LYS A CE    1 
ATOM   5660  N NZ    . LYS A 1 2033 ? 193.957 159.977 165.131 1.00 23.09  ? 2033 LYS A NZ    1 
ATOM   5661  N N     . LYS A 1 2034 ? 200.009 161.231 160.876 1.00 21.77  ? 2034 LYS A N     1 
ATOM   5662  C CA    . LYS A 1 2034 ? 201.453 161.076 160.768 1.00 21.77  ? 2034 LYS A CA    1 
ATOM   5663  C C     . LYS A 1 2034 ? 202.164 162.354 160.341 1.00 21.77  ? 2034 LYS A C     1 
ATOM   5664  O O     . LYS A 1 2034 ? 203.394 162.349 160.226 1.00 21.77  ? 2034 LYS A O     1 
ATOM   5665  C CB    . LYS A 1 2034 ? 201.788 159.953 159.783 1.00 21.77  ? 2034 LYS A CB    1 
ATOM   5666  C CG    . LYS A 1 2034 ? 200.802 158.797 159.803 1.00 21.77  ? 2034 LYS A CG    1 
ATOM   5667  C CD    . LYS A 1 2034 ? 201.232 157.685 158.860 1.00 21.77  ? 2034 LYS A CD    1 
ATOM   5668  C CE    . LYS A 1 2034 ? 202.670 157.266 159.117 1.00 21.77  ? 2034 LYS A CE    1 
ATOM   5669  N NZ    . LYS A 1 2034 ? 202.848 156.706 160.485 1.00 21.77  ? 2034 LYS A NZ    1 
ATOM   5670  N N     . LEU A 1 2035 ? 201.431 163.441 160.103 1.00 20.24  ? 2035 LEU A N     1 
ATOM   5671  C CA    . LEU A 1 2035 ? 202.023 164.683 159.629 1.00 20.24  ? 2035 LEU A CA    1 
ATOM   5672  C C     . LEU A 1 2035 ? 201.961 165.821 160.637 1.00 20.24  ? 2035 LEU A C     1 
ATOM   5673  O O     . LEU A 1 2035 ? 202.616 166.846 160.422 1.00 20.24  ? 2035 LEU A O     1 
ATOM   5674  C CB    . LEU A 1 2035 ? 201.339 165.137 158.331 1.00 20.24  ? 2035 LEU A CB    1 
ATOM   5675  C CG    . LEU A 1 2035 ? 201.564 164.275 157.091 1.00 20.24  ? 2035 LEU A CG    1 
ATOM   5676  C CD1   . LEU A 1 2035 ? 200.573 164.646 156.004 1.00 20.24  ? 2035 LEU A CD1   1 
ATOM   5677  C CD2   . LEU A 1 2035 ? 202.988 164.428 156.594 1.00 20.24  ? 2035 LEU A CD2   1 
ATOM   5678  N N     . PHE A 1 2036 ? 201.201 165.679 161.719 1.00 16.12  ? 2036 PHE A N     1 
ATOM   5679  C CA    . PHE A 1 2036 ? 200.993 166.756 162.676 1.00 16.12  ? 2036 PHE A CA    1 
ATOM   5680  C C     . PHE A 1 2036 ? 201.387 166.293 164.069 1.00 16.12  ? 2036 PHE A C     1 
ATOM   5681  O O     . PHE A 1 2036 ? 201.006 165.199 164.496 1.00 16.12  ? 2036 PHE A O     1 
ATOM   5682  C CB    . PHE A 1 2036 ? 199.537 167.224 162.662 1.00 16.12  ? 2036 PHE A CB    1 
ATOM   5683  C CG    . PHE A 1 2036 ? 199.229 168.200 161.566 1.00 16.12  ? 2036 PHE A CG    1 
ATOM   5684  C CD1   . PHE A 1 2036 ? 199.186 167.788 160.247 1.00 16.12  ? 2036 PHE A CD1   1 
ATOM   5685  C CD2   . PHE A 1 2036 ? 198.988 169.529 161.854 1.00 16.12  ? 2036 PHE A CD2   1 
ATOM   5686  C CE1   . PHE A 1 2036 ? 198.905 168.683 159.238 1.00 16.12  ? 2036 PHE A CE1   1 
ATOM   5687  C CE2   . PHE A 1 2036 ? 198.709 170.427 160.848 1.00 16.12  ? 2036 PHE A CE2   1 
ATOM   5688  C CZ    . PHE A 1 2036 ? 198.667 170.004 159.539 1.00 16.12  ? 2036 PHE A CZ    1 
ATOM   5689  N N     . ARG A 1 2037 ? 202.148 167.128 164.772 1.00 14.94  ? 2037 ARG A N     1 
ATOM   5690  C CA    . ARG A 1 2037 ? 202.563 166.839 166.136 1.00 14.94  ? 2037 ARG A CA    1 
ATOM   5691  C C     . ARG A 1 2037 ? 201.573 167.460 167.112 1.00 14.94  ? 2037 ARG A C     1 
ATOM   5692  O O     . ARG A 1 2037 ? 201.468 168.687 167.203 1.00 14.94  ? 2037 ARG A O     1 
ATOM   5693  C CB    . ARG A 1 2037 ? 203.971 167.374 166.395 1.00 14.94  ? 2037 ARG A CB    1 
ATOM   5694  C CG    . ARG A 1 2037 ? 204.570 166.928 167.715 1.00 14.94  ? 2037 ARG A CG    1 
ATOM   5695  C CD    . ARG A 1 2037 ? 205.279 165.590 167.577 1.00 14.94  ? 2037 ARG A CD    1 
ATOM   5696  N NE    . ARG A 1 2037 ? 206.406 165.656 166.654 1.00 14.94  ? 2037 ARG A NE    1 
ATOM   5697  C CZ    . ARG A 1 2037 ? 207.572 166.222 166.932 1.00 14.94  ? 2037 ARG A CZ    1 
ATOM   5698  N NH1   . ARG A 1 2037 ? 207.805 166.788 168.105 1.00 14.94  ? 2037 ARG A NH1   1 
ATOM   5699  N NH2   . ARG A 1 2037 ? 208.530 166.220 166.010 1.00 14.94  ? 2037 ARG A NH2   1 
ATOM   5700  N N     . SER A 1 2038 ? 200.857 166.613 167.841 1.00 17.12  ? 2038 SER A N     1 
ATOM   5701  C CA    . SER A 1 2038 ? 199.836 167.067 168.771 1.00 17.12  ? 2038 SER A CA    1 
ATOM   5702  C C     . SER A 1 2038 ? 200.469 167.677 170.015 1.00 17.12  ? 2038 SER A C     1 
ATOM   5703  O O     . SER A 1 2038 ? 201.653 167.486 170.301 1.00 17.12  ? 2038 SER A O     1 
ATOM   5704  C CB    . SER A 1 2038 ? 198.916 165.912 169.166 1.00 17.12  ? 2038 SER A CB    1 
ATOM   5705  O OG    . SER A 1 2038 ? 198.246 165.387 168.035 1.00 17.12  ? 2038 SER A OG    1 
ATOM   5706  N N     . LEU A 1 2039 ? 199.656 168.425 170.758 1.00 15.93  ? 2039 LEU A N     1 
ATOM   5707  C CA    . LEU A 1 2039 ? 200.107 169.063 171.992 1.00 15.93  ? 2039 LEU A CA    1 
ATOM   5708  C C     . LEU A 1 2039 ? 198.893 169.305 172.875 1.00 15.93  ? 2039 LEU A C     1 
ATOM   5709  O O     . LEU A 1 2039 ? 197.939 169.960 172.449 1.00 15.93  ? 2039 LEU A O     1 
ATOM   5710  C CB    . LEU A 1 2039 ? 200.836 170.367 171.703 1.00 15.93  ? 2039 LEU A CB    1 
ATOM   5711  C CG    . LEU A 1 2039 ? 201.320 171.092 172.954 1.00 15.93  ? 2039 LEU A CG    1 
ATOM   5712  C CD1   . LEU A 1 2039 ? 202.372 170.272 173.677 1.00 15.93  ? 2039 LEU A CD1   1 
ATOM   5713  C CD2   . LEU A 1 2039 ? 201.856 172.448 172.582 1.00 15.93  ? 2039 LEU A CD2   1 
ATOM   5714  N N     . ALA A 1 2040 ? 198.929 168.784 174.097 1.00 17.70  ? 2040 ALA A N     1 
ATOM   5715  C CA    . ALA A 1 2040 ? 197.811 168.955 175.015 1.00 17.70  ? 2040 ALA A CA    1 
ATOM   5716  C C     . ALA A 1 2040 ? 197.894 170.314 175.697 1.00 17.70  ? 2040 ALA A C     1 
ATOM   5717  O O     . ALA A 1 2040 ? 198.780 170.549 176.525 1.00 17.70  ? 2040 ALA A O     1 
ATOM   5718  C CB    . ALA A 1 2040 ? 197.801 167.838 176.053 1.00 17.70  ? 2040 ALA A CB    1 
ATOM   5719  N N     . MET A 1 2041 ? 196.972 171.205 175.353 1.00 16.75  ? 2041 MET A N     1 
ATOM   5720  C CA    . MET A 1 2041 ? 196.822 172.497 176.014 1.00 16.75  ? 2041 MET A CA    1 
ATOM   5721  C C     . MET A 1 2041 ? 195.490 172.484 176.758 1.00 16.75  ? 2041 MET A C     1 
ATOM   5722  O O     . MET A 1 2041 ? 194.469 172.938 176.237 1.00 16.75  ? 2041 MET A O     1 
ATOM   5723  C CB    . MET A 1 2041 ? 196.895 173.641 174.997 1.00 16.75  ? 2041 MET A CB    1 
ATOM   5724  C CG    . MET A 1 2041 ? 198.269 173.833 174.379 1.00 16.75  ? 2041 MET A CG    1 
ATOM   5725  S SD    . MET A 1 2041 ? 198.563 175.509 173.789 1.00 16.75  ? 2041 MET A SD    1 
ATOM   5726  C CE    . MET A 1 2041 ? 198.015 176.465 175.197 1.00 16.75  ? 2041 MET A CE    1 
ATOM   5727  N N     . THR A 1 2042 ? 195.506 171.964 177.985 1.00 20.24  ? 2042 THR A N     1 
ATOM   5728  C CA    . THR A 1 2042 ? 194.261 171.693 178.696 1.00 20.24  ? 2042 THR A CA    1 
ATOM   5729  C C     . THR A 1 2042 ? 194.015 172.695 179.818 1.00 20.24  ? 2042 THR A C     1 
ATOM   5730  O O     . THR A 1 2042 ? 192.909 173.227 179.957 1.00 20.24  ? 2042 THR A O     1 
ATOM   5731  C CB    . THR A 1 2042 ? 194.275 170.266 179.249 1.00 20.24  ? 2042 THR A CB    1 
ATOM   5732  O OG1   . THR A 1 2042 ? 195.401 170.101 180.120 1.00 20.24  ? 2042 THR A OG1   1 
ATOM   5733  C CG2   . THR A 1 2042 ? 194.362 169.257 178.116 1.00 20.24  ? 2042 THR A CG2   1 
ATOM   5734  N N     . LYS A 1 2043 ? 195.026 172.950 180.640 1.00 17.20  ? 2043 LYS A N     1 
ATOM   5735  C CA    . LYS A 1 2043 ? 194.859 173.828 181.792 1.00 17.20  ? 2043 LYS A CA    1 
ATOM   5736  C C     . LYS A 1 2043 ? 195.747 175.054 181.656 1.00 17.20  ? 2043 LYS A C     1 
ATOM   5737  O O     . LYS A 1 2043 ? 196.955 174.969 181.927 1.00 17.20  ? 2043 LYS A O     1 
ATOM   5738  C CB    . LYS A 1 2043 ? 195.180 173.078 183.085 1.00 17.20  ? 2043 LYS A CB    1 
ATOM   5739  C CG    . LYS A 1 2043 ? 194.590 173.716 184.331 1.00 17.20  ? 2043 LYS A CG    1 
ATOM   5740  C CD    . LYS A 1 2043 ? 194.876 172.887 185.575 1.00 17.20  ? 2043 LYS A CD    1 
ATOM   5741  C CE    . LYS A 1 2043 ? 194.662 171.401 185.326 1.00 17.20  ? 2043 LYS A CE    1 
ATOM   5742  N NZ    . LYS A 1 2043 ? 193.286 171.101 184.837 1.00 17.20  ? 2043 LYS A NZ    1 
ATOM   5743  N N     . PRO A 1 2044 ? 195.214 176.201 181.244 1.00 15.56  ? 2044 PRO A N     1 
ATOM   5744  C CA    . PRO A 1 2044 ? 196.025 177.420 181.210 1.00 15.56  ? 2044 PRO A CA    1 
ATOM   5745  C C     . PRO A 1 2044 ? 196.400 177.866 182.613 1.00 15.56  ? 2044 PRO A C     1 
ATOM   5746  O O     . PRO A 1 2044 ? 195.681 177.633 183.586 1.00 15.56  ? 2044 PRO A O     1 
ATOM   5747  C CB    . PRO A 1 2044 ? 195.105 178.438 180.530 1.00 15.56  ? 2044 PRO A CB    1 
ATOM   5748  C CG    . PRO A 1 2044 ? 193.734 177.954 180.854 1.00 15.56  ? 2044 PRO A CG    1 
ATOM   5749  C CD    . PRO A 1 2044 ? 193.825 176.454 180.828 1.00 15.56  ? 2044 PRO A CD    1 
ATOM   5750  N N     . ASP A 1 2045 ? 197.554 178.520 182.708 1.00 14.71  ? 2045 ASP A N     1 
ATOM   5751  C CA    . ASP A 1 2045 ? 198.064 179.005 183.987 1.00 14.71  ? 2045 ASP A CA    1 
ATOM   5752  C C     . ASP A 1 2045 ? 197.471 180.386 184.238 1.00 14.71  ? 2045 ASP A C     1 
ATOM   5753  O O     . ASP A 1 2045 ? 198.066 181.404 183.880 1.00 14.71  ? 2045 ASP A O     1 
ATOM   5754  C CB    . ASP A 1 2045 ? 199.588 179.038 183.982 1.00 14.71  ? 2045 ASP A CB    1 
ATOM   5755  C CG    . ASP A 1 2045 ? 200.172 179.144 185.376 1.00 14.71  ? 2045 ASP A CG    1 
ATOM   5756  O OD1   . ASP A 1 2045 ? 199.391 179.186 186.349 1.00 14.71  ? 2045 ASP A OD1   1 
ATOM   5757  O OD2   . ASP A 1 2045 ? 201.414 179.184 185.501 1.00 14.71  ? 2045 ASP A OD2   1 
ATOM   5758  N N     . ARG A 1 2046 ? 196.292 180.422 184.856 1.00 12.09  ? 2046 ARG A N     1 
ATOM   5759  C CA    . ARG A 1 2046 ? 195.592 181.672 185.113 1.00 12.09  ? 2046 ARG A CA    1 
ATOM   5760  C C     . ARG A 1 2046 ? 196.178 182.469 186.270 1.00 12.09  ? 2046 ARG A C     1 
ATOM   5761  O O     . ARG A 1 2046 ? 196.119 183.702 186.241 1.00 12.09  ? 2046 ARG A O     1 
ATOM   5762  C CB    . ARG A 1 2046 ? 194.110 181.400 185.382 1.00 12.09  ? 2046 ARG A CB    1 
ATOM   5763  C CG    . ARG A 1 2046 ? 193.475 180.444 184.392 1.00 12.09  ? 2046 ARG A CG    1 
ATOM   5764  C CD    . ARG A 1 2046 ? 192.078 180.040 184.821 1.00 12.09  ? 2046 ARG A CD    1 
ATOM   5765  N NE    . ARG A 1 2046 ? 191.168 179.956 183.686 1.00 12.09  ? 2046 ARG A NE    1 
ATOM   5766  C CZ    . ARG A 1 2046 ? 190.835 178.827 183.076 1.00 12.09  ? 2046 ARG A CZ    1 
ATOM   5767  N NH1   . ARG A 1 2046 ? 191.325 177.662 183.465 1.00 12.09  ? 2046 ARG A NH1   1 
ATOM   5768  N NH2   . ARG A 1 2046 ? 189.992 178.869 182.049 1.00 12.09  ? 2046 ARG A NH2   1 
ATOM   5769  N N     . GLN A 1 2047 ? 196.745 181.808 187.277 1.00 12.48  ? 2047 GLN A N     1 
ATOM   5770  C CA    . GLN A 1 2047 ? 197.328 182.490 188.424 1.00 12.48  ? 2047 GLN A CA    1 
ATOM   5771  C C     . GLN A 1 2047 ? 198.598 183.252 188.069 1.00 12.48  ? 2047 GLN A C     1 
ATOM   5772  O O     . GLN A 1 2047 ? 199.075 184.052 188.879 1.00 12.48  ? 2047 GLN A O     1 
ATOM   5773  C CB    . GLN A 1 2047 ? 197.609 181.493 189.550 1.00 12.48  ? 2047 GLN A CB    1 
ATOM   5774  C CG    . GLN A 1 2047 ? 196.367 180.802 190.089 1.00 12.48  ? 2047 GLN A CG    1 
ATOM   5775  C CD    . GLN A 1 2047 ? 196.159 179.423 189.497 1.00 12.48  ? 2047 GLN A CD    1 
ATOM   5776  O OE1   . GLN A 1 2047 ? 196.962 178.951 188.692 1.00 12.48  ? 2047 GLN A OE1   1 
ATOM   5777  N NE2   . GLN A 1 2047 ? 195.074 178.767 189.893 1.00 12.48  ? 2047 GLN A NE2   1 
ATOM   5778  N N     . LEU A 1 2048 ? 199.159 183.017 186.882 1.00 11.17  ? 2048 LEU A N     1 
ATOM   5779  C CA    . LEU A 1 2048 ? 200.262 183.816 186.372 1.00 11.17  ? 2048 LEU A CA    1 
ATOM   5780  C C     . LEU A 1 2048 ? 199.834 184.836 185.331 1.00 11.17  ? 2048 LEU A C     1 
ATOM   5781  O O     . LEU A 1 2048 ? 200.367 185.952 185.333 1.00 11.17  ? 2048 LEU A O     1 
ATOM   5782  C CB    . LEU A 1 2048 ? 201.349 182.915 185.765 1.00 11.17  ? 2048 LEU A CB    1 
ATOM   5783  C CG    . LEU A 1 2048 ? 202.590 183.630 185.232 1.00 11.17  ? 2048 LEU A CG    1 
ATOM   5784  C CD1   . LEU A 1 2048 ? 203.362 184.273 186.369 1.00 11.17  ? 2048 LEU A CD1   1 
ATOM   5785  C CD2   . LEU A 1 2048 ? 203.475 182.667 184.465 1.00 11.17  ? 2048 LEU A CD2   1 
ATOM   5786  N N     . ILE A 1 2049 ? 198.889 184.494 184.454 1.00 11.13  ? 2049 ILE A N     1 
ATOM   5787  C CA    . ILE A 1 2049 ? 198.317 185.472 183.538 1.00 11.13  ? 2049 ILE A CA    1 
ATOM   5788  C C     . ILE A 1 2049 ? 197.666 186.631 184.277 1.00 11.13  ? 2049 ILE A C     1 
ATOM   5789  O O     . ILE A 1 2049 ? 197.881 187.792 183.902 1.00 11.13  ? 2049 ILE A O     1 
ATOM   5790  C CB    . ILE A 1 2049 ? 197.286 184.811 182.608 1.00 11.13  ? 2049 ILE A CB    1 
ATOM   5791  C CG1   . ILE A 1 2049 ? 197.966 183.783 181.709 1.00 11.13  ? 2049 ILE A CG1   1 
ATOM   5792  C CG2   . ILE A 1 2049 ? 196.567 185.855 181.774 1.00 11.13  ? 2049 ILE A CG2   1 
ATOM   5793  C CD1   . ILE A 1 2049 ? 197.007 182.846 181.031 1.00 11.13  ? 2049 ILE A CD1   1 
ATOM   5794  N N     . ALA A 1 2050 ? 196.883 186.354 185.318 1.00 10.51  ? 2050 ALA A N     1 
ATOM   5795  C CA    . ALA A 1 2050 ? 196.307 187.414 186.132 1.00 10.51  ? 2050 ALA A CA    1 
ATOM   5796  C C     . ALA A 1 2050 ? 197.373 188.228 186.850 1.00 10.51  ? 2050 ALA A C     1 
ATOM   5797  O O     . ALA A 1 2050 ? 197.274 189.457 186.905 1.00 10.51  ? 2050 ALA A O     1 
ATOM   5798  C CB    . ALA A 1 2050 ? 195.326 186.826 187.147 1.00 10.51  ? 2050 ALA A CB    1 
ATOM   5799  N N     . GLN A 1 2051 ? 198.399 187.568 187.392 1.00 11.52  ? 2051 GLN A N     1 
ATOM   5800  C CA    . GLN A 1 2051 ? 199.436 188.282 188.131 1.00 11.52  ? 2051 GLN A CA    1 
ATOM   5801  C C     . GLN A 1 2051 ? 200.200 189.241 187.228 1.00 11.52  ? 2051 GLN A C     1 
ATOM   5802  O O     . GLN A 1 2051 ? 200.411 190.407 187.581 1.00 11.52  ? 2051 GLN A O     1 
ATOM   5803  C CB    . GLN A 1 2051 ? 200.395 187.287 188.783 1.00 11.52  ? 2051 GLN A CB    1 
ATOM   5804  C CG    . GLN A 1 2051 ? 201.668 187.925 189.308 1.00 11.52  ? 2051 GLN A CG    1 
ATOM   5805  C CD    . GLN A 1 2051 ? 202.729 186.906 189.659 1.00 11.52  ? 2051 GLN A CD    1 
ATOM   5806  O OE1   . GLN A 1 2051 ? 202.420 185.779 190.042 1.00 11.52  ? 2051 GLN A OE1   1 
ATOM   5807  N NE2   . GLN A 1 2051 ? 203.991 187.296 189.527 1.00 11.52  ? 2051 GLN A NE2   1 
ATOM   5808  N N     . VAL A 1 2052 ? 200.623 188.770 186.055 1.00 10.38  ? 2052 VAL A N     1 
ATOM   5809  C CA    . VAL A 1 2052 ? 201.403 189.619 185.162 1.00 10.38  ? 2052 VAL A CA    1 
ATOM   5810  C C     . VAL A 1 2052 ? 200.558 190.777 184.648 1.00 10.38  ? 2052 VAL A C     1 
ATOM   5811  O O     . VAL A 1 2052 ? 201.029 191.917 184.563 1.00 10.38  ? 2052 VAL A O     1 
ATOM   5812  C CB    . VAL A 1 2052 ? 201.991 188.787 184.010 1.00 10.38  ? 2052 VAL A CB    1 
ATOM   5813  C CG1   . VAL A 1 2052 ? 202.561 189.694 182.937 1.00 10.38  ? 2052 VAL A CG1   1 
ATOM   5814  C CG2   . VAL A 1 2052 ? 203.060 187.848 184.536 1.00 10.38  ? 2052 VAL A CG2   1 
ATOM   5815  N N     . MET A 1 2053 ? 199.297 190.509 184.302 1.00 12.60  ? 2053 MET A N     1 
ATOM   5816  C CA    . MET A 1 2053 ? 198.425 191.573 183.819 1.00 12.60  ? 2053 MET A CA    1 
ATOM   5817  C C     . MET A 1 2053 ? 198.156 192.608 184.904 1.00 12.60  ? 2053 MET A C     1 
ATOM   5818  O O     . MET A 1 2053 ? 198.142 193.813 184.627 1.00 12.60  ? 2053 MET A O     1 
ATOM   5819  C CB    . MET A 1 2053 ? 197.116 190.985 183.297 1.00 12.60  ? 2053 MET A CB    1 
ATOM   5820  C CG    . MET A 1 2053 ? 197.236 190.364 181.919 1.00 12.60  ? 2053 MET A CG    1 
ATOM   5821  S SD    . MET A 1 2053 ? 195.659 190.263 181.060 1.00 12.60  ? 2053 MET A SD    1 
ATOM   5822  C CE    . MET A 1 2053 ? 195.026 191.911 181.345 1.00 12.60  ? 2053 MET A CE    1 
ATOM   5823  N N     . LEU A 1 2054 ? 197.939 192.164 186.144 1.00 10.69  ? 2054 LEU A N     1 
ATOM   5824  C CA    . LEU A 1 2054 ? 197.730 193.106 187.238 1.00 10.69  ? 2054 LEU A CA    1 
ATOM   5825  C C     . LEU A 1 2054 ? 198.986 193.921 187.509 1.00 10.69  ? 2054 LEU A C     1 
ATOM   5826  O O     . LEU A 1 2054 ? 198.902 195.111 187.832 1.00 10.69  ? 2054 LEU A O     1 
ATOM   5827  C CB    . LEU A 1 2054 ? 197.290 192.358 188.494 1.00 10.69  ? 2054 LEU A CB    1 
ATOM   5828  C CG    . LEU A 1 2054 ? 195.806 191.999 188.563 1.00 10.69  ? 2054 LEU A CG    1 
ATOM   5829  C CD1   . LEU A 1 2054 ? 195.582 190.830 189.503 1.00 10.69  ? 2054 LEU A CD1   1 
ATOM   5830  C CD2   . LEU A 1 2054 ? 194.985 193.198 188.993 1.00 10.69  ? 2054 LEU A CD2   1 
ATOM   5831  N N     . TYR A 1 2055 ? 200.159 193.297 187.394 1.00 11.66  ? 2055 TYR A N     1 
ATOM   5832  C CA    . TYR A 1 2055 ? 201.406 194.038 187.549 1.00 11.66  ? 2055 TYR A CA    1 
ATOM   5833  C C     . TYR A 1 2055 ? 201.561 195.082 186.452 1.00 11.66  ? 2055 TYR A C     1 
ATOM   5834  O O     . TYR A 1 2055 ? 202.024 196.200 186.708 1.00 11.66  ? 2055 TYR A O     1 
ATOM   5835  C CB    . TYR A 1 2055 ? 202.590 193.073 187.547 1.00 11.66  ? 2055 TYR A CB    1 
ATOM   5836  C CG    . TYR A 1 2055 ? 203.910 193.719 187.892 1.00 11.66  ? 2055 TYR A CG    1 
ATOM   5837  C CD1   . TYR A 1 2055 ? 203.980 194.753 188.813 1.00 11.66  ? 2055 TYR A CD1   1 
ATOM   5838  C CD2   . TYR A 1 2055 ? 205.088 193.293 187.296 1.00 11.66  ? 2055 TYR A CD2   1 
ATOM   5839  C CE1   . TYR A 1 2055 ? 205.186 195.345 189.130 1.00 11.66  ? 2055 TYR A CE1   1 
ATOM   5840  C CE2   . TYR A 1 2055 ? 206.297 193.878 187.607 1.00 11.66  ? 2055 TYR A CE2   1 
ATOM   5841  C CZ    . TYR A 1 2055 ? 206.341 194.903 188.524 1.00 11.66  ? 2055 TYR A CZ    1 
ATOM   5842  O OH    . TYR A 1 2055 ? 207.544 195.489 188.838 1.00 11.66  ? 2055 TYR A OH    1 
ATOM   5843  N N     . SER A 1 2056 ? 201.179 194.736 185.221 1.00 11.37  ? 2056 SER A N     1 
ATOM   5844  C CA    . SER A 1 2056 ? 201.261 195.691 184.122 1.00 11.37  ? 2056 SER A CA    1 
ATOM   5845  C C     . SER A 1 2056 ? 200.252 196.820 184.280 1.00 11.37  ? 2056 SER A C     1 
ATOM   5846  O O     . SER A 1 2056 ? 200.504 197.941 183.826 1.00 11.37  ? 2056 SER A O     1 
ATOM   5847  C CB    . SER A 1 2056 ? 201.052 194.976 182.790 1.00 11.37  ? 2056 SER A CB    1 
ATOM   5848  O OG    . SER A 1 2056 ? 199.674 194.827 182.505 1.00 11.37  ? 2056 SER A OG    1 
ATOM   5849  N N     . GLN A 1 2057 ? 199.111 196.550 184.915 1.00 11.58  ? 2057 GLN A N     1 
ATOM   5850  C CA    . GLN A 1 2057 ? 198.114 197.586 185.149 1.00 11.58  ? 2057 GLN A CA    1 
ATOM   5851  C C     . GLN A 1 2057 ? 198.550 198.596 186.201 1.00 11.58  ? 2057 GLN A C     1 
ATOM   5852  O O     . GLN A 1 2057 ? 197.878 199.618 186.368 1.00 11.58  ? 2057 GLN A O     1 
ATOM   5853  C CB    . GLN A 1 2057 ? 196.784 196.957 185.567 1.00 11.58  ? 2057 GLN A CB    1 
ATOM   5854  C CG    . GLN A 1 2057 ? 196.027 196.270 184.441 1.00 11.58  ? 2057 GLN A CG    1 
ATOM   5855  C CD    . GLN A 1 2057 ? 195.994 197.089 183.168 1.00 11.58  ? 2057 GLN A CD    1 
ATOM   5856  O OE1   . GLN A 1 2057 ? 195.638 198.267 183.181 1.00 11.58  ? 2057 GLN A OE1   1 
ATOM   5857  N NE2   . GLN A 1 2057 ? 196.360 196.465 182.056 1.00 11.58  ? 2057 GLN A NE2   1 
ATOM   5858  N N     . GLY A 1 2058 ? 199.647 198.338 186.910 1.00 11.43  ? 2058 GLY A N     1 
ATOM   5859  C CA    . GLY A 1 2058 ? 200.143 199.234 187.930 1.00 11.43  ? 2058 GLY A CA    1 
ATOM   5860  C C     . GLY A 1 2058 ? 199.911 198.774 189.353 1.00 11.43  ? 2058 GLY A C     1 
ATOM   5861  O O     . GLY A 1 2058 ? 200.417 199.417 190.280 1.00 11.43  ? 2058 GLY A O     1 
ATOM   5862  N N     . PHE A 1 2059 ? 199.163 197.693 189.554 1.00 12.01  ? 2059 PHE A N     1 
ATOM   5863  C CA    . PHE A 1 2059 ? 198.930 197.181 190.898 1.00 12.01  ? 2059 PHE A CA    1 
ATOM   5864  C C     . PHE A 1 2059 ? 200.241 196.718 191.520 1.00 12.01  ? 2059 PHE A C     1 
ATOM   5865  O O     . PHE A 1 2059 ? 201.030 196.016 190.881 1.00 12.01  ? 2059 PHE A O     1 
ATOM   5866  C CB    . PHE A 1 2059 ? 197.927 196.029 190.859 1.00 12.01  ? 2059 PHE A CB    1 
ATOM   5867  C CG    . PHE A 1 2059 ? 196.527 196.454 190.522 1.00 12.01  ? 2059 PHE A CG    1 
ATOM   5868  C CD1   . PHE A 1 2059 ? 196.142 196.639 189.206 1.00 12.01  ? 2059 PHE A CD1   1 
ATOM   5869  C CD2   . PHE A 1 2059 ? 195.595 196.665 191.520 1.00 12.01  ? 2059 PHE A CD2   1 
ATOM   5870  C CE1   . PHE A 1 2059 ? 194.856 197.028 188.895 1.00 12.01  ? 2059 PHE A CE1   1 
ATOM   5871  C CE2   . PHE A 1 2059 ? 194.308 197.054 191.214 1.00 12.01  ? 2059 PHE A CE2   1 
ATOM   5872  C CZ    . PHE A 1 2059 ? 193.938 197.235 189.900 1.00 12.01  ? 2059 PHE A CZ    1 
ATOM   5873  N N     . ARG A 1 2060 ? 200.475 197.115 192.769 1.00 25.65  ? 2060 ARG A N     1 
ATOM   5874  C CA    . ARG A 1 2060 ? 201.698 196.757 193.474 1.00 25.65  ? 2060 ARG A CA    1 
ATOM   5875  C C     . ARG A 1 2060 ? 201.586 195.450 194.247 1.00 25.65  ? 2060 ARG A C     1 
ATOM   5876  O O     . ARG A 1 2060 ? 202.603 194.955 194.746 1.00 25.65  ? 2060 ARG A O     1 
ATOM   5877  C CB    . ARG A 1 2060 ? 202.099 197.886 194.430 1.00 25.65  ? 2060 ARG A CB    1 
ATOM   5878  C CG    . ARG A 1 2060 ? 201.355 197.864 195.751 1.00 25.65  ? 2060 ARG A CG    1 
ATOM   5879  C CD    . ARG A 1 2060 ? 202.086 198.658 196.823 1.00 25.65  ? 2060 ARG A CD    1 
ATOM   5880  N NE    . ARG A 1 2060 ? 201.691 198.262 198.170 1.00 25.65  ? 2060 ARG A NE    1 
ATOM   5881  C CZ    . ARG A 1 2060 ? 200.491 198.466 198.699 1.00 25.65  ? 2060 ARG A CZ    1 
ATOM   5882  N NH1   . ARG A 1 2060 ? 199.535 199.089 198.030 1.00 25.65  ? 2060 ARG A NH1   1 
ATOM   5883  N NH2   . ARG A 1 2060 ? 200.247 198.041 199.935 1.00 25.65  ? 2060 ARG A NH2   1 
ATOM   5884  N N     . THR A 1 2061 ? 200.387 194.880 194.356 1.00 20.62  ? 2061 THR A N     1 
ATOM   5885  C CA    . THR A 1 2061 ? 200.187 193.603 195.032 1.00 20.62  ? 2061 THR A CA    1 
ATOM   5886  C C     . THR A 1 2061 ? 199.587 192.593 194.065 1.00 20.62  ? 2061 THR A C     1 
ATOM   5887  O O     . THR A 1 2061 ? 198.605 191.919 194.390 1.00 20.62  ? 2061 THR A O     1 
ATOM   5888  C CB    . THR A 1 2061 ? 199.284 193.762 196.257 1.00 20.62  ? 2061 THR A CB    1 
ATOM   5889  O OG1   . THR A 1 2061 ? 197.931 193.969 195.834 1.00 20.62  ? 2061 THR A OG1   1 
ATOM   5890  C CG2   . THR A 1 2061 ? 199.734 194.933 197.112 1.00 20.62  ? 2061 THR A CG2   1 
ATOM   5891  N N     . ALA A 1 2062 ? 200.171 192.495 192.868 1.00 15.01  ? 2062 ALA A N     1 
ATOM   5892  C CA    . ALA A 1 2062 ? 199.570 191.700 191.801 1.00 15.01  ? 2062 ALA A CA    1 
ATOM   5893  C C     . ALA A 1 2062 ? 199.468 190.226 192.175 1.00 15.01  ? 2062 ALA A C     1 
ATOM   5894  O O     . ALA A 1 2062 ? 198.499 189.555 191.804 1.00 15.01  ? 2062 ALA A O     1 
ATOM   5895  C CB    . ALA A 1 2062 ? 200.374 191.869 190.514 1.00 15.01  ? 2062 ALA A CB    1 
ATOM   5896  N N     . GLU A 1 2063 ? 200.459 189.700 192.897 1.00 13.00  ? 2063 GLU A N     1 
ATOM   5897  C CA    . GLU A 1 2063 ? 200.467 188.272 193.208 1.00 13.00  ? 2063 GLU A CA    1 
ATOM   5898  C C     . GLU A 1 2063 ? 199.287 187.889 194.095 1.00 13.00  ? 2063 GLU A C     1 
ATOM   5899  O O     . GLU A 1 2063 ? 198.570 186.920 193.813 1.00 13.00  ? 2063 GLU A O     1 
ATOM   5900  C CB    . GLU A 1 2063 ? 201.787 187.890 193.875 1.00 13.00  ? 2063 GLU A CB    1 
ATOM   5901  C CG    . GLU A 1 2063 ? 201.899 186.416 194.219 1.00 13.00  ? 2063 GLU A CG    1 
ATOM   5902  C CD    . GLU A 1 2063 ? 203.278 186.038 194.723 1.00 13.00  ? 2063 GLU A CD    1 
ATOM   5903  O OE1   . GLU A 1 2063 ? 204.267 186.299 194.007 1.00 13.00  ? 2063 GLU A OE1   1 
ATOM   5904  O OE2   . GLU A 1 2063 ? 203.371 185.481 195.837 1.00 13.00  ? 2063 GLU A OE2   1 
ATOM   5905  N N     . VAL A 1 2064 ? 199.068 188.643 195.174 1.00 13.67  ? 2064 VAL A N     1 
ATOM   5906  C CA    . VAL A 1 2064 ? 197.960 188.350 196.078 1.00 13.67  ? 2064 VAL A CA    1 
ATOM   5907  C C     . VAL A 1 2064 ? 196.628 188.534 195.363 1.00 13.67  ? 2064 VAL A C     1 
ATOM   5908  O O     . VAL A 1 2064 ? 195.697 187.734 195.530 1.00 13.67  ? 2064 VAL A O     1 
ATOM   5909  C CB    . VAL A 1 2064 ? 198.052 189.231 197.336 1.00 13.67  ? 2064 VAL A CB    1 
ATOM   5910  C CG1   . VAL A 1 2064 ? 196.963 188.859 198.323 1.00 13.67  ? 2064 VAL A CG1   1 
ATOM   5911  C CG2   . VAL A 1 2064 ? 199.423 189.098 197.973 1.00 13.67  ? 2064 VAL A CG2   1 
ATOM   5912  N N     . LEU A 1 2065 ? 196.517 189.588 194.555 1.00 13.75  ? 2065 LEU A N     1 
ATOM   5913  C CA    . LEU A 1 2065 ? 195.273 189.837 193.838 1.00 13.75  ? 2065 LEU A CA    1 
ATOM   5914  C C     . LEU A 1 2065 ? 194.962 188.713 192.860 1.00 13.75  ? 2065 LEU A C     1 
ATOM   5915  O O     . LEU A 1 2065 ? 193.805 188.312 192.719 1.00 13.75  ? 2065 LEU A O     1 
ATOM   5916  C CB    . LEU A 1 2065 ? 195.344 191.180 193.115 1.00 13.75  ? 2065 LEU A CB    1 
ATOM   5917  C CG    . LEU A 1 2065 ? 195.298 192.406 194.025 1.00 13.75  ? 2065 LEU A CG    1 
ATOM   5918  C CD1   . LEU A 1 2065 ? 194.950 193.645 193.226 1.00 13.75  ? 2065 LEU A CD1   1 
ATOM   5919  C CD2   . LEU A 1 2065 ? 194.305 192.197 195.152 1.00 13.75  ? 2065 LEU A CD2   1 
ATOM   5920  N N     . ALA A 1 2066 ? 195.980 188.190 192.174 1.00 13.48  ? 2066 ALA A N     1 
ATOM   5921  C CA    . ALA A 1 2066 ? 195.758 187.069 191.265 1.00 13.48  ? 2066 ALA A CA    1 
ATOM   5922  C C     . ALA A 1 2066 ? 195.368 185.810 192.030 1.00 13.48  ? 2066 ALA A C     1 
ATOM   5923  O O     . ALA A 1 2066 ? 194.432 185.094 191.641 1.00 13.48  ? 2066 ALA A O     1 
ATOM   5924  C CB    . ALA A 1 2066 ? 197.008 186.821 190.425 1.00 13.48  ? 2066 ALA A CB    1 
ATOM   5925  N N     . ASN A 1 2067 ? 196.080 185.524 193.126 1.00 15.37  ? 2067 ASN A N     1 
ATOM   5926  C CA    . ASN A 1 2067 ? 195.769 184.355 193.940 1.00 15.37  ? 2067 ASN A CA    1 
ATOM   5927  C C     . ASN A 1 2067 ? 194.387 184.444 194.567 1.00 15.37  ? 2067 ASN A C     1 
ATOM   5928  O O     . ASN A 1 2067 ? 193.840 183.418 194.982 1.00 15.37  ? 2067 ASN A O     1 
ATOM   5929  C CB    . ASN A 1 2067 ? 196.821 184.177 195.035 1.00 15.37  ? 2067 ASN A CB    1 
ATOM   5930  C CG    . ASN A 1 2067 ? 198.177 183.796 194.484 1.00 15.37  ? 2067 ASN A CG    1 
ATOM   5931  O OD1   . ASN A 1 2067 ? 198.442 183.952 193.293 1.00 15.37  ? 2067 ASN A OD1   1 
ATOM   5932  N ND2   . ASN A 1 2067 ? 199.047 183.292 195.350 1.00 15.37  ? 2067 ASN A ND2   1 
ATOM   5933  N N     . LYS A 1 2068 ? 193.827 185.646 194.675 1.00 13.69  ? 2068 LYS A N     1 
ATOM   5934  C CA    . LYS A 1 2068 ? 192.449 185.786 195.130 1.00 13.69  ? 2068 LYS A CA    1 
ATOM   5935  C C     . LYS A 1 2068 ? 191.447 185.739 193.982 1.00 13.69  ? 2068 LYS A C     1 
ATOM   5936  O O     . LYS A 1 2068 ? 190.354 185.188 194.138 1.00 13.69  ? 2068 LYS A O     1 
ATOM   5937  C CB    . LYS A 1 2068 ? 192.280 187.092 195.909 1.00 13.69  ? 2068 LYS A CB    1 
ATOM   5938  C CG    . LYS A 1 2068 ? 192.959 187.096 197.265 1.00 13.69  ? 2068 LYS A CG    1 
ATOM   5939  C CD    . LYS A 1 2068 ? 192.688 188.386 198.015 1.00 13.69  ? 2068 LYS A CD    1 
ATOM   5940  C CE    . LYS A 1 2068 ? 193.407 188.405 199.350 1.00 13.69  ? 2068 LYS A CE    1 
ATOM   5941  N NZ    . LYS A 1 2068 ? 192.856 187.388 200.285 1.00 13.69  ? 2068 LYS A NZ    1 
ATOM   5942  N N     . ILE A 1 2069 ? 191.799 186.296 192.822 1.00 11.13  ? 2069 ILE A N     1 
ATOM   5943  C CA    . ILE A 1 2069 ? 190.822 186.464 191.753 1.00 11.13  ? 2069 ILE A CA    1 
ATOM   5944  C C     . ILE A 1 2069 ? 190.654 185.215 190.898 1.00 11.13  ? 2069 ILE A C     1 
ATOM   5945  O O     . ILE A 1 2069 ? 189.588 185.033 190.298 1.00 11.13  ? 2069 ILE A O     1 
ATOM   5946  C CB    . ILE A 1 2069 ? 191.196 187.670 190.872 1.00 11.13  ? 2069 ILE A CB    1 
ATOM   5947  C CG1   . ILE A 1 2069 ? 189.969 188.183 190.120 1.00 11.13  ? 2069 ILE A CG1   1 
ATOM   5948  C CG2   . ILE A 1 2069 ? 192.305 187.315 189.899 1.00 11.13  ? 2069 ILE A CG2   1 
ATOM   5949  C CD1   . ILE A 1 2069 ? 188.902 188.749 191.021 1.00 11.13  ? 2069 ILE A CD1   1 
ATOM   5950  N N     . VAL A 1 2070 ? 191.656 184.344 190.817 1.00 11.69  ? 2070 VAL A N     1 
ATOM   5951  C CA    . VAL A 1 2070 ? 191.493 183.134 190.010 1.00 11.69  ? 2070 VAL A CA    1 
ATOM   5952  C C     . VAL A 1 2070 ? 190.599 182.130 190.738 1.00 11.69  ? 2070 VAL A C     1 
ATOM   5953  O O     . VAL A 1 2070 ? 189.618 181.646 190.144 1.00 11.69  ? 2070 VAL A O     1 
ATOM   5954  C CB    . VAL A 1 2070 ? 192.851 182.521 189.633 1.00 11.69  ? 2070 VAL A CB    1 
ATOM   5955  C CG1   . VAL A 1 2070 ? 192.647 181.208 188.901 1.00 11.69  ? 2070 VAL A CG1   1 
ATOM   5956  C CG2   . VAL A 1 2070 ? 193.644 183.493 188.780 1.00 11.69  ? 2070 VAL A CG2   1 
ATOM   5957  N N     . PRO A 1 2071 ? 190.871 181.779 192.004 1.00 12.75  ? 2071 PRO A N     1 
ATOM   5958  C CA    . PRO A 1 2071 ? 189.931 180.897 192.713 1.00 12.75  ? 2071 PRO A CA    1 
ATOM   5959  C C     . PRO A 1 2071 ? 188.540 181.481 192.827 1.00 12.75  ? 2071 PRO A C     1 
ATOM   5960  O O     . PRO A 1 2071 ? 187.565 180.724 192.848 1.00 12.75  ? 2071 PRO A O     1 
ATOM   5961  C CB    . PRO A 1 2071 ? 190.583 180.721 194.091 1.00 12.75  ? 2071 PRO A CB    1 
ATOM   5962  C CG    . PRO A 1 2071 ? 192.013 180.993 193.865 1.00 12.75  ? 2071 PRO A CG    1 
ATOM   5963  C CD    . PRO A 1 2071 ? 192.038 182.086 192.850 1.00 12.75  ? 2071 PRO A CD    1 
ATOM   5964  N N     . PHE A 1 2072 ? 188.413 182.807 192.904 1.00 10.51  ? 2072 PHE A N     1 
ATOM   5965  C CA    . PHE A 1 2072 ? 187.088 183.412 192.980 1.00 10.51  ? 2072 PHE A CA    1 
ATOM   5966  C C     . PHE A 1 2072 ? 186.290 183.155 191.708 1.00 10.51  ? 2072 PHE A C     1 
ATOM   5967  O O     . PHE A 1 2072 ? 185.097 182.839 191.768 1.00 10.51  ? 2072 PHE A O     1 
ATOM   5968  C CB    . PHE A 1 2072 ? 187.206 184.910 193.246 1.00 10.51  ? 2072 PHE A CB    1 
ATOM   5969  C CG    . PHE A 1 2072 ? 185.932 185.660 193.017 1.00 10.51  ? 2072 PHE A CG    1 
ATOM   5970  C CD1   . PHE A 1 2072 ? 184.874 185.536 193.898 1.00 10.51  ? 2072 PHE A CD1   1 
ATOM   5971  C CD2   . PHE A 1 2072 ? 185.787 186.485 191.918 1.00 10.51  ? 2072 PHE A CD2   1 
ATOM   5972  C CE1   . PHE A 1 2072 ? 183.700 186.222 193.688 1.00 10.51  ? 2072 PHE A CE1   1 
ATOM   5973  C CE2   . PHE A 1 2072 ? 184.615 187.173 191.704 1.00 10.51  ? 2072 PHE A CE2   1 
ATOM   5974  C CZ    . PHE A 1 2072 ? 183.571 187.043 192.590 1.00 10.51  ? 2072 PHE A CZ    1 
ATOM   5975  N N     . PHE A 1 2073 ? 186.929 183.284 190.543 1.00 10.80  ? 2073 PHE A N     1 
ATOM   5976  C CA    . PHE A 1 2073 ? 186.230 182.974 189.300 1.00 10.80  ? 2073 PHE A CA    1 
ATOM   5977  C C     . PHE A 1 2073 ? 185.956 181.483 189.170 1.00 10.80  ? 2073 PHE A C     1 
ATOM   5978  O O     . PHE A 1 2073 ? 184.935 181.086 188.597 1.00 10.80  ? 2073 PHE A O     1 
ATOM   5979  C CB    . PHE A 1 2073 ? 187.013 183.493 188.096 1.00 10.80  ? 2073 PHE A CB    1 
ATOM   5980  C CG    . PHE A 1 2073 ? 186.819 184.957 187.841 1.00 10.80  ? 2073 PHE A CG    1 
ATOM   5981  C CD1   . PHE A 1 2073 ? 185.791 185.645 188.460 1.00 10.80  ? 2073 PHE A CD1   1 
ATOM   5982  C CD2   . PHE A 1 2073 ? 187.642 185.640 186.968 1.00 10.80  ? 2073 PHE A CD2   1 
ATOM   5983  C CE1   . PHE A 1 2073 ? 185.598 186.988 188.226 1.00 10.80  ? 2073 PHE A CE1   1 
ATOM   5984  C CE2   . PHE A 1 2073 ? 187.450 186.985 186.731 1.00 10.80  ? 2073 PHE A CE2   1 
ATOM   5985  C CZ    . PHE A 1 2073 ? 186.428 187.659 187.360 1.00 10.80  ? 2073 PHE A CZ    1 
ATOM   5986  N N     . LYS A 1 2074 ? 186.844 180.637 189.700 1.00 13.19  ? 2074 LYS A N     1 
ATOM   5987  C CA    . LYS A 1 2074 ? 186.533 179.209 189.727 1.00 13.19  ? 2074 LYS A CA    1 
ATOM   5988  C C     . LYS A 1 2074 ? 185.283 178.938 190.561 1.00 13.19  ? 2074 LYS A C     1 
ATOM   5989  O O     . LYS A 1 2074 ? 184.408 178.162 190.155 1.00 13.19  ? 2074 LYS A O     1 
ATOM   5990  C CB    . LYS A 1 2074 ? 187.725 178.419 190.266 1.00 13.19  ? 2074 LYS A CB    1 
ATOM   5991  C CG    . LYS A 1 2074 ? 187.758 176.971 189.809 1.00 13.19  ? 2074 LYS A CG    1 
ATOM   5992  C CD    . LYS A 1 2074 ? 189.180 176.434 189.769 1.00 13.19  ? 2074 LYS A CD    1 
ATOM   5993  C CE    . LYS A 1 2074 ? 189.827 176.480 191.143 1.00 13.19  ? 2074 LYS A CE    1 
ATOM   5994  N NZ    . LYS A 1 2074 ? 188.988 175.810 192.175 1.00 13.19  ? 2074 LYS A NZ    1 
ATOM   5995  N N     . LEU A 1 2075 ? 185.177 179.586 191.723 1.00 12.38  ? 2075 LEU A N     1 
ATOM   5996  C CA    . LEU A 1 2075 ? 183.985 179.447 192.554 1.00 12.38  ? 2075 LEU A CA    1 
ATOM   5997  C C     . LEU A 1 2075 ? 182.746 179.944 191.824 1.00 12.38  ? 2075 LEU A C     1 
ATOM   5998  O O     . LEU A 1 2075 ? 181.695 179.294 191.853 1.00 12.38  ? 2075 LEU A O     1 
ATOM   5999  C CB    . LEU A 1 2075 ? 184.158 180.215 193.864 1.00 12.38  ? 2075 LEU A CB    1 
ATOM   6000  C CG    . LEU A 1 2075 ? 185.295 179.840 194.810 1.00 12.38  ? 2075 LEU A CG    1 
ATOM   6001  C CD1   . LEU A 1 2075 ? 184.961 180.286 196.218 1.00 12.38  ? 2075 LEU A CD1   1 
ATOM   6002  C CD2   . LEU A 1 2075 ? 185.578 178.352 194.763 1.00 12.38  ? 2075 LEU A CD2   1 
ATOM   6003  N N     . CYS A 1 2076 ? 182.852 181.100 191.166 1.00 14.02  ? 2076 CYS A N     1 
ATOM   6004  C CA    . CYS A 1 2076 ? 181.715 181.641 190.430 1.00 14.02  ? 2076 CYS A CA    1 
ATOM   6005  C C     . CYS A 1 2076 ? 181.266 180.693 189.330 1.00 14.02  ? 2076 CYS A C     1 
ATOM   6006  O O     . CYS A 1 2076 ? 180.062 180.517 189.115 1.00 14.02  ? 2076 CYS A O     1 
ATOM   6007  C CB    . CYS A 1 2076 ? 182.071 183.005 189.842 1.00 14.02  ? 2076 CYS A CB    1 
ATOM   6008  S SG    . CYS A 1 2076 ? 182.059 184.350 191.037 1.00 14.02  ? 2076 CYS A SG    1 
ATOM   6009  N N     . ASP A 1 2077 ? 182.213 180.078 188.623 1.00 14.76  ? 2077 ASP A N     1 
ATOM   6010  C CA    . ASP A 1 2077 ? 181.853 179.070 187.634 1.00 14.76  ? 2077 ASP A CA    1 
ATOM   6011  C C     . ASP A 1 2077 ? 181.222 177.847 188.286 1.00 14.76  ? 2077 ASP A C     1 
ATOM   6012  O O     . ASP A 1 2077 ? 180.389 177.178 187.664 1.00 14.76  ? 2077 ASP A O     1 
ATOM   6013  C CB    . ASP A 1 2077 ? 183.084 178.666 186.825 1.00 14.76  ? 2077 ASP A CB    1 
ATOM   6014  C CG    . ASP A 1 2077 ? 182.752 177.709 185.701 1.00 14.76  ? 2077 ASP A CG    1 
ATOM   6015  O OD1   . ASP A 1 2077 ? 182.178 178.158 184.688 1.00 14.76  ? 2077 ASP A OD1   1 
ATOM   6016  O OD2   . ASP A 1 2077 ? 183.063 176.507 185.831 1.00 14.76  ? 2077 ASP A OD2   1 
ATOM   6017  N N     . GLU A 1 2078 ? 181.596 177.540 189.530 1.00 16.66  ? 2078 GLU A N     1 
ATOM   6018  C CA    . GLU A 1 2078 ? 181.085 176.356 190.216 1.00 16.66  ? 2078 GLU A CA    1 
ATOM   6019  C C     . GLU A 1 2078 ? 179.883 176.662 191.106 1.00 16.66  ? 2078 GLU A C     1 
ATOM   6020  O O     . GLU A 1 2078 ? 178.813 176.073 190.930 1.00 16.66  ? 2078 GLU A O     1 
ATOM   6021  C CB    . GLU A 1 2078 ? 182.203 175.711 191.045 1.00 16.66  ? 2078 GLU A CB    1 
ATOM   6022  C CG    . GLU A 1 2078 ? 183.027 174.687 190.285 1.00 16.66  ? 2078 GLU A CG    1 
ATOM   6023  C CD    . GLU A 1 2078 ? 184.031 173.978 191.171 1.00 16.66  ? 2078 GLU A CD    1 
ATOM   6024  O OE1   . GLU A 1 2078 ? 183.961 174.150 192.406 1.00 16.66  ? 2078 GLU A OE1   1 
ATOM   6025  O OE2   . GLU A 1 2078 ? 184.891 173.249 190.633 1.00 16.66  ? 2078 GLU A OE2   1 
ATOM   6026  N N     . GLN A 1 2079 ? 180.043 177.574 192.069 1.00 19.57  ? 2079 GLN A N     1 
ATOM   6027  C CA    . GLN A 1 2079 ? 179.000 177.790 193.069 1.00 19.57  ? 2079 GLN A CA    1 
ATOM   6028  C C     . GLN A 1 2079 ? 177.743 178.401 192.461 1.00 19.57  ? 2079 GLN A C     1 
ATOM   6029  O O     . GLN A 1 2079 ? 176.625 178.009 192.814 1.00 19.57  ? 2079 GLN A O     1 
ATOM   6030  C CB    . GLN A 1 2079 ? 179.530 178.674 194.196 1.00 19.57  ? 2079 GLN A CB    1 
ATOM   6031  C CG    . GLN A 1 2079 ? 180.741 178.105 194.912 1.00 19.57  ? 2079 GLN A CG    1 
ATOM   6032  C CD    . GLN A 1 2079 ? 180.366 177.080 195.959 1.00 19.57  ? 2079 GLN A CD    1 
ATOM   6033  O OE1   . GLN A 1 2079 ? 179.698 177.396 196.942 1.00 19.57  ? 2079 GLN A OE1   1 
ATOM   6034  N NE2   . GLN A 1 2079 ? 180.797 175.842 195.755 1.00 19.57  ? 2079 GLN A NE2   1 
ATOM   6035  N N     . LEU A 1 2080 ? 177.901 179.362 191.556 1.00 16.70  ? 2080 LEU A N     1 
ATOM   6036  C CA    . LEU A 1 2080 ? 176.751 180.044 190.984 1.00 16.70  ? 2080 LEU A CA    1 
ATOM   6037  C C     . LEU A 1 2080 ? 175.960 179.109 190.072 1.00 16.70  ? 2080 LEU A C     1 
ATOM   6038  O O     . LEU A 1 2080 ? 176.449 178.071 189.620 1.00 16.70  ? 2080 LEU A O     1 
ATOM   6039  C CB    . LEU A 1 2080 ? 177.190 181.283 190.206 1.00 16.70  ? 2080 LEU A CB    1 
ATOM   6040  C CG    . LEU A 1 2080 ? 177.205 182.609 190.966 1.00 16.70  ? 2080 LEU A CG    1 
ATOM   6041  C CD1   . LEU A 1 2080 ? 178.279 182.614 192.031 1.00 16.70  ? 2080 LEU A CD1   1 
ATOM   6042  C CD2   . LEU A 1 2080 ? 177.413 183.759 190.001 1.00 16.70  ? 2080 LEU A CD2   1 
ATOM   6043  N N     . SER A 1 2081 ? 174.716 179.496 189.808 1.00 16.26  ? 2081 SER A N     1 
ATOM   6044  C CA    . SER A 1 2081 ? 173.834 178.698 188.973 1.00 16.26  ? 2081 SER A CA    1 
ATOM   6045  C C     . SER A 1 2081 ? 174.336 178.680 187.531 1.00 16.26  ? 2081 SER A C     1 
ATOM   6046  O O     . SER A 1 2081 ? 175.149 179.506 187.111 1.00 16.26  ? 2081 SER A O     1 
ATOM   6047  C CB    . SER A 1 2081 ? 172.408 179.240 189.034 1.00 16.26  ? 2081 SER A CB    1 
ATOM   6048  O OG    . SER A 1 2081 ? 172.309 180.483 188.363 1.00 16.26  ? 2081 SER A OG    1 
ATOM   6049  N N     . SER A 1 2082 ? 173.838 177.712 186.768 1.00 15.68  ? 2082 SER A N     1 
ATOM   6050  C CA    . SER A 1 2082 ? 174.241 177.535 185.380 1.00 15.68  ? 2082 SER A CA    1 
ATOM   6051  C C     . SER A 1 2082 ? 173.325 178.356 184.481 1.00 15.68  ? 2082 SER A C     1 
ATOM   6052  O O     . SER A 1 2082 ? 172.108 178.146 184.467 1.00 15.68  ? 2082 SER A O     1 
ATOM   6053  C CB    . SER A 1 2082 ? 174.195 176.058 184.990 1.00 15.68  ? 2082 SER A CB    1 
ATOM   6054  O OG    . SER A 1 2082 ? 174.551 175.878 183.631 1.00 15.68  ? 2082 SER A OG    1 
ATOM   6055  N N     . GLN A 1 2083 ? 173.910 179.289 183.734 1.00 16.49  ? 2083 GLN A N     1 
ATOM   6056  C CA    . GLN A 1 2083 ? 173.168 180.132 182.811 1.00 16.49  ? 2083 GLN A CA    1 
ATOM   6057  C C     . GLN A 1 2083 ? 173.917 180.223 181.490 1.00 16.49  ? 2083 GLN A C     1 
ATOM   6058  O O     . GLN A 1 2083 ? 175.143 180.092 181.442 1.00 16.49  ? 2083 GLN A O     1 
ATOM   6059  C CB    . GLN A 1 2083 ? 172.941 181.535 183.385 1.00 16.49  ? 2083 GLN A CB    1 
ATOM   6060  C CG    . GLN A 1 2083 ? 172.037 181.562 184.605 1.00 16.49  ? 2083 GLN A CG    1 
ATOM   6061  C CD    . GLN A 1 2083 ? 170.569 181.587 184.239 1.00 16.49  ? 2083 GLN A CD    1 
ATOM   6062  O OE1   . GLN A 1 2083 ? 170.212 181.666 183.064 1.00 16.49  ? 2083 GLN A OE1   1 
ATOM   6063  N NE2   . GLN A 1 2083 ? 169.707 181.512 185.245 1.00 16.49  ? 2083 GLN A NE2   1 
ATOM   6064  N N     . SER A 1 2084 ? 173.161 180.446 180.414 1.00 13.46  ? 2084 SER A N     1 
ATOM   6065  C CA    . SER A 1 2084 ? 173.763 180.517 179.088 1.00 13.46  ? 2084 SER A CA    1 
ATOM   6066  C C     . SER A 1 2084 ? 174.684 181.723 178.955 1.00 13.46  ? 2084 SER A C     1 
ATOM   6067  O O     . SER A 1 2084 ? 175.753 181.629 178.340 1.00 13.46  ? 2084 SER A O     1 
ATOM   6068  C CB    . SER A 1 2084 ? 172.671 180.559 178.019 1.00 13.46  ? 2084 SER A CB    1 
ATOM   6069  O OG    . SER A 1 2084 ? 173.226 180.766 176.732 1.00 13.46  ? 2084 SER A OG    1 
ATOM   6070  N N     . HIS A 1 2085 ? 174.291 182.861 179.521 1.00 16.65  ? 2085 HIS A N     1 
ATOM   6071  C CA    . HIS A 1 2085 ? 175.031 184.102 179.340 1.00 16.65  ? 2085 HIS A CA    1 
ATOM   6072  C C     . HIS A 1 2085 ? 176.194 184.263 180.309 1.00 16.65  ? 2085 HIS A C     1 
ATOM   6073  O O     . HIS A 1 2085 ? 176.987 185.196 180.144 1.00 16.65  ? 2085 HIS A O     1 
ATOM   6074  C CB    . HIS A 1 2085 ? 174.088 185.299 179.480 1.00 16.65  ? 2085 HIS A CB    1 
ATOM   6075  C CG    . HIS A 1 2085 ? 173.480 185.433 180.840 1.00 16.65  ? 2085 HIS A CG    1 
ATOM   6076  N ND1   . HIS A 1 2085 ? 172.451 184.629 181.278 1.00 16.65  ? 2085 HIS A ND1   1 
ATOM   6077  C CD2   . HIS A 1 2085 ? 173.753 186.283 181.858 1.00 16.65  ? 2085 HIS A CD2   1 
ATOM   6078  C CE1   . HIS A 1 2085 ? 172.120 184.973 182.509 1.00 16.65  ? 2085 HIS A CE1   1 
ATOM   6079  N NE2   . HIS A 1 2085 ? 172.894 185.975 182.884 1.00 16.65  ? 2085 HIS A NE2   1 
ATOM   6080  N N     . TYR A 1 2086 ? 176.316 183.393 181.307 1.00 15.80  ? 2086 TYR A N     1 
ATOM   6081  C CA    . TYR A 1 2086 ? 177.439 183.475 182.229 1.00 15.80  ? 2086 TYR A CA    1 
ATOM   6082  C C     . TYR A 1 2086 ? 178.742 183.153 181.511 1.00 15.80  ? 2086 TYR A C     1 
ATOM   6083  O O     . TYR A 1 2086 ? 178.817 182.210 180.718 1.00 15.80  ? 2086 TYR A O     1 
ATOM   6084  C CB    . TYR A 1 2086 ? 177.242 182.515 183.402 1.00 15.80  ? 2086 TYR A CB    1 
ATOM   6085  C CG    . TYR A 1 2086 ? 176.293 183.016 184.464 1.00 15.80  ? 2086 TYR A CG    1 
ATOM   6086  C CD1   . TYR A 1 2086 ? 175.792 184.307 184.425 1.00 15.80  ? 2086 TYR A CD1   1 
ATOM   6087  C CD2   . TYR A 1 2086 ? 175.903 182.195 185.511 1.00 15.80  ? 2086 TYR A CD2   1 
ATOM   6088  C CE1   . TYR A 1 2086 ? 174.926 184.764 185.397 1.00 15.80  ? 2086 TYR A CE1   1 
ATOM   6089  C CE2   . TYR A 1 2086 ? 175.039 182.644 186.486 1.00 15.80  ? 2086 TYR A CE2   1 
ATOM   6090  C CZ    . TYR A 1 2086 ? 174.554 183.928 186.425 1.00 15.80  ? 2086 TYR A CZ    1 
ATOM   6091  O OH    . TYR A 1 2086 ? 173.692 184.376 187.397 1.00 15.80  ? 2086 TYR A OH    1 
ATOM   6092  N N     . ASP A 1 2087 ? 179.774 183.943 181.795 1.00 16.16  ? 2087 ASP A N     1 
ATOM   6093  C CA    . ASP A 1 2087 ? 181.091 183.722 181.204 1.00 16.16  ? 2087 ASP A CA    1 
ATOM   6094  C C     . ASP A 1 2087 ? 182.139 184.053 182.256 1.00 16.16  ? 2087 ASP A C     1 
ATOM   6095  O O     . ASP A 1 2087 ? 182.345 185.226 182.578 1.00 16.16  ? 2087 ASP A O     1 
ATOM   6096  C CB    . ASP A 1 2087 ? 181.287 184.569 179.951 1.00 16.16  ? 2087 ASP A CB    1 
ATOM   6097  C CG    . ASP A 1 2087 ? 182.515 184.163 179.162 1.00 16.16  ? 2087 ASP A CG    1 
ATOM   6098  O OD1   . ASP A 1 2087 ? 182.853 182.961 179.165 1.00 16.16  ? 2087 ASP A OD1   1 
ATOM   6099  O OD2   . ASP A 1 2087 ? 183.144 185.044 178.539 1.00 16.16  ? 2087 ASP A OD2   1 
ATOM   6100  N N     . PHE A 1 2088 ? 182.794 183.023 182.786 1.00 12.51  ? 2088 PHE A N     1 
ATOM   6101  C CA    . PHE A 1 2088 ? 183.849 183.184 183.777 1.00 12.51  ? 2088 PHE A CA    1 
ATOM   6102  C C     . PHE A 1 2088 ? 185.176 182.638 183.261 1.00 12.51  ? 2088 PHE A C     1 
ATOM   6103  O O     . PHE A 1 2088 ? 186.016 182.185 184.039 1.00 12.51  ? 2088 PHE A O     1 
ATOM   6104  C CB    . PHE A 1 2088 ? 183.462 182.510 185.091 1.00 12.51  ? 2088 PHE A CB    1 
ATOM   6105  C CG    . PHE A 1 2088 ? 182.210 183.062 185.706 1.00 12.51  ? 2088 PHE A CG    1 
ATOM   6106  C CD1   . PHE A 1 2088 ? 182.213 184.299 186.323 1.00 12.51  ? 2088 PHE A CD1   1 
ATOM   6107  C CD2   . PHE A 1 2088 ? 181.028 182.344 185.663 1.00 12.51  ? 2088 PHE A CD2   1 
ATOM   6108  C CE1   . PHE A 1 2088 ? 181.063 184.808 186.888 1.00 12.51  ? 2088 PHE A CE1   1 
ATOM   6109  C CE2   . PHE A 1 2088 ? 179.875 182.850 186.227 1.00 12.51  ? 2088 PHE A CE2   1 
ATOM   6110  C CZ    . PHE A 1 2088 ? 179.893 184.084 186.839 1.00 12.51  ? 2088 PHE A CZ    1 
ATOM   6111  N N     . GLY A 1 2089 ? 185.373 182.681 181.946 1.00 15.40  ? 2089 GLY A N     1 
ATOM   6112  C CA    . GLY A 1 2089 ? 186.574 182.143 181.340 1.00 15.40  ? 2089 GLY A CA    1 
ATOM   6113  C C     . GLY A 1 2089 ? 187.769 183.063 181.454 1.00 15.40  ? 2089 GLY A C     1 
ATOM   6114  O O     . GLY A 1 2089 ? 187.756 184.019 182.234 1.00 15.40  ? 2089 GLY A O     1 
ATOM   6115  N N     . LEU A 1 2090 ? 188.815 182.779 180.676 1.00 19.45  ? 2090 LEU A N     1 
ATOM   6116  C CA    . LEU A 1 2090 ? 190.035 183.576 180.756 1.00 19.45  ? 2090 LEU A CA    1 
ATOM   6117  C C     . LEU A 1 2090 ? 189.842 184.954 180.136 1.00 19.45  ? 2090 LEU A C     1 
ATOM   6118  O O     . LEU A 1 2090 ? 190.393 185.946 180.630 1.00 19.45  ? 2090 LEU A O     1 
ATOM   6119  C CB    . LEU A 1 2090 ? 191.183 182.832 180.077 1.00 19.45  ? 2090 LEU A CB    1 
ATOM   6120  C CG    . LEU A 1 2090 ? 192.598 183.306 180.394 1.00 19.45  ? 2090 LEU A CG    1 
ATOM   6121  C CD1   . LEU A 1 2090 ? 192.759 183.554 181.881 1.00 19.45  ? 2090 LEU A CD1   1 
ATOM   6122  C CD2   . LEU A 1 2090 ? 193.598 182.273 179.916 1.00 19.45  ? 2090 LEU A CD2   1 
ATOM   6123  N N     . ARG A 1 2091 ? 189.071 185.037 179.049 1.00 18.87  ? 2091 ARG A N     1 
ATOM   6124  C CA    . ARG A 1 2091 ? 188.812 186.331 178.425 1.00 18.87  ? 2091 ARG A CA    1 
ATOM   6125  C C     . ARG A 1 2091 ? 188.060 187.257 179.370 1.00 18.87  ? 2091 ARG A C     1 
ATOM   6126  O O     . ARG A 1 2091 ? 188.369 188.452 179.459 1.00 18.87  ? 2091 ARG A O     1 
ATOM   6127  C CB    . ARG A 1 2091 ? 188.026 186.140 177.129 1.00 18.87  ? 2091 ARG A CB    1 
ATOM   6128  C CG    . ARG A 1 2091 ? 187.907 187.399 176.293 1.00 18.87  ? 2091 ARG A CG    1 
ATOM   6129  C CD    . ARG A 1 2091 ? 187.223 187.117 174.967 1.00 18.87  ? 2091 ARG A CD    1 
ATOM   6130  N NE    . ARG A 1 2091 ? 187.822 185.985 174.272 1.00 18.87  ? 2091 ARG A NE    1 
ATOM   6131  C CZ    . ARG A 1 2091 ? 188.493 186.077 173.132 1.00 18.87  ? 2091 ARG A CZ    1 
ATOM   6132  N NH1   . ARG A 1 2091 ? 188.679 187.241 172.532 1.00 18.87  ? 2091 ARG A NH1   1 
ATOM   6133  N NH2   . ARG A 1 2091 ? 188.990 184.974 172.580 1.00 18.87  ? 2091 ARG A NH2   1 
ATOM   6134  N N     . ALA A 1 2092 ? 187.067 186.723 180.084 1.00 14.37  ? 2092 ALA A N     1 
ATOM   6135  C CA    . ALA A 1 2092 ? 186.342 187.530 181.058 1.00 14.37  ? 2092 ALA A CA    1 
ATOM   6136  C C     . ALA A 1 2092 ? 187.265 188.002 182.171 1.00 14.37  ? 2092 ALA A C     1 
ATOM   6137  O O     . ALA A 1 2092 ? 187.171 189.150 182.619 1.00 14.37  ? 2092 ALA A O     1 
ATOM   6138  C CB    . ALA A 1 2092 ? 185.170 186.736 181.631 1.00 14.37  ? 2092 ALA A CB    1 
ATOM   6139  N N     . LEU A 1 2093 ? 188.164 187.129 182.632 1.00 11.78  ? 2093 LEU A N     1 
ATOM   6140  C CA    . LEU A 1 2093 ? 189.115 187.524 183.665 1.00 11.78  ? 2093 LEU A CA    1 
ATOM   6141  C C     . LEU A 1 2093 ? 190.021 188.650 183.182 1.00 11.78  ? 2093 LEU A C     1 
ATOM   6142  O O     . LEU A 1 2093 ? 190.266 189.614 183.915 1.00 11.78  ? 2093 LEU A O     1 
ATOM   6143  C CB    . LEU A 1 2093 ? 189.939 186.313 184.104 1.00 11.78  ? 2093 LEU A CB    1 
ATOM   6144  C CG    . LEU A 1 2093 ? 191.204 186.565 184.924 1.00 11.78  ? 2093 LEU A CG    1 
ATOM   6145  C CD1   . LEU A 1 2093 ? 190.884 187.275 186.225 1.00 11.78  ? 2093 LEU A CD1   1 
ATOM   6146  C CD2   . LEU A 1 2093 ? 191.919 185.254 185.196 1.00 11.78  ? 2093 LEU A CD2   1 
ATOM   6147  N N     . LYS A 1 2094 ? 190.518 188.553 181.948 1.00 12.98  ? 2094 LYS A N     1 
ATOM   6148  C CA    . LYS A 1 2094 ? 191.373 189.612 181.418 1.00 12.98  ? 2094 LYS A CA    1 
ATOM   6149  C C     . LYS A 1 2094 ? 190.608 190.922 181.269 1.00 12.98  ? 2094 LYS A C     1 
ATOM   6150  O O     . LYS A 1 2094 ? 191.148 192.002 181.545 1.00 12.98  ? 2094 LYS A O     1 
ATOM   6151  C CB    . LYS A 1 2094 ? 191.976 189.183 180.082 1.00 12.98  ? 2094 LYS A CB    1 
ATOM   6152  C CG    . LYS A 1 2094 ? 192.898 187.981 180.177 1.00 12.98  ? 2094 LYS A CG    1 
ATOM   6153  C CD    . LYS A 1 2094 ? 193.254 187.459 178.800 1.00 12.98  ? 2094 LYS A CD    1 
ATOM   6154  C CE    . LYS A 1 2094 ? 193.937 188.527 177.966 1.00 12.98  ? 2094 LYS A CE    1 
ATOM   6155  N NZ    . LYS A 1 2094 ? 195.354 188.724 178.370 1.00 12.98  ? 2094 LYS A NZ    1 
ATOM   6156  N N     . SER A 1 2095 ? 189.353 190.851 180.819 1.00 11.48  ? 2095 SER A N     1 
ATOM   6157  C CA    . SER A 1 2095 ? 188.544 192.061 180.707 1.00 11.48  ? 2095 SER A CA    1 
ATOM   6158  C C     . SER A 1 2095 ? 188.313 192.698 182.071 1.00 11.48  ? 2095 SER A C     1 
ATOM   6159  O O     . SER A 1 2095 ? 188.394 193.925 182.217 1.00 11.48  ? 2095 SER A O     1 
ATOM   6160  C CB    . SER A 1 2095 ? 187.213 191.742 180.030 1.00 11.48  ? 2095 SER A CB    1 
ATOM   6161  O OG    . SER A 1 2095 ? 187.411 191.346 178.684 1.00 11.48  ? 2095 SER A OG    1 
ATOM   6162  N N     . VAL A 1 2096 ? 188.032 191.881 183.087 1.00 10.81  ? 2096 VAL A N     1 
ATOM   6163  C CA    . VAL A 1 2096 ? 187.860 192.411 184.436 1.00 10.81  ? 2096 VAL A CA    1 
ATOM   6164  C C     . VAL A 1 2096 ? 189.155 193.040 184.931 1.00 10.81  ? 2096 VAL A C     1 
ATOM   6165  O O     . VAL A 1 2096 ? 189.138 194.068 185.614 1.00 10.81  ? 2096 VAL A O     1 
ATOM   6166  C CB    . VAL A 1 2096 ? 187.362 191.308 185.388 1.00 10.81  ? 2096 VAL A CB    1 
ATOM   6167  C CG1   . VAL A 1 2096 ? 187.307 191.826 186.806 1.00 10.81  ? 2096 VAL A CG1   1 
ATOM   6168  C CG2   . VAL A 1 2096 ? 185.985 190.837 184.963 1.00 10.81  ? 2096 VAL A CG2   1 
ATOM   6169  N N     . LEU A 1 2097 ? 190.297 192.442 184.590 1.00 11.34  ? 2097 LEU A N     1 
ATOM   6170  C CA    . LEU A 1 2097 ? 191.573 193.000 185.031 1.00 11.34  ? 2097 LEU A CA    1 
ATOM   6171  C C     . LEU A 1 2097 ? 191.852 194.351 184.381 1.00 11.34  ? 2097 LEU A C     1 
ATOM   6172  O O     . LEU A 1 2097 ? 192.302 195.287 185.054 1.00 11.34  ? 2097 LEU A O     1 
ATOM   6173  C CB    . LEU A 1 2097 ? 192.703 192.018 184.739 1.00 11.34  ? 2097 LEU A CB    1 
ATOM   6174  C CG    . LEU A 1 2097 ? 192.675 190.748 185.588 1.00 11.34  ? 2097 LEU A CG    1 
ATOM   6175  C CD1   . LEU A 1 2097 ? 193.899 189.905 185.315 1.00 11.34  ? 2097 LEU A CD1   1 
ATOM   6176  C CD2   . LEU A 1 2097 ? 192.569 191.085 187.064 1.00 11.34  ? 2097 LEU A CD2   1 
ATOM   6177  N N     . VAL A 1 2098 ? 191.597 194.478 183.076 1.00 12.34  ? 2098 VAL A N     1 
ATOM   6178  C CA    . VAL A 1 2098 ? 191.820 195.774 182.438 1.00 12.34  ? 2098 VAL A CA    1 
ATOM   6179  C C     . VAL A 1 2098 ? 190.826 196.807 182.961 1.00 12.34  ? 2098 VAL A C     1 
ATOM   6180  O O     . VAL A 1 2098 ? 191.172 197.986 183.120 1.00 12.34  ? 2098 VAL A O     1 
ATOM   6181  C CB    . VAL A 1 2098 ? 191.784 195.664 180.899 1.00 12.34  ? 2098 VAL A CB    1 
ATOM   6182  C CG1   . VAL A 1 2098 ? 192.725 194.572 180.423 1.00 12.34  ? 2098 VAL A CG1   1 
ATOM   6183  C CG2   . VAL A 1 2098 ? 190.377 195.427 180.383 1.00 12.34  ? 2098 VAL A CG2   1 
ATOM   6184  N N     . SER A 1 2099 ? 189.591 196.392 183.258 1.00 12.29  ? 2099 SER A N     1 
ATOM   6185  C CA    . SER A 1 2099 ? 188.634 197.319 183.854 1.00 12.29  ? 2099 SER A CA    1 
ATOM   6186  C C     . SER A 1 2099 ? 189.094 197.769 185.235 1.00 12.29  ? 2099 SER A C     1 
ATOM   6187  O O     . SER A 1 2099 ? 188.937 198.939 185.599 1.00 12.29  ? 2099 SER A O     1 
ATOM   6188  C CB    . SER A 1 2099 ? 187.253 196.671 183.930 1.00 12.29  ? 2099 SER A CB    1 
ATOM   6189  O OG    . SER A 1 2099 ? 186.653 196.597 182.649 1.00 12.29  ? 2099 SER A OG    1 
ATOM   6190  N N     . ALA A 1 2100 ? 189.662 196.851 186.020 1.00 11.84  ? 2100 ALA A N     1 
ATOM   6191  C CA    . ALA A 1 2100 ? 190.182 197.213 187.333 1.00 11.84  ? 2100 ALA A CA    1 
ATOM   6192  C C     . ALA A 1 2100 ? 191.350 198.181 187.214 1.00 11.84  ? 2100 ALA A C     1 
ATOM   6193  O O     . ALA A 1 2100 ? 191.477 199.113 188.015 1.00 11.84  ? 2100 ALA A O     1 
ATOM   6194  C CB    . ALA A 1 2100 ? 190.602 195.957 188.095 1.00 11.84  ? 2100 ALA A CB    1 
ATOM   6195  N N     . GLY A 1 2101 ? 192.219 197.968 186.227 1.00 13.08  ? 2101 GLY A N     1 
ATOM   6196  C CA    . GLY A 1 2101 ? 193.293 198.920 185.992 1.00 13.08  ? 2101 GLY A CA    1 
ATOM   6197  C C     . GLY A 1 2101 ? 192.774 200.299 185.630 1.00 13.08  ? 2101 GLY A C     1 
ATOM   6198  O O     . GLY A 1 2101 ? 193.275 201.315 186.126 1.00 13.08  ? 2101 GLY A O     1 
ATOM   6199  N N     . ASN A 1 2102 ? 191.755 200.352 184.769 1.00 15.21  ? 2102 ASN A N     1 
ATOM   6200  C CA    . ASN A 1 2102 ? 191.151 201.634 184.416 1.00 15.21  ? 2102 ASN A CA    1 
ATOM   6201  C C     . ASN A 1 2102 ? 190.534 202.307 185.636 1.00 15.21  ? 2102 ASN A C     1 
ATOM   6202  O O     . ASN A 1 2102 ? 190.663 203.524 185.814 1.00 15.21  ? 2102 ASN A O     1 
ATOM   6203  C CB    . ASN A 1 2102 ? 190.098 201.437 183.327 1.00 15.21  ? 2102 ASN A CB    1 
ATOM   6204  C CG    . ASN A 1 2102 ? 190.708 201.230 181.958 1.00 15.21  ? 2102 ASN A CG    1 
ATOM   6205  O OD1   . ASN A 1 2102 ? 191.905 201.437 181.762 1.00 15.21  ? 2102 ASN A OD1   1 
ATOM   6206  N ND2   . ASN A 1 2102 ? 189.885 200.821 181.000 1.00 15.21  ? 2102 ASN A ND2   1 
ATOM   6207  N N     . VAL A 1 2103 ? 189.857 201.531 186.485 1.00 14.65  ? 2103 VAL A N     1 
ATOM   6208  C CA    . VAL A 1 2103 ? 189.245 202.087 187.689 1.00 14.65  ? 2103 VAL A CA    1 
ATOM   6209  C C     . VAL A 1 2103 ? 190.311 202.639 188.626 1.00 14.65  ? 2103 VAL A C     1 
ATOM   6210  O O     . VAL A 1 2103 ? 190.151 203.720 189.207 1.00 14.65  ? 2103 VAL A O     1 
ATOM   6211  C CB    . VAL A 1 2103 ? 188.374 201.024 188.384 1.00 14.65  ? 2103 VAL A CB    1 
ATOM   6212  C CG1   . VAL A 1 2103 ? 188.005 201.469 189.786 1.00 14.65  ? 2103 VAL A CG1   1 
ATOM   6213  C CG2   . VAL A 1 2103 ? 187.123 200.750 187.569 1.00 14.65  ? 2103 VAL A CG2   1 
ATOM   6214  N N     . LYS A 1 2104 ? 191.412 201.904 188.796 1.00 17.15  ? 2104 LYS A N     1 
ATOM   6215  C CA    . LYS A 1 2104 ? 192.489 202.377 189.659 1.00 17.15  ? 2104 LYS A CA    1 
ATOM   6216  C C     . LYS A 1 2104 ? 193.101 203.664 189.124 1.00 17.15  ? 2104 LYS A C     1 
ATOM   6217  O O     . LYS A 1 2104 ? 193.383 204.593 189.891 1.00 17.15  ? 2104 LYS A O     1 
ATOM   6218  C CB    . LYS A 1 2104 ? 193.559 201.297 189.807 1.00 17.15  ? 2104 LYS A CB    1 
ATOM   6219  C CG    . LYS A 1 2104 ? 194.773 201.740 190.602 1.00 17.15  ? 2104 LYS A CG    1 
ATOM   6220  C CD    . LYS A 1 2104 ? 195.578 200.550 191.084 1.00 17.15  ? 2104 LYS A CD    1 
ATOM   6221  C CE    . LYS A 1 2104 ? 196.633 200.975 192.086 1.00 17.15  ? 2104 LYS A CE    1 
ATOM   6222  N NZ    . LYS A 1 2104 ? 197.913 201.322 191.418 1.00 17.15  ? 2104 LYS A NZ    1 
ATOM   6223  N N     . ARG A 1 2105 ? 193.318 203.740 187.809 1.00 18.39  ? 2105 ARG A N     1 
ATOM   6224  C CA    . ARG A 1 2105 ? 193.870 204.963 187.233 1.00 18.39  ? 2105 ARG A CA    1 
ATOM   6225  C C     . ARG A 1 2105 ? 192.905 206.133 187.384 1.00 18.39  ? 2105 ARG A C     1 
ATOM   6226  O O     . ARG A 1 2105 ? 193.327 207.266 187.649 1.00 18.39  ? 2105 ARG A O     1 
ATOM   6227  C CB    . ARG A 1 2105 ? 194.224 204.738 185.766 1.00 18.39  ? 2105 ARG A CB    1 
ATOM   6228  C CG    . ARG A 1 2105 ? 195.595 204.124 185.566 1.00 18.39  ? 2105 ARG A CG    1 
ATOM   6229  C CD    . ARG A 1 2105 ? 195.923 204.003 184.097 1.00 18.39  ? 2105 ARG A CD    1 
ATOM   6230  N NE    . ARG A 1 2105 ? 195.025 203.080 183.415 1.00 18.39  ? 2105 ARG A NE    1 
ATOM   6231  C CZ    . ARG A 1 2105 ? 195.128 201.759 183.467 1.00 18.39  ? 2105 ARG A CZ    1 
ATOM   6232  N NH1   . ARG A 1 2105 ? 196.085 201.167 184.161 1.00 18.39  ? 2105 ARG A NH1   1 
ATOM   6233  N NH2   . ARG A 1 2105 ? 194.249 201.013 182.804 1.00 18.39  ? 2105 ARG A NH2   1 
ATOM   6234  N N     . GLU A 1 2106 ? 191.605 205.881 187.214 1.00 23.26  ? 2106 GLU A N     1 
ATOM   6235  C CA    . GLU A 1 2106 ? 190.617 206.936 187.415 1.00 23.26  ? 2106 GLU A CA    1 
ATOM   6236  C C     . GLU A 1 2106 ? 190.618 207.423 188.859 1.00 23.26  ? 2106 GLU A C     1 
ATOM   6237  O O     . GLU A 1 2106 ? 190.514 208.628 189.116 1.00 23.26  ? 2106 GLU A O     1 
ATOM   6238  C CB    . GLU A 1 2106 ? 189.228 206.436 187.015 1.00 23.26  ? 2106 GLU A CB    1 
ATOM   6239  C CG    . GLU A 1 2106 ? 188.065 207.223 187.610 1.00 23.26  ? 2106 GLU A CG    1 
ATOM   6240  C CD    . GLU A 1 2106 ? 187.915 208.623 187.032 1.00 23.26  ? 2106 GLU A CD    1 
ATOM   6241  O OE1   . GLU A 1 2106 ? 188.753 209.037 186.203 1.00 23.26  ? 2106 GLU A OE1   1 
ATOM   6242  O OE2   . GLU A 1 2106 ? 186.949 209.316 187.414 1.00 23.26  ? 2106 GLU A OE2   1 
ATOM   6243  N N     . ARG A 1 2107 ? 190.732 206.500 189.816 1.00 23.97  ? 2107 ARG A N     1 
ATOM   6244  C CA    . ARG A 1 2107 ? 190.811 206.895 191.218 1.00 23.97  ? 2107 ARG A CA    1 
ATOM   6245  C C     . ARG A 1 2107 ? 192.070 207.709 191.491 1.00 23.97  ? 2107 ARG A C     1 
ATOM   6246  O O     . ARG A 1 2107 ? 192.038 208.680 192.257 1.00 23.97  ? 2107 ARG A O     1 
ATOM   6247  C CB    . ARG A 1 2107 ? 190.765 205.660 192.117 1.00 23.97  ? 2107 ARG A CB    1 
ATOM   6248  C CG    . ARG A 1 2107 ? 190.176 205.919 193.491 1.00 23.97  ? 2107 ARG A CG    1 
ATOM   6249  C CD    . ARG A 1 2107 ? 189.974 204.623 194.258 1.00 23.97  ? 2107 ARG A CD    1 
ATOM   6250  N NE    . ARG A 1 2107 ? 188.793 203.898 193.805 1.00 23.97  ? 2107 ARG A NE    1 
ATOM   6251  C CZ    . ARG A 1 2107 ? 188.047 203.125 194.582 1.00 23.97  ? 2107 ARG A CZ    1 
ATOM   6252  N NH1   . ARG A 1 2107 ? 188.329 202.956 195.864 1.00 23.97  ? 2107 ARG A NH1   1 
ATOM   6253  N NH2   . ARG A 1 2107 ? 186.992 202.507 194.061 1.00 23.97  ? 2107 ARG A NH2   1 
ATOM   6254  N N     . ILE A 1 2108 ? 193.191 207.322 190.878 1.00 27.95  ? 2108 ILE A N     1 
ATOM   6255  C CA    . ILE A 1 2108 ? 194.429 208.084 191.029 1.00 27.95  ? 2108 ILE A CA    1 
ATOM   6256  C C     . ILE A 1 2108 ? 194.246 209.502 190.503 1.00 27.95  ? 2108 ILE A C     1 
ATOM   6257  O O     . ILE A 1 2108 ? 194.658 210.479 191.140 1.00 27.95  ? 2108 ILE A O     1 
ATOM   6258  C CB    . ILE A 1 2108 ? 195.592 207.366 190.320 1.00 27.95  ? 2108 ILE A CB    1 
ATOM   6259  C CG1   . ILE A 1 2108 ? 196.088 206.189 191.159 1.00 27.95  ? 2108 ILE A CG1   1 
ATOM   6260  C CG2   . ILE A 1 2108 ? 196.730 208.333 190.036 1.00 27.95  ? 2108 ILE A CG2   1 
ATOM   6261  C CD1   . ILE A 1 2108 ? 196.742 206.608 192.452 1.00 27.95  ? 2108 ILE A CD1   1 
ATOM   6262  N N     . GLN A 1 2109 ? 193.624 209.633 189.330 1.00 29.77  ? 2109 GLN A N     1 
ATOM   6263  C CA    . GLN A 1 2109 ? 193.381 210.958 188.767 1.00 29.77  ? 2109 GLN A CA    1 
ATOM   6264  C C     . GLN A 1 2109 ? 192.458 211.779 189.660 1.00 29.77  ? 2109 GLN A C     1 
ATOM   6265  O O     . GLN A 1 2109 ? 192.672 212.982 189.847 1.00 29.77  ? 2109 GLN A O     1 
ATOM   6266  C CB    . GLN A 1 2109 ? 192.797 210.836 187.361 1.00 29.77  ? 2109 GLN A CB    1 
ATOM   6267  C CG    . GLN A 1 2109 ? 193.769 210.287 186.331 1.00 29.77  ? 2109 GLN A CG    1 
ATOM   6268  C CD    . GLN A 1 2109 ? 195.087 211.036 186.317 1.00 29.77  ? 2109 GLN A CD    1 
ATOM   6269  O OE1   . GLN A 1 2109 ? 195.115 212.266 186.332 1.00 29.77  ? 2109 GLN A OE1   1 
ATOM   6270  N NE2   . GLN A 1 2109 ? 196.187 210.295 186.288 1.00 29.77  ? 2109 GLN A NE2   1 
ATOM   6271  N N     . LYS A 1 2110 ? 191.421 211.146 190.212 1.00 31.29  ? 2110 LYS A N     1 
ATOM   6272  C CA    . LYS A 1 2110 ? 190.502 211.858 191.096 1.00 31.29  ? 2110 LYS A CA    1 
ATOM   6273  C C     . LYS A 1 2110 ? 191.209 212.353 192.350 1.00 31.29  ? 2110 LYS A C     1 
ATOM   6274  O O     . LYS A 1 2110 ? 190.993 213.489 192.786 1.00 31.29  ? 2110 LYS A O     1 
ATOM   6275  C CB    . LYS A 1 2110 ? 189.328 210.953 191.468 1.00 31.29  ? 2110 LYS A CB    1 
ATOM   6276  C CG    . LYS A 1 2110 ? 188.103 211.699 191.967 1.00 31.29  ? 2110 LYS A CG    1 
ATOM   6277  C CD    . LYS A 1 2110 ? 186.939 210.751 192.200 1.00 31.29  ? 2110 LYS A CD    1 
ATOM   6278  C CE    . LYS A 1 2110 ? 186.489 210.096 190.905 1.00 31.29  ? 2110 LYS A CE    1 
ATOM   6279  N NZ    . LYS A 1 2110 ? 186.425 211.070 189.781 1.00 31.29  ? 2110 LYS A NZ    1 
ATOM   6280  N N     . ILE A 1 2111 ? 192.057 211.513 192.946 1.00 33.45  ? 2111 ILE A N     1 
ATOM   6281  C CA    . ILE A 1 2111 ? 192.764 211.912 194.160 1.00 33.45  ? 2111 ILE A CA    1 
ATOM   6282  C C     . ILE A 1 2111 ? 193.785 213.002 193.854 1.00 33.45  ? 2111 ILE A C     1 
ATOM   6283  O O     . ILE A 1 2111 ? 193.973 213.934 194.645 1.00 33.45  ? 2111 ILE A O     1 
ATOM   6284  C CB    . ILE A 1 2111 ? 193.419 210.687 194.823 1.00 33.45  ? 2111 ILE A CB    1 
ATOM   6285  C CG1   . ILE A 1 2111 ? 192.347 209.707 195.301 1.00 33.45  ? 2111 ILE A CG1   1 
ATOM   6286  C CG2   . ILE A 1 2111 ? 194.301 211.110 195.986 1.00 33.45  ? 2111 ILE A CG2   1 
ATOM   6287  C CD1   . ILE A 1 2111 ? 191.378 210.302 196.297 1.00 33.45  ? 2111 ILE A CD1   1 
ATOM   6288  N N     . LYS A 1 2112 ? 194.453 212.909 192.701 1.00 37.30  ? 2112 LYS A N     1 
ATOM   6289  C CA    . LYS A 1 2112 ? 195.479 213.889 192.355 1.00 37.30  ? 2112 LYS A CA    1 
ATOM   6290  C C     . LYS A 1 2112 ? 194.887 215.285 192.204 1.00 37.30  ? 2112 LYS A C     1 
ATOM   6291  O O     . LYS A 1 2112 ? 195.492 216.274 192.633 1.00 37.30  ? 2112 LYS A O     1 
ATOM   6292  C CB    . LYS A 1 2112 ? 196.195 213.467 191.073 1.00 37.30  ? 2112 LYS A CB    1 
ATOM   6293  C CG    . LYS A 1 2112 ? 197.316 214.403 190.651 1.00 37.30  ? 2112 LYS A CG    1 
ATOM   6294  C CD    . LYS A 1 2112 ? 198.091 213.841 189.470 1.00 37.30  ? 2112 LYS A CD    1 
ATOM   6295  C CE    . LYS A 1 2112 ? 197.282 213.924 188.187 1.00 37.30  ? 2112 LYS A CE    1 
ATOM   6296  N NZ    . LYS A 1 2112 ? 197.100 215.331 187.737 1.00 37.30  ? 2112 LYS A NZ    1 
ATOM   6297  N N     . ARG A 1 2113 ? 193.706 215.387 191.598 1.00 40.45  ? 2113 ARG A N     1 
ATOM   6298  C CA    . ARG A 1 2113 ? 193.042 216.676 191.407 1.00 40.45  ? 2113 ARG A CA    1 
ATOM   6299  C C     . ARG A 1 2113 ? 192.167 217.013 192.616 1.00 40.45  ? 2113 ARG A C     1 
ATOM   6300  O O     . ARG A 1 2113 ? 190.978 217.310 192.506 1.00 40.45  ? 2113 ARG A O     1 
ATOM   6301  C CB    . ARG A 1 2113 ? 192.226 216.661 190.121 1.00 40.45  ? 2113 ARG A CB    1 
ATOM   6302  C CG    . ARG A 1 2113 ? 193.058 216.552 188.857 1.00 40.45  ? 2113 ARG A CG    1 
ATOM   6303  C CD    . ARG A 1 2113 ? 192.177 216.483 187.620 1.00 40.45  ? 2113 ARG A CD    1 
ATOM   6304  N NE    . ARG A 1 2113 ? 191.161 215.441 187.725 1.00 40.45  ? 2113 ARG A NE    1 
ATOM   6305  C CZ    . ARG A 1 2113 ? 189.872 215.667 187.936 1.00 40.45  ? 2113 ARG A CZ    1 
ATOM   6306  N NH1   . ARG A 1 2113 ? 189.399 216.895 188.079 1.00 40.45  ? 2113 ARG A NH1   1 
ATOM   6307  N NH2   . ARG A 1 2113 ? 189.036 214.635 188.009 1.00 40.45  ? 2113 ARG A NH2   1 
ATOM   6308  N N     . GLU A 1 2114 ? 192.790 216.967 193.789 1.00 42.90  ? 2114 GLU A N     1 
ATOM   6309  C CA    . GLU A 1 2114 ? 192.101 217.262 195.039 1.00 42.90  ? 2114 GLU A CA    1 
ATOM   6310  C C     . GLU A 1 2114 ? 193.103 217.535 196.155 1.00 42.90  ? 2114 GLU A C     1 
ATOM   6311  O O     . GLU A 1 2114 ? 192.898 218.411 196.995 0.00 42.90  ? 2114 GLU A O     1 
ATOM   6312  C CB    . GLU A 1 2114 ? 191.175 216.106 195.428 1.00 42.90  ? 2114 GLU A CB    1 
ATOM   6313  C CG    . GLU A 1 2114 ? 190.535 216.250 196.799 1.00 42.90  ? 2114 GLU A CG    1 
ATOM   6314  C CD    . GLU A 1 2114 ? 189.691 215.049 197.176 1.00 42.90  ? 2114 GLU A CD    1 
ATOM   6315  O OE1   . GLU A 1 2114 ? 188.629 214.847 196.551 1.00 42.90  ? 2114 GLU A OE1   1 
ATOM   6316  O OE2   . GLU A 1 2114 ? 190.090 214.307 198.097 1.00 42.90  ? 2114 GLU A OE2   1 
ATOM   6317  N N     . ILE A 1 2127 ? 204.020 207.560 195.538 1.00 58.16  ? 2127 ILE A N     1 
ATOM   6318  C CA    . ILE A 1 2127 ? 203.009 208.593 195.716 1.00 58.16  ? 2127 ILE A CA    1 
ATOM   6319  C C     . ILE A 1 2127 ? 201.622 208.030 195.416 1.00 58.16  ? 2127 ILE A C     1 
ATOM   6320  O O     . ILE A 1 2127 ? 201.422 207.346 194.411 1.00 58.16  ? 2127 ILE A O     1 
ATOM   6321  C CB    . ILE A 1 2127 ? 203.320 209.831 194.841 1.00 58.16  ? 2127 ILE A CB    1 
ATOM   6322  C CG1   . ILE A 1 2127 ? 202.280 210.931 195.068 1.00 58.16  ? 2127 ILE A CG1   1 
ATOM   6323  C CG2   . ILE A 1 2127 ? 203.424 209.455 193.366 1.00 58.16  ? 2127 ILE A CG2   1 
ATOM   6324  C CD1   . ILE A 1 2127 ? 202.675 212.273 194.491 1.00 58.16  ? 2127 ILE A CD1   1 
ATOM   6325  N N     . ALA A 1 2128 ? 200.673 208.316 196.311 1.00 52.16  ? 2128 ALA A N     1 
ATOM   6326  C CA    . ALA A 1 2128 ? 199.288 207.860 196.178 1.00 52.16  ? 2128 ALA A CA    1 
ATOM   6327  C C     . ALA A 1 2128 ? 199.214 206.346 195.983 1.00 52.16  ? 2128 ALA A C     1 
ATOM   6328  O O     . ALA A 1 2128 ? 198.445 205.843 195.162 1.00 52.16  ? 2128 ALA A O     1 
ATOM   6329  C CB    . ALA A 1 2128 ? 198.571 208.592 195.041 1.00 52.16  ? 2128 ALA A CB    1 
ATOM   6330  N N     . GLU A 1 2129 ? 200.025 205.615 196.743 1.00 48.13  ? 2129 GLU A N     1 
ATOM   6331  C CA    . GLU A 1 2129 ? 200.064 204.161 196.677 1.00 48.13  ? 2129 GLU A CA    1 
ATOM   6332  C C     . GLU A 1 2129 ? 199.265 203.496 197.788 1.00 48.13  ? 2129 GLU A C     1 
ATOM   6333  O O     . GLU A 1 2129 ? 199.319 202.270 197.923 1.00 48.13  ? 2129 GLU A O     1 
ATOM   6334  C CB    . GLU A 1 2129 ? 201.516 203.672 196.720 1.00 48.13  ? 2129 GLU A CB    1 
ATOM   6335  C CG    . GLU A 1 2129 ? 202.279 204.096 197.964 1.00 48.13  ? 2129 GLU A CG    1 
ATOM   6336  C CD    . GLU A 1 2129 ? 202.233 203.055 199.064 1.00 48.13  ? 2129 GLU A CD    1 
ATOM   6337  O OE1   . GLU A 1 2129 ? 201.998 201.869 198.752 1.00 48.13  ? 2129 GLU A OE1   1 
ATOM   6338  O OE2   . GLU A 1 2129 ? 202.429 203.422 200.242 1.00 48.13  ? 2129 GLU A OE2   1 
ATOM   6339  N N     . ASN A 1 2130 ? 198.526 204.268 198.582 1.00 42.18  ? 2130 ASN A N     1 
ATOM   6340  C CA    . ASN A 1 2130 ? 197.756 203.741 199.701 1.00 42.18  ? 2130 ASN A CA    1 
ATOM   6341  C C     . ASN A 1 2130 ? 196.340 203.317 199.314 1.00 42.18  ? 2130 ASN A C     1 
ATOM   6342  O O     . ASN A 1 2130 ? 195.479 203.210 200.195 1.00 42.18  ? 2130 ASN A O     1 
ATOM   6343  C CB    . ASN A 1 2130 ? 197.715 204.771 200.835 1.00 42.18  ? 2130 ASN A CB    1 
ATOM   6344  C CG    . ASN A 1 2130 ? 196.999 206.057 200.444 1.00 42.18  ? 2130 ASN A CG    1 
ATOM   6345  O OD1   . ASN A 1 2130 ? 196.415 206.164 199.365 1.00 42.18  ? 2130 ASN A OD1   1 
ATOM   6346  N ND2   . ASN A 1 2130 ? 197.046 207.045 201.330 1.00 42.18  ? 2130 ASN A ND2   1 
ATOM   6347  N N     . LEU A 1 2131 ? 196.081 203.079 198.032 1.00 30.37  ? 2131 LEU A N     1 
ATOM   6348  C CA    . LEU A 1 2131 ? 194.744 202.710 197.602 1.00 30.37  ? 2131 LEU A CA    1 
ATOM   6349  C C     . LEU A 1 2131 ? 194.397 201.293 198.059 1.00 30.37  ? 2131 LEU A C     1 
ATOM   6350  O O     . LEU A 1 2131 ? 195.274 200.432 198.167 1.00 30.37  ? 2131 LEU A O     1 
ATOM   6351  C CB    . LEU A 1 2131 ? 194.624 202.800 196.085 1.00 30.37  ? 2131 LEU A CB    1 
ATOM   6352  C CG    . LEU A 1 2131 ? 194.735 204.188 195.459 1.00 30.37  ? 2131 LEU A CG    1 
ATOM   6353  C CD1   . LEU A 1 2131 ? 194.673 204.079 193.948 1.00 30.37  ? 2131 LEU A CD1   1 
ATOM   6354  C CD2   . LEU A 1 2131 ? 193.639 205.100 195.980 1.00 30.37  ? 2131 LEU A CD2   1 
ATOM   6355  N N     . PRO A 1 2132 ? 193.120 201.030 198.337 1.00 20.48  ? 2132 PRO A N     1 
ATOM   6356  C CA    . PRO A 1 2132 ? 192.690 199.655 198.621 1.00 20.48  ? 2132 PRO A CA    1 
ATOM   6357  C C     . PRO A 1 2132 ? 192.519 198.845 197.346 1.00 20.48  ? 2132 PRO A C     1 
ATOM   6358  O O     . PRO A 1 2132 ? 191.413 198.760 196.804 1.00 20.48  ? 2132 PRO A O     1 
ATOM   6359  C CB    . PRO A 1 2132 ? 191.359 199.850 199.353 1.00 20.48  ? 2132 PRO A CB    1 
ATOM   6360  C CG    . PRO A 1 2132 ? 190.833 201.142 198.826 1.00 20.48  ? 2132 PRO A CG    1 
ATOM   6361  C CD    . PRO A 1 2132 ? 192.021 202.001 198.478 1.00 20.48  ? 2132 PRO A CD    1 
ATOM   6362  N N     . GLU A 1 2133 ? 193.613 198.258 196.854 1.00 19.20  ? 2133 GLU A N     1 
ATOM   6363  C CA    . GLU A 1 2133 ? 193.586 197.595 195.553 1.00 19.20  ? 2133 GLU A CA    1 
ATOM   6364  C C     . GLU A 1 2133 ? 192.575 196.455 195.521 1.00 19.20  ? 2133 GLU A C     1 
ATOM   6365  O O     . GLU A 1 2133 ? 191.969 196.184 194.477 1.00 19.20  ? 2133 GLU A O     1 
ATOM   6366  C CB    . GLU A 1 2133 ? 194.982 197.090 195.199 1.00 19.20  ? 2133 GLU A CB    1 
ATOM   6367  C CG    . GLU A 1 2133 ? 195.905 198.176 194.679 1.00 19.20  ? 2133 GLU A CG    1 
ATOM   6368  C CD    . GLU A 1 2133 ? 197.340 197.981 195.116 1.00 19.20  ? 2133 GLU A CD    1 
ATOM   6369  O OE1   . GLU A 1 2133 ? 198.112 198.961 195.083 1.00 19.20  ? 2133 GLU A OE1   1 
ATOM   6370  O OE2   . GLU A 1 2133 ? 197.694 196.846 195.494 1.00 19.20  ? 2133 GLU A OE2   1 
ATOM   6371  N N     . GLN A 1 2134 ? 192.379 195.772 196.651 1.00 16.07  ? 2134 GLN A N     1 
ATOM   6372  C CA    . GLN A 1 2134 ? 191.353 194.736 196.712 1.00 16.07  ? 2134 GLN A CA    1 
ATOM   6373  C C     . GLN A 1 2134 ? 189.964 195.327 196.504 1.00 16.07  ? 2134 GLN A C     1 
ATOM   6374  O O     . GLN A 1 2134 ? 189.120 194.730 195.823 1.00 16.07  ? 2134 GLN A O     1 
ATOM   6375  C CB    . GLN A 1 2134 ? 191.429 194.000 198.049 1.00 16.07  ? 2134 GLN A CB    1 
ATOM   6376  C CG    . GLN A 1 2134 ? 192.766 193.336 198.313 1.00 16.07  ? 2134 GLN A CG    1 
ATOM   6377  C CD    . GLN A 1 2134 ? 192.692 192.300 199.414 1.00 16.07  ? 2134 GLN A CD    1 
ATOM   6378  O OE1   . GLN A 1 2134 ? 191.619 192.015 199.943 1.00 16.07  ? 2134 GLN A OE1   1 
ATOM   6379  N NE2   . GLN A 1 2134 ? 193.837 191.729 199.766 1.00 16.07  ? 2134 GLN A NE2   1 
ATOM   6380  N N     . GLU A 1 2135 ? 189.707 196.498 197.091 1.00 17.10  ? 2135 GLU A N     1 
ATOM   6381  C CA    . GLU A 1 2135 ? 188.422 197.158 196.893 1.00 17.10  ? 2135 GLU A CA    1 
ATOM   6382  C C     . GLU A 1 2135 ? 188.216 197.531 195.432 1.00 17.10  ? 2135 GLU A C     1 
ATOM   6383  O O     . GLU A 1 2135 ? 187.118 197.362 194.891 1.00 17.10  ? 2135 GLU A O     1 
ATOM   6384  C CB    . GLU A 1 2135 ? 188.324 198.395 197.785 1.00 17.10  ? 2135 GLU A CB    1 
ATOM   6385  C CG    . GLU A 1 2135 ? 187.011 199.145 197.658 1.00 17.10  ? 2135 GLU A CG    1 
ATOM   6386  C CD    . GLU A 1 2135 ? 186.978 200.408 198.495 1.00 17.10  ? 2135 GLU A CD    1 
ATOM   6387  O OE1   . GLU A 1 2135 ? 187.165 200.312 199.726 1.00 17.10  ? 2135 GLU A OE1   1 
ATOM   6388  O OE2   . GLU A 1 2135 ? 186.767 201.498 197.923 1.00 17.10  ? 2135 GLU A OE2   1 
ATOM   6389  N N     . ILE A 1 2136 ? 189.263 198.030 194.773 1.00 14.41  ? 2136 ILE A N     1 
ATOM   6390  C CA    . ILE A 1 2136 ? 189.164 198.361 193.353 1.00 14.41  ? 2136 ILE A CA    1 
ATOM   6391  C C     . ILE A 1 2136 ? 188.878 197.111 192.533 1.00 14.41  ? 2136 ILE A C     1 
ATOM   6392  O O     . ILE A 1 2136 ? 188.043 197.124 191.618 1.00 14.41  ? 2136 ILE A O     1 
ATOM   6393  C CB    . ILE A 1 2136 ? 190.450 199.063 192.881 1.00 14.41  ? 2136 ILE A CB    1 
ATOM   6394  C CG1   . ILE A 1 2136 ? 190.613 200.410 193.584 1.00 14.41  ? 2136 ILE A CG1   1 
ATOM   6395  C CG2   . ILE A 1 2136 ? 190.442 199.240 191.377 1.00 14.41  ? 2136 ILE A CG2   1 
ATOM   6396  C CD1   . ILE A 1 2136 ? 192.050 200.802 193.817 1.00 14.41  ? 2136 ILE A CD1   1 
ATOM   6397  N N     . LEU A 1 2137 ? 189.567 196.012 192.845 1.00 14.30  ? 2137 LEU A N     1 
ATOM   6398  C CA    . LEU A 1 2137 ? 189.369 194.776 192.097 1.00 14.30  ? 2137 LEU A CA    1 
ATOM   6399  C C     . LEU A 1 2137 ? 187.946 194.255 192.255 1.00 14.30  ? 2137 LEU A C     1 
ATOM   6400  O O     . LEU A 1 2137 ? 187.306 193.858 191.273 1.00 14.30  ? 2137 LEU A O     1 
ATOM   6401  C CB    . LEU A 1 2137 ? 190.381 193.724 192.547 1.00 14.30  ? 2137 LEU A CB    1 
ATOM   6402  C CG    . LEU A 1 2137 ? 190.522 192.509 191.633 1.00 14.30  ? 2137 LEU A CG    1 
ATOM   6403  C CD1   . LEU A 1 2137 ? 190.922 192.942 190.236 1.00 14.30  ? 2137 LEU A CD1   1 
ATOM   6404  C CD2   . LEU A 1 2137 ? 191.531 191.529 192.203 1.00 14.30  ? 2137 LEU A CD2   1 
ATOM   6405  N N     . ILE A 1 2138 ? 187.424 194.253 193.485 1.00 16.37  ? 2138 ILE A N     1 
ATOM   6406  C CA    . ILE A 1 2138 ? 186.069 193.741 193.666 1.00 16.37  ? 2138 ILE A CA    1 
ATOM   6407  C C     . ILE A 1 2138 ? 185.049 194.702 193.073 1.00 16.37  ? 2138 ILE A C     1 
ATOM   6408  O O     . ILE A 1 2138 ? 183.990 194.273 192.606 1.00 16.37  ? 2138 ILE A O     1 
ATOM   6409  C CB    . ILE A 1 2138 ? 185.751 193.444 195.143 1.00 16.37  ? 2138 ILE A CB    1 
ATOM   6410  C CG1   . ILE A 1 2138 ? 185.788 194.715 195.982 1.00 16.37  ? 2138 ILE A CG1   1 
ATOM   6411  C CG2   . ILE A 1 2138 ? 186.721 192.418 195.698 1.00 16.37  ? 2138 ILE A CG2   1 
ATOM   6412  C CD1   . ILE A 1 2138 ? 185.233 194.518 197.366 1.00 16.37  ? 2138 ILE A CD1   1 
ATOM   6413  N N     . GLN A 1 2139 ? 185.334 196.008 193.079 1.00 17.19  ? 2139 GLN A N     1 
ATOM   6414  C CA    . GLN A 1 2139 ? 184.436 196.952 192.425 1.00 17.19  ? 2139 GLN A CA    1 
ATOM   6415  C C     . GLN A 1 2139 ? 184.363 196.687 190.930 1.00 17.19  ? 2139 GLN A C     1 
ATOM   6416  O O     . GLN A 1 2139 ? 183.278 196.709 190.341 1.00 17.19  ? 2139 GLN A O     1 
ATOM   6417  C CB    . GLN A 1 2139 ? 184.890 198.387 192.691 1.00 17.19  ? 2139 GLN A CB    1 
ATOM   6418  C CG    . GLN A 1 2139 ? 184.251 199.413 191.772 1.00 17.19  ? 2139 GLN A CG    1 
ATOM   6419  C CD    . GLN A 1 2139 ? 184.846 200.795 191.938 1.00 17.19  ? 2139 GLN A CD    1 
ATOM   6420  O OE1   . GLN A 1 2139 ? 185.459 201.101 192.959 1.00 17.19  ? 2139 GLN A OE1   1 
ATOM   6421  N NE2   . GLN A 1 2139 ? 184.668 201.639 190.930 1.00 17.19  ? 2139 GLN A NE2   1 
ATOM   6422  N N     . SER A 1 2140 ? 185.510 196.431 190.300 1.00 12.62  ? 2140 SER A N     1 
ATOM   6423  C CA    . SER A 1 2140 ? 185.506 196.080 188.883 1.00 12.62  ? 2140 SER A CA    1 
ATOM   6424  C C     . SER A 1 2140 ? 184.759 194.775 188.642 1.00 12.62  ? 2140 SER A C     1 
ATOM   6425  O O     . SER A 1 2140 ? 183.969 194.666 187.694 1.00 12.62  ? 2140 SER A O     1 
ATOM   6426  C CB    . SER A 1 2140 ? 186.938 195.980 188.366 1.00 12.62  ? 2140 SER A CB    1 
ATOM   6427  O OG    . SER A 1 2140 ? 186.955 195.786 186.965 1.00 12.62  ? 2140 SER A OG    1 
ATOM   6428  N N     . VAL A 1 2141 ? 184.986 193.777 189.501 1.00 12.98  ? 2141 VAL A N     1 
ATOM   6429  C CA    . VAL A 1 2141 ? 184.307 192.491 189.358 1.00 12.98  ? 2141 VAL A CA    1 
ATOM   6430  C C     . VAL A 1 2141 ? 182.798 192.678 189.432 1.00 12.98  ? 2141 VAL A C     1 
ATOM   6431  O O     . VAL A 1 2141 ? 182.045 192.135 188.615 1.00 12.98  ? 2141 VAL A O     1 
ATOM   6432  C CB    . VAL A 1 2141 ? 184.799 191.503 190.430 1.00 12.98  ? 2141 VAL A CB    1 
ATOM   6433  C CG1   . VAL A 1 2141 ? 183.809 190.366 190.593 1.00 12.98  ? 2141 VAL A CG1   1 
ATOM   6434  C CG2   . VAL A 1 2141 ? 186.170 190.970 190.075 1.00 12.98  ? 2141 VAL A CG2   1 
ATOM   6435  N N     . CYS A 1 2142 ? 182.336 193.447 190.417 1.00 15.68  ? 2142 CYS A N     1 
ATOM   6436  C CA    . CYS A 1 2142 ? 180.906 193.679 190.574 1.00 15.68  ? 2142 CYS A CA    1 
ATOM   6437  C C     . CYS A 1 2142 ? 180.343 194.451 189.390 1.00 15.68  ? 2142 CYS A C     1 
ATOM   6438  O O     . CYS A 1 2142 ? 179.336 194.046 188.803 1.00 15.68  ? 2142 CYS A O     1 
ATOM   6439  C CB    . CYS A 1 2142 ? 180.638 194.418 191.882 1.00 15.68  ? 2142 CYS A CB    1 
ATOM   6440  S SG    . CYS A 1 2142 ? 180.881 193.412 193.360 1.00 15.68  ? 2142 CYS A SG    1 
ATOM   6441  N N     . GLU A 1 2143 ? 181.002 195.544 189.000 1.00 15.01  ? 2143 GLU A N     1 
ATOM   6442  C CA    . GLU A 1 2143 ? 180.525 196.342 187.877 1.00 15.01  ? 2143 GLU A CA    1 
ATOM   6443  C C     . GLU A 1 2143 ? 180.449 195.524 186.596 1.00 15.01  ? 2143 GLU A C     1 
ATOM   6444  O O     . GLU A 1 2143 ? 179.622 195.815 185.724 1.00 15.01  ? 2143 GLU A O     1 
ATOM   6445  C CB    . GLU A 1 2143 ? 181.434 197.552 187.676 1.00 15.01  ? 2143 GLU A CB    1 
ATOM   6446  C CG    . GLU A 1 2143 ? 180.720 198.799 187.197 1.00 15.01  ? 2143 GLU A CG    1 
ATOM   6447  C CD    . GLU A 1 2143 ? 181.620 200.016 187.201 1.00 15.01  ? 2143 GLU A CD    1 
ATOM   6448  O OE1   . GLU A 1 2143 ? 181.094 201.148 187.216 1.00 15.01  ? 2143 GLU A OE1   1 
ATOM   6449  O OE2   . GLU A 1 2143 ? 182.856 199.840 187.188 1.00 15.01  ? 2143 GLU A OE2   1 
ATOM   6450  N N     . THR A 1 2144 ? 181.296 194.504 186.458 1.00 12.79  ? 2144 THR A N     1 
ATOM   6451  C CA    . THR A 1 2144 ? 181.269 193.682 185.257 1.00 12.79  ? 2144 THR A CA    1 
ATOM   6452  C C     . THR A 1 2144 ? 180.285 192.520 185.338 1.00 12.79  ? 2144 THR A C     1 
ATOM   6453  O O     . THR A 1 2144 ? 179.732 192.120 184.307 1.00 12.79  ? 2144 THR A O     1 
ATOM   6454  C CB    . THR A 1 2144 ? 182.670 193.139 184.963 1.00 12.79  ? 2144 THR A CB    1 
ATOM   6455  O OG1   . THR A 1 2144 ? 183.638 194.171 185.186 1.00 12.79  ? 2144 THR A OG1   1 
ATOM   6456  C CG2   . THR A 1 2144 ? 182.770 192.670 183.520 1.00 12.79  ? 2144 THR A CG2   1 
ATOM   6457  N N     . MET A 1 2145 ? 180.039 191.972 186.528 1.00 14.82  ? 2145 MET A N     1 
ATOM   6458  C CA    . MET A 1 2145 ? 179.280 190.731 186.644 1.00 14.82  ? 2145 MET A CA    1 
ATOM   6459  C C     . MET A 1 2145 ? 177.866 190.914 187.183 1.00 14.82  ? 2145 MET A C     1 
ATOM   6460  O O     . MET A 1 2145 ? 176.951 190.224 186.728 1.00 14.82  ? 2145 MET A O     1 
ATOM   6461  C CB    . MET A 1 2145 ? 180.031 189.739 187.537 1.00 14.82  ? 2145 MET A CB    1 
ATOM   6462  C CG    . MET A 1 2145 ? 181.424 189.391 187.037 1.00 14.82  ? 2145 MET A CG    1 
ATOM   6463  S SD    . MET A 1 2145 ? 181.427 188.067 185.816 1.00 14.82  ? 2145 MET A SD    1 
ATOM   6464  C CE    . MET A 1 2145 ? 182.095 188.922 184.392 1.00 14.82  ? 2145 MET A CE    1 
ATOM   6465  N N     . VAL A 1 2146 ? 177.665 191.815 188.151 1.00 14.04  ? 2146 VAL A N     1 
ATOM   6466  C CA    . VAL A 1 2146 ? 176.345 191.956 188.774 1.00 14.04  ? 2146 VAL A CA    1 
ATOM   6467  C C     . VAL A 1 2146 ? 175.244 192.244 187.763 1.00 14.04  ? 2146 VAL A C     1 
ATOM   6468  O O     . VAL A 1 2146 ? 174.157 191.659 187.888 1.00 14.04  ? 2146 VAL A O     1 
ATOM   6469  C CB    . VAL A 1 2146 ? 176.406 192.990 189.907 1.00 14.04  ? 2146 VAL A CB    1 
ATOM   6470  C CG1   . VAL A 1 2146 ? 175.009 193.374 190.363 1.00 14.04  ? 2146 VAL A CG1   1 
ATOM   6471  C CG2   . VAL A 1 2146 ? 177.214 192.447 191.071 1.00 14.04  ? 2146 VAL A CG2   1 
ATOM   6472  N N     . PRO A 1 2147 ? 175.424 193.114 186.760 1.00 14.73  ? 2147 PRO A N     1 
ATOM   6473  C CA    . PRO A 1 2147 ? 174.313 193.376 185.831 1.00 14.73  ? 2147 PRO A CA    1 
ATOM   6474  C C     . PRO A 1 2147 ? 173.774 192.140 185.130 1.00 14.73  ? 2147 PRO A C     1 
ATOM   6475  O O     . PRO A 1 2147 ? 172.586 192.112 184.786 1.00 14.73  ? 2147 PRO A O     1 
ATOM   6476  C CB    . PRO A 1 2147 ? 174.927 194.362 184.830 1.00 14.73  ? 2147 PRO A CB    1 
ATOM   6477  C CG    . PRO A 1 2147 ? 175.937 195.085 185.616 1.00 14.73  ? 2147 PRO A CG    1 
ATOM   6478  C CD    . PRO A 1 2147 ? 176.529 194.068 186.547 1.00 14.73  ? 2147 PRO A CD    1 
ATOM   6479  N N     . LYS A 1 2148 ? 174.595 191.116 184.908 1.00 11.17  ? 2148 LYS A N     1 
ATOM   6480  C CA    . LYS A 1 2148 ? 174.158 189.924 184.195 1.00 11.17  ? 2148 LYS A CA    1 
ATOM   6481  C C     . LYS A 1 2148 ? 173.828 188.760 185.121 1.00 11.17  ? 2148 LYS A C     1 
ATOM   6482  O O     . LYS A 1 2148 ? 173.763 187.617 184.658 1.00 11.17  ? 2148 LYS A O     1 
ATOM   6483  C CB    . LYS A 1 2148 ? 175.217 189.495 183.178 1.00 11.17  ? 2148 LYS A CB    1 
ATOM   6484  C CG    . LYS A 1 2148 ? 176.522 189.019 183.788 1.00 11.17  ? 2148 LYS A CG    1 
ATOM   6485  C CD    . LYS A 1 2148 ? 177.623 188.947 182.745 1.00 11.17  ? 2148 LYS A CD    1 
ATOM   6486  C CE    . LYS A 1 2148 ? 177.769 190.262 182.003 1.00 11.17  ? 2148 LYS A CE    1 
ATOM   6487  N NZ    . LYS A 1 2148 ? 178.780 190.170 180.916 1.00 11.17  ? 2148 LYS A NZ    1 
ATOM   6488  N N     . LEU A 1 2149 ? 173.612 189.015 186.408 1.00 13.75  ? 2149 LEU A N     1 
ATOM   6489  C CA    . LEU A 1 2149 ? 173.319 187.962 187.371 1.00 13.75  ? 2149 LEU A CA    1 
ATOM   6490  C C     . LEU A 1 2149 ? 171.825 187.885 187.644 1.00 13.75  ? 2149 LEU A C     1 
ATOM   6491  O O     . LEU A 1 2149 ? 171.160 188.915 187.794 1.00 13.75  ? 2149 LEU A O     1 
ATOM   6492  C CB    . LEU A 1 2149 ? 174.061 188.188 188.687 1.00 13.75  ? 2149 LEU A CB    1 
ATOM   6493  C CG    . LEU A 1 2149 ? 175.578 188.052 188.679 1.00 13.75  ? 2149 LEU A CG    1 
ATOM   6494  C CD1   . LEU A 1 2149 ? 176.110 188.428 190.038 1.00 13.75  ? 2149 LEU A CD1   1 
ATOM   6495  C CD2   . LEU A 1 2149 ? 175.987 186.641 188.313 1.00 13.75  ? 2149 LEU A CD2   1 
ATOM   6496  N N     . VAL A 1 2150 ? 171.306 186.658 187.713 1.00 18.60  ? 2150 VAL A N     1 
ATOM   6497  C CA    . VAL A 1 2150 ? 169.946 186.450 188.184 1.00 18.60  ? 2150 VAL A CA    1 
ATOM   6498  C C     . VAL A 1 2150 ? 169.849 186.857 189.652 1.00 18.60  ? 2150 VAL A C     1 
ATOM   6499  O O     . VAL A 1 2150 ? 170.829 186.821 190.406 1.00 18.60  ? 2150 VAL A O     1 
ATOM   6500  C CB    . VAL A 1 2150 ? 169.533 184.984 187.974 1.00 18.60  ? 2150 VAL A CB    1 
ATOM   6501  C CG1   . VAL A 1 2150 ? 168.065 184.768 188.307 1.00 18.60  ? 2150 VAL A CG1   1 
ATOM   6502  C CG2   . VAL A 1 2150 ? 169.828 184.557 186.548 1.00 18.60  ? 2150 VAL A CG2   1 
ATOM   6503  N N     . ALA A 1 2151 ? 168.645 187.264 190.061 1.00 16.34  ? 2151 ALA A N     1 
ATOM   6504  C CA    . ALA A 1 2151 ? 168.440 187.738 191.426 1.00 16.34  ? 2151 ALA A CA    1 
ATOM   6505  C C     . ALA A 1 2151 ? 168.775 186.682 192.471 1.00 16.34  ? 2151 ALA A C     1 
ATOM   6506  O O     . ALA A 1 2151 ? 169.036 187.033 193.627 1.00 16.34  ? 2151 ALA A O     1 
ATOM   6507  C CB    . ALA A 1 2151 ? 166.996 188.204 191.611 1.00 16.34  ? 2151 ALA A CB    1 
ATOM   6508  N N     . GLU A 1 2152 ? 168.767 185.401 192.100 1.00 18.45  ? 2152 GLU A N     1 
ATOM   6509  C CA    . GLU A 1 2152 ? 169.104 184.356 193.060 1.00 18.45  ? 2152 GLU A CA    1 
ATOM   6510  C C     . GLU A 1 2152 ? 170.609 184.268 193.288 1.00 18.45  ? 2152 GLU A C     1 
ATOM   6511  O O     . GLU A 1 2152 ? 171.053 183.824 194.352 1.00 18.45  ? 2152 GLU A O     1 
ATOM   6512  C CB    . GLU A 1 2152 ? 168.547 183.013 192.587 1.00 18.45  ? 2152 GLU A CB    1 
ATOM   6513  C CG    . GLU A 1 2152 ? 169.171 182.492 191.304 1.00 18.45  ? 2152 GLU A CG    1 
ATOM   6514  C CD    . GLU A 1 2152 ? 168.546 181.193 190.837 1.00 18.45  ? 2152 GLU A CD    1 
ATOM   6515  O OE1   . GLU A 1 2152 ? 167.609 180.710 191.505 1.00 18.45  ? 2152 GLU A OE1   1 
ATOM   6516  O OE2   . GLU A 1 2152 ? 168.991 180.654 189.801 1.00 18.45  ? 2152 GLU A OE2   1 
ATOM   6517  N N     . ASP A 1 2153 ? 171.409 184.683 192.306 1.00 14.98  ? 2153 ASP A N     1 
ATOM   6518  C CA    . ASP A 1 2153 ? 172.857 184.531 192.377 1.00 14.98  ? 2153 ASP A CA    1 
ATOM   6519  C C     . ASP A 1 2153 ? 173.573 185.729 192.988 1.00 14.98  ? 2153 ASP A C     1 
ATOM   6520  O O     . ASP A 1 2153 ? 174.758 185.611 193.318 1.00 14.98  ? 2153 ASP A O     1 
ATOM   6521  C CB    . ASP A 1 2153 ? 173.430 184.267 190.982 1.00 14.98  ? 2153 ASP A CB    1 
ATOM   6522  C CG    . ASP A 1 2153 ? 172.905 182.988 190.369 1.00 14.98  ? 2153 ASP A CG    1 
ATOM   6523  O OD1   . ASP A 1 2153 ? 172.409 182.126 191.123 1.00 14.98  ? 2153 ASP A OD1   1 
ATOM   6524  O OD2   . ASP A 1 2153 ? 172.992 182.841 189.132 1.00 14.98  ? 2153 ASP A OD2   1 
ATOM   6525  N N     . ILE A 1 2154 ? 172.902 186.872 193.139 1.00 12.12  ? 2154 ILE A N     1 
ATOM   6526  C CA    . ILE A 1 2154 ? 173.564 188.046 193.714 1.00 12.12  ? 2154 ILE A CA    1 
ATOM   6527  C C     . ILE A 1 2154 ? 174.024 187.800 195.147 1.00 12.12  ? 2154 ILE A C     1 
ATOM   6528  O O     . ILE A 1 2154 ? 175.199 188.074 195.451 1.00 12.12  ? 2154 ILE A O     1 
ATOM   6529  C CB    . ILE A 1 2154 ? 172.654 189.282 193.584 1.00 12.12  ? 2154 ILE A CB    1 
ATOM   6530  C CG1   . ILE A 1 2154 ? 172.370 189.582 192.114 1.00 12.12  ? 2154 ILE A CG1   1 
ATOM   6531  C CG2   . ILE A 1 2154 ? 173.288 190.482 194.259 1.00 12.12  ? 2154 ILE A CG2   1 
ATOM   6532  C CD1   . ILE A 1 2154 ? 171.292 190.618 191.906 1.00 12.12  ? 2154 ILE A CD1   1 
ATOM   6533  N N     . PRO A 1 2155 ? 173.185 187.301 196.066 1.00 12.58  ? 2155 PRO A N     1 
ATOM   6534  C CA    . PRO A 1 2155 ? 173.708 186.969 197.399 1.00 12.58  ? 2155 PRO A CA    1 
ATOM   6535  C C     . PRO A 1 2155 ? 174.801 185.922 197.359 1.00 12.58  ? 2155 PRO A C     1 
ATOM   6536  O O     . PRO A 1 2155 ? 175.737 185.991 198.162 1.00 12.58  ? 2155 PRO A O     1 
ATOM   6537  C CB    . PRO A 1 2155 ? 172.467 186.470 198.152 1.00 12.58  ? 2155 PRO A CB    1 
ATOM   6538  C CG    . PRO A 1 2155 ? 171.520 186.053 197.092 1.00 12.58  ? 2155 PRO A CG    1 
ATOM   6539  C CD    . PRO A 1 2155 ? 171.741 187.018 195.976 1.00 12.58  ? 2155 PRO A CD    1 
ATOM   6540  N N     . LEU A 1 2156 ? 174.718 184.956 196.440 1.00 12.59  ? 2156 LEU A N     1 
ATOM   6541  C CA    . LEU A 1 2156 ? 175.796 183.983 196.299 1.00 12.59  ? 2156 LEU A CA    1 
ATOM   6542  C C     . LEU A 1 2156 ? 177.089 184.655 195.857 1.00 12.59  ? 2156 LEU A C     1 
ATOM   6543  O O     . LEU A 1 2156 ? 178.168 184.335 196.370 1.00 12.59  ? 2156 LEU A O     1 
ATOM   6544  C CB    . LEU A 1 2156 ? 175.396 182.885 195.314 1.00 12.59  ? 2156 LEU A CB    1 
ATOM   6545  C CG    . LEU A 1 2156 ? 174.658 181.675 195.892 1.00 12.59  ? 2156 LEU A CG    1 
ATOM   6546  C CD1   . LEU A 1 2156 ? 173.235 182.032 196.295 1.00 12.59  ? 2156 LEU A CD1   1 
ATOM   6547  C CD2   . LEU A 1 2156 ? 174.663 180.523 194.901 1.00 12.59  ? 2156 LEU A CD2   1 
ATOM   6548  N N     . LEU A 1 2157 ? 177.005 185.590 194.905 1.00 10.95  ? 2157 LEU A N     1 
ATOM   6549  C CA    . LEU A 1 2157 ? 178.205 186.299 194.470 1.00 10.95  ? 2157 LEU A CA    1 
ATOM   6550  C C     . LEU A 1 2157 ? 178.828 187.079 195.617 1.00 10.95  ? 2157 LEU A C     1 
ATOM   6551  O O     . LEU A 1 2157 ? 180.051 187.061 195.799 1.00 10.95  ? 2157 LEU A O     1 
ATOM   6552  C CB    . LEU A 1 2157 ? 177.887 187.251 193.320 1.00 10.95  ? 2157 LEU A CB    1 
ATOM   6553  C CG    . LEU A 1 2157 ? 179.132 188.018 192.863 1.00 10.95  ? 2157 LEU A CG    1 
ATOM   6554  C CD1   . LEU A 1 2157 ? 180.050 187.115 192.060 1.00 10.95  ? 2157 LEU A CD1   1 
ATOM   6555  C CD2   . LEU A 1 2157 ? 178.800 189.286 192.098 1.00 10.95  ? 2157 LEU A CD2   1 
ATOM   6556  N N     . PHE A 1 2158 ? 178.004 187.775 196.402 1.00 10.65  ? 2158 PHE A N     1 
ATOM   6557  C CA    . PHE A 1 2158 ? 178.567 188.561 197.493 1.00 10.65  ? 2158 PHE A CA    1 
ATOM   6558  C C     . PHE A 1 2158 ? 179.101 187.673 198.610 1.00 10.65  ? 2158 PHE A C     1 
ATOM   6559  O O     . PHE A 1 2158 ? 180.099 188.021 199.252 1.00 10.65  ? 2158 PHE A O     1 
ATOM   6560  C CB    . PHE A 1 2158 ? 177.529 189.552 198.011 1.00 10.65  ? 2158 PHE A CB    1 
ATOM   6561  C CG    . PHE A 1 2158 ? 177.401 190.775 197.154 1.00 10.65  ? 2158 PHE A CG    1 
ATOM   6562  C CD1   . PHE A 1 2158 ? 178.390 191.743 197.159 1.00 10.65  ? 2158 PHE A CD1   1 
ATOM   6563  C CD2   . PHE A 1 2158 ? 176.309 190.947 196.323 1.00 10.65  ? 2158 PHE A CD2   1 
ATOM   6564  C CE1   . PHE A 1 2158 ? 178.284 192.865 196.365 1.00 10.65  ? 2158 PHE A CE1   1 
ATOM   6565  C CE2   . PHE A 1 2158 ? 176.199 192.068 195.527 1.00 10.65  ? 2158 PHE A CE2   1 
ATOM   6566  C CZ    . PHE A 1 2158 ? 177.187 193.028 195.548 1.00 10.65  ? 2158 PHE A CZ    1 
ATOM   6567  N N     . SER A 1 2159 ? 178.478 186.515 198.840 1.00 12.62  ? 2159 SER A N     1 
ATOM   6568  C CA    . SER A 1 2159 ? 179.027 185.562 199.796 1.00 12.62  ? 2159 SER A CA    1 
ATOM   6569  C C     . SER A 1 2159 ? 180.379 185.034 199.332 1.00 12.62  ? 2159 SER A C     1 
ATOM   6570  O O     . SER A 1 2159 ? 181.303 184.883 200.138 1.00 12.62  ? 2159 SER A O     1 
ATOM   6571  C CB    . SER A 1 2159 ? 178.047 184.410 200.013 1.00 12.62  ? 2159 SER A CB    1 
ATOM   6572  O OG    . SER A 1 2159 ? 178.682 183.318 200.654 1.00 12.62  ? 2159 SER A OG    1 
ATOM   6573  N N     . LEU A 1 2160 ? 180.514 184.748 198.035 1.00 11.62  ? 2160 LEU A N     1 
ATOM   6574  C CA    . LEU A 1 2160 ? 181.803 184.307 197.509 1.00 11.62  ? 2160 LEU A CA    1 
ATOM   6575  C C     . LEU A 1 2160 ? 182.854 185.402 197.638 1.00 11.62  ? 2160 LEU A C     1 
ATOM   6576  O O     . LEU A 1 2160 ? 184.013 185.126 197.972 1.00 11.62  ? 2160 LEU A O     1 
ATOM   6577  C CB    . LEU A 1 2160 ? 181.660 183.871 196.052 1.00 11.62  ? 2160 LEU A CB    1 
ATOM   6578  C CG    . LEU A 1 2160 ? 180.806 182.632 195.788 1.00 11.62  ? 2160 LEU A CG    1 
ATOM   6579  C CD1   . LEU A 1 2160 ? 181.014 182.138 194.371 1.00 11.62  ? 2160 LEU A CD1   1 
ATOM   6580  C CD2   . LEU A 1 2160 ? 181.117 181.537 196.792 1.00 11.62  ? 2160 LEU A CD2   1 
ATOM   6581  N N     . LEU A 1 2161 ? 182.469 186.651 197.367 1.00 9.75   ? 2161 LEU A N     1 
ATOM   6582  C CA    . LEU A 1 2161 ? 183.398 187.764 197.535 1.00 9.75   ? 2161 LEU A CA    1 
ATOM   6583  C C     . LEU A 1 2161 ? 183.842 187.896 198.985 1.00 9.75   ? 2161 LEU A C     1 
ATOM   6584  O O     . LEU A 1 2161 ? 185.018 188.154 199.260 1.00 9.75   ? 2161 LEU A O     1 
ATOM   6585  C CB    . LEU A 1 2161 ? 182.758 189.064 197.052 1.00 9.75   ? 2161 LEU A CB    1 
ATOM   6586  C CG    . LEU A 1 2161 ? 182.730 189.281 195.541 1.00 9.75   ? 2161 LEU A CG    1 
ATOM   6587  C CD1   . LEU A 1 2161 ? 181.838 190.454 195.193 1.00 9.75   ? 2161 LEU A CD1   1 
ATOM   6588  C CD2   . LEU A 1 2161 ? 184.137 189.514 195.028 1.00 9.75   ? 2161 LEU A CD2   1 
ATOM   6589  N N     . SER A 1 2162 ? 182.912 187.728 199.927 1.00 11.24  ? 2162 SER A N     1 
ATOM   6590  C CA    . SER A 1 2162 ? 183.281 187.755 201.339 1.00 11.24  ? 2162 SER A CA    1 
ATOM   6591  C C     . SER A 1 2162 ? 184.208 186.597 201.687 1.00 11.24  ? 2162 SER A C     1 
ATOM   6592  O O     . SER A 1 2162 ? 185.139 186.755 202.485 1.00 11.24  ? 2162 SER A O     1 
ATOM   6593  C CB    . SER A 1 2162 ? 182.026 187.719 202.209 1.00 11.24  ? 2162 SER A CB    1 
ATOM   6594  O OG    . SER A 1 2162 ? 182.356 187.824 203.582 1.00 11.24  ? 2162 SER A OG    1 
ATOM   6595  N N     . ASP A 1 2163 ? 183.959 185.422 201.107 1.00 13.57  ? 2163 ASP A N     1 
ATOM   6596  C CA    . ASP A 1 2163 ? 184.799 184.261 201.384 1.00 13.57  ? 2163 ASP A CA    1 
ATOM   6597  C C     . ASP A 1 2163 ? 186.224 184.473 200.891 1.00 13.57  ? 2163 ASP A C     1 
ATOM   6598  O O     . ASP A 1 2163 ? 187.187 184.171 201.604 1.00 13.57  ? 2163 ASP A O     1 
ATOM   6599  C CB    . ASP A 1 2163 ? 184.196 183.012 200.742 1.00 13.57  ? 2163 ASP A CB    1 
ATOM   6600  C CG    . ASP A 1 2163 ? 183.331 182.222 201.702 1.00 13.57  ? 2163 ASP A CG    1 
ATOM   6601  O OD1   . ASP A 1 2163 ? 183.457 182.428 202.927 1.00 13.57  ? 2163 ASP A OD1   1 
ATOM   6602  O OD2   . ASP A 1 2163 ? 182.524 181.394 201.231 1.00 13.57  ? 2163 ASP A OD2   1 
ATOM   6603  N N     . VAL A 1 2164 ? 186.381 184.994 199.677 1.00 11.35  ? 2164 VAL A N     1 
ATOM   6604  C CA    . VAL A 1 2164 ? 187.708 185.151 199.086 1.00 11.35  ? 2164 VAL A CA    1 
ATOM   6605  C C     . VAL A 1 2164 ? 188.347 186.471 199.493 1.00 11.35  ? 2164 VAL A C     1 
ATOM   6606  O O     . VAL A 1 2164 ? 189.520 186.512 199.872 1.00 11.35  ? 2164 VAL A O     1 
ATOM   6607  C CB    . VAL A 1 2164 ? 187.625 185.015 197.553 1.00 11.35  ? 2164 VAL A CB    1 
ATOM   6608  C CG1   . VAL A 1 2164 ? 189.011 185.064 196.956 1.00 11.35  ? 2164 VAL A CG1   1 
ATOM   6609  C CG2   . VAL A 1 2164 ? 186.931 183.721 197.177 1.00 11.35  ? 2164 VAL A CG2   1 
ATOM   6610  N N     . PHE A 1 2165 ? 187.600 187.570 199.408 1.00 11.42  ? 2165 PHE A N     1 
ATOM   6611  C CA    . PHE A 1 2165 ? 188.073 188.861 199.891 1.00 11.42  ? 2165 PHE A CA    1 
ATOM   6612  C C     . PHE A 1 2165 ? 187.402 189.162 201.224 1.00 11.42  ? 2165 PHE A C     1 
ATOM   6613  O O     . PHE A 1 2165 ? 186.308 189.739 201.251 1.00 11.42  ? 2165 PHE A O     1 
ATOM   6614  C CB    . PHE A 1 2165 ? 187.772 189.974 198.886 1.00 11.42  ? 2165 PHE A CB    1 
ATOM   6615  C CG    . PHE A 1 2165 ? 188.365 189.750 197.524 1.00 11.42  ? 2165 PHE A CG    1 
ATOM   6616  C CD1   . PHE A 1 2165 ? 187.669 189.049 196.556 1.00 11.42  ? 2165 PHE A CD1   1 
ATOM   6617  C CD2   . PHE A 1 2165 ? 189.614 190.254 197.208 1.00 11.42  ? 2165 PHE A CD2   1 
ATOM   6618  C CE1   . PHE A 1 2165 ? 188.209 188.849 195.304 1.00 11.42  ? 2165 PHE A CE1   1 
ATOM   6619  C CE2   . PHE A 1 2165 ? 190.159 190.056 195.957 1.00 11.42  ? 2165 PHE A CE2   1 
ATOM   6620  C CZ    . PHE A 1 2165 ? 189.456 189.353 195.004 1.00 11.42  ? 2165 PHE A CZ    1 
ATOM   6621  N N     . PRO A 1 2166 ? 188.018 188.796 202.348 1.00 15.18  ? 2166 PRO A N     1 
ATOM   6622  C CA    . PRO A 1 2166 ? 187.339 188.942 203.643 1.00 15.18  ? 2166 PRO A CA    1 
ATOM   6623  C C     . PRO A 1 2166 ? 187.386 190.382 204.135 1.00 15.18  ? 2166 PRO A C     1 
ATOM   6624  O O     . PRO A 1 2166 ? 188.443 191.017 204.144 1.00 15.18  ? 2166 PRO A O     1 
ATOM   6625  C CB    . PRO A 1 2166 ? 188.133 188.010 204.563 1.00 15.18  ? 2166 PRO A CB    1 
ATOM   6626  C CG    . PRO A 1 2166 ? 189.506 188.005 203.979 1.00 15.18  ? 2166 PRO A CG    1 
ATOM   6627  C CD    . PRO A 1 2166 ? 189.377 188.249 202.493 1.00 15.18  ? 2166 PRO A CD    1 
ATOM   6628  N N     . GLY A 1 2167 ? 186.227 190.894 204.542 1.00 17.47  ? 2167 GLY A N     1 
ATOM   6629  C CA    . GLY A 1 2167 ? 186.155 192.210 205.141 1.00 17.47  ? 2167 GLY A CA    1 
ATOM   6630  C C     . GLY A 1 2167 ? 186.316 193.371 204.190 1.00 17.47  ? 2167 GLY A C     1 
ATOM   6631  O O     . GLY A 1 2167 ? 186.451 194.510 204.647 1.00 17.47  ? 2167 GLY A O     1 
ATOM   6632  N N     . VAL A 1 2168 ? 186.306 193.127 202.884 1.00 21.59  ? 2168 VAL A N     1 
ATOM   6633  C CA    . VAL A 1 2168 ? 186.439 194.177 201.882 1.00 21.59  ? 2168 VAL A CA    1 
ATOM   6634  C C     . VAL A 1 2168 ? 185.092 194.314 201.186 1.00 21.59  ? 2168 VAL A C     1 
ATOM   6635  O O     . VAL A 1 2168 ? 184.608 193.361 200.563 1.00 21.59  ? 2168 VAL A O     1 
ATOM   6636  C CB    . VAL A 1 2168 ? 187.559 193.865 200.879 1.00 21.59  ? 2168 VAL A CB    1 
ATOM   6637  C CG1   . VAL A 1 2168 ? 187.657 194.960 199.840 1.00 21.59  ? 2168 VAL A CG1   1 
ATOM   6638  C CG2   . VAL A 1 2168 ? 188.884 193.691 201.602 1.00 21.59  ? 2168 VAL A CG2   1 
ATOM   6639  N N     . GLN A 1 2169 ? 184.491 195.495 201.288 1.00 33.44  ? 2169 GLN A N     1 
ATOM   6640  C CA    . GLN A 1 2169 ? 183.123 195.719 200.846 1.00 33.44  ? 2169 GLN A CA    1 
ATOM   6641  C C     . GLN A 1 2169 ? 183.090 196.555 199.574 1.00 33.44  ? 2169 GLN A C     1 
ATOM   6642  O O     . GLN A 1 2169 ? 184.049 197.251 199.229 1.00 33.44  ? 2169 GLN A O     1 
ATOM   6643  C CB    . GLN A 1 2169 ? 182.302 196.403 201.944 1.00 33.44  ? 2169 GLN A CB    1 
ATOM   6644  C CG    . GLN A 1 2169 ? 181.663 195.433 202.924 1.00 33.44  ? 2169 GLN A CG    1 
ATOM   6645  C CD    . GLN A 1 2169 ? 181.643 195.964 204.343 1.00 33.44  ? 2169 GLN A CD    1 
ATOM   6646  O OE1   . GLN A 1 2169 ? 182.113 197.070 204.611 1.00 33.44  ? 2169 GLN A OE1   1 
ATOM   6647  N NE2   . GLN A 1 2169 ? 181.099 195.175 205.262 1.00 33.44  ? 2169 GLN A NE2   1 
ATOM   6648  N N     . TYR A 1 2170 ? 181.955 196.478 198.881 1.00 37.77  ? 2170 TYR A N     1 
ATOM   6649  C CA    . TYR A 1 2170 ? 181.741 197.155 197.606 1.00 37.77  ? 2170 TYR A CA    1 
ATOM   6650  C C     . TYR A 1 2170 ? 180.674 198.225 197.792 1.00 37.77  ? 2170 TYR A C     1 
ATOM   6651  O O     . TYR A 1 2170 ? 179.568 197.931 198.259 1.00 37.77  ? 2170 TYR A O     1 
ATOM   6652  C CB    . TYR A 1 2170 ? 181.323 196.157 196.527 1.00 37.77  ? 2170 TYR A CB    1 
ATOM   6653  C CG    . TYR A 1 2170 ? 180.737 196.789 195.282 1.00 37.77  ? 2170 TYR A CG    1 
ATOM   6654  C CD1   . TYR A 1 2170 ? 181.370 197.850 194.648 1.00 37.77  ? 2170 TYR A CD1   1 
ATOM   6655  C CD2   . TYR A 1 2170 ? 179.539 196.333 194.751 1.00 37.77  ? 2170 TYR A CD2   1 
ATOM   6656  C CE1   . TYR A 1 2170 ? 180.832 198.428 193.514 1.00 37.77  ? 2170 TYR A CE1   1 
ATOM   6657  C CE2   . TYR A 1 2170 ? 178.992 196.906 193.621 1.00 37.77  ? 2170 TYR A CE2   1 
ATOM   6658  C CZ    . TYR A 1 2170 ? 179.643 197.951 193.005 1.00 37.77  ? 2170 TYR A CZ    1 
ATOM   6659  O OH    . TYR A 1 2170 ? 179.101 198.523 191.878 1.00 37.77  ? 2170 TYR A OH    1 
ATOM   6660  N N     . HIS A 1 2171 ? 181.002 199.459 197.425 1.00 46.62  ? 2171 HIS A N     1 
ATOM   6661  C CA    . HIS A 1 2171 ? 180.038 200.549 197.385 1.00 46.62  ? 2171 HIS A CA    1 
ATOM   6662  C C     . HIS A 1 2171 ? 179.824 200.980 195.941 1.00 46.62  ? 2171 HIS A C     1 
ATOM   6663  O O     . HIS A 1 2171 ? 180.788 201.254 195.219 1.00 46.62  ? 2171 HIS A O     1 
ATOM   6664  C CB    . HIS A 1 2171 ? 180.506 201.732 198.233 1.00 46.62  ? 2171 HIS A CB    1 
ATOM   6665  C CG    . HIS A 1 2171 ? 180.933 201.352 199.617 1.00 46.62  ? 2171 HIS A CG    1 
ATOM   6666  N ND1   . HIS A 1 2171 ? 182.213 201.556 200.084 1.00 46.62  ? 2171 HIS A ND1   1 
ATOM   6667  C CD2   . HIS A 1 2171 ? 180.245 200.786 200.637 1.00 46.62  ? 2171 HIS A CD2   1 
ATOM   6668  C CE1   . HIS A 1 2171 ? 182.297 201.129 201.331 1.00 46.62  ? 2171 HIS A CE1   1 
ATOM   6669  N NE2   . HIS A 1 2171 ? 181.117 200.657 201.691 1.00 46.62  ? 2171 HIS A NE2   1 
ATOM   6670  N N     . ARG A 1 2172 ? 178.563 201.041 195.530 1.00 44.12  ? 2172 ARG A N     1 
ATOM   6671  C CA    . ARG A 1 2172 ? 178.206 201.396 194.163 1.00 44.12  ? 2172 ARG A CA    1 
ATOM   6672  C C     . ARG A 1 2172 ? 178.456 202.887 193.938 1.00 44.12  ? 2172 ARG A C     1 
ATOM   6673  O O     . ARG A 1 2172 ? 178.867 203.625 194.838 1.00 44.12  ? 2172 ARG A O     1 
ATOM   6674  C CB    . ARG A 1 2172 ? 176.752 201.024 193.895 1.00 44.12  ? 2172 ARG A CB    1 
ATOM   6675  C CG    . ARG A 1 2172 ? 175.783 201.833 194.738 1.00 44.12  ? 2172 ARG A CG    1 
ATOM   6676  C CD    . ARG A 1 2172 ? 174.332 201.438 194.535 1.00 44.12  ? 2172 ARG A CD    1 
ATOM   6677  N NE    . ARG A 1 2172 ? 173.461 202.257 195.370 1.00 44.12  ? 2172 ARG A NE    1 
ATOM   6678  C CZ    . ARG A 1 2172 ? 172.139 202.162 195.406 1.00 44.12  ? 2172 ARG A CZ    1 
ATOM   6679  N NH1   . ARG A 1 2172 ? 171.489 201.276 194.671 1.00 44.12  ? 2172 ARG A NH1   1 
ATOM   6680  N NH2   . ARG A 1 2172 ? 171.453 202.978 196.201 1.00 44.12  ? 2172 ARG A NH2   1 
ATOM   6681  N N     . GLY A 1 2173 ? 178.206 203.346 192.717 1.00 45.48  ? 2173 GLY A N     1 
ATOM   6682  C CA    . GLY A 1 2173 ? 178.272 204.760 192.389 1.00 45.48  ? 2173 GLY A CA    1 
ATOM   6683  C C     . GLY A 1 2173 ? 176.952 205.434 192.720 1.00 45.48  ? 2173 GLY A C     1 
ATOM   6684  O O     . GLY A 1 2173 ? 175.881 204.895 192.441 1.00 45.48  ? 2173 GLY A O     1 
ATOM   6685  N N     . GLU A 1 2174 ? 177.042 206.616 193.333 1.00 40.94  ? 2174 GLU A N     1 
ATOM   6686  C CA    . GLU A 1 2174 ? 175.832 207.312 193.758 1.00 40.94  ? 2174 GLU A CA    1 
ATOM   6687  C C     . GLU A 1 2174 ? 174.989 207.757 192.566 1.00 40.94  ? 2174 GLU A C     1 
ATOM   6688  O O     . GLU A 1 2174 ? 173.771 207.546 192.554 1.00 40.94  ? 2174 GLU A O     1 
ATOM   6689  C CB    . GLU A 1 2174 ? 176.197 208.494 194.661 1.00 40.94  ? 2174 GLU A CB    1 
ATOM   6690  C CG    . GLU A 1 2174 ? 176.985 209.606 193.987 1.00 40.94  ? 2174 GLU A CG    1 
ATOM   6691  C CD    . GLU A 1 2174 ? 177.370 210.713 194.944 1.00 40.94  ? 2174 GLU A CD    1 
ATOM   6692  O OE1   . GLU A 1 2174 ? 177.042 210.606 196.144 1.00 40.94  ? 2174 GLU A OE1   1 
ATOM   6693  O OE2   . GLU A 1 2174 ? 178.005 211.690 194.496 1.00 40.94  ? 2174 GLU A OE2   1 
ATOM   6694  N N     . MET A 1 2175 ? 175.622 208.348 191.547 1.00 33.00  ? 2175 MET A N     1 
ATOM   6695  C CA    . MET A 1 2175 ? 174.942 208.852 190.357 1.00 33.00  ? 2175 MET A CA    1 
ATOM   6696  C C     . MET A 1 2175 ? 173.716 209.684 190.706 1.00 33.00  ? 2175 MET A C     1 
ATOM   6697  O O     . MET A 1 2175 ? 172.655 209.522 190.096 1.00 33.00  ? 2175 MET A O     1 
ATOM   6698  C CB    . MET A 1 2175 ? 174.548 207.700 189.431 1.00 33.00  ? 2175 MET A CB    1 
ATOM   6699  C CG    . MET A 1 2175 ? 175.731 206.993 188.804 1.00 33.00  ? 2175 MET A CG    1 
ATOM   6700  S SD    . MET A 1 2175 ? 175.250 205.637 187.722 1.00 33.00  ? 2175 MET A SD    1 
ATOM   6701  C CE    . MET A 1 2175 ? 176.861 205.009 187.265 1.00 33.00  ? 2175 MET A CE    1 
ATOM   6702  N N     . THR A 1 2176 ? 173.852 210.581 191.685 1.00 28.33  ? 2176 THR A N     1 
ATOM   6703  C CA    . THR A 1 2176 ? 172.719 211.396 192.104 1.00 28.33  ? 2176 THR A CA    1 
ATOM   6704  C C     . THR A 1 2176 ? 172.297 212.396 191.037 1.00 28.33  ? 2176 THR A C     1 
ATOM   6705  O O     . THR A 1 2176 ? 171.203 212.962 191.134 1.00 28.33  ? 2176 THR A O     1 
ATOM   6706  C CB    . THR A 1 2176 ? 173.052 212.132 193.400 1.00 28.33  ? 2176 THR A CB    1 
ATOM   6707  O OG1   . THR A 1 2176 ? 171.864 212.732 193.928 1.00 28.33  ? 2176 THR A OG1   1 
ATOM   6708  C CG2   . THR A 1 2176 ? 174.090 213.210 193.145 1.00 28.33  ? 2176 THR A CG2   1 
ATOM   6709  N N     . ALA A 1 2177 ? 173.138 212.638 190.031 1.00 23.89  ? 2177 ALA A N     1 
ATOM   6710  C CA    . ALA A 1 2177 ? 172.764 213.544 188.950 1.00 23.89  ? 2177 ALA A CA    1 
ATOM   6711  C C     . ALA A 1 2177 ? 171.628 212.961 188.118 1.00 23.89  ? 2177 ALA A C     1 
ATOM   6712  O O     . ALA A 1 2177 ? 170.620 213.628 187.862 1.00 23.89  ? 2177 ALA A O     1 
ATOM   6713  C CB    . ALA A 1 2177 ? 173.981 213.846 188.075 1.00 23.89  ? 2177 ALA A CB    1 
ATOM   6714  N N     . LEU A 1 2178 ? 171.777 211.711 187.684 1.00 22.84  ? 2178 LEU A N     1 
ATOM   6715  C CA    . LEU A 1 2178 ? 170.754 211.032 186.899 1.00 22.84  ? 2178 LEU A CA    1 
ATOM   6716  C C     . LEU A 1 2178 ? 169.646 210.439 187.758 1.00 22.84  ? 2178 LEU A C     1 
ATOM   6717  O O     . LEU A 1 2178 ? 168.535 210.233 187.256 1.00 22.84  ? 2178 LEU A O     1 
ATOM   6718  C CB    . LEU A 1 2178 ? 171.398 209.935 186.045 1.00 22.84  ? 2178 LEU A CB    1 
ATOM   6719  C CG    . LEU A 1 2178 ? 170.492 209.140 185.105 1.00 22.84  ? 2178 LEU A CG    1 
ATOM   6720  C CD1   . LEU A 1 2178 ? 170.237 209.923 183.834 1.00 22.84  ? 2178 LEU A CD1   1 
ATOM   6721  C CD2   . LEU A 1 2178 ? 171.102 207.789 184.788 1.00 22.84  ? 2178 LEU A CD2   1 
ATOM   6722  N N     . ARG A 1 2179 ? 169.910 210.176 189.037 1.00 25.60  ? 2179 ARG A N     1 
ATOM   6723  C CA    . ARG A 1 2179 ? 168.945 209.546 189.925 1.00 25.60  ? 2179 ARG A CA    1 
ATOM   6724  C C     . ARG A 1 2179 ? 167.861 210.520 190.381 1.00 25.60  ? 2179 ARG A C     1 
ATOM   6725  O O     . ARG A 1 2179 ? 166.949 210.127 191.116 1.00 25.60  ? 2179 ARG A O     1 
ATOM   6726  C CB    . ARG A 1 2179 ? 169.668 208.931 191.126 1.00 25.60  ? 2179 ARG A CB    1 
ATOM   6727  C CG    . ARG A 1 2179 ? 168.874 207.867 191.861 1.00 25.60  ? 2179 ARG A CG    1 
ATOM   6728  C CD    . ARG A 1 2179 ? 169.558 207.436 193.146 1.00 25.60  ? 2179 ARG A CD    1 
ATOM   6729  N NE    . ARG A 1 2179 ? 170.537 206.377 192.934 1.00 25.60  ? 2179 ARG A NE    1 
ATOM   6730  C CZ    . ARG A 1 2179 ? 170.260 205.082 192.999 1.00 25.60  ? 2179 ARG A CZ    1 
ATOM   6731  N NH1   . ARG A 1 2179 ? 169.032 204.649 193.230 1.00 25.60  ? 2179 ARG A NH1   1 
ATOM   6732  N NH2   . ARG A 1 2179 ? 171.241 204.199 192.840 1.00 25.60  ? 2179 ARG A NH2   1 
ATOM   6733  N N     . GLU A 1 2180 ? 167.939 211.781 189.955 1.00 23.64  ? 2180 GLU A N     1 
ATOM   6734  C CA    . GLU A 1 2180 ? 166.860 212.741 190.167 1.00 23.64  ? 2180 GLU A CA    1 
ATOM   6735  C C     . GLU A 1 2180 ? 166.019 212.910 188.908 1.00 23.64  ? 2180 GLU A C     1 
ATOM   6736  O O     . GLU A 1 2180 ? 164.791 213.033 189.000 1.00 23.64  ? 2180 GLU A O     1 
ATOM   6737  C CB    . GLU A 1 2180 ? 167.434 214.085 190.644 1.00 23.64  ? 2180 GLU A CB    1 
ATOM   6738  C CG    . GLU A 1 2180 ? 168.049 214.950 189.552 1.00 23.64  ? 2180 GLU A CG    1 
ATOM   6739  C CD    . GLU A 1 2180 ? 168.306 216.372 190.004 1.00 23.64  ? 2180 GLU A CD    1 
ATOM   6740  O OE1   . GLU A 1 2180 ? 169.208 216.577 190.843 1.00 23.64  ? 2180 GLU A OE1   1 
ATOM   6741  O OE2   . GLU A 1 2180 ? 167.610 217.287 189.516 1.00 23.64  ? 2180 GLU A OE2   1 
ATOM   6742  N N     . GLU A 1 2181 ? 166.641 212.891 187.727 1.00 22.61  ? 2181 GLU A N     1 
ATOM   6743  C CA    . GLU A 1 2181 ? 165.867 212.868 186.493 1.00 22.61  ? 2181 GLU A CA    1 
ATOM   6744  C C     . GLU A 1 2181 ? 165.084 211.571 186.375 1.00 22.61  ? 2181 GLU A C     1 
ATOM   6745  O O     . GLU A 1 2181 ? 163.968 211.555 185.843 1.00 22.61  ? 2181 GLU A O     1 
ATOM   6746  C CB    . GLU A 1 2181 ? 166.787 213.059 185.288 1.00 22.61  ? 2181 GLU A CB    1 
ATOM   6747  C CG    . GLU A 1 2181 ? 167.617 214.331 185.342 1.00 22.61  ? 2181 GLU A CG    1 
ATOM   6748  C CD    . GLU A 1 2181 ? 166.779 215.585 185.180 1.00 22.61  ? 2181 GLU A CD    1 
ATOM   6749  O OE1   . GLU A 1 2181 ? 165.648 215.486 184.659 1.00 22.61  ? 2181 GLU A OE1   1 
ATOM   6750  O OE2   . GLU A 1 2181 ? 167.251 216.672 185.572 1.00 22.61  ? 2181 GLU A OE2   1 
ATOM   6751  N N     . LEU A 1 2182 ? 165.647 210.471 186.880 1.00 20.05  ? 2182 LEU A N     1 
ATOM   6752  C CA    . LEU A 1 2182 ? 164.895 209.222 186.931 1.00 20.05  ? 2182 LEU A CA    1 
ATOM   6753  C C     . LEU A 1 2182 ? 163.649 209.373 187.791 1.00 20.05  ? 2182 LEU A C     1 
ATOM   6754  O O     . LEU A 1 2182 ? 162.562 208.928 187.404 1.00 20.05  ? 2182 LEU A O     1 
ATOM   6755  C CB    . LEU A 1 2182 ? 165.775 208.095 187.467 1.00 20.05  ? 2182 LEU A CB    1 
ATOM   6756  C CG    . LEU A 1 2182 ? 166.823 207.508 186.524 1.00 20.05  ? 2182 LEU A CG    1 
ATOM   6757  C CD1   . LEU A 1 2182 ? 167.380 206.234 187.112 1.00 20.05  ? 2182 LEU A CD1   1 
ATOM   6758  C CD2   . LEU A 1 2182 ? 166.231 207.246 185.158 1.00 20.05  ? 2182 LEU A CD2   1 
ATOM   6759  N N     . LYS A 1 2183 ? 163.786 210.004 188.961 1.00 20.20  ? 2183 LYS A N     1 
ATOM   6760  C CA    . LYS A 1 2183 ? 162.632 210.223 189.825 1.00 20.20  ? 2183 LYS A CA    1 
ATOM   6761  C C     . LYS A 1 2183 ? 161.585 211.087 189.137 1.00 20.20  ? 2183 LYS A C     1 
ATOM   6762  O O     . LYS A 1 2183 ? 160.387 210.786 189.194 1.00 20.20  ? 2183 LYS A O     1 
ATOM   6763  C CB    . LYS A 1 2183 ? 163.069 210.870 191.138 1.00 20.20  ? 2183 LYS A CB    1 
ATOM   6764  C CG    . LYS A 1 2183 ? 161.923 211.138 192.099 1.00 20.20  ? 2183 LYS A CG    1 
ATOM   6765  C CD    . LYS A 1 2183 ? 162.343 212.061 193.232 1.00 20.20  ? 2183 LYS A CD    1 
ATOM   6766  C CE    . LYS A 1 2183 ? 163.206 211.343 194.253 1.00 20.20  ? 2183 LYS A CE    1 
ATOM   6767  N NZ    . LYS A 1 2183 ? 163.526 212.213 195.418 1.00 20.20  ? 2183 LYS A NZ    1 
ATOM   6768  N N     . LYS A 1 2184 ? 162.018 212.165 188.482 1.00 20.83  ? 2184 LYS A N     1 
ATOM   6769  C CA    . LYS A 1 2184 ? 161.068 213.050 187.810 1.00 20.83  ? 2184 LYS A CA    1 
ATOM   6770  C C     . LYS A 1 2184 ? 160.336 212.326 186.684 1.00 20.83  ? 2184 LYS A C     1 
ATOM   6771  O O     . LYS A 1 2184 ? 159.111 212.443 186.547 1.00 20.83  ? 2184 LYS A O     1 
ATOM   6772  C CB    . LYS A 1 2184 ? 161.790 214.289 187.282 1.00 20.83  ? 2184 LYS A CB    1 
ATOM   6773  C CG    . LYS A 1 2184 ? 162.286 215.221 188.375 1.00 20.83  ? 2184 LYS A CG    1 
ATOM   6774  C CD    . LYS A 1 2184 ? 162.993 216.435 187.799 1.00 20.83  ? 2184 LYS A CD    1 
ATOM   6775  C CE    . LYS A 1 2184 ? 163.366 217.423 188.892 1.00 20.83  ? 2184 LYS A CE    1 
ATOM   6776  N NZ    . LYS A 1 2184 ? 164.375 216.860 189.829 1.00 20.83  ? 2184 LYS A NZ    1 
ATOM   6777  N N     . VAL A 1 2185 ? 161.070 211.561 185.872 1.00 18.80  ? 2185 VAL A N     1 
ATOM   6778  C CA    . VAL A 1 2185 ? 160.450 210.855 184.754 1.00 18.80  ? 2185 VAL A CA    1 
ATOM   6779  C C     . VAL A 1 2185 ? 159.489 209.789 185.261 1.00 18.80  ? 2185 VAL A C     1 
ATOM   6780  O O     . VAL A 1 2185 ? 158.394 209.609 184.715 1.00 18.80  ? 2185 VAL A O     1 
ATOM   6781  C CB    . VAL A 1 2185 ? 161.529 210.260 183.832 1.00 18.80  ? 2185 VAL A CB    1 
ATOM   6782  C CG1   . VAL A 1 2185 ? 160.905 209.305 182.832 1.00 18.80  ? 2185 VAL A CG1   1 
ATOM   6783  C CG2   . VAL A 1 2185 ? 162.268 211.368 183.108 1.00 18.80  ? 2185 VAL A CG2   1 
ATOM   6784  N N     . CYS A 1 2186 ? 159.878 209.065 186.314 1.00 19.89  ? 2186 CYS A N     1 
ATOM   6785  C CA    . CYS A 1 2186 ? 158.986 208.065 186.889 1.00 19.89  ? 2186 CYS A CA    1 
ATOM   6786  C C     . CYS A 1 2186 ? 157.729 208.711 187.452 1.00 19.89  ? 2186 CYS A C     1 
ATOM   6787  O O     . CYS A 1 2186 ? 156.630 208.160 187.328 1.00 19.89  ? 2186 CYS A O     1 
ATOM   6788  C CB    . CYS A 1 2186 ? 159.718 207.274 187.971 1.00 19.89  ? 2186 CYS A CB    1 
ATOM   6789  S SG    . CYS A 1 2186 ? 160.977 206.147 187.338 1.00 19.89  ? 2186 CYS A SG    1 
ATOM   6790  N N     . GLN A 1 2187 ? 157.870 209.880 188.081 1.00 21.33  ? 2187 GLN A N     1 
ATOM   6791  C CA    . GLN A 1 2187 ? 156.703 210.580 188.605 1.00 21.33  ? 2187 GLN A CA    1 
ATOM   6792  C C     . GLN A 1 2187 ? 155.774 210.997 187.473 1.00 21.33  ? 2187 GLN A C     1 
ATOM   6793  O O     . GLN A 1 2187 ? 154.550 210.865 187.586 1.00 21.33  ? 2187 GLN A O     1 
ATOM   6794  C CB    . GLN A 1 2187 ? 157.168 211.773 189.457 1.00 21.33  ? 2187 GLN A CB    1 
ATOM   6795  C CG    . GLN A 1 2187 ? 156.113 212.641 190.198 1.00 21.33  ? 2187 GLN A CG    1 
ATOM   6796  C CD    . GLN A 1 2187 ? 155.030 213.279 189.337 1.00 21.33  ? 2187 GLN A CD    1 
ATOM   6797  O OE1   . GLN A 1 2187 ? 155.249 213.606 188.170 1.00 21.33  ? 2187 GLN A OE1   1 
ATOM   6798  N NE2   . GLN A 1 2187 ? 153.851 213.457 189.918 1.00 21.33  ? 2187 GLN A NE2   1 
ATOM   6799  N N     . GLU A 1 2188 ? 156.332 211.488 186.365 1.00 23.13  ? 2188 GLU A N     1 
ATOM   6800  C CA    . GLU A 1 2188 ? 155.481 211.942 185.272 1.00 23.13  ? 2188 GLU A CA    1 
ATOM   6801  C C     . GLU A 1 2188 ? 155.035 210.813 184.352 1.00 23.13  ? 2188 GLU A C     1 
ATOM   6802  O O     . GLU A 1 2188 ? 154.313 211.077 183.386 1.00 23.13  ? 2188 GLU A O     1 
ATOM   6803  C CB    . GLU A 1 2188 ? 156.187 213.025 184.452 1.00 23.13  ? 2188 GLU A CB    1 
ATOM   6804  C CG    . GLU A 1 2188 ? 157.419 212.563 183.706 1.00 23.13  ? 2188 GLU A CG    1 
ATOM   6805  C CD    . GLU A 1 2188 ? 158.102 213.698 182.971 1.00 23.13  ? 2188 GLU A CD    1 
ATOM   6806  O OE1   . GLU A 1 2188 ? 157.618 214.845 183.070 1.00 23.13  ? 2188 GLU A OE1   1 
ATOM   6807  O OE2   . GLU A 1 2188 ? 159.118 213.446 182.290 1.00 23.13  ? 2188 GLU A OE2   1 
ATOM   6808  N N     . MET A 1 2189 ? 155.446 209.573 184.616 1.00 20.73  ? 2189 MET A N     1 
ATOM   6809  C CA    . MET A 1 2189 ? 154.941 208.417 183.886 1.00 20.73  ? 2189 MET A CA    1 
ATOM   6810  C C     . MET A 1 2189 ? 154.228 207.422 184.793 1.00 20.73  ? 2189 MET A C     1 
ATOM   6811  O O     . MET A 1 2189 ? 154.053 206.262 184.408 1.00 20.73  ? 2189 MET A O     1 
ATOM   6812  C CB    . MET A 1 2189 ? 156.073 207.719 183.130 1.00 20.73  ? 2189 MET A CB    1 
ATOM   6813  C CG    . MET A 1 2189 ? 156.626 208.527 181.971 1.00 20.73  ? 2189 MET A CG    1 
ATOM   6814  S SD    . MET A 1 2189 ? 158.031 207.736 181.168 1.00 20.73  ? 2189 MET A SD    1 
ATOM   6815  C CE    . MET A 1 2189 ? 157.680 206.012 181.494 1.00 20.73  ? 2189 MET A CE    1 
ATOM   6816  N N     . TYR A 1 2190 ? 153.824 207.849 185.990 1.00 18.51  ? 2190 TYR A N     1 
ATOM   6817  C CA    . TYR A 1 2190 ? 153.011 207.058 186.912 1.00 18.51  ? 2190 TYR A CA    1 
ATOM   6818  C C     . TYR A 1 2190 ? 153.705 205.778 187.364 1.00 18.51  ? 2190 TYR A C     1 
ATOM   6819  O O     . TYR A 1 2190 ? 153.038 204.804 187.727 1.00 18.51  ? 2190 TYR A O     1 
ATOM   6820  C CB    . TYR A 1 2190 ? 151.646 206.731 186.297 1.00 18.51  ? 2190 TYR A CB    1 
ATOM   6821  C CG    . TYR A 1 2190 ? 150.987 207.918 185.638 1.00 18.51  ? 2190 TYR A CG    1 
ATOM   6822  C CD1   . TYR A 1 2190 ? 150.644 209.043 186.374 1.00 18.51  ? 2190 TYR A CD1   1 
ATOM   6823  C CD2   . TYR A 1 2190 ? 150.717 207.919 184.277 1.00 18.51  ? 2190 TYR A CD2   1 
ATOM   6824  C CE1   . TYR A 1 2190 ? 150.048 210.133 185.774 1.00 18.51  ? 2190 TYR A CE1   1 
ATOM   6825  C CE2   . TYR A 1 2190 ? 150.119 209.005 183.668 1.00 18.51  ? 2190 TYR A CE2   1 
ATOM   6826  C CZ    . TYR A 1 2190 ? 149.787 210.108 184.422 1.00 18.51  ? 2190 TYR A CZ    1 
ATOM   6827  O OH    . TYR A 1 2190 ? 149.191 211.192 183.822 1.00 18.51  ? 2190 TYR A OH    1 
ATOM   6828  N N     . LEU A 1 2191 ? 155.034 205.756 187.356 1.00 17.74  ? 2191 LEU A N     1 
ATOM   6829  C CA    . LEU A 1 2191 ? 155.777 204.595 187.814 1.00 17.74  ? 2191 LEU A CA    1 
ATOM   6830  C C     . LEU A 1 2191 ? 156.136 204.752 189.290 1.00 17.74  ? 2191 LEU A C     1 
ATOM   6831  O O     . LEU A 1 2191 ? 155.780 205.735 189.944 1.00 17.74  ? 2191 LEU A O     1 
ATOM   6832  C CB    . LEU A 1 2191 ? 157.026 204.390 186.959 1.00 17.74  ? 2191 LEU A CB    1 
ATOM   6833  C CG    . LEU A 1 2191 ? 156.806 204.291 185.449 1.00 17.74  ? 2191 LEU A CG    1 
ATOM   6834  C CD1   . LEU A 1 2191 ? 158.076 203.838 184.761 1.00 17.74  ? 2191 LEU A CD1   1 
ATOM   6835  C CD2   . LEU A 1 2191 ? 155.663 203.346 185.131 1.00 17.74  ? 2191 LEU A CD2   1 
ATOM   6836  N N     . THR A 1 2192 ? 156.849 203.767 189.826 1.00 18.56  ? 2192 THR A N     1 
ATOM   6837  C CA    . THR A 1 2192 ? 157.286 203.772 191.215 1.00 18.56  ? 2192 THR A CA    1 
ATOM   6838  C C     . THR A 1 2192 ? 158.806 203.806 191.266 1.00 18.56  ? 2192 THR A C     1 
ATOM   6839  O O     . THR A 1 2192 ? 159.472 203.009 190.597 1.00 18.56  ? 2192 THR A O     1 
ATOM   6840  C CB    . THR A 1 2192 ? 156.760 202.546 191.963 1.00 18.56  ? 2192 THR A CB    1 
ATOM   6841  O OG1   . THR A 1 2192 ? 155.329 202.521 191.894 1.00 18.56  ? 2192 THR A OG1   1 
ATOM   6842  C CG2   . THR A 1 2192 ? 157.187 202.589 193.420 1.00 18.56  ? 2192 THR A CG2   1 
ATOM   6843  N N     . TYR A 1 2193 ? 159.346 204.727 192.058 1.00 24.35  ? 2193 TYR A N     1 
ATOM   6844  C CA    . TYR A 1 2193 ? 160.782 204.906 192.205 1.00 24.35  ? 2193 TYR A CA    1 
ATOM   6845  C C     . TYR A 1 2193 ? 161.163 204.835 193.677 1.00 24.35  ? 2193 TYR A C     1 
ATOM   6846  O O     . TYR A 1 2193 ? 160.464 205.381 194.537 1.00 24.35  ? 2193 TYR A O     1 
ATOM   6847  C CB    . TYR A 1 2193 ? 161.231 206.243 191.598 1.00 24.35  ? 2193 TYR A CB    1 
ATOM   6848  C CG    . TYR A 1 2193 ? 162.574 206.741 192.086 1.00 24.35  ? 2193 TYR A CG    1 
ATOM   6849  C CD1   . TYR A 1 2193 ? 162.669 207.548 193.212 1.00 24.35  ? 2193 TYR A CD1   1 
ATOM   6850  C CD2   . TYR A 1 2193 ? 163.745 206.414 191.417 1.00 24.35  ? 2193 TYR A CD2   1 
ATOM   6851  C CE1   . TYR A 1 2193 ? 163.885 208.003 193.663 1.00 24.35  ? 2193 TYR A CE1   1 
ATOM   6852  C CE2   . TYR A 1 2193 ? 164.970 206.871 191.861 1.00 24.35  ? 2193 TYR A CE2   1 
ATOM   6853  C CZ    . TYR A 1 2193 ? 165.031 207.666 192.986 1.00 24.35  ? 2193 TYR A CZ    1 
ATOM   6854  O OH    . TYR A 1 2193 ? 166.238 208.130 193.446 1.00 24.35  ? 2193 TYR A OH    1 
ATOM   6855  N N     . GLY A 1 2194 ? 162.276 204.165 193.957 1.00 30.54  ? 2194 GLY A N     1 
ATOM   6856  C CA    . GLY A 1 2194 ? 162.798 204.078 195.307 1.00 30.54  ? 2194 GLY A CA    1 
ATOM   6857  C C     . GLY A 1 2194 ? 164.270 203.744 195.265 1.00 30.54  ? 2194 GLY A C     1 
ATOM   6858  O O     . GLY A 1 2194 ? 164.753 203.117 194.320 1.00 30.54  ? 2194 GLY A O     1 
ATOM   6859  N N     . ASP A 1 2195 ? 164.982 204.165 196.304 1.00 35.70  ? 2195 ASP A N     1 
ATOM   6860  C CA    . ASP A 1 2195 ? 166.433 204.046 196.358 1.00 35.70  ? 2195 ASP A CA    1 
ATOM   6861  C C     . ASP A 1 2195 ? 166.835 202.878 197.247 1.00 35.70  ? 2195 ASP A C     1 
ATOM   6862  O O     . ASP A 1 2195 ? 166.611 202.911 198.461 1.00 35.70  ? 2195 ASP A O     1 
ATOM   6863  C CB    . ASP A 1 2195 ? 167.064 205.341 196.874 1.00 35.70  ? 2195 ASP A CB    1 
ATOM   6864  C CG    . ASP A 1 2195 ? 168.578 205.293 196.869 1.00 35.70  ? 2195 ASP A CG    1 
ATOM   6865  O OD1   . ASP A 1 2195 ? 169.169 205.323 195.771 1.00 35.70  ? 2195 ASP A OD1   1 
ATOM   6866  O OD2   . ASP A 1 2195 ? 169.178 205.229 197.963 1.00 35.70  ? 2195 ASP A OD2   1 
ATOM   6867  N N     . GLY A 1 2196 ? 167.440 201.857 196.646 1.00 35.49  ? 2196 GLY A N     1 
ATOM   6868  C CA    . GLY A 1 2196 ? 167.965 200.736 197.401 1.00 35.49  ? 2196 GLY A CA    1 
ATOM   6869  C C     . GLY A 1 2196 ? 166.914 199.819 197.991 1.00 35.49  ? 2196 GLY A C     1 
ATOM   6870  O O     . GLY A 1 2196 ? 166.236 199.088 197.263 1.00 35.49  ? 2196 GLY A O     1 
ATOM   6871  N N     . GLU A 1 2197 ? 166.776 199.841 199.316 1.00 41.34  ? 2197 GLU A N     1 
ATOM   6872  C CA    . GLU A 1 2197 ? 165.858 198.946 200.009 1.00 41.34  ? 2197 GLU A CA    1 
ATOM   6873  C C     . GLU A 1 2197 ? 164.394 199.323 199.826 1.00 41.34  ? 2197 GLU A C     1 
ATOM   6874  O O     . GLU A 1 2197 ? 163.526 198.463 200.010 1.00 41.34  ? 2197 GLU A O     1 
ATOM   6875  C CB    . GLU A 1 2197 ? 166.191 198.905 201.502 1.00 41.34  ? 2197 GLU A CB    1 
ATOM   6876  C CG    . GLU A 1 2197 ? 167.509 198.220 201.826 1.00 41.34  ? 2197 GLU A CG    1 
ATOM   6877  C CD    . GLU A 1 2197 ? 168.694 199.160 201.738 1.00 41.34  ? 2197 GLU A CD    1 
ATOM   6878  O OE1   . GLU A 1 2197 ? 168.483 200.361 201.469 1.00 41.34  ? 2197 GLU A OE1   1 
ATOM   6879  O OE2   . GLU A 1 2197 ? 169.837 198.698 201.938 1.00 41.34  ? 2197 GLU A OE2   1 
ATOM   6880  N N     . GLU A 1 2198 ? 164.097 200.572 199.476 1.00 36.28  ? 2198 GLU A N     1 
ATOM   6881  C CA    . GLU A 1 2198 ? 162.717 200.987 199.278 1.00 36.28  ? 2198 GLU A CA    1 
ATOM   6882  C C     . GLU A 1 2198 ? 162.107 200.275 198.071 1.00 36.28  ? 2198 GLU A C     1 
ATOM   6883  O O     . GLU A 1 2198 ? 162.792 199.610 197.288 1.00 36.28  ? 2198 GLU A O     1 
ATOM   6884  C CB    . GLU A 1 2198 ? 162.633 202.503 199.104 1.00 36.28  ? 2198 GLU A CB    1 
ATOM   6885  C CG    . GLU A 1 2198 ? 162.554 203.285 200.409 1.00 36.28  ? 2198 GLU A CG    1 
ATOM   6886  C CD    . GLU A 1 2198 ? 163.897 203.446 201.094 1.00 36.28  ? 2198 GLU A CD    1 
ATOM   6887  O OE1   . GLU A 1 2198 ? 164.913 202.985 200.540 1.00 36.28  ? 2198 GLU A OE1   1 
ATOM   6888  O OE2   . GLU A 1 2198 ? 163.936 204.042 202.191 1.00 36.28  ? 2198 GLU A OE2   1 
ATOM   6889  N N     . VAL A 1 2199 ? 160.787 200.419 197.933 1.00 26.28  ? 2199 VAL A N     1 
ATOM   6890  C CA    . VAL A 1 2199 ? 160.075 199.775 196.837 1.00 26.28  ? 2199 VAL A CA    1 
ATOM   6891  C C     . VAL A 1 2199 ? 160.542 200.364 195.516 1.00 26.28  ? 2199 VAL A C     1 
ATOM   6892  O O     . VAL A 1 2199 ? 160.603 201.588 195.347 1.00 26.28  ? 2199 VAL A O     1 
ATOM   6893  C CB    . VAL A 1 2199 ? 158.559 199.935 197.020 1.00 26.28  ? 2199 VAL A CB    1 
ATOM   6894  C CG1   . VAL A 1 2199 ? 157.818 199.370 195.821 1.00 26.28  ? 2199 VAL A CG1   1 
ATOM   6895  C CG2   . VAL A 1 2199 ? 158.108 199.253 198.299 1.00 26.28  ? 2199 VAL A CG2   1 
ATOM   6896  N N     . GLY A 1 2200 ? 160.874 199.490 194.570 1.00 22.37  ? 2200 GLY A N     1 
ATOM   6897  C CA    . GLY A 1 2200 ? 161.421 199.912 193.301 1.00 22.37  ? 2200 GLY A CA    1 
ATOM   6898  C C     . GLY A 1 2200 ? 162.915 200.135 193.295 1.00 22.37  ? 2200 GLY A C     1 
ATOM   6899  O O     . GLY A 1 2200 ? 163.445 200.633 192.295 1.00 22.37  ? 2200 GLY A O     1 
ATOM   6900  N N     . GLY A 1 2201 ? 163.610 199.793 194.381 1.00 21.26  ? 2201 GLY A N     1 
ATOM   6901  C CA    . GLY A 1 2201 ? 165.051 199.975 194.409 1.00 21.26  ? 2201 GLY A CA    1 
ATOM   6902  C C     . GLY A 1 2201 ? 165.772 199.103 193.401 1.00 21.26  ? 2201 GLY A C     1 
ATOM   6903  O O     . GLY A 1 2201 ? 166.682 199.561 192.707 1.00 21.26  ? 2201 GLY A O     1 
ATOM   6904  N N     . MET A 1 2202 ? 165.372 197.834 193.302 1.00 19.74  ? 2202 MET A N     1 
ATOM   6905  C CA    . MET A 1 2202 ? 166.008 196.939 192.342 1.00 19.74  ? 2202 MET A CA    1 
ATOM   6906  C C     . MET A 1 2202 ? 165.791 197.425 190.915 1.00 19.74  ? 2202 MET A C     1 
ATOM   6907  O O     . MET A 1 2202 ? 166.684 197.311 190.069 1.00 19.74  ? 2202 MET A O     1 
ATOM   6908  C CB    . MET A 1 2202 ? 165.477 195.518 192.519 1.00 19.74  ? 2202 MET A CB    1 
ATOM   6909  C CG    . MET A 1 2202 ? 166.101 194.766 193.685 1.00 19.74  ? 2202 MET A CG    1 
ATOM   6910  S SD    . MET A 1 2202 ? 164.895 193.848 194.661 1.00 19.74  ? 2202 MET A SD    1 
ATOM   6911  C CE    . MET A 1 2202 ? 164.063 195.184 195.513 1.00 19.74  ? 2202 MET A CE    1 
ATOM   6912  N N     . TRP A 1 2203 ? 164.615 197.989 190.634 1.00 12.07  ? 2203 TRP A N     1 
ATOM   6913  C CA    . TRP A 1 2203 ? 164.334 198.459 189.282 1.00 12.07  ? 2203 TRP A CA    1 
ATOM   6914  C C     . TRP A 1 2203 ? 165.202 199.657 188.913 1.00 12.07  ? 2203 TRP A C     1 
ATOM   6915  O O     . TRP A 1 2203 ? 165.747 199.716 187.805 1.00 12.07  ? 2203 TRP A O     1 
ATOM   6916  C CB    . TRP A 1 2203 ? 162.854 198.802 189.139 1.00 12.07  ? 2203 TRP A CB    1 
ATOM   6917  C CG    . TRP A 1 2203 ? 162.486 199.186 187.751 1.00 12.07  ? 2203 TRP A CG    1 
ATOM   6918  C CD1   . TRP A 1 2203 ? 162.345 198.352 186.683 1.00 12.07  ? 2203 TRP A CD1   1 
ATOM   6919  C CD2   . TRP A 1 2203 ? 162.232 200.506 187.267 1.00 12.07  ? 2203 TRP A CD2   1 
ATOM   6920  N NE1   . TRP A 1 2203 ? 162.007 199.071 185.564 1.00 12.07  ? 2203 TRP A NE1   1 
ATOM   6921  C CE2   . TRP A 1 2203 ? 161.933 200.398 185.897 1.00 12.07  ? 2203 TRP A CE2   1 
ATOM   6922  C CE3   . TRP A 1 2203 ? 162.224 201.770 187.861 1.00 12.07  ? 2203 TRP A CE3   1 
ATOM   6923  C CZ2   . TRP A 1 2203 ? 161.628 201.504 185.113 1.00 12.07  ? 2203 TRP A CZ2   1 
ATOM   6924  C CZ3   . TRP A 1 2203 ? 161.923 202.864 187.082 1.00 12.07  ? 2203 TRP A CZ3   1 
ATOM   6925  C CH2   . TRP A 1 2203 ? 161.629 202.726 185.722 1.00 12.07  ? 2203 TRP A CH2   1 
ATOM   6926  N N     . VAL A 1 2204 ? 165.347 200.623 189.822 1.00 15.85  ? 2204 VAL A N     1 
ATOM   6927  C CA    . VAL A 1 2204 ? 166.189 201.772 189.508 1.00 15.85  ? 2204 VAL A CA    1 
ATOM   6928  C C     . VAL A 1 2204 ? 167.653 201.354 189.455 1.00 15.85  ? 2204 VAL A C     1 
ATOM   6929  O O     . VAL A 1 2204 ? 168.437 201.915 188.679 1.00 15.85  ? 2204 VAL A O     1 
ATOM   6930  C CB    . VAL A 1 2204 ? 165.950 202.920 190.507 1.00 15.85  ? 2204 VAL A CB    1 
ATOM   6931  C CG1   . VAL A 1 2204 ? 166.478 202.565 191.874 1.00 15.85  ? 2204 VAL A CG1   1 
ATOM   6932  C CG2   . VAL A 1 2204 ? 166.580 204.205 190.004 1.00 15.85  ? 2204 VAL A CG2   1 
ATOM   6933  N N     . GLU A 1 2205 ? 168.050 200.360 190.257 1.00 17.36  ? 2205 GLU A N     1 
ATOM   6934  C CA    . GLU A 1 2205 ? 169.401 199.822 190.136 1.00 17.36  ? 2205 GLU A CA    1 
ATOM   6935  C C     . GLU A 1 2205 ? 169.620 199.206 188.763 1.00 17.36  ? 2205 GLU A C     1 
ATOM   6936  O O     . GLU A 1 2205 ? 170.685 199.379 188.161 1.00 17.36  ? 2205 GLU A O     1 
ATOM   6937  C CB    . GLU A 1 2205 ? 169.662 198.787 191.228 1.00 17.36  ? 2205 GLU A CB    1 
ATOM   6938  C CG    . GLU A 1 2205 ? 169.760 199.364 192.624 1.00 17.36  ? 2205 GLU A CG    1 
ATOM   6939  C CD    . GLU A 1 2205 ? 170.152 198.327 193.658 1.00 17.36  ? 2205 GLU A CD    1 
ATOM   6940  O OE1   . GLU A 1 2205 ? 170.341 197.150 193.282 1.00 17.36  ? 2205 GLU A OE1   1 
ATOM   6941  O OE2   . GLU A 1 2205 ? 170.271 198.689 194.847 1.00 17.36  ? 2205 GLU A OE2   1 
ATOM   6942  N N     . LYS A 1 2206 ? 168.619 198.488 188.252 1.00 12.25  ? 2206 LYS A N     1 
ATOM   6943  C CA    . LYS A 1 2206 ? 168.724 197.919 186.915 1.00 12.25  ? 2206 LYS A CA    1 
ATOM   6944  C C     . LYS A 1 2206 ? 168.790 199.013 185.856 1.00 12.25  ? 2206 LYS A C     1 
ATOM   6945  O O     . LYS A 1 2206 ? 169.519 198.886 184.868 1.00 12.25  ? 2206 LYS A O     1 
ATOM   6946  C CB    . LYS A 1 2206 ? 167.546 196.983 186.656 1.00 12.25  ? 2206 LYS A CB    1 
ATOM   6947  C CG    . LYS A 1 2206 ? 167.663 195.644 187.362 1.00 12.25  ? 2206 LYS A CG    1 
ATOM   6948  C CD    . LYS A 1 2206 ? 168.851 194.849 186.860 1.00 12.25  ? 2206 LYS A CD    1 
ATOM   6949  C CE    . LYS A 1 2206 ? 169.180 193.710 187.805 1.00 12.25  ? 2206 LYS A CE    1 
ATOM   6950  N NZ    . LYS A 1 2206 ? 170.315 192.893 187.302 1.00 12.25  ? 2206 LYS A NZ    1 
ATOM   6951  N N     . VAL A 1 2207 ? 168.033 200.095 186.046 1.00 12.69  ? 2207 VAL A N     1 
ATOM   6952  C CA    . VAL A 1 2207 ? 168.090 201.215 185.106 1.00 12.69  ? 2207 VAL A CA    1 
ATOM   6953  C C     . VAL A 1 2207 ? 169.484 201.833 185.095 1.00 12.69  ? 2207 VAL A C     1 
ATOM   6954  O O     . VAL A 1 2207 ? 170.049 202.122 184.031 1.00 12.69  ? 2207 VAL A O     1 
ATOM   6955  C CB    . VAL A 1 2207 ? 167.013 202.260 185.450 1.00 12.69  ? 2207 VAL A CB    1 
ATOM   6956  C CG1   . VAL A 1 2207 ? 167.201 203.510 184.607 1.00 12.69  ? 2207 VAL A CG1   1 
ATOM   6957  C CG2   . VAL A 1 2207 ? 165.628 201.685 185.242 1.00 12.69  ? 2207 VAL A CG2   1 
ATOM   6958  N N     . LEU A 1 2208 ? 170.062 202.044 186.279 1.00 12.90  ? 2208 LEU A N     1 
ATOM   6959  C CA    . LEU A 1 2208 ? 171.403 202.615 186.355 1.00 12.90  ? 2208 LEU A CA    1 
ATOM   6960  C C     . LEU A 1 2208 ? 172.442 201.674 185.759 1.00 12.90  ? 2208 LEU A C     1 
ATOM   6961  O O     . LEU A 1 2208 ? 173.401 202.123 185.122 1.00 12.90  ? 2208 LEU A O     1 
ATOM   6962  C CB    . LEU A 1 2208 ? 171.748 202.958 187.802 1.00 12.90  ? 2208 LEU A CB    1 
ATOM   6963  C CG    . LEU A 1 2208 ? 170.926 204.094 188.404 1.00 12.90  ? 2208 LEU A CG    1 
ATOM   6964  C CD1   . LEU A 1 2208 ? 171.571 204.584 189.678 1.00 12.90  ? 2208 LEU A CD1   1 
ATOM   6965  C CD2   . LEU A 1 2208 ? 170.801 205.226 187.409 1.00 12.90  ? 2208 LEU A CD2   1 
ATOM   6966  N N     . GLN A 1 2209 ? 172.278 200.366 185.959 1.00 14.77  ? 2209 GLN A N     1 
ATOM   6967  C CA    . GLN A 1 2209 ? 173.179 199.410 185.322 1.00 14.77  ? 2209 GLN A CA    1 
ATOM   6968  C C     . GLN A 1 2209 ? 173.056 199.471 183.806 1.00 14.77  ? 2209 GLN A C     1 
ATOM   6969  O O     . GLN A 1 2209 ? 174.061 199.403 183.088 1.00 14.77  ? 2209 GLN A O     1 
ATOM   6970  C CB    . GLN A 1 2209 ? 172.894 197.997 185.827 1.00 14.77  ? 2209 GLN A CB    1 
ATOM   6971  C CG    . GLN A 1 2209 ? 173.310 197.766 187.264 1.00 14.77  ? 2209 GLN A CG    1 
ATOM   6972  C CD    . GLN A 1 2209 ? 172.773 196.469 187.823 1.00 14.77  ? 2209 GLN A CD    1 
ATOM   6973  O OE1   . GLN A 1 2209 ? 172.221 195.646 187.094 1.00 14.77  ? 2209 GLN A OE1   1 
ATOM   6974  N NE2   . GLN A 1 2209 ? 172.930 196.278 189.126 1.00 14.77  ? 2209 GLN A NE2   1 
ATOM   6975  N N     . LEU A 1 2210 ? 171.829 199.587 183.299 1.00 14.34  ? 2210 LEU A N     1 
ATOM   6976  C CA    . LEU A 1 2210 ? 171.639 199.746 181.864 1.00 14.34  ? 2210 LEU A CA    1 
ATOM   6977  C C     . LEU A 1 2210 ? 172.354 200.991 181.362 1.00 14.34  ? 2210 LEU A C     1 
ATOM   6978  O O     . LEU A 1 2210 ? 172.985 200.969 180.302 1.00 14.34  ? 2210 LEU A O     1 
ATOM   6979  C CB    . LEU A 1 2210 ? 170.148 199.804 181.535 1.00 14.34  ? 2210 LEU A CB    1 
ATOM   6980  C CG    . LEU A 1 2210 ? 169.790 200.097 180.081 1.00 14.34  ? 2210 LEU A CG    1 
ATOM   6981  C CD1   . LEU A 1 2210 ? 170.129 198.908 179.206 1.00 14.34  ? 2210 LEU A CD1   1 
ATOM   6982  C CD2   . LEU A 1 2210 ? 168.320 200.440 179.966 1.00 14.34  ? 2210 LEU A CD2   1 
ATOM   6983  N N     . TYR A 1 2211 ? 172.289 202.080 182.131 1.00 16.42  ? 2211 TYR A N     1 
ATOM   6984  C CA    . TYR A 1 2211 ? 173.035 203.285 181.775 1.00 16.42  ? 2211 TYR A CA    1 
ATOM   6985  C C     . TYR A 1 2211 ? 174.538 203.026 181.767 1.00 16.42  ? 2211 TYR A C     1 
ATOM   6986  O O     . TYR A 1 2211 ? 175.258 203.515 180.887 1.00 16.42  ? 2211 TYR A O     1 
ATOM   6987  C CB    . TYR A 1 2211 ? 172.694 204.414 182.745 1.00 16.42  ? 2211 TYR A CB    1 
ATOM   6988  C CG    . TYR A 1 2211 ? 173.426 205.704 182.471 1.00 16.42  ? 2211 TYR A CG    1 
ATOM   6989  C CD1   . TYR A 1 2211 ? 173.391 206.289 181.214 1.00 16.42  ? 2211 TYR A CD1   1 
ATOM   6990  C CD2   . TYR A 1 2211 ? 174.149 206.341 183.470 1.00 16.42  ? 2211 TYR A CD2   1 
ATOM   6991  C CE1   . TYR A 1 2211 ? 174.056 207.469 180.959 1.00 16.42  ? 2211 TYR A CE1   1 
ATOM   6992  C CE2   . TYR A 1 2211 ? 174.817 207.522 183.224 1.00 16.42  ? 2211 TYR A CE2   1 
ATOM   6993  C CZ    . TYR A 1 2211 ? 174.768 208.082 181.966 1.00 16.42  ? 2211 TYR A CZ    1 
ATOM   6994  O OH    . TYR A 1 2211 ? 175.431 209.259 181.713 1.00 16.42  ? 2211 TYR A OH    1 
ATOM   6995  N N     . GLN A 1 2212 ? 175.031 202.265 182.748 1.00 17.82  ? 2212 GLN A N     1 
ATOM   6996  C CA    . GLN A 1 2212 ? 176.461 201.977 182.819 1.00 17.82  ? 2212 GLN A CA    1 
ATOM   6997  C C     . GLN A 1 2212 ? 176.937 201.219 181.588 1.00 17.82  ? 2212 GLN A C     1 
ATOM   6998  O O     . GLN A 1 2212 ? 177.912 201.620 180.943 1.00 17.82  ? 2212 GLN A O     1 
ATOM   6999  C CB    . GLN A 1 2212 ? 176.785 201.173 184.077 1.00 17.82  ? 2212 GLN A CB    1 
ATOM   7000  C CG    . GLN A 1 2212 ? 176.575 201.910 185.382 1.00 17.82  ? 2212 GLN A CG    1 
ATOM   7001  C CD    . GLN A 1 2212 ? 176.943 201.061 186.584 1.00 17.82  ? 2212 GLN A CD    1 
ATOM   7002  O OE1   . GLN A 1 2212 ? 176.973 199.833 186.505 1.00 17.82  ? 2212 GLN A OE1   1 
ATOM   7003  N NE2   . GLN A 1 2212 ? 177.228 201.714 187.704 1.00 17.82  ? 2212 GLN A NE2   1 
ATOM   7004  N N     . ILE A 1 2213 ? 176.265 200.118 181.245 1.00 17.26  ? 2213 ILE A N     1 
ATOM   7005  C CA    . ILE A 1 2213 ? 176.687 199.368 180.062 1.00 17.26  ? 2213 ILE A CA    1 
ATOM   7006  C C     . ILE A 1 2213 ? 176.402 200.150 178.779 1.00 17.26  ? 2213 ILE A C     1 
ATOM   7007  O O     . ILE A 1 2213 ? 177.091 199.961 177.769 1.00 17.26  ? 2213 ILE A O     1 
ATOM   7008  C CB    . ILE A 1 2213 ? 176.087 197.944 180.037 1.00 17.26  ? 2213 ILE A CB    1 
ATOM   7009  C CG1   . ILE A 1 2213 ? 176.586 197.100 181.219 1.00 17.26  ? 2213 ILE A CG1   1 
ATOM   7010  C CG2   . ILE A 1 2213 ? 176.469 197.206 178.779 1.00 17.26  ? 2213 ILE A CG2   1 
ATOM   7011  C CD1   . ILE A 1 2213 ? 175.797 197.164 182.474 1.00 17.26  ? 2213 ILE A CD1   1 
ATOM   7012  N N     . THR A 1 2214 ? 175.425 201.060 178.790 1.00 18.11  ? 2214 THR A N     1 
ATOM   7013  C CA    . THR A 1 2214 ? 175.244 201.952 177.647 1.00 18.11  ? 2214 THR A CA    1 
ATOM   7014  C C     . THR A 1 2214 ? 176.474 202.828 177.443 1.00 18.11  ? 2214 THR A C     1 
ATOM   7015  O O     . THR A 1 2214 ? 176.950 203.001 176.316 1.00 18.11  ? 2214 THR A O     1 
ATOM   7016  C CB    . THR A 1 2214 ? 173.997 202.815 177.844 1.00 18.11  ? 2214 THR A CB    1 
ATOM   7017  O OG1   . THR A 1 2214 ? 172.833 201.982 177.873 1.00 18.11  ? 2214 THR A OG1   1 
ATOM   7018  C CG2   . THR A 1 2214 ? 173.861 203.825 176.717 1.00 18.11  ? 2214 THR A CG2   1 
ATOM   7019  N N     . GLN A 1 2215 ? 177.001 203.389 178.533 1.00 19.07  ? 2215 GLN A N     1 
ATOM   7020  C CA    . GLN A 1 2215 ? 178.237 204.163 178.444 1.00 19.07  ? 2215 GLN A CA    1 
ATOM   7021  C C     . GLN A 1 2215 ? 179.413 203.288 178.026 1.00 19.07  ? 2215 GLN A C     1 
ATOM   7022  O O     . GLN A 1 2215 ? 180.262 203.713 177.234 1.00 19.07  ? 2215 GLN A O     1 
ATOM   7023  C CB    . GLN A 1 2215 ? 178.531 204.848 179.778 1.00 19.07  ? 2215 GLN A CB    1 
ATOM   7024  C CG    . GLN A 1 2215 ? 177.528 205.915 180.168 1.00 19.07  ? 2215 GLN A CG    1 
ATOM   7025  C CD    . GLN A 1 2215 ? 177.760 207.215 179.426 1.00 19.07  ? 2215 GLN A CD    1 
ATOM   7026  O OE1   . GLN A 1 2215 ? 178.856 207.470 178.928 1.00 19.07  ? 2215 GLN A OE1   1 
ATOM   7027  N NE2   . GLN A 1 2215 ? 176.728 208.044 179.343 1.00 19.07  ? 2215 GLN A NE2   1 
ATOM   7028  N N     . ILE A 1 2216 ? 179.481 202.065 178.555 1.00 21.83  ? 2216 ILE A N     1 
ATOM   7029  C CA    . ILE A 1 2216 ? 180.648 201.216 178.336 1.00 21.83  ? 2216 ILE A CA    1 
ATOM   7030  C C     . ILE A 1 2216 ? 180.759 200.813 176.870 1.00 21.83  ? 2216 ILE A C     1 
ATOM   7031  O O     . ILE A 1 2216 ? 181.829 200.923 176.260 1.00 21.83  ? 2216 ILE A O     1 
ATOM   7032  C CB    . ILE A 1 2216 ? 180.594 199.984 179.258 1.00 21.83  ? 2216 ILE A CB    1 
ATOM   7033  C CG1   . ILE A 1 2216 ? 181.081 200.347 180.662 1.00 21.83  ? 2216 ILE A CG1   1 
ATOM   7034  C CG2   . ILE A 1 2216 ? 181.424 198.845 178.687 1.00 21.83  ? 2216 ILE A CG2   1 
ATOM   7035  C CD1   . ILE A 1 2216 ? 180.995 199.204 181.649 1.00 21.83  ? 2216 ILE A CD1   1 
ATOM   7036  N N     . ASN A 1 2217 ? 179.661 200.348 176.278 1.00 24.93  ? 2217 ASN A N     1 
ATOM   7037  C CA    . ASN A 1 2217 ? 179.721 199.825 174.922 1.00 24.93  ? 2217 ASN A CA    1 
ATOM   7038  C C     . ASN A 1 2217 ? 178.362 199.948 174.252 1.00 24.93  ? 2217 ASN A C     1 
ATOM   7039  O O     . ASN A 1 2217 ? 177.336 200.149 174.907 1.00 24.93  ? 2217 ASN A O     1 
ATOM   7040  C CB    . ASN A 1 2217 ? 180.186 198.362 174.906 1.00 24.93  ? 2217 ASN A CB    1 
ATOM   7041  C CG    . ASN A 1 2217 ? 179.392 197.483 175.856 1.00 24.93  ? 2217 ASN A CG    1 
ATOM   7042  O OD1   . ASN A 1 2217 ? 178.270 197.811 176.235 1.00 24.93  ? 2217 ASN A OD1   1 
ATOM   7043  N ND2   . ASN A 1 2217 ? 179.975 196.356 176.244 1.00 24.93  ? 2217 ASN A ND2   1 
ATOM   7044  N N     . HIS A 1 2218 ? 178.374 199.827 172.928 1.00 31.70  ? 2218 HIS A N     1 
ATOM   7045  C CA    . HIS A 1 2218 ? 177.149 199.728 172.153 1.00 31.70  ? 2218 HIS A CA    1 
ATOM   7046  C C     . HIS A 1 2218 ? 176.680 198.275 172.126 1.00 31.70  ? 2218 HIS A C     1 
ATOM   7047  O O     . HIS A 1 2218 ? 177.312 197.379 172.693 1.00 31.70  ? 2218 HIS A O     1 
ATOM   7048  C CB    . HIS A 1 2218 ? 177.366 200.259 170.739 1.00 31.70  ? 2218 HIS A CB    1 
ATOM   7049  C CG    . HIS A 1 2218 ? 178.321 199.442 169.927 1.00 31.70  ? 2218 HIS A CG    1 
ATOM   7050  N ND1   . HIS A 1 2218 ? 179.638 199.255 170.287 1.00 31.70  ? 2218 HIS A ND1   1 
ATOM   7051  C CD2   . HIS A 1 2218 ? 178.147 198.755 168.773 1.00 31.70  ? 2218 HIS A CD2   1 
ATOM   7052  C CE1   . HIS A 1 2218 ? 180.235 198.491 169.390 1.00 31.70  ? 2218 HIS A CE1   1 
ATOM   7053  N NE2   . HIS A 1 2218 ? 179.352 198.174 168.461 1.00 31.70  ? 2218 HIS A NE2   1 
ATOM   7054  N N     . GLY A 1 2219 ? 175.560 198.034 171.452 1.00 26.13  ? 2219 GLY A N     1 
ATOM   7055  C CA    . GLY A 1 2219 ? 175.033 196.689 171.345 1.00 26.13  ? 2219 GLY A CA    1 
ATOM   7056  C C     . GLY A 1 2219 ? 174.596 196.117 172.676 1.00 26.13  ? 2219 GLY A C     1 
ATOM   7057  O O     . GLY A 1 2219 ? 175.208 195.175 173.184 1.00 26.13  ? 2219 GLY A O     1 
ATOM   7058  N N     . LEU A 1 2220 ? 173.548 196.686 173.259 1.00 21.68  ? 2220 LEU A N     1 
ATOM   7059  C CA    . LEU A 1 2220 ? 173.052 196.216 174.541 1.00 21.68  ? 2220 LEU A CA    1 
ATOM   7060  C C     . LEU A 1 2220 ? 172.141 195.007 174.350 1.00 21.68  ? 2220 LEU A C     1 
ATOM   7061  O O     . LEU A 1 2220 ? 171.754 194.657 173.232 1.00 21.68  ? 2220 LEU A O     1 
ATOM   7062  C CB    . LEU A 1 2220 ? 172.307 197.339 175.258 1.00 21.68  ? 2220 LEU A CB    1 
ATOM   7063  C CG    . LEU A 1 2220 ? 173.166 198.573 175.530 1.00 21.68  ? 2220 LEU A CG    1 
ATOM   7064  C CD1   . LEU A 1 2220 ? 172.337 199.833 175.510 1.00 21.68  ? 2220 LEU A CD1   1 
ATOM   7065  C CD2   . LEU A 1 2220 ? 173.843 198.435 176.865 1.00 21.68  ? 2220 LEU A CD2   1 
ATOM   7066  N N     . MET A 1 2221 ? 171.803 194.363 175.464 1.00 22.22  ? 2221 MET A N     1 
ATOM   7067  C CA    . MET A 1 2221 ? 170.897 193.217 175.456 1.00 22.22  ? 2221 MET A CA    1 
ATOM   7068  C C     . MET A 1 2221 ? 170.258 193.105 176.831 1.00 22.22  ? 2221 MET A C     1 
ATOM   7069  O O     . MET A 1 2221 ? 170.892 192.620 177.772 1.00 22.22  ? 2221 MET A O     1 
ATOM   7070  C CB    . MET A 1 2221 ? 171.628 191.926 175.093 1.00 22.22  ? 2221 MET A CB    1 
ATOM   7071  C CG    . MET A 1 2221 ? 170.695 190.763 174.805 1.00 22.22  ? 2221 MET A CG    1 
ATOM   7072  S SD    . MET A 1 2221 ? 171.311 189.664 173.521 1.00 22.22  ? 2221 MET A SD    1 
ATOM   7073  C CE    . MET A 1 2221 ? 172.993 189.437 174.083 1.00 22.22  ? 2221 MET A CE    1 
ATOM   7074  N N     . MET A 1 2222 ? 169.008 193.541 176.944 1.00 15.40  ? 2222 MET A N     1 
ATOM   7075  C CA    . MET A 1 2222 ? 168.255 193.484 178.190 1.00 15.40  ? 2222 MET A CA    1 
ATOM   7076  C C     . MET A 1 2222 ? 167.427 192.205 178.193 1.00 15.40  ? 2222 MET A C     1 
ATOM   7077  O O     . MET A 1 2222 ? 166.451 192.089 177.446 1.00 15.40  ? 2222 MET A O     1 
ATOM   7078  C CB    . MET A 1 2222 ? 167.368 194.716 178.334 1.00 15.40  ? 2222 MET A CB    1 
ATOM   7079  C CG    . MET A 1 2222 ? 168.091 196.014 178.057 1.00 15.40  ? 2222 MET A CG    1 
ATOM   7080  S SD    . MET A 1 2222 ? 166.969 197.416 178.059 1.00 15.40  ? 2222 MET A SD    1 
ATOM   7081  C CE    . MET A 1 2222 ? 166.292 197.265 176.410 1.00 15.40  ? 2222 MET A CE    1 
ATOM   7082  N N     . VAL A 1 2223 ? 167.813 191.253 179.033 1.00 16.69  ? 2223 VAL A N     1 
ATOM   7083  C CA    . VAL A 1 2223 ? 167.187 189.940 179.074 1.00 16.69  ? 2223 VAL A CA    1 
ATOM   7084  C C     . VAL A 1 2223 ? 166.435 189.809 180.391 1.00 16.69  ? 2223 VAL A C     1 
ATOM   7085  O O     . VAL A 1 2223 ? 166.851 190.351 181.420 1.00 16.69  ? 2223 VAL A O     1 
ATOM   7086  C CB    . VAL A 1 2223 ? 168.241 188.822 178.921 1.00 16.69  ? 2223 VAL A CB    1 
ATOM   7087  C CG1   . VAL A 1 2223 ? 167.603 187.449 179.017 1.00 16.69  ? 2223 VAL A CG1   1 
ATOM   7088  C CG2   . VAL A 1 2223 ? 169.016 188.985 177.628 1.00 16.69  ? 2223 VAL A CG2   1 
ATOM   7089  N N     . GLY A 1 2224 ? 165.318 189.089 180.357 1.00 15.20  ? 2224 GLY A N     1 
ATOM   7090  C CA    . GLY A 1 2224 ? 164.559 188.827 181.556 1.00 15.20  ? 2224 GLY A CA    1 
ATOM   7091  C C     . GLY A 1 2224 ? 163.232 188.159 181.275 1.00 15.20  ? 2224 GLY A C     1 
ATOM   7092  O O     . GLY A 1 2224 ? 162.673 188.272 180.180 1.00 15.20  ? 2224 GLY A O     1 
ATOM   7093  N N     . PRO A 1 2225 ? 162.701 187.443 182.266 1.00 13.53  ? 2225 PRO A N     1 
ATOM   7094  C CA    . PRO A 1 2225 ? 161.406 186.780 182.084 1.00 13.53  ? 2225 PRO A CA    1 
ATOM   7095  C C     . PRO A 1 2225 ? 160.308 187.789 181.796 1.00 13.53  ? 2225 PRO A C     1 
ATOM   7096  O O     . PRO A 1 2225 ? 160.336 188.924 182.275 1.00 13.53  ? 2225 PRO A O     1 
ATOM   7097  C CB    . PRO A 1 2225 ? 161.176 186.072 183.424 1.00 13.53  ? 2225 PRO A CB    1 
ATOM   7098  C CG    . PRO A 1 2225 ? 162.531 185.947 184.028 1.00 13.53  ? 2225 PRO A CG    1 
ATOM   7099  C CD    . PRO A 1 2225 ? 163.284 187.160 183.586 1.00 13.53  ? 2225 PRO A CD    1 
ATOM   7100  N N     . SER A 1 2226 ? 159.339 187.364 180.987 1.00 14.84  ? 2226 SER A N     1 
ATOM   7101  C CA    . SER A 1 2226 ? 158.240 188.243 180.616 1.00 14.84  ? 2226 SER A CA    1 
ATOM   7102  C C     . SER A 1 2226 ? 157.482 188.691 181.856 1.00 14.84  ? 2226 SER A C     1 
ATOM   7103  O O     . SER A 1 2226 ? 156.993 187.868 182.634 1.00 14.84  ? 2226 SER A O     1 
ATOM   7104  C CB    . SER A 1 2226 ? 157.296 187.532 179.649 1.00 14.84  ? 2226 SER A CB    1 
ATOM   7105  O OG    . SER A 1 2226 ? 156.233 188.388 179.268 1.00 14.84  ? 2226 SER A OG    1 
ATOM   7106  N N     . GLY A 1 2227 ? 157.381 190.004 182.032 1.00 12.75  ? 2227 GLY A N     1 
ATOM   7107  C CA    . GLY A 1 2227 ? 156.782 190.588 183.212 1.00 12.75  ? 2227 GLY A CA    1 
ATOM   7108  C C     . GLY A 1 2227 ? 157.713 191.455 184.026 1.00 12.75  ? 2227 GLY A C     1 
ATOM   7109  O O     . GLY A 1 2227 ? 157.260 192.080 184.991 1.00 12.75  ? 2227 GLY A O     1 
ATOM   7110  N N     . SER A 1 2228 ? 158.995 191.513 183.679 1.00 12.00  ? 2228 SER A N     1 
ATOM   7111  C CA    . SER A 1 2228 ? 159.925 192.387 184.370 1.00 12.00  ? 2228 SER A CA    1 
ATOM   7112  C C     . SER A 1 2228 ? 159.893 193.785 183.763 1.00 12.00  ? 2228 SER A C     1 
ATOM   7113  O O     . SER A 1 2228 ? 159.370 194.005 182.667 1.00 12.00  ? 2228 SER A O     1 
ATOM   7114  C CB    . SER A 1 2228 ? 161.343 191.823 184.309 1.00 12.00  ? 2228 SER A CB    1 
ATOM   7115  O OG    . SER A 1 2228 ? 161.392 190.518 184.853 1.00 12.00  ? 2228 SER A OG    1 
ATOM   7116  N N     . GLY A 1 2229 ? 160.464 194.738 184.490 1.00 11.85  ? 2229 GLY A N     1 
ATOM   7117  C CA    . GLY A 1 2229 ? 160.504 196.105 184.013 1.00 11.85  ? 2229 GLY A CA    1 
ATOM   7118  C C     . GLY A 1 2229 ? 161.604 196.338 183.002 1.00 11.85  ? 2229 GLY A C     1 
ATOM   7119  O O     . GLY A 1 2229 ? 162.601 196.996 183.309 1.00 11.85  ? 2229 GLY A O     1 
ATOM   7120  N N     . LYS A 1 2230 ? 161.441 195.803 181.791 1.00 11.76  ? 2230 LYS A N     1 
ATOM   7121  C CA    . LYS A 1 2230 ? 162.461 195.930 180.754 1.00 11.76  ? 2230 LYS A CA    1 
ATOM   7122  C C     . LYS A 1 2230 ? 162.214 197.143 179.863 1.00 11.76  ? 2230 LYS A C     1 
ATOM   7123  O O     . LYS A 1 2230 ? 163.062 198.036 179.771 1.00 11.76  ? 2230 LYS A O     1 
ATOM   7124  C CB    . LYS A 1 2230 ? 162.511 194.656 179.903 1.00 11.76  ? 2230 LYS A CB    1 
ATOM   7125  C CG    . LYS A 1 2230 ? 163.141 193.468 180.593 1.00 11.76  ? 2230 LYS A CG    1 
ATOM   7126  C CD    . LYS A 1 2230 ? 163.517 192.394 179.593 1.00 11.76  ? 2230 LYS A CD    1 
ATOM   7127  C CE    . LYS A 1 2230 ? 162.286 191.734 179.008 1.00 11.76  ? 2230 LYS A CE    1 
ATOM   7128  N NZ    . LYS A 1 2230 ? 161.499 191.026 180.050 1.00 11.76  ? 2230 LYS A NZ    1 
ATOM   7129  N N     . SER A 1 2231 ? 161.059 197.182 179.196 1.00 13.88  ? 2231 SER A N     1 
ATOM   7130  C CA    . SER A 1 2231 ? 160.764 198.287 178.290 1.00 13.88  ? 2231 SER A CA    1 
ATOM   7131  C C     . SER A 1 2231 ? 160.682 199.608 179.042 1.00 13.88  ? 2231 SER A C     1 
ATOM   7132  O O     . SER A 1 2231 ? 161.221 200.627 178.589 1.00 13.88  ? 2231 SER A O     1 
ATOM   7133  C CB    . SER A 1 2231 ? 159.462 198.014 177.538 1.00 13.88  ? 2231 SER A CB    1 
ATOM   7134  O OG    . SER A 1 2231 ? 159.449 196.705 176.994 1.00 13.88  ? 2231 SER A OG    1 
ATOM   7135  N N     . MET A 1 2232 ? 160.020 199.606 180.200 1.00 14.07  ? 2232 MET A N     1 
ATOM   7136  C CA    . MET A 1 2232 ? 159.908 200.827 180.987 1.00 14.07  ? 2232 MET A CA    1 
ATOM   7137  C C     . MET A 1 2232 ? 161.274 201.311 181.449 1.00 14.07  ? 2232 MET A C     1 
ATOM   7138  O O     . MET A 1 2232 ? 161.517 202.519 181.523 1.00 14.07  ? 2232 MET A O     1 
ATOM   7139  C CB    . MET A 1 2232 ? 158.986 200.598 182.182 1.00 14.07  ? 2232 MET A CB    1 
ATOM   7140  C CG    . MET A 1 2232 ? 157.510 200.629 181.840 1.00 14.07  ? 2232 MET A CG    1 
ATOM   7141  S SD    . MET A 1 2232 ? 156.968 202.247 181.264 1.00 14.07  ? 2232 MET A SD    1 
ATOM   7142  C CE    . MET A 1 2232 ? 155.684 201.781 180.107 1.00 14.07  ? 2232 MET A CE    1 
ATOM   7143  N N     . ALA A 1 2233 ? 162.186 200.382 181.749 1.00 12.49  ? 2233 ALA A N     1 
ATOM   7144  C CA    . ALA A 1 2233 ? 163.514 200.773 182.210 1.00 12.49  ? 2233 ALA A CA    1 
ATOM   7145  C C     . ALA A 1 2233 ? 164.236 201.611 181.165 1.00 12.49  ? 2233 ALA A C     1 
ATOM   7146  O O     . ALA A 1 2233 ? 164.700 202.720 181.454 1.00 12.49  ? 2233 ALA A O     1 
ATOM   7147  C CB    . ALA A 1 2233 ? 164.335 199.535 182.564 1.00 12.49  ? 2233 ALA A CB    1 
ATOM   7148  N N     . TRP A 1 2234 ? 164.319 201.112 179.930 1.00 13.07  ? 2234 TRP A N     1 
ATOM   7149  C CA    . TRP A 1 2234 ? 165.051 201.859 178.916 1.00 13.07  ? 2234 TRP A CA    1 
ATOM   7150  C C     . TRP A 1 2234 ? 164.270 203.068 178.421 1.00 13.07  ? 2234 TRP A C     1 
ATOM   7151  O O     . TRP A 1 2234 ? 164.883 204.064 178.028 1.00 13.07  ? 2234 TRP A O     1 
ATOM   7152  C CB    . TRP A 1 2234 ? 165.448 200.947 177.751 1.00 13.07  ? 2234 TRP A CB    1 
ATOM   7153  C CG    . TRP A 1 2234 ? 164.342 200.509 176.847 1.00 13.07  ? 2234 TRP A CG    1 
ATOM   7154  C CD1   . TRP A 1 2234 ? 163.686 199.318 176.880 1.00 13.07  ? 2234 TRP A CD1   1 
ATOM   7155  C CD2   . TRP A 1 2234 ? 163.796 201.237 175.742 1.00 13.07  ? 2234 TRP A CD2   1 
ATOM   7156  N NE1   . TRP A 1 2234 ? 162.750 199.263 175.877 1.00 13.07  ? 2234 TRP A NE1   1 
ATOM   7157  C CE2   . TRP A 1 2234 ? 162.797 200.431 175.165 1.00 13.07  ? 2234 TRP A CE2   1 
ATOM   7158  C CE3   . TRP A 1 2234 ? 164.046 202.496 175.192 1.00 13.07  ? 2234 TRP A CE3   1 
ATOM   7159  C CZ2   . TRP A 1 2234 ? 162.049 200.843 174.067 1.00 13.07  ? 2234 TRP A CZ2   1 
ATOM   7160  C CZ3   . TRP A 1 2234 ? 163.303 202.902 174.105 1.00 13.07  ? 2234 TRP A CZ3   1 
ATOM   7161  C CH2   . TRP A 1 2234 ? 162.318 202.079 173.552 1.00 13.07  ? 2234 TRP A CH2   1 
ATOM   7162  N N     . ARG A 1 2235 ? 162.935 203.028 178.456 1.00 13.20  ? 2235 ARG A N     1 
ATOM   7163  C CA    . ARG A 1 2235 ? 162.167 204.225 178.124 1.00 13.20  ? 2235 ARG A CA    1 
ATOM   7164  C C     . ARG A 1 2235 ? 162.443 205.347 179.120 1.00 13.20  ? 2235 ARG A C     1 
ATOM   7165  O O     . ARG A 1 2235 ? 162.687 206.500 178.733 1.00 13.20  ? 2235 ARG A O     1 
ATOM   7166  C CB    . ARG A 1 2235 ? 160.675 203.895 178.082 1.00 13.20  ? 2235 ARG A CB    1 
ATOM   7167  C CG    . ARG A 1 2235 ? 160.246 203.125 176.848 1.00 13.20  ? 2235 ARG A CG    1 
ATOM   7168  C CD    . ARG A 1 2235 ? 158.928 203.644 176.302 1.00 13.20  ? 2235 ARG A CD    1 
ATOM   7169  N NE    . ARG A 1 2235 ? 158.489 202.888 175.136 1.00 13.20  ? 2235 ARG A NE    1 
ATOM   7170  C CZ    . ARG A 1 2235 ? 157.942 201.682 175.189 1.00 13.20  ? 2235 ARG A CZ    1 
ATOM   7171  N NH1   . ARG A 1 2235 ? 157.741 201.064 176.341 1.00 13.20  ? 2235 ARG A NH1   1 
ATOM   7172  N NH2   . ARG A 1 2235 ? 157.586 201.081 174.057 1.00 13.20  ? 2235 ARG A NH2   1 
ATOM   7173  N N     . VAL A 1 2236 ? 162.422 205.021 180.415 1.00 13.04  ? 2236 VAL A N     1 
ATOM   7174  C CA    . VAL A 1 2236 ? 162.707 206.013 181.442 1.00 13.04  ? 2236 VAL A CA    1 
ATOM   7175  C C     . VAL A 1 2236 ? 164.148 206.487 181.336 1.00 13.04  ? 2236 VAL A C     1 
ATOM   7176  O O     . VAL A 1 2236 ? 164.438 207.673 181.526 1.00 13.04  ? 2236 VAL A O     1 
ATOM   7177  C CB    . VAL A 1 2236 ? 162.395 205.438 182.835 1.00 13.04  ? 2236 VAL A CB    1 
ATOM   7178  C CG1   . VAL A 1 2236 ? 163.001 206.300 183.923 1.00 13.04  ? 2236 VAL A CG1   1 
ATOM   7179  C CG2   . VAL A 1 2236 ? 160.900 205.320 183.030 1.00 13.04  ? 2236 VAL A CG2   1 
ATOM   7180  N N     . LEU A 1 2237 ? 165.074 205.577 181.023 1.00 15.69  ? 2237 LEU A N     1 
ATOM   7181  C CA    . LEU A 1 2237 ? 166.464 205.982 180.849 1.00 15.69  ? 2237 LEU A CA    1 
ATOM   7182  C C     . LEU A 1 2237 ? 166.616 206.954 179.688 1.00 15.69  ? 2237 LEU A C     1 
ATOM   7183  O O     . LEU A 1 2237 ? 167.337 207.951 179.798 1.00 15.69  ? 2237 LEU A O     1 
ATOM   7184  C CB    . LEU A 1 2237 ? 167.350 204.757 180.634 1.00 15.69  ? 2237 LEU A CB    1 
ATOM   7185  C CG    . LEU A 1 2237 ? 168.844 205.073 180.617 1.00 15.69  ? 2237 LEU A CG    1 
ATOM   7186  C CD1   . LEU A 1 2237 ? 169.289 205.563 181.982 1.00 15.69  ? 2237 LEU A CD1   1 
ATOM   7187  C CD2   . LEU A 1 2237 ? 169.648 203.861 180.188 1.00 15.69  ? 2237 LEU A CD2   1 
ATOM   7188  N N     . LEU A 1 2238 ? 165.945 206.683 178.566 1.00 15.73  ? 2238 LEU A N     1 
ATOM   7189  C CA    . LEU A 1 2238 ? 166.025 207.582 177.420 1.00 15.73  ? 2238 LEU A CA    1 
ATOM   7190  C C     . LEU A 1 2238 ? 165.455 208.953 177.753 1.00 15.73  ? 2238 LEU A C     1 
ATOM   7191  O O     . LEU A 1 2238 ? 166.054 209.981 177.415 1.00 15.73  ? 2238 LEU A O     1 
ATOM   7192  C CB    . LEU A 1 2238 ? 165.291 206.976 176.225 1.00 15.73  ? 2238 LEU A CB    1 
ATOM   7193  C CG    . LEU A 1 2238 ? 165.428 207.722 174.899 1.00 15.73  ? 2238 LEU A CG    1 
ATOM   7194  C CD1   . LEU A 1 2238 ? 166.871 207.722 174.434 1.00 15.73  ? 2238 LEU A CD1   1 
ATOM   7195  C CD2   . LEU A 1 2238 ? 164.528 207.097 173.848 1.00 15.73  ? 2238 LEU A CD2   1 
ATOM   7196  N N     . LYS A 1 2239 ? 164.301 208.991 178.423 1.00 16.54  ? 2239 LYS A N     1 
ATOM   7197  C CA    . LYS A 1 2239 ? 163.708 210.281 178.765 1.00 16.54  ? 2239 LYS A CA    1 
ATOM   7198  C C     . LYS A 1 2239 ? 164.570 211.043 179.767 1.00 16.54  ? 2239 LYS A C     1 
ATOM   7199  O O     . LYS A 1 2239 ? 164.724 212.268 179.661 1.00 16.54  ? 2239 LYS A O     1 
ATOM   7200  C CB    . LYS A 1 2239 ? 162.290 210.082 179.298 1.00 16.54  ? 2239 LYS A CB    1 
ATOM   7201  C CG    . LYS A 1 2239 ? 161.255 209.924 178.195 1.00 16.54  ? 2239 LYS A CG    1 
ATOM   7202  C CD    . LYS A 1 2239 ? 159.851 209.774 178.751 1.00 16.54  ? 2239 LYS A CD    1 
ATOM   7203  C CE    . LYS A 1 2239 ? 158.920 209.152 177.723 1.00 16.54  ? 2239 LYS A CE    1 
ATOM   7204  N NZ    . LYS A 1 2239 ? 159.633 208.192 176.835 1.00 16.54  ? 2239 LYS A NZ    1 
ATOM   7205  N N     . ALA A 1 2240 ? 165.151 210.338 180.741 1.00 16.88  ? 2240 ALA A N     1 
ATOM   7206  C CA    . ALA A 1 2240 ? 166.013 210.993 181.718 1.00 16.88  ? 2240 ALA A CA    1 
ATOM   7207  C C     . ALA A 1 2240 ? 167.287 211.519 181.072 1.00 16.88  ? 2240 ALA A C     1 
ATOM   7208  O O     . ALA A 1 2240 ? 167.772 212.594 181.436 1.00 16.88  ? 2240 ALA A O     1 
ATOM   7209  C CB    . ALA A 1 2240 ? 166.347 210.028 182.854 1.00 16.88  ? 2240 ALA A CB    1 
ATOM   7210  N N     . LEU A 1 2241 ? 167.855 210.769 180.125 1.00 19.22  ? 2241 LEU A N     1 
ATOM   7211  C CA    . LEU A 1 2241 ? 169.019 211.260 179.397 1.00 19.22  ? 2241 LEU A CA    1 
ATOM   7212  C C     . LEU A 1 2241 ? 168.665 212.477 178.554 1.00 19.22  ? 2241 LEU A C     1 
ATOM   7213  O O     . LEU A 1 2241 ? 169.459 213.419 178.449 1.00 19.22  ? 2241 LEU A O     1 
ATOM   7214  C CB    . LEU A 1 2241 ? 169.599 210.151 178.521 1.00 19.22  ? 2241 LEU A CB    1 
ATOM   7215  C CG    . LEU A 1 2241 ? 170.357 209.040 179.246 1.00 19.22  ? 2241 LEU A CG    1 
ATOM   7216  C CD1   . LEU A 1 2241 ? 171.188 208.234 178.265 1.00 19.22  ? 2241 LEU A CD1   1 
ATOM   7217  C CD2   . LEU A 1 2241 ? 171.235 209.621 180.337 1.00 19.22  ? 2241 LEU A CD2   1 
ATOM   7218  N N     . GLU A 1 2242 ? 167.481 212.471 177.937 1.00 25.08  ? 2242 GLU A N     1 
ATOM   7219  C CA    . GLU A 1 2242 ? 167.052 213.626 177.156 1.00 25.08  ? 2242 GLU A CA    1 
ATOM   7220  C C     . GLU A 1 2242 ? 166.898 214.861 178.034 1.00 25.08  ? 2242 GLU A C     1 
ATOM   7221  O O     . GLU A 1 2242 ? 167.313 215.961 177.650 1.00 25.08  ? 2242 GLU A O     1 
ATOM   7222  C CB    . GLU A 1 2242 ? 165.741 213.314 176.437 1.00 25.08  ? 2242 GLU A CB    1 
ATOM   7223  C CG    . GLU A 1 2242 ? 165.180 214.477 175.639 1.00 25.08  ? 2242 GLU A CG    1 
ATOM   7224  C CD    . GLU A 1 2242 ? 163.764 214.224 175.163 1.00 25.08  ? 2242 GLU A CD    1 
ATOM   7225  O OE1   . GLU A 1 2242 ? 163.533 213.186 174.509 1.00 25.08  ? 2242 GLU A OE1   1 
ATOM   7226  O OE2   . GLU A 1 2242 ? 162.883 215.062 175.444 1.00 25.08  ? 2242 GLU A OE2   1 
ATOM   7227  N N     . ARG A 1 2243 ? 166.303 214.702 179.217 1.00 23.41  ? 2243 ARG A N     1 
ATOM   7228  C CA    . ARG A 1 2243 ? 166.100 215.850 180.093 1.00 23.41  ? 2243 ARG A CA    1 
ATOM   7229  C C     . ARG A 1 2243 ? 167.387 216.296 180.778 1.00 23.41  ? 2243 ARG A C     1 
ATOM   7230  O O     . ARG A 1 2243 ? 167.534 217.481 181.094 1.00 23.41  ? 2243 ARG A O     1 
ATOM   7231  C CB    . ARG A 1 2243 ? 165.031 215.532 181.139 1.00 23.41  ? 2243 ARG A CB    1 
ATOM   7232  C CG    . ARG A 1 2243 ? 163.626 215.447 180.570 1.00 23.41  ? 2243 ARG A CG    1 
ATOM   7233  C CD    . ARG A 1 2243 ? 162.673 214.781 181.543 1.00 23.41  ? 2243 ARG A CD    1 
ATOM   7234  N NE    . ARG A 1 2243 ? 162.719 215.406 182.859 1.00 23.41  ? 2243 ARG A NE    1 
ATOM   7235  C CZ    . ARG A 1 2243 ? 161.668 215.926 183.477 1.00 23.41  ? 2243 ARG A CZ    1 
ATOM   7236  N NH1   . ARG A 1 2243 ? 160.466 215.911 182.926 1.00 23.41  ? 2243 ARG A NH1   1 
ATOM   7237  N NH2   . ARG A 1 2243 ? 161.828 216.475 184.678 1.00 23.41  ? 2243 ARG A NH2   1 
ATOM   7238  N N     . LEU A 1 2244 ? 168.320 215.375 181.016 1.00 25.36  ? 2244 LEU A N     1 
ATOM   7239  C CA    . LEU A 1 2244 ? 169.555 215.708 181.720 1.00 25.36  ? 2244 LEU A CA    1 
ATOM   7240  C C     . LEU A 1 2244 ? 170.603 216.282 180.773 1.00 25.36  ? 2244 LEU A C     1 
ATOM   7241  O O     . LEU A 1 2244 ? 171.049 217.422 180.938 1.00 25.36  ? 2244 LEU A O     1 
ATOM   7242  C CB    . LEU A 1 2244 ? 170.100 214.466 182.430 1.00 25.36  ? 2244 LEU A CB    1 
ATOM   7243  C CG    . LEU A 1 2244 ? 171.420 214.627 183.184 1.00 25.36  ? 2244 LEU A CG    1 
ATOM   7244  C CD1   . LEU A 1 2244 ? 171.176 215.169 184.582 1.00 25.36  ? 2244 LEU A CD1   1 
ATOM   7245  C CD2   . LEU A 1 2244 ? 172.170 213.306 183.237 1.00 25.36  ? 2244 LEU A CD2   1 
ATOM   7246  N N     . GLU A 1 2245 ? 171.007 215.501 179.772 1.00 29.24  ? 2245 GLU A N     1 
ATOM   7247  C CA    . GLU A 1 2245 ? 172.064 215.912 178.859 1.00 29.24  ? 2245 GLU A CA    1 
ATOM   7248  C C     . GLU A 1 2245 ? 171.588 216.888 177.792 1.00 29.24  ? 2245 GLU A C     1 
ATOM   7249  O O     . GLU A 1 2245 ? 172.422 217.427 177.057 1.00 29.24  ? 2245 GLU A O     1 
ATOM   7250  C CB    . GLU A 1 2245 ? 172.682 214.685 178.185 1.00 29.24  ? 2245 GLU A CB    1 
ATOM   7251  C CG    . GLU A 1 2245 ? 173.347 213.718 179.149 1.00 29.24  ? 2245 GLU A CG    1 
ATOM   7252  C CD    . GLU A 1 2245 ? 173.986 212.538 178.443 1.00 29.24  ? 2245 GLU A CD    1 
ATOM   7253  O OE1   . GLU A 1 2245 ? 173.806 212.410 177.215 1.00 29.24  ? 2245 GLU A OE1   1 
ATOM   7254  O OE2   . GLU A 1 2245 ? 174.668 211.738 179.117 1.00 29.24  ? 2245 GLU A OE2   1 
ATOM   7255  N N     . GLY A 1 2246 ? 170.284 217.123 177.684 1.00 31.13  ? 2246 GLY A N     1 
ATOM   7256  C CA    . GLY A 1 2246 ? 169.767 218.011 176.665 1.00 31.13  ? 2246 GLY A CA    1 
ATOM   7257  C C     . GLY A 1 2246 ? 169.793 217.452 175.262 1.00 31.13  ? 2246 GLY A C     1 
ATOM   7258  O O     . GLY A 1 2246 ? 169.609 218.213 174.306 1.00 31.13  ? 2246 GLY A O     1 
ATOM   7259  N N     . VAL A 1 2247 ? 170.015 216.151 175.107 1.00 34.33  ? 2247 VAL A N     1 
ATOM   7260  C CA    . VAL A 1 2247 ? 170.100 215.503 173.804 1.00 34.33  ? 2247 VAL A CA    1 
ATOM   7261  C C     . VAL A 1 2247 ? 168.810 214.728 173.581 1.00 34.33  ? 2247 VAL A C     1 
ATOM   7262  O O     . VAL A 1 2247 ? 168.495 213.802 174.338 1.00 34.33  ? 2247 VAL A O     1 
ATOM   7263  C CB    . VAL A 1 2247 ? 171.322 214.577 173.714 1.00 34.33  ? 2247 VAL A CB    1 
ATOM   7264  C CG1   . VAL A 1 2247 ? 171.317 213.819 172.402 1.00 34.33  ? 2247 VAL A CG1   1 
ATOM   7265  C CG2   . VAL A 1 2247 ? 172.604 215.377 173.869 1.00 34.33  ? 2247 VAL A CG2   1 
ATOM   7266  N N     . GLU A 1 2248 ? 168.067 215.104 172.542 1.00 38.79  ? 2248 GLU A N     1 
ATOM   7267  C CA    . GLU A 1 2248 ? 166.798 214.449 172.254 1.00 38.79  ? 2248 GLU A CA    1 
ATOM   7268  C C     . GLU A 1 2248 ? 167.019 212.979 171.920 1.00 38.79  ? 2248 GLU A C     1 
ATOM   7269  O O     . GLU A 1 2248 ? 167.923 212.627 171.158 1.00 38.79  ? 2248 GLU A O     1 
ATOM   7270  C CB    . GLU A 1 2248 ? 166.090 215.157 171.099 1.00 38.79  ? 2248 GLU A CB    1 
ATOM   7271  C CG    . GLU A 1 2248 ? 165.041 214.313 170.396 1.00 38.79  ? 2248 GLU A CG    1 
ATOM   7272  C CD    . GLU A 1 2248 ? 163.966 215.152 169.735 1.00 38.79  ? 2248 GLU A CD    1 
ATOM   7273  O OE1   . GLU A 1 2248 ? 164.274 216.282 169.303 1.00 38.79  ? 2248 GLU A OE1   1 
ATOM   7274  O OE2   . GLU A 1 2248 ? 162.812 214.680 169.646 1.00 38.79  ? 2248 GLU A OE2   1 
ATOM   7275  N N     . GLY A 1 2249 ? 166.189 212.118 172.500 1.00 29.34  ? 2249 GLY A N     1 
ATOM   7276  C CA    . GLY A 1 2249 ? 166.288 210.683 172.308 1.00 29.34  ? 2249 GLY A CA    1 
ATOM   7277  C C     . GLY A 1 2249 ? 165.162 210.175 171.423 1.00 29.34  ? 2249 GLY A C     1 
ATOM   7278  O O     . GLY A 1 2249 ? 163.989 210.457 171.672 1.00 29.34  ? 2249 GLY A O     1 
ATOM   7279  N N     . VAL A 1 2250 ? 165.540 209.425 170.392 1.00 23.27  ? 2250 VAL A N     1 
ATOM   7280  C CA    . VAL A 1 2250 ? 164.600 208.801 169.470 1.00 23.27  ? 2250 VAL A CA    1 
ATOM   7281  C C     . VAL A 1 2250 ? 164.862 207.303 169.473 1.00 23.27  ? 2250 VAL A C     1 
ATOM   7282  O O     . VAL A 1 2250 ? 166.006 206.870 169.297 1.00 23.27  ? 2250 VAL A O     1 
ATOM   7283  C CB    . VAL A 1 2250 ? 164.727 209.376 168.049 1.00 23.27  ? 2250 VAL A CB    1 
ATOM   7284  C CG1   . VAL A 1 2250 ? 163.809 208.632 167.093 1.00 23.27  ? 2250 VAL A CG1   1 
ATOM   7285  C CG2   . VAL A 1 2250 ? 164.409 210.863 168.050 1.00 23.27  ? 2250 VAL A CG2   1 
ATOM   7286  N N     . ALA A 1 2251 ? 163.808 206.517 169.670 1.00 19.80  ? 2251 ALA A N     1 
ATOM   7287  C CA    . ALA A 1 2251 ? 163.916 205.070 169.774 1.00 19.80  ? 2251 ALA A CA    1 
ATOM   7288  C C     . ALA A 1 2251 ? 163.115 204.410 168.663 1.00 19.80  ? 2251 ALA A C     1 
ATOM   7289  O O     . ALA A 1 2251 ? 161.927 204.699 168.493 1.00 19.80  ? 2251 ALA A O     1 
ATOM   7290  C CB    . ALA A 1 2251 ? 163.424 204.582 171.136 1.00 19.80  ? 2251 ALA A CB    1 
ATOM   7291  N N     . HIS A 1 2252 ? 163.766 203.521 167.918 1.00 22.02  ? 2252 HIS A N     1 
ATOM   7292  C CA    . HIS A 1 2252 ? 163.127 202.750 166.858 1.00 22.02  ? 2252 HIS A CA    1 
ATOM   7293  C C     . HIS A 1 2252 ? 162.972 201.317 167.347 1.00 22.02  ? 2252 HIS A C     1 
ATOM   7294  O O     . HIS A 1 2252 ? 163.946 200.558 167.382 1.00 22.02  ? 2252 HIS A O     1 
ATOM   7295  C CB    . HIS A 1 2252 ? 163.944 202.804 165.569 1.00 22.02  ? 2252 HIS A CB    1 
ATOM   7296  C CG    . HIS A 1 2252 ? 164.399 204.180 165.199 1.00 22.02  ? 2252 HIS A CG    1 
ATOM   7297  N ND1   . HIS A 1 2252 ? 163.541 205.140 164.710 1.00 22.02  ? 2252 HIS A ND1   1 
ATOM   7298  C CD2   . HIS A 1 2252 ? 165.623 204.756 165.244 1.00 22.02  ? 2252 HIS A CD2   1 
ATOM   7299  C CE1   . HIS A 1 2252 ? 164.216 206.250 164.471 1.00 22.02  ? 2252 HIS A CE1   1 
ATOM   7300  N NE2   . HIS A 1 2252 ? 165.482 206.044 164.787 1.00 22.02  ? 2252 HIS A NE2   1 
ATOM   7301  N N     . ILE A 1 2253 ? 161.751 200.948 167.721 1.00 21.68  ? 2253 ILE A N     1 
ATOM   7302  C CA    . ILE A 1 2253 ? 161.464 199.612 168.228 1.00 21.68  ? 2253 ILE A CA    1 
ATOM   7303  C C     . ILE A 1 2253 ? 161.139 198.722 167.035 1.00 21.68  ? 2253 ILE A C     1 
ATOM   7304  O O     . ILE A 1 2253 ? 160.160 198.953 166.323 1.00 21.68  ? 2253 ILE A O     1 
ATOM   7305  C CB    . ILE A 1 2253 ? 160.317 199.632 169.244 1.00 21.68  ? 2253 ILE A CB    1 
ATOM   7306  C CG1   . ILE A 1 2253 ? 160.468 200.830 170.181 1.00 21.68  ? 2253 ILE A CG1   1 
ATOM   7307  C CG2   . ILE A 1 2253 ? 160.294 198.341 170.038 1.00 21.68  ? 2253 ILE A CG2   1 
ATOM   7308  C CD1   . ILE A 1 2253 ? 159.333 200.985 171.163 1.00 21.68  ? 2253 ILE A CD1   1 
ATOM   7309  N N     . ILE A 1 2254 ? 161.964 197.702 166.818 1.00 23.67  ? 2254 ILE A N     1 
ATOM   7310  C CA    . ILE A 1 2254 ? 161.857 196.819 165.664 1.00 23.67  ? 2254 ILE A CA    1 
ATOM   7311  C C     . ILE A 1 2254 ? 161.630 195.399 166.157 1.00 23.67  ? 2254 ILE A C     1 
ATOM   7312  O O     . ILE A 1 2254 ? 162.387 194.899 166.997 1.00 23.67  ? 2254 ILE A O     1 
ATOM   7313  C CB    . ILE A 1 2254 ? 163.116 196.895 164.783 1.00 23.67  ? 2254 ILE A CB    1 
ATOM   7314  C CG1   . ILE A 1 2254 ? 163.264 198.292 164.181 1.00 23.67  ? 2254 ILE A CG1   1 
ATOM   7315  C CG2   . ILE A 1 2254 ? 163.072 195.839 163.693 1.00 23.67  ? 2254 ILE A CG2   1 
ATOM   7316  C CD1   . ILE A 1 2254 ? 164.567 198.500 163.450 1.00 23.67  ? 2254 ILE A CD1   1 
ATOM   7317  N N     . ASP A 1 2255 ? 160.590 194.749 165.636 1.00 29.21  ? 2255 ASP A N     1 
ATOM   7318  C CA    . ASP A 1 2255 ? 160.354 193.342 165.921 1.00 29.21  ? 2255 ASP A CA    1 
ATOM   7319  C C     . ASP A 1 2255 ? 160.990 192.516 164.812 1.00 29.21  ? 2255 ASP A C     1 
ATOM   7320  O O     . ASP A 1 2255 ? 160.542 192.603 163.659 1.00 29.21  ? 2255 ASP A O     1 
ATOM   7321  C CB    . ASP A 1 2255 ? 158.864 193.051 166.018 1.00 29.21  ? 2255 ASP A CB    1 
ATOM   7322  C CG    . ASP A 1 2255 ? 158.566 191.810 166.835 1.00 29.21  ? 2255 ASP A CG    1 
ATOM   7323  O OD1   . ASP A 1 2255 ? 159.045 190.720 166.458 1.00 29.21  ? 2255 ASP A OD1   1 
ATOM   7324  O OD2   . ASP A 1 2255 ? 157.853 191.923 167.853 1.00 29.21  ? 2255 ASP A OD2   1 
ATOM   7325  N N     . PRO A 1 2256 ? 162.018 191.716 165.099 1.00 31.44  ? 2256 PRO A N     1 
ATOM   7326  C CA    . PRO A 1 2256 ? 162.702 191.007 164.007 1.00 31.44  ? 2256 PRO A CA    1 
ATOM   7327  C C     . PRO A 1 2256 ? 161.911 189.833 163.465 1.00 31.44  ? 2256 PRO A C     1 
ATOM   7328  O O     . PRO A 1 2256 ? 161.976 189.552 162.263 1.00 31.44  ? 2256 PRO A O     1 
ATOM   7329  C CB    . PRO A 1 2256 ? 164.013 190.559 164.661 1.00 31.44  ? 2256 PRO A CB    1 
ATOM   7330  C CG    . PRO A 1 2256 ? 163.655 190.386 166.096 1.00 31.44  ? 2256 PRO A CG    1 
ATOM   7331  C CD    . PRO A 1 2256 ? 162.634 191.446 166.408 1.00 31.44  ? 2256 PRO A CD    1 
ATOM   7332  N N     . LYS A 1 2257 ? 161.166 189.131 164.319 1.00 32.40  ? 2257 LYS A N     1 
ATOM   7333  C CA    . LYS A 1 2257 ? 160.425 187.959 163.875 1.00 32.40  ? 2257 LYS A CA    1 
ATOM   7334  C C     . LYS A 1 2257 ? 159.155 188.309 163.116 1.00 32.40  ? 2257 LYS A C     1 
ATOM   7335  O O     . LYS A 1 2257 ? 158.635 187.452 162.396 1.00 32.40  ? 2257 LYS A O     1 
ATOM   7336  C CB    . LYS A 1 2257 ? 160.087 187.072 165.073 1.00 32.40  ? 2257 LYS A CB    1 
ATOM   7337  C CG    . LYS A 1 2257 ? 161.300 186.689 165.895 1.00 32.40  ? 2257 LYS A CG    1 
ATOM   7338  C CD    . LYS A 1 2257 ? 162.373 186.110 164.997 1.00 32.40  ? 2257 LYS A CD    1 
ATOM   7339  C CE    . LYS A 1 2257 ? 162.073 184.666 164.657 1.00 32.40  ? 2257 LYS A CE    1 
ATOM   7340  N NZ    . LYS A 1 2257 ? 162.601 183.754 165.707 1.00 32.40  ? 2257 LYS A NZ    1 
ATOM   7341  N N     . ALA A 1 2258 ? 158.647 189.536 163.252 1.00 33.71  ? 2258 ALA A N     1 
ATOM   7342  C CA    . ALA A 1 2258 ? 157.428 189.911 162.544 1.00 33.71  ? 2258 ALA A CA    1 
ATOM   7343  C C     . ALA A 1 2258 ? 157.645 189.928 161.037 1.00 33.71  ? 2258 ALA A C     1 
ATOM   7344  O O     . ALA A 1 2258 ? 156.729 189.620 160.266 1.00 33.71  ? 2258 ALA A O     1 
ATOM   7345  C CB    . ALA A 1 2258 ? 156.938 191.274 163.032 1.00 33.71  ? 2258 ALA A CB    1 
ATOM   7346  N N     . ILE A 1 2259 ? 158.848 190.283 160.598 1.00 40.86  ? 2259 ILE A N     1 
ATOM   7347  C CA    . ILE A 1 2259 ? 159.168 190.372 159.183 1.00 40.86  ? 2259 ILE A CA    1 
ATOM   7348  C C     . ILE A 1 2259 ? 160.275 189.373 158.858 1.00 40.86  ? 2259 ILE A C     1 
ATOM   7349  O O     . ILE A 1 2259 ? 161.001 188.903 159.734 1.00 40.86  ? 2259 ILE A O     1 
ATOM   7350  C CB    . ILE A 1 2259 ? 159.572 191.800 158.774 1.00 40.86  ? 2259 ILE A CB    1 
ATOM   7351  C CG1   . ILE A 1 2259 ? 160.780 192.261 159.589 1.00 40.86  ? 2259 ILE A CG1   1 
ATOM   7352  C CG2   . ILE A 1 2259 ? 158.405 192.755 158.958 1.00 40.86  ? 2259 ILE A CG2   1 
ATOM   7353  C CD1   . ILE A 1 2259 ? 161.166 193.700 159.345 1.00 40.86  ? 2259 ILE A CD1   1 
ATOM   7354  N N     . SER A 1 2260 ? 160.397 189.049 157.574 1.00 50.47  ? 2260 SER A N     1 
ATOM   7355  C CA    . SER A 1 2260 ? 161.406 188.101 157.131 1.00 50.47  ? 2260 SER A CA    1 
ATOM   7356  C C     . SER A 1 2260 ? 162.790 188.749 157.139 1.00 50.47  ? 2260 SER A C     1 
ATOM   7357  O O     . SER A 1 2260 ? 162.939 189.970 157.238 1.00 50.47  ? 2260 SER A O     1 
ATOM   7358  C CB    . SER A 1 2260 ? 161.073 187.580 155.735 1.00 50.47  ? 2260 SER A CB    1 
ATOM   7359  O OG    . SER A 1 2260 ? 161.043 188.638 154.793 1.00 50.47  ? 2260 SER A OG    1 
ATOM   7360  N N     . LYS A 1 2261 ? 163.816 187.900 157.032 1.00 53.05  ? 2261 LYS A N     1 
ATOM   7361  C CA    . LYS A 1 2261 ? 165.189 188.394 156.989 1.00 53.05  ? 2261 LYS A CA    1 
ATOM   7362  C C     . LYS A 1 2261 ? 165.413 189.286 155.775 1.00 53.05  ? 2261 LYS A C     1 
ATOM   7363  O O     . LYS A 1 2261 ? 166.092 190.316 155.867 1.00 53.05  ? 2261 LYS A O     1 
ATOM   7364  C CB    . LYS A 1 2261 ? 166.166 187.219 156.981 1.00 53.05  ? 2261 LYS A CB    1 
ATOM   7365  C CG    . LYS A 1 2261 ? 167.626 187.610 157.132 1.00 53.05  ? 2261 LYS A CG    1 
ATOM   7366  C CD    . LYS A 1 2261 ? 168.524 186.386 157.048 1.00 53.05  ? 2261 LYS A CD    1 
ATOM   7367  C CE    . LYS A 1 2261 ? 169.991 186.770 156.963 1.00 53.05  ? 2261 LYS A CE    1 
ATOM   7368  N NZ    . LYS A 1 2261 ? 170.323 187.907 157.862 1.00 53.05  ? 2261 LYS A NZ    1 
ATOM   7369  N N     . ASP A 1 2262 ? 164.853 188.901 154.625 1.00 58.98  ? 2262 ASP A N     1 
ATOM   7370  C CA    . ASP A 1 2262 ? 164.977 189.726 153.428 1.00 58.98  ? 2262 ASP A CA    1 
ATOM   7371  C C     . ASP A 1 2262 ? 164.304 191.078 153.619 1.00 58.98  ? 2262 ASP A C     1 
ATOM   7372  O O     . ASP A 1 2262 ? 164.814 192.104 153.157 1.00 58.98  ? 2262 ASP A O     1 
ATOM   7373  C CB    . ASP A 1 2262 ? 164.386 188.994 152.224 1.00 58.98  ? 2262 ASP A CB    1 
ATOM   7374  C CG    . ASP A 1 2262 ? 165.168 187.748 151.859 1.00 58.98  ? 2262 ASP A CG    1 
ATOM   7375  O OD1   . ASP A 1 2262 ? 166.198 187.873 151.164 1.00 58.98  ? 2262 ASP A OD1   1 
ATOM   7376  O OD2   . ASP A 1 2262 ? 164.753 186.642 152.267 1.00 58.98  ? 2262 ASP A OD2   1 
ATOM   7377  N N     . HIS A 1 2263 ? 163.152 191.102 154.292 1.00 52.05  ? 2263 HIS A N     1 
ATOM   7378  C CA    . HIS A 1 2263 ? 162.505 192.376 154.581 1.00 52.05  ? 2263 HIS A CA    1 
ATOM   7379  C C     . HIS A 1 2263 ? 163.226 193.132 155.689 1.00 52.05  ? 2263 HIS A C     1 
ATOM   7380  O O     . HIS A 1 2263 ? 163.164 194.366 155.736 1.00 52.05  ? 2263 HIS A O     1 
ATOM   7381  C CB    . HIS A 1 2263 ? 161.042 192.152 154.958 1.00 52.05  ? 2263 HIS A CB    1 
ATOM   7382  C CG    . HIS A 1 2263 ? 160.141 191.941 153.782 1.00 52.05  ? 2263 HIS A CG    1 
ATOM   7383  N ND1   . HIS A 1 2263 ? 158.943 191.267 153.873 1.00 52.05  ? 2263 HIS A ND1   1 
ATOM   7384  C CD2   . HIS A 1 2263 ? 160.262 192.320 152.488 1.00 52.05  ? 2263 HIS A CD2   1 
ATOM   7385  C CE1   . HIS A 1 2263 ? 158.365 191.238 152.685 1.00 52.05  ? 2263 HIS A CE1   1 
ATOM   7386  N NE2   . HIS A 1 2263 ? 159.145 191.870 151.827 1.00 52.05  ? 2263 HIS A NE2   1 
ATOM   7387  N N     . LEU A 1 2264 ? 163.908 192.417 156.584 1.00 48.75  ? 2264 LEU A N     1 
ATOM   7388  C CA    . LEU A 1 2264 ? 164.590 193.075 157.693 1.00 48.75  ? 2264 LEU A CA    1 
ATOM   7389  C C     . LEU A 1 2264 ? 165.856 193.781 157.224 1.00 48.75  ? 2264 LEU A C     1 
ATOM   7390  O O     . LEU A 1 2264 ? 166.151 194.901 157.658 1.00 48.75  ? 2264 LEU A O     1 
ATOM   7391  C CB    . LEU A 1 2264 ? 164.912 192.056 158.786 1.00 48.75  ? 2264 LEU A CB    1 
ATOM   7392  C CG    . LEU A 1 2264 ? 165.755 192.552 159.962 1.00 48.75  ? 2264 LEU A CG    1 
ATOM   7393  C CD1   . LEU A 1 2264 ? 165.021 193.640 160.726 1.00 48.75  ? 2264 LEU A CD1   1 
ATOM   7394  C CD2   . LEU A 1 2264 ? 166.115 191.398 160.883 1.00 48.75  ? 2264 LEU A CD2   1 
ATOM   7395  N N     . TYR A 1 2265 ? 166.618 193.144 156.336 1.00 52.07  ? 2265 TYR A N     1 
ATOM   7396  C CA    . TYR A 1 2265 ? 167.895 193.688 155.891 1.00 52.07  ? 2265 TYR A CA    1 
ATOM   7397  C C     . TYR A 1 2265 ? 167.871 194.215 154.465 1.00 52.07  ? 2265 TYR A C     1 
ATOM   7398  O O     . TYR A 1 2265 ? 168.709 195.050 154.113 1.00 52.07  ? 2265 TYR A O     1 
ATOM   7399  C CB    . TYR A 1 2265 ? 168.992 192.624 156.006 1.00 52.07  ? 2265 TYR A CB    1 
ATOM   7400  C CG    . TYR A 1 2265 ? 169.443 192.369 157.423 1.00 52.07  ? 2265 TYR A CG    1 
ATOM   7401  C CD1   . TYR A 1 2265 ? 169.682 191.080 157.873 1.00 52.07  ? 2265 TYR A CD1   1 
ATOM   7402  C CD2   . TYR A 1 2265 ? 169.627 193.418 158.313 1.00 52.07  ? 2265 TYR A CD2   1 
ATOM   7403  C CE1   . TYR A 1 2265 ? 170.092 190.840 159.169 1.00 52.07  ? 2265 TYR A CE1   1 
ATOM   7404  C CE2   . TYR A 1 2265 ? 170.038 193.188 159.611 1.00 52.07  ? 2265 TYR A CE2   1 
ATOM   7405  C CZ    . TYR A 1 2265 ? 170.269 191.897 160.032 1.00 52.07  ? 2265 TYR A CZ    1 
ATOM   7406  O OH    . TYR A 1 2265 ? 170.678 191.660 161.323 1.00 52.07  ? 2265 TYR A OH    1 
ATOM   7407  N N     . GLY A 1 2266 ? 166.940 193.757 153.636 1.00 61.78  ? 2266 GLY A N     1 
ATOM   7408  C CA    . GLY A 1 2266 ? 166.916 194.165 152.246 1.00 61.78  ? 2266 GLY A CA    1 
ATOM   7409  C C     . GLY A 1 2266 ? 167.195 193.008 151.312 1.00 61.78  ? 2266 GLY A C     1 
ATOM   7410  O O     . GLY A 1 2266 ? 167.738 191.983 151.734 1.00 61.78  ? 2266 GLY A O     1 
ATOM   7411  N N     . THR A 1 2267 ? 166.833 193.156 150.041 1.00 72.79  ? 2267 THR A N     1 
ATOM   7412  C CA    . THR A 1 2267 ? 167.021 192.094 149.066 1.00 72.79  ? 2267 THR A CA    1 
ATOM   7413  C C     . THR A 1 2267 ? 167.703 192.652 147.827 1.00 72.79  ? 2267 THR A C     1 
ATOM   7414  O O     . THR A 1 2267 ? 167.500 193.810 147.451 1.00 72.79  ? 2267 THR A O     1 
ATOM   7415  C CB    . THR A 1 2267 ? 165.690 191.433 148.677 1.00 72.79  ? 2267 THR A CB    1 
ATOM   7416  O OG1   . THR A 1 2267 ? 165.912 190.489 147.623 1.00 72.79  ? 2267 THR A OG1   1 
ATOM   7417  C CG2   . THR A 1 2267 ? 164.685 192.477 148.215 1.00 72.79  ? 2267 THR A CG2   1 
ATOM   7418  N N     . LEU A 1 2268 ? 168.521 191.813 147.203 1.00 80.21  ? 2268 LEU A N     1 
ATOM   7419  C CA    . LEU A 1 2268 ? 169.195 192.146 145.957 1.00 80.21  ? 2268 LEU A CA    1 
ATOM   7420  C C     . LEU A 1 2268 ? 168.481 191.441 144.812 1.00 80.21  ? 2268 LEU A C     1 
ATOM   7421  O O     . LEU A 1 2268 ? 168.291 190.221 144.852 1.00 80.21  ? 2268 LEU A O     1 
ATOM   7422  C CB    . LEU A 1 2268 ? 170.667 191.735 146.007 1.00 80.21  ? 2268 LEU A CB    1 
ATOM   7423  C CG    . LEU A 1 2268 ? 171.524 192.067 144.785 1.00 80.21  ? 2268 LEU A CG    1 
ATOM   7424  C CD1   . LEU A 1 2268 ? 171.592 193.570 144.572 1.00 80.21  ? 2268 LEU A CD1   1 
ATOM   7425  C CD2   . LEU A 1 2268 ? 172.917 191.481 144.942 1.00 80.21  ? 2268 LEU A CD2   1 
ATOM   7426  N N     . ASP A 1 2269 ? 168.082 192.209 143.805 1.00 88.27  ? 2269 ASP A N     1 
ATOM   7427  C CA    . ASP A 1 2269 ? 167.302 191.650 142.708 1.00 88.27  ? 2269 ASP A CA    1 
ATOM   7428  C C     . ASP A 1 2269 ? 168.131 190.621 141.947 1.00 88.27  ? 2269 ASP A C     1 
ATOM   7429  O O     . ASP A 1 2269 ? 169.263 190.918 141.546 1.00 88.27  ? 2269 ASP A O     1 
ATOM   7430  C CB    . ASP A 1 2269 ? 166.833 192.758 141.770 1.00 88.27  ? 2269 ASP A CB    1 
ATOM   7431  C CG    . ASP A 1 2269 ? 165.749 193.619 142.387 1.00 88.27  ? 2269 ASP A CG    1 
ATOM   7432  O OD1   . ASP A 1 2269 ? 164.990 193.102 143.233 1.00 88.27  ? 2269 ASP A OD1   1 
ATOM   7433  O OD2   . ASP A 1 2269 ? 165.655 194.810 142.026 1.00 88.27  ? 2269 ASP A OD2   1 
ATOM   7434  N N     . PRO A 1 2270 ? 167.614 189.407 141.740 1.00 91.76  ? 2270 PRO A N     1 
ATOM   7435  C CA    . PRO A 1 2270 ? 168.422 188.364 141.084 1.00 91.76  ? 2270 PRO A CA    1 
ATOM   7436  C C     . PRO A 1 2270 ? 168.873 188.728 139.681 1.00 91.76  ? 2270 PRO A C     1 
ATOM   7437  O O     . PRO A 1 2270 ? 169.980 188.346 139.280 1.00 91.76  ? 2270 PRO A O     1 
ATOM   7438  C CB    . PRO A 1 2270 ? 167.482 187.150 141.075 1.00 91.76  ? 2270 PRO A CB    1 
ATOM   7439  C CG    . PRO A 1 2270 ? 166.486 187.423 142.159 1.00 91.76  ? 2270 PRO A CG    1 
ATOM   7440  C CD    . PRO A 1 2270 ? 166.296 188.907 142.163 1.00 91.76  ? 2270 PRO A CD    1 
ATOM   7441  N N     . ASN A 1 2271 ? 168.056 189.454 138.919 1.00 95.07  ? 2271 ASN A N     1 
ATOM   7442  C CA    . ASN A 1 2271 ? 168.391 189.816 137.547 1.00 95.07  ? 2271 ASN A CA    1 
ATOM   7443  C C     . ASN A 1 2271 ? 168.763 191.287 137.403 1.00 95.07  ? 2271 ASN A C     1 
ATOM   7444  O O     . ASN A 1 2271 ? 169.786 191.610 136.793 1.00 95.07  ? 2271 ASN A O     1 
ATOM   7445  C CB    . ASN A 1 2271 ? 167.222 189.477 136.613 1.00 95.07  ? 2271 ASN A CB    1 
ATOM   7446  C CG    . ASN A 1 2271 ? 165.899 190.032 137.107 1.00 95.07  ? 2271 ASN A CG    1 
ATOM   7447  O OD1   . ASN A 1 2271 ? 165.738 191.243 137.260 1.00 95.07  ? 2271 ASN A OD1   1 
ATOM   7448  N ND2   . ASN A 1 2271 ? 164.943 189.145 137.356 1.00 95.07  ? 2271 ASN A ND2   1 
ATOM   7449  N N     . THR A 1 2272 ? 167.947 192.187 137.954 1.00 92.29  ? 2272 THR A N     1 
ATOM   7450  C CA    . THR A 1 2272 ? 168.208 193.615 137.828 1.00 92.29  ? 2272 THR A CA    1 
ATOM   7451  C C     . THR A 1 2272 ? 169.448 194.042 138.607 1.00 92.29  ? 2272 THR A C     1 
ATOM   7452  O O     . THR A 1 2272 ? 170.065 195.055 138.259 1.00 92.29  ? 2272 THR A O     1 
ATOM   7453  C CB    . THR A 1 2272 ? 166.977 194.401 138.295 1.00 92.29  ? 2272 THR A CB    1 
ATOM   7454  O OG1   . THR A 1 2272 ? 165.846 194.026 137.499 1.00 92.29  ? 2272 THR A OG1   1 
ATOM   7455  C CG2   . THR A 1 2272 ? 167.187 195.902 138.148 1.00 92.29  ? 2272 THR A CG2   1 
ATOM   7456  N N     . ARG A 1 2273 ? 169.846 193.270 139.620 1.00 87.25  ? 2273 ARG A N     1 
ATOM   7457  C CA    . ARG A 1 2273 ? 170.963 193.629 140.495 1.00 87.25  ? 2273 ARG A CA    1 
ATOM   7458  C C     . ARG A 1 2273 ? 170.728 195.003 141.120 1.00 87.25  ? 2273 ARG A C     1 
ATOM   7459  O O     . ARG A 1 2273 ? 171.634 195.832 141.231 1.00 87.25  ? 2273 ARG A O     1 
ATOM   7460  C CB    . ARG A 1 2273 ? 172.297 193.571 139.741 1.00 87.25  ? 2273 ARG A CB    1 
ATOM   7461  C CG    . ARG A 1 2273 ? 173.538 193.552 140.628 1.00 87.25  ? 2273 ARG A CG    1 
ATOM   7462  C CD    . ARG A 1 2273 ? 173.655 192.247 141.395 1.00 87.25  ? 2273 ARG A CD    1 
ATOM   7463  N NE    . ARG A 1 2273 ? 173.781 191.099 140.506 1.00 87.25  ? 2273 ARG A NE    1 
ATOM   7464  C CZ    . ARG A 1 2273 ? 172.858 190.157 140.362 1.00 87.25  ? 2273 ARG A CZ    1 
ATOM   7465  N NH1   . ARG A 1 2273 ? 171.717 190.200 141.031 1.00 87.25  ? 2273 ARG A NH1   1 
ATOM   7466  N NH2   . ARG A 1 2273 ? 173.085 189.148 139.526 1.00 87.25  ? 2273 ARG A NH2   1 
ATOM   7467  N N     . GLU A 1 2274 ? 169.484 195.250 141.517 1.00 82.66  ? 2274 GLU A N     1 
ATOM   7468  C CA    . GLU A 1 2274 ? 169.099 196.480 142.193 1.00 82.66  ? 2274 GLU A CA    1 
ATOM   7469  C C     . GLU A 1 2274 ? 168.821 196.173 143.657 1.00 82.66  ? 2274 GLU A C     1 
ATOM   7470  O O     . GLU A 1 2274 ? 168.089 195.227 143.970 1.00 82.66  ? 2274 GLU A O     1 
ATOM   7471  C CB    . GLU A 1 2274 ? 167.869 197.107 141.535 1.00 82.66  ? 2274 GLU A CB    1 
ATOM   7472  C CG    . GLU A 1 2274 ? 167.671 198.579 141.857 1.00 82.66  ? 2274 GLU A CG    1 
ATOM   7473  C CD    . GLU A 1 2274 ? 166.911 198.794 143.151 1.00 82.66  ? 2274 GLU A CD    1 
ATOM   7474  O OE1   . GLU A 1 2274 ? 166.190 197.868 143.578 1.00 82.66  ? 2274 GLU A OE1   1 
ATOM   7475  O OE2   . GLU A 1 2274 ? 167.035 199.888 143.741 1.00 82.66  ? 2274 GLU A OE2   1 
ATOM   7476  N N     . TRP A 1 2275 ? 169.404 196.968 144.547 1.00 71.50  ? 2275 TRP A N     1 
ATOM   7477  C CA    . TRP A 1 2275 ? 169.308 196.743 145.982 1.00 71.50  ? 2275 TRP A CA    1 
ATOM   7478  C C     . TRP A 1 2275 ? 168.280 197.694 146.582 1.00 71.50  ? 2275 TRP A C     1 
ATOM   7479  O O     . TRP A 1 2275 ? 168.376 198.913 146.402 1.00 71.50  ? 2275 TRP A O     1 
ATOM   7480  C CB    . TRP A 1 2275 ? 170.666 196.935 146.654 1.00 71.50  ? 2275 TRP A CB    1 
ATOM   7481  C CG    . TRP A 1 2275 ? 170.594 196.965 148.148 1.00 71.50  ? 2275 TRP A CG    1 
ATOM   7482  C CD1   . TRP A 1 2275 ? 170.580 198.072 148.945 1.00 71.50  ? 2275 TRP A CD1   1 
ATOM   7483  C CD2   . TRP A 1 2275 ? 170.526 195.837 149.027 1.00 71.50  ? 2275 TRP A CD2   1 
ATOM   7484  N NE1   . TRP A 1 2275 ? 170.508 197.704 150.266 1.00 71.50  ? 2275 TRP A NE1   1 
ATOM   7485  C CE2   . TRP A 1 2275 ? 170.473 196.336 150.343 1.00 71.50  ? 2275 TRP A CE2   1 
ATOM   7486  C CE3   . TRP A 1 2275 ? 170.505 194.453 148.829 1.00 71.50  ? 2275 TRP A CE3   1 
ATOM   7487  C CZ2   . TRP A 1 2275 ? 170.401 195.501 151.454 1.00 71.50  ? 2275 TRP A CZ2   1 
ATOM   7488  C CZ3   . TRP A 1 2275 ? 170.433 193.627 149.934 1.00 71.50  ? 2275 TRP A CZ3   1 
ATOM   7489  C CH2   . TRP A 1 2275 ? 170.382 194.153 151.230 1.00 71.50  ? 2275 TRP A CH2   1 
ATOM   7490  N N     . THR A 1 2276 ? 167.303 197.135 147.289 1.00 68.19  ? 2276 THR A N     1 
ATOM   7491  C CA    . THR A 1 2276 ? 166.358 197.905 148.086 1.00 68.19  ? 2276 THR A CA    1 
ATOM   7492  C C     . THR A 1 2276 ? 166.598 197.581 149.556 1.00 68.19  ? 2276 THR A C     1 
ATOM   7493  O O     . THR A 1 2276 ? 166.686 196.407 149.933 1.00 68.19  ? 2276 THR A O     1 
ATOM   7494  C CB    . THR A 1 2276 ? 164.912 197.617 147.670 1.00 68.19  ? 2276 THR A CB    1 
ATOM   7495  O OG1   . THR A 1 2276 ? 164.013 198.383 148.482 1.00 68.19  ? 2276 THR A OG1   1 
ATOM   7496  C CG2   . THR A 1 2276 ? 164.579 196.132 147.776 1.00 68.19  ? 2276 THR A CG2   1 
ATOM   7497  N N     . ASP A 1 2277 ? 166.740 198.619 150.372 1.00 56.02  ? 2277 ASP A N     1 
ATOM   7498  C CA    . ASP A 1 2277 ? 167.120 198.430 151.764 1.00 56.02  ? 2277 ASP A CA    1 
ATOM   7499  C C     . ASP A 1 2277 ? 165.960 197.880 152.587 1.00 56.02  ? 2277 ASP A C     1 
ATOM   7500  O O     . ASP A 1 2277 ? 164.788 198.160 152.323 1.00 56.02  ? 2277 ASP A O     1 
ATOM   7501  C CB    . ASP A 1 2277 ? 167.613 199.748 152.361 1.00 56.02  ? 2277 ASP A CB    1 
ATOM   7502  C CG    . ASP A 1 2277 ? 166.637 200.890 152.149 1.00 56.02  ? 2277 ASP A CG    1 
ATOM   7503  O OD1   . ASP A 1 2277 ? 165.618 200.687 151.456 1.00 56.02  ? 2277 ASP A OD1   1 
ATOM   7504  O OD2   . ASP A 1 2277 ? 166.891 201.994 152.674 1.00 56.02  ? 2277 ASP A OD2   1 
ATOM   7505  N N     . GLY A 1 2278 ? 166.303 197.082 153.594 1.00 50.00  ? 2278 GLY A N     1 
ATOM   7506  C CA    . GLY A 1 2278 ? 165.338 196.551 154.533 1.00 50.00  ? 2278 GLY A CA    1 
ATOM   7507  C C     . GLY A 1 2278 ? 165.075 197.522 155.662 1.00 50.00  ? 2278 GLY A C     1 
ATOM   7508  O O     . GLY A 1 2278 ? 165.567 198.652 155.672 1.00 50.00  ? 2278 GLY A O     1 
ATOM   7509  N N     . LEU A 1 2279 ? 164.291 197.064 156.640 1.00 43.61  ? 2279 LEU A N     1 
ATOM   7510  C CA    . LEU A 1 2279 ? 163.874 197.943 157.728 1.00 43.61  ? 2279 LEU A CA    1 
ATOM   7511  C C     . LEU A 1 2279 ? 165.071 198.433 158.535 1.00 43.61  ? 2279 LEU A C     1 
ATOM   7512  O O     . LEU A 1 2279 ? 165.264 199.641 158.718 1.00 43.61  ? 2279 LEU A O     1 
ATOM   7513  C CB    . LEU A 1 2279 ? 162.875 197.215 158.626 1.00 43.61  ? 2279 LEU A CB    1 
ATOM   7514  C CG    . LEU A 1 2279 ? 162.295 198.030 159.780 1.00 43.61  ? 2279 LEU A CG    1 
ATOM   7515  C CD1   . LEU A 1 2279 ? 161.502 199.212 159.251 1.00 43.61  ? 2279 LEU A CD1   1 
ATOM   7516  C CD2   . LEU A 1 2279 ? 161.426 197.150 160.659 1.00 43.61  ? 2279 LEU A CD2   1 
ATOM   7517  N N     . PHE A 1 2280 ? 165.903 197.503 159.011 1.00 42.60  ? 2280 PHE A N     1 
ATOM   7518  C CA    . PHE A 1 2280 ? 167.060 197.894 159.809 1.00 42.60  ? 2280 PHE A CA    1 
ATOM   7519  C C     . PHE A 1 2280 ? 168.055 198.694 158.979 1.00 42.60  ? 2280 PHE A C     1 
ATOM   7520  O O     . PHE A 1 2280 ? 168.607 199.696 159.450 1.00 42.60  ? 2280 PHE A O     1 
ATOM   7521  C CB    . PHE A 1 2280 ? 167.732 196.657 160.403 1.00 42.60  ? 2280 PHE A CB    1 
ATOM   7522  C CG    . PHE A 1 2280 ? 169.008 196.956 161.133 1.00 42.60  ? 2280 PHE A CG    1 
ATOM   7523  C CD1   . PHE A 1 2280 ? 169.006 197.772 162.251 1.00 42.60  ? 2280 PHE A CD1   1 
ATOM   7524  C CD2   . PHE A 1 2280 ? 170.210 196.425 160.701 1.00 42.60  ? 2280 PHE A CD2   1 
ATOM   7525  C CE1   . PHE A 1 2280 ? 170.177 198.051 162.924 1.00 42.60  ? 2280 PHE A CE1   1 
ATOM   7526  C CE2   . PHE A 1 2280 ? 171.384 196.701 161.371 1.00 42.60  ? 2280 PHE A CE2   1 
ATOM   7527  C CZ    . PHE A 1 2280 ? 171.368 197.515 162.484 1.00 42.60  ? 2280 PHE A CZ    1 
ATOM   7528  N N     . THR A 1 2281 ? 168.292 198.269 157.737 1.00 48.18  ? 2281 THR A N     1 
ATOM   7529  C CA    . THR A 1 2281 ? 169.237 198.981 156.886 1.00 48.18  ? 2281 THR A CA    1 
ATOM   7530  C C     . THR A 1 2281 ? 168.704 200.351 156.492 1.00 48.18  ? 2281 THR A C     1 
ATOM   7531  O O     . THR A 1 2281 ? 169.469 201.317 156.410 1.00 48.18  ? 2281 THR A O     1 
ATOM   7532  C CB    . THR A 1 2281 ? 169.565 198.147 155.651 1.00 48.18  ? 2281 THR A CB    1 
ATOM   7533  O OG1   . THR A 1 2281 ? 168.354 197.791 154.974 1.00 48.18  ? 2281 THR A OG1   1 
ATOM   7534  C CG2   . THR A 1 2281 ? 170.304 196.886 156.061 1.00 48.18  ? 2281 THR A CG2   1 
ATOM   7535  N N     . HIS A 1 2282 ? 167.395 200.462 156.246 1.00 46.90  ? 2282 HIS A N     1 
ATOM   7536  C CA    . HIS A 1 2282 ? 166.814 201.776 155.984 1.00 46.90  ? 2282 HIS A CA    1 
ATOM   7537  C C     . HIS A 1 2282 ? 166.966 202.690 157.190 1.00 46.90  ? 2282 HIS A C     1 
ATOM   7538  O O     . HIS A 1 2282 ? 167.299 203.872 157.043 1.00 46.90  ? 2282 HIS A O     1 
ATOM   7539  C CB    . HIS A 1 2282 ? 165.340 201.652 155.602 1.00 46.90  ? 2282 HIS A CB    1 
ATOM   7540  C CG    . HIS A 1 2282 ? 164.591 202.947 155.661 1.00 46.90  ? 2282 HIS A CG    1 
ATOM   7541  N ND1   . HIS A 1 2282 ? 164.846 203.995 154.803 1.00 46.90  ? 2282 HIS A ND1   1 
ATOM   7542  C CD2   . HIS A 1 2282 ? 163.597 203.366 156.479 1.00 46.90  ? 2282 HIS A CD2   1 
ATOM   7543  C CE1   . HIS A 1 2282 ? 164.040 205.001 155.087 1.00 46.90  ? 2282 HIS A CE1   1 
ATOM   7544  N NE2   . HIS A 1 2282 ? 163.271 204.645 156.101 1.00 46.90  ? 2282 HIS A NE2   1 
ATOM   7545  N N     . VAL A 1 2283 ? 166.728 202.160 158.392 1.00 44.92  ? 2283 VAL A N     1 
ATOM   7546  C CA    . VAL A 1 2283 ? 166.882 202.967 159.599 1.00 44.92  ? 2283 VAL A CA    1 
ATOM   7547  C C     . VAL A 1 2283 ? 168.322 203.445 159.736 1.00 44.92  ? 2283 VAL A C     1 
ATOM   7548  O O     . VAL A 1 2283 ? 168.583 204.628 159.988 1.00 44.92  ? 2283 VAL A O     1 
ATOM   7549  C CB    . VAL A 1 2283 ? 166.431 202.172 160.837 1.00 44.92  ? 2283 VAL A CB    1 
ATOM   7550  C CG1   . VAL A 1 2283 ? 166.941 202.831 162.107 1.00 44.92  ? 2283 VAL A CG1   1 
ATOM   7551  C CG2   . VAL A 1 2283 ? 164.917 202.053 160.867 1.00 44.92  ? 2283 VAL A CG2   1 
ATOM   7552  N N     . LEU A 1 2284 ? 169.280 202.533 159.552 1.00 47.06  ? 2284 LEU A N     1 
ATOM   7553  C CA    . LEU A 1 2284 ? 170.686 202.898 159.697 1.00 47.06  ? 2284 LEU A CA    1 
ATOM   7554  C C     . LEU A 1 2284 ? 171.110 203.914 158.643 1.00 47.06  ? 2284 LEU A C     1 
ATOM   7555  O O     . LEU A 1 2284 ? 171.825 204.876 158.952 1.00 47.06  ? 2284 LEU A O     1 
ATOM   7556  C CB    . LEU A 1 2284 ? 171.560 201.646 159.623 1.00 47.06  ? 2284 LEU A CB    1 
ATOM   7557  C CG    . LEU A 1 2284 ? 172.917 201.720 160.323 1.00 47.06  ? 2284 LEU A CG    1 
ATOM   7558  C CD1   . LEU A 1 2284 ? 172.766 202.287 161.723 1.00 47.06  ? 2284 LEU A CD1   1 
ATOM   7559  C CD2   . LEU A 1 2284 ? 173.563 200.347 160.370 1.00 47.06  ? 2284 LEU A CD2   1 
ATOM   7560  N N     . ARG A 1 2285 ? 170.674 203.727 157.396 1.00 50.52  ? 2285 ARG A N     1 
ATOM   7561  C CA    . ARG A 1 2285 ? 171.021 204.669 156.339 1.00 50.52  ? 2285 ARG A CA    1 
ATOM   7562  C C     . ARG A 1 2285 ? 170.416 206.040 156.603 1.00 50.52  ? 2285 ARG A C     1 
ATOM   7563  O O     . ARG A 1 2285 ? 171.068 207.065 156.373 1.00 50.52  ? 2285 ARG A O     1 
ATOM   7564  C CB    . ARG A 1 2285 ? 170.565 204.126 154.985 1.00 50.52  ? 2285 ARG A CB    1 
ATOM   7565  C CG    . ARG A 1 2285 ? 170.595 205.143 153.857 1.00 50.52  ? 2285 ARG A CG    1 
ATOM   7566  C CD    . ARG A 1 2285 ? 170.569 204.453 152.505 1.00 50.52  ? 2285 ARG A CD    1 
ATOM   7567  N NE    . ARG A 1 2285 ? 171.758 203.635 152.295 1.00 50.52  ? 2285 ARG A NE    1 
ATOM   7568  C CZ    . ARG A 1 2285 ? 171.737 202.337 152.025 1.00 50.52  ? 2285 ARG A CZ    1 
ATOM   7569  N NH1   . ARG A 1 2285 ? 170.598 201.673 151.915 1.00 50.52  ? 2285 ARG A NH1   1 
ATOM   7570  N NH2   . ARG A 1 2285 ? 172.887 201.690 151.862 1.00 50.52  ? 2285 ARG A NH2   1 
ATOM   7571  N N     . LYS A 1 2286 ? 169.172 206.084 157.085 1.00 49.27  ? 2286 LYS A N     1 
ATOM   7572  C CA    . LYS A 1 2286 ? 168.567 207.364 157.432 1.00 49.27  ? 2286 LYS A CA    1 
ATOM   7573  C C     . LYS A 1 2286 ? 169.336 208.044 158.554 1.00 49.27  ? 2286 LYS A C     1 
ATOM   7574  O O     . LYS A 1 2286 ? 169.564 209.258 158.513 1.00 49.27  ? 2286 LYS A O     1 
ATOM   7575  C CB    . LYS A 1 2286 ? 167.108 207.165 157.836 1.00 49.27  ? 2286 LYS A CB    1 
ATOM   7576  C CG    . LYS A 1 2286 ? 166.370 208.462 158.102 1.00 49.27  ? 2286 LYS A CG    1 
ATOM   7577  C CD    . LYS A 1 2286 ? 164.960 208.196 158.587 1.00 49.27  ? 2286 LYS A CD    1 
ATOM   7578  C CE    . LYS A 1 2286 ? 164.071 207.716 157.458 1.00 49.27  ? 2286 LYS A CE    1 
ATOM   7579  N NZ    . LYS A 1 2286 ? 162.662 207.572 157.909 1.00 49.27  ? 2286 LYS A NZ    1 
ATOM   7580  N N     . ILE A 1 2287 ? 169.763 207.274 159.556 1.00 47.41  ? 2287 ILE A N     1 
ATOM   7581  C CA    . ILE A 1 2287 ? 170.511 207.859 160.665 1.00 47.41  ? 2287 ILE A CA    1 
ATOM   7582  C C     . ILE A 1 2287 ? 171.860 208.373 160.179 1.00 47.41  ? 2287 ILE A C     1 
ATOM   7583  O O     . ILE A 1 2287 ? 172.382 209.372 160.686 1.00 47.41  ? 2287 ILE A O     1 
ATOM   7584  C CB    . ILE A 1 2287 ? 170.666 206.831 161.802 1.00 47.41  ? 2287 ILE A CB    1 
ATOM   7585  C CG1   . ILE A 1 2287 ? 169.293 206.433 162.349 1.00 47.41  ? 2287 ILE A CG1   1 
ATOM   7586  C CG2   . ILE A 1 2287 ? 171.526 207.393 162.921 1.00 47.41  ? 2287 ILE A CG2   1 
ATOM   7587  C CD1   . ILE A 1 2287 ? 169.343 205.700 163.669 1.00 47.41  ? 2287 ILE A CD1   1 
ATOM   7588  N N     . ILE A 1 2288 ? 172.432 207.717 159.169 1.00 52.52  ? 2288 ILE A N     1 
ATOM   7589  C CA    . ILE A 1 2288 ? 173.753 208.108 158.684 1.00 52.52  ? 2288 ILE A CA    1 
ATOM   7590  C C     . ILE A 1 2288 ? 173.664 209.356 157.810 1.00 52.52  ? 2288 ILE A C     1 
ATOM   7591  O O     . ILE A 1 2288 ? 174.473 210.282 157.940 1.00 52.52  ? 2288 ILE A O     1 
ATOM   7592  C CB    . ILE A 1 2288 ? 174.413 206.939 157.932 1.00 52.52  ? 2288 ILE A CB    1 
ATOM   7593  C CG1   . ILE A 1 2288 ? 174.943 205.904 158.924 1.00 52.52  ? 2288 ILE A CG1   1 
ATOM   7594  C CG2   . ILE A 1 2288 ? 175.536 207.438 157.038 1.00 52.52  ? 2288 ILE A CG2   1 
ATOM   7595  C CD1   . ILE A 1 2288 ? 175.159 204.541 158.316 1.00 52.52  ? 2288 ILE A CD1   1 
ATOM   7596  N N     . ASP A 1 2289 ? 172.670 209.407 156.919 1.00 57.90  ? 2289 ASP A N     1 
ATOM   7597  C CA    . ASP A 1 2289 ? 172.626 210.453 155.898 1.00 57.90  ? 2289 ASP A CA    1 
ATOM   7598  C C     . ASP A 1 2289 ? 172.502 211.839 156.520 1.00 57.90  ? 2289 ASP A C     1 
ATOM   7599  O O     . ASP A 1 2289 ? 173.098 212.805 156.030 1.00 57.90  ? 2289 ASP A O     1 
ATOM   7600  C CB    . ASP A 1 2289 ? 171.473 210.194 154.929 1.00 57.90  ? 2289 ASP A CB    1 
ATOM   7601  C CG    . ASP A 1 2289 ? 171.667 208.930 154.117 1.00 57.90  ? 2289 ASP A CG    1 
ATOM   7602  O OD1   . ASP A 1 2289 ? 172.743 208.308 154.233 1.00 57.90  ? 2289 ASP A OD1   1 
ATOM   7603  O OD2   . ASP A 1 2289 ? 170.742 208.558 153.365 1.00 57.90  ? 2289 ASP A OD2   1 
ATOM   7604  N N     . SER A 1 2290 ? 171.713 211.957 157.587 1.00 63.93  ? 2290 SER A N     1 
ATOM   7605  C CA    . SER A 1 2290 ? 171.535 213.212 158.318 1.00 63.93  ? 2290 SER A CA    1 
ATOM   7606  C C     . SER A 1 2290 ? 170.898 214.286 157.437 1.00 63.93  ? 2290 SER A C     1 
ATOM   7607  O O     . SER A 1 2290 ? 171.381 215.417 157.339 1.00 63.93  ? 2290 SER A O     1 
ATOM   7608  C CB    . SER A 1 2290 ? 172.861 213.699 158.909 1.00 63.93  ? 2290 SER A CB    1 
ATOM   7609  O OG    . SER A 1 2290 ? 173.681 214.283 157.912 1.00 63.93  ? 2290 SER A OG    1 
ATOM   7610  N N     . VAL A 1 2291 ? 169.796 213.917 156.781 1.00 72.21  ? 2291 VAL A N     1 
ATOM   7611  C CA    . VAL A 1 2291 ? 169.010 214.904 156.045 1.00 72.21  ? 2291 VAL A CA    1 
ATOM   7612  C C     . VAL A 1 2291 ? 168.241 215.798 157.012 1.00 72.21  ? 2291 VAL A C     1 
ATOM   7613  O O     . VAL A 1 2291 ? 168.066 216.998 156.768 1.00 72.21  ? 2291 VAL A O     1 
ATOM   7614  C CB    . VAL A 1 2291 ? 168.077 214.205 155.036 1.00 72.21  ? 2291 VAL A CB    1 
ATOM   7615  C CG1   . VAL A 1 2291 ? 167.194 213.180 155.731 1.00 72.21  ? 2291 VAL A CG1   1 
ATOM   7616  C CG2   . VAL A 1 2291 ? 167.232 215.229 154.289 1.00 72.21  ? 2291 VAL A CG2   1 
ATOM   7617  N N     . ARG A 1 2292 ? 167.775 215.230 158.126 1.00 71.43  ? 2292 ARG A N     1 
ATOM   7618  C CA    . ARG A 1 2292 ? 167.013 215.989 159.108 1.00 71.43  ? 2292 ARG A CA    1 
ATOM   7619  C C     . ARG A 1 2292 ? 167.854 216.434 160.296 1.00 71.43  ? 2292 ARG A C     1 
ATOM   7620  O O     . ARG A 1 2292 ? 167.493 217.411 160.960 1.00 71.43  ? 2292 ARG A O     1 
ATOM   7621  C CB    . ARG A 1 2292 ? 165.827 215.159 159.605 1.00 71.43  ? 2292 ARG A CB    1 
ATOM   7622  C CG    . ARG A 1 2292 ? 165.045 214.477 158.498 1.00 71.43  ? 2292 ARG A CG    1 
ATOM   7623  C CD    . ARG A 1 2292 ? 163.562 214.314 158.831 1.00 71.43  ? 2292 ARG A CD    1 
ATOM   7624  N NE    . ARG A 1 2292 ? 162.822 215.573 158.828 1.00 71.43  ? 2292 ARG A NE    1 
ATOM   7625  C CZ    . ARG A 1 2292 ? 162.666 216.362 159.883 1.00 71.43  ? 2292 ARG A CZ    1 
ATOM   7626  N NH1   . ARG A 1 2292 ? 163.157 216.039 161.068 1.00 71.43  ? 2292 ARG A NH1   1 
ATOM   7627  N NH2   . ARG A 1 2292 ? 161.987 217.497 159.748 1.00 71.43  ? 2292 ARG A NH2   1 
ATOM   7628  N N     . GLY A 1 2293 ? 168.956 215.746 160.580 1.00 63.15  ? 2293 GLY A N     1 
ATOM   7629  C CA    . GLY A 1 2293 ? 169.780 216.090 161.721 1.00 63.15  ? 2293 GLY A CA    1 
ATOM   7630  C C     . GLY A 1 2293 ? 169.591 215.144 162.889 1.00 63.15  ? 2293 GLY A C     1 
ATOM   7631  O O     . GLY A 1 2293 ? 169.537 215.577 164.043 1.00 63.15  ? 2293 GLY A O     1 
ATOM   7632  N N     . GLU A 1 2294 ? 169.474 213.847 162.598 1.00 57.63  ? 2294 GLU A N     1 
ATOM   7633  C CA    . GLU A 1 2294 ? 169.290 212.867 163.664 1.00 57.63  ? 2294 GLU A CA    1 
ATOM   7634  C C     . GLU A 1 2294 ? 170.567 212.663 164.470 1.00 57.63  ? 2294 GLU A C     1 
ATOM   7635  O O     . GLU A 1 2294 ? 170.524 212.122 165.581 1.00 57.63  ? 2294 GLU A O     1 
ATOM   7636  C CB    . GLU A 1 2294 ? 168.775 211.548 163.085 1.00 57.63  ? 2294 GLU A CB    1 
ATOM   7637  C CG    . GLU A 1 2294 ? 167.753 211.738 161.975 1.00 57.63  ? 2294 GLU A CG    1 
ATOM   7638  C CD    . GLU A 1 2294 ? 168.361 211.691 160.597 1.00 57.63  ? 2294 GLU A CD    1 
ATOM   7639  O OE1   . GLU A 1 2294 ? 167.843 210.944 159.742 1.00 57.63  ? 2294 GLU A OE1   1 
ATOM   7640  O OE2   . GLU A 1 2294 ? 169.361 212.401 160.373 1.00 57.63  ? 2294 GLU A OE2   1 
ATOM   7641  N N     . LEU A 1 2295 ? 171.713 213.080 163.936 1.00 55.62  ? 2295 LEU A N     1 
ATOM   7642  C CA    . LEU A 1 2295 ? 172.881 213.202 164.792 1.00 55.62  ? 2295 LEU A CA    1 
ATOM   7643  C C     . LEU A 1 2295 ? 172.680 214.367 165.759 1.00 55.62  ? 2295 LEU A C     1 
ATOM   7644  O O     . LEU A 1 2295 ? 171.812 215.222 165.573 1.00 55.62  ? 2295 LEU A O     1 
ATOM   7645  C CB    . LEU A 1 2295 ? 174.160 213.385 163.975 1.00 55.62  ? 2295 LEU A CB    1 
ATOM   7646  C CG    . LEU A 1 2295 ? 174.768 212.143 163.311 1.00 55.62  ? 2295 LEU A CG    1 
ATOM   7647  C CD1   . LEU A 1 2295 ? 173.941 211.655 162.135 1.00 55.62  ? 2295 LEU A CD1   1 
ATOM   7648  C CD2   . LEU A 1 2295 ? 176.210 212.393 162.895 1.00 55.62  ? 2295 LEU A CD2   1 
ATOM   7649  N N     . GLN A 1 2296 ? 173.494 214.380 166.816 1.00 57.03  ? 2296 GLN A N     1 
ATOM   7650  C CA    . GLN A 1 2296 ? 173.270 215.210 167.999 1.00 57.03  ? 2296 GLN A CA    1 
ATOM   7651  C C     . GLN A 1 2296 ? 171.990 214.810 168.723 1.00 57.03  ? 2296 GLN A C     1 
ATOM   7652  O O     . GLN A 1 2296 ? 171.503 215.543 169.589 1.00 57.03  ? 2296 GLN A O     1 
ATOM   7653  C CB    . GLN A 1 2296 ? 173.243 216.709 167.662 1.00 57.03  ? 2296 GLN A CB    1 
ATOM   7654  C CG    . GLN A 1 2296 ? 174.594 217.305 167.291 1.00 57.03  ? 2296 GLN A CG    1 
ATOM   7655  C CD    . GLN A 1 2296 ? 175.103 216.825 165.945 1.00 57.03  ? 2296 GLN A CD    1 
ATOM   7656  O OE1   . GLN A 1 2296 ? 176.169 216.219 165.852 1.00 57.03  ? 2296 GLN A OE1   1 
ATOM   7657  N NE2   . GLN A 1 2296 ? 174.339 217.096 164.892 1.00 57.03  ? 2296 GLN A NE2   1 
ATOM   7658  N N     . LYS A 1 2297 ? 171.437 213.652 168.363 1.00 45.12  ? 2297 LYS A N     1 
ATOM   7659  C CA    . LYS A 1 2297 ? 170.278 213.072 169.021 1.00 45.12  ? 2297 LYS A CA    1 
ATOM   7660  C C     . LYS A 1 2297 ? 170.561 211.601 169.279 1.00 45.12  ? 2297 LYS A C     1 
ATOM   7661  O O     . LYS A 1 2297 ? 171.162 210.923 168.442 1.00 45.12  ? 2297 LYS A O     1 
ATOM   7662  C CB    . LYS A 1 2297 ? 169.005 213.219 168.179 1.00 45.12  ? 2297 LYS A CB    1 
ATOM   7663  C CG    . LYS A 1 2297 ? 168.343 214.583 168.274 1.00 45.12  ? 2297 LYS A CG    1 
ATOM   7664  C CD    . LYS A 1 2297 ? 167.453 214.855 167.071 1.00 45.12  ? 2297 LYS A CD    1 
ATOM   7665  C CE    . LYS A 1 2297 ? 166.685 213.611 166.655 1.00 45.12  ? 2297 LYS A CE    1 
ATOM   7666  N NZ    . LYS A 1 2297 ? 165.939 213.812 165.383 1.00 45.12  ? 2297 LYS A NZ    1 
ATOM   7667  N N     . ARG A 1 2298 ? 170.126 211.113 170.435 1.00 30.02  ? 2298 ARG A N     1 
ATOM   7668  C CA    . ARG A 1 2298 ? 170.385 209.731 170.829 1.00 30.02  ? 2298 ARG A CA    1 
ATOM   7669  C C     . ARG A 1 2298 ? 169.410 208.814 170.104 1.00 30.02  ? 2298 ARG A C     1 
ATOM   7670  O O     . ARG A 1 2298 ? 168.204 208.844 170.355 1.00 30.02  ? 2298 ARG A O     1 
ATOM   7671  C CB    . ARG A 1 2298 ? 170.269 209.578 172.340 1.00 30.02  ? 2298 ARG A CB    1 
ATOM   7672  C CG    . ARG A 1 2298 ? 170.808 208.262 172.868 1.00 30.02  ? 2298 ARG A CG    1 
ATOM   7673  C CD    . ARG A 1 2298 ? 170.902 208.274 174.380 1.00 30.02  ? 2298 ARG A CD    1 
ATOM   7674  N NE    . ARG A 1 2298 ? 171.083 209.622 174.902 1.00 30.02  ? 2298 ARG A NE    1 
ATOM   7675  C CZ    . ARG A 1 2298 ? 172.213 210.077 175.425 1.00 30.02  ? 2298 ARG A CZ    1 
ATOM   7676  N NH1   . ARG A 1 2298 ? 173.289 209.312 175.514 1.00 30.02  ? 2298 ARG A NH1   1 
ATOM   7677  N NH2   . ARG A 1 2298 ? 172.265 211.328 175.870 1.00 30.02  ? 2298 ARG A NH2   1 
ATOM   7678  N N     . GLN A 1 2299 ? 169.931 207.994 169.197 1.00 29.25  ? 2299 GLN A N     1 
ATOM   7679  C CA    . GLN A 1 2299 ? 169.134 207.026 168.456 1.00 29.25  ? 2299 GLN A CA    1 
ATOM   7680  C C     . GLN A 1 2299 ? 169.340 205.646 169.066 1.00 29.25  ? 2299 GLN A C     1 
ATOM   7681  O O     . GLN A 1 2299 ? 170.480 205.210 169.251 1.00 29.25  ? 2299 GLN A O     1 
ATOM   7682  C CB    . GLN A 1 2299 ? 169.513 207.022 166.977 1.00 29.25  ? 2299 GLN A CB    1 
ATOM   7683  C CG    . GLN A 1 2299 ? 169.518 208.394 166.328 1.00 29.25  ? 2299 GLN A CG    1 
ATOM   7684  C CD    . GLN A 1 2299 ? 168.144 208.809 165.842 1.00 29.25  ? 2299 GLN A CD    1 
ATOM   7685  O OE1   . GLN A 1 2299 ? 167.518 208.109 165.047 1.00 29.25  ? 2299 GLN A OE1   1 
ATOM   7686  N NE2   . GLN A 1 2299 ? 167.669 209.954 166.317 1.00 29.25  ? 2299 GLN A NE2   1 
ATOM   7687  N N     . TRP A 1 2300 ? 168.239 204.964 169.372 1.00 21.20  ? 2300 TRP A N     1 
ATOM   7688  C CA    . TRP A 1 2300 ? 168.267 203.654 170.013 1.00 21.20  ? 2300 TRP A CA    1 
ATOM   7689  C C     . TRP A 1 2300 ? 167.436 202.688 169.181 1.00 21.20  ? 2300 TRP A C     1 
ATOM   7690  O O     . TRP A 1 2300 ? 166.212 202.834 169.090 1.00 21.20  ? 2300 TRP A O     1 
ATOM   7691  C CB    . TRP A 1 2300 ? 167.741 203.741 171.444 1.00 21.20  ? 2300 TRP A CB    1 
ATOM   7692  C CG    . TRP A 1 2300 ? 168.770 204.190 172.430 1.00 21.20  ? 2300 TRP A CG    1 
ATOM   7693  C CD1   . TRP A 1 2300 ? 170.070 204.504 172.172 1.00 21.20  ? 2300 TRP A CD1   1 
ATOM   7694  C CD2   . TRP A 1 2300 ? 168.581 204.387 173.835 1.00 21.20  ? 2300 TRP A CD2   1 
ATOM   7695  N NE1   . TRP A 1 2300 ? 170.706 204.876 173.329 1.00 21.20  ? 2300 TRP A NE1   1 
ATOM   7696  C CE2   . TRP A 1 2300 ? 169.813 204.813 174.365 1.00 21.20  ? 2300 TRP A CE2   1 
ATOM   7697  C CE3   . TRP A 1 2300 ? 167.491 204.241 174.696 1.00 21.20  ? 2300 TRP A CE3   1 
ATOM   7698  C CZ2   . TRP A 1 2300 ? 169.986 205.094 175.717 1.00 21.20  ? 2300 TRP A CZ2   1 
ATOM   7699  C CZ3   . TRP A 1 2300 ? 167.666 204.517 176.038 1.00 21.20  ? 2300 TRP A CZ3   1 
ATOM   7700  C CH2   . TRP A 1 2300 ? 168.902 204.941 176.535 1.00 21.20  ? 2300 TRP A CH2   1 
ATOM   7701  N N     . ILE A 1 2301 ? 168.097 201.701 168.579 1.00 22.13  ? 2301 ILE A N     1 
ATOM   7702  C CA    . ILE A 1 2301 ? 167.420 200.697 167.756 1.00 22.13  ? 2301 ILE A CA    1 
ATOM   7703  C C     . ILE A 1 2301 ? 167.155 199.502 168.667 1.00 22.13  ? 2301 ILE A C     1 
ATOM   7704  O O     . ILE A 1 2301 ? 167.994 198.617 168.832 1.00 22.13  ? 2301 ILE A O     1 
ATOM   7705  C CB    . ILE A 1 2301 ? 168.239 200.321 166.525 1.00 22.13  ? 2301 ILE A CB    1 
ATOM   7706  C CG1   . ILE A 1 2301 ? 168.581 201.570 165.712 1.00 22.13  ? 2301 ILE A CG1   1 
ATOM   7707  C CG2   . ILE A 1 2301 ? 167.484 199.318 165.670 1.00 22.13  ? 2301 ILE A CG2   1 
ATOM   7708  C CD1   . ILE A 1 2301 ? 169.451 201.292 164.509 1.00 22.13  ? 2301 ILE A CD1   1 
ATOM   7709  N N     . VAL A 1 2302 ? 165.968 199.477 169.263 1.00 18.76  ? 2302 VAL A N     1 
ATOM   7710  C CA    . VAL A 1 2302 ? 165.592 198.428 170.204 1.00 18.76  ? 2302 VAL A CA    1 
ATOM   7711  C C     . VAL A 1 2302 ? 164.980 197.272 169.426 1.00 18.76  ? 2302 VAL A C     1 
ATOM   7712  O O     . VAL A 1 2302 ? 163.968 197.442 168.738 1.00 18.76  ? 2302 VAL A O     1 
ATOM   7713  C CB    . VAL A 1 2302 ? 164.617 198.956 171.265 1.00 18.76  ? 2302 VAL A CB    1 
ATOM   7714  C CG1   . VAL A 1 2302 ? 164.171 197.829 172.176 1.00 18.76  ? 2302 VAL A CG1   1 
ATOM   7715  C CG2   . VAL A 1 2302 ? 165.262 200.073 172.067 1.00 18.76  ? 2302 VAL A CG2   1 
ATOM   7716  N N     . PHE A 1 2303 ? 165.588 196.095 169.539 1.00 22.28  ? 2303 PHE A N     1 
ATOM   7717  C CA    . PHE A 1 2303 ? 165.126 194.911 168.819 1.00 22.28  ? 2303 PHE A CA    1 
ATOM   7718  C C     . PHE A 1 2303 ? 164.222 194.078 169.726 1.00 22.28  ? 2303 PHE A C     1 
ATOM   7719  O O     . PHE A 1 2303 ? 164.574 192.995 170.195 1.00 22.28  ? 2303 PHE A O     1 
ATOM   7720  C CB    . PHE A 1 2303 ? 166.315 194.103 168.312 1.00 22.28  ? 2303 PHE A CB    1 
ATOM   7721  C CG    . PHE A 1 2303 ? 166.817 194.548 166.971 1.00 22.28  ? 2303 PHE A CG    1 
ATOM   7722  C CD1   . PHE A 1 2303 ? 166.041 194.385 165.839 1.00 22.28  ? 2303 PHE A CD1   1 
ATOM   7723  C CD2   . PHE A 1 2303 ? 168.063 195.134 166.844 1.00 22.28  ? 2303 PHE A CD2   1 
ATOM   7724  C CE1   . PHE A 1 2303 ? 166.499 194.795 164.604 1.00 22.28  ? 2303 PHE A CE1   1 
ATOM   7725  C CE2   . PHE A 1 2303 ? 168.526 195.546 165.613 1.00 22.28  ? 2303 PHE A CE2   1 
ATOM   7726  C CZ    . PHE A 1 2303 ? 167.743 195.376 164.492 1.00 22.28  ? 2303 PHE A CZ    1 
ATOM   7727  N N     . ASP A 1 2304 ? 163.030 194.617 169.965 1.00 23.47  ? 2304 ASP A N     1 
ATOM   7728  C CA    . ASP A 1 2304 ? 162.055 193.938 170.808 1.00 23.47  ? 2304 ASP A CA    1 
ATOM   7729  C C     . ASP A 1 2304 ? 161.592 192.648 170.147 1.00 23.47  ? 2304 ASP A C     1 
ATOM   7730  O O     . ASP A 1 2304 ? 161.157 192.649 168.993 1.00 23.47  ? 2304 ASP A O     1 
ATOM   7731  C CB    . ASP A 1 2304 ? 160.864 194.859 171.071 1.00 23.47  ? 2304 ASP A CB    1 
ATOM   7732  C CG    . ASP A 1 2304 ? 160.060 194.442 172.282 1.00 23.47  ? 2304 ASP A CG    1 
ATOM   7733  O OD1   . ASP A 1 2304 ? 159.642 193.268 172.349 1.00 23.47  ? 2304 ASP A OD1   1 
ATOM   7734  O OD2   . ASP A 1 2304 ? 159.842 195.293 173.169 1.00 23.47  ? 2304 ASP A OD2   1 
ATOM   7735  N N     . GLY A 1 2305 ? 161.677 191.545 170.885 1.00 25.76  ? 2305 GLY A N     1 
ATOM   7736  C CA    . GLY A 1 2305 ? 161.287 190.256 170.351 1.00 25.76  ? 2305 GLY A CA    1 
ATOM   7737  C C     . GLY A 1 2305 ? 162.239 189.142 170.730 1.00 25.76  ? 2305 GLY A C     1 
ATOM   7738  O O     . GLY A 1 2305 ? 162.930 189.230 171.748 1.00 25.76  ? 2305 GLY A O     1 
ATOM   7739  N N     . ASP A 1 2306 ? 162.284 188.088 169.922 1.00 34.71  ? 2306 ASP A N     1 
ATOM   7740  C CA    . ASP A 1 2306 ? 163.149 186.946 170.172 1.00 34.71  ? 2306 ASP A CA    1 
ATOM   7741  C C     . ASP A 1 2306 ? 164.403 187.030 169.311 1.00 34.71  ? 2306 ASP A C     1 
ATOM   7742  O O     . ASP A 1 2306 ? 164.441 187.738 168.302 1.00 34.71  ? 2306 ASP A O     1 
ATOM   7743  C CB    . ASP A 1 2306 ? 162.412 185.635 169.895 1.00 34.71  ? 2306 ASP A CB    1 
ATOM   7744  C CG    . ASP A 1 2306 ? 161.050 185.587 170.552 1.00 34.71  ? 2306 ASP A CG    1 
ATOM   7745  O OD1   . ASP A 1 2306 ? 160.869 186.251 171.594 1.00 34.71  ? 2306 ASP A OD1   1 
ATOM   7746  O OD2   . ASP A 1 2306 ? 160.159 184.887 170.028 1.00 34.71  ? 2306 ASP A OD2   1 
ATOM   7747  N N     . VAL A 1 2307 ? 165.435 186.299 169.724 1.00 35.44  ? 2307 VAL A N     1 
ATOM   7748  C CA    . VAL A 1 2307 ? 166.728 186.298 169.052 1.00 35.44  ? 2307 VAL A CA    1 
ATOM   7749  C C     . VAL A 1 2307 ? 167.088 184.864 168.683 1.00 35.44  ? 2307 VAL A C     1 
ATOM   7750  O O     . VAL A 1 2307 ? 166.945 183.949 169.502 1.00 35.44  ? 2307 VAL A O     1 
ATOM   7751  C CB    . VAL A 1 2307 ? 167.821 186.948 169.925 1.00 35.44  ? 2307 VAL A CB    1 
ATOM   7752  C CG1   . VAL A 1 2307 ? 167.957 186.229 171.259 1.00 35.44  ? 2307 VAL A CG1   1 
ATOM   7753  C CG2   . VAL A 1 2307 ? 169.149 186.966 169.189 1.00 35.44  ? 2307 VAL A CG2   1 
ATOM   7754  N N     . ASP A 1 2308 ? 167.520 184.670 167.444 1.00 40.60  ? 2308 ASP A N     1 
ATOM   7755  C CA    . ASP A 1 2308 ? 167.945 183.378 166.932 1.00 40.60  ? 2308 ASP A CA    1 
ATOM   7756  C C     . ASP A 1 2308 ? 169.145 183.601 166.026 1.00 40.60  ? 2308 ASP A C     1 
ATOM   7757  O O     . ASP A 1 2308 ? 169.386 184.726 165.576 1.00 40.60  ? 2308 ASP A O     1 
ATOM   7758  C CB    . ASP A 1 2308 ? 166.812 182.670 166.175 1.00 40.60  ? 2308 ASP A CB    1 
ATOM   7759  C CG    . ASP A 1 2308 ? 166.155 183.552 165.138 1.00 40.60  ? 2308 ASP A CG    1 
ATOM   7760  O OD1   . ASP A 1 2308 ? 166.868 184.117 164.284 1.00 40.60  ? 2308 ASP A OD1   1 
ATOM   7761  O OD2   . ASP A 1 2308 ? 164.918 183.680 165.180 1.00 40.60  ? 2308 ASP A OD2   1 
ATOM   7762  N N     . PRO A 1 2309 ? 169.923 182.546 165.735 1.00 43.05  ? 2309 PRO A N     1 
ATOM   7763  C CA    . PRO A 1 2309 ? 171.145 182.740 164.941 1.00 43.05  ? 2309 PRO A CA    1 
ATOM   7764  C C     . PRO A 1 2309 ? 170.893 183.081 163.479 1.00 43.05  ? 2309 PRO A C     1 
ATOM   7765  O O     . PRO A 1 2309 ? 171.841 183.131 162.689 1.00 43.05  ? 2309 PRO A O     1 
ATOM   7766  C CB    . PRO A 1 2309 ? 171.867 181.390 165.070 1.00 43.05  ? 2309 PRO A CB    1 
ATOM   7767  C CG    . PRO A 1 2309 ? 171.213 180.694 166.219 1.00 43.05  ? 2309 PRO A CG    1 
ATOM   7768  C CD    . PRO A 1 2309 ? 169.805 181.160 166.216 1.00 43.05  ? 2309 PRO A CD    1 
ATOM   7769  N N     . GLU A 1 2310 ? 169.638 183.316 163.098 1.00 44.18  ? 2310 GLU A N     1 
ATOM   7770  C CA    . GLU A 1 2310 ? 169.318 183.598 161.702 1.00 44.18  ? 2310 GLU A CA    1 
ATOM   7771  C C     . GLU A 1 2310 ? 169.403 185.087 161.379 1.00 44.18  ? 2310 GLU A C     1 
ATOM   7772  O O     . GLU A 1 2310 ? 170.189 185.497 160.519 1.00 44.18  ? 2310 GLU A O     1 
ATOM   7773  C CB    . GLU A 1 2310 ? 167.922 183.062 161.364 1.00 44.18  ? 2310 GLU A CB    1 
ATOM   7774  C CG    . GLU A 1 2310 ? 167.685 181.628 161.792 1.00 44.18  ? 2310 GLU A CG    1 
ATOM   7775  C CD    . GLU A 1 2310 ? 168.577 180.644 161.062 1.00 44.18  ? 2310 GLU A CD    1 
ATOM   7776  O OE1   . GLU A 1 2310 ? 169.687 180.362 161.560 1.00 44.18  ? 2310 GLU A OE1   1 
ATOM   7777  O OE2   . GLU A 1 2310 ? 168.167 180.150 159.991 1.00 44.18  ? 2310 GLU A OE2   1 
ATOM   7778  N N     . TRP A 1 2311 ? 168.604 185.909 162.059 1.00 37.72  ? 2311 TRP A N     1 
ATOM   7779  C CA    . TRP A 1 2311 ? 168.516 187.320 161.708 1.00 37.72  ? 2311 TRP A CA    1 
ATOM   7780  C C     . TRP A 1 2311 ? 169.633 188.162 162.309 1.00 37.72  ? 2311 TRP A C     1 
ATOM   7781  O O     . TRP A 1 2311 ? 169.725 189.352 161.991 1.00 37.72  ? 2311 TRP A O     1 
ATOM   7782  C CB    . TRP A 1 2311 ? 167.158 187.887 162.133 1.00 37.72  ? 2311 TRP A CB    1 
ATOM   7783  C CG    . TRP A 1 2311 ? 166.978 188.009 163.613 1.00 37.72  ? 2311 TRP A CG    1 
ATOM   7784  C CD1   . TRP A 1 2311 ? 166.576 187.032 164.472 1.00 37.72  ? 2311 TRP A CD1   1 
ATOM   7785  C CD2   . TRP A 1 2311 ? 167.182 189.182 164.409 1.00 37.72  ? 2311 TRP A CD2   1 
ATOM   7786  N NE1   . TRP A 1 2311 ? 166.522 187.518 165.754 1.00 37.72  ? 2311 TRP A NE1   1 
ATOM   7787  C CE2   . TRP A 1 2311 ? 166.889 188.837 165.742 1.00 37.72  ? 2311 TRP A CE2   1 
ATOM   7788  C CE3   . TRP A 1 2311 ? 167.586 190.488 164.123 1.00 37.72  ? 2311 TRP A CE3   1 
ATOM   7789  C CZ2   . TRP A 1 2311 ? 166.990 189.750 166.787 1.00 37.72  ? 2311 TRP A CZ2   1 
ATOM   7790  C CZ3   . TRP A 1 2311 ? 167.683 191.393 165.161 1.00 37.72  ? 2311 TRP A CZ3   1 
ATOM   7791  C CH2   . TRP A 1 2311 ? 167.385 191.021 166.476 1.00 37.72  ? 2311 TRP A CH2   1 
ATOM   7792  N N     . VAL A 1 2312 ? 170.483 187.584 163.159 1.00 41.80  ? 2312 VAL A N     1 
ATOM   7793  C CA    . VAL A 1 2312 ? 171.580 188.319 163.776 1.00 41.80  ? 2312 VAL A CA    1 
ATOM   7794  C C     . VAL A 1 2312 ? 172.907 188.062 163.071 1.00 41.80  ? 2312 VAL A C     1 
ATOM   7795  O O     . VAL A 1 2312 ? 173.954 188.508 163.551 1.00 41.80  ? 2312 VAL A O     1 
ATOM   7796  C CB    . VAL A 1 2312 ? 171.689 187.995 165.273 1.00 41.80  ? 2312 VAL A CB    1 
ATOM   7797  C CG1   . VAL A 1 2312 ? 170.385 188.315 165.978 1.00 41.80  ? 2312 VAL A CG1   1 
ATOM   7798  C CG2   . VAL A 1 2312 ? 172.068 186.538 165.472 1.00 41.80  ? 2312 VAL A CG2   1 
ATOM   7799  N N     . GLU A 1 2313 ? 172.891 187.345 161.945 1.00 48.30  ? 2313 GLU A N     1 
ATOM   7800  C CA    . GLU A 1 2313 ? 174.130 187.054 161.232 1.00 48.30  ? 2313 GLU A CA    1 
ATOM   7801  C C     . GLU A 1 2313 ? 174.776 188.329 160.704 1.00 48.30  ? 2313 GLU A C     1 
ATOM   7802  O O     . GLU A 1 2313 ? 175.988 188.528 160.846 1.00 48.30  ? 2313 GLU A O     1 
ATOM   7803  C CB    . GLU A 1 2313 ? 173.859 186.074 160.091 1.00 48.30  ? 2313 GLU A CB    1 
ATOM   7804  C CG    . GLU A 1 2313 ? 173.899 184.615 160.508 1.00 48.30  ? 2313 GLU A CG    1 
ATOM   7805  C CD    . GLU A 1 2313 ? 173.840 183.670 159.327 1.00 48.30  ? 2313 GLU A CD    1 
ATOM   7806  O OE1   . GLU A 1 2313 ? 174.679 182.747 159.261 1.00 48.30  ? 2313 GLU A OE1   1 
ATOM   7807  O OE2   . GLU A 1 2313 ? 172.955 183.849 158.464 1.00 48.30  ? 2313 GLU A OE2   1 
ATOM   7808  N N     . ASN A 1 2314 ? 173.981 189.209 160.093 1.00 51.15  ? 2314 ASN A N     1 
ATOM   7809  C CA    . ASN A 1 2314 ? 174.518 190.471 159.600 1.00 51.15  ? 2314 ASN A CA    1 
ATOM   7810  C C     . ASN A 1 2314 ? 174.780 191.463 160.724 1.00 51.15  ? 2314 ASN A C     1 
ATOM   7811  O O     . ASN A 1 2314 ? 175.534 192.421 160.524 1.00 51.15  ? 2314 ASN A O     1 
ATOM   7812  C CB    . ASN A 1 2314 ? 173.565 191.087 158.575 1.00 51.15  ? 2314 ASN A CB    1 
ATOM   7813  C CG    . ASN A 1 2314 ? 173.336 190.187 157.378 1.00 51.15  ? 2314 ASN A CG    1 
ATOM   7814  O OD1   . ASN A 1 2314 ? 173.037 189.002 157.526 1.00 51.15  ? 2314 ASN A OD1   1 
ATOM   7815  N ND2   . ASN A 1 2314 ? 173.474 190.746 156.182 1.00 51.15  ? 2314 ASN A ND2   1 
ATOM   7816  N N     . LEU A 1 2315 ? 174.175 191.258 161.893 1.00 43.85  ? 2315 LEU A N     1 
ATOM   7817  C CA    . LEU A 1 2315 ? 174.386 192.141 163.031 1.00 43.85  ? 2315 LEU A CA    1 
ATOM   7818  C C     . LEU A 1 2315 ? 175.649 191.814 163.814 1.00 43.85  ? 2315 LEU A C     1 
ATOM   7819  O O     . LEU A 1 2315 ? 176.069 192.628 164.643 1.00 43.85  ? 2315 LEU A O     1 
ATOM   7820  C CB    . LEU A 1 2315 ? 173.177 192.086 163.968 1.00 43.85  ? 2315 LEU A CB    1 
ATOM   7821  C CG    . LEU A 1 2315 ? 172.161 193.217 163.818 1.00 43.85  ? 2315 LEU A CG    1 
ATOM   7822  C CD1   . LEU A 1 2315 ? 171.073 193.099 164.867 1.00 43.85  ? 2315 LEU A CD1   1 
ATOM   7823  C CD2   . LEU A 1 2315 ? 172.853 194.564 163.909 1.00 43.85  ? 2315 LEU A CD2   1 
ATOM   7824  N N     . ASN A 1 2316 ? 176.256 190.649 163.581 1.00 44.51  ? 2316 ASN A N     1 
ATOM   7825  C CA    . ASN A 1 2316 ? 177.467 190.288 164.309 1.00 44.51  ? 2316 ASN A CA    1 
ATOM   7826  C C     . ASN A 1 2316 ? 178.613 191.236 163.980 1.00 44.51  ? 2316 ASN A C     1 
ATOM   7827  O O     . ASN A 1 2316 ? 179.393 191.607 164.865 1.00 44.51  ? 2316 ASN A O     1 
ATOM   7828  C CB    . ASN A 1 2316 ? 177.855 188.843 163.998 1.00 44.51  ? 2316 ASN A CB    1 
ATOM   7829  C CG    . ASN A 1 2316 ? 177.058 187.840 164.808 1.00 44.51  ? 2316 ASN A CG    1 
ATOM   7830  O OD1   . ASN A 1 2316 ? 176.222 188.214 165.630 1.00 44.51  ? 2316 ASN A OD1   1 
ATOM   7831  N ND2   . ASN A 1 2316 ? 177.312 186.558 164.578 1.00 44.51  ? 2316 ASN A ND2   1 
ATOM   7832  N N     . SER A 1 2317 ? 178.732 191.639 162.714 1.00 46.06  ? 2317 SER A N     1 
ATOM   7833  C CA    . SER A 1 2317 ? 179.766 192.586 162.317 1.00 46.06  ? 2317 SER A CA    1 
ATOM   7834  C C     . SER A 1 2317 ? 179.483 194.002 162.801 1.00 46.06  ? 2317 SER A C     1 
ATOM   7835  O O     . SER A 1 2317 ? 180.367 194.859 162.701 1.00 46.06  ? 2317 SER A O     1 
ATOM   7836  C CB    . SER A 1 2317 ? 179.925 192.580 160.796 1.00 46.06  ? 2317 SER A CB    1 
ATOM   7837  O OG    . SER A 1 2317 ? 178.835 193.230 160.168 1.00 46.06  ? 2317 SER A OG    1 
ATOM   7838  N N     . VAL A 1 2318 ? 178.284 194.268 163.307 1.00 43.97  ? 2318 VAL A N     1 
ATOM   7839  C CA    . VAL A 1 2318 ? 177.942 195.569 163.864 1.00 43.97  ? 2318 VAL A CA    1 
ATOM   7840  C C     . VAL A 1 2318 ? 178.133 195.598 165.375 1.00 43.97  ? 2318 VAL A C     1 
ATOM   7841  O O     . VAL A 1 2318 ? 178.600 196.595 165.926 1.00 43.97  ? 2318 VAL A O     1 
ATOM   7842  C CB    . VAL A 1 2318 ? 176.494 195.945 163.482 1.00 43.97  ? 2318 VAL A CB    1 
ATOM   7843  C CG1   . VAL A 1 2318 ? 176.086 197.250 164.143 1.00 43.97  ? 2318 VAL A CG1   1 
ATOM   7844  C CG2   . VAL A 1 2318 ? 176.353 196.040 161.977 1.00 43.97  ? 2318 VAL A CG2   1 
ATOM   7845  N N     . LEU A 1 2319 ? 177.782 194.504 166.052 1.00 42.71  ? 2319 LEU A N     1 
ATOM   7846  C CA    . LEU A 1 2319 ? 177.860 194.473 167.509 1.00 42.71  ? 2319 LEU A CA    1 
ATOM   7847  C C     . LEU A 1 2319 ? 179.303 194.528 167.994 1.00 42.71  ? 2319 LEU A C     1 
ATOM   7848  O O     . LEU A 1 2319 ? 179.590 195.116 169.043 1.00 42.71  ? 2319 LEU A O     1 
ATOM   7849  C CB    . LEU A 1 2319 ? 177.161 193.222 168.039 1.00 42.71  ? 2319 LEU A CB    1 
ATOM   7850  C CG    . LEU A 1 2319 ? 175.662 193.142 167.743 1.00 42.71  ? 2319 LEU A CG    1 
ATOM   7851  C CD1   . LEU A 1 2319 ? 175.117 191.760 168.061 1.00 42.71  ? 2319 LEU A CD1   1 
ATOM   7852  C CD2   . LEU A 1 2319 ? 174.905 194.216 168.506 1.00 42.71  ? 2319 LEU A CD2   1 
ATOM   7853  N N     . ASP A 1 2320 ? 180.226 193.929 167.246 1.00 51.26  ? 2320 ASP A N     1 
ATOM   7854  C CA    . ASP A 1 2320 ? 181.621 193.861 167.661 1.00 51.26  ? 2320 ASP A CA    1 
ATOM   7855  C C     . ASP A 1 2320 ? 182.304 195.211 167.431 1.00 51.26  ? 2320 ASP A C     1 
ATOM   7856  O O     . ASP A 1 2320 ? 181.663 196.217 167.117 1.00 51.26  ? 2320 ASP A O     1 
ATOM   7857  C CB    . ASP A 1 2320 ? 182.331 192.716 166.941 1.00 51.26  ? 2320 ASP A CB    1 
ATOM   7858  C CG    . ASP A 1 2320 ? 182.373 192.899 165.433 1.00 51.26  ? 2320 ASP A CG    1 
ATOM   7859  O OD1   . ASP A 1 2320 ? 181.816 193.894 164.925 1.00 51.26  ? 2320 ASP A OD1   1 
ATOM   7860  O OD2   . ASP A 1 2320 ? 182.969 192.039 164.752 1.00 51.26  ? 2320 ASP A OD2   1 
ATOM   7861  N N     . ASP A 1 2321 ? 183.630 195.240 167.589 1.00 57.51  ? 2321 ASP A N     1 
ATOM   7862  C CA    . ASP A 1 2321 ? 184.375 196.489 167.472 1.00 57.51  ? 2321 ASP A CA    1 
ATOM   7863  C C     . ASP A 1 2321 ? 184.370 197.049 166.057 1.00 57.51  ? 2321 ASP A C     1 
ATOM   7864  O O     . ASP A 1 2321 ? 184.719 198.219 165.869 1.00 57.51  ? 2321 ASP A O     1 
ATOM   7865  C CB    . ASP A 1 2321 ? 185.816 196.287 167.942 1.00 57.51  ? 2321 ASP A CB    1 
ATOM   7866  C CG    . ASP A 1 2321 ? 185.913 196.048 169.434 1.00 57.51  ? 2321 ASP A CG    1 
ATOM   7867  O OD1   . ASP A 1 2321 ? 185.047 196.556 170.175 1.00 57.51  ? 2321 ASP A OD1   1 
ATOM   7868  O OD2   . ASP A 1 2321 ? 186.856 195.353 169.867 1.00 57.51  ? 2321 ASP A OD2   1 
ATOM   7869  N N     . ASN A 1 2322 ? 183.995 196.245 165.059 1.00 50.84  ? 2322 ASN A N     1 
ATOM   7870  C CA    . ASN A 1 2322 ? 183.939 196.750 163.692 1.00 50.84  ? 2322 ASN A CA    1 
ATOM   7871  C C     . ASN A 1 2322 ? 182.903 197.859 163.554 1.00 50.84  ? 2322 ASN A C     1 
ATOM   7872  O O     . ASN A 1 2322 ? 183.153 198.866 162.881 1.00 50.84  ? 2322 ASN A O     1 
ATOM   7873  C CB    . ASN A 1 2322 ? 183.636 195.611 162.719 1.00 50.84  ? 2322 ASN A CB    1 
ATOM   7874  C CG    . ASN A 1 2322 ? 184.694 194.527 162.745 1.00 50.84  ? 2322 ASN A CG    1 
ATOM   7875  O OD1   . ASN A 1 2322 ? 185.690 194.633 163.459 1.00 50.84  ? 2322 ASN A OD1   1 
ATOM   7876  N ND2   . ASN A 1 2322 ? 184.483 193.475 161.962 1.00 50.84  ? 2322 ASN A ND2   1 
ATOM   7877  N N     . LYS A 1 2323 ? 181.743 197.697 164.194 1.00 46.82  ? 2323 LYS A N     1 
ATOM   7878  C CA    . LYS A 1 2323 ? 180.629 198.637 164.065 1.00 46.82  ? 2323 LYS A CA    1 
ATOM   7879  C C     . LYS A 1 2323 ? 180.301 198.861 162.593 1.00 46.82  ? 2323 LYS A C     1 
ATOM   7880  O O     . LYS A 1 2323 ? 180.106 199.986 162.129 1.00 46.82  ? 2323 LYS A O     1 
ATOM   7881  C CB    . LYS A 1 2323 ? 180.936 199.957 164.774 1.00 46.82  ? 2323 LYS A CB    1 
ATOM   7882  C CG    . LYS A 1 2323 ? 181.581 199.786 166.139 1.00 46.82  ? 2323 LYS A CG    1 
ATOM   7883  C CD    . LYS A 1 2323 ? 182.164 201.092 166.647 1.00 46.82  ? 2323 LYS A CD    1 
ATOM   7884  C CE    . LYS A 1 2323 ? 181.100 202.170 166.744 1.00 46.82  ? 2323 LYS A CE    1 
ATOM   7885  N NZ    . LYS A 1 2323 ? 181.656 203.447 167.269 1.00 46.82  ? 2323 LYS A NZ    1 
ATOM   7886  N N     . LEU A 1 2324 ? 180.239 197.756 161.854 1.00 51.94  ? 2324 LEU A N     1 
ATOM   7887  C CA    . LEU A 1 2324 ? 180.304 197.780 160.397 1.00 51.94  ? 2324 LEU A CA    1 
ATOM   7888  C C     . LEU A 1 2324 ? 179.234 196.852 159.842 1.00 51.94  ? 2324 LEU A C     1 
ATOM   7889  O O     . LEU A 1 2324 ? 179.259 195.647 160.107 1.00 51.94  ? 2324 LEU A O     1 
ATOM   7890  C CB    . LEU A 1 2324 ? 181.694 197.354 159.928 1.00 51.94  ? 2324 LEU A CB    1 
ATOM   7891  C CG    . LEU A 1 2324 ? 182.236 197.876 158.605 1.00 51.94  ? 2324 LEU A CG    1 
ATOM   7892  C CD1   . LEU A 1 2324 ? 182.463 199.375 158.683 1.00 51.94  ? 2324 LEU A CD1   1 
ATOM   7893  C CD2   . LEU A 1 2324 ? 183.532 197.151 158.279 1.00 51.94  ? 2324 LEU A CD2   1 
ATOM   7894  N N     . LEU A 1 2325 ? 178.302 197.407 159.074 1.00 55.27  ? 2325 LEU A N     1 
ATOM   7895  C CA    . LEU A 1 2325 ? 177.264 196.617 158.424 1.00 55.27  ? 2325 LEU A CA    1 
ATOM   7896  C C     . LEU A 1 2325 ? 177.610 196.460 156.950 1.00 55.27  ? 2325 LEU A C     1 
ATOM   7897  O O     . LEU A 1 2325 ? 177.619 197.443 156.201 1.00 55.27  ? 2325 LEU A O     1 
ATOM   7898  C CB    . LEU A 1 2325 ? 175.896 197.278 158.589 1.00 55.27  ? 2325 LEU A CB    1 
ATOM   7899  C CG    . LEU A 1 2325 ? 174.727 196.585 157.888 1.00 55.27  ? 2325 LEU A CG    1 
ATOM   7900  C CD1   . LEU A 1 2325 ? 174.497 195.201 158.472 1.00 55.27  ? 2325 LEU A CD1   1 
ATOM   7901  C CD2   . LEU A 1 2325 ? 173.467 197.426 157.988 1.00 55.27  ? 2325 LEU A CD2   1 
ATOM   7902  N N     . THR A 1 2326 ? 177.889 195.228 156.533 1.00 63.01  ? 2326 THR A N     1 
ATOM   7903  C CA    . THR A 1 2326 ? 178.241 194.928 155.147 1.00 63.01  ? 2326 THR A CA    1 
ATOM   7904  C C     . THR A 1 2326 ? 176.996 194.401 154.437 1.00 63.01  ? 2326 THR A C     1 
ATOM   7905  O O     . THR A 1 2326 ? 176.410 193.391 154.836 1.00 63.01  ? 2326 THR A O     1 
ATOM   7906  C CB    . THR A 1 2326 ? 179.419 193.955 155.079 1.00 63.01  ? 2326 THR A CB    1 
ATOM   7907  O OG1   . THR A 1 2326 ? 179.781 193.724 153.711 1.00 63.01  ? 2326 THR A OG1   1 
ATOM   7908  C CG2   . THR A 1 2326 ? 179.119 192.631 155.782 1.00 63.01  ? 2326 THR A CG2   1 
ATOM   7909  N N     . LEU A 1 2327 ? 176.568 195.120 153.405 1.00 68.18  ? 2327 LEU A N     1 
ATOM   7910  C CA    . LEU A 1 2327 ? 175.397 194.714 152.651 1.00 68.18  ? 2327 LEU A CA    1 
ATOM   7911  C C     . LEU A 1 2327 ? 175.790 193.741 151.539 1.00 68.18  ? 2327 LEU A C     1 
ATOM   7912  O O     . LEU A 1 2327 ? 176.930 193.755 151.066 1.00 68.18  ? 2327 LEU A O     1 
ATOM   7913  C CB    . LEU A 1 2327 ? 174.697 195.932 152.057 1.00 68.18  ? 2327 LEU A CB    1 
ATOM   7914  C CG    . LEU A 1 2327 ? 174.043 196.879 153.063 1.00 68.18  ? 2327 LEU A CG    1 
ATOM   7915  C CD1   . LEU A 1 2327 ? 173.255 197.966 152.350 1.00 68.18  ? 2327 LEU A CD1   1 
ATOM   7916  C CD2   . LEU A 1 2327 ? 173.151 196.098 154.008 1.00 68.18  ? 2327 LEU A CD2   1 
ATOM   7917  N N     . PRO A 1 2328 ? 174.865 192.875 151.115 1.00 73.71  ? 2328 PRO A N     1 
ATOM   7918  C CA    . PRO A 1 2328 ? 175.181 191.957 150.008 1.00 73.71  ? 2328 PRO A CA    1 
ATOM   7919  C C     . PRO A 1 2328 ? 175.563 192.665 148.720 1.00 73.71  ? 2328 PRO A C     1 
ATOM   7920  O O     . PRO A 1 2328 ? 176.393 192.145 147.963 1.00 73.71  ? 2328 PRO A O     1 
ATOM   7921  C CB    . PRO A 1 2328 ? 173.885 191.151 149.845 1.00 73.71  ? 2328 PRO A CB    1 
ATOM   7922  C CG    . PRO A 1 2328 ? 173.227 191.227 151.181 1.00 73.71  ? 2328 PRO A CG    1 
ATOM   7923  C CD    . PRO A 1 2328 ? 173.548 192.593 151.708 1.00 73.71  ? 2328 PRO A CD    1 
ATOM   7924  N N     . ASN A 1 2329 ? 174.983 193.836 148.442 1.00 69.77  ? 2329 ASN A N     1 
ATOM   7925  C CA    . ASN A 1 2329 ? 175.318 194.555 147.218 1.00 69.77  ? 2329 ASN A CA    1 
ATOM   7926  C C     . ASN A 1 2329 ? 176.739 195.102 147.237 1.00 69.77  ? 2329 ASN A C     1 
ATOM   7927  O O     . ASN A 1 2329 ? 177.304 195.361 146.169 1.00 69.77  ? 2329 ASN A O     1 
ATOM   7928  C CB    . ASN A 1 2329 ? 174.321 195.693 146.983 1.00 69.77  ? 2329 ASN A CB    1 
ATOM   7929  C CG    . ASN A 1 2329 ? 174.433 196.799 148.018 1.00 69.77  ? 2329 ASN A CG    1 
ATOM   7930  O OD1   . ASN A 1 2329 ? 175.102 196.649 149.039 1.00 69.77  ? 2329 ASN A OD1   1 
ATOM   7931  N ND2   . ASN A 1 2329 ? 173.776 197.921 147.753 1.00 69.77  ? 2329 ASN A ND2   1 
ATOM   7932  N N     . GLY A 1 2330 ? 177.324 195.285 148.418 1.00 68.32  ? 2330 GLY A N     1 
ATOM   7933  C CA    . GLY A 1 2330 ? 178.676 195.796 148.520 1.00 68.32  ? 2330 GLY A CA    1 
ATOM   7934  C C     . GLY A 1 2330 ? 178.778 197.033 149.386 1.00 68.32  ? 2330 GLY A C     1 
ATOM   7935  O O     . GLY A 1 2330 ? 179.837 197.310 149.959 1.00 68.32  ? 2330 GLY A O     1 
ATOM   7936  N N     . GLU A 1 2331 ? 177.682 197.786 149.485 1.00 68.10  ? 2331 GLU A N     1 
ATOM   7937  C CA    . GLU A 1 2331 ? 177.680 199.008 150.278 1.00 68.10  ? 2331 GLU A CA    1 
ATOM   7938  C C     . GLU A 1 2331 ? 177.898 198.688 151.751 1.00 68.10  ? 2331 GLU A C     1 
ATOM   7939  O O     . GLU A 1 2331 ? 177.378 197.700 152.276 1.00 68.10  ? 2331 GLU A O     1 
ATOM   7940  C CB    . GLU A 1 2331 ? 176.363 199.767 150.088 1.00 68.10  ? 2331 GLU A CB    1 
ATOM   7941  C CG    . GLU A 1 2331 ? 176.122 200.903 151.088 1.00 68.10  ? 2331 GLU A CG    1 
ATOM   7942  C CD    . GLU A 1 2331 ? 177.183 201.999 151.044 1.00 68.10  ? 2331 GLU A CD    1 
ATOM   7943  O OE1   . GLU A 1 2331 ? 177.194 202.846 151.963 1.00 68.10  ? 2331 GLU A OE1   1 
ATOM   7944  O OE2   . GLU A 1 2331 ? 177.985 202.040 150.086 1.00 68.10  ? 2331 GLU A OE2   1 
ATOM   7945  N N     . ARG A 1 2332 ? 178.678 199.535 152.416 1.00 60.43  ? 2332 ARG A N     1 
ATOM   7946  C CA    . ARG A 1 2332 ? 179.114 199.313 153.788 1.00 60.43  ? 2332 ARG A CA    1 
ATOM   7947  C C     . ARG A 1 2332 ? 178.636 200.476 154.643 1.00 60.43  ? 2332 ARG A C     1 
ATOM   7948  O O     . ARG A 1 2332 ? 178.908 201.637 154.321 1.00 60.43  ? 2332 ARG A O     1 
ATOM   7949  C CB    . ARG A 1 2332 ? 180.635 199.178 153.841 1.00 60.43  ? 2332 ARG A CB    1 
ATOM   7950  C CG    . ARG A 1 2332 ? 181.209 198.849 155.202 1.00 60.43  ? 2332 ARG A CG    1 
ATOM   7951  C CD    . ARG A 1 2332 ? 182.710 198.510 155.145 1.00 60.43  ? 2332 ARG A CD    1 
ATOM   7952  N NE    . ARG A 1 2332 ? 183.513 199.165 154.110 1.00 60.43  ? 2332 ARG A NE    1 
ATOM   7953  C CZ    . ARG A 1 2332 ? 183.557 200.470 153.862 1.00 60.43  ? 2332 ARG A CZ    1 
ATOM   7954  N NH1   . ARG A 1 2332 ? 182.898 201.345 154.605 1.00 60.43  ? 2332 ARG A NH1   1 
ATOM   7955  N NH2   . ARG A 1 2332 ? 184.303 200.910 152.853 1.00 60.43  ? 2332 ARG A NH2   1 
ATOM   7956  N N     . LEU A 1 2333 ? 177.925 200.168 155.724 1.00 56.65  ? 2333 LEU A N     1 
ATOM   7957  C CA    . LEU A 1 2333 ? 177.377 201.182 156.617 1.00 56.65  ? 2333 LEU A CA    1 
ATOM   7958  C C     . LEU A 1 2333 ? 178.157 201.208 157.924 1.00 56.65  ? 2333 LEU A C     1 
ATOM   7959  O O     . LEU A 1 2333 ? 178.348 200.168 158.562 1.00 56.65  ? 2333 LEU A O     1 
ATOM   7960  C CB    . LEU A 1 2333 ? 175.895 200.925 156.890 1.00 56.65  ? 2333 LEU A CB    1 
ATOM   7961  C CG    . LEU A 1 2333 ? 174.959 201.066 155.690 1.00 56.65  ? 2333 LEU A CG    1 
ATOM   7962  C CD1   . LEU A 1 2333 ? 173.553 200.648 156.068 1.00 56.65  ? 2333 LEU A CD1   1 
ATOM   7963  C CD2   . LEU A 1 2333 ? 174.968 202.499 155.185 1.00 56.65  ? 2333 LEU A CD2   1 
ATOM   7964  N N     . SER A 1 2334 ? 178.595 202.399 158.320 1.00 54.52  ? 2334 SER A N     1 
ATOM   7965  C CA    . SER A 1 2334 ? 179.353 202.595 159.547 1.00 54.52  ? 2334 SER A CA    1 
ATOM   7966  C C     . SER A 1 2334 ? 178.421 203.086 160.646 1.00 54.52  ? 2334 SER A C     1 
ATOM   7967  O O     . SER A 1 2334 ? 177.631 204.012 160.430 1.00 54.52  ? 2334 SER A O     1 
ATOM   7968  C CB    . SER A 1 2334 ? 180.489 203.594 159.328 1.00 54.52  ? 2334 SER A CB    1 
ATOM   7969  O OG    . SER A 1 2334 ? 181.219 203.810 160.523 1.00 54.52  ? 2334 SER A OG    1 
ATOM   7970  N N     . LEU A 1 2335 ? 178.515 202.471 161.815 1.00 42.77  ? 2335 LEU A N     1 
ATOM   7971  C CA    . LEU A 1 2335 ? 177.632 202.818 162.921 1.00 42.77  ? 2335 LEU A CA    1 
ATOM   7972  C C     . LEU A 1 2335 ? 178.086 204.121 163.567 1.00 42.77  ? 2335 LEU A C     1 
ATOM   7973  O O     . LEU A 1 2335 ? 179.227 204.201 164.039 1.00 42.77  ? 2335 LEU A O     1 
ATOM   7974  C CB    . LEU A 1 2335 ? 177.615 201.690 163.948 1.00 42.77  ? 2335 LEU A CB    1 
ATOM   7975  C CG    . LEU A 1 2335 ? 176.681 201.872 165.142 1.00 42.77  ? 2335 LEU A CG    1 
ATOM   7976  C CD1   . LEU A 1 2335 ? 175.242 201.945 164.667 1.00 42.77  ? 2335 LEU A CD1   1 
ATOM   7977  C CD2   . LEU A 1 2335 ? 176.857 200.745 166.146 1.00 42.77  ? 2335 LEU A CD2   1 
ATOM   7978  N N     . PRO A 1 2336 ? 177.248 205.152 163.612 1.00 39.80  ? 2336 PRO A N     1 
ATOM   7979  C CA    . PRO A 1 2336 ? 177.644 206.409 164.258 1.00 39.80  ? 2336 PRO A CA    1 
ATOM   7980  C C     . PRO A 1 2336 ? 177.775 206.230 165.759 1.00 39.80  ? 2336 PRO A C     1 
ATOM   7981  O O     . PRO A 1 2336 ? 177.180 205.309 166.338 1.00 39.80  ? 2336 PRO A O     1 
ATOM   7982  C CB    . PRO A 1 2336 ? 176.497 207.369 163.903 1.00 39.80  ? 2336 PRO A CB    1 
ATOM   7983  C CG    . PRO A 1 2336 ? 175.352 206.497 163.559 1.00 39.80  ? 2336 PRO A CG    1 
ATOM   7984  C CD    . PRO A 1 2336 ? 175.917 205.235 162.990 1.00 39.80  ? 2336 PRO A CD    1 
ATOM   7985  N N     . PRO A 1 2337 ? 178.557 207.085 166.427 1.00 37.23  ? 2337 PRO A N     1 
ATOM   7986  C CA    . PRO A 1 2337 ? 178.797 206.889 167.866 1.00 37.23  ? 2337 PRO A CA    1 
ATOM   7987  C C     . PRO A 1 2337 ? 177.570 207.094 168.738 1.00 37.23  ? 2337 PRO A C     1 
ATOM   7988  O O     . PRO A 1 2337 ? 177.593 206.690 169.907 1.00 37.23  ? 2337 PRO A O     1 
ATOM   7989  C CB    . PRO A 1 2337 ? 179.880 207.928 168.184 1.00 37.23  ? 2337 PRO A CB    1 
ATOM   7990  C CG    . PRO A 1 2337 ? 179.690 208.986 167.152 1.00 37.23  ? 2337 PRO A CG    1 
ATOM   7991  C CD    . PRO A 1 2337 ? 179.271 208.262 165.905 1.00 37.23  ? 2337 PRO A CD    1 
ATOM   7992  N N     . ASN A 1 2338 ? 176.506 207.706 168.222 1.00 35.86  ? 2338 ASN A N     1 
ATOM   7993  C CA    . ASN A 1 2338 ? 175.338 208.044 169.024 1.00 35.86  ? 2338 ASN A CA    1 
ATOM   7994  C C     . ASN A 1 2338 ? 174.216 207.020 168.908 1.00 35.86  ? 2338 ASN A C     1 
ATOM   7995  O O     . ASN A 1 2338 ? 173.093 207.301 169.336 1.00 35.86  ? 2338 ASN A O     1 
ATOM   7996  C CB    . ASN A 1 2338 ? 174.816 209.428 168.635 1.00 35.86  ? 2338 ASN A CB    1 
ATOM   7997  C CG    . ASN A 1 2338 ? 174.305 209.477 167.210 1.00 35.86  ? 2338 ASN A CG    1 
ATOM   7998  O OD1   . ASN A 1 2338 ? 175.021 209.136 166.270 1.00 35.86  ? 2338 ASN A OD1   1 
ATOM   7999  N ND2   . ASN A 1 2338 ? 173.060 209.905 167.043 1.00 35.86  ? 2338 ASN A ND2   1 
ATOM   8000  N N     . VAL A 1 2339 ? 174.487 205.846 168.345 1.00 28.93  ? 2339 VAL A N     1 
ATOM   8001  C CA    . VAL A 1 2339 ? 173.471 204.824 168.120 1.00 28.93  ? 2339 VAL A CA    1 
ATOM   8002  C C     . VAL A 1 2339 ? 173.841 203.575 168.905 1.00 28.93  ? 2339 VAL A C     1 
ATOM   8003  O O     . VAL A 1 2339 ? 174.973 203.086 168.812 1.00 28.93  ? 2339 VAL A O     1 
ATOM   8004  C CB    . VAL A 1 2339 ? 173.312 204.505 166.625 1.00 28.93  ? 2339 VAL A CB    1 
ATOM   8005  C CG1   . VAL A 1 2339 ? 172.376 203.326 166.433 1.00 28.93  ? 2339 VAL A CG1   1 
ATOM   8006  C CG2   . VAL A 1 2339 ? 172.785 205.718 165.890 1.00 28.93  ? 2339 VAL A CG2   1 
ATOM   8007  N N     . ARG A 1 2340 ? 172.884 203.063 169.675 1.00 26.14  ? 2340 ARG A N     1 
ATOM   8008  C CA    . ARG A 1 2340 ? 173.032 201.823 170.422 1.00 26.14  ? 2340 ARG A CA    1 
ATOM   8009  C C     . ARG A 1 2340 ? 171.968 200.837 169.964 1.00 26.14  ? 2340 ARG A C     1 
ATOM   8010  O O     . ARG A 1 2340 ? 170.814 201.215 169.740 1.00 26.14  ? 2340 ARG A O     1 
ATOM   8011  C CB    . ARG A 1 2340 ? 172.908 202.062 171.930 1.00 26.14  ? 2340 ARG A CB    1 
ATOM   8012  C CG    . ARG A 1 2340 ? 173.779 203.186 172.457 1.00 26.14  ? 2340 ARG A CG    1 
ATOM   8013  C CD    . ARG A 1 2340 ? 175.252 202.882 172.261 1.00 26.14  ? 2340 ARG A CD    1 
ATOM   8014  N NE    . ARG A 1 2340 ? 176.089 203.604 173.212 1.00 26.14  ? 2340 ARG A NE    1 
ATOM   8015  C CZ    . ARG A 1 2340 ? 176.409 204.886 173.105 1.00 26.14  ? 2340 ARG A CZ    1 
ATOM   8016  N NH1   . ARG A 1 2340 ? 175.985 205.622 172.091 1.00 26.14  ? 2340 ARG A NH1   1 
ATOM   8017  N NH2   . ARG A 1 2340 ? 177.173 205.443 174.039 1.00 26.14  ? 2340 ARG A NH2   1 
ATOM   8018  N N     . ILE A 1 2341 ? 172.358 199.576 169.823 1.00 22.94  ? 2341 ILE A N     1 
ATOM   8019  C CA    . ILE A 1 2341 ? 171.468 198.523 169.351 1.00 22.94  ? 2341 ILE A CA    1 
ATOM   8020  C C     . ILE A 1 2341 ? 171.080 197.667 170.549 1.00 22.94  ? 2341 ILE A C     1 
ATOM   8021  O O     . ILE A 1 2341 ? 171.879 196.859 171.031 1.00 22.94  ? 2341 ILE A O     1 
ATOM   8022  C CB    . ILE A 1 2341 ? 172.129 197.681 168.253 1.00 22.94  ? 2341 ILE A CB    1 
ATOM   8023  C CG1   . ILE A 1 2341 ? 172.501 198.565 167.062 1.00 22.94  ? 2341 ILE A CG1   1 
ATOM   8024  C CG2   . ILE A 1 2341 ? 171.208 196.556 167.820 1.00 22.94  ? 2341 ILE A CG2   1 
ATOM   8025  C CD1   . ILE A 1 2341 ? 172.855 197.794 165.816 1.00 22.94  ? 2341 ILE A CD1   1 
ATOM   8026  N N     . MET A 1 2342 ? 169.850 197.829 171.025 1.00 21.52  ? 2342 MET A N     1 
ATOM   8027  C CA    . MET A 1 2342 ? 169.364 197.100 172.187 1.00 21.52  ? 2342 MET A CA    1 
ATOM   8028  C C     . MET A 1 2342 ? 168.581 195.866 171.764 1.00 21.52  ? 2342 MET A C     1 
ATOM   8029  O O     . MET A 1 2342 ? 167.803 195.905 170.807 1.00 21.52  ? 2342 MET A O     1 
ATOM   8030  C CB    . MET A 1 2342 ? 168.482 197.985 173.067 1.00 21.52  ? 2342 MET A CB    1 
ATOM   8031  C CG    . MET A 1 2342 ? 169.214 199.117 173.753 1.00 21.52  ? 2342 MET A CG    1 
ATOM   8032  S SD    . MET A 1 2342 ? 168.094 200.103 174.759 1.00 21.52  ? 2342 MET A SD    1 
ATOM   8033  C CE    . MET A 1 2342 ? 169.196 201.379 175.348 1.00 21.52  ? 2342 MET A CE    1 
ATOM   8034  N N     . PHE A 1 2343 ? 168.796 194.771 172.486 1.00 22.84  ? 2343 PHE A N     1 
ATOM   8035  C CA    . PHE A 1 2343 ? 168.060 193.525 172.299 1.00 22.84  ? 2343 PHE A CA    1 
ATOM   8036  C C     . PHE A 1 2343 ? 167.195 193.321 173.537 1.00 22.84  ? 2343 PHE A C     1 
ATOM   8037  O O     . PHE A 1 2343 ? 167.701 192.969 174.606 1.00 22.84  ? 2343 PHE A O     1 
ATOM   8038  C CB    . PHE A 1 2343 ? 169.007 192.348 172.092 1.00 22.84  ? 2343 PHE A CB    1 
ATOM   8039  C CG    . PHE A 1 2343 ? 169.721 192.357 170.773 1.00 22.84  ? 2343 PHE A CG    1 
ATOM   8040  C CD1   . PHE A 1 2343 ? 170.726 193.273 170.519 1.00 22.84  ? 2343 PHE A CD1   1 
ATOM   8041  C CD2   . PHE A 1 2343 ? 169.403 191.433 169.794 1.00 22.84  ? 2343 PHE A CD2   1 
ATOM   8042  C CE1   . PHE A 1 2343 ? 171.388 193.278 169.310 1.00 22.84  ? 2343 PHE A CE1   1 
ATOM   8043  C CE2   . PHE A 1 2343 ? 170.063 191.433 168.583 1.00 22.84  ? 2343 PHE A CE2   1 
ATOM   8044  C CZ    . PHE A 1 2343 ? 171.057 192.356 168.341 1.00 22.84  ? 2343 PHE A CZ    1 
ATOM   8045  N N     . GLU A 1 2344 ? 165.891 193.547 173.397 1.00 18.71  ? 2344 GLU A N     1 
ATOM   8046  C CA    . GLU A 1 2344 ? 164.948 193.314 174.489 1.00 18.71  ? 2344 GLU A CA    1 
ATOM   8047  C C     . GLU A 1 2344 ? 164.315 191.948 174.267 1.00 18.71  ? 2344 GLU A C     1 
ATOM   8048  O O     . GLU A 1 2344 ? 163.266 191.819 173.635 1.00 18.71  ? 2344 GLU A O     1 
ATOM   8049  C CB    . GLU A 1 2344 ? 163.903 194.420 174.549 1.00 18.71  ? 2344 GLU A CB    1 
ATOM   8050  C CG    . GLU A 1 2344 ? 163.002 194.353 175.769 1.00 18.71  ? 2344 GLU A CG    1 
ATOM   8051  C CD    . GLU A 1 2344 ? 161.891 195.380 175.729 1.00 18.71  ? 2344 GLU A CD    1 
ATOM   8052  O OE1   . GLU A 1 2344 ? 162.193 196.578 175.551 1.00 18.71  ? 2344 GLU A OE1   1 
ATOM   8053  O OE2   . GLU A 1 2344 ? 160.714 194.992 175.883 1.00 18.71  ? 2344 GLU A OE2   1 
ATOM   8054  N N     . VAL A 1 2345 ? 164.961 190.911 174.795 1.00 19.74  ? 2345 VAL A N     1 
ATOM   8055  C CA    . VAL A 1 2345 ? 164.493 189.542 174.611 1.00 19.74  ? 2345 VAL A CA    1 
ATOM   8056  C C     . VAL A 1 2345 ? 164.004 189.003 175.946 1.00 19.74  ? 2345 VAL A C     1 
ATOM   8057  O O     . VAL A 1 2345 ? 164.075 189.692 176.969 1.00 19.74  ? 2345 VAL A O     1 
ATOM   8058  C CB    . VAL A 1 2345 ? 165.595 188.645 174.019 1.00 19.74  ? 2345 VAL A CB    1 
ATOM   8059  C CG1   . VAL A 1 2345 ? 166.042 189.175 172.667 1.00 19.74  ? 2345 VAL A CG1   1 
ATOM   8060  C CG2   . VAL A 1 2345 ? 166.763 188.553 174.967 1.00 19.74  ? 2345 VAL A CG2   1 
ATOM   8061  N N     . GLN A 1 2346 ? 163.500 187.771 175.946 1.00 19.58  ? 2346 GLN A N     1 
ATOM   8062  C CA    . GLN A 1 2346 ? 162.875 187.182 177.122 1.00 19.58  ? 2346 GLN A CA    1 
ATOM   8063  C C     . GLN A 1 2346 ? 163.701 186.072 177.755 1.00 19.58  ? 2346 GLN A C     1 
ATOM   8064  O O     . GLN A 1 2346 ? 163.983 186.120 178.955 1.00 19.58  ? 2346 GLN A O     1 
ATOM   8065  C CB    . GLN A 1 2346 ? 161.486 186.642 176.756 1.00 19.58  ? 2346 GLN A CB    1 
ATOM   8066  C CG    . GLN A 1 2346 ? 160.730 186.039 177.924 1.00 19.58  ? 2346 GLN A CG    1 
ATOM   8067  C CD    . GLN A 1 2346 ? 159.586 185.152 177.478 1.00 19.58  ? 2346 GLN A CD    1 
ATOM   8068  O OE1   . GLN A 1 2346 ? 159.345 184.983 176.283 1.00 19.58  ? 2346 GLN A OE1   1 
ATOM   8069  N NE2   . GLN A 1 2346 ? 158.875 184.575 178.439 1.00 19.58  ? 2346 GLN A NE2   1 
ATOM   8070  N N     . ASP A 1 2347 ? 164.100 185.068 176.980 1.00 26.39  ? 2347 ASP A N     1 
ATOM   8071  C CA    . ASP A 1 2347 ? 164.739 183.883 177.532 1.00 26.39  ? 2347 ASP A CA    1 
ATOM   8072  C C     . ASP A 1 2347 ? 166.201 183.717 177.148 1.00 26.39  ? 2347 ASP A C     1 
ATOM   8073  O O     . ASP A 1 2347 ? 166.953 183.122 177.923 1.00 26.39  ? 2347 ASP A O     1 
ATOM   8074  C CB    . ASP A 1 2347 ? 163.969 182.619 177.112 1.00 26.39  ? 2347 ASP A CB    1 
ATOM   8075  C CG    . ASP A 1 2347 ? 163.819 182.495 175.605 1.00 26.39  ? 2347 ASP A CG    1 
ATOM   8076  O OD1   . ASP A 1 2347 ? 162.972 181.692 175.161 1.00 26.39  ? 2347 ASP A OD1   1 
ATOM   8077  O OD2   . ASP A 1 2347 ? 164.537 183.198 174.863 1.00 26.39  ? 2347 ASP A OD2   1 
ATOM   8078  N N     . LEU A 1 2348 ? 166.621 184.221 175.985 1.00 26.87  ? 2348 LEU A N     1 
ATOM   8079  C CA    . LEU A 1 2348 ? 167.990 184.045 175.499 1.00 26.87  ? 2348 LEU A CA    1 
ATOM   8080  C C     . LEU A 1 2348 ? 168.360 182.564 175.431 1.00 26.87  ? 2348 LEU A C     1 
ATOM   8081  O O     . LEU A 1 2348 ? 169.443 182.146 175.843 1.00 26.87  ? 2348 LEU A O     1 
ATOM   8082  C CB    . LEU A 1 2348 ? 168.987 184.814 176.368 1.00 26.87  ? 2348 LEU A CB    1 
ATOM   8083  C CG    . LEU A 1 2348 ? 170.345 185.113 175.735 1.00 26.87  ? 2348 LEU A CG    1 
ATOM   8084  C CD1   . LEU A 1 2348 ? 170.187 185.942 174.473 1.00 26.87  ? 2348 LEU A CD1   1 
ATOM   8085  C CD2   . LEU A 1 2348 ? 171.254 185.789 176.731 1.00 26.87  ? 2348 LEU A CD2   1 
ATOM   8086  N N     . LYS A 1 2349 ? 167.437 181.761 174.910 1.00 31.55  ? 2349 LYS A N     1 
ATOM   8087  C CA    . LYS A 1 2349 ? 167.620 180.318 174.875 1.00 31.55  ? 2349 LYS A CA    1 
ATOM   8088  C C     . LYS A 1 2349 ? 168.130 179.807 173.538 1.00 31.55  ? 2349 LYS A C     1 
ATOM   8089  O O     . LYS A 1 2349 ? 168.745 178.737 173.492 1.00 31.55  ? 2349 LYS A O     1 
ATOM   8090  C CB    . LYS A 1 2349 ? 166.303 179.612 175.212 1.00 31.55  ? 2349 LYS A CB    1 
ATOM   8091  C CG    . LYS A 1 2349 ? 166.475 178.223 175.796 1.00 31.55  ? 2349 LYS A CG    1 
ATOM   8092  C CD    . LYS A 1 2349 ? 165.201 177.754 176.478 1.00 31.55  ? 2349 LYS A CD    1 
ATOM   8093  C CE    . LYS A 1 2349 ? 164.653 178.815 177.419 1.00 31.55  ? 2349 LYS A CE    1 
ATOM   8094  N NZ    . LYS A 1 2349 ? 165.415 178.869 178.698 1.00 31.55  ? 2349 LYS A NZ    1 
ATOM   8095  N N     . TYR A 1 2350 ? 167.891 180.538 172.454 1.00 37.74  ? 2350 TYR A N     1 
ATOM   8096  C CA    . TYR A 1 2350 ? 168.287 180.122 171.116 1.00 37.74  ? 2350 TYR A CA    1 
ATOM   8097  C C     . TYR A 1 2350 ? 169.228 181.140 170.484 1.00 37.74  ? 2350 TYR A C     1 
ATOM   8098  O O     . TYR A 1 2350 ? 169.097 181.486 169.310 1.00 37.74  ? 2350 TYR A O     1 
ATOM   8099  C CB    . TYR A 1 2350 ? 167.062 179.903 170.233 1.00 37.74  ? 2350 TYR A CB    1 
ATOM   8100  C CG    . TYR A 1 2350 ? 166.159 178.790 170.710 1.00 37.74  ? 2350 TYR A CG    1 
ATOM   8101  C CD1   . TYR A 1 2350 ? 165.150 179.036 171.631 1.00 37.74  ? 2350 TYR A CD1   1 
ATOM   8102  C CD2   . TYR A 1 2350 ? 166.319 177.492 170.245 1.00 37.74  ? 2350 TYR A CD2   1 
ATOM   8103  C CE1   . TYR A 1 2350 ? 164.323 178.023 172.073 1.00 37.74  ? 2350 TYR A CE1   1 
ATOM   8104  C CE2   . TYR A 1 2350 ? 165.497 176.472 170.681 1.00 37.74  ? 2350 TYR A CE2   1 
ATOM   8105  C CZ    . TYR A 1 2350 ? 164.501 176.743 171.595 1.00 37.74  ? 2350 TYR A CZ    1 
ATOM   8106  O OH    . TYR A 1 2350 ? 163.680 175.730 172.032 1.00 37.74  ? 2350 TYR A OH    1 
ATOM   8107  N N     . ALA A 1 2351 ? 170.188 181.636 171.258 1.00 36.35  ? 2351 ALA A N     1 
ATOM   8108  C CA    . ALA A 1 2351 ? 171.146 182.626 170.785 1.00 36.35  ? 2351 ALA A CA    1 
ATOM   8109  C C     . ALA A 1 2351 ? 172.549 182.042 170.841 1.00 36.35  ? 2351 ALA A C     1 
ATOM   8110  O O     . ALA A 1 2351 ? 172.935 181.440 171.848 1.00 36.35  ? 2351 ALA A O     1 
ATOM   8111  C CB    . ALA A 1 2351 ? 171.071 183.908 171.616 1.00 36.35  ? 2351 ALA A CB    1 
ATOM   8112  N N     . THR A 1 2352 ? 173.305 182.221 169.762 1.00 41.15  ? 2352 THR A N     1 
ATOM   8113  C CA    . THR A 1 2352 ? 174.677 181.742 169.717 1.00 41.15  ? 2352 THR A CA    1 
ATOM   8114  C C     . THR A 1 2352 ? 175.560 182.545 170.667 1.00 41.15  ? 2352 THR A C     1 
ATOM   8115  O O     . THR A 1 2352 ? 175.279 183.700 170.998 1.00 41.15  ? 2352 THR A O     1 
ATOM   8116  C CB    . THR A 1 2352 ? 175.235 181.828 168.297 1.00 41.15  ? 2352 THR A CB    1 
ATOM   8117  O OG1   . THR A 1 2352 ? 174.969 183.128 167.754 1.00 41.15  ? 2352 THR A OG1   1 
ATOM   8118  C CG2   . THR A 1 2352 ? 174.610 180.766 167.410 1.00 41.15  ? 2352 THR A CG2   1 
ATOM   8119  N N     . LEU A 1 2353 ? 176.648 181.908 171.108 1.00 42.23  ? 2353 LEU A N     1 
ATOM   8120  C CA    . LEU A 1 2353 ? 177.573 182.569 172.022 1.00 42.23  ? 2353 LEU A CA    1 
ATOM   8121  C C     . LEU A 1 2353 ? 178.255 183.762 171.368 1.00 42.23  ? 2353 LEU A C     1 
ATOM   8122  O O     . LEU A 1 2353 ? 178.692 184.683 172.066 1.00 42.23  ? 2353 LEU A O     1 
ATOM   8123  C CB    . LEU A 1 2353 ? 178.620 181.576 172.531 1.00 42.23  ? 2353 LEU A CB    1 
ATOM   8124  C CG    . LEU A 1 2353 ? 178.257 180.669 173.713 1.00 42.23  ? 2353 LEU A CG    1 
ATOM   8125  C CD1   . LEU A 1 2353 ? 178.003 181.501 174.963 1.00 42.23  ? 2353 LEU A CD1   1 
ATOM   8126  C CD2   . LEU A 1 2353 ? 177.070 179.760 173.412 1.00 42.23  ? 2353 LEU A CD2   1 
ATOM   8127  N N     . ALA A 1 2354 ? 178.358 183.764 170.036 1.00 41.10  ? 2354 ALA A N     1 
ATOM   8128  C CA    . ALA A 1 2354 ? 178.993 184.883 169.348 1.00 41.10  ? 2354 ALA A CA    1 
ATOM   8129  C C     . ALA A 1 2354 ? 178.221 186.178 169.565 1.00 41.10  ? 2354 ALA A C     1 
ATOM   8130  O O     . ALA A 1 2354 ? 178.818 187.228 169.830 1.00 41.10  ? 2354 ALA A O     1 
ATOM   8131  C CB    . ALA A 1 2354 ? 179.119 184.577 167.856 1.00 41.10  ? 2354 ALA A CB    1 
ATOM   8132  N N     . THR A 1 2355 ? 176.892 186.126 169.458 1.00 38.78  ? 2355 THR A N     1 
ATOM   8133  C CA    . THR A 1 2355 ? 176.090 187.327 169.663 1.00 38.78  ? 2355 THR A CA    1 
ATOM   8134  C C     . THR A 1 2355 ? 176.073 187.740 171.129 1.00 38.78  ? 2355 THR A C     1 
ATOM   8135  O O     . THR A 1 2355 ? 176.147 188.934 171.444 1.00 38.78  ? 2355 THR A O     1 
ATOM   8136  C CB    . THR A 1 2355 ? 174.667 187.101 169.154 1.00 38.78  ? 2355 THR A CB    1 
ATOM   8137  O OG1   . THR A 1 2355 ? 174.710 186.676 167.786 1.00 38.78  ? 2355 THR A OG1   1 
ATOM   8138  C CG2   . THR A 1 2355 ? 173.855 188.382 169.253 1.00 38.78  ? 2355 THR A CG2   1 
ATOM   8139  N N     . VAL A 1 2356 ? 175.975 186.769 172.039 1.00 36.27  ? 2356 VAL A N     1 
ATOM   8140  C CA    . VAL A 1 2356 ? 175.915 187.084 173.463 1.00 36.27  ? 2356 VAL A CA    1 
ATOM   8141  C C     . VAL A 1 2356 ? 177.217 187.720 173.933 1.00 36.27  ? 2356 VAL A C     1 
ATOM   8142  O O     . VAL A 1 2356 ? 177.207 188.705 174.681 1.00 36.27  ? 2356 VAL A O     1 
ATOM   8143  C CB    . VAL A 1 2356 ? 175.577 185.820 174.272 1.00 36.27  ? 2356 VAL A CB    1 
ATOM   8144  C CG1   . VAL A 1 2356 ? 175.462 186.151 175.748 1.00 36.27  ? 2356 VAL A CG1   1 
ATOM   8145  C CG2   . VAL A 1 2356 ? 174.291 185.197 173.763 1.00 36.27  ? 2356 VAL A CG2   1 
ATOM   8146  N N     . SER A 1 2357 ? 178.357 187.172 173.507 1.00 35.96  ? 2357 SER A N     1 
ATOM   8147  C CA    . SER A 1 2357 ? 179.647 187.682 173.957 1.00 35.96  ? 2357 SER A CA    1 
ATOM   8148  C C     . SER A 1 2357 ? 179.957 189.064 173.401 1.00 35.96  ? 2357 SER A C     1 
ATOM   8149  O O     . SER A 1 2357 ? 180.760 189.790 173.997 1.00 35.96  ? 2357 SER A O     1 
ATOM   8150  C CB    . SER A 1 2357 ? 180.758 186.706 173.569 1.00 35.96  ? 2357 SER A CB    1 
ATOM   8151  O OG    . SER A 1 2357 ? 180.595 186.259 172.235 1.00 35.96  ? 2357 SER A OG    1 
ATOM   8152  N N     . ARG A 1 2358 ? 179.347 189.445 172.284 1.00 39.36  ? 2358 ARG A N     1 
ATOM   8153  C CA    . ARG A 1 2358 ? 179.584 190.744 171.671 1.00 39.36  ? 2358 ARG A CA    1 
ATOM   8154  C C     . ARG A 1 2358 ? 178.732 191.851 172.275 1.00 39.36  ? 2358 ARG A C     1 
ATOM   8155  O O     . ARG A 1 2358 ? 178.899 193.015 171.896 1.00 39.36  ? 2358 ARG A O     1 
ATOM   8156  C CB    . ARG A 1 2358 ? 179.320 190.673 170.164 1.00 39.36  ? 2358 ARG A CB    1 
ATOM   8157  C CG    . ARG A 1 2358 ? 180.401 189.971 169.364 1.00 39.36  ? 2358 ARG A CG    1 
ATOM   8158  C CD    . ARG A 1 2358 ? 180.084 190.009 167.878 1.00 39.36  ? 2358 ARG A CD    1 
ATOM   8159  N NE    . ARG A 1 2358 ? 180.225 188.701 167.249 1.00 39.36  ? 2358 ARG A NE    1 
ATOM   8160  C CZ    . ARG A 1 2358 ? 181.378 188.181 166.851 1.00 39.36  ? 2358 ARG A CZ    1 
ATOM   8161  N NH1   . ARG A 1 2358 ? 182.519 188.834 166.997 1.00 39.36  ? 2358 ARG A NH1   1 
ATOM   8162  N NH2   . ARG A 1 2358 ? 181.385 186.975 166.291 1.00 39.36  ? 2358 ARG A NH2   1 
ATOM   8163  N N     . CYS A 1 2359 ? 177.831 191.525 173.197 1.00 33.96  ? 2359 CYS A N     1 
ATOM   8164  C CA    . CYS A 1 2359 ? 176.844 192.468 173.703 1.00 33.96  ? 2359 CYS A CA    1 
ATOM   8165  C C     . CYS A 1 2359 ? 176.939 192.577 175.217 1.00 33.96  ? 2359 CYS A C     1 
ATOM   8166  O O     . CYS A 1 2359 ? 176.974 191.559 175.916 1.00 33.96  ? 2359 CYS A O     1 
ATOM   8167  C CB    . CYS A 1 2359 ? 175.431 192.038 173.303 1.00 33.96  ? 2359 CYS A CB    1 
ATOM   8168  S SG    . CYS A 1 2359 ? 175.033 192.311 171.569 1.00 33.96  ? 2359 CYS A SG    1 
ATOM   8169  N N     . GLY A 1 2360 ? 176.980 193.810 175.718 1.00 24.91  ? 2360 GLY A N     1 
ATOM   8170  C CA    . GLY A 1 2360 ? 176.777 194.028 177.136 1.00 24.91  ? 2360 GLY A CA    1 
ATOM   8171  C C     . GLY A 1 2360 ? 175.350 193.708 177.536 1.00 24.91  ? 2360 GLY A C     1 
ATOM   8172  O O     . GLY A 1 2360 ? 174.414 193.850 176.750 1.00 24.91  ? 2360 GLY A O     1 
ATOM   8173  N N     . MET A 1 2361 ? 175.177 193.264 178.777 1.00 22.49  ? 2361 MET A N     1 
ATOM   8174  C CA    . MET A 1 2361 ? 173.920 192.651 179.176 1.00 22.49  ? 2361 MET A CA    1 
ATOM   8175  C C     . MET A 1 2361 ? 173.485 193.115 180.557 1.00 22.49  ? 2361 MET A C     1 
ATOM   8176  O O     . MET A 1 2361 ? 174.311 193.270 181.462 1.00 22.49  ? 2361 MET A O     1 
ATOM   8177  C CB    . MET A 1 2361 ? 174.045 191.130 179.166 1.00 22.49  ? 2361 MET A CB    1 
ATOM   8178  C CG    . MET A 1 2361 ? 172.759 190.391 179.443 1.00 22.49  ? 2361 MET A CG    1 
ATOM   8179  S SD    . MET A 1 2361 ? 173.067 188.629 179.386 1.00 22.49  ? 2361 MET A SD    1 
ATOM   8180  C CE    . MET A 1 2361 ? 173.306 188.446 177.625 1.00 22.49  ? 2361 MET A CE    1 
ATOM   8181  N N     . VAL A 1 2362 ? 172.181 193.335 180.705 1.00 15.79  ? 2362 VAL A N     1 
ATOM   8182  C CA    . VAL A 1 2362 ? 171.533 193.544 181.994 1.00 15.79  ? 2362 VAL A CA    1 
ATOM   8183  C C     . VAL A 1 2362 ? 170.393 192.542 182.105 1.00 15.79  ? 2362 VAL A C     1 
ATOM   8184  O O     . VAL A 1 2362 ? 169.552 192.454 181.203 1.00 15.79  ? 2362 VAL A O     1 
ATOM   8185  C CB    . VAL A 1 2362 ? 171.009 194.983 182.147 1.00 15.79  ? 2362 VAL A CB    1 
ATOM   8186  C CG1   . VAL A 1 2362 ? 170.383 195.173 183.516 1.00 15.79  ? 2362 VAL A CG1   1 
ATOM   8187  C CG2   . VAL A 1 2362 ? 172.126 195.984 181.926 1.00 15.79  ? 2362 VAL A CG2   1 
ATOM   8188  N N     . TRP A 1 2363 ? 170.362 191.792 183.203 1.00 13.81  ? 2363 TRP A N     1 
ATOM   8189  C CA    . TRP A 1 2363 ? 169.346 190.770 183.421 1.00 13.81  ? 2363 TRP A CA    1 
ATOM   8190  C C     . TRP A 1 2363 ? 168.243 191.323 184.311 1.00 13.81  ? 2363 TRP A C     1 
ATOM   8191  O O     . TRP A 1 2363 ? 168.511 191.779 185.427 1.00 13.81  ? 2363 TRP A O     1 
ATOM   8192  C CB    . TRP A 1 2363 ? 169.951 189.516 184.054 1.00 13.81  ? 2363 TRP A CB    1 
ATOM   8193  C CG    . TRP A 1 2363 ? 168.969 188.392 184.211 1.00 13.81  ? 2363 TRP A CG    1 
ATOM   8194  C CD1   . TRP A 1 2363 ? 168.074 188.225 185.226 1.00 13.81  ? 2363 TRP A CD1   1 
ATOM   8195  C CD2   . TRP A 1 2363 ? 168.792 187.273 183.335 1.00 13.81  ? 2363 TRP A CD2   1 
ATOM   8196  N NE1   . TRP A 1 2363 ? 167.346 187.078 185.033 1.00 13.81  ? 2363 TRP A NE1   1 
ATOM   8197  C CE2   . TRP A 1 2363 ? 167.768 186.475 183.879 1.00 13.81  ? 2363 TRP A CE2   1 
ATOM   8198  C CE3   . TRP A 1 2363 ? 169.396 186.871 182.141 1.00 13.81  ? 2363 TRP A CE3   1 
ATOM   8199  C CZ2   . TRP A 1 2363 ? 167.336 185.300 183.271 1.00 13.81  ? 2363 TRP A CZ2   1 
ATOM   8200  C CZ3   . TRP A 1 2363 ? 168.969 185.701 181.544 1.00 13.81  ? 2363 TRP A CZ3   1 
ATOM   8201  C CH2   . TRP A 1 2363 ? 167.947 184.932 182.106 1.00 13.81  ? 2363 TRP A CH2   1 
ATOM   8202  N N     . PHE A 1 2364 ? 167.008 191.268 183.821 1.00 10.63  ? 2364 PHE A N     1 
ATOM   8203  C CA    . PHE A 1 2364 ? 165.838 191.789 184.523 1.00 10.63  ? 2364 PHE A CA    1 
ATOM   8204  C C     . PHE A 1 2364 ? 165.041 190.608 185.071 1.00 10.63  ? 2364 PHE A C     1 
ATOM   8205  O O     . PHE A 1 2364 ? 164.121 190.111 184.423 1.00 10.63  ? 2364 PHE A O     1 
ATOM   8206  C CB    . PHE A 1 2364 ? 164.980 192.639 183.595 1.00 10.63  ? 2364 PHE A CB    1 
ATOM   8207  C CG    . PHE A 1 2364 ? 165.531 194.009 183.336 1.00 10.63  ? 2364 PHE A CG    1 
ATOM   8208  C CD1   . PHE A 1 2364 ? 166.426 194.228 182.306 1.00 10.63  ? 2364 PHE A CD1   1 
ATOM   8209  C CD2   . PHE A 1 2364 ? 165.136 195.082 184.111 1.00 10.63  ? 2364 PHE A CD2   1 
ATOM   8210  C CE1   . PHE A 1 2364 ? 166.925 195.490 182.063 1.00 10.63  ? 2364 PHE A CE1   1 
ATOM   8211  C CE2   . PHE A 1 2364 ? 165.629 196.344 183.871 1.00 10.63  ? 2364 PHE A CE2   1 
ATOM   8212  C CZ    . PHE A 1 2364 ? 166.526 196.549 182.848 1.00 10.63  ? 2364 PHE A CZ    1 
ATOM   8213  N N     . SER A 1 2365 ? 165.393 190.169 186.274 1.00 12.77  ? 2365 SER A N     1 
ATOM   8214  C CA    . SER A 1 2365 ? 164.643 189.105 186.922 1.00 12.77  ? 2365 SER A CA    1 
ATOM   8215  C C     . SER A 1 2365 ? 163.259 189.604 187.331 1.00 12.77  ? 2365 SER A C     1 
ATOM   8216  O O     . SER A 1 2365 ? 163.022 190.804 187.483 1.00 12.77  ? 2365 SER A O     1 
ATOM   8217  C CB    . SER A 1 2365 ? 165.399 188.585 188.141 1.00 12.77  ? 2365 SER A CB    1 
ATOM   8218  O OG    . SER A 1 2365 ? 165.549 189.605 189.111 1.00 12.77  ? 2365 SER A OG    1 
ATOM   8219  N N     . GLU A 1 2366 ? 162.331 188.660 187.499 1.00 13.08  ? 2366 GLU A N     1 
ATOM   8220  C CA    . GLU A 1 2366 ? 160.972 189.025 187.883 1.00 13.08  ? 2366 GLU A CA    1 
ATOM   8221  C C     . GLU A 1 2366 ? 160.904 189.637 189.275 1.00 13.08  ? 2366 GLU A C     1 
ATOM   8222  O O     . GLU A 1 2366 ? 159.981 190.409 189.552 1.00 13.08  ? 2366 GLU A O     1 
ATOM   8223  C CB    . GLU A 1 2366 ? 160.053 187.807 187.809 1.00 13.08  ? 2366 GLU A CB    1 
ATOM   8224  C CG    . GLU A 1 2366 ? 159.571 187.482 186.408 1.00 13.08  ? 2366 GLU A CG    1 
ATOM   8225  C CD    . GLU A 1 2366 ? 158.140 186.986 186.389 1.00 13.08  ? 2366 GLU A CD    1 
ATOM   8226  O OE1   . GLU A 1 2366 ? 157.355 187.401 187.267 1.00 13.08  ? 2366 GLU A OE1   1 
ATOM   8227  O OE2   . GLU A 1 2366 ? 157.798 186.181 185.498 1.00 13.08  ? 2366 GLU A OE2   1 
ATOM   8228  N N     . ASP A 1 2367 ? 161.854 189.313 190.155 1.00 16.01  ? 2367 ASP A N     1 
ATOM   8229  C CA    . ASP A 1 2367 ? 161.878 189.918 191.482 1.00 16.01  ? 2367 ASP A CA    1 
ATOM   8230  C C     . ASP A 1 2367 ? 162.146 191.414 191.425 1.00 16.01  ? 2367 ASP A C     1 
ATOM   8231  O O     . ASP A 1 2367 ? 161.889 192.117 192.408 1.00 16.01  ? 2367 ASP A O     1 
ATOM   8232  C CB    . ASP A 1 2367 ? 162.935 189.236 192.351 1.00 16.01  ? 2367 ASP A CB    1 
ATOM   8233  C CG    . ASP A 1 2367 ? 162.568 187.810 192.704 1.00 16.01  ? 2367 ASP A CG    1 
ATOM   8234  O OD1   . ASP A 1 2367 ? 161.359 187.509 192.787 1.00 16.01  ? 2367 ASP A OD1   1 
ATOM   8235  O OD2   . ASP A 1 2367 ? 163.488 186.990 192.901 1.00 16.01  ? 2367 ASP A OD2   1 
ATOM   8236  N N     . VAL A 1 2368 ? 162.666 191.910 190.301 1.00 14.27  ? 2368 VAL A N     1 
ATOM   8237  C CA    . VAL A 1 2368 ? 162.933 193.337 190.154 1.00 14.27  ? 2368 VAL A CA    1 
ATOM   8238  C C     . VAL A 1 2368 ? 161.639 194.136 190.225 1.00 14.27  ? 2368 VAL A C     1 
ATOM   8239  O O     . VAL A 1 2368 ? 161.563 195.165 190.906 1.00 14.27  ? 2368 VAL A O     1 
ATOM   8240  C CB    . VAL A 1 2368 ? 163.688 193.594 188.837 1.00 14.27  ? 2368 VAL A CB    1 
ATOM   8241  C CG1   . VAL A 1 2368 ? 163.864 195.070 188.607 1.00 14.27  ? 2368 VAL A CG1   1 
ATOM   8242  C CG2   . VAL A 1 2368 ? 165.038 192.901 188.865 1.00 14.27  ? 2368 VAL A CG2   1 
ATOM   8243  N N     . LEU A 1 2369 ? 160.602 193.674 189.534 1.00 12.50  ? 2369 LEU A N     1 
ATOM   8244  C CA    . LEU A 1 2369 ? 159.326 194.380 189.452 1.00 12.50  ? 2369 LEU A CA    1 
ATOM   8245  C C     . LEU A 1 2369 ? 158.343 193.705 190.403 1.00 12.50  ? 2369 LEU A C     1 
ATOM   8246  O O     . LEU A 1 2369 ? 157.732 192.689 190.064 1.00 12.50  ? 2369 LEU A O     1 
ATOM   8247  C CB    . LEU A 1 2369 ? 158.813 194.382 188.017 1.00 12.50  ? 2369 LEU A CB    1 
ATOM   8248  C CG    . LEU A 1 2369 ? 157.501 195.109 187.742 1.00 12.50  ? 2369 LEU A CG    1 
ATOM   8249  C CD1   . LEU A 1 2369 ? 157.596 196.556 188.176 1.00 12.50  ? 2369 LEU A CD1   1 
ATOM   8250  C CD2   . LEU A 1 2369 ? 157.172 195.018 186.271 1.00 12.50  ? 2369 LEU A CD2   1 
ATOM   8251  N N     . SER A 1 2370 ? 158.191 194.276 191.594 1.00 13.45  ? 2370 SER A N     1 
ATOM   8252  C CA    . SER A 1 2370 ? 157.321 193.699 192.605 1.00 13.45  ? 2370 SER A CA    1 
ATOM   8253  C C     . SER A 1 2370 ? 155.860 194.025 192.314 1.00 13.45  ? 2370 SER A C     1 
ATOM   8254  O O     . SER A 1 2370 ? 155.536 194.914 191.523 1.00 13.45  ? 2370 SER A O     1 
ATOM   8255  C CB    . SER A 1 2370 ? 157.706 194.203 193.995 1.00 13.45  ? 2370 SER A CB    1 
ATOM   8256  O OG    . SER A 1 2370 ? 157.646 195.616 194.057 1.00 13.45  ? 2370 SER A OG    1 
ATOM   8257  N N     . THR A 1 2371 ? 154.969 193.280 192.973 1.00 12.99  ? 2371 THR A N     1 
ATOM   8258  C CA    . THR A 1 2371 ? 153.538 193.450 192.745 1.00 12.99  ? 2371 THR A CA    1 
ATOM   8259  C C     . THR A 1 2371 ? 153.044 194.803 193.244 1.00 12.99  ? 2371 THR A C     1 
ATOM   8260  O O     . THR A 1 2371 ? 152.150 195.404 192.631 1.00 12.99  ? 2371 THR A O     1 
ATOM   8261  C CB    . THR A 1 2371 ? 152.767 192.317 193.422 1.00 12.99  ? 2371 THR A CB    1 
ATOM   8262  O OG1   . THR A 1 2371 ? 153.314 191.059 193.012 1.00 12.99  ? 2371 THR A OG1   1 
ATOM   8263  C CG2   . THR A 1 2371 ? 151.306 192.360 193.028 1.00 12.99  ? 2371 THR A CG2   1 
ATOM   8264  N N     . ASP A 1 2372 ? 153.606 195.296 194.351 1.00 15.17  ? 2372 ASP A N     1 
ATOM   8265  C CA    . ASP A 1 2372 ? 153.218 196.607 194.857 1.00 15.17  ? 2372 ASP A CA    1 
ATOM   8266  C C     . ASP A 1 2372 ? 153.478 197.691 193.822 1.00 15.17  ? 2372 ASP A C     1 
ATOM   8267  O O     . ASP A 1 2372 ? 152.728 198.668 193.732 1.00 15.17  ? 2372 ASP A O     1 
ATOM   8268  C CB    . ASP A 1 2372 ? 153.967 196.915 196.152 1.00 15.17  ? 2372 ASP A CB    1 
ATOM   8269  C CG    . ASP A 1 2372 ? 154.059 195.716 197.070 1.00 15.17  ? 2372 ASP A CG    1 
ATOM   8270  O OD1   . ASP A 1 2372 ? 153.000 195.177 197.454 1.00 15.17  ? 2372 ASP A OD1   1 
ATOM   8271  O OD2   . ASP A 1 2372 ? 155.192 195.312 197.408 1.00 15.17  ? 2372 ASP A OD2   1 
ATOM   8272  N N     . MET A 1 2373 ? 154.540 197.534 193.031 1.00 13.23  ? 2373 MET A N     1 
ATOM   8273  C CA    . MET A 1 2373 ? 154.822 198.483 191.961 1.00 13.23  ? 2373 MET A CA    1 
ATOM   8274  C C     . MET A 1 2373 ? 153.703 198.486 190.925 1.00 13.23  ? 2373 MET A C     1 
ATOM   8275  O O     . MET A 1 2373 ? 153.261 199.551 190.474 1.00 13.23  ? 2373 MET A O     1 
ATOM   8276  C CB    . MET A 1 2373 ? 156.163 198.132 191.320 1.00 13.23  ? 2373 MET A CB    1 
ATOM   8277  C CG    . MET A 1 2373 ? 157.347 198.326 192.256 1.00 13.23  ? 2373 MET A CG    1 
ATOM   8278  S SD    . MET A 1 2373 ? 158.931 197.832 191.553 1.00 13.23  ? 2373 MET A SD    1 
ATOM   8279  C CE    . MET A 1 2373 ? 159.188 199.108 190.333 1.00 13.23  ? 2373 MET A CE    1 
ATOM   8280  N N     . ILE A 1 2374 ? 153.220 197.297 190.553 1.00 10.96  ? 2374 ILE A N     1 
ATOM   8281  C CA    . ILE A 1 2374 ? 152.121 197.195 189.596 1.00 10.96  ? 2374 ILE A CA    1 
ATOM   8282  C C     . ILE A 1 2374 ? 150.868 197.852 190.159 1.00 10.96  ? 2374 ILE A C     1 
ATOM   8283  O O     . ILE A 1 2374 ? 150.162 198.591 189.461 1.00 10.96  ? 2374 ILE A O     1 
ATOM   8284  C CB    . ILE A 1 2374 ? 151.856 195.723 189.236 1.00 10.96  ? 2374 ILE A CB    1 
ATOM   8285  C CG1   . ILE A 1 2374 ? 153.162 194.994 188.932 1.00 10.96  ? 2374 ILE A CG1   1 
ATOM   8286  C CG2   . ILE A 1 2374 ? 150.922 195.635 188.045 1.00 10.96  ? 2374 ILE A CG2   1 
ATOM   8287  C CD1   . ILE A 1 2374 ? 153.867 195.513 187.723 1.00 10.96  ? 2374 ILE A CD1   1 
ATOM   8288  N N     . PHE A 1 2375 ? 150.566 197.575 191.430 1.00 13.19  ? 2375 PHE A N     1 
ATOM   8289  C CA    . PHE A 1 2375 ? 149.377 198.152 192.048 1.00 13.19  ? 2375 PHE A CA    1 
ATOM   8290  C C     . PHE A 1 2375 ? 149.468 199.671 192.108 1.00 13.19  ? 2375 PHE A C     1 
ATOM   8291  O O     . PHE A 1 2375 ? 148.484 200.371 191.837 1.00 13.19  ? 2375 PHE A O     1 
ATOM   8292  C CB    . PHE A 1 2375 ? 149.176 197.573 193.446 1.00 13.19  ? 2375 PHE A CB    1 
ATOM   8293  C CG    . PHE A 1 2375 ? 148.788 196.125 193.454 1.00 13.19  ? 2375 PHE A CG    1 
ATOM   8294  C CD1   . PHE A 1 2375 ? 148.372 195.498 192.294 1.00 13.19  ? 2375 PHE A CD1   1 
ATOM   8295  C CD2   . PHE A 1 2375 ? 148.836 195.391 194.625 1.00 13.19  ? 2375 PHE A CD2   1 
ATOM   8296  C CE1   . PHE A 1 2375 ? 148.013 194.168 192.301 1.00 13.19  ? 2375 PHE A CE1   1 
ATOM   8297  C CE2   . PHE A 1 2375 ? 148.478 194.061 194.638 1.00 13.19  ? 2375 PHE A CE2   1 
ATOM   8298  C CZ    . PHE A 1 2375 ? 148.065 193.449 193.475 1.00 13.19  ? 2375 PHE A CZ    1 
ATOM   8299  N N     . ASN A 1 2376 ? 150.640 200.198 192.468 1.00 15.19  ? 2376 ASN A N     1 
ATOM   8300  C CA    . ASN A 1 2376 ? 150.820 201.643 192.525 1.00 15.19  ? 2376 ASN A CA    1 
ATOM   8301  C C     . ASN A 1 2376 ? 150.651 202.273 191.151 1.00 15.19  ? 2376 ASN A C     1 
ATOM   8302  O O     . ASN A 1 2376 ? 150.016 203.325 191.019 1.00 15.19  ? 2376 ASN A O     1 
ATOM   8303  C CB    . ASN A 1 2376 ? 152.192 201.980 193.104 1.00 15.19  ? 2376 ASN A CB    1 
ATOM   8304  C CG    . ASN A 1 2376 ? 152.285 201.689 194.587 1.00 15.19  ? 2376 ASN A CG    1 
ATOM   8305  O OD1   . ASN A 1 2376 ? 151.305 201.286 195.214 1.00 15.19  ? 2376 ASN A OD1   1 
ATOM   8306  N ND2   . ASN A 1 2376 ? 153.466 201.893 195.157 1.00 15.19  ? 2376 ASN A ND2   1 
ATOM   8307  N N     . ASN A 1 2377 ? 151.213 201.646 190.114 1.00 14.20  ? 2377 ASN A N     1 
ATOM   8308  C CA    . ASN A 1 2377 ? 151.046 202.180 188.765 1.00 14.20  ? 2377 ASN A CA    1 
ATOM   8309  C C     . ASN A 1 2377 ? 149.583 202.172 188.345 1.00 14.20  ? 2377 ASN A C     1 
ATOM   8310  O O     . ASN A 1 2377 ? 149.089 203.150 187.769 1.00 14.20  ? 2377 ASN A O     1 
ATOM   8311  C CB    . ASN A 1 2377 ? 151.883 201.380 187.773 1.00 14.20  ? 2377 ASN A CB    1 
ATOM   8312  C CG    . ASN A 1 2377 ? 151.559 201.718 186.335 1.00 14.20  ? 2377 ASN A CG    1 
ATOM   8313  O OD1   . ASN A 1 2377 ? 151.098 200.869 185.575 1.00 14.20  ? 2377 ASN A OD1   1 
ATOM   8314  N ND2   . ASN A 1 2377 ? 151.803 202.963 185.952 1.00 14.20  ? 2377 ASN A ND2   1 
ATOM   8315  N N     . PHE A 1 2378 ? 148.874 201.076 188.625 1.00 14.86  ? 2378 PHE A N     1 
ATOM   8316  C CA    . PHE A 1 2378 ? 147.463 201.000 188.262 1.00 14.86  ? 2378 PHE A CA    1 
ATOM   8317  C C     . PHE A 1 2378 ? 146.655 202.073 188.976 1.00 14.86  ? 2378 PHE A C     1 
ATOM   8318  O O     . PHE A 1 2378 ? 145.827 202.751 188.357 1.00 14.86  ? 2378 PHE A O     1 
ATOM   8319  C CB    . PHE A 1 2378 ? 146.908 199.614 188.582 1.00 14.86  ? 2378 PHE A CB    1 
ATOM   8320  C CG    . PHE A 1 2378 ? 145.412 199.576 188.724 1.00 14.86  ? 2378 PHE A CG    1 
ATOM   8321  C CD1   . PHE A 1 2378 ? 144.592 199.839 187.640 1.00 14.86  ? 2378 PHE A CD1   1 
ATOM   8322  C CD2   . PHE A 1 2378 ? 144.826 199.276 189.942 1.00 14.86  ? 2378 PHE A CD2   1 
ATOM   8323  C CE1   . PHE A 1 2378 ? 143.218 199.805 187.769 1.00 14.86  ? 2378 PHE A CE1   1 
ATOM   8324  C CE2   . PHE A 1 2378 ? 143.452 199.239 190.076 1.00 14.86  ? 2378 PHE A CE2   1 
ATOM   8325  C CZ    . PHE A 1 2378 ? 142.648 199.504 188.989 1.00 14.86  ? 2378 PHE A CZ    1 
ATOM   8326  N N     . LEU A 1 2379 ? 146.891 202.252 190.277 1.00 14.96  ? 2379 LEU A N     1 
ATOM   8327  C CA    . LEU A 1 2379 ? 146.136 203.247 191.030 1.00 14.96  ? 2379 LEU A CA    1 
ATOM   8328  C C     . LEU A 1 2379 ? 146.462 204.662 190.566 1.00 14.96  ? 2379 LEU A C     1 
ATOM   8329  O O     . LEU A 1 2379 ? 145.567 205.509 190.474 1.00 14.96  ? 2379 LEU A O     1 
ATOM   8330  C CB    . LEU A 1 2379 ? 146.404 203.087 192.524 1.00 14.96  ? 2379 LEU A CB    1 
ATOM   8331  C CG    . LEU A 1 2379 ? 145.753 201.854 193.152 1.00 14.96  ? 2379 LEU A CG    1 
ATOM   8332  C CD1   . LEU A 1 2379 ? 146.173 201.694 194.601 1.00 14.96  ? 2379 LEU A CD1   1 
ATOM   8333  C CD2   . LEU A 1 2379 ? 144.243 201.937 193.038 1.00 14.96  ? 2379 LEU A CD2   1 
ATOM   8334  N N     . ALA A 1 2380 ? 147.733 204.940 190.264 1.00 16.63  ? 2380 ALA A N     1 
ATOM   8335  C CA    . ALA A 1 2380 ? 148.100 206.267 189.780 1.00 16.63  ? 2380 ALA A CA    1 
ATOM   8336  C C     . ALA A 1 2380 ? 147.461 206.561 188.429 1.00 16.63  ? 2380 ALA A C     1 
ATOM   8337  O O     . ALA A 1 2380 ? 146.946 207.663 188.205 1.00 16.63  ? 2380 ALA A O     1 
ATOM   8338  C CB    . ALA A 1 2380 ? 149.619 206.393 189.696 1.00 16.63  ? 2380 ALA A CB    1 
ATOM   8339  N N     . ARG A 1 2381 ? 147.480 205.587 187.515 1.00 15.81  ? 2381 ARG A N     1 
ATOM   8340  C CA    . ARG A 1 2381 ? 146.848 205.796 186.216 1.00 15.81  ? 2381 ARG A CA    1 
ATOM   8341  C C     . ARG A 1 2381 ? 145.339 205.949 186.355 1.00 15.81  ? 2381 ARG A C     1 
ATOM   8342  O O     . ARG A 1 2381 ? 144.720 206.731 185.624 1.00 15.81  ? 2381 ARG A O     1 
ATOM   8343  C CB    . ARG A 1 2381 ? 147.192 204.647 185.270 1.00 15.81  ? 2381 ARG A CB    1 
ATOM   8344  C CG    . ARG A 1 2381 ? 148.649 204.618 184.850 1.00 15.81  ? 2381 ARG A CG    1 
ATOM   8345  C CD    . ARG A 1 2381 ? 148.919 203.488 183.877 1.00 15.81  ? 2381 ARG A CD    1 
ATOM   8346  N NE    . ARG A 1 2381 ? 148.053 203.565 182.708 1.00 15.81  ? 2381 ARG A NE    1 
ATOM   8347  C CZ    . ARG A 1 2381 ? 148.289 204.332 181.654 1.00 15.81  ? 2381 ARG A CZ    1 
ATOM   8348  N NH1   . ARG A 1 2381 ? 149.360 205.105 181.588 1.00 15.81  ? 2381 ARG A NH1   1 
ATOM   8349  N NH2   . ARG A 1 2381 ? 147.430 204.323 180.639 1.00 15.81  ? 2381 ARG A NH2   1 
ATOM   8350  N N     . LEU A 1 2382 ? 144.729 205.207 187.282 1.00 18.96  ? 2382 LEU A N     1 
ATOM   8351  C CA    . LEU A 1 2382 ? 143.304 205.372 187.543 1.00 18.96  ? 2382 LEU A CA    1 
ATOM   8352  C C     . LEU A 1 2382 ? 142.997 206.768 188.067 1.00 18.96  ? 2382 LEU A C     1 
ATOM   8353  O O     . LEU A 1 2382 ? 142.013 207.392 187.655 1.00 18.96  ? 2382 LEU A O     1 
ATOM   8354  C CB    . LEU A 1 2382 ? 142.832 204.310 188.536 1.00 18.96  ? 2382 LEU A CB    1 
ATOM   8355  C CG    . LEU A 1 2382 ? 141.325 204.130 188.701 1.00 18.96  ? 2382 LEU A CG    1 
ATOM   8356  C CD1   . LEU A 1 2382 ? 140.714 203.579 187.429 1.00 18.96  ? 2382 LEU A CD1   1 
ATOM   8357  C CD2   . LEU A 1 2382 ? 141.031 203.214 189.875 1.00 18.96  ? 2382 LEU A CD2   1 
ATOM   8358  N N     . ARG A 1 2383 ? 143.831 207.275 188.975 1.00 19.77  ? 2383 ARG A N     1 
ATOM   8359  C CA    . ARG A 1 2383 ? 143.594 208.581 189.573 1.00 19.77  ? 2383 ARG A CA    1 
ATOM   8360  C C     . ARG A 1 2383 ? 143.941 209.733 188.643 1.00 19.77  ? 2383 ARG A C     1 
ATOM   8361  O O     . ARG A 1 2383 ? 143.473 210.853 188.872 1.00 19.77  ? 2383 ARG A O     1 
ATOM   8362  C CB    . ARG A 1 2383 ? 144.396 208.716 190.868 1.00 19.77  ? 2383 ARG A CB    1 
ATOM   8363  C CG    . ARG A 1 2383 ? 143.829 207.927 192.031 1.00 19.77  ? 2383 ARG A CG    1 
ATOM   8364  C CD    . ARG A 1 2383 ? 144.275 208.507 193.359 1.00 19.77  ? 2383 ARG A CD    1 
ATOM   8365  N NE    . ARG A 1 2383 ? 144.041 207.583 194.461 1.00 19.77  ? 2383 ARG A NE    1 
ATOM   8366  C CZ    . ARG A 1 2383 ? 144.949 206.742 194.936 1.00 19.77  ? 2383 ARG A CZ    1 
ATOM   8367  N NH1   . ARG A 1 2383 ? 146.167 206.678 194.424 1.00 19.77  ? 2383 ARG A NH1   1 
ATOM   8368  N NH2   . ARG A 1 2383 ? 144.628 205.947 195.952 1.00 19.77  ? 2383 ARG A NH2   1 
ATOM   8369  N N     . SER A 1 2384 ? 144.744 209.496 187.608 1.00 19.72  ? 2384 SER A N     1 
ATOM   8370  C CA    . SER A 1 2384 ? 145.181 210.565 186.718 1.00 19.72  ? 2384 SER A CA    1 
ATOM   8371  C C     . SER A 1 2384 ? 144.575 210.480 185.325 1.00 19.72  ? 2384 SER A C     1 
ATOM   8372  O O     . SER A 1 2384 ? 143.960 211.445 184.862 1.00 19.72  ? 2384 SER A O     1 
ATOM   8373  C CB    . SER A 1 2384 ? 146.712 210.564 186.616 1.00 19.72  ? 2384 SER A CB    1 
ATOM   8374  O OG    . SER A 1 2384 ? 147.304 210.856 187.869 1.00 19.72  ? 2384 SER A OG    1 
ATOM   8375  N N     . ILE A 1 2385 ? 144.732 209.353 184.639 1.00 23.21  ? 2385 ILE A N     1 
ATOM   8376  C CA    . ILE A 1 2385 ? 144.267 209.220 183.260 1.00 23.21  ? 2385 ILE A CA    1 
ATOM   8377  C C     . ILE A 1 2385 ? 142.758 209.007 183.242 1.00 23.21  ? 2385 ILE A C     1 
ATOM   8378  O O     . ILE A 1 2385 ? 142.260 208.047 183.849 1.00 23.21  ? 2385 ILE A O     1 
ATOM   8379  C CB    . ILE A 1 2385 ? 144.991 208.073 182.537 1.00 23.21  ? 2385 ILE A CB    1 
ATOM   8380  C CG1   . ILE A 1 2385 ? 146.445 208.452 182.254 1.00 23.21  ? 2385 ILE A CG1   1 
ATOM   8381  C CG2   . ILE A 1 2385 ? 144.274 207.723 181.244 1.00 23.21  ? 2385 ILE A CG2   1 
ATOM   8382  C CD1   . ILE A 1 2385 ? 146.608 209.813 181.618 1.00 23.21  ? 2385 ILE A CD1   1 
ATOM   8383  N N     . PRO A 1 2386 ? 141.994 209.867 182.570 1.00 26.52  ? 2386 PRO A N     1 
ATOM   8384  C CA    . PRO A 1 2386 ? 140.551 209.629 182.453 1.00 26.52  ? 2386 PRO A CA    1 
ATOM   8385  C C     . PRO A 1 2386 ? 140.261 208.493 181.486 1.00 26.52  ? 2386 PRO A C     1 
ATOM   8386  O O     . PRO A 1 2386 ? 140.853 208.403 180.408 1.00 26.52  ? 2386 PRO A O     1 
ATOM   8387  C CB    . PRO A 1 2386 ? 140.006 210.964 181.927 1.00 26.52  ? 2386 PRO A CB    1 
ATOM   8388  C CG    . PRO A 1 2386 ? 141.143 211.945 182.040 1.00 26.52  ? 2386 PRO A CG    1 
ATOM   8389  C CD    . PRO A 1 2386 ? 142.394 211.141 181.957 1.00 26.52  ? 2386 PRO A CD    1 
ATOM   8390  N N     . LEU A 1 2387 ? 139.335 207.614 181.877 1.00 27.83  ? 2387 LEU A N     1 
ATOM   8391  C CA    . LEU A 1 2387 ? 138.996 206.446 181.026 1.00 27.83  ? 2387 LEU A CA    1 
ATOM   8392  C C     . LEU A 1 2387 ? 138.201 206.922 179.805 1.00 27.83  ? 2387 LEU A C     1 
ATOM   8393  O O     . LEU A 1 2387 ? 137.356 206.147 179.313 1.00 27.83  ? 2387 LEU A O     1 
ATOM   8394  C CB    . LEU A 1 2387 ? 138.204 205.434 181.850 1.00 27.83  ? 2387 LEU A CB    1 
ATOM   8395  C CG    . LEU A 1 2387 ? 138.996 204.704 182.937 1.00 27.83  ? 2387 LEU A CG    1 
ATOM   8396  C CD1   . LEU A 1 2387 ? 138.075 203.887 183.821 1.00 27.83  ? 2387 LEU A CD1   1 
ATOM   8397  C CD2   . LEU A 1 2387 ? 140.054 203.831 182.297 1.00 27.83  ? 2387 LEU A CD2   1 
ATOM   8398  N N     . ASP A 1 2388 ? 138.456 208.150 179.347 1.00 33.44  ? 2388 ASP A N     1 
ATOM   8399  C CA    . ASP A 1 2388 ? 137.751 208.695 178.153 1.00 33.44  ? 2388 ASP A CA    1 
ATOM   8400  C C     . ASP A 1 2388 ? 138.748 209.469 177.285 1.00 33.44  ? 2388 ASP A C     1 
ATOM   8401  O O     . ASP A 1 2388 ? 139.294 210.469 177.800 1.00 33.44  ? 2388 ASP A O     1 
ATOM   8402  C CB    . ASP A 1 2388 ? 136.557 209.546 178.555 1.00 30.00  ? 2388 ASP A CB    1 
ATOM   8403  C CG    . ASP A 1 2388 ? 136.362 209.726 180.053 1.00 30.00  ? 2388 ASP A CG    1 
ATOM   8404  O OD1   . ASP A 1 2388 ? 135.794 208.810 180.682 1.00 30.00  ? 2388 ASP A OD1   1 
ATOM   8405  O OD2   . ASP A 1 2388 ? 136.785 210.777 180.576 1.00 30.00  ? 2388 ASP A OD2   1 
ATOM   8406  N N     . SER A 1 2410 ? 135.964 215.294 183.483 1.00 45.89  ? 2410 SER A N     1 
ATOM   8407  C CA    . SER A 1 2410 ? 136.211 215.566 184.896 1.00 45.89  ? 2410 SER A CA    1 
ATOM   8408  C C     . SER A 1 2410 ? 135.322 214.743 185.845 1.00 45.89  ? 2410 SER A C     1 
ATOM   8409  O O     . SER A 1 2410 ? 135.833 214.197 186.823 1.00 45.89  ? 2410 SER A O     1 
ATOM   8410  C CB    . SER A 1 2410 ? 136.049 217.062 185.187 1.00 45.89  ? 2410 SER A CB    1 
ATOM   8411  O OG    . SER A 1 2410 ? 136.281 217.340 186.557 1.00 45.89  ? 2410 SER A OG    1 
ATOM   8412  N N     . PRO A 1 2411 ? 134.006 214.659 185.591 1.00 44.86  ? 2411 PRO A N     1 
ATOM   8413  C CA    . PRO A 1 2411 ? 133.186 213.763 186.428 1.00 44.86  ? 2411 PRO A CA    1 
ATOM   8414  C C     . PRO A 1 2411 ? 133.645 212.318 186.371 1.00 44.86  ? 2411 PRO A C     1 
ATOM   8415  O O     . PRO A 1 2411 ? 133.610 211.615 187.391 1.00 44.86  ? 2411 PRO A O     1 
ATOM   8416  C CB    . PRO A 1 2411 ? 131.772 213.941 185.854 1.00 44.86  ? 2411 PRO A CB    1 
ATOM   8417  C CG    . PRO A 1 2411 ? 131.980 214.477 184.483 1.00 44.86  ? 2411 PRO A CG    1 
ATOM   8418  C CD    . PRO A 1 2411 ? 133.170 215.366 184.603 1.00 44.86  ? 2411 PRO A CD    1 
ATOM   8419  N N     . MET A 1 2412 ? 134.088 211.855 185.200 1.00 38.99  ? 2412 MET A N     1 
ATOM   8420  C CA    . MET A 1 2412 ? 134.680 210.526 185.110 1.00 38.99  ? 2412 MET A CA    1 
ATOM   8421  C C     . MET A 1 2412 ? 135.947 210.441 185.949 1.00 38.99  ? 2412 MET A C     1 
ATOM   8422  O O     . MET A 1 2412 ? 136.204 209.421 186.597 1.00 38.99  ? 2412 MET A O     1 
ATOM   8423  C CB    . MET A 1 2412 ? 134.972 210.175 183.652 1.00 38.99  ? 2412 MET A CB    1 
ATOM   8424  N N     . LEU A 1 2413 ? 136.751 211.507 185.950 1.00 34.72  ? 2413 LEU A N     1 
ATOM   8425  C CA    . LEU A 1 2413 ? 137.938 211.539 186.798 1.00 34.72  ? 2413 LEU A CA    1 
ATOM   8426  C C     . LEU A 1 2413 ? 137.564 211.487 188.273 1.00 34.72  ? 2413 LEU A C     1 
ATOM   8427  O O     . LEU A 1 2413 ? 138.233 210.815 189.065 1.00 34.72  ? 2413 LEU A O     1 
ATOM   8428  C CB    . LEU A 1 2413 ? 138.765 212.789 186.499 1.00 34.72  ? 2413 LEU A CB    1 
ATOM   8429  C CG    . LEU A 1 2413 ? 139.823 212.645 185.406 1.00 34.72  ? 2413 LEU A CG    1 
ATOM   8430  C CD1   . LEU A 1 2413 ? 140.689 213.890 185.332 1.00 34.72  ? 2413 LEU A CD1   1 
ATOM   8431  C CD2   . LEU A 1 2413 ? 140.675 211.416 185.665 1.00 34.72  ? 2413 LEU A CD2   1 
ATOM   8432  N N     . GLN A 1 2414 ? 136.505 212.199 188.665 1.00 35.93  ? 2414 GLN A N     1 
ATOM   8433  C CA    . GLN A 1 2414 ? 136.058 212.151 190.054 1.00 35.93  ? 2414 GLN A CA    1 
ATOM   8434  C C     . GLN A 1 2414 ? 135.600 210.750 190.437 1.00 35.93  ? 2414 GLN A C     1 
ATOM   8435  O O     . GLN A 1 2414 ? 135.910 210.262 191.531 1.00 35.93  ? 2414 GLN A O     1 
ATOM   8436  C CB    . GLN A 1 2414 ? 134.936 213.163 190.280 1.00 35.93  ? 2414 GLN A CB    1 
ATOM   8437  C CG    . GLN A 1 2414 ? 134.481 213.266 191.725 1.00 35.93  ? 2414 GLN A CG    1 
ATOM   8438  C CD    . GLN A 1 2414 ? 135.591 213.713 192.654 1.00 35.93  ? 2414 GLN A CD    1 
ATOM   8439  O OE1   . GLN A 1 2414 ? 136.139 212.916 193.414 1.00 35.93  ? 2414 GLN A OE1   1 
ATOM   8440  N NE2   . GLN A 1 2414 ? 135.931 214.995 192.595 1.00 35.93  ? 2414 GLN A NE2   1 
ATOM   8441  N N     . ILE A 1 2415 ? 134.862 210.086 189.545 1.00 34.14  ? 2415 ILE A N     1 
ATOM   8442  C CA    . ILE A 1 2415 ? 134.426 208.717 189.809 1.00 34.14  ? 2415 ILE A CA    1 
ATOM   8443  C C     . ILE A 1 2415 ? 135.626 207.786 189.926 1.00 34.14  ? 2415 ILE A C     1 
ATOM   8444  O O     . ILE A 1 2415 ? 135.674 206.917 190.805 1.00 34.14  ? 2415 ILE A O     1 
ATOM   8445  C CB    . ILE A 1 2415 ? 133.447 208.251 188.716 1.00 34.14  ? 2415 ILE A CB    1 
ATOM   8446  C CG1   . ILE A 1 2415 ? 132.140 209.037 188.809 1.00 34.14  ? 2415 ILE A CG1   1 
ATOM   8447  C CG2   . ILE A 1 2415 ? 133.189 206.760 188.828 1.00 34.14  ? 2415 ILE A CG2   1 
ATOM   8448  C CD1   . ILE A 1 2415 ? 131.232 208.852 187.621 1.00 34.14  ? 2415 ILE A CD1   1 
ATOM   8449  N N     . GLN A 1 2416 ? 136.611 207.950 189.039 1.00 29.51  ? 2416 GLN A N     1 
ATOM   8450  C CA    . GLN A 1 2416 ? 137.809 207.118 189.095 1.00 29.51  ? 2416 GLN A CA    1 
ATOM   8451  C C     . GLN A 1 2416 ? 138.567 207.327 190.397 1.00 29.51  ? 2416 GLN A C     1 
ATOM   8452  O O     . GLN A 1 2416 ? 139.039 206.364 191.010 1.00 29.51  ? 2416 GLN A O     1 
ATOM   8453  C CB    . GLN A 1 2416 ? 138.712 207.419 187.900 1.00 29.51  ? 2416 GLN A CB    1 
ATOM   8454  C CG    . GLN A 1 2416 ? 138.222 206.852 186.584 1.00 29.51  ? 2416 GLN A CG    1 
ATOM   8455  C CD    . GLN A 1 2416 ? 139.030 207.352 185.405 1.00 29.51  ? 2416 GLN A CD    1 
ATOM   8456  O OE1   . GLN A 1 2416 ? 138.480 207.683 184.356 1.00 29.51  ? 2416 GLN A OE1   1 
ATOM   8457  N NE2   . GLN A 1 2416 ? 140.344 207.415 185.575 1.00 29.51  ? 2416 GLN A NE2   1 
ATOM   8458  N N     . ARG A 1 2417 ? 138.702 208.581 190.833 1.00 30.47  ? 2417 ARG A N     1 
ATOM   8459  C CA    . ARG A 1 2417 ? 139.402 208.860 192.082 1.00 30.47  ? 2417 ARG A CA    1 
ATOM   8460  C C     . ARG A 1 2417 ? 138.653 208.282 193.275 1.00 30.47  ? 2417 ARG A C     1 
ATOM   8461  O O     . ARG A 1 2417 ? 139.270 207.736 194.198 1.00 30.47  ? 2417 ARG A O     1 
ATOM   8462  C CB    . ARG A 1 2417 ? 139.607 210.365 192.243 1.00 30.47  ? 2417 ARG A CB    1 
ATOM   8463  C CG    . ARG A 1 2417 ? 140.582 210.955 191.239 1.00 30.47  ? 2417 ARG A CG    1 
ATOM   8464  C CD    . ARG A 1 2417 ? 140.723 212.456 191.404 1.00 30.47  ? 2417 ARG A CD    1 
ATOM   8465  N NE    . ARG A 1 2417 ? 141.627 213.023 190.412 1.00 30.47  ? 2417 ARG A NE    1 
ATOM   8466  C CZ    . ARG A 1 2417 ? 141.898 214.316 190.297 1.00 30.47  ? 2417 ARG A CZ    1 
ATOM   8467  N NH1   . ARG A 1 2417 ? 141.349 215.211 191.102 1.00 30.47  ? 2417 ARG A NH1   1 
ATOM   8468  N NH2   . ARG A 1 2417 ? 142.742 214.721 189.353 1.00 30.47  ? 2417 ARG A NH2   1 
ATOM   8469  N N     . ASP A 1 2418 ? 137.322 208.390 193.276 1.00 32.95  ? 2418 ASP A N     1 
ATOM   8470  C CA    . ASP A 1 2418 ? 136.539 207.798 194.357 1.00 32.95  ? 2418 ASP A CA    1 
ATOM   8471  C C     . ASP A 1 2418 ? 136.702 206.284 194.388 1.00 32.95  ? 2418 ASP A C     1 
ATOM   8472  O O     . ASP A 1 2418 ? 136.877 205.691 195.460 1.00 32.95  ? 2418 ASP A O     1 
ATOM   8473  C CB    . ASP A 1 2418 ? 135.067 208.176 194.206 1.00 32.95  ? 2418 ASP A CB    1 
ATOM   8474  C CG    . ASP A 1 2418 ? 134.809 209.639 194.498 1.00 32.95  ? 2418 ASP A CG    1 
ATOM   8475  O OD1   . ASP A 1 2418 ? 135.538 210.217 195.332 1.00 32.95  ? 2418 ASP A OD1   1 
ATOM   8476  O OD2   . ASP A 1 2418 ? 133.880 210.213 193.893 1.00 32.95  ? 2418 ASP A OD2   1 
ATOM   8477  N N     . ALA A 1 2419 ? 136.657 205.641 193.219 1.00 30.58  ? 2419 ALA A N     1 
ATOM   8478  C CA    . ALA A 1 2419 ? 136.835 204.194 193.163 1.00 30.58  ? 2419 ALA A CA    1 
ATOM   8479  C C     . ALA A 1 2419 ? 138.226 203.789 193.632 1.00 30.58  ? 2419 ALA A C     1 
ATOM   8480  O O     . ALA A 1 2419 ? 138.383 202.794 194.350 1.00 30.58  ? 2419 ALA A O     1 
ATOM   8481  C CB    . ALA A 1 2419 ? 136.576 203.687 191.745 1.00 30.58  ? 2419 ALA A CB    1 
ATOM   8482  N N     . ALA A 1 2420 ? 139.250 204.545 193.228 1.00 28.53  ? 2420 ALA A N     1 
ATOM   8483  C CA    . ALA A 1 2420 ? 140.609 204.249 193.665 1.00 28.53  ? 2420 ALA A CA    1 
ATOM   8484  C C     . ALA A 1 2420 ? 140.742 204.390 195.173 1.00 28.53  ? 2420 ALA A C     1 
ATOM   8485  O O     . ALA A 1 2420 ? 141.379 203.558 195.827 1.00 28.53  ? 2420 ALA A O     1 
ATOM   8486  C CB    . ALA A 1 2420 ? 141.602 205.163 192.951 1.00 28.53  ? 2420 ALA A CB    1 
ATOM   8487  N N     . THR A 1 2421 ? 140.145 205.437 195.744 1.00 29.65  ? 2421 THR A N     1 
ATOM   8488  C CA    . THR A 1 2421 ? 140.167 205.598 197.194 1.00 29.65  ? 2421 THR A CA    1 
ATOM   8489  C C     . THR A 1 2421 ? 139.468 204.432 197.882 1.00 29.65  ? 2421 THR A C     1 
ATOM   8490  O O     . THR A 1 2421 ? 139.939 203.934 198.911 1.00 29.65  ? 2421 THR A O     1 
ATOM   8491  C CB    . THR A 1 2421 ? 139.513 206.925 197.581 1.00 29.65  ? 2421 THR A CB    1 
ATOM   8492  O OG1   . THR A 1 2421 ? 140.318 208.012 197.107 1.00 29.65  ? 2421 THR A OG1   1 
ATOM   8493  C CG2   . THR A 1 2421 ? 139.369 207.034 199.090 1.00 29.65  ? 2421 THR A CG2   1 
ATOM   8494  N N     . ILE A 1 2422 ? 138.346 203.979 197.320 1.00 28.55  ? 2422 ILE A N     1 
ATOM   8495  C CA    . ILE A 1 2422 ? 137.606 202.871 197.917 1.00 28.55  ? 2422 ILE A CA    1 
ATOM   8496  C C     . ILE A 1 2422 ? 138.422 201.584 197.878 1.00 28.55  ? 2422 ILE A C     1 
ATOM   8497  O O     . ILE A 1 2422 ? 138.482 200.843 198.866 1.00 28.55  ? 2422 ILE A O     1 
ATOM   8498  C CB    . ILE A 1 2422 ? 136.247 202.705 197.213 1.00 28.55  ? 2422 ILE A CB    1 
ATOM   8499  C CG1   . ILE A 1 2422 ? 135.326 203.874 197.560 1.00 28.55  ? 2422 ILE A CG1   1 
ATOM   8500  C CG2   . ILE A 1 2422 ? 135.600 201.388 197.599 1.00 28.55  ? 2422 ILE A CG2   1 
ATOM   8501  C CD1   . ILE A 1 2422 ? 134.121 203.984 196.662 1.00 28.55  ? 2422 ILE A CD1   1 
ATOM   8502  N N     . MET A 1 2423 ? 139.063 201.296 196.747 1.00 27.10  ? 2423 MET A N     1 
ATOM   8503  C CA    . MET A 1 2423 ? 139.753 200.024 196.559 1.00 27.10  ? 2423 MET A CA    1 
ATOM   8504  C C     . MET A 1 2423 ? 141.214 200.055 196.990 1.00 27.10  ? 2423 MET A C     1 
ATOM   8505  O O     . MET A 1 2423 ? 141.890 199.027 196.894 1.00 27.10  ? 2423 MET A O     1 
ATOM   8506  C CB    . MET A 1 2423 ? 139.666 199.585 195.094 1.00 27.10  ? 2423 MET A CB    1 
ATOM   8507  C CG    . MET A 1 2423 ? 140.519 200.407 194.148 1.00 27.10  ? 2423 MET A CG    1 
ATOM   8508  S SD    . MET A 1 2423 ? 140.322 199.900 192.430 1.00 27.10  ? 2423 MET A SD    1 
ATOM   8509  C CE    . MET A 1 2423 ? 138.723 200.606 192.052 1.00 27.10  ? 2423 MET A CE    1 
ATOM   8510  N N     . GLN A 1 2424 ? 141.717 201.200 197.448 1.00 24.84  ? 2424 GLN A N     1 
ATOM   8511  C CA    . GLN A 1 2424 ? 143.106 201.276 197.899 1.00 24.84  ? 2424 GLN A CA    1 
ATOM   8512  C C     . GLN A 1 2424 ? 143.439 200.301 199.023 1.00 24.84  ? 2424 GLN A C     1 
ATOM   8513  O O     . GLN A 1 2424 ? 144.506 199.666 198.954 1.00 24.84  ? 2424 GLN A O     1 
ATOM   8514  C CB    . GLN A 1 2424 ? 143.427 202.721 198.298 1.00 24.84  ? 2424 GLN A CB    1 
ATOM   8515  C CG    . GLN A 1 2424 ? 144.712 202.883 199.084 1.00 24.84  ? 2424 GLN A CG    1 
ATOM   8516  C CD    . GLN A 1 2424 ? 145.888 203.232 198.197 1.00 24.84  ? 2424 GLN A CD    1 
ATOM   8517  O OE1   . GLN A 1 2424 ? 145.803 204.132 197.362 1.00 24.84  ? 2424 GLN A OE1   1 
ATOM   8518  N NE2   . GLN A 1 2424 ? 146.994 202.518 198.371 1.00 24.84  ? 2424 GLN A NE2   1 
ATOM   8519  N N     . PRO A 1 2425 ? 142.618 200.132 200.069 1.00 24.90  ? 2425 PRO A N     1 
ATOM   8520  C CA    . PRO A 1 2425 ? 143.010 199.205 201.146 1.00 24.90  ? 2425 PRO A CA    1 
ATOM   8521  C C     . PRO A 1 2425 ? 143.251 197.780 200.681 1.00 24.90  ? 2425 PRO A C     1 
ATOM   8522  O O     . PRO A 1 2425 ? 144.083 197.080 201.272 1.00 24.90  ? 2425 PRO A O     1 
ATOM   8523  C CB    . PRO A 1 2425 ? 141.827 199.284 202.120 1.00 24.90  ? 2425 PRO A CB    1 
ATOM   8524  C CG    . PRO A 1 2425 ? 141.249 200.621 201.889 1.00 24.90  ? 2425 PRO A CG    1 
ATOM   8525  C CD    . PRO A 1 2425 ? 141.388 200.866 200.420 1.00 24.90  ? 2425 PRO A CD    1 
ATOM   8526  N N     . TYR A 1 2426 ? 142.549 197.322 199.646 1.00 28.32  ? 2426 TYR A N     1 
ATOM   8527  C CA    . TYR A 1 2426 ? 142.728 195.956 199.171 1.00 28.32  ? 2426 TYR A CA    1 
ATOM   8528  C C     . TYR A 1 2426 ? 143.996 195.773 198.349 1.00 28.32  ? 2426 TYR A C     1 
ATOM   8529  O O     . TYR A 1 2426 ? 144.471 194.640 198.216 1.00 28.32  ? 2426 TYR A O     1 
ATOM   8530  C CB    . TYR A 1 2426 ? 141.510 195.525 198.354 1.00 28.32  ? 2426 TYR A CB    1 
ATOM   8531  C CG    . TYR A 1 2426 ? 140.239 195.469 199.168 1.00 28.32  ? 2426 TYR A CG    1 
ATOM   8532  C CD1   . TYR A 1 2426 ? 139.202 196.363 198.940 1.00 28.32  ? 2426 TYR A CD1   1 
ATOM   8533  C CD2   . TYR A 1 2426 ? 140.080 194.524 200.172 1.00 28.32  ? 2426 TYR A CD2   1 
ATOM   8534  C CE1   . TYR A 1 2426 ? 138.042 196.313 199.687 1.00 28.32  ? 2426 TYR A CE1   1 
ATOM   8535  C CE2   . TYR A 1 2426 ? 138.926 194.467 200.922 1.00 28.32  ? 2426 TYR A CE2   1 
ATOM   8536  C CZ    . TYR A 1 2426 ? 137.910 195.362 200.677 1.00 28.32  ? 2426 TYR A CZ    1 
ATOM   8537  O OH    . TYR A 1 2426 ? 136.760 195.302 201.429 1.00 28.32  ? 2426 TYR A OH    1 
ATOM   8538  N N     . PHE A 1 2427 ? 144.550 196.846 197.794 1.00 24.49  ? 2427 PHE A N     1 
ATOM   8539  C CA    . PHE A 1 2427 ? 145.796 196.768 197.030 1.00 24.49  ? 2427 PHE A CA    1 
ATOM   8540  C C     . PHE A 1 2427 ? 147.006 197.126 197.890 1.00 24.49  ? 2427 PHE A C     1 
ATOM   8541  O O     . PHE A 1 2427 ? 147.756 198.052 197.585 1.00 24.49  ? 2427 PHE A O     1 
ATOM   8542  C CB    . PHE A 1 2427 ? 145.711 197.669 195.804 1.00 24.49  ? 2427 PHE A CB    1 
ATOM   8543  C CG    . PHE A 1 2427 ? 144.827 197.133 194.716 1.00 24.49  ? 2427 PHE A CG    1 
ATOM   8544  C CD1   . PHE A 1 2427 ? 143.453 197.272 194.788 1.00 24.49  ? 2427 PHE A CD1   1 
ATOM   8545  C CD2   . PHE A 1 2427 ? 145.370 196.491 193.619 1.00 24.49  ? 2427 PHE A CD2   1 
ATOM   8546  C CE1   . PHE A 1 2427 ? 142.640 196.780 193.787 1.00 24.49  ? 2427 PHE A CE1   1 
ATOM   8547  C CE2   . PHE A 1 2427 ? 144.562 195.997 192.615 1.00 24.49  ? 2427 PHE A CE2   1 
ATOM   8548  C CZ    . PHE A 1 2427 ? 143.196 196.142 192.700 1.00 24.49  ? 2427 PHE A CZ    1 
ATOM   8549  N N     . THR A 1 2428 ? 147.205 196.388 198.978 1.00 29.20  ? 2428 THR A N     1 
ATOM   8550  C CA    . THR A 1 2428 ? 148.315 196.615 199.889 1.00 29.20  ? 2428 THR A CA    1 
ATOM   8551  C C     . THR A 1 2428 ? 149.323 195.473 199.776 1.00 29.20  ? 2428 THR A C     1 
ATOM   8552  O O     . THR A 1 2428 ? 149.197 194.584 198.926 1.00 29.20  ? 2428 THR A O     1 
ATOM   8553  C CB    . THR A 1 2428 ? 147.802 196.777 201.322 1.00 29.20  ? 2428 THR A CB    1 
ATOM   8554  O OG1   . THR A 1 2428 ? 146.795 195.795 201.587 1.00 29.20  ? 2428 THR A OG1   1 
ATOM   8555  C CG2   . THR A 1 2428 ? 147.213 198.165 201.520 1.00 29.20  ? 2428 THR A CG2   1 
ATOM   8556  N N     . SER A 1 2429 ? 150.342 195.508 200.639 1.00 33.40  ? 2429 SER A N     1 
ATOM   8557  C CA    . SER A 1 2429 ? 151.384 194.486 200.602 1.00 33.40  ? 2429 SER A CA    1 
ATOM   8558  C C     . SER A 1 2429 ? 150.823 193.105 200.916 1.00 33.40  ? 2429 SER A C     1 
ATOM   8559  O O     . SER A 1 2429 ? 151.173 192.120 200.256 1.00 33.40  ? 2429 SER A O     1 
ATOM   8560  C CB    . SER A 1 2429 ? 152.501 194.845 201.582 1.00 33.40  ? 2429 SER A CB    1 
ATOM   8561  O OG    . SER A 1 2429 ? 152.009 194.925 202.908 1.00 33.40  ? 2429 SER A OG    1 
ATOM   8562  N N     . ASN A 1 2430 ? 149.953 193.012 201.917 1.00 37.25  ? 2430 ASN A N     1 
ATOM   8563  C CA    . ASN A 1 2430 ? 149.328 191.758 202.317 1.00 37.25  ? 2430 ASN A CA    1 
ATOM   8564  C C     . ASN A 1 2430 ? 147.808 191.856 202.253 1.00 37.25  ? 2430 ASN A C     1 
ATOM   8565  O O     . ASN A 1 2430 ? 147.092 191.309 203.094 1.00 37.25  ? 2430 ASN A O     1 
ATOM   8566  C CB    . ASN A 1 2430 ? 149.801 191.335 203.709 1.00 37.25  ? 2430 ASN A CB    1 
ATOM   8567  C CG    . ASN A 1 2430 ? 149.397 192.318 204.801 1.00 37.25  ? 2430 ASN A CG    1 
ATOM   8568  O OD1   . ASN A 1 2430 ? 148.655 193.272 204.565 1.00 37.25  ? 2430 ASN A OD1   1 
ATOM   8569  N ND2   . ASN A 1 2430 ? 149.890 192.081 206.011 1.00 37.25  ? 2430 ASN A ND2   1 
ATOM   8570  N N     . GLY A 1 2431 ? 147.301 192.556 201.243 1.00 36.55  ? 2431 GLY A N     1 
ATOM   8571  C CA    . GLY A 1 2431 ? 145.878 192.754 201.087 1.00 36.55  ? 2431 GLY A CA    1 
ATOM   8572  C C     . GLY A 1 2431 ? 145.194 191.561 200.449 1.00 36.55  ? 2431 GLY A C     1 
ATOM   8573  O O     . GLY A 1 2431 ? 145.777 190.495 200.243 1.00 36.55  ? 2431 GLY A O     1 
ATOM   8574  N N     . LEU A 1 2432 ? 143.910 191.757 200.140 1.00 33.66  ? 2432 LEU A N     1 
ATOM   8575  C CA    . LEU A 1 2432 ? 143.117 190.684 199.549 1.00 33.66  ? 2432 LEU A CA    1 
ATOM   8576  C C     . LEU A 1 2432 ? 143.661 190.273 198.187 1.00 33.66  ? 2432 LEU A C     1 
ATOM   8577  O O     . LEU A 1 2432 ? 143.738 189.079 197.878 1.00 33.66  ? 2432 LEU A O     1 
ATOM   8578  C CB    . LEU A 1 2432 ? 141.656 191.119 199.434 1.00 33.66  ? 2432 LEU A CB    1 
ATOM   8579  C CG    . LEU A 1 2432 ? 140.786 190.345 198.441 1.00 33.66  ? 2432 LEU A CG    1 
ATOM   8580  C CD1   . LEU A 1 2432 ? 140.532 188.931 198.933 1.00 33.66  ? 2432 LEU A CD1   1 
ATOM   8581  C CD2   . LEU A 1 2432 ? 139.475 191.073 198.198 1.00 33.66  ? 2432 LEU A CD2   1 
ATOM   8582  N N     . VAL A 1 2433 ? 144.046 191.247 197.361 1.00 30.21  ? 2433 VAL A N     1 
ATOM   8583  C CA    . VAL A 1 2433 ? 144.481 190.935 196.004 1.00 30.21  ? 2433 VAL A CA    1 
ATOM   8584  C C     . VAL A 1 2433 ? 145.774 190.129 196.019 1.00 30.21  ? 2433 VAL A C     1 
ATOM   8585  O O     . VAL A 1 2433 ? 145.916 189.151 195.278 1.00 30.21  ? 2433 VAL A O     1 
ATOM   8586  C CB    . VAL A 1 2433 ? 144.628 192.225 195.179 1.00 30.21  ? 2433 VAL A CB    1 
ATOM   8587  C CG1   . VAL A 1 2433 ? 144.875 191.890 193.718 1.00 30.21  ? 2433 VAL A CG1   1 
ATOM   8588  C CG2   . VAL A 1 2433 ? 143.390 193.092 195.330 1.00 30.21  ? 2433 VAL A CG2   1 
ATOM   8589  N N     . THR A 1 2434 ? 146.736 190.521 196.858 1.00 31.00  ? 2434 THR A N     1 
ATOM   8590  C CA    . THR A 1 2434 ? 148.019 189.824 196.889 1.00 31.00  ? 2434 THR A CA    1 
ATOM   8591  C C     . THR A 1 2434 ? 147.860 188.388 197.375 1.00 31.00  ? 2434 THR A C     1 
ATOM   8592  O O     . THR A 1 2434 ? 148.416 187.455 196.783 1.00 31.00  ? 2434 THR A O     1 
ATOM   8593  C CB    . THR A 1 2434 ? 149.007 190.582 197.775 1.00 31.00  ? 2434 THR A CB    1 
ATOM   8594  O OG1   . THR A 1 2434 ? 148.991 191.973 197.430 1.00 31.00  ? 2434 THR A OG1   1 
ATOM   8595  C CG2   . THR A 1 2434 ? 150.413 190.036 197.587 1.00 31.00  ? 2434 THR A CG2   1 
ATOM   8596  N N     . LYS A 1 2435 ? 147.106 188.192 198.460 1.00 34.48  ? 2435 LYS A N     1 
ATOM   8597  C CA    . LYS A 1 2435 ? 146.882 186.844 198.972 1.00 34.48  ? 2435 LYS A CA    1 
ATOM   8598  C C     . LYS A 1 2435 ? 146.117 185.996 197.966 1.00 34.48  ? 2435 LYS A C     1 
ATOM   8599  O O     . LYS A 1 2435 ? 146.433 184.815 197.767 1.00 34.48  ? 2435 LYS A O     1 
ATOM   8600  C CB    . LYS A 1 2435 ? 146.132 186.907 200.301 1.00 34.48  ? 2435 LYS A CB    1 
ATOM   8601  C CG    . LYS A 1 2435 ? 146.987 187.349 201.473 1.00 34.48  ? 2435 LYS A CG    1 
ATOM   8602  C CD    . LYS A 1 2435 ? 146.128 187.730 202.664 1.00 34.48  ? 2435 LYS A CD    1 
ATOM   8603  C CE    . LYS A 1 2435 ? 146.980 188.005 203.891 1.00 34.48  ? 2435 LYS A CE    1 
ATOM   8604  N NZ    . LYS A 1 2435 ? 146.341 189.002 204.792 1.00 34.48  ? 2435 LYS A NZ    1 
ATOM   8605  N N     . ALA A 1 2436 ? 145.107 186.582 197.320 1.00 31.75  ? 2436 ALA A N     1 
ATOM   8606  C CA    . ALA A 1 2436 ? 144.347 185.849 196.316 1.00 31.75  ? 2436 ALA A CA    1 
ATOM   8607  C C     . ALA A 1 2436 ? 145.234 185.439 195.151 1.00 31.75  ? 2436 ALA A C     1 
ATOM   8608  O O     . ALA A 1 2436 ? 145.122 184.321 194.643 1.00 31.75  ? 2436 ALA A O     1 
ATOM   8609  C CB    . ALA A 1 2436 ? 143.170 186.692 195.827 1.00 31.75  ? 2436 ALA A CB    1 
ATOM   8610  N N     . LEU A 1 2437 ? 146.127 186.331 194.714 1.00 30.29  ? 2437 LEU A N     1 
ATOM   8611  C CA    . LEU A 1 2437 ? 147.039 185.997 193.626 1.00 30.29  ? 2437 LEU A CA    1 
ATOM   8612  C C     . LEU A 1 2437 ? 148.003 184.888 194.027 1.00 30.29  ? 2437 LEU A C     1 
ATOM   8613  O O     . LEU A 1 2437 ? 148.251 183.955 193.249 1.00 30.29  ? 2437 LEU A O     1 
ATOM   8614  C CB    . LEU A 1 2437 ? 147.800 187.248 193.190 1.00 30.29  ? 2437 LEU A CB    1 
ATOM   8615  C CG    . LEU A 1 2437 ? 148.554 187.139 191.870 1.00 30.29  ? 2437 LEU A CG    1 
ATOM   8616  C CD1   . LEU A 1 2437 ? 147.665 186.491 190.837 1.00 30.29  ? 2437 LEU A CD1   1 
ATOM   8617  C CD2   . LEU A 1 2437 ? 149.014 188.506 191.398 1.00 30.29  ? 2437 LEU A CD2   1 
ATOM   8618  N N     . GLU A 1 2438 ? 148.554 184.973 195.240 1.00 35.26  ? 2438 GLU A N     1 
ATOM   8619  C CA    . GLU A 1 2438 ? 149.476 183.944 195.706 1.00 35.26  ? 2438 GLU A CA    1 
ATOM   8620  C C     . GLU A 1 2438 ? 148.782 182.590 195.756 1.00 35.26  ? 2438 GLU A C     1 
ATOM   8621  O O     . GLU A 1 2438 ? 149.352 181.570 195.352 1.00 35.26  ? 2438 GLU A O     1 
ATOM   8622  C CB    . GLU A 1 2438 ? 150.032 184.325 197.079 1.00 35.26  ? 2438 GLU A CB    1 
ATOM   8623  C CG    . GLU A 1 2438 ? 150.885 183.256 197.752 1.00 35.26  ? 2438 GLU A CG    1 
ATOM   8624  C CD    . GLU A 1 2438 ? 151.824 182.550 196.789 1.00 35.26  ? 2438 GLU A CD    1 
ATOM   8625  O OE1   . GLU A 1 2438 ? 152.634 183.239 196.135 1.00 35.26  ? 2438 GLU A OE1   1 
ATOM   8626  O OE2   . GLU A 1 2438 ? 151.758 181.306 196.694 1.00 35.26  ? 2438 GLU A OE2   1 
ATOM   8627  N N     . HIS A 1 2439 ? 147.540 182.564 196.240 1.00 37.71  ? 2439 HIS A N     1 
ATOM   8628  C CA    . HIS A 1 2439 ? 146.780 181.319 196.233 1.00 37.71  ? 2439 HIS A CA    1 
ATOM   8629  C C     . HIS A 1 2439 ? 146.500 180.847 194.810 1.00 37.71  ? 2439 HIS A C     1 
ATOM   8630  O O     . HIS A 1 2439 ? 146.602 179.651 194.517 1.00 37.71  ? 2439 HIS A O     1 
ATOM   8631  C CB    . HIS A 1 2439 ? 145.475 181.496 197.005 1.00 37.71  ? 2439 HIS A CB    1 
ATOM   8632  C CG    . HIS A 1 2439 ? 144.704 180.226 197.185 1.00 37.71  ? 2439 HIS A CG    1 
ATOM   8633  N ND1   . HIS A 1 2439 ? 143.472 180.015 196.606 1.00 37.71  ? 2439 HIS A ND1   1 
ATOM   8634  C CD2   . HIS A 1 2439 ? 144.991 179.100 197.880 1.00 37.71  ? 2439 HIS A CD2   1 
ATOM   8635  C CE1   . HIS A 1 2439 ? 143.033 178.814 196.935 1.00 37.71  ? 2439 HIS A CE1   1 
ATOM   8636  N NE2   . HIS A 1 2439 ? 143.936 178.238 197.708 1.00 37.71  ? 2439 HIS A NE2   1 
ATOM   8637  N N     . ALA A 1 2440 ? 146.161 181.775 193.910 1.00 32.56  ? 2440 ALA A N     1 
ATOM   8638  C CA    . ALA A 1 2440 ? 145.779 181.404 192.553 1.00 32.56  ? 2440 ALA A CA    1 
ATOM   8639  C C     . ALA A 1 2440 ? 146.944 180.818 191.771 1.00 32.56  ? 2440 ALA A C     1 
ATOM   8640  O O     . ALA A 1 2440 ? 146.727 180.021 190.852 1.00 32.56  ? 2440 ALA A O     1 
ATOM   8641  C CB    . ALA A 1 2440 ? 145.207 182.615 191.817 1.00 32.56  ? 2440 ALA A CB    1 
ATOM   8642  N N     . PHE A 1 2441 ? 148.180 181.208 192.098 1.00 34.16  ? 2441 PHE A N     1 
ATOM   8643  C CA    . PHE A 1 2441 ? 149.317 180.535 191.471 1.00 34.16  ? 2441 PHE A CA    1 
ATOM   8644  C C     . PHE A 1 2441 ? 149.335 179.044 191.790 1.00 34.16  ? 2441 PHE A C     1 
ATOM   8645  O O     . PHE A 1 2441 ? 149.824 178.245 190.984 1.00 34.16  ? 2441 PHE A O     1 
ATOM   8646  C CB    . PHE A 1 2441 ? 150.652 181.160 191.884 1.00 34.16  ? 2441 PHE A CB    1 
ATOM   8647  C CG    . PHE A 1 2441 ? 150.916 182.506 191.276 1.00 34.16  ? 2441 PHE A CG    1 
ATOM   8648  C CD1   . PHE A 1 2441 ? 151.278 182.611 189.944 1.00 34.16  ? 2441 PHE A CD1   1 
ATOM   8649  C CD2   . PHE A 1 2441 ? 150.882 183.653 192.043 1.00 34.16  ? 2441 PHE A CD2   1 
ATOM   8650  C CE1   . PHE A 1 2441 ? 151.541 183.840 189.377 1.00 34.16  ? 2441 PHE A CE1   1 
ATOM   8651  C CE2   . PHE A 1 2441 ? 151.148 184.886 191.483 1.00 34.16  ? 2441 PHE A CE2   1 
ATOM   8652  C CZ    . PHE A 1 2441 ? 151.478 184.979 190.148 1.00 34.16  ? 2441 PHE A CZ    1 
ATOM   8653  N N     . GLN A 1 2442 ? 148.808 178.649 192.950 1.00 38.97  ? 2442 GLN A N     1 
ATOM   8654  C CA    . GLN A 1 2442 ? 148.814 177.245 193.341 1.00 38.97  ? 2442 GLN A CA    1 
ATOM   8655  C C     . GLN A 1 2442 ? 147.797 176.410 192.575 1.00 38.97  ? 2442 GLN A C     1 
ATOM   8656  O O     . GLN A 1 2442 ? 148.000 175.201 192.421 1.00 38.97  ? 2442 GLN A O     1 
ATOM   8657  C CB    . GLN A 1 2442 ? 148.556 177.120 194.844 1.00 38.97  ? 2442 GLN A CB    1 
ATOM   8658  C CG    . GLN A 1 2442 ? 149.656 177.713 195.707 1.00 38.97  ? 2442 GLN A CG    1 
ATOM   8659  C CD    . GLN A 1 2442 ? 149.349 177.624 197.187 1.00 38.97  ? 2442 GLN A CD    1 
ATOM   8660  O OE1   . GLN A 1 2442 ? 148.275 177.172 197.584 1.00 38.97  ? 2442 GLN A OE1   1 
ATOM   8661  N NE2   . GLN A 1 2442 ? 150.292 178.059 198.014 1.00 38.97  ? 2442 GLN A NE2   1 
ATOM   8662  N N     . LEU A 1 2443 ? 146.715 177.019 192.095 1.00 39.93  ? 2443 LEU A N     1 
ATOM   8663  C CA    . LEU A 1 2443 ? 145.698 176.287 191.357 1.00 39.93  ? 2443 LEU A CA    1 
ATOM   8664  C C     . LEU A 1 2443 ? 146.225 175.855 189.989 1.00 39.93  ? 2443 LEU A C     1 
ATOM   8665  O O     . LEU A 1 2443 ? 147.353 176.162 189.593 1.00 39.93  ? 2443 LEU A O     1 
ATOM   8666  C CB    . LEU A 1 2443 ? 144.437 177.136 191.188 1.00 39.93  ? 2443 LEU A CB    1 
ATOM   8667  C CG    . LEU A 1 2443 ? 143.476 177.287 192.370 1.00 39.93  ? 2443 LEU A CG    1 
ATOM   8668  C CD1   . LEU A 1 2443 ? 144.047 178.158 193.471 1.00 39.93  ? 2443 LEU A CD1   1 
ATOM   8669  C CD2   . LEU A 1 2443 ? 142.163 177.863 191.883 1.00 39.93  ? 2443 LEU A CD2   1 
ATOM   8670  N N     . GLU A 1 2444 ? 145.382 175.128 189.262 1.00 44.57  ? 2444 GLU A N     1 
ATOM   8671  C CA    . GLU A 1 2444 ? 145.704 174.644 187.927 1.00 44.57  ? 2444 GLU A CA    1 
ATOM   8672  C C     . GLU A 1 2444 ? 144.948 175.464 186.891 1.00 44.57  ? 2444 GLU A C     1 
ATOM   8673  O O     . GLU A 1 2444 ? 143.725 175.608 186.979 1.00 44.57  ? 2444 GLU A O     1 
ATOM   8674  C CB    . GLU A 1 2444 ? 145.353 173.164 187.782 1.00 44.57  ? 2444 GLU A CB    1 
ATOM   8675  C CG    . GLU A 1 2444 ? 145.731 172.563 186.439 1.00 44.57  ? 2444 GLU A CG    1 
ATOM   8676  C CD    . GLU A 1 2444 ? 145.412 171.084 186.355 1.00 44.57  ? 2444 GLU A CD    1 
ATOM   8677  O OE1   . GLU A 1 2444 ? 144.876 170.533 187.340 1.00 44.57  ? 2444 GLU A OE1   1 
ATOM   8678  O OE2   . GLU A 1 2444 ? 145.695 170.472 185.304 1.00 44.57  ? 2444 GLU A OE2   1 
ATOM   8679  N N     . HIS A 1 2445 ? 145.677 175.992 185.913 1.00 35.11  ? 2445 HIS A N     1 
ATOM   8680  C CA    . HIS A 1 2445 ? 145.103 176.806 184.855 1.00 35.11  ? 2445 HIS A CA    1 
ATOM   8681  C C     . HIS A 1 2445 ? 145.350 176.148 183.506 1.00 35.11  ? 2445 HIS A C     1 
ATOM   8682  O O     . HIS A 1 2445 ? 146.355 175.458 183.309 1.00 35.11  ? 2445 HIS A O     1 
ATOM   8683  C CB    . HIS A 1 2445 ? 145.690 178.220 184.862 1.00 35.11  ? 2445 HIS A CB    1 
ATOM   8684  C CG    . HIS A 1 2445 ? 145.540 178.929 186.171 1.00 35.11  ? 2445 HIS A CG    1 
ATOM   8685  N ND1   . HIS A 1 2445 ? 144.613 179.928 186.373 1.00 35.11  ? 2445 HIS A ND1   1 
ATOM   8686  C CD2   . HIS A 1 2445 ? 146.199 178.783 187.344 1.00 35.11  ? 2445 HIS A CD2   1 
ATOM   8687  C CE1   . HIS A 1 2445 ? 144.707 180.367 187.615 1.00 35.11  ? 2445 HIS A CE1   1 
ATOM   8688  N NE2   . HIS A 1 2445 ? 145.661 179.688 188.226 1.00 35.11  ? 2445 HIS A NE2   1 
ATOM   8689  N N     . ILE A 1 2446 ? 144.417 176.364 182.577 1.00 31.43  ? 2446 ILE A N     1 
ATOM   8690  C CA    . ILE A 1 2446 ? 144.544 175.762 181.255 1.00 31.43  ? 2446 ILE A CA    1 
ATOM   8691  C C     . ILE A 1 2446 ? 145.743 176.340 180.513 1.00 31.43  ? 2446 ILE A C     1 
ATOM   8692  O O     . ILE A 1 2446 ? 146.340 175.667 179.664 1.00 31.43  ? 2446 ILE A O     1 
ATOM   8693  C CB    . ILE A 1 2446 ? 143.237 175.939 180.461 1.00 31.43  ? 2446 ILE A CB    1 
ATOM   8694  C CG1   . ILE A 1 2446 ? 143.267 175.095 179.188 1.00 31.43  ? 2446 ILE A CG1   1 
ATOM   8695  C CG2   . ILE A 1 2446 ? 143.008 177.400 180.114 1.00 31.43  ? 2446 ILE A CG2   1 
ATOM   8696  C CD1   . ILE A 1 2446 ? 141.924 174.962 178.531 1.00 31.43  ? 2446 ILE A CD1   1 
ATOM   8697  N N     . MET A 1 2447 ? 146.119 177.578 180.819 1.00 30.96  ? 2447 MET A N     1 
ATOM   8698  C CA    . MET A 1 2447 ? 147.310 178.198 180.263 1.00 30.96  ? 2447 MET A CA    1 
ATOM   8699  C C     . MET A 1 2447 ? 148.191 178.682 181.403 1.00 30.96  ? 2447 MET A C     1 
ATOM   8700  O O     . MET A 1 2447 ? 147.704 178.990 182.494 1.00 30.96  ? 2447 MET A O     1 
ATOM   8701  C CB    . MET A 1 2447 ? 146.965 179.366 179.331 1.00 30.96  ? 2447 MET A CB    1 
ATOM   8702  C CG    . MET A 1 2447 ? 146.755 178.958 177.885 1.00 30.96  ? 2447 MET A CG    1 
ATOM   8703  S SD    . MET A 1 2447 ? 145.896 180.218 176.927 1.00 30.96  ? 2447 MET A SD    1 
ATOM   8704  C CE    . MET A 1 2447 ? 146.021 179.528 175.280 1.00 30.96  ? 2447 MET A CE    1 
ATOM   8705  N N     . ASP A 1 2448 ? 149.495 178.730 181.144 1.00 27.86  ? 2448 ASP A N     1 
ATOM   8706  C CA    . ASP A 1 2448 ? 150.461 179.120 182.162 1.00 27.86  ? 2448 ASP A CA    1 
ATOM   8707  C C     . ASP A 1 2448 ? 150.121 180.488 182.732 1.00 27.86  ? 2448 ASP A C     1 
ATOM   8708  O O     . ASP A 1 2448 ? 150.147 181.494 182.019 1.00 27.86  ? 2448 ASP A O     1 
ATOM   8709  C CB    . ASP A 1 2448 ? 151.868 179.123 181.564 1.00 27.86  ? 2448 ASP A CB    1 
ATOM   8710  C CG    . ASP A 1 2448 ? 152.150 177.883 180.741 1.00 27.86  ? 2448 ASP A CG    1 
ATOM   8711  O OD1   . ASP A 1 2448 ? 152.363 176.808 181.339 1.00 27.86  ? 2448 ASP A OD1   1 
ATOM   8712  O OD2   . ASP A 1 2448 ? 152.155 177.982 179.496 1.00 27.86  ? 2448 ASP A OD2   1 
ATOM   8713  N N     . LEU A 1 2449 ? 149.793 180.517 184.022 1.00 24.67  ? 2449 LEU A N     1 
ATOM   8714  C CA    . LEU A 1 2449 ? 149.356 181.752 184.658 1.00 24.67  ? 2449 LEU A CA    1 
ATOM   8715  C C     . LEU A 1 2449 ? 150.523 182.723 184.773 1.00 24.67  ? 2449 LEU A C     1 
ATOM   8716  O O     . LEU A 1 2449 ? 151.572 182.385 185.333 1.00 24.67  ? 2449 LEU A O     1 
ATOM   8717  C CB    . LEU A 1 2449 ? 148.763 181.460 186.034 1.00 24.67  ? 2449 LEU A CB    1 
ATOM   8718  C CG    . LEU A 1 2449 ? 148.327 182.684 186.840 1.00 24.67  ? 2449 LEU A CG    1 
ATOM   8719  C CD1   . LEU A 1 2449 ? 147.284 183.486 186.082 1.00 24.67  ? 2449 LEU A CD1   1 
ATOM   8720  C CD2   . LEU A 1 2449 ? 147.796 182.270 188.199 1.00 24.67  ? 2449 LEU A CD2   1 
ATOM   8721  N N     . THR A 1 2450 ? 150.338 183.926 184.244 1.00 19.51  ? 2450 THR A N     1 
ATOM   8722  C CA    . THR A 1 2450 ? 151.321 184.994 184.328 1.00 19.51  ? 2450 THR A CA    1 
ATOM   8723  C C     . THR A 1 2450 ? 150.753 186.114 185.187 1.00 19.51  ? 2450 THR A C     1 
ATOM   8724  O O     . THR A 1 2450 ? 149.559 186.421 185.108 1.00 19.51  ? 2450 THR A O     1 
ATOM   8725  C CB    . THR A 1 2450 ? 151.680 185.519 182.934 1.00 19.51  ? 2450 THR A CB    1 
ATOM   8726  O OG1   . THR A 1 2450 ? 152.100 184.427 182.107 1.00 19.51  ? 2450 THR A OG1   1 
ATOM   8727  C CG2   . THR A 1 2450 ? 152.809 186.533 183.016 1.00 19.51  ? 2450 THR A CG2   1 
ATOM   8728  N N     . ARG A 1 2451 ? 151.609 186.715 186.017 1.00 13.98  ? 2451 ARG A N     1 
ATOM   8729  C CA    . ARG A 1 2451 ? 151.143 187.739 186.947 1.00 13.98  ? 2451 ARG A CA    1 
ATOM   8730  C C     . ARG A 1 2451 ? 150.522 188.921 186.214 1.00 13.98  ? 2451 ARG A C     1 
ATOM   8731  O O     . ARG A 1 2451 ? 149.435 189.386 186.578 1.00 13.98  ? 2451 ARG A O     1 
ATOM   8732  C CB    . ARG A 1 2451 ? 152.300 188.204 187.829 1.00 13.98  ? 2451 ARG A CB    1 
ATOM   8733  C CG    . ARG A 1 2451 ? 151.988 189.415 188.689 1.00 13.98  ? 2451 ARG A CG    1 
ATOM   8734  C CD    . ARG A 1 2451 ? 153.239 189.930 189.383 1.00 13.98  ? 2451 ARG A CD    1 
ATOM   8735  N NE    . ARG A 1 2451 ? 154.322 190.193 188.442 1.00 13.98  ? 2451 ARG A NE    1 
ATOM   8736  C CZ    . ARG A 1 2451 ? 155.528 190.617 188.790 1.00 13.98  ? 2451 ARG A CZ    1 
ATOM   8737  N NH1   . ARG A 1 2451 ? 155.843 190.847 190.054 1.00 13.98  ? 2451 ARG A NH1   1 
ATOM   8738  N NH2   . ARG A 1 2451 ? 156.444 190.812 187.846 1.00 13.98  ? 2451 ARG A NH2   1 
ATOM   8739  N N     . LEU A 1 2452 ? 151.182 189.408 185.164 1.00 13.53  ? 2452 LEU A N     1 
ATOM   8740  C CA    . LEU A 1 2452 ? 150.670 190.600 184.501 1.00 13.53  ? 2452 LEU A CA    1 
ATOM   8741  C C     . LEU A 1 2452 ? 149.427 190.312 183.671 1.00 13.53  ? 2452 LEU A C     1 
ATOM   8742  O O     . LEU A 1 2452 ? 148.603 191.205 183.485 1.00 13.53  ? 2452 LEU A O     1 
ATOM   8743  C CB    . LEU A 1 2452 ? 151.749 191.250 183.638 1.00 13.53  ? 2452 LEU A CB    1 
ATOM   8744  C CG    . LEU A 1 2452 ? 152.851 191.960 184.420 1.00 13.53  ? 2452 LEU A CG    1 
ATOM   8745  C CD1   . LEU A 1 2452 ? 153.898 192.504 183.477 1.00 13.53  ? 2452 LEU A CD1   1 
ATOM   8746  C CD2   . LEU A 1 2452 ? 152.261 193.075 185.261 1.00 13.53  ? 2452 LEU A CD2   1 
ATOM   8747  N N     . ARG A 1 2453 ? 149.252 189.084 183.177 1.00 14.70  ? 2453 ARG A N     1 
ATOM   8748  C CA    . ARG A 1 2453 ? 148.030 188.776 182.438 1.00 14.70  ? 2453 ARG A CA    1 
ATOM   8749  C C     . ARG A 1 2453 ? 146.800 188.917 183.328 1.00 14.70  ? 2453 ARG A C     1 
ATOM   8750  O O     . ARG A 1 2453 ? 145.850 189.643 182.996 1.00 14.70  ? 2453 ARG A O     1 
ATOM   8751  C CB    . ARG A 1 2453 ? 148.106 187.366 181.851 1.00 14.70  ? 2453 ARG A CB    1 
ATOM   8752  C CG    . ARG A 1 2453 ? 146.742 186.748 181.572 1.00 14.70  ? 2453 ARG A CG    1 
ATOM   8753  C CD    . ARG A 1 2453 ? 146.828 185.562 180.624 1.00 14.70  ? 2453 ARG A CD    1 
ATOM   8754  N NE    . ARG A 1 2453 ? 147.222 184.327 181.291 1.00 14.70  ? 2453 ARG A NE    1 
ATOM   8755  C CZ    . ARG A 1 2453 ? 146.407 183.570 182.012 1.00 14.70  ? 2453 ARG A CZ    1 
ATOM   8756  N NH1   . ARG A 1 2453 ? 145.147 183.913 182.218 1.00 14.70  ? 2453 ARG A NH1   1 
ATOM   8757  N NH2   . ARG A 1 2453 ? 146.869 182.442 182.541 1.00 14.70  ? 2453 ARG A NH2   1 
ATOM   8758  N N     . CYS A 1 2454 ? 146.811 188.246 184.481 1.00 14.64  ? 2454 CYS A N     1 
ATOM   8759  C CA    . CYS A 1 2454 ? 145.675 188.316 185.391 1.00 14.64  ? 2454 CYS A CA    1 
ATOM   8760  C C     . CYS A 1 2454 ? 145.536 189.712 185.986 1.00 14.64  ? 2454 CYS A C     1 
ATOM   8761  O O     . CYS A 1 2454 ? 144.420 190.211 186.166 1.00 14.64  ? 2454 CYS A O     1 
ATOM   8762  C CB    . CYS A 1 2454 ? 145.809 187.259 186.485 1.00 14.64  ? 2454 CYS A CB    1 
ATOM   8763  S SG    . CYS A 1 2454 ? 147.214 187.492 187.572 1.00 14.64  ? 2454 CYS A SG    1 
ATOM   8764  N N     . LEU A 1 2455 ? 146.661 190.364 186.295 1.00 12.79  ? 2455 LEU A N     1 
ATOM   8765  C CA    . LEU A 1 2455 ? 146.583 191.727 186.813 1.00 12.79  ? 2455 LEU A CA    1 
ATOM   8766  C C     . LEU A 1 2455 ? 145.992 192.686 185.784 1.00 12.79  ? 2455 LEU A C     1 
ATOM   8767  O O     . LEU A 1 2455 ? 145.202 193.566 186.137 1.00 12.79  ? 2455 LEU A O     1 
ATOM   8768  C CB    . LEU A 1 2455 ? 147.960 192.201 187.268 1.00 12.79  ? 2455 LEU A CB    1 
ATOM   8769  C CG    . LEU A 1 2455 ? 148.447 191.604 188.588 1.00 12.79  ? 2455 LEU A CG    1 
ATOM   8770  C CD1   . LEU A 1 2455 ? 149.744 192.257 189.014 1.00 12.79  ? 2455 LEU A CD1   1 
ATOM   8771  C CD2   . LEU A 1 2455 ? 147.388 191.762 189.664 1.00 12.79  ? 2455 LEU A CD2   1 
ATOM   8772  N N     . GLY A 1 2456 ? 146.355 192.535 184.509 1.00 13.53  ? 2456 GLY A N     1 
ATOM   8773  C CA    . GLY A 1 2456 ? 145.791 193.390 183.480 1.00 13.53  ? 2456 GLY A CA    1 
ATOM   8774  C C     . GLY A 1 2456 ? 144.312 193.144 183.265 1.00 13.53  ? 2456 GLY A C     1 
ATOM   8775  O O     . GLY A 1 2456 ? 143.541 194.086 183.070 1.00 13.53  ? 2456 GLY A O     1 
ATOM   8776  N N     . SER A 1 2457 ? 143.892 191.876 183.298 1.00 13.95  ? 2457 SER A N     1 
ATOM   8777  C CA    . SER A 1 2457 ? 142.463 191.589 183.216 1.00 13.95  ? 2457 SER A CA    1 
ATOM   8778  C C     . SER A 1 2457 ? 141.713 192.196 184.398 1.00 13.95  ? 2457 SER A C     1 
ATOM   8779  O O     . SER A 1 2457 ? 140.626 192.766 184.232 1.00 13.95  ? 2457 SER A O     1 
ATOM   8780  C CB    . SER A 1 2457 ? 142.233 190.081 183.145 1.00 13.95  ? 2457 SER A CB    1 
ATOM   8781  O OG    . SER A 1 2457 ? 142.629 189.453 184.349 1.00 13.95  ? 2457 SER A OG    1 
ATOM   8782  N N     . LEU A 1 2458 ? 142.286 192.089 185.600 1.00 13.45  ? 2458 LEU A N     1 
ATOM   8783  C CA    . LEU A 1 2458 ? 141.671 192.683 186.783 1.00 13.45  ? 2458 LEU A CA    1 
ATOM   8784  C C     . LEU A 1 2458 ? 141.561 194.197 186.650 1.00 13.45  ? 2458 LEU A C     1 
ATOM   8785  O O     . LEU A 1 2458 ? 140.519 194.783 186.967 1.00 13.45  ? 2458 LEU A O     1 
ATOM   8786  C CB    . LEU A 1 2458 ? 142.482 192.309 188.023 1.00 13.45  ? 2458 LEU A CB    1 
ATOM   8787  C CG    . LEU A 1 2458 ? 142.104 192.914 189.374 1.00 13.45  ? 2458 LEU A CG    1 
ATOM   8788  C CD1   . LEU A 1 2458 ? 140.749 192.417 189.828 1.00 13.45  ? 2458 LEU A CD1   1 
ATOM   8789  C CD2   . LEU A 1 2458 ? 143.165 192.588 190.409 1.00 13.45  ? 2458 LEU A CD2   1 
ATOM   8790  N N     . PHE A 1 2459 ? 142.626 194.848 186.179 1.00 13.72  ? 2459 PHE A N     1 
ATOM   8791  C CA    . PHE A 1 2459 ? 142.597 196.296 186.009 1.00 13.72  ? 2459 PHE A CA    1 
ATOM   8792  C C     . PHE A 1 2459 ? 141.569 196.704 184.963 1.00 13.72  ? 2459 PHE A C     1 
ATOM   8793  O O     . PHE A 1 2459 ? 140.857 197.699 185.138 1.00 13.72  ? 2459 PHE A O     1 
ATOM   8794  C CB    . PHE A 1 2459 ? 143.987 196.811 185.632 1.00 13.72  ? 2459 PHE A CB    1 
ATOM   8795  C CG    . PHE A 1 2459 ? 145.046 196.518 186.659 1.00 13.72  ? 2459 PHE A CG    1 
ATOM   8796  C CD1   . PHE A 1 2459 ? 144.711 196.324 187.988 1.00 13.72  ? 2459 PHE A CD1   1 
ATOM   8797  C CD2   . PHE A 1 2459 ? 146.378 196.434 186.294 1.00 13.72  ? 2459 PHE A CD2   1 
ATOM   8798  C CE1   . PHE A 1 2459 ? 145.680 196.048 188.928 1.00 13.72  ? 2459 PHE A CE1   1 
ATOM   8799  C CE2   . PHE A 1 2459 ? 147.350 196.160 187.231 1.00 13.72  ? 2459 PHE A CE2   1 
ATOM   8800  C CZ    . PHE A 1 2459 ? 147.001 195.967 188.549 1.00 13.72  ? 2459 PHE A CZ    1 
ATOM   8801  N N     . SER A 1 2460 ? 141.468 195.941 183.872 1.00 17.00  ? 2460 SER A N     1 
ATOM   8802  C CA    . SER A 1 2460 ? 140.481 196.251 182.843 1.00 17.00  ? 2460 SER A CA    1 
ATOM   8803  C C     . SER A 1 2460 ? 139.059 196.128 183.380 1.00 17.00  ? 2460 SER A C     1 
ATOM   8804  O O     . SER A 1 2460 ? 138.198 196.968 183.087 1.00 17.00  ? 2460 SER A O     1 
ATOM   8805  C CB    . SER A 1 2460 ? 140.683 195.337 181.636 1.00 17.00  ? 2460 SER A CB    1 
ATOM   8806  O OG    . SER A 1 2460 ? 140.020 195.854 180.498 1.00 17.00  ? 2460 SER A OG    1 
ATOM   8807  N N     . MET A 1 2461 ? 138.791 195.090 184.173 1.00 19.66  ? 2461 MET A N     1 
ATOM   8808  C CA    . MET A 1 2461 ? 137.442 194.916 184.701 1.00 19.66  ? 2461 MET A CA    1 
ATOM   8809  C C     . MET A 1 2461 ? 137.119 195.957 185.772 1.00 19.66  ? 2461 MET A C     1 
ATOM   8810  O O     . MET A 1 2461 ? 135.968 196.394 185.892 1.00 19.66  ? 2461 MET A O     1 
ATOM   8811  C CB    . MET A 1 2461 ? 137.272 193.481 185.202 1.00 19.66  ? 2461 MET A CB    1 
ATOM   8812  C CG    . MET A 1 2461 ? 137.444 192.491 184.050 1.00 19.66  ? 2461 MET A CG    1 
ATOM   8813  S SD    . MET A 1 2461 ? 136.776 190.828 184.213 1.00 19.66  ? 2461 MET A SD    1 
ATOM   8814  C CE    . MET A 1 2461 ? 137.250 190.452 185.881 1.00 19.66  ? 2461 MET A CE    1 
ATOM   8815  N N     . LEU A 1 2462 ? 138.121 196.403 186.535 1.00 16.10  ? 2462 LEU A N     1 
ATOM   8816  C CA    . LEU A 1 2462 ? 137.884 197.528 187.441 1.00 16.10  ? 2462 LEU A CA    1 
ATOM   8817  C C     . LEU A 1 2462 ? 137.610 198.817 186.670 1.00 16.10  ? 2462 LEU A C     1 
ATOM   8818  O O     . LEU A 1 2462 ? 136.769 199.631 187.080 1.00 16.10  ? 2462 LEU A O     1 
ATOM   8819  C CB    . LEU A 1 2462 ? 139.060 197.710 188.401 1.00 16.10  ? 2462 LEU A CB    1 
ATOM   8820  C CG    . LEU A 1 2462 ? 139.003 196.943 189.726 1.00 16.10  ? 2462 LEU A CG    1 
ATOM   8821  C CD1   . LEU A 1 2462 ? 137.831 197.428 190.553 1.00 16.10  ? 2462 LEU A CD1   1 
ATOM   8822  C CD2   . LEU A 1 2462 ? 138.911 195.451 189.523 1.00 16.10  ? 2462 LEU A CD2   1 
ATOM   8823  N N     . HIS A 1 2463 ? 138.311 199.025 185.553 1.00 19.64  ? 2463 HIS A N     1 
ATOM   8824  C CA    . HIS A 1 2463 ? 138.007 200.169 184.702 1.00 19.64  ? 2463 HIS A CA    1 
ATOM   8825  C C     . HIS A 1 2463 ? 136.573 200.100 184.198 1.00 19.64  ? 2463 HIS A C     1 
ATOM   8826  O O     . HIS A 1 2463 ? 135.874 201.119 184.135 1.00 19.64  ? 2463 HIS A O     1 
ATOM   8827  C CB    . HIS A 1 2463 ? 138.979 200.229 183.525 1.00 19.64  ? 2463 HIS A CB    1 
ATOM   8828  C CG    . HIS A 1 2463 ? 140.364 200.644 183.903 1.00 19.64  ? 2463 HIS A CG    1 
ATOM   8829  N ND1   . HIS A 1 2463 ? 141.387 200.733 182.985 1.00 19.64  ? 2463 HIS A ND1   1 
ATOM   8830  C CD2   . HIS A 1 2463 ? 140.898 200.994 185.097 1.00 19.64  ? 2463 HIS A CD2   1 
ATOM   8831  C CE1   . HIS A 1 2463 ? 142.491 201.122 183.596 1.00 19.64  ? 2463 HIS A CE1   1 
ATOM   8832  N NE2   . HIS A 1 2463 ? 142.222 201.287 184.878 1.00 19.64  ? 2463 HIS A NE2   1 
ATOM   8833  N N     . GLN A 1 2464 ? 136.121 198.903 183.825 1.00 22.75  ? 2464 GLN A N     1 
ATOM   8834  C CA    . GLN A 1 2464 ? 134.733 198.740 183.411 1.00 22.75  ? 2464 GLN A CA    1 
ATOM   8835  C C     . GLN A 1 2464 ? 133.765 198.989 184.560 1.00 22.75  ? 2464 GLN A C     1 
ATOM   8836  O O     . GLN A 1 2464 ? 132.653 199.470 184.332 1.00 22.75  ? 2464 GLN A O     1 
ATOM   8837  C CB    . GLN A 1 2464 ? 134.512 197.350 182.826 1.00 22.75  ? 2464 GLN A CB    1 
ATOM   8838  C CG    . GLN A 1 2464 ? 133.111 197.120 182.285 1.00 22.75  ? 2464 GLN A CG    1 
ATOM   8839  C CD    . GLN A 1 2464 ? 132.686 198.176 181.283 1.00 22.75  ? 2464 GLN A CD    1 
ATOM   8840  O OE1   . GLN A 1 2464 ? 133.497 198.680 180.508 1.00 22.75  ? 2464 GLN A OE1   1 
ATOM   8841  N NE2   . GLN A 1 2464 ? 131.404 198.519 181.297 1.00 22.75  ? 2464 GLN A NE2   1 
ATOM   8842  N N     . ALA A 1 2465 ? 134.154 198.658 185.791 1.00 23.21  ? 2465 ALA A N     1 
ATOM   8843  C CA    . ALA A 1 2465 ? 133.317 199.001 186.939 1.00 23.21  ? 2465 ALA A CA    1 
ATOM   8844  C C     . ALA A 1 2465 ? 133.162 200.511 187.069 1.00 23.21  ? 2465 ALA A C     1 
ATOM   8845  O O     . ALA A 1 2465 ? 132.059 201.018 187.317 1.00 23.21  ? 2465 ALA A O     1 
ATOM   8846  C CB    . ALA A 1 2465 ? 133.907 198.415 188.219 1.00 23.21  ? 2465 ALA A CB    1 
ATOM   8847  N N     . CYS A 1 2466 ? 134.263 201.245 186.902 1.00 24.00  ? 2466 CYS A N     1 
ATOM   8848  C CA    . CYS A 1 2466 ? 134.181 202.705 186.929 1.00 24.00  ? 2466 CYS A CA    1 
ATOM   8849  C C     . CYS A 1 2466 ? 133.307 203.227 185.793 1.00 24.00  ? 2466 CYS A C     1 
ATOM   8850  O O     . CYS A 1 2466 ? 132.525 204.171 185.976 1.00 24.00  ? 2466 CYS A O     1 
ATOM   8851  C CB    . CYS A 1 2466 ? 135.579 203.314 186.855 1.00 24.00  ? 2466 CYS A CB    1 
ATOM   8852  S SG    . CYS A 1 2466 ? 136.709 202.737 188.140 1.00 24.00  ? 2466 CYS A SG    1 
ATOM   8853  N N     . ARG A 1 2467 ? 133.427 202.621 184.609 1.00 26.25  ? 2467 ARG A N     1 
ATOM   8854  C CA    . ARG A 1 2467 ? 132.582 203.010 183.484 1.00 26.25  ? 2467 ARG A CA    1 
ATOM   8855  C C     . ARG A 1 2467 ? 131.111 202.751 183.783 1.00 26.25  ? 2467 ARG A C     1 
ATOM   8856  O O     . ARG A 1 2467 ? 130.243 203.544 183.404 1.00 26.25  ? 2467 ARG A O     1 
ATOM   8857  C CB    . ARG A 1 2467 ? 133.008 202.259 182.224 1.00 26.25  ? 2467 ARG A CB    1 
ATOM   8858  C CG    . ARG A 1 2467 ? 134.277 202.782 181.581 1.00 26.25  ? 2467 ARG A CG    1 
ATOM   8859  C CD    . ARG A 1 2467 ? 134.579 202.038 180.292 1.00 26.25  ? 2467 ARG A CD    1 
ATOM   8860  N NE    . ARG A 1 2467 ? 136.005 202.014 179.996 1.00 26.25  ? 2467 ARG A NE    1 
ATOM   8861  C CZ    . ARG A 1 2467 ? 136.544 202.469 178.874 1.00 26.25  ? 2467 ARG A CZ    1 
ATOM   8862  N NH1   . ARG A 1 2467 ? 135.801 202.993 177.913 1.00 26.25  ? 2467 ARG A NH1   1 
ATOM   8863  N NH2   . ARG A 1 2467 ? 137.862 202.398 178.712 1.00 26.25  ? 2467 ARG A NH2   1 
ATOM   8864  N N     . ASN A 1 2468 ? 130.811 201.631 184.443 1.00 27.48  ? 2468 ASN A N     1 
ATOM   8865  C CA    . ASN A 1 2468 ? 129.436 201.332 184.827 1.00 27.48  ? 2468 ASN A CA    1 
ATOM   8866  C C     . ASN A 1 2468 ? 128.907 202.364 185.811 1.00 27.48  ? 2468 ASN A C     1 
ATOM   8867  O O     . ASN A 1 2468 ? 127.744 202.774 185.727 1.00 27.48  ? 2468 ASN A O     1 
ATOM   8868  C CB    . ASN A 1 2468 ? 129.350 199.930 185.429 1.00 27.48  ? 2468 ASN A CB    1 
ATOM   8869  C CG    . ASN A 1 2468 ? 129.580 198.841 184.404 1.00 27.48  ? 2468 ASN A CG    1 
ATOM   8870  O OD1   . ASN A 1 2468 ? 129.696 199.110 183.209 1.00 27.48  ? 2468 ASN A OD1   1 
ATOM   8871  N ND2   . ASN A 1 2468 ? 129.647 197.599 184.868 1.00 27.48  ? 2468 ASN A ND2   1 
ATOM   8872  N N     . VAL A 1 2469 ? 129.743 202.782 186.763 1.00 30.21  ? 2469 VAL A N     1 
ATOM   8873  C CA    . VAL A 1 2469 ? 129.328 203.828 187.697 1.00 30.21  ? 2469 VAL A CA    1 
ATOM   8874  C C     . VAL A 1 2469 ? 129.021 205.117 186.945 1.00 30.21  ? 2469 VAL A C     1 
ATOM   8875  O O     . VAL A 1 2469 ? 128.022 205.795 187.222 1.00 30.21  ? 2469 VAL A O     1 
ATOM   8876  C CB    . VAL A 1 2469 ? 130.403 204.047 188.776 1.00 30.21  ? 2469 VAL A CB    1 
ATOM   8877  C CG1   . VAL A 1 2469 ? 130.013 205.202 189.680 1.00 30.21  ? 2469 VAL A CG1   1 
ATOM   8878  C CG2   . VAL A 1 2469 ? 130.603 202.786 189.585 1.00 30.21  ? 2469 VAL A CG2   1 
ATOM   8879  N N     . ALA A 1 2470 ? 129.874 205.474 185.983 1.00 30.80  ? 2470 ALA A N     1 
ATOM   8880  C CA    . ALA A 1 2470 ? 129.633 206.679 185.193 1.00 30.80  ? 2470 ALA A CA    1 
ATOM   8881  C C     . ALA A 1 2470 ? 128.339 206.571 184.395 1.00 30.80  ? 2470 ALA A C     1 
ATOM   8882  O O     . ALA A 1 2470 ? 127.572 207.537 184.301 1.00 30.80  ? 2470 ALA A O     1 
ATOM   8883  C CB    . ALA A 1 2470 ? 130.816 206.944 184.263 1.00 30.80  ? 2470 ALA A CB    1 
ATOM   8884  N N     . GLN A 1 2471 ? 128.083 205.401 183.807 1.00 34.40  ? 2471 GLN A N     1 
ATOM   8885  C CA    . GLN A 1 2471 ? 126.854 205.201 183.045 1.00 34.40  ? 2471 GLN A CA    1 
ATOM   8886  C C     . GLN A 1 2471 ? 125.626 205.305 183.940 1.00 34.40  ? 2471 GLN A C     1 
ATOM   8887  O O     . GLN A 1 2471 ? 124.608 205.883 183.543 1.00 34.40  ? 2471 GLN A O     1 
ATOM   8888  C CB    . GLN A 1 2471 ? 126.891 203.847 182.338 1.00 34.40  ? 2471 GLN A CB    1 
ATOM   8889  C CG    . GLN A 1 2471 ? 125.665 203.553 181.495 1.00 34.40  ? 2471 GLN A CG    1 
ATOM   8890  C CD    . GLN A 1 2471 ? 125.562 202.090 181.115 1.00 34.40  ? 2471 GLN A CD    1 
ATOM   8891  O OE1   . GLN A 1 2471 ? 126.572 201.407 180.948 1.00 34.40  ? 2471 GLN A OE1   1 
ATOM   8892  N NE2   . GLN A 1 2471 ? 124.335 201.599 180.979 1.00 34.40  ? 2471 GLN A NE2   1 
ATOM   8893  N N     . TYR A 1 2472 ? 125.697 204.740 185.148 1.00 39.49  ? 2472 TYR A N     1 
ATOM   8894  C CA    . TYR A 1 2472 ? 124.583 204.857 186.082 1.00 39.49  ? 2472 TYR A CA    1 
ATOM   8895  C C     . TYR A 1 2472 ? 124.347 206.308 186.478 1.00 39.49  ? 2472 TYR A C     1 
ATOM   8896  O O     . TYR A 1 2472 ? 123.198 206.752 186.584 1.00 39.49  ? 2472 TYR A O     1 
ATOM   8897  C CB    . TYR A 1 2472 ? 124.835 204.006 187.324 1.00 39.49  ? 2472 TYR A CB    1 
ATOM   8898  C CG    . TYR A 1 2472 ? 123.854 204.275 188.442 1.00 39.49  ? 2472 TYR A CG    1 
ATOM   8899  C CD1   . TYR A 1 2472 ? 122.540 203.839 188.358 1.00 39.49  ? 2472 TYR A CD1   1 
ATOM   8900  C CD2   . TYR A 1 2472 ? 124.241 204.972 189.578 1.00 39.49  ? 2472 TYR A CD2   1 
ATOM   8901  C CE1   . TYR A 1 2472 ? 121.640 204.085 189.375 1.00 39.49  ? 2472 TYR A CE1   1 
ATOM   8902  C CE2   . TYR A 1 2472 ? 123.347 205.222 190.600 1.00 39.49  ? 2472 TYR A CE2   1 
ATOM   8903  C CZ    . TYR A 1 2472 ? 122.048 204.777 190.493 1.00 39.49  ? 2472 TYR A CZ    1 
ATOM   8904  O OH    . TYR A 1 2472 ? 121.154 205.024 191.509 1.00 39.49  ? 2472 TYR A OH    1 
ATOM   8905  N N     . ASN A 1 2473 ? 125.425 207.059 186.713 1.00 42.45  ? 2473 ASN A N     1 
ATOM   8906  C CA    . ASN A 1 2473 ? 125.275 208.477 187.023 1.00 42.45  ? 2473 ASN A CA    1 
ATOM   8907  C C     . ASN A 1 2473 ? 124.628 209.225 185.864 1.00 42.45  ? 2473 ASN A C     1 
ATOM   8908  O O     . ASN A 1 2473 ? 123.790 210.109 186.075 1.00 42.45  ? 2473 ASN A O     1 
ATOM   8909  C CB    . ASN A 1 2473 ? 126.631 209.089 187.370 1.00 42.45  ? 2473 ASN A CB    1 
ATOM   8910  C CG    . ASN A 1 2473 ? 126.963 208.968 188.842 1.00 42.45  ? 2473 ASN A CG    1 
ATOM   8911  O OD1   . ASN A 1 2473 ? 126.160 208.474 189.632 1.00 42.45  ? 2473 ASN A OD1   1 
ATOM   8912  N ND2   . ASN A 1 2473 ? 128.152 209.423 189.220 1.00 42.45  ? 2473 ASN A ND2   1 
ATOM   8913  N N     . ALA A 1 2474 ? 125.010 208.885 184.631 1.00 40.36  ? 2474 ALA A N     1 
ATOM   8914  C CA    . ALA A 1 2474 ? 124.386 209.506 183.466 1.00 40.36  ? 2474 ALA A CA    1 
ATOM   8915  C C     . ALA A 1 2474 ? 122.905 209.154 183.377 1.00 40.36  ? 2474 ALA A C     1 
ATOM   8916  O O     . ALA A 1 2474 ? 122.079 210.000 183.017 1.00 40.36  ? 2474 ALA A O     1 
ATOM   8917  C CB    . ALA A 1 2474 ? 125.117 209.085 182.192 1.00 40.36  ? 2474 ALA A CB    1 
ATOM   8918  N N     . ASN A 1 2475 ? 122.552 207.906 183.695 1.00 46.06  ? 2475 ASN A N     1 
ATOM   8919  C CA    . ASN A 1 2475 ? 121.156 207.485 183.655 1.00 46.06  ? 2475 ASN A CA    1 
ATOM   8920  C C     . ASN A 1 2475 ? 120.316 208.142 184.742 1.00 46.06  ? 2475 ASN A C     1 
ATOM   8921  O O     . ASN A 1 2475 ? 119.088 208.181 184.619 1.00 46.06  ? 2475 ASN A O     1 
ATOM   8922  C CB    . ASN A 1 2475 ? 121.059 205.964 183.782 1.00 46.06  ? 2475 ASN A CB    1 
ATOM   8923  C CG    . ASN A 1 2475 ? 121.261 205.255 182.458 1.00 46.06  ? 2475 ASN A CG    1 
ATOM   8924  O OD1   . ASN A 1 2475 ? 121.336 205.888 181.406 1.00 46.06  ? 2475 ASN A OD1   1 
ATOM   8925  N ND2   . ASN A 1 2475 ? 121.349 203.930 182.505 1.00 46.06  ? 2475 ASN A ND2   1 
ATOM   8926  N N     . HIS A 1 2476 ? 120.944 208.651 185.800 1.00 50.68  ? 2476 HIS A N     1 
ATOM   8927  C CA    . HIS A 1 2476 ? 120.249 209.318 186.900 1.00 50.68  ? 2476 HIS A CA    1 
ATOM   8928  C C     . HIS A 1 2476 ? 120.863 210.697 187.089 1.00 50.68  ? 2476 HIS A C     1 
ATOM   8929  O O     . HIS A 1 2476 ? 121.715 210.896 187.966 1.00 50.68  ? 2476 HIS A O     1 
ATOM   8930  C CB    . HIS A 1 2476 ? 120.328 208.500 188.191 1.00 50.68  ? 2476 HIS A CB    1 
ATOM   8931  C CG    . HIS A 1 2476 ? 119.627 207.179 188.119 1.00 50.68  ? 2476 HIS A CG    1 
ATOM   8932  N ND1   . HIS A 1 2476 ? 119.933 206.222 187.176 1.00 50.68  ? 2476 HIS A ND1   1 
ATOM   8933  C CD2   . HIS A 1 2476 ? 118.639 206.654 188.881 1.00 50.68  ? 2476 HIS A CD2   1 
ATOM   8934  C CE1   . HIS A 1 2476 ? 119.160 205.166 187.356 1.00 50.68  ? 2476 HIS A CE1   1 
ATOM   8935  N NE2   . HIS A 1 2476 ? 118.367 205.402 188.385 1.00 50.68  ? 2476 HIS A NE2   1 
ATOM   8936  N N     . PRO A 1 2477 ? 120.462 211.675 186.272 1.00 54.02  ? 2477 PRO A N     1 
ATOM   8937  C CA    . PRO A 1 2477 ? 120.995 213.036 186.448 1.00 54.02  ? 2477 PRO A CA    1 
ATOM   8938  C C     . PRO A 1 2477 ? 120.712 213.613 187.821 1.00 54.02  ? 2477 PRO A C     1 
ATOM   8939  O O     . PRO A 1 2477 ? 121.536 214.370 188.349 1.00 54.02  ? 2477 PRO A O     1 
ATOM   8940  C CB    . PRO A 1 2477 ? 120.291 213.834 185.341 1.00 54.02  ? 2477 PRO A CB    1 
ATOM   8941  C CG    . PRO A 1 2477 ? 119.862 212.808 184.341 1.00 54.02  ? 2477 PRO A CG    1 
ATOM   8942  C CD    . PRO A 1 2477 ? 119.531 211.585 185.136 1.00 54.02  ? 2477 PRO A CD    1 
ATOM   8943  N N     . ASP A 1 2478 ? 119.573 213.279 188.416 1.00 62.38  ? 2478 ASP A N     1 
ATOM   8944  C CA    . ASP A 1 2478 ? 119.260 213.658 189.784 1.00 62.38  ? 2478 ASP A CA    1 
ATOM   8945  C C     . ASP A 1 2478 ? 119.538 212.480 190.707 1.00 62.38  ? 2478 ASP A C     1 
ATOM   8946  O O     . ASP A 1 2478 ? 119.258 211.329 190.359 1.00 62.38  ? 2478 ASP A O     1 
ATOM   8947  C CB    . ASP A 1 2478 ? 117.801 214.098 189.914 1.00 62.38  ? 2478 ASP A CB    1 
ATOM   8948  C CG    . ASP A 1 2478 ? 117.452 215.236 188.976 1.00 62.38  ? 2478 ASP A CG    1 
ATOM   8949  O OD1   . ASP A 1 2478 ? 118.383 215.853 188.417 1.00 62.38  ? 2478 ASP A OD1   1 
ATOM   8950  O OD2   . ASP A 1 2478 ? 116.248 215.513 188.797 1.00 62.38  ? 2478 ASP A OD2   1 
ATOM   8951  N N     . PHE A 1 2479 ? 120.096 212.778 191.881 1.00 71.23  ? 2479 PHE A N     1 
ATOM   8952  C CA    . PHE A 1 2479 ? 120.486 211.772 192.864 1.00 71.23  ? 2479 PHE A CA    1 
ATOM   8953  C C     . PHE A 1 2479 ? 121.464 210.776 192.251 1.00 71.23  ? 2479 PHE A C     1 
ATOM   8954  O O     . PHE A 1 2479 ? 121.105 209.613 192.026 1.00 71.23  ? 2479 PHE A O     1 
ATOM   8955  C CB    . PHE A 1 2479 ? 119.259 211.042 193.416 1.00 71.23  ? 2479 PHE A CB    1 
ATOM   8956  C CG    . PHE A 1 2479 ? 118.363 211.910 194.250 1.00 71.23  ? 2479 PHE A CG    1 
ATOM   8957  C CD1   . PHE A 1 2479 ? 118.657 212.153 195.581 1.00 71.23  ? 2479 PHE A CD1   1 
ATOM   8958  C CD2   . PHE A 1 2479 ? 117.229 212.484 193.702 1.00 71.23  ? 2479 PHE A CD2   1 
ATOM   8959  C CE1   . PHE A 1 2479 ? 117.834 212.951 196.352 1.00 71.23  ? 2479 PHE A CE1   1 
ATOM   8960  C CE2   . PHE A 1 2479 ? 116.402 213.283 194.467 1.00 71.23  ? 2479 PHE A CE2   1 
ATOM   8961  C CZ    . PHE A 1 2479 ? 116.705 213.517 195.794 1.00 71.23  ? 2479 PHE A CZ    1 
ATOM   8962  N N     . PRO A 1 2480 ? 122.703 211.186 191.967 1.00 63.37  ? 2480 PRO A N     1 
ATOM   8963  C CA    . PRO A 1 2480 ? 123.674 210.247 191.391 1.00 63.37  ? 2480 PRO A CA    1 
ATOM   8964  C C     . PRO A 1 2480 ? 124.167 209.239 192.415 1.00 63.37  ? 2480 PRO A C     1 
ATOM   8965  O O     . PRO A 1 2480 ? 123.666 209.198 193.543 1.00 63.37  ? 2480 PRO A O     1 
ATOM   8966  C CB    . PRO A 1 2480 ? 124.803 211.166 190.911 1.00 63.37  ? 2480 PRO A CB    1 
ATOM   8967  C CG    . PRO A 1 2480 ? 124.745 212.324 191.843 1.00 63.37  ? 2480 PRO A CG    1 
ATOM   8968  C CD    . PRO A 1 2480 ? 123.290 212.520 192.190 1.00 63.37  ? 2480 PRO A CD    1 
ATOM   8969  N N     . MET A 1 2481 ? 125.141 208.416 192.030 1.00 48.38  ? 2481 MET A N     1 
ATOM   8970  C CA    . MET A 1 2481 ? 125.662 207.399 192.933 1.00 48.38  ? 2481 MET A CA    1 
ATOM   8971  C C     . MET A 1 2481 ? 126.261 208.045 194.176 1.00 48.38  ? 2481 MET A C     1 
ATOM   8972  O O     . MET A 1 2481 ? 127.066 208.976 194.082 1.00 48.38  ? 2481 MET A O     1 
ATOM   8973  C CB    . MET A 1 2481 ? 126.713 206.553 192.214 1.00 48.38  ? 2481 MET A CB    1 
ATOM   8974  C CG    . MET A 1 2481 ? 127.275 205.414 193.044 1.00 48.38  ? 2481 MET A CG    1 
ATOM   8975  S SD    . MET A 1 2481 ? 126.454 203.846 192.706 1.00 48.38  ? 2481 MET A SD    1 
ATOM   8976  C CE    . MET A 1 2481 ? 127.218 203.386 191.154 1.00 48.38  ? 2481 MET A CE    1 
ATOM   8977  N N     . GLN A 1 2482 ? 125.866 207.544 195.344 1.00 47.93  ? 2482 GLN A N     1 
ATOM   8978  C CA    . GLN A 1 2482 ? 126.329 208.084 196.611 1.00 47.93  ? 2482 GLN A CA    1 
ATOM   8979  C C     . GLN A 1 2482 ? 127.557 207.315 197.093 1.00 47.93  ? 2482 GLN A C     1 
ATOM   8980  O O     . GLN A 1 2482 ? 127.907 206.257 196.567 1.00 47.93  ? 2482 GLN A O     1 
ATOM   8981  C CB    . GLN A 1 2482 ? 125.208 208.047 197.648 1.00 47.93  ? 2482 GLN A CB    1 
ATOM   8982  C CG    . GLN A 1 2482 ? 124.101 209.054 197.390 1.00 47.93  ? 2482 GLN A CG    1 
ATOM   8983  C CD    . GLN A 1 2482 ? 124.629 210.464 197.211 1.00 47.93  ? 2482 GLN A CD    1 
ATOM   8984  O OE1   . GLN A 1 2482 ? 125.277 211.014 198.101 1.00 47.93  ? 2482 GLN A OE1   1 
ATOM   8985  N NE2   . GLN A 1 2482 ? 124.355 211.056 196.054 1.00 47.93  ? 2482 GLN A NE2   1 
ATOM   8986  N N     . ILE A 1 2483 ? 128.221 207.856 198.116 1.00 46.31  ? 2483 ILE A N     1 
ATOM   8987  C CA    . ILE A 1 2483 ? 129.491 207.287 198.557 1.00 46.31  ? 2483 ILE A CA    1 
ATOM   8988  C C     . ILE A 1 2483 ? 129.288 205.911 199.186 1.00 46.31  ? 2483 ILE A C     1 
ATOM   8989  O O     . ILE A 1 2483 ? 130.129 205.021 199.030 1.00 46.31  ? 2483 ILE A O     1 
ATOM   8990  C CB    . ILE A 1 2483 ? 130.221 208.263 199.502 1.00 46.31  ? 2483 ILE A CB    1 
ATOM   8991  C CG1   . ILE A 1 2483 ? 131.702 207.891 199.612 1.00 46.31  ? 2483 ILE A CG1   1 
ATOM   8992  C CG2   . ILE A 1 2483 ? 129.558 208.325 200.868 1.00 46.31  ? 2483 ILE A CG2   1 
ATOM   8993  C CD1   . ILE A 1 2483 ? 132.405 207.796 198.278 1.00 46.31  ? 2483 ILE A CD1   1 
ATOM   8994  N N     . GLU A 1 2484 ? 128.175 205.705 199.896 1.00 47.53  ? 2484 GLU A N     1 
ATOM   8995  C CA    . GLU A 1 2484 ? 127.908 204.383 200.457 1.00 47.53  ? 2484 GLU A CA    1 
ATOM   8996  C C     . GLU A 1 2484 ? 127.594 203.369 199.363 1.00 47.53  ? 2484 GLU A C     1 
ATOM   8997  O O     . GLU A 1 2484 ? 128.138 202.256 199.361 1.00 47.53  ? 2484 GLU A O     1 
ATOM   8998  C CB    . GLU A 1 2484 ? 126.757 204.451 201.462 1.00 47.53  ? 2484 GLU A CB    1 
ATOM   8999  C CG    . GLU A 1 2484 ? 127.126 205.030 202.819 1.00 47.53  ? 2484 GLU A CG    1 
ATOM   9000  C CD    . GLU A 1 2484 ? 126.999 206.538 202.870 1.00 47.53  ? 2484 GLU A CD    1 
ATOM   9001  O OE1   . GLU A 1 2484 ? 127.948 207.198 203.342 1.00 47.53  ? 2484 GLU A OE1   1 
ATOM   9002  O OE2   . GLU A 1 2484 ? 125.952 207.063 202.438 1.00 47.53  ? 2484 GLU A OE2   1 
ATOM   9003  N N     . GLN A 1 2485 ? 126.713 203.734 198.429 1.00 42.87  ? 2485 GLN A N     1 
ATOM   9004  C CA    . GLN A 1 2485 ? 126.383 202.833 197.331 1.00 42.87  ? 2485 GLN A CA    1 
ATOM   9005  C C     . GLN A 1 2485 ? 127.600 202.565 196.458 1.00 42.87  ? 2485 GLN A C     1 
ATOM   9006  O O     . GLN A 1 2485 ? 127.832 201.424 196.042 1.00 42.87  ? 2485 GLN A O     1 
ATOM   9007  C CB    . GLN A 1 2485 ? 125.242 203.417 196.500 1.00 42.87  ? 2485 GLN A CB    1 
ATOM   9008  C CG    . GLN A 1 2485 ? 124.723 202.489 195.418 1.00 42.87  ? 2485 GLN A CG    1 
ATOM   9009  C CD    . GLN A 1 2485 ? 123.455 203.005 194.770 1.00 42.87  ? 2485 GLN A CD    1 
ATOM   9010  O OE1   . GLN A 1 2485 ? 122.895 204.016 195.194 1.00 42.87  ? 2485 GLN A OE1   1 
ATOM   9011  N NE2   . GLN A 1 2485 ? 122.996 202.314 193.734 1.00 42.87  ? 2485 GLN A NE2   1 
ATOM   9012  N N     . LEU A 1 2486 ? 128.390 203.603 196.172 1.00 38.37  ? 2486 LEU A N     1 
ATOM   9013  C CA    . LEU A 1 2486 ? 129.611 203.413 195.397 1.00 38.37  ? 2486 LEU A CA    1 
ATOM   9014  C C     . LEU A 1 2486 ? 130.593 202.513 196.132 1.00 38.37  ? 2486 LEU A C     1 
ATOM   9015  O O     . LEU A 1 2486 ? 131.239 201.656 195.519 1.00 38.37  ? 2486 LEU A O     1 
ATOM   9016  C CB    . LEU A 1 2486 ? 130.253 204.765 195.086 1.00 38.37  ? 2486 LEU A CB    1 
ATOM   9017  C CG    . LEU A 1 2486 ? 131.478 204.768 194.171 1.00 38.37  ? 2486 LEU A CG    1 
ATOM   9018  C CD1   . LEU A 1 2486 ? 131.270 203.841 192.990 1.00 38.37  ? 2486 LEU A CD1   1 
ATOM   9019  C CD2   . LEU A 1 2486 ? 131.783 206.179 193.696 1.00 38.37  ? 2486 LEU A CD2   1 
ATOM   9020  N N     . GLU A 1 2487 ? 130.722 202.695 197.448 1.00 38.36  ? 2487 GLU A N     1 
ATOM   9021  C CA    . GLU A 1 2487 ? 131.617 201.853 198.232 1.00 38.36  ? 2487 GLU A CA    1 
ATOM   9022  C C     . GLU A 1 2487 ? 131.192 200.394 198.161 1.00 38.36  ? 2487 GLU A C     1 
ATOM   9023  O O     . GLU A 1 2487 ? 132.019 199.508 197.923 1.00 38.36  ? 2487 GLU A O     1 
ATOM   9024  C CB    . GLU A 1 2487 ? 131.653 202.333 199.682 1.00 38.36  ? 2487 GLU A CB    1 
ATOM   9025  C CG    . GLU A 1 2487 ? 132.386 201.396 200.627 1.00 38.36  ? 2487 GLU A CG    1 
ATOM   9026  C CD    . GLU A 1 2487 ? 132.899 202.101 201.866 1.00 38.36  ? 2487 GLU A CD    1 
ATOM   9027  O OE1   . GLU A 1 2487 ? 132.110 202.825 202.508 1.00 38.36  ? 2487 GLU A OE1   1 
ATOM   9028  O OE2   . GLU A 1 2487 ? 134.090 201.932 202.199 1.00 38.36  ? 2487 GLU A OE2   1 
ATOM   9029  N N     . ARG A 1 2488 ? 129.898 200.128 198.350 1.00 36.39  ? 2488 ARG A N     1 
ATOM   9030  C CA    . ARG A 1 2488 ? 129.412 198.753 198.284 1.00 36.39  ? 2488 ARG A CA    1 
ATOM   9031  C C     . ARG A 1 2488 ? 129.625 198.162 196.895 1.00 36.39  ? 2488 ARG A C     1 
ATOM   9032  O O     . ARG A 1 2488 ? 130.084 197.020 196.753 1.00 36.39  ? 2488 ARG A O     1 
ATOM   9033  C CB    . ARG A 1 2488 ? 127.933 198.696 198.669 1.00 36.39  ? 2488 ARG A CB    1 
ATOM   9034  C CG    . ARG A 1 2488 ? 127.648 199.032 200.122 1.00 36.39  ? 2488 ARG A CG    1 
ATOM   9035  C CD    . ARG A 1 2488 ? 126.307 198.466 200.565 1.00 36.39  ? 2488 ARG A CD    1 
ATOM   9036  N NE    . ARG A 1 2488 ? 125.239 199.455 200.482 1.00 36.39  ? 2488 ARG A NE    1 
ATOM   9037  C CZ    . ARG A 1 2488 ? 124.486 199.659 199.410 1.00 36.39  ? 2488 ARG A CZ    1 
ATOM   9038  N NH1   . ARG A 1 2488 ? 124.650 198.950 198.305 1.00 36.39  ? 2488 ARG A NH1   1 
ATOM   9039  N NH2   . ARG A 1 2488 ? 123.544 200.596 199.447 1.00 36.39  ? 2488 ARG A NH2   1 
ATOM   9040  N N     . TYR A 1 2489 ? 129.304 198.935 195.854 1.00 30.98  ? 2489 TYR A N     1 
ATOM   9041  C CA    . TYR A 1 2489 ? 129.425 198.430 194.492 1.00 30.98  ? 2489 TYR A CA    1 
ATOM   9042  C C     . TYR A 1 2489 ? 130.871 198.110 194.145 1.00 30.98  ? 2489 TYR A C     1 
ATOM   9043  O O     . TYR A 1 2489 ? 131.154 197.056 193.571 1.00 30.98  ? 2489 TYR A O     1 
ATOM   9044  C CB    . TYR A 1 2489 ? 128.850 199.439 193.501 1.00 30.98  ? 2489 TYR A CB    1 
ATOM   9045  C CG    . TYR A 1 2489 ? 128.962 199.003 192.059 1.00 30.98  ? 2489 TYR A CG    1 
ATOM   9046  C CD1   . TYR A 1 2489 ? 128.345 197.843 191.617 1.00 30.98  ? 2489 TYR A CD1   1 
ATOM   9047  C CD2   . TYR A 1 2489 ? 129.678 199.753 191.140 1.00 30.98  ? 2489 TYR A CD2   1 
ATOM   9048  C CE1   . TYR A 1 2489 ? 128.442 197.440 190.300 1.00 30.98  ? 2489 TYR A CE1   1 
ATOM   9049  C CE2   . TYR A 1 2489 ? 129.780 199.358 189.821 1.00 30.98  ? 2489 TYR A CE2   1 
ATOM   9050  C CZ    . TYR A 1 2489 ? 129.159 198.202 189.407 1.00 30.98  ? 2489 TYR A CZ    1 
ATOM   9051  O OH    . TYR A 1 2489 ? 129.258 197.806 188.094 1.00 30.98  ? 2489 TYR A OH    1 
ATOM   9052  N N     . ILE A 1 2490 ? 131.803 198.999 194.494 1.00 28.18  ? 2490 ILE A N     1 
ATOM   9053  C CA    . ILE A 1 2490 ? 133.207 198.750 194.185 1.00 28.18  ? 2490 ILE A CA    1 
ATOM   9054  C C     . ILE A 1 2490 ? 133.747 197.600 195.026 1.00 28.18  ? 2490 ILE A C     1 
ATOM   9055  O O     . ILE A 1 2490 ? 134.516 196.766 194.535 1.00 28.18  ? 2490 ILE A O     1 
ATOM   9056  C CB    . ILE A 1 2490 ? 134.034 200.034 194.373 1.00 28.18  ? 2490 ILE A CB    1 
ATOM   9057  C CG1   . ILE A 1 2490 ? 133.603 201.090 193.357 1.00 28.18  ? 2490 ILE A CG1   1 
ATOM   9058  C CG2   . ILE A 1 2490 ? 135.516 199.743 194.223 1.00 28.18  ? 2490 ILE A CG2   1 
ATOM   9059  C CD1   . ILE A 1 2490 ? 133.831 200.676 191.924 1.00 28.18  ? 2490 ILE A CD1   1 
ATOM   9060  N N     . GLN A 1 2491 ? 133.340 197.522 196.296 1.00 30.60  ? 2491 GLN A N     1 
ATOM   9061  C CA    . GLN A 1 2491 ? 133.817 196.449 197.160 1.00 30.60  ? 2491 GLN A CA    1 
ATOM   9062  C C     . GLN A 1 2491 ? 133.384 195.087 196.636 1.00 30.60  ? 2491 GLN A C     1 
ATOM   9063  O O     . GLN A 1 2491 ? 134.161 194.127 196.665 1.00 30.60  ? 2491 GLN A O     1 
ATOM   9064  C CB    . GLN A 1 2491 ? 133.304 196.665 198.583 1.00 30.60  ? 2491 GLN A CB    1 
ATOM   9065  C CG    . GLN A 1 2491 ? 134.310 196.337 199.670 1.00 30.60  ? 2491 GLN A CG    1 
ATOM   9066  C CD    . GLN A 1 2491 ? 133.725 196.463 201.064 1.00 30.60  ? 2491 GLN A CD    1 
ATOM   9067  O OE1   . GLN A 1 2491 ? 132.801 197.243 201.294 1.00 30.60  ? 2491 GLN A OE1   1 
ATOM   9068  N NE2   . GLN A 1 2491 ? 134.264 195.695 202.003 1.00 30.60  ? 2491 GLN A NE2   1 
ATOM   9069  N N     . ARG A 1 2492 ? 132.143 194.981 196.156 1.00 32.91  ? 2492 ARG A N     1 
ATOM   9070  C CA    . ARG A 1 2492 ? 131.678 193.705 195.621 1.00 32.91  ? 2492 ARG A CA    1 
ATOM   9071  C C     . ARG A 1 2492 ? 132.230 193.435 194.223 1.00 32.91  ? 2492 ARG A C     1 
ATOM   9072  O O     . ARG A 1 2492 ? 132.543 192.285 193.887 1.00 32.91  ? 2492 ARG A O     1 
ATOM   9073  C CB    . ARG A 1 2492 ? 130.151 193.669 195.627 1.00 32.91  ? 2492 ARG A CB    1 
ATOM   9074  C CG    . ARG A 1 2492 ? 129.559 193.573 197.022 1.00 32.91  ? 2492 ARG A CG    1 
ATOM   9075  C CD    . ARG A 1 2492 ? 128.206 194.252 197.110 1.00 32.91  ? 2492 ARG A CD    1 
ATOM   9076  N NE    . ARG A 1 2492 ? 127.981 194.840 198.425 1.00 32.91  ? 2492 ARG A NE    1 
ATOM   9077  C CZ    . ARG A 1 2492 ? 127.716 194.145 199.523 1.00 32.91  ? 2492 ARG A CZ    1 
ATOM   9078  N NH1   . ARG A 1 2492 ? 127.613 192.827 199.499 1.00 32.91  ? 2492 ARG A NH1   1 
ATOM   9079  N NH2   . ARG A 1 2492 ? 127.546 194.790 200.674 1.00 32.91  ? 2492 ARG A NH2   1 
ATOM   9080  N N     . TYR A 1 2493 ? 132.366 194.477 193.396 1.00 20.91  ? 2493 TYR A N     1 
ATOM   9081  C CA    . TYR A 1 2493 ? 132.919 194.293 192.061 1.00 20.91  ? 2493 TYR A CA    1 
ATOM   9082  C C     . TYR A 1 2493 ? 134.375 193.867 192.114 1.00 20.91  ? 2493 TYR A C     1 
ATOM   9083  O O     . TYR A 1 2493 ? 134.833 193.143 191.228 1.00 20.91  ? 2493 TYR A O     1 
ATOM   9084  C CB    . TYR A 1 2493 ? 132.778 195.576 191.243 1.00 20.91  ? 2493 TYR A CB    1 
ATOM   9085  C CG    . TYR A 1 2493 ? 132.811 195.351 189.748 1.00 20.91  ? 2493 TYR A CG    1 
ATOM   9086  C CD1   . TYR A 1 2493 ? 134.001 195.073 189.092 1.00 20.91  ? 2493 TYR A CD1   1 
ATOM   9087  C CD2   . TYR A 1 2493 ? 131.652 195.413 188.994 1.00 20.91  ? 2493 TYR A CD2   1 
ATOM   9088  C CE1   . TYR A 1 2493 ? 134.034 194.863 187.731 1.00 20.91  ? 2493 TYR A CE1   1 
ATOM   9089  C CE2   . TYR A 1 2493 ? 131.674 195.204 187.631 1.00 20.91  ? 2493 TYR A CE2   1 
ATOM   9090  C CZ    . TYR A 1 2493 ? 132.868 194.931 187.005 1.00 20.91  ? 2493 TYR A CZ    1 
ATOM   9091  O OH    . TYR A 1 2493 ? 132.893 194.725 185.646 1.00 20.91  ? 2493 TYR A OH    1 
ATOM   9092  N N     . LEU A 1 2494 ? 135.122 194.306 193.127 1.00 24.04  ? 2494 LEU A N     1 
ATOM   9093  C CA    . LEU A 1 2494 ? 136.507 193.869 193.243 1.00 24.04  ? 2494 LEU A CA    1 
ATOM   9094  C C     . LEU A 1 2494 ? 136.590 192.363 193.443 1.00 24.04  ? 2494 LEU A C     1 
ATOM   9095  O O     . LEU A 1 2494 ? 137.414 191.689 192.815 1.00 24.04  ? 2494 LEU A O     1 
ATOM   9096  C CB    . LEU A 1 2494 ? 137.194 194.602 194.391 1.00 24.04  ? 2494 LEU A CB    1 
ATOM   9097  C CG    . LEU A 1 2494 ? 138.693 194.345 194.475 1.00 24.04  ? 2494 LEU A CG    1 
ATOM   9098  C CD1   . LEU A 1 2494 ? 139.359 194.749 193.175 1.00 24.04  ? 2494 LEU A CD1   1 
ATOM   9099  C CD2   . LEU A 1 2494 ? 139.279 195.110 195.634 1.00 24.04  ? 2494 LEU A CD2   1 
ATOM   9100  N N     . VAL A 1 2495 ? 135.728 191.813 194.298 1.00 24.63  ? 2495 VAL A N     1 
ATOM   9101  C CA    . VAL A 1 2495 ? 135.699 190.368 194.494 1.00 24.63  ? 2495 VAL A CA    1 
ATOM   9102  C C     . VAL A 1 2495 ? 135.227 189.665 193.229 1.00 24.63  ? 2495 VAL A C     1 
ATOM   9103  O O     . VAL A 1 2495 ? 135.778 188.631 192.836 1.00 24.63  ? 2495 VAL A O     1 
ATOM   9104  C CB    . VAL A 1 2495 ? 134.818 190.019 195.704 1.00 24.63  ? 2495 VAL A CB    1 
ATOM   9105  C CG1   . VAL A 1 2495 ? 134.704 188.515 195.863 1.00 24.63  ? 2495 VAL A CG1   1 
ATOM   9106  C CG2   . VAL A 1 2495 ? 135.401 190.640 196.948 1.00 24.63  ? 2495 VAL A CG2   1 
ATOM   9107  N N     . TYR A 1 2496 ? 134.206 190.217 192.570 1.00 22.76  ? 2496 TYR A N     1 
ATOM   9108  C CA    . TYR A 1 2496 ? 133.729 189.622 191.325 1.00 22.76  ? 2496 TYR A CA    1 
ATOM   9109  C C     . TYR A 1 2496 ? 134.848 189.560 190.289 1.00 22.76  ? 2496 TYR A C     1 
ATOM   9110  O O     . TYR A 1 2496 ? 135.035 188.537 189.617 1.00 22.76  ? 2496 TYR A O     1 
ATOM   9111  C CB    . TYR A 1 2496 ? 132.532 190.418 190.805 1.00 22.76  ? 2496 TYR A CB    1 
ATOM   9112  C CG    . TYR A 1 2496 ? 132.202 190.232 189.341 1.00 22.76  ? 2496 TYR A CG    1 
ATOM   9113  C CD1   . TYR A 1 2496 ? 131.448 189.151 188.915 1.00 22.76  ? 2496 TYR A CD1   1 
ATOM   9114  C CD2   . TYR A 1 2496 ? 132.604 191.162 188.394 1.00 22.76  ? 2496 TYR A CD2   1 
ATOM   9115  C CE1   . TYR A 1 2496 ? 131.128 188.986 187.583 1.00 22.76  ? 2496 TYR A CE1   1 
ATOM   9116  C CE2   . TYR A 1 2496 ? 132.290 191.005 187.057 1.00 22.76  ? 2496 TYR A CE2   1 
ATOM   9117  C CZ    . TYR A 1 2496 ? 131.552 189.913 186.658 1.00 22.76  ? 2496 TYR A CZ    1 
ATOM   9118  O OH    . TYR A 1 2496 ? 131.235 189.750 185.331 1.00 22.76  ? 2496 TYR A OH    1 
ATOM   9119  N N     . ALA A 1 2497 ? 135.628 190.635 190.180 1.00 23.18  ? 2497 ALA A N     1 
ATOM   9120  C CA    . ALA A 1 2497 ? 136.702 190.693 189.206 1.00 23.18  ? 2497 ALA A CA    1 
ATOM   9121  C C     . ALA A 1 2497 ? 137.877 189.808 189.596 1.00 23.18  ? 2497 ALA A C     1 
ATOM   9122  O O     . ALA A 1 2497 ? 138.566 189.274 188.716 1.00 23.18  ? 2497 ALA A O     1 
ATOM   9123  C CB    . ALA A 1 2497 ? 137.164 192.138 189.020 1.00 23.18  ? 2497 ALA A CB    1 
ATOM   9124  N N     . ILE A 1 2498 ? 138.139 189.646 190.895 1.00 23.79  ? 2498 ILE A N     1 
ATOM   9125  C CA    . ILE A 1 2498 ? 139.179 188.713 191.318 1.00 23.79  ? 2498 ILE A CA    1 
ATOM   9126  C C     . ILE A 1 2498 ? 138.784 187.286 190.962 1.00 23.79  ? 2498 ILE A C     1 
ATOM   9127  O O     . ILE A 1 2498 ? 139.602 186.511 190.452 1.00 23.79  ? 2498 ILE A O     1 
ATOM   9128  C CB    . ILE A 1 2498 ? 139.467 188.873 192.821 1.00 23.79  ? 2498 ILE A CB    1 
ATOM   9129  C CG1   . ILE A 1 2498 ? 140.227 190.171 193.078 1.00 23.79  ? 2498 ILE A CG1   1 
ATOM   9130  C CG2   . ILE A 1 2498 ? 140.278 187.705 193.331 1.00 23.79  ? 2498 ILE A CG2   1 
ATOM   9131  C CD1   . ILE A 1 2498 ? 140.273 190.569 194.530 1.00 23.79  ? 2498 ILE A CD1   1 
ATOM   9132  N N     . LEU A 1 2499 ? 137.524 186.916 191.212 1.00 26.73  ? 2499 LEU A N     1 
ATOM   9133  C CA    . LEU A 1 2499 ? 137.068 185.587 190.809 1.00 26.73  ? 2499 LEU A CA    1 
ATOM   9134  C C     . LEU A 1 2499 ? 137.151 185.394 189.300 1.00 26.73  ? 2499 LEU A C     1 
ATOM   9135  O O     . LEU A 1 2499 ? 137.606 184.345 188.832 1.00 26.73  ? 2499 LEU A O     1 
ATOM   9136  C CB    . LEU A 1 2499 ? 135.641 185.319 191.293 1.00 26.73  ? 2499 LEU A CB    1 
ATOM   9137  C CG    . LEU A 1 2499 ? 135.392 184.819 192.720 1.00 26.73  ? 2499 LEU A CG    1 
ATOM   9138  C CD1   . LEU A 1 2499 ? 136.024 183.443 192.887 1.00 26.73  ? 2499 LEU A CD1   1 
ATOM   9139  C CD2   . LEU A 1 2499 ? 135.878 185.760 193.799 1.00 26.73  ? 2499 LEU A CD2   1 
ATOM   9140  N N     . TRP A 1 2500 ? 136.726 186.386 188.519 1.00 27.19  ? 2500 TRP A N     1 
ATOM   9141  C CA    . TRP A 1 2500 ? 136.667 186.166 187.079 1.00 27.19  ? 2500 TRP A CA    1 
ATOM   9142  C C     . TRP A 1 2500 ? 137.983 186.436 186.363 1.00 27.19  ? 2500 TRP A C     1 
ATOM   9143  O O     . TRP A 1 2500 ? 138.077 186.168 185.161 1.00 27.19  ? 2500 TRP A O     1 
ATOM   9144  C CB    . TRP A 1 2500 ? 135.560 187.015 186.459 1.00 27.19  ? 2500 TRP A CB    1 
ATOM   9145  C CG    . TRP A 1 2500 ? 134.296 186.246 186.284 1.00 27.19  ? 2500 TRP A CG    1 
ATOM   9146  C CD1   . TRP A 1 2500 ? 133.082 186.543 186.818 1.00 27.19  ? 2500 TRP A CD1   1 
ATOM   9147  C CD2   . TRP A 1 2500 ? 134.121 185.037 185.535 1.00 27.19  ? 2500 TRP A CD2   1 
ATOM   9148  N NE1   . TRP A 1 2500 ? 132.156 185.603 186.443 1.00 27.19  ? 2500 TRP A NE1   1 
ATOM   9149  C CE2   . TRP A 1 2500 ? 132.770 184.666 185.655 1.00 27.19  ? 2500 TRP A CE2   1 
ATOM   9150  C CE3   . TRP A 1 2500 ? 134.976 184.234 184.773 1.00 27.19  ? 2500 TRP A CE3   1 
ATOM   9151  C CZ2   . TRP A 1 2500 ? 132.252 183.530 185.043 1.00 27.19  ? 2500 TRP A CZ2   1 
ATOM   9152  C CZ3   . TRP A 1 2500 ? 134.458 183.108 184.164 1.00 27.19  ? 2500 TRP A CZ3   1 
ATOM   9153  C CH2   . TRP A 1 2500 ? 133.110 182.766 184.303 1.00 27.19  ? 2500 TRP A CH2   1 
ATOM   9154  N N     . SER A 1 2501 ? 138.991 186.953 187.058 1.00 24.21  ? 2501 SER A N     1 
ATOM   9155  C CA    . SER A 1 2501 ? 140.320 187.147 186.493 1.00 24.21  ? 2501 SER A CA    1 
ATOM   9156  C C     . SER A 1 2501 ? 141.340 186.160 187.033 1.00 24.21  ? 2501 SER A C     1 
ATOM   9157  O O     . SER A 1 2501 ? 142.117 185.594 186.262 1.00 24.21  ? 2501 SER A O     1 
ATOM   9158  C CB    . SER A 1 2501 ? 140.803 188.572 186.770 1.00 24.21  ? 2501 SER A CB    1 
ATOM   9159  O OG    . SER A 1 2501 ? 140.730 188.863 188.153 1.00 24.21  ? 2501 SER A OG    1 
ATOM   9160  N N     . LEU A 1 2502 ? 141.355 185.951 188.345 1.00 26.19  ? 2502 LEU A N     1 
ATOM   9161  C CA    . LEU A 1 2502 ? 142.158 184.901 188.953 1.00 26.19  ? 2502 LEU A CA    1 
ATOM   9162  C C     . LEU A 1 2502 ? 141.382 183.593 188.874 1.00 26.19  ? 2502 LEU A C     1 
ATOM   9163  O O     . LEU A 1 2502 ? 140.232 183.521 189.320 1.00 26.19  ? 2502 LEU A O     1 
ATOM   9164  C CB    . LEU A 1 2502 ? 142.486 185.251 190.402 1.00 26.19  ? 2502 LEU A CB    1 
ATOM   9165  C CG    . LEU A 1 2502 ? 143.469 186.386 190.688 1.00 26.19  ? 2502 LEU A CG    1 
ATOM   9166  C CD1   . LEU A 1 2502 ? 142.858 187.753 190.439 1.00 26.19  ? 2502 LEU A CD1   1 
ATOM   9167  C CD2   . LEU A 1 2502 ? 143.904 186.284 192.124 1.00 26.19  ? 2502 LEU A CD2   1 
ATOM   9168  N N     . SER A 1 2503 ? 142.002 182.568 188.293 1.00 34.86  ? 2503 SER A N     1 
ATOM   9169  C CA    . SER A 1 2503 ? 141.367 181.277 188.039 1.00 34.86  ? 2503 SER A CA    1 
ATOM   9170  C C     . SER A 1 2503 ? 140.108 181.412 187.190 1.00 34.86  ? 2503 SER A C     1 
ATOM   9171  O O     . SER A 1 2503 ? 139.231 180.545 187.234 1.00 34.86  ? 2503 SER A O     1 
ATOM   9172  C CB    . SER A 1 2503 ? 141.036 180.540 189.340 1.00 34.86  ? 2503 SER A CB    1 
ATOM   9173  O OG    . SER A 1 2503 ? 139.910 181.120 189.970 1.00 34.86  ? 2503 SER A OG    1 
ATOM   9174  N N     . GLY A 1 2504 ? 139.999 182.491 186.417 1.00 30.72  ? 2504 GLY A N     1 
ATOM   9175  C CA    . GLY A 1 2504 ? 138.925 182.610 185.453 1.00 30.72  ? 2504 GLY A CA    1 
ATOM   9176  C C     . GLY A 1 2504 ? 139.112 181.769 184.217 1.00 30.72  ? 2504 GLY A C     1 
ATOM   9177  O O     . GLY A 1 2504 ? 138.205 181.693 183.383 1.00 30.72  ? 2504 GLY A O     1 
ATOM   9178  N N     . ASP A 1 2505 ? 140.278 181.140 184.083 1.00 30.46  ? 2505 ASP A N     1 
ATOM   9179  C CA    . ASP A 1 2505 ? 140.583 180.231 182.988 1.00 30.46  ? 2505 ASP A CA    1 
ATOM   9180  C C     . ASP A 1 2505 ? 140.790 178.803 183.482 1.00 30.46  ? 2505 ASP A C     1 
ATOM   9181  O O     . ASP A 1 2505 ? 141.527 178.027 182.870 1.00 30.46  ? 2505 ASP A O     1 
ATOM   9182  C CB    . ASP A 1 2505 ? 141.813 180.719 182.224 1.00 30.46  ? 2505 ASP A CB    1 
ATOM   9183  C CG    . ASP A 1 2505 ? 142.983 181.037 183.139 1.00 30.46  ? 2505 ASP A CG    1 
ATOM   9184  O OD1   . ASP A 1 2505 ? 143.307 180.210 184.016 1.00 30.46  ? 2505 ASP A OD1   1 
ATOM   9185  O OD2   . ASP A 1 2505 ? 143.582 182.121 182.983 1.00 30.46  ? 2505 ASP A OD2   1 
ATOM   9186  N N     . SER A 1 2506 ? 140.147 178.444 184.589 1.00 35.90  ? 2506 SER A N     1 
ATOM   9187  C CA    . SER A 1 2506 ? 140.281 177.125 185.184 1.00 35.90  ? 2506 SER A CA    1 
ATOM   9188  C C     . SER A 1 2506 ? 138.925 176.432 185.196 1.00 35.90  ? 2506 SER A C     1 
ATOM   9189  O O     . SER A 1 2506 ? 137.912 176.988 184.765 1.00 35.90  ? 2506 SER A O     1 
ATOM   9190  C CB    . SER A 1 2506 ? 140.849 177.211 186.605 1.00 35.90  ? 2506 SER A CB    1 
ATOM   9191  O OG    . SER A 1 2506 ? 139.900 177.769 187.495 1.00 35.90  ? 2506 SER A OG    1 
ATOM   9192  N N     . ARG A 1 2507 ? 138.917 175.202 185.702 1.00 40.78  ? 2507 ARG A N     1 
ATOM   9193  C CA    . ARG A 1 2507 ? 137.695 174.417 185.764 1.00 40.78  ? 2507 ARG A CA    1 
ATOM   9194  C C     . ARG A 1 2507 ? 136.754 174.985 186.826 1.00 40.78  ? 2507 ARG A C     1 
ATOM   9195  O O     . ARG A 1 2507 ? 137.078 175.932 187.548 1.00 40.78  ? 2507 ARG A O     1 
ATOM   9196  C CB    . ARG A 1 2507 ? 138.018 172.953 186.052 1.00 40.78  ? 2507 ARG A CB    1 
ATOM   9197  C CG    . ARG A 1 2507 ? 139.403 172.516 185.607 1.00 40.78  ? 2507 ARG A CG    1 
ATOM   9198  C CD    . ARG A 1 2507 ? 139.444 172.248 184.113 1.00 40.78  ? 2507 ARG A CD    1 
ATOM   9199  N NE    . ARG A 1 2507 ? 138.351 171.384 183.684 1.00 40.78  ? 2507 ARG A NE    1 
ATOM   9200  C CZ    . ARG A 1 2507 ? 138.338 170.065 183.823 1.00 40.78  ? 2507 ARG A CZ    1 
ATOM   9201  N NH1   . ARG A 1 2507 ? 139.353 169.418 184.371 1.00 40.78  ? 2507 ARG A NH1   1 
ATOM   9202  N NH2   . ARG A 1 2507 ? 137.280 169.379 183.401 1.00 40.78  ? 2507 ARG A NH2   1 
ATOM   9203  N N     . LEU A 1 2508 ? 135.563 174.390 186.915 1.00 43.41  ? 2508 LEU A N     1 
ATOM   9204  C CA    . LEU A 1 2508 ? 134.589 174.830 187.908 1.00 43.41  ? 2508 LEU A CA    1 
ATOM   9205  C C     . LEU A 1 2508 ? 135.091 174.563 189.322 1.00 43.41  ? 2508 LEU A C     1 
ATOM   9206  O O     . LEU A 1 2508 ? 134.897 175.386 190.225 1.00 43.41  ? 2508 LEU A O     1 
ATOM   9207  C CB    . LEU A 1 2508 ? 133.250 174.131 187.666 1.00 43.41  ? 2508 LEU A CB    1 
ATOM   9208  C CG    . LEU A 1 2508 ? 132.105 174.264 188.677 1.00 43.41  ? 2508 LEU A CG    1 
ATOM   9209  C CD1   . LEU A 1 2508 ? 131.943 175.696 189.178 1.00 43.41  ? 2508 LEU A CD1   1 
ATOM   9210  C CD2   . LEU A 1 2508 ? 130.804 173.754 188.076 1.00 43.41  ? 2508 LEU A CD2   1 
ATOM   9211  N N     . LYS A 1 2509 ? 135.741 173.415 189.534 1.00 41.31  ? 2509 LYS A N     1 
ATOM   9212  C CA    . LYS A 1 2509 ? 136.215 173.071 190.871 1.00 41.31  ? 2509 LYS A CA    1 
ATOM   9213  C C     . LYS A 1 2509 ? 137.256 174.067 191.367 1.00 41.31  ? 2509 LYS A C     1 
ATOM   9214  O O     . LYS A 1 2509 ? 137.241 174.458 192.539 1.00 41.31  ? 2509 LYS A O     1 
ATOM   9215  C CB    . LYS A 1 2509 ? 136.770 171.644 190.883 1.00 41.31  ? 2509 LYS A CB    1 
ATOM   9216  C CG    . LYS A 1 2509 ? 137.936 171.398 189.937 1.00 41.31  ? 2509 LYS A CG    1 
ATOM   9217  C CD    . LYS A 1 2509 ? 138.369 169.942 189.965 1.00 41.31  ? 2509 LYS A CD    1 
ATOM   9218  C CE    . LYS A 1 2509 ? 139.583 169.707 189.082 1.00 41.31  ? 2509 LYS A CE    1 
ATOM   9219  N NZ    . LYS A 1 2509 ? 139.269 169.900 187.641 1.00 41.31  ? 2509 LYS A NZ    1 
ATOM   9220  N N     . MET A 1 2510 ? 138.163 174.501 190.488 1.00 42.87  ? 2510 MET A N     1 
ATOM   9221  C CA    . MET A 1 2510 ? 139.178 175.465 190.900 1.00 42.87  ? 2510 MET A CA    1 
ATOM   9222  C C     . MET A 1 2510 ? 138.568 176.838 191.157 1.00 42.87  ? 2510 MET A C     1 
ATOM   9223  O O     . MET A 1 2510 ? 138.993 177.550 192.075 1.00 42.87  ? 2510 MET A O     1 
ATOM   9224  C CB    . MET A 1 2510 ? 140.281 175.543 189.847 1.00 42.87  ? 2510 MET A CB    1 
ATOM   9225  C CG    . MET A 1 2510 ? 140.797 174.182 189.423 1.00 42.87  ? 2510 MET A CG    1 
ATOM   9226  S SD    . MET A 1 2510 ? 141.341 173.212 190.842 1.00 42.87  ? 2510 MET A SD    1 
ATOM   9227  C CE    . MET A 1 2510 ? 142.776 172.385 190.166 1.00 42.87  ? 2510 MET A CE    1 
ATOM   9228  N N     . ARG A 1 2511 ? 137.569 177.227 190.362 1.00 37.68  ? 2511 ARG A N     1 
ATOM   9229  C CA    . ARG A 1 2511 ? 136.862 178.474 190.635 1.00 37.68  ? 2511 ARG A CA    1 
ATOM   9230  C C     . ARG A 1 2511 ? 136.183 178.427 191.997 1.00 37.68  ? 2511 ARG A C     1 
ATOM   9231  O O     . ARG A 1 2511 ? 136.239 179.397 192.762 1.00 37.68  ? 2511 ARG A O     1 
ATOM   9232  C CB    . ARG A 1 2511 ? 135.841 178.753 189.534 1.00 37.68  ? 2511 ARG A CB    1 
ATOM   9233  C CG    . ARG A 1 2511 ? 136.451 179.117 188.194 1.00 37.68  ? 2511 ARG A CG    1 
ATOM   9234  C CD    . ARG A 1 2511 ? 135.382 179.531 187.198 1.00 37.68  ? 2511 ARG A CD    1 
ATOM   9235  N NE    . ARG A 1 2511 ? 135.897 179.588 185.836 1.00 37.68  ? 2511 ARG A NE    1 
ATOM   9236  C CZ    . ARG A 1 2511 ? 135.137 179.646 184.751 1.00 37.68  ? 2511 ARG A CZ    1 
ATOM   9237  N NH1   . ARG A 1 2511 ? 133.817 179.645 184.832 1.00 37.68  ? 2511 ARG A NH1   1 
ATOM   9238  N NH2   . ARG A 1 2511 ? 135.716 179.703 183.556 1.00 37.68  ? 2511 ARG A NH2   1 
ATOM   9239  N N     . ALA A 1 2512 ? 135.547 177.299 192.322 1.00 43.60  ? 2512 ALA A N     1 
ATOM   9240  C CA    . ALA A 1 2512 ? 134.919 177.151 193.631 1.00 43.60  ? 2512 ALA A CA    1 
ATOM   9241  C C     . ALA A 1 2512 ? 135.956 177.172 194.748 1.00 43.60  ? 2512 ALA A C     1 
ATOM   9242  O O     . ALA A 1 2512 ? 135.714 177.739 195.820 1.00 43.60  ? 2512 ALA A O     1 
ATOM   9243  C CB    . ALA A 1 2512 ? 134.103 175.860 193.680 1.00 43.60  ? 2512 ALA A CB    1 
ATOM   9244  N N     . GLU A 1 2513 ? 137.113 176.546 194.520 1.00 43.72  ? 2513 GLU A N     1 
ATOM   9245  C CA    . GLU A 1 2513 ? 138.173 176.557 195.523 1.00 43.72  ? 2513 GLU A CA    1 
ATOM   9246  C C     . GLU A 1 2513 ? 138.669 177.972 195.789 1.00 43.72  ? 2513 GLU A C     1 
ATOM   9247  O O     . GLU A 1 2513 ? 138.847 178.371 196.947 1.00 43.72  ? 2513 GLU A O     1 
ATOM   9248  C CB    . GLU A 1 2513 ? 139.326 175.661 195.069 1.00 43.72  ? 2513 GLU A CB    1 
ATOM   9249  C CG    . GLU A 1 2513 ? 140.571 175.764 195.930 1.00 43.72  ? 2513 GLU A CG    1 
ATOM   9250  C CD    . GLU A 1 2513 ? 141.552 174.639 195.667 1.00 43.72  ? 2513 GLU A CD    1 
ATOM   9251  O OE1   . GLU A 1 2513 ? 142.525 174.504 196.438 1.00 43.72  ? 2513 GLU A OE1   1 
ATOM   9252  O OE2   . GLU A 1 2513 ? 141.351 173.889 194.689 1.00 43.72  ? 2513 GLU A OE2   1 
ATOM   9253  N N     . LEU A 1 2514 ? 138.896 178.749 194.727 1.00 39.49  ? 2514 LEU A N     1 
ATOM   9254  C CA    . LEU A 1 2514 ? 139.331 180.128 194.916 1.00 39.49  ? 2514 LEU A CA    1 
ATOM   9255  C C     . LEU A 1 2514 ? 138.247 180.954 195.596 1.00 39.49  ? 2514 LEU A C     1 
ATOM   9256  O O     . LEU A 1 2514 ? 138.549 181.810 196.434 1.00 39.49  ? 2514 LEU A O     1 
ATOM   9257  C CB    . LEU A 1 2514 ? 139.728 180.761 193.584 1.00 39.49  ? 2514 LEU A CB    1 
ATOM   9258  C CG    . LEU A 1 2514 ? 140.308 182.167 193.769 1.00 39.49  ? 2514 LEU A CG    1 
ATOM   9259  C CD1   . LEU A 1 2514 ? 141.597 182.107 194.572 1.00 39.49  ? 2514 LEU A CD1   1 
ATOM   9260  C CD2   . LEU A 1 2514 ? 140.538 182.868 192.449 1.00 39.49  ? 2514 LEU A CD2   1 
ATOM   9261  N N     . GLY A 1 2515 ? 136.981 180.718 195.245 1.00 42.54  ? 2515 GLY A N     1 
ATOM   9262  C CA    . GLY A 1 2515 ? 135.901 181.415 195.922 1.00 42.54  ? 2515 GLY A CA    1 
ATOM   9263  C C     . GLY A 1 2515 ? 135.858 181.114 197.407 1.00 42.54  ? 2515 GLY A C     1 
ATOM   9264  O O     . GLY A 1 2515 ? 135.666 182.014 198.228 1.00 42.54  ? 2515 GLY A O     1 
ATOM   9265  N N     . GLU A 1 2516 ? 136.044 179.843 197.772 1.00 48.16  ? 2516 GLU A N     1 
ATOM   9266  C CA    . GLU A 1 2516 ? 136.066 179.474 199.184 1.00 48.16  ? 2516 GLU A CA    1 
ATOM   9267  C C     . GLU A 1 2516 ? 137.247 180.113 199.904 1.00 48.16  ? 2516 GLU A C     1 
ATOM   9268  O O     . GLU A 1 2516 ? 137.102 180.616 201.026 1.00 48.16  ? 2516 GLU A O     1 
ATOM   9269  C CB    . GLU A 1 2516 ? 136.107 177.953 199.329 1.00 48.16  ? 2516 GLU A CB    1 
ATOM   9270  C CG    . GLU A 1 2516 ? 134.768 177.264 199.101 1.00 48.16  ? 2516 GLU A CG    1 
ATOM   9271  C CD    . GLU A 1 2516 ? 133.601 178.015 199.716 1.00 48.16  ? 2516 GLU A CD    1 
ATOM   9272  O OE1   . GLU A 1 2516 ? 132.587 178.215 199.015 1.00 48.16  ? 2516 GLU A OE1   1 
ATOM   9273  O OE2   . GLU A 1 2516 ? 133.685 178.389 200.906 1.00 48.16  ? 2516 GLU A OE2   1 
ATOM   9274  N N     . TYR A 1 2517 ? 138.424 180.110 199.274 1.00 43.25  ? 2517 TYR A N     1 
ATOM   9275  C CA    . TYR A 1 2517 ? 139.586 180.738 199.896 1.00 43.25  ? 2517 TYR A CA    1 
ATOM   9276  C C     . TYR A 1 2517 ? 139.360 182.231 200.098 1.00 43.25  ? 2517 TYR A C     1 
ATOM   9277  O O     . TYR A 1 2517 ? 139.687 182.781 201.157 1.00 43.25  ? 2517 TYR A O     1 
ATOM   9278  C CB    . TYR A 1 2517 ? 140.834 180.497 199.048 1.00 43.25  ? 2517 TYR A CB    1 
ATOM   9279  C CG    . TYR A 1 2517 ? 142.076 181.163 199.594 1.00 43.25  ? 2517 TYR A CG    1 
ATOM   9280  C CD1   . TYR A 1 2517 ? 142.778 180.603 200.652 1.00 43.25  ? 2517 TYR A CD1   1 
ATOM   9281  C CD2   . TYR A 1 2517 ? 142.546 182.352 199.055 1.00 43.25  ? 2517 TYR A CD2   1 
ATOM   9282  C CE1   . TYR A 1 2517 ? 143.913 181.206 201.157 1.00 43.25  ? 2517 TYR A CE1   1 
ATOM   9283  C CE2   . TYR A 1 2517 ? 143.679 182.963 199.555 1.00 43.25  ? 2517 TYR A CE2   1 
ATOM   9284  C CZ    . TYR A 1 2517 ? 144.359 182.386 200.604 1.00 43.25  ? 2517 TYR A CZ    1 
ATOM   9285  O OH    . TYR A 1 2517 ? 145.489 182.990 201.104 1.00 43.25  ? 2517 TYR A OH    1 
ATOM   9286  N N     . ILE A 1 2518 ? 138.792 182.900 199.094 1.00 44.07  ? 2518 ILE A N     1 
ATOM   9287  C CA    . ILE A 1 2518 ? 138.533 184.332 199.199 1.00 44.07  ? 2518 ILE A CA    1 
ATOM   9288  C C     . ILE A 1 2518 ? 137.514 184.610 200.294 1.00 44.07  ? 2518 ILE A C     1 
ATOM   9289  O O     . ILE A 1 2518 ? 137.676 185.545 201.087 1.00 44.07  ? 2518 ILE A O     1 
ATOM   9290  C CB    . ILE A 1 2518 ? 138.084 184.888 197.836 1.00 44.07  ? 2518 ILE A CB    1 
ATOM   9291  C CG1   . ILE A 1 2518 ? 139.295 185.019 196.914 1.00 44.07  ? 2518 ILE A CG1   1 
ATOM   9292  C CG2   . ILE A 1 2518 ? 137.389 186.229 198.000 1.00 44.07  ? 2518 ILE A CG2   1 
ATOM   9293  C CD1   . ILE A 1 2518 ? 138.943 185.182 195.470 1.00 44.07  ? 2518 ILE A CD1   1 
ATOM   9294  N N     . ARG A 1 2519 ? 136.460 183.793 200.370 1.00 48.56  ? 2519 ARG A N     1 
ATOM   9295  C CA    . ARG A 1 2519 ? 135.499 183.926 201.460 1.00 48.56  ? 2519 ARG A CA    1 
ATOM   9296  C C     . ARG A 1 2519 ? 136.181 183.767 202.812 1.00 48.56  ? 2519 ARG A C     1 
ATOM   9297  O O     . ARG A 1 2519 ? 135.858 184.479 203.770 1.00 48.56  ? 2519 ARG A O     1 
ATOM   9298  C CB    . ARG A 1 2519 ? 134.380 182.897 201.300 1.00 48.56  ? 2519 ARG A CB    1 
ATOM   9299  C CG    . ARG A 1 2519 ? 133.499 182.738 202.531 1.00 48.56  ? 2519 ARG A CG    1 
ATOM   9300  C CD    . ARG A 1 2519 ? 132.377 181.741 202.291 1.00 48.56  ? 2519 ARG A CD    1 
ATOM   9301  N NE    . ARG A 1 2519 ? 131.594 182.065 201.105 1.00 48.56  ? 2519 ARG A NE    1 
ATOM   9302  C CZ    . ARG A 1 2519 ? 130.384 182.608 201.132 1.00 48.56  ? 2519 ARG A CZ    1 
ATOM   9303  N NH1   . ARG A 1 2519 ? 129.787 182.908 202.274 1.00 48.56  ? 2519 ARG A NH1   1 
ATOM   9304  N NH2   . ARG A 1 2519 ? 129.759 182.857 199.986 1.00 48.56  ? 2519 ARG A NH2   1 
ATOM   9305  N N     . ARG A 1 2520 ? 137.133 182.837 202.906 1.00 46.70  ? 2520 ARG A N     1 
ATOM   9306  C CA    . ARG A 1 2520 ? 137.861 182.647 204.156 1.00 46.70  ? 2520 ARG A CA    1 
ATOM   9307  C C     . ARG A 1 2520 ? 138.694 183.874 204.511 1.00 46.70  ? 2520 ARG A C     1 
ATOM   9308  O O     . ARG A 1 2520 ? 138.752 184.274 205.679 1.00 46.70  ? 2520 ARG A O     1 
ATOM   9309  C CB    . ARG A 1 2520 ? 138.749 181.407 204.063 1.00 46.70  ? 2520 ARG A CB    1 
ATOM   9310  C CG    . ARG A 1 2520 ? 137.995 180.092 204.162 1.00 46.70  ? 2520 ARG A CG    1 
ATOM   9311  C CD    . ARG A 1 2520 ? 138.892 178.977 204.675 1.00 46.70  ? 2520 ARG A CD    1 
ATOM   9312  N NE    . ARG A 1 2520 ? 140.003 178.702 203.773 1.00 46.70  ? 2520 ARG A NE    1 
ATOM   9313  C CZ    . ARG A 1 2520 ? 141.271 178.981 204.040 1.00 46.70  ? 2520 ARG A CZ    1 
ATOM   9314  N NH1   . ARG A 1 2520 ? 141.627 179.561 205.174 1.00 46.70  ? 2520 ARG A NH1   1 
ATOM   9315  N NH2   . ARG A 1 2520 ? 142.206 178.671 203.146 1.00 46.70  ? 2520 ARG A NH2   1 
ATOM   9316  N N     . ILE A 1 2521 ? 139.344 184.486 203.522 1.00 42.74  ? 2521 ILE A N     1 
ATOM   9317  C CA    . ILE A 1 2521 ? 140.301 185.546 203.828 1.00 42.74  ? 2521 ILE A CA    1 
ATOM   9318  C C     . ILE A 1 2521 ? 139.677 186.943 203.846 1.00 42.74  ? 2521 ILE A C     1 
ATOM   9319  O O     . ILE A 1 2521 ? 140.165 187.822 204.564 1.00 42.74  ? 2521 ILE A O     1 
ATOM   9320  C CB    . ILE A 1 2521 ? 141.491 185.498 202.853 1.00 42.74  ? 2521 ILE A CB    1 
ATOM   9321  C CG1   . ILE A 1 2521 ? 141.087 186.022 201.473 1.00 42.74  ? 2521 ILE A CG1   1 
ATOM   9322  C CG2   . ILE A 1 2521 ? 142.062 184.091 202.769 1.00 42.74  ? 2521 ILE A CG2   1 
ATOM   9323  C CD1   . ILE A 1 2521 ? 142.208 186.004 200.464 1.00 42.74  ? 2521 ILE A CD1   1 
ATOM   9324  N N     . THR A 1 2522 ? 138.615 187.180 203.082 1.00 47.23  ? 2522 THR A N     1 
ATOM   9325  C CA    . THR A 1 2522 ? 138.098 188.533 202.943 1.00 47.23  ? 2522 THR A CA    1 
ATOM   9326  C C     . THR A 1 2522 ? 137.128 188.875 204.072 1.00 47.23  ? 2522 THR A C     1 
ATOM   9327  O O     . THR A 1 2522 ? 136.699 188.018 204.847 1.00 47.23  ? 2522 THR A O     1 
ATOM   9328  C CB    . THR A 1 2522 ? 137.408 188.715 201.591 1.00 47.23  ? 2522 THR A CB    1 
ATOM   9329  O OG1   . THR A 1 2522 ? 137.308 190.113 201.294 1.00 47.23  ? 2522 THR A OG1   1 
ATOM   9330  C CG2   . THR A 1 2522 ? 136.009 188.122 201.625 1.00 47.23  ? 2522 THR A CG2   1 
ATOM   9331  N N     . THR A 1 2523 ? 136.790 190.163 204.158 1.00 52.57  ? 2523 THR A N     1 
ATOM   9332  C CA    . THR A 1 2523 ? 135.805 190.659 205.107 1.00 52.57  ? 2523 THR A CA    1 
ATOM   9333  C C     . THR A 1 2523 ? 134.588 191.280 204.437 1.00 52.57  ? 2523 THR A C     1 
ATOM   9334  O O     . THR A 1 2523 ? 133.624 191.618 205.132 1.00 52.57  ? 2523 THR A O     1 
ATOM   9335  C CB    . THR A 1 2523 ? 136.441 191.696 206.045 1.00 52.57  ? 2523 THR A CB    1 
ATOM   9336  O OG1   . THR A 1 2523 ? 136.911 192.810 205.278 1.00 52.57  ? 2523 THR A OG1   1 
ATOM   9337  C CG2   . THR A 1 2523 ? 137.607 191.083 206.803 1.00 52.57  ? 2523 THR A CG2   1 
ATOM   9338  N N     . VAL A 1 2524 ? 134.611 191.442 203.118 1.00 45.83  ? 2524 VAL A N     1 
ATOM   9339  C CA    . VAL A 1 2524 ? 133.509 192.026 202.357 1.00 45.83  ? 2524 VAL A CA    1 
ATOM   9340  C C     . VAL A 1 2524 ? 132.311 191.084 202.414 1.00 45.83  ? 2524 VAL A C     1 
ATOM   9341  O O     . VAL A 1 2524 ? 132.493 189.858 202.451 1.00 45.83  ? 2524 VAL A O     1 
ATOM   9342  C CB    . VAL A 1 2524 ? 133.944 192.305 200.909 1.00 45.83  ? 2524 VAL A CB    1 
ATOM   9343  C CG1   . VAL A 1 2524 ? 134.324 191.013 200.223 1.00 45.83  ? 2524 VAL A CG1   1 
ATOM   9344  C CG2   . VAL A 1 2524 ? 132.856 193.024 200.126 1.00 45.83  ? 2524 VAL A CG2   1 
ATOM   9345  N N     . PRO A 1 2525 ? 131.081 191.598 202.459 1.00 48.93  ? 2525 PRO A N     1 
ATOM   9346  C CA    . PRO A 1 2525 ? 129.915 190.713 202.373 1.00 48.93  ? 2525 PRO A CA    1 
ATOM   9347  C C     . PRO A 1 2525 ? 129.905 189.925 201.073 1.00 48.93  ? 2525 PRO A C     1 
ATOM   9348  O O     . PRO A 1 2525 ? 130.318 190.413 200.018 1.00 48.93  ? 2525 PRO A O     1 
ATOM   9349  C CB    . PRO A 1 2525 ? 128.729 191.680 202.451 1.00 48.93  ? 2525 PRO A CB    1 
ATOM   9350  C CG    . PRO A 1 2525 ? 129.254 192.846 203.206 1.00 48.93  ? 2525 PRO A CG    1 
ATOM   9351  C CD    . PRO A 1 2525 ? 130.704 192.974 202.830 1.00 48.93  ? 2525 PRO A CD    1 
ATOM   9352  N N     . LEU A 1 2526 ? 129.426 188.694 201.162 1.00 53.68  ? 2526 LEU A N     1 
ATOM   9353  C CA    . LEU A 1 2526 ? 129.390 187.744 200.063 1.00 53.68  ? 2526 LEU A CA    1 
ATOM   9354  C C     . LEU A 1 2526 ? 128.009 187.118 199.987 1.00 53.68  ? 2526 LEU A C     1 
ATOM   9355  O O     . LEU A 1 2526 ? 127.237 187.186 200.950 1.00 53.68  ? 2526 LEU A O     1 
ATOM   9356  C CB    . LEU A 1 2526 ? 130.455 186.653 200.249 1.00 53.68  ? 2526 LEU A CB    1 
ATOM   9357  C CG    . LEU A 1 2526 ? 131.877 187.040 199.843 1.00 53.68  ? 2526 LEU A CG    1 
ATOM   9358  C CD1   . LEU A 1 2526 ? 132.888 186.316 200.706 1.00 53.68  ? 2526 LEU A CD1   1 
ATOM   9359  C CD2   . LEU A 1 2526 ? 132.111 186.737 198.372 1.00 53.68  ? 2526 LEU A CD2   1 
ATOM   9360  N N     . PRO A 1 2527 ? 127.647 186.526 198.832 1.00 53.95  ? 2527 PRO A N     1 
ATOM   9361  C CA    . PRO A 1 2527 ? 126.356 185.830 198.727 1.00 53.95  ? 2527 PRO A CA    1 
ATOM   9362  C C     . PRO A 1 2527 ? 126.113 184.858 199.870 1.00 53.95  ? 2527 PRO A C     1 
ATOM   9363  O O     . PRO A 1 2527 ? 126.892 183.925 200.088 1.00 53.95  ? 2527 PRO A O     1 
ATOM   9364  C CB    . PRO A 1 2527 ? 126.466 185.101 197.384 1.00 53.95  ? 2527 PRO A CB    1 
ATOM   9365  C CG    . PRO A 1 2527 ? 127.355 185.971 196.573 1.00 53.95  ? 2527 PRO A CG    1 
ATOM   9366  C CD    . PRO A 1 2527 ? 128.336 186.603 197.530 1.00 53.95  ? 2527 PRO A CD    1 
ATOM   9367  N N     . THR A 1 2528 ? 125.023 185.079 200.608 1.00 59.30  ? 2528 THR A N     1 
ATOM   9368  C CA    . THR A 1 2528 ? 124.754 184.306 201.814 1.00 59.30  ? 2528 THR A CA    1 
ATOM   9369  C C     . THR A 1 2528 ? 124.355 182.866 201.517 1.00 59.30  ? 2528 THR A C     1 
ATOM   9370  O O     . THR A 1 2528 ? 124.424 182.023 202.418 1.00 59.30  ? 2528 THR A O     1 
ATOM   9371  C CB    . THR A 1 2528 ? 123.659 184.984 202.637 1.00 59.30  ? 2528 THR A CB    1 
ATOM   9372  O OG1   . THR A 1 2528 ? 122.449 185.039 201.870 1.00 59.30  ? 2528 THR A OG1   1 
ATOM   9373  C CG2   . THR A 1 2528 ? 124.076 186.397 203.011 1.00 59.30  ? 2528 THR A CG2   1 
ATOM   9374  N N     . ALA A 1 2529 ? 123.942 182.567 200.295 1.00 65.23  ? 2529 ALA A N     1 
ATOM   9375  C CA    . ALA A 1 2529 ? 123.528 181.210 199.957 1.00 65.23  ? 2529 ALA A CA    1 
ATOM   9376  C C     . ALA A 1 2529 ? 124.728 180.274 200.007 1.00 65.23  ? 2529 ALA A C     1 
ATOM   9377  O O     . ALA A 1 2529 ? 125.717 180.511 199.301 1.00 65.23  ? 2529 ALA A O     1 
ATOM   9378  C CB    . ALA A 1 2529 ? 122.886 181.179 198.574 1.00 65.23  ? 2529 ALA A CB    1 
ATOM   9379  N N     . PRO A 1 2530 ? 124.693 179.213 200.811 1.00 64.67  ? 2530 PRO A N     1 
ATOM   9380  C CA    . PRO A 1 2530 ? 125.840 178.304 200.918 1.00 64.67  ? 2530 PRO A CA    1 
ATOM   9381  C C     . PRO A 1 2530 ? 125.875 177.191 199.883 1.00 64.67  ? 2530 PRO A C     1 
ATOM   9382  O O     . PRO A 1 2530 ? 126.815 176.388 199.902 1.00 64.67  ? 2530 PRO A O     1 
ATOM   9383  C CB    . PRO A 1 2530 ? 125.660 177.722 202.326 1.00 64.67  ? 2530 PRO A CB    1 
ATOM   9384  C CG    . PRO A 1 2530 ? 124.177 177.686 202.517 1.00 64.67  ? 2530 PRO A CG    1 
ATOM   9385  C CD    . PRO A 1 2530 ? 123.591 178.823 201.708 1.00 64.67  ? 2530 PRO A CD    1 
ATOM   9386  N N     . ASN A 1 2531 ? 124.889 177.117 198.992 1.00 66.48  ? 2531 ASN A N     1 
ATOM   9387  C CA    . ASN A 1 2531 ? 124.834 176.078 197.971 1.00 66.48  ? 2531 ASN A CA    1 
ATOM   9388  C C     . ASN A 1 2531 ? 125.376 176.535 196.623 1.00 66.48  ? 2531 ASN A C     1 
ATOM   9389  O O     . ASN A 1 2531 ? 126.103 175.783 195.967 1.00 66.48  ? 2531 ASN A O     1 
ATOM   9390  C CB    . ASN A 1 2531 ? 123.393 175.584 197.800 1.00 66.48  ? 2531 ASN A CB    1 
ATOM   9391  C CG    . ASN A 1 2531 ? 122.414 176.714 197.536 1.00 66.48  ? 2531 ASN A CG    1 
ATOM   9392  O OD1   . ASN A 1 2531 ? 122.802 177.878 197.434 1.00 66.48  ? 2531 ASN A OD1   1 
ATOM   9393  N ND2   . ASN A 1 2531 ? 121.135 176.374 197.425 1.00 66.48  ? 2531 ASN A ND2   1 
ATOM   9394  N N     . ILE A 1 2532 ? 125.039 177.748 196.196 1.00 63.08  ? 2532 ILE A N     1 
ATOM   9395  C CA    . ILE A 1 2532 ? 125.459 178.261 194.895 1.00 63.08  ? 2532 ILE A CA    1 
ATOM   9396  C C     . ILE A 1 2532 ? 126.833 178.908 195.021 1.00 63.08  ? 2532 ILE A C     1 
ATOM   9397  O O     . ILE A 1 2532 ? 127.030 179.784 195.876 1.00 63.08  ? 2532 ILE A O     1 
ATOM   9398  C CB    . ILE A 1 2532 ? 124.431 179.252 194.331 1.00 63.08  ? 2532 ILE A CB    1 
ATOM   9399  C CG1   . ILE A 1 2532 ? 123.074 178.567 194.162 1.00 63.08  ? 2532 ILE A CG1   1 
ATOM   9400  C CG2   . ILE A 1 2532 ? 124.911 179.819 193.006 1.00 63.08  ? 2532 ILE A CG2   1 
ATOM   9401  C CD1   . ILE A 1 2532 ? 123.098 177.392 193.210 1.00 63.08  ? 2532 ILE A CD1   1 
ATOM   9402  N N     . PRO A 1 2533 ? 127.807 178.506 194.206 1.00 58.43  ? 2533 PRO A N     1 
ATOM   9403  C CA    . PRO A 1 2533 ? 129.121 179.156 194.243 1.00 58.43  ? 2533 PRO A CA    1 
ATOM   9404  C C     . PRO A 1 2533 ? 129.033 180.626 193.859 1.00 58.43  ? 2533 PRO A C     1 
ATOM   9405  O O     . PRO A 1 2533 ? 128.154 181.053 193.108 1.00 58.43  ? 2533 PRO A O     1 
ATOM   9406  C CB    . PRO A 1 2533 ? 129.943 178.362 193.220 1.00 58.43  ? 2533 PRO A CB    1 
ATOM   9407  C CG    . PRO A 1 2533 ? 129.242 177.051 193.098 1.00 58.43  ? 2533 PRO A CG    1 
ATOM   9408  C CD    . PRO A 1 2533 ? 127.788 177.337 193.311 1.00 58.43  ? 2533 PRO A CD    1 
ATOM   9409  N N     . ILE A 1 2534 ? 129.973 181.405 194.400 1.00 50.60  ? 2534 ILE A N     1 
ATOM   9410  C CA    . ILE A 1 2534 ? 129.982 182.850 194.184 1.00 50.60  ? 2534 ILE A CA    1 
ATOM   9411  C C     . ILE A 1 2534 ? 130.185 183.181 192.711 1.00 50.60  ? 2534 ILE A C     1 
ATOM   9412  O O     . ILE A 1 2534 ? 129.760 184.244 192.241 1.00 50.60  ? 2534 ILE A O     1 
ATOM   9413  C CB    . ILE A 1 2534 ? 131.059 183.514 195.067 1.00 50.60  ? 2534 ILE A CB    1 
ATOM   9414  C CG1   . ILE A 1 2534 ? 130.916 183.068 196.525 1.00 50.60  ? 2534 ILE A CG1   1 
ATOM   9415  C CG2   . ILE A 1 2534 ? 130.967 185.028 194.987 1.00 50.60  ? 2534 ILE A CG2   1 
ATOM   9416  C CD1   . ILE A 1 2534 ? 131.844 181.936 196.925 1.00 50.60  ? 2534 ILE A CD1   1 
ATOM   9417  N N     . ILE A 1 2535 ? 130.823 182.282 191.957 1.00 46.61  ? 2535 ILE A N     1 
ATOM   9418  C CA    . ILE A 1 2535 ? 131.087 182.546 190.545 1.00 46.61  ? 2535 ILE A CA    1 
ATOM   9419  C C     . ILE A 1 2535 ? 129.788 182.695 189.761 1.00 46.61  ? 2535 ILE A C     1 
ATOM   9420  O O     . ILE A 1 2535 ? 129.754 183.375 188.729 1.00 46.61  ? 2535 ILE A O     1 
ATOM   9421  C CB    . ILE A 1 2535 ? 131.984 181.440 189.957 1.00 46.61  ? 2535 ILE A CB    1 
ATOM   9422  C CG1   . ILE A 1 2535 ? 132.524 181.856 188.588 1.00 46.61  ? 2535 ILE A CG1   1 
ATOM   9423  C CG2   . ILE A 1 2535 ? 131.229 180.124 189.858 1.00 46.61  ? 2535 ILE A CG2   1 
ATOM   9424  C CD1   . ILE A 1 2535 ? 133.466 183.033 188.642 1.00 46.61  ? 2535 ILE A CD1   1 
ATOM   9425  N N     . ASP A 1 2536 ? 128.702 182.079 190.231 1.00 51.30  ? 2536 ASP A N     1 
ATOM   9426  C CA    . ASP A 1 2536 ? 127.417 182.180 189.551 1.00 51.30  ? 2536 ASP A CA    1 
ATOM   9427  C C     . ASP A 1 2536 ? 126.647 183.442 189.914 1.00 51.30  ? 2536 ASP A C     1 
ATOM   9428  O O     . ASP A 1 2536 ? 125.567 183.668 189.360 1.00 51.30  ? 2536 ASP A O     1 
ATOM   9429  C CB    . ASP A 1 2536 ? 126.559 180.951 189.858 1.00 51.30  ? 2536 ASP A CB    1 
ATOM   9430  C CG    . ASP A 1 2536 ? 127.326 179.654 189.699 1.00 51.30  ? 2536 ASP A CG    1 
ATOM   9431  O OD1   . ASP A 1 2536 ? 127.447 179.170 188.554 1.00 51.30  ? 2536 ASP A OD1   1 
ATOM   9432  O OD2   . ASP A 1 2536 ? 127.812 179.122 190.717 1.00 51.30  ? 2536 ASP A OD2   1 
ATOM   9433  N N     . TYR A 1 2537 ? 127.161 184.256 190.828 1.00 51.22  ? 2537 TYR A N     1 
ATOM   9434  C CA    . TYR A 1 2537 ? 126.526 185.516 191.174 1.00 51.22  ? 2537 TYR A CA    1 
ATOM   9435  C C     . TYR A 1 2537 ? 127.151 186.665 190.385 1.00 51.22  ? 2537 TYR A C     1 
ATOM   9436  O O     . TYR A 1 2537 ? 128.199 186.526 189.752 1.00 51.22  ? 2537 TYR A O     1 
ATOM   9437  C CB    . TYR A 1 2537 ? 126.644 185.783 192.674 1.00 51.22  ? 2537 TYR A CB    1 
ATOM   9438  C CG    . TYR A 1 2537 ? 125.592 185.095 193.513 1.00 51.22  ? 2537 TYR A CG    1 
ATOM   9439  C CD1   . TYR A 1 2537 ? 125.677 183.740 193.795 1.00 51.22  ? 2537 TYR A CD1   1 
ATOM   9440  C CD2   . TYR A 1 2537 ? 124.515 185.804 194.025 1.00 51.22  ? 2537 TYR A CD2   1 
ATOM   9441  C CE1   . TYR A 1 2537 ? 124.718 183.109 194.563 1.00 51.22  ? 2537 TYR A CE1   1 
ATOM   9442  C CE2   . TYR A 1 2537 ? 123.551 185.183 194.793 1.00 51.22  ? 2537 TYR A CE2   1 
ATOM   9443  C CZ    . TYR A 1 2537 ? 123.658 183.836 195.059 1.00 51.22  ? 2537 TYR A CZ    1 
ATOM   9444  O OH    . TYR A 1 2537 ? 122.700 183.213 195.823 1.00 51.22  ? 2537 TYR A OH    1 
ATOM   9445  N N     . GLU A 1 2538 ? 126.485 187.815 190.429 1.00 45.96  ? 2538 GLU A N     1 
ATOM   9446  C CA    . GLU A 1 2538 ? 127.045 189.044 189.891 1.00 45.96  ? 2538 GLU A CA    1 
ATOM   9447  C C     . GLU A 1 2538 ? 126.729 190.174 190.854 1.00 45.96  ? 2538 GLU A C     1 
ATOM   9448  O O     . GLU A 1 2538 ? 126.037 189.987 191.857 1.00 45.96  ? 2538 GLU A O     1 
ATOM   9449  C CB    . GLU A 1 2538 ? 126.502 189.387 188.501 1.00 45.96  ? 2538 GLU A CB    1 
ATOM   9450  C CG    . GLU A 1 2538 ? 125.046 189.801 188.495 1.00 45.96  ? 2538 GLU A CG    1 
ATOM   9451  C CD    . GLU A 1 2538 ? 124.623 190.397 187.171 1.00 45.96  ? 2538 GLU A CD    1 
ATOM   9452  O OE1   . GLU A 1 2538 ? 125.498 190.597 186.305 1.00 45.96  ? 2538 GLU A OE1   1 
ATOM   9453  O OE2   . GLU A 1 2538 ? 123.419 190.668 186.995 1.00 45.96  ? 2538 GLU A OE2   1 
ATOM   9454  N N     . VAL A 1 2539 ? 127.246 191.354 190.538 1.00 37.86  ? 2539 VAL A N     1 
ATOM   9455  C CA    . VAL A 1 2539 ? 127.032 192.543 191.349 1.00 37.86  ? 2539 VAL A CA    1 
ATOM   9456  C C     . VAL A 1 2539 ? 126.136 193.492 190.563 1.00 37.86  ? 2539 VAL A C     1 
ATOM   9457  O O     . VAL A 1 2539 ? 126.419 193.827 189.407 1.00 37.86  ? 2539 VAL A O     1 
ATOM   9458  C CB    . VAL A 1 2539 ? 128.361 193.194 191.748 1.00 37.86  ? 2539 VAL A CB    1 
ATOM   9459  C CG1   . VAL A 1 2539 ? 129.157 192.224 192.586 1.00 37.86  ? 2539 VAL A CG1   1 
ATOM   9460  C CG2   . VAL A 1 2539 ? 129.169 193.576 190.524 1.00 37.86  ? 2539 VAL A CG2   1 
ATOM   9461  N N     . SER A 1 2540 ? 125.028 193.897 191.173 1.00 35.88  ? 2540 SER A N     1 
ATOM   9462  C CA    . SER A 1 2540 ? 124.139 194.852 190.539 1.00 35.88  ? 2540 SER A CA    1 
ATOM   9463  C C     . SER A 1 2540 ? 124.626 196.273 190.794 1.00 35.88  ? 2540 SER A C     1 
ATOM   9464  O O     . SER A 1 2540 ? 125.435 196.530 191.689 1.00 35.88  ? 2540 SER A O     1 
ATOM   9465  C CB    . SER A 1 2540 ? 122.709 194.684 191.051 1.00 35.88  ? 2540 SER A CB    1 
ATOM   9466  O OG    . SER A 1 2540 ? 121.879 195.739 190.597 1.00 35.88  ? 2540 SER A OG    1 
ATOM   9467  N N     . ILE A 1 2541 ? 124.115 197.208 189.990 1.00 34.75  ? 2541 ILE A N     1 
ATOM   9468  C CA    . ILE A 1 2541 ? 124.508 198.602 190.141 1.00 34.75  ? 2541 ILE A CA    1 
ATOM   9469  C C     . ILE A 1 2541 ? 124.048 199.169 191.477 1.00 34.75  ? 2541 ILE A C     1 
ATOM   9470  O O     . ILE A 1 2541 ? 124.579 200.189 191.931 1.00 34.75  ? 2541 ILE A O     1 
ATOM   9471  C CB    . ILE A 1 2541 ? 123.969 199.442 188.969 1.00 34.75  ? 2541 ILE A CB    1 
ATOM   9472  C CG1   . ILE A 1 2541 ? 124.781 200.727 188.817 1.00 34.75  ? 2541 ILE A CG1   1 
ATOM   9473  C CG2   . ILE A 1 2541 ? 122.496 199.759 189.167 1.00 34.75  ? 2541 ILE A CG2   1 
ATOM   9474  C CD1   . ILE A 1 2541 ? 126.269 200.495 188.707 1.00 34.75  ? 2541 ILE A CD1   1 
ATOM   9475  N N     . SER A 1 2542 ? 123.072 198.532 192.126 1.00 36.35  ? 2542 SER A N     1 
ATOM   9476  C CA    . SER A 1 2542 ? 122.643 198.960 193.450 1.00 36.35  ? 2542 SER A CA    1 
ATOM   9477  C C     . SER A 1 2542 ? 123.632 198.570 194.539 1.00 36.35  ? 2542 SER A C     1 
ATOM   9478  O O     . SER A 1 2542 ? 123.602 199.159 195.624 1.00 36.35  ? 2542 SER A O     1 
ATOM   9479  C CB    . SER A 1 2542 ? 121.267 198.375 193.772 1.00 36.35  ? 2542 SER A CB    1 
ATOM   9480  O OG    . SER A 1 2542 ? 120.854 198.737 195.078 1.00 36.35  ? 2542 SER A OG    1 
ATOM   9481  N N     . GLY A 1 2543 ? 124.501 197.598 194.278 1.00 37.40  ? 2543 GLY A N     1 
ATOM   9482  C CA    . GLY A 1 2543 ? 125.486 197.182 195.256 1.00 37.40  ? 2543 GLY A CA    1 
ATOM   9483  C C     . GLY A 1 2543 ? 125.081 195.947 196.032 1.00 37.40  ? 2543 GLY A C     1 
ATOM   9484  O O     . GLY A 1 2543 ? 125.391 195.825 197.221 1.00 37.40  ? 2543 GLY A O     1 
ATOM   9485  N N     . GLU A 1 2544 ? 124.385 195.023 195.375 1.00 43.01  ? 2544 GLU A N     1 
ATOM   9486  C CA    . GLU A 1 2544 ? 123.953 193.787 196.007 1.00 43.01  ? 2544 GLU A CA    1 
ATOM   9487  C C     . GLU A 1 2544 ? 124.239 192.617 195.080 1.00 43.01  ? 2544 GLU A C     1 
ATOM   9488  O O     . GLU A 1 2544 ? 124.171 192.745 193.854 1.00 43.01  ? 2544 GLU A O     1 
ATOM   9489  C CB    . GLU A 1 2544 ? 122.460 193.823 196.360 1.00 43.01  ? 2544 GLU A CB    1 
ATOM   9490  C CG    . GLU A 1 2544 ? 122.111 194.768 197.497 1.00 43.01  ? 2544 GLU A CG    1 
ATOM   9491  C CD    . GLU A 1 2544 ? 120.621 195.024 197.606 1.00 43.01  ? 2544 GLU A CD    1 
ATOM   9492  O OE1   . GLU A 1 2544 ? 120.237 196.121 198.064 1.00 43.01  ? 2544 GLU A OE1   1 
ATOM   9493  O OE2   . GLU A 1 2544 ? 119.834 194.129 197.233 1.00 43.01  ? 2544 GLU A OE2   1 
ATOM   9494  N N     . TRP A 1 2545 ? 124.558 191.473 195.678 1.00 45.30  ? 2545 TRP A N     1 
ATOM   9495  C CA    . TRP A 1 2545 ? 124.821 190.260 194.916 1.00 45.30  ? 2545 TRP A CA    1 
ATOM   9496  C C     . TRP A 1 2545 ? 123.512 189.719 194.355 1.00 45.30  ? 2545 TRP A C     1 
ATOM   9497  O O     . TRP A 1 2545 ? 122.583 189.419 195.112 1.00 45.30  ? 2545 TRP A O     1 
ATOM   9498  C CB    . TRP A 1 2545 ? 125.500 189.211 195.793 1.00 45.30  ? 2545 TRP A CB    1 
ATOM   9499  C CG    . TRP A 1 2545 ? 126.910 189.543 196.166 1.00 45.30  ? 2545 TRP A CG    1 
ATOM   9500  C CD1   . TRP A 1 2545 ? 127.343 190.065 197.349 1.00 45.30  ? 2545 TRP A CD1   1 
ATOM   9501  C CD2   . TRP A 1 2545 ? 128.077 189.359 195.356 1.00 45.30  ? 2545 TRP A CD2   1 
ATOM   9502  N NE1   . TRP A 1 2545 ? 128.707 190.226 197.323 1.00 45.30  ? 2545 TRP A NE1   1 
ATOM   9503  C CE2   . TRP A 1 2545 ? 129.182 189.799 196.111 1.00 45.30  ? 2545 TRP A CE2   1 
ATOM   9504  C CE3   . TRP A 1 2545 ? 128.295 188.869 194.066 1.00 45.30  ? 2545 TRP A CE3   1 
ATOM   9505  C CZ2   . TRP A 1 2545 ? 130.483 189.763 195.618 1.00 45.30  ? 2545 TRP A CZ2   1 
ATOM   9506  C CZ3   . TRP A 1 2545 ? 129.588 188.834 193.579 1.00 45.30  ? 2545 TRP A CZ3   1 
ATOM   9507  C CH2   . TRP A 1 2545 ? 130.665 189.279 194.353 1.00 45.30  ? 2545 TRP A CH2   1 
ATOM   9508  N N     . SER A 1 2546 ? 123.438 189.594 193.032 1.00 47.56  ? 2546 SER A N     1 
ATOM   9509  C CA    . SER A 1 2546 ? 122.267 189.034 192.389 1.00 47.56  ? 2546 SER A CA    1 
ATOM   9510  C C     . SER A 1 2546 ? 122.657 187.818 191.559 1.00 47.56  ? 2546 SER A C     1 
ATOM   9511  O O     . SER A 1 2546 ? 123.691 187.836 190.884 1.00 47.56  ? 2546 SER A O     1 
ATOM   9512  C CB    . SER A 1 2546 ? 121.579 190.068 191.489 1.00 47.56  ? 2546 SER A CB    1 
ATOM   9513  O OG    . SER A 1 2546 ? 122.385 190.380 190.367 1.00 47.56  ? 2546 SER A OG    1 
ATOM   9514  N N     . PRO A 1 2547 ? 121.860 186.751 191.592 1.00 48.90  ? 2547 PRO A N     1 
ATOM   9515  C CA    . PRO A 1 2547 ? 122.201 185.556 190.814 1.00 48.90  ? 2547 PRO A CA    1 
ATOM   9516  C C     . PRO A 1 2547 ? 122.165 185.836 189.320 1.00 48.90  ? 2547 PRO A C     1 
ATOM   9517  O O     . PRO A 1 2547 ? 121.397 186.669 188.837 1.00 48.90  ? 2547 PRO A O     1 
ATOM   9518  C CB    . PRO A 1 2547 ? 121.123 184.545 191.219 1.00 48.90  ? 2547 PRO A CB    1 
ATOM   9519  C CG    . PRO A 1 2547 ? 119.991 185.379 191.723 1.00 48.90  ? 2547 PRO A CG    1 
ATOM   9520  C CD    . PRO A 1 2547 ? 120.617 186.578 192.362 1.00 48.90  ? 2547 PRO A CD    1 
ATOM   9521  N N     . TRP A 1 2548 ? 123.019 185.121 188.585 1.00 45.39  ? 2548 TRP A N     1 
ATOM   9522  C CA    . TRP A 1 2548 ? 123.049 185.277 187.136 1.00 45.39  ? 2548 TRP A CA    1 
ATOM   9523  C C     . TRP A 1 2548 ? 121.814 184.669 186.483 1.00 45.39  ? 2548 TRP A C     1 
ATOM   9524  O O     . TRP A 1 2548 ? 121.507 184.988 185.329 1.00 45.39  ? 2548 TRP A O     1 
ATOM   9525  C CB    . TRP A 1 2548 ? 124.317 184.642 186.568 1.00 45.39  ? 2548 TRP A CB    1 
ATOM   9526  C CG    . TRP A 1 2548 ? 125.469 185.592 186.450 1.00 45.39  ? 2548 TRP A CG    1 
ATOM   9527  C CD1   . TRP A 1 2548 ? 126.601 185.607 187.212 1.00 45.39  ? 2548 TRP A CD1   1 
ATOM   9528  C CD2   . TRP A 1 2548 ? 125.607 186.660 185.506 1.00 45.39  ? 2548 TRP A CD2   1 
ATOM   9529  N NE1   . TRP A 1 2548 ? 127.432 186.621 186.805 1.00 45.39  ? 2548 TRP A NE1   1 
ATOM   9530  C CE2   . TRP A 1 2548 ? 126.845 187.282 185.759 1.00 45.39  ? 2548 TRP A CE2   1 
ATOM   9531  C CE3   . TRP A 1 2548 ? 124.804 187.151 184.475 1.00 45.39  ? 2548 TRP A CE3   1 
ATOM   9532  C CZ2   . TRP A 1 2548 ? 127.299 188.369 185.016 1.00 45.39  ? 2548 TRP A CZ2   1 
ATOM   9533  C CZ3   . TRP A 1 2548 ? 125.256 188.231 183.739 1.00 45.39  ? 2548 TRP A CZ3   1 
ATOM   9534  C CH2   . TRP A 1 2548 ? 126.491 188.827 184.012 1.00 45.39  ? 2548 TRP A CH2   1 
ATOM   9535  N N     . GLN A 1 2549 ? 121.101 183.796 187.199 1.00 47.57  ? 2549 GLN A N     1 
ATOM   9536  C CA    . GLN A 1 2549 ? 119.904 183.172 186.644 1.00 47.57  ? 2549 GLN A CA    1 
ATOM   9537  C C     . GLN A 1 2549 ? 118.820 184.196 186.334 1.00 47.57  ? 2549 GLN A C     1 
ATOM   9538  O O     . GLN A 1 2549 ? 118.139 184.084 185.308 1.00 47.57  ? 2549 GLN A O     1 
ATOM   9539  C CB    . GLN A 1 2549 ? 119.366 182.116 187.609 1.00 47.57  ? 2549 GLN A CB    1 
ATOM   9540  C CG    . GLN A 1 2549 ? 120.394 181.088 188.039 1.00 47.57  ? 2549 GLN A CG    1 
ATOM   9541  C CD    . GLN A 1 2549 ? 120.342 179.830 187.195 1.00 47.57  ? 2549 GLN A CD    1 
ATOM   9542  O OE1   . GLN A 1 2549 ? 119.898 179.858 186.047 1.00 47.57  ? 2549 GLN A OE1   1 
ATOM   9543  N NE2   . GLN A 1 2549 ? 120.795 178.719 187.761 1.00 47.57  ? 2549 GLN A NE2   1 
ATOM   9544  N N     . ALA A 1 2550 ? 118.642 185.193 187.204 1.00 43.75  ? 2550 ALA A N     1 
ATOM   9545  C CA    . ALA A 1 2550 ? 117.565 186.161 187.034 1.00 43.75  ? 2550 ALA A CA    1 
ATOM   9546  C C     . ALA A 1 2550 ? 117.682 186.956 185.741 1.00 43.75  ? 2550 ALA A C     1 
ATOM   9547  O O     . ALA A 1 2550 ? 116.673 187.481 185.259 1.00 43.75  ? 2550 ALA A O     1 
ATOM   9548  C CB    . ALA A 1 2550 ? 117.527 187.118 188.226 1.00 43.75  ? 2550 ALA A CB    1 
ATOM   9549  N N     . LYS A 1 2551 ? 118.879 187.061 185.170 1.00 44.57  ? 2551 LYS A N     1 
ATOM   9550  C CA    . LYS A 1 2551 ? 119.080 187.791 183.927 1.00 44.57  ? 2551 LYS A CA    1 
ATOM   9551  C C     . LYS A 1 2551 ? 119.054 186.896 182.696 1.00 44.57  ? 2551 LYS A C     1 
ATOM   9552  O O     . LYS A 1 2551 ? 119.342 187.376 181.595 1.00 44.57  ? 2551 LYS A O     1 
ATOM   9553  C CB    . LYS A 1 2551 ? 120.400 188.566 183.978 1.00 44.57  ? 2551 LYS A CB    1 
ATOM   9554  C CG    . LYS A 1 2551 ? 120.708 189.161 185.340 1.00 44.57  ? 2551 LYS A CG    1 
ATOM   9555  C CD    . LYS A 1 2551 ? 119.870 190.406 185.586 1.00 44.57  ? 2551 LYS A CD    1 
ATOM   9556  C CE    . LYS A 1 2551 ? 120.333 191.156 186.822 1.00 44.57  ? 2551 LYS A CE    1 
ATOM   9557  N NZ    . LYS A 1 2551 ? 120.544 190.241 187.977 1.00 44.57  ? 2551 LYS A NZ    1 
ATOM   9558  N N     . VAL A 1 2552 ? 118.720 185.617 182.848 1.00 47.45  ? 2552 VAL A N     1 
ATOM   9559  C CA    . VAL A 1 2552 ? 118.625 184.691 181.724 1.00 47.45  ? 2552 VAL A CA    1 
ATOM   9560  C C     . VAL A 1 2552 ? 117.187 184.730 181.210 1.00 47.45  ? 2552 VAL A C     1 
ATOM   9561  O O     . VAL A 1 2552 ? 116.273 184.303 181.935 1.00 47.45  ? 2552 VAL A O     1 
ATOM   9562  C CB    . VAL A 1 2552 ? 119.025 183.267 182.129 1.00 47.45  ? 2552 VAL A CB    1 
ATOM   9563  C CG1   . VAL A 1 2552 ? 119.167 182.395 180.896 1.00 47.45  ? 2552 VAL A CG1   1 
ATOM   9564  C CG2   . VAL A 1 2552 ? 120.318 183.285 182.919 1.00 47.45  ? 2552 VAL A CG2   1 
ATOM   9565  N N     . PRO A 1 2553 ? 116.943 185.219 179.998 1.00 54.61  ? 2553 PRO A N     1 
ATOM   9566  C CA    . PRO A 1 2553 ? 115.579 185.240 179.469 1.00 54.61  ? 2553 PRO A CA    1 
ATOM   9567  C C     . PRO A 1 2553 ? 115.198 183.908 178.841 1.00 54.61  ? 2553 PRO A C     1 
ATOM   9568  O O     . PRO A 1 2553 ? 116.044 183.113 178.429 1.00 54.61  ? 2553 PRO A O     1 
ATOM   9569  C CB    . PRO A 1 2553 ? 115.634 186.348 178.413 1.00 54.61  ? 2553 PRO A CB    1 
ATOM   9570  C CG    . PRO A 1 2553 ? 117.042 186.295 177.914 1.00 54.61  ? 2553 PRO A CG    1 
ATOM   9571  C CD    . PRO A 1 2553 ? 117.907 185.834 179.069 1.00 54.61  ? 2553 PRO A CD    1 
ATOM   9572  N N     . GLN A 1 2554 ? 113.890 183.676 178.777 1.00 56.11  ? 2554 GLN A N     1 
ATOM   9573  C CA    . GLN A 1 2554 ? 113.345 182.499 178.114 1.00 56.11  ? 2554 GLN A CA    1 
ATOM   9574  C C     . GLN A 1 2554 ? 113.000 182.859 176.675 1.00 56.11  ? 2554 GLN A C     1 
ATOM   9575  O O     . GLN A 1 2554 ? 112.132 183.704 176.431 1.00 56.11  ? 2554 GLN A O     1 
ATOM   9576  C CB    . GLN A 1 2554 ? 112.114 181.977 178.853 1.00 56.11  ? 2554 GLN A CB    1 
ATOM   9577  C CG    . GLN A 1 2554 ? 111.554 180.693 178.270 1.00 56.11  ? 2554 GLN A CG    1 
ATOM   9578  C CD    . GLN A 1 2554 ? 112.561 179.561 178.290 1.00 56.11  ? 2554 GLN A CD    1 
ATOM   9579  O OE1   . GLN A 1 2554 ? 113.132 179.205 177.259 1.00 56.11  ? 2554 GLN A OE1   1 
ATOM   9580  N NE2   . GLN A 1 2554 ? 112.786 178.989 179.467 1.00 56.11  ? 2554 GLN A NE2   1 
ATOM   9581  N N     . ILE A 1 2555 ? 113.677 182.217 175.726 1.00 52.99  ? 2555 ILE A N     1 
ATOM   9582  C CA    . ILE A 1 2555 ? 113.503 182.523 174.311 1.00 52.99  ? 2555 ILE A CA    1 
ATOM   9583  C C     . ILE A 1 2555 ? 112.682 181.411 173.670 1.00 52.99  ? 2555 ILE A C     1 
ATOM   9584  O O     . ILE A 1 2555 ? 112.615 180.293 174.194 1.00 52.99  ? 2555 ILE A O     1 
ATOM   9585  C CB    . ILE A 1 2555 ? 114.869 182.698 173.618 1.00 52.99  ? 2555 ILE A CB    1 
ATOM   9586  C CG1   . ILE A 1 2555 ? 114.706 183.270 172.207 1.00 52.99  ? 2555 ILE A CG1   1 
ATOM   9587  C CG2   . ILE A 1 2555 ? 115.622 181.379 173.578 1.00 52.99  ? 2555 ILE A CG2   1 
ATOM   9588  C CD1   . ILE A 1 2555 ? 115.999 183.763 171.599 1.00 52.99  ? 2555 ILE A CD1   1 
ATOM   9589  N N     . GLU A 1 2556 ? 112.033 181.712 172.542 1.00 57.32  ? 2556 GLU A N     1 
ATOM   9590  C CA    . GLU A 1 2556 ? 111.241 180.732 171.794 1.00 57.32  ? 2556 GLU A CA    1 
ATOM   9591  C C     . GLU A 1 2556 ? 111.624 180.867 170.321 1.00 57.32  ? 2556 GLU A C     1 
ATOM   9592  O O     . GLU A 1 2556 ? 111.061 181.688 169.594 1.00 57.32  ? 2556 GLU A O     1 
ATOM   9593  C CB    . GLU A 1 2556 ? 109.747 180.938 172.012 1.00 57.32  ? 2556 GLU A CB    1 
ATOM   9594  C CG    . GLU A 1 2556 ? 109.302 180.855 173.467 1.00 57.32  ? 2556 GLU A CG    1 
ATOM   9595  C CD    . GLU A 1 2556 ? 109.337 179.441 174.023 1.00 57.32  ? 2556 GLU A CD    1 
ATOM   9596  O OE1   . GLU A 1 2556 ? 109.614 178.496 173.255 1.00 57.32  ? 2556 GLU A OE1   1 
ATOM   9597  O OE2   . GLU A 1 2556 ? 109.086 179.276 175.235 1.00 57.32  ? 2556 GLU A OE2   1 
ATOM   9598  N N     . VAL A 1 2557 ? 112.590 180.052 169.890 1.00 57.24  ? 2557 VAL A N     1 
ATOM   9599  C CA    . VAL A 1 2557 ? 113.054 180.126 168.513 1.00 57.24  ? 2557 VAL A CA    1 
ATOM   9600  C C     . VAL A 1 2557 ? 112.003 179.520 167.578 1.00 57.24  ? 2557 VAL A C     1 
ATOM   9601  O O     . VAL A 1 2557 ? 111.133 178.743 167.988 1.00 57.24  ? 2557 VAL A O     1 
ATOM   9602  C CB    . VAL A 1 2557 ? 114.416 179.426 168.365 1.00 57.24  ? 2557 VAL A CB    1 
ATOM   9603  C CG1   . VAL A 1 2557 ? 114.273 177.923 168.524 1.00 57.24  ? 2557 VAL A CG1   1 
ATOM   9604  C CG2   . VAL A 1 2557 ? 115.090 179.785 167.044 1.00 57.24  ? 2557 VAL A CG2   1 
ATOM   9605  N N     . GLU A 1 2558 ? 112.081 179.906 166.305 1.00 65.32  ? 2558 GLU A N     1 
ATOM   9606  C CA    . GLU A 1 2558 ? 111.110 179.463 165.314 1.00 65.32  ? 2558 GLU A CA    1 
ATOM   9607  C C     . GLU A 1 2558 ? 111.219 177.960 165.079 1.00 65.32  ? 2558 GLU A C     1 
ATOM   9608  O O     . GLU A 1 2558 ? 112.287 177.364 165.242 1.00 65.32  ? 2558 GLU A O     1 
ATOM   9609  C CB    . GLU A 1 2558 ? 111.326 180.226 164.003 1.00 65.32  ? 2558 GLU A CB    1 
ATOM   9610  C CG    . GLU A 1 2558 ? 110.347 179.892 162.885 1.00 65.32  ? 2558 GLU A CG    1 
ATOM   9611  C CD    . GLU A 1 2558 ? 108.920 180.292 163.210 1.00 65.32  ? 2558 GLU A CD    1 
ATOM   9612  O OE1   . GLU A 1 2558 ? 108.729 181.224 164.020 1.00 65.32  ? 2558 GLU A OE1   1 
ATOM   9613  O OE2   . GLU A 1 2558 ? 107.989 179.672 162.655 1.00 65.32  ? 2558 GLU A OE2   1 
ATOM   9614  N N     . THR A 1 2559 ? 110.093 177.345 164.700 1.00 63.19  ? 2559 THR A N     1 
ATOM   9615  C CA    . THR A 1 2559 ? 110.093 175.926 164.363 1.00 63.19  ? 2559 THR A CA    1 
ATOM   9616  C C     . THR A 1 2559 ? 111.050 175.623 163.219 1.00 63.19  ? 2559 THR A C     1 
ATOM   9617  O O     . THR A 1 2559 ? 111.682 174.561 163.203 1.00 63.19  ? 2559 THR A O     1 
ATOM   9618  C CB    . THR A 1 2559 ? 108.684 175.471 163.981 1.00 63.19  ? 2559 THR A CB    1 
ATOM   9619  O OG1   . THR A 1 2559 ? 108.246 176.196 162.826 1.00 63.19  ? 2559 THR A OG1   1 
ATOM   9620  C CG2   . THR A 1 2559 ? 107.713 175.729 165.115 1.00 63.19  ? 2559 THR A CG2   1 
ATOM   9621  N N     . HIS A 1 2560 ? 111.171 176.538 162.263 1.00 62.36  ? 2560 HIS A N     1 
ATOM   9622  C CA    . HIS A 1 2560 ? 112.014 176.355 161.091 1.00 62.36  ? 2560 HIS A CA    1 
ATOM   9623  C C     . HIS A 1 2560 ? 113.478 176.682 161.365 1.00 62.36  ? 2560 HIS A C     1 
ATOM   9624  O O     . HIS A 1 2560 ? 114.322 176.489 160.484 1.00 62.36  ? 2560 HIS A O     1 
ATOM   9625  C CB    . HIS A 1 2560 ? 111.482 177.214 159.939 1.00 62.36  ? 2560 HIS A CB    1 
ATOM   9626  C CG    . HIS A 1 2560 ? 112.181 176.987 158.635 1.00 62.36  ? 2560 HIS A CG    1 
ATOM   9627  N ND1   . HIS A 1 2560 ? 113.331 177.659 158.282 1.00 62.36  ? 2560 HIS A ND1   1 
ATOM   9628  C CD2   . HIS A 1 2560 ? 111.892 176.165 157.598 1.00 62.36  ? 2560 HIS A CD2   1 
ATOM   9629  C CE1   . HIS A 1 2560 ? 113.721 177.261 157.085 1.00 62.36  ? 2560 HIS A CE1   1 
ATOM   9630  N NE2   . HIS A 1 2560 ? 112.865 176.355 156.648 1.00 62.36  ? 2560 HIS A NE2   1 
ATOM   9631  N N     . LYS A 1 2561 ? 113.800 177.158 162.569 1.00 60.36  ? 2561 LYS A N     1 
ATOM   9632  C CA    . LYS A 1 2561 ? 115.161 177.556 162.904 1.00 60.36  ? 2561 LYS A CA    1 
ATOM   9633  C C     . LYS A 1 2561 ? 115.730 176.710 164.042 1.00 60.36  ? 2561 LYS A C     1 
ATOM   9634  O O     . LYS A 1 2561 ? 116.756 177.077 164.626 1.00 60.36  ? 2561 LYS A O     1 
ATOM   9635  C CB    . LYS A 1 2561 ? 115.188 179.054 163.251 1.00 60.36  ? 2561 LYS A CB    1 
ATOM   9636  C CG    . LYS A 1 2561 ? 116.565 179.691 163.381 1.00 60.36  ? 2561 LYS A CG    1 
ATOM   9637  C CD    . LYS A 1 2561 ? 116.462 181.175 163.673 1.00 60.36  ? 2561 LYS A CD    1 
ATOM   9638  C CE    . LYS A 1 2561 ? 116.013 181.939 162.440 1.00 60.36  ? 2561 LYS A CE    1 
ATOM   9639  N NZ    . LYS A 1 2561 ? 117.037 181.898 161.359 1.00 60.36  ? 2561 LYS A NZ    1 
ATOM   9640  N N     . VAL A 1 2562 ? 115.102 175.575 164.360 1.00 51.76  ? 2562 VAL A N     1 
ATOM   9641  C CA    . VAL A 1 2562 ? 115.580 174.745 165.457 1.00 51.76  ? 2562 VAL A CA    1 
ATOM   9642  C C     . VAL A 1 2562 ? 116.949 174.176 165.118 1.00 51.76  ? 2562 VAL A C     1 
ATOM   9643  O O     . VAL A 1 2562 ? 117.178 173.671 164.013 1.00 51.76  ? 2562 VAL A O     1 
ATOM   9644  C CB    . VAL A 1 2562 ? 114.570 173.626 165.765 1.00 51.76  ? 2562 VAL A CB    1 
ATOM   9645  C CG1   . VAL A 1 2562 ? 115.040 172.799 166.949 1.00 51.76  ? 2562 VAL A CG1   1 
ATOM   9646  C CG2   . VAL A 1 2562 ? 113.199 174.214 166.035 1.00 51.76  ? 2562 VAL A CG2   1 
ATOM   9647  N N     . ALA A 1 2563 ? 117.868 174.265 166.083 1.00 47.12  ? 2563 ALA A N     1 
ATOM   9648  C CA    . ALA A 1 2563 ? 119.238 173.772 165.935 1.00 47.12  ? 2563 ALA A CA    1 
ATOM   9649  C C     . ALA A 1 2563 ? 119.935 174.413 164.737 1.00 47.12  ? 2563 ALA A C     1 
ATOM   9650  O O     . ALA A 1 2563 ? 120.688 173.761 164.011 1.00 47.12  ? 2563 ALA A O     1 
ATOM   9651  C CB    . ALA A 1 2563 ? 119.272 172.246 165.833 1.00 47.12  ? 2563 ALA A CB    1 
ATOM   9652  N N     . ALA A 1 2564 ? 119.681 175.700 164.530 1.00 47.43  ? 2564 ALA A N     1 
ATOM   9653  C CA    . ALA A 1 2564 ? 120.330 176.413 163.442 1.00 47.43  ? 2564 ALA A CA    1 
ATOM   9654  C C     . ALA A 1 2564 ? 121.820 176.571 163.737 1.00 47.43  ? 2564 ALA A C     1 
ATOM   9655  O O     . ALA A 1 2564 ? 122.214 176.697 164.900 1.00 47.43  ? 2564 ALA A O     1 
ATOM   9656  C CB    . ALA A 1 2564 ? 119.687 177.783 163.237 1.00 47.43  ? 2564 ALA A CB    1 
ATOM   9657  N N     . PRO A 1 2565 ? 122.673 176.562 162.708 1.00 49.35  ? 2565 PRO A N     1 
ATOM   9658  C CA    . PRO A 1 2565 ? 124.120 176.688 162.945 1.00 49.35  ? 2565 PRO A CA    1 
ATOM   9659  C C     . PRO A 1 2565 ? 124.534 178.013 163.565 1.00 49.35  ? 2565 PRO A C     1 
ATOM   9660  O O     . PRO A 1 2565 ? 125.628 178.087 164.139 1.00 49.35  ? 2565 PRO A O     1 
ATOM   9661  C CB    . PRO A 1 2565 ? 124.725 176.525 161.542 1.00 49.35  ? 2565 PRO A CB    1 
ATOM   9662  C CG    . PRO A 1 2565 ? 123.653 175.865 160.728 1.00 49.35  ? 2565 PRO A CG    1 
ATOM   9663  C CD    . PRO A 1 2565 ? 122.362 176.375 161.281 1.00 49.35  ? 2565 PRO A CD    1 
ATOM   9664  N N     . ASP A 1 2566 ? 123.711 179.053 163.472 1.00 47.43  ? 2566 ASP A N     1 
ATOM   9665  C CA    . ASP A 1 2566 ? 124.069 180.373 163.977 1.00 47.43  ? 2566 ASP A CA    1 
ATOM   9666  C C     . ASP A 1 2566 ? 123.161 180.867 165.091 1.00 47.43  ? 2566 ASP A C     1 
ATOM   9667  O O     . ASP A 1 2566 ? 123.474 181.877 165.727 1.00 47.43  ? 2566 ASP A O     1 
ATOM   9668  C CB    . ASP A 1 2566 ? 124.061 181.394 162.830 1.00 47.43  ? 2566 ASP A CB    1 
ATOM   9669  C CG    . ASP A 1 2566 ? 122.694 181.543 162.192 1.00 47.43  ? 2566 ASP A CG    1 
ATOM   9670  O OD1   . ASP A 1 2566 ? 122.166 180.538 161.673 1.00 47.43  ? 2566 ASP A OD1   1 
ATOM   9671  O OD2   . ASP A 1 2566 ? 122.147 182.665 162.213 1.00 47.43  ? 2566 ASP A OD2   1 
ATOM   9672  N N     . VAL A 1 2567 ? 122.038 180.190 165.345 1.00 46.04  ? 2567 VAL A N     1 
ATOM   9673  C CA    . VAL A 1 2567 ? 121.113 180.654 166.371 1.00 46.04  ? 2567 VAL A CA    1 
ATOM   9674  C C     . VAL A 1 2567 ? 121.759 180.515 167.743 1.00 46.04  ? 2567 VAL A C     1 
ATOM   9675  O O     . VAL A 1 2567 ? 122.624 179.659 167.960 1.00 46.04  ? 2567 VAL A O     1 
ATOM   9676  C CB    . VAL A 1 2567 ? 119.782 179.884 166.286 1.00 46.04  ? 2567 VAL A CB    1 
ATOM   9677  C CG1   . VAL A 1 2567 ? 119.934 178.478 166.845 1.00 46.04  ? 2567 VAL A CG1   1 
ATOM   9678  C CG2   . VAL A 1 2567 ? 118.679 180.640 167.010 1.00 46.04  ? 2567 VAL A CG2   1 
ATOM   9679  N N     . VAL A 1 2568 ? 121.351 181.378 168.671 1.00 41.21  ? 2568 VAL A N     1 
ATOM   9680  C CA    . VAL A 1 2568 ? 121.911 181.417 170.016 1.00 41.21  ? 2568 VAL A CA    1 
ATOM   9681  C C     . VAL A 1 2568 ? 120.772 181.362 171.019 1.00 41.21  ? 2568 VAL A C     1 
ATOM   9682  O O     . VAL A 1 2568 ? 119.823 182.148 170.929 1.00 41.21  ? 2568 VAL A O     1 
ATOM   9683  C CB    . VAL A 1 2568 ? 122.754 182.684 170.246 1.00 41.21  ? 2568 VAL A CB    1 
ATOM   9684  C CG1   . VAL A 1 2568 ? 123.242 182.745 171.689 1.00 41.21  ? 2568 VAL A CG1   1 
ATOM   9685  C CG2   . VAL A 1 2568 ? 123.899 182.738 169.269 1.00 41.21  ? 2568 VAL A CG2   1 
ATOM   9686  N N     . VAL A 1 2569 ? 120.870 180.447 171.976 1.00 39.25  ? 2569 VAL A N     1 
ATOM   9687  C CA    . VAL A 1 2569 ? 119.932 180.376 173.091 1.00 39.25  ? 2569 VAL A CA    1 
ATOM   9688  C C     . VAL A 1 2569 ? 120.643 180.911 174.331 1.00 39.25  ? 2569 VAL A C     1 
ATOM   9689  O O     . VAL A 1 2569 ? 121.604 180.278 174.795 1.00 39.25  ? 2569 VAL A O     1 
ATOM   9690  C CB    . VAL A 1 2569 ? 119.434 178.946 173.316 1.00 39.25  ? 2569 VAL A CB    1 
ATOM   9691  C CG1   . VAL A 1 2569 ? 118.542 178.879 174.546 1.00 39.25  ? 2569 VAL A CG1   1 
ATOM   9692  C CG2   . VAL A 1 2569 ? 118.697 178.448 172.085 1.00 39.25  ? 2569 VAL A CG2   1 
ATOM   9693  N N     . PRO A 1 2570 ? 120.230 182.054 174.875 1.00 39.41  ? 2570 PRO A N     1 
ATOM   9694  C CA    . PRO A 1 2570 ? 120.907 182.593 176.060 1.00 39.41  ? 2570 PRO A CA    1 
ATOM   9695  C C     . PRO A 1 2570 ? 120.822 181.641 177.245 1.00 39.41  ? 2570 PRO A C     1 
ATOM   9696  O O     . PRO A 1 2570 ? 119.801 180.990 177.474 1.00 39.41  ? 2570 PRO A O     1 
ATOM   9697  C CB    . PRO A 1 2570 ? 120.153 183.899 176.334 1.00 39.41  ? 2570 PRO A CB    1 
ATOM   9698  C CG    . PRO A 1 2570 ? 119.556 184.274 175.019 1.00 39.41  ? 2570 PRO A CG    1 
ATOM   9699  C CD    . PRO A 1 2570 ? 119.215 182.979 174.346 1.00 39.41  ? 2570 PRO A CD    1 
ATOM   9700  N N     . THR A 1 2571 ? 121.915 181.572 178.001 1.00 38.18  ? 2571 THR A N     1 
ATOM   9701  C CA    . THR A 1 2571 ? 121.981 180.767 179.211 1.00 38.18  ? 2571 THR A CA    1 
ATOM   9702  C C     . THR A 1 2571 ? 122.935 181.448 180.184 1.00 38.18  ? 2571 THR A C     1 
ATOM   9703  O O     . THR A 1 2571 ? 123.449 182.537 179.916 1.00 38.18  ? 2571 THR A O     1 
ATOM   9704  C CB    . THR A 1 2571 ? 122.420 179.333 178.904 1.00 38.18  ? 2571 THR A CB    1 
ATOM   9705  O OG1   . THR A 1 2571 ? 122.567 178.604 180.129 1.00 38.18  ? 2571 THR A OG1   1 
ATOM   9706  C CG2   . THR A 1 2571 ? 123.743 179.331 178.158 1.00 38.18  ? 2571 THR A CG2   1 
ATOM   9707  N N     . LEU A 1 2572 ? 123.170 180.795 181.324 1.00 38.16  ? 2572 LEU A N     1 
ATOM   9708  C CA    . LEU A 1 2572 ? 124.028 181.379 182.351 1.00 38.16  ? 2572 LEU A CA    1 
ATOM   9709  C C     . LEU A 1 2572 ? 125.448 181.580 181.833 1.00 38.16  ? 2572 LEU A C     1 
ATOM   9710  O O     . LEU A 1 2572 ? 126.030 182.664 181.976 1.00 38.16  ? 2572 LEU A O     1 
ATOM   9711  C CB    . LEU A 1 2572 ? 124.021 180.493 183.598 1.00 38.16  ? 2572 LEU A CB    1 
ATOM   9712  C CG    . LEU A 1 2572 ? 124.800 180.968 184.826 1.00 38.16  ? 2572 LEU A CG    1 
ATOM   9713  C CD1   . LEU A 1 2572 ? 124.033 180.636 186.092 1.00 38.16  ? 2572 LEU A CD1   1 
ATOM   9714  C CD2   . LEU A 1 2572 ? 126.176 180.331 184.870 1.00 38.16  ? 2572 LEU A CD2   1 
ATOM   9715  N N     . ASP A 1 2573 ? 126.021 180.542 181.218 1.00 36.97  ? 2573 ASP A N     1 
ATOM   9716  C CA    . ASP A 1 2573 ? 127.366 180.663 180.667 1.00 36.97  ? 2573 ASP A CA    1 
ATOM   9717  C C     . ASP A 1 2573 ? 127.421 181.732 179.588 1.00 36.97  ? 2573 ASP A C     1 
ATOM   9718  O O     . ASP A 1 2573 ? 128.352 182.547 179.556 1.00 36.97  ? 2573 ASP A O     1 
ATOM   9719  C CB    . ASP A 1 2573 ? 127.827 179.319 180.104 1.00 36.97  ? 2573 ASP A CB    1 
ATOM   9720  C CG    . ASP A 1 2573 ? 127.881 178.231 181.156 1.00 36.97  ? 2573 ASP A CG    1 
ATOM   9721  O OD1   . ASP A 1 2573 ? 127.365 178.452 182.270 1.00 36.97  ? 2573 ASP A OD1   1 
ATOM   9722  O OD2   . ASP A 1 2573 ? 128.440 177.153 180.867 1.00 36.97  ? 2573 ASP A OD2   1 
ATOM   9723  N N     . THR A 1 2574 ? 126.425 181.750 178.701 1.00 37.04  ? 2574 THR A N     1 
ATOM   9724  C CA    . THR A 1 2574 ? 126.423 182.706 177.601 1.00 37.04  ? 2574 THR A CA    1 
ATOM   9725  C C     . THR A 1 2574 ? 126.362 184.137 178.120 1.00 37.04  ? 2574 THR A C     1 
ATOM   9726  O O     . THR A 1 2574 ? 127.116 185.001 177.666 1.00 37.04  ? 2574 THR A O     1 
ATOM   9727  C CB    . THR A 1 2574 ? 125.253 182.419 176.659 1.00 37.04  ? 2574 THR A CB    1 
ATOM   9728  O OG1   . THR A 1 2574 ? 125.539 181.243 175.892 1.00 37.04  ? 2574 THR A OG1   1 
ATOM   9729  C CG2   . THR A 1 2574 ? 125.024 183.587 175.710 1.00 37.04  ? 2574 THR A CG2   1 
ATOM   9730  N N     . VAL A 1 2575 ? 125.491 184.402 179.095 1.00 38.67  ? 2575 VAL A N     1 
ATOM   9731  C CA    . VAL A 1 2575 ? 125.338 185.770 179.584 1.00 38.67  ? 2575 VAL A CA    1 
ATOM   9732  C C     . VAL A 1 2575 ? 126.563 186.202 180.391 1.00 38.67  ? 2575 VAL A C     1 
ATOM   9733  O O     . VAL A 1 2575 ? 127.030 187.344 180.269 1.00 38.67  ? 2575 VAL A O     1 
ATOM   9734  C CB    . VAL A 1 2575 ? 124.022 185.917 180.375 1.00 38.67  ? 2575 VAL A CB    1 
ATOM   9735  C CG1   . VAL A 1 2575 ? 124.047 185.135 181.679 1.00 38.67  ? 2575 VAL A CG1   1 
ATOM   9736  C CG2   . VAL A 1 2575 ? 123.717 187.384 180.629 1.00 38.67  ? 2575 VAL A CG2   1 
ATOM   9737  N N     . ARG A 1 2576 ? 127.119 185.300 181.207 1.00 35.66  ? 2576 ARG A N     1 
ATOM   9738  C CA    . ARG A 1 2576 ? 128.327 185.637 181.957 1.00 35.66  ? 2576 ARG A CA    1 
ATOM   9739  C C     . ARG A 1 2576 ? 129.477 185.964 181.013 1.00 35.66  ? 2576 ARG A C     1 
ATOM   9740  O O     . ARG A 1 2576 ? 130.154 186.994 181.160 1.00 35.66  ? 2576 ARG A O     1 
ATOM   9741  C CB    . ARG A 1 2576 ? 128.706 184.476 182.873 1.00 35.66  ? 2576 ARG A CB    1 
ATOM   9742  C CG    . ARG A 1 2576 ? 127.979 184.454 184.197 1.00 35.66  ? 2576 ARG A CG    1 
ATOM   9743  C CD    . ARG A 1 2576 ? 128.620 183.455 185.136 1.00 35.66  ? 2576 ARG A CD    1 
ATOM   9744  N NE    . ARG A 1 2576 ? 129.105 182.280 184.422 1.00 35.66  ? 2576 ARG A NE    1 
ATOM   9745  C CZ    . ARG A 1 2576 ? 129.524 181.171 185.013 1.00 35.66  ? 2576 ARG A CZ    1 
ATOM   9746  N NH1   . ARG A 1 2576 ? 129.521 181.047 186.330 1.00 35.66  ? 2576 ARG A NH1   1 
ATOM   9747  N NH2   . ARG A 1 2576 ? 129.953 180.159 184.265 1.00 35.66  ? 2576 ARG A NH2   1 
ATOM   9748  N N     . HIS A 1 2577 ? 129.701 185.103 180.018 1.00 33.42  ? 2577 HIS A N     1 
ATOM   9749  C CA    . HIS A 1 2577 ? 130.765 185.358 179.059 1.00 33.42  ? 2577 HIS A CA    1 
ATOM   9750  C C     . HIS A 1 2577 ? 130.488 186.608 178.241 1.00 33.42  ? 2577 HIS A C     1 
ATOM   9751  O O     . HIS A 1 2577 ? 131.419 187.341 177.916 1.00 33.42  ? 2577 HIS A O     1 
ATOM   9752  C CB    . HIS A 1 2577 ? 130.960 184.142 178.156 1.00 33.42  ? 2577 HIS A CB    1 
ATOM   9753  C CG    . HIS A 1 2577 ? 131.399 182.916 178.892 1.00 33.42  ? 2577 HIS A CG    1 
ATOM   9754  N ND1   . HIS A 1 2577 ? 130.601 181.801 179.030 1.00 33.42  ? 2577 HIS A ND1   1 
ATOM   9755  C CD2   . HIS A 1 2577 ? 132.547 182.640 179.556 1.00 33.42  ? 2577 HIS A CD2   1 
ATOM   9756  C CE1   . HIS A 1 2577 ? 131.242 180.887 179.736 1.00 33.42  ? 2577 HIS A CE1   1 
ATOM   9757  N NE2   . HIS A 1 2577 ? 132.425 181.371 180.068 1.00 33.42  ? 2577 HIS A NE2   1 
ATOM   9758  N N     . GLU A 1 2578 ? 129.227 186.887 177.924 1.00 35.95  ? 2578 GLU A N     1 
ATOM   9759  C CA    . GLU A 1 2578 ? 128.907 188.100 177.183 1.00 35.95  ? 2578 GLU A CA    1 
ATOM   9760  C C     . GLU A 1 2578 ? 129.270 189.344 177.986 1.00 35.95  ? 2578 GLU A C     1 
ATOM   9761  O O     . GLU A 1 2578 ? 129.820 190.312 177.438 1.00 35.95  ? 2578 GLU A O     1 
ATOM   9762  C CB    . GLU A 1 2578 ? 127.427 188.092 176.810 1.00 35.95  ? 2578 GLU A CB    1 
ATOM   9763  C CG    . GLU A 1 2578 ? 126.856 189.451 176.498 1.00 35.95  ? 2578 GLU A CG    1 
ATOM   9764  C CD    . GLU A 1 2578 ? 125.422 189.384 176.001 1.00 35.95  ? 2578 GLU A CD    1 
ATOM   9765  O OE1   . GLU A 1 2578 ? 124.835 188.283 175.992 1.00 35.95  ? 2578 GLU A OE1   1 
ATOM   9766  O OE2   . GLU A 1 2578 ? 124.876 190.432 175.603 1.00 35.95  ? 2578 GLU A OE2   1 
ATOM   9767  N N     . ALA A 1 2579 ? 128.980 189.330 179.289 1.00 31.55  ? 2579 ALA A N     1 
ATOM   9768  C CA    . ALA A 1 2579 ? 129.399 190.429 180.151 1.00 31.55  ? 2579 ALA A CA    1 
ATOM   9769  C C     . ALA A 1 2579 ? 130.915 190.569 180.161 1.00 31.55  ? 2579 ALA A C     1 
ATOM   9770  O O     . ALA A 1 2579 ? 131.447 191.680 180.048 1.00 31.55  ? 2579 ALA A O     1 
ATOM   9771  C CB    . ALA A 1 2579 ? 128.873 190.216 181.570 1.00 31.55  ? 2579 ALA A CB    1 
ATOM   9772  N N     . LEU A 1 2580 ? 131.633 189.449 180.287 1.00 27.47  ? 2580 LEU A N     1 
ATOM   9773  C CA    . LEU A 1 2580 ? 133.095 189.525 180.318 1.00 27.47  ? 2580 LEU A CA    1 
ATOM   9774  C C     . LEU A 1 2580 ? 133.669 190.056 179.006 1.00 27.47  ? 2580 LEU A C     1 
ATOM   9775  O O     . LEU A 1 2580 ? 134.610 190.858 179.014 1.00 27.47  ? 2580 LEU A O     1 
ATOM   9776  C CB    . LEU A 1 2580 ? 133.694 188.162 180.649 1.00 27.47  ? 2580 LEU A CB    1 
ATOM   9777  C CG    . LEU A 1 2580 ? 133.237 187.543 181.962 1.00 27.47  ? 2580 LEU A CG    1 
ATOM   9778  C CD1   . LEU A 1 2580 ? 133.955 186.228 182.175 1.00 27.47  ? 2580 LEU A CD1   1 
ATOM   9779  C CD2   . LEU A 1 2580 ? 133.497 188.508 183.108 1.00 27.47  ? 2580 LEU A CD2   1 
ATOM   9780  N N     . LEU A 1 2581 ? 133.134 189.608 177.867 1.00 27.83  ? 2581 LEU A N     1 
ATOM   9781  C CA    . LEU A 1 2581 ? 133.588 190.121 176.572 1.00 27.83  ? 2581 LEU A CA    1 
ATOM   9782  C C     . LEU A 1 2581 ? 133.300 191.605 176.404 1.00 27.83  ? 2581 LEU A C     1 
ATOM   9783  O O     . LEU A 1 2581 ? 134.146 192.345 175.899 1.00 27.83  ? 2581 LEU A O     1 
ATOM   9784  C CB    . LEU A 1 2581 ? 132.993 189.325 175.408 1.00 27.83  ? 2581 LEU A CB    1 
ATOM   9785  C CG    . LEU A 1 2581 ? 133.528 187.966 174.951 1.00 27.83  ? 2581 LEU A CG    1 
ATOM   9786  C CD1   . LEU A 1 2581 ? 133.299 186.788 175.839 1.00 27.83  ? 2581 LEU A CD1   1 
ATOM   9787  C CD2   . LEU A 1 2581 ? 132.798 187.718 173.653 1.00 27.83  ? 2581 LEU A CD2   1 
ATOM   9788  N N     . TYR A 1 2582 ? 132.115 192.067 176.801 1.00 30.54  ? 2582 TYR A N     1 
ATOM   9789  C CA    . TYR A 1 2582 ? 131.883 193.505 176.715 1.00 30.54  ? 2582 TYR A CA    1 
ATOM   9790  C C     . TYR A 1 2582 ? 132.850 194.270 177.611 1.00 30.54  ? 2582 TYR A C     1 
ATOM   9791  O O     . TYR A 1 2582 ? 133.382 195.317 177.212 1.00 30.54  ? 2582 TYR A O     1 
ATOM   9792  C CB    . TYR A 1 2582 ? 130.437 193.843 177.061 1.00 30.54  ? 2582 TYR A CB    1 
ATOM   9793  C CG    . TYR A 1 2582 ? 129.439 193.360 176.038 1.00 30.54  ? 2582 TYR A CG    1 
ATOM   9794  C CD1   . TYR A 1 2582 ? 129.760 193.342 174.687 1.00 30.54  ? 2582 TYR A CD1   1 
ATOM   9795  C CD2   . TYR A 1 2582 ? 128.151 193.006 176.407 1.00 30.54  ? 2582 TYR A CD2   1 
ATOM   9796  C CE1   . TYR A 1 2582 ? 128.847 192.928 173.739 1.00 30.54  ? 2582 TYR A CE1   1 
ATOM   9797  C CE2   . TYR A 1 2582 ? 127.226 192.604 175.465 1.00 30.54  ? 2582 TYR A CE2   1 
ATOM   9798  C CZ    . TYR A 1 2582 ? 127.580 192.562 174.132 1.00 30.54  ? 2582 TYR A CZ    1 
ATOM   9799  O OH    . TYR A 1 2582 ? 126.665 192.157 173.187 1.00 30.54  ? 2582 TYR A OH    1 
ATOM   9800  N N     . THR A 1 2583 ? 133.116 193.746 178.809 1.00 23.67  ? 2583 THR A N     1 
ATOM   9801  C CA    . THR A 1 2583 ? 134.058 194.400 179.712 1.00 23.67  ? 2583 THR A CA    1 
ATOM   9802  C C     . THR A 1 2583 ? 135.447 194.500 179.092 1.00 23.67  ? 2583 THR A C     1 
ATOM   9803  O O     . THR A 1 2583 ? 136.088 195.555 179.147 1.00 23.67  ? 2583 THR A O     1 
ATOM   9804  C CB    . THR A 1 2583 ? 134.116 193.647 181.040 1.00 23.67  ? 2583 THR A CB    1 
ATOM   9805  O OG1   . THR A 1 2583 ? 132.908 193.868 181.778 1.00 23.67  ? 2583 THR A OG1   1 
ATOM   9806  C CG2   . THR A 1 2583 ? 135.299 194.103 181.853 1.00 23.67  ? 2583 THR A CG2   1 
ATOM   9807  N N     . TRP A 1 2584 ? 135.925 193.414 178.484 1.00 18.33  ? 2584 TRP A N     1 
ATOM   9808  C CA    . TRP A 1 2584 ? 137.279 193.392 177.942 1.00 18.33  ? 2584 TRP A CA    1 
ATOM   9809  C C     . TRP A 1 2584 ? 137.387 193.983 176.544 1.00 18.33  ? 2584 TRP A C     1 
ATOM   9810  O O     . TRP A 1 2584 ? 138.507 194.183 176.063 1.00 18.33  ? 2584 TRP A O     1 
ATOM   9811  C CB    . TRP A 1 2584 ? 137.821 191.963 177.937 1.00 18.33  ? 2584 TRP A CB    1 
ATOM   9812  C CG    . TRP A 1 2584 ? 138.358 191.547 179.262 1.00 18.33  ? 2584 TRP A CG    1 
ATOM   9813  C CD1   . TRP A 1 2584 ? 139.118 192.298 180.106 1.00 18.33  ? 2584 TRP A CD1   1 
ATOM   9814  C CD2   . TRP A 1 2584 ? 138.166 190.287 179.910 1.00 18.33  ? 2584 TRP A CD2   1 
ATOM   9815  N NE1   . TRP A 1 2584 ? 139.419 191.582 181.236 1.00 18.33  ? 2584 TRP A NE1   1 
ATOM   9816  C CE2   . TRP A 1 2584 ? 138.845 190.343 181.141 1.00 18.33  ? 2584 TRP A CE2   1 
ATOM   9817  C CE3   . TRP A 1 2584 ? 137.488 189.115 179.567 1.00 18.33  ? 2584 TRP A CE3   1 
ATOM   9818  C CZ2   . TRP A 1 2584 ? 138.868 189.273 182.028 1.00 18.33  ? 2584 TRP A CZ2   1 
ATOM   9819  C CZ3   . TRP A 1 2584 ? 137.510 188.058 180.450 1.00 18.33  ? 2584 TRP A CZ3   1 
ATOM   9820  C CH2   . TRP A 1 2584 ? 138.195 188.142 181.666 1.00 18.33  ? 2584 TRP A CH2   1 
ATOM   9821  N N     . LEU A 1 2585 ? 136.268 194.251 175.878 1.00 27.85  ? 2585 LEU A N     1 
ATOM   9822  C CA    . LEU A 1 2585 ? 136.284 194.970 174.613 1.00 27.85  ? 2585 LEU A CA    1 
ATOM   9823  C C     . LEU A 1 2585 ? 136.065 196.463 174.791 1.00 27.85  ? 2585 LEU A C     1 
ATOM   9824  O O     . LEU A 1 2585 ? 136.367 197.234 173.872 1.00 27.85  ? 2585 LEU A O     1 
ATOM   9825  C CB    . LEU A 1 2585 ? 135.219 194.405 173.670 1.00 27.85  ? 2585 LEU A CB    1 
ATOM   9826  C CG    . LEU A 1 2585 ? 135.436 192.968 173.194 1.00 27.85  ? 2585 LEU A CG    1 
ATOM   9827  C CD1   . LEU A 1 2585 ? 134.240 192.499 172.392 1.00 27.85  ? 2585 LEU A CD1   1 
ATOM   9828  C CD2   . LEU A 1 2585 ? 136.712 192.858 172.374 1.00 27.85  ? 2585 LEU A CD2   1 
ATOM   9829  N N     . ALA A 1 2586 ? 135.542 196.887 175.945 1.00 26.23  ? 2586 ALA A N     1 
ATOM   9830  C CA    . ALA A 1 2586 ? 135.466 198.315 176.226 1.00 26.23  ? 2586 ALA A CA    1 
ATOM   9831  C C     . ALA A 1 2586 ? 136.851 198.945 176.293 1.00 26.23  ? 2586 ALA A C     1 
ATOM   9832  O O     . ALA A 1 2586 ? 137.053 200.054 175.787 1.00 26.23  ? 2586 ALA A O     1 
ATOM   9833  C CB    . ALA A 1 2586 ? 134.706 198.555 177.529 1.00 26.23  ? 2586 ALA A CB    1 
ATOM   9834  N N     . GLU A 1 2587 ? 137.815 198.255 176.902 1.00 25.83  ? 2587 GLU A N     1 
ATOM   9835  C CA    . GLU A 1 2587 ? 139.194 198.720 176.969 1.00 25.83  ? 2587 GLU A CA    1 
ATOM   9836  C C     . GLU A 1 2587 ? 140.028 198.240 175.791 1.00 25.83  ? 2587 GLU A C     1 
ATOM   9837  O O     . GLU A 1 2587 ? 141.243 198.463 175.773 1.00 25.83  ? 2587 GLU A O     1 
ATOM   9838  C CB    . GLU A 1 2587 ? 139.845 198.281 178.283 1.00 25.83  ? 2587 GLU A CB    1 
ATOM   9839  C CG    . GLU A 1 2587 ? 139.481 199.143 179.485 1.00 25.83  ? 2587 GLU A CG    1 
ATOM   9840  C CD    . GLU A 1 2587 ? 138.014 199.060 179.860 1.00 25.83  ? 2587 GLU A CD    1 
ATOM   9841  O OE1   . GLU A 1 2587 ? 137.544 199.937 180.614 1.00 25.83  ? 2587 GLU A OE1   1 
ATOM   9842  O OE2   . GLU A 1 2587 ? 137.334 198.111 179.418 1.00 25.83  ? 2587 GLU A OE2   1 
ATOM   9843  N N     . HIS A 1 2588 ? 139.405 197.568 174.825 1.00 28.16  ? 2588 HIS A N     1 
ATOM   9844  C CA    . HIS A 1 2588 ? 140.038 197.145 173.578 1.00 28.16  ? 2588 HIS A CA    1 
ATOM   9845  C C     . HIS A 1 2588 ? 141.143 196.123 173.809 1.00 28.16  ? 2588 HIS A C     1 
ATOM   9846  O O     . HIS A 1 2588 ? 142.001 195.921 172.944 1.00 28.16  ? 2588 HIS A O     1 
ATOM   9847  C CB    . HIS A 1 2588 ? 140.577 198.350 172.803 1.00 28.16  ? 2588 HIS A CB    1 
ATOM   9848  C CG    . HIS A 1 2588 ? 139.505 199.276 172.326 1.00 28.16  ? 2588 HIS A CG    1 
ATOM   9849  N ND1   . HIS A 1 2588 ? 139.032 200.321 173.090 1.00 28.16  ? 2588 HIS A ND1   1 
ATOM   9850  C CD2   . HIS A 1 2588 ? 138.781 199.288 171.184 1.00 28.16  ? 2588 HIS A CD2   1 
ATOM   9851  C CE1   . HIS A 1 2588 ? 138.082 200.955 172.426 1.00 28.16  ? 2588 HIS A CE1   1 
ATOM   9852  N NE2   . HIS A 1 2588 ? 137.911 200.348 171.265 1.00 28.16  ? 2588 HIS A NE2   1 
ATOM   9853  N N     . LYS A 1 2589 ? 141.134 195.476 174.967 1.00 18.75  ? 2589 LYS A N     1 
ATOM   9854  C CA    . LYS A 1 2589 ? 142.118 194.449 175.271 1.00 18.75  ? 2589 LYS A CA    1 
ATOM   9855  C C     . LYS A 1 2589 ? 141.768 193.170 174.524 1.00 18.75  ? 2589 LYS A C     1 
ATOM   9856  O O     . LYS A 1 2589 ? 140.645 192.673 174.665 1.00 18.75  ? 2589 LYS A O     1 
ATOM   9857  C CB    . LYS A 1 2589 ? 142.163 194.187 176.770 1.00 18.75  ? 2589 LYS A CB    1 
ATOM   9858  C CG    . LYS A 1 2589 ? 143.400 193.447 177.235 1.00 18.75  ? 2589 LYS A CG    1 
ATOM   9859  C CD    . LYS A 1 2589 ? 143.501 193.450 178.748 1.00 18.75  ? 2589 LYS A CD    1 
ATOM   9860  C CE    . LYS A 1 2589 ? 143.510 194.865 179.294 1.00 18.75  ? 2589 LYS A CE    1 
ATOM   9861  N NZ    . LYS A 1 2589 ? 144.759 195.588 178.928 1.00 18.75  ? 2589 LYS A NZ    1 
ATOM   9862  N N     . PRO A 1 2590 ? 142.671 192.619 173.719 1.00 17.51  ? 2590 PRO A N     1 
ATOM   9863  C CA    . PRO A 1 2590 ? 142.378 191.347 173.054 1.00 17.51  ? 2590 PRO A CA    1 
ATOM   9864  C C     . PRO A 1 2590 ? 142.198 190.231 174.067 1.00 17.51  ? 2590 PRO A C     1 
ATOM   9865  O O     . PRO A 1 2590 ? 142.849 190.200 175.112 1.00 17.51  ? 2590 PRO A O     1 
ATOM   9866  C CB    . PRO A 1 2590 ? 143.610 191.106 172.171 1.00 17.51  ? 2590 PRO A CB    1 
ATOM   9867  C CG    . PRO A 1 2590 ? 144.381 192.389 172.185 1.00 17.51  ? 2590 PRO A CG    1 
ATOM   9868  C CD    . PRO A 1 2590 ? 144.042 193.079 173.458 1.00 17.51  ? 2590 PRO A CD    1 
ATOM   9869  N N     . LEU A 1 2591 ? 141.294 189.308 173.749 1.00 15.51  ? 2591 LEU A N     1 
ATOM   9870  C CA    . LEU A 1 2591 ? 140.994 188.200 174.641 1.00 15.51  ? 2591 LEU A CA    1 
ATOM   9871  C C     . LEU A 1 2591 ? 140.919 186.912 173.836 1.00 15.51  ? 2591 LEU A C     1 
ATOM   9872  O O     . LEU A 1 2591 ? 140.645 186.919 172.634 1.00 15.51  ? 2591 LEU A O     1 
ATOM   9873  C CB    . LEU A 1 2591 ? 139.683 188.413 175.410 1.00 15.51  ? 2591 LEU A CB    1 
ATOM   9874  C CG    . LEU A 1 2591 ? 138.358 188.269 174.661 1.00 15.51  ? 2591 LEU A CG    1 
ATOM   9875  C CD1   . LEU A 1 2591 ? 137.216 188.134 175.652 1.00 15.51  ? 2591 LEU A CD1   1 
ATOM   9876  C CD2   . LEU A 1 2591 ? 138.111 189.446 173.735 1.00 15.51  ? 2591 LEU A CD2   1 
ATOM   9877  N N     . VAL A 1 2592 ? 141.171 185.800 174.521 1.00 17.52  ? 2592 VAL A N     1 
ATOM   9878  C CA    . VAL A 1 2592 ? 141.158 184.475 173.917 1.00 17.52  ? 2592 VAL A CA    1 
ATOM   9879  C C     . VAL A 1 2592 ? 140.188 183.604 174.699 1.00 17.52  ? 2592 VAL A C     1 
ATOM   9880  O O     . VAL A 1 2592 ? 140.259 183.541 175.931 1.00 17.52  ? 2592 VAL A O     1 
ATOM   9881  C CB    . VAL A 1 2592 ? 142.563 183.843 173.899 1.00 17.52  ? 2592 VAL A CB    1 
ATOM   9882  C CG1   . VAL A 1 2592 ? 142.501 182.422 173.376 1.00 17.52  ? 2592 VAL A CG1   1 
ATOM   9883  C CG2   . VAL A 1 2592 ? 143.507 184.681 173.057 1.00 17.52  ? 2592 VAL A CG2   1 
ATOM   9884  N N     . LEU A 1 2593 ? 139.278 182.943 173.991 1.00 21.06  ? 2593 LEU A N     1 
ATOM   9885  C CA    . LEU A 1 2593 ? 138.337 182.008 174.596 1.00 21.06  ? 2593 LEU A CA    1 
ATOM   9886  C C     . LEU A 1 2593 ? 138.893 180.601 174.412 1.00 21.06  ? 2593 LEU A C     1 
ATOM   9887  O O     . LEU A 1 2593 ? 138.907 180.075 173.296 1.00 21.06  ? 2593 LEU A O     1 
ATOM   9888  C CB    . LEU A 1 2593 ? 136.952 182.142 173.969 1.00 21.06  ? 2593 LEU A CB    1 
ATOM   9889  C CG    . LEU A 1 2593 ? 136.205 183.447 174.241 1.00 21.06  ? 2593 LEU A CG    1 
ATOM   9890  C CD1   . LEU A 1 2593 ? 134.789 183.372 173.701 1.00 21.06  ? 2593 LEU A CD1   1 
ATOM   9891  C CD2   . LEU A 1 2593 ? 136.195 183.752 175.728 1.00 21.06  ? 2593 LEU A CD2   1 
ATOM   9892  N N     . CYS A 1 2594 ? 139.349 179.996 175.502 1.00 24.89  ? 2594 CYS A N     1 
ATOM   9893  C CA    . CYS A 1 2594 ? 139.983 178.688 175.453 1.00 24.89  ? 2594 CYS A CA    1 
ATOM   9894  C C     . CYS A 1 2594 ? 139.088 177.648 176.112 1.00 24.89  ? 2594 CYS A C     1 
ATOM   9895  O O     . CYS A 1 2594 ? 138.550 177.876 177.197 1.00 24.89  ? 2594 CYS A O     1 
ATOM   9896  C CB    . CYS A 1 2594 ? 141.347 178.721 176.142 1.00 24.89  ? 2594 CYS A CB    1 
ATOM   9897  S SG    . CYS A 1 2594 ? 142.345 177.240 175.887 1.00 24.89  ? 2594 CYS A SG    1 
ATOM   9898  N N     . GLY A 1 2595 ? 138.930 176.506 175.449 1.00 28.84  ? 2595 GLY A N     1 
ATOM   9899  C CA    . GLY A 1 2595 ? 138.102 175.443 175.964 1.00 28.84  ? 2595 GLY A CA    1 
ATOM   9900  C C     . GLY A 1 2595 ? 138.056 174.236 175.051 1.00 28.84  ? 2595 GLY A C     1 
ATOM   9901  O O     . GLY A 1 2595 ? 138.573 174.254 173.930 1.00 28.84  ? 2595 GLY A O     1 
ATOM   9902  N N     . PRO A 1 2596 ? 137.419 173.165 175.514 1.00 29.52  ? 2596 PRO A N     1 
ATOM   9903  C CA    . PRO A 1 2596 ? 137.362 171.928 174.731 1.00 29.52  ? 2596 PRO A CA    1 
ATOM   9904  C C     . PRO A 1 2596 ? 136.573 172.130 173.451 1.00 29.52  ? 2596 PRO A C     1 
ATOM   9905  O O     . PRO A 1 2596 ? 135.730 173.036 173.372 1.00 29.52  ? 2596 PRO A O     1 
ATOM   9906  C CB    . PRO A 1 2596 ? 136.654 170.941 175.673 1.00 29.52  ? 2596 PRO A CB    1 
ATOM   9907  C CG    . PRO A 1 2596 ? 136.712 171.571 177.029 1.00 29.52  ? 2596 PRO A CG    1 
ATOM   9908  C CD    . PRO A 1 2596 ? 136.704 173.041 176.793 1.00 29.52  ? 2596 PRO A CD    1 
ATOM   9909  N N     . PRO A 1 2597 ? 136.832 171.324 172.422 1.00 30.55  ? 2597 PRO A N     1 
ATOM   9910  C CA    . PRO A 1 2597 ? 136.099 171.481 171.161 1.00 30.55  ? 2597 PRO A CA    1 
ATOM   9911  C C     . PRO A 1 2597 ? 134.602 171.299 171.357 1.00 30.55  ? 2597 PRO A C     1 
ATOM   9912  O O     . PRO A 1 2597 ? 134.154 170.435 172.113 1.00 30.55  ? 2597 PRO A O     1 
ATOM   9913  C CB    . PRO A 1 2597 ? 136.685 170.381 170.269 1.00 30.55  ? 2597 PRO A CB    1 
ATOM   9914  C CG    . PRO A 1 2597 ? 138.002 170.047 170.882 1.00 30.55  ? 2597 PRO A CG    1 
ATOM   9915  C CD    . PRO A 1 2597 ? 137.827 170.241 172.352 1.00 30.55  ? 2597 PRO A CD    1 
ATOM   9916  N N     . GLY A 1 2598 ? 133.828 172.130 170.664 1.00 31.44  ? 2598 GLY A N     1 
ATOM   9917  C CA    . GLY A 1 2598 ? 132.385 172.063 170.722 1.00 31.44  ? 2598 GLY A CA    1 
ATOM   9918  C C     . GLY A 1 2598 ? 131.755 172.698 171.940 1.00 31.44  ? 2598 GLY A C     1 
ATOM   9919  O O     . GLY A 1 2598 ? 130.525 172.672 172.061 1.00 31.44  ? 2598 GLY A O     1 
ATOM   9920  N N     . SER A 1 2599 ? 132.548 173.279 172.842 1.00 28.31  ? 2599 SER A N     1 
ATOM   9921  C CA    . SER A 1 2599 ? 132.006 173.831 174.077 1.00 28.31  ? 2599 SER A CA    1 
ATOM   9922  C C     . SER A 1 2599 ? 131.186 175.094 173.857 1.00 28.31  ? 2599 SER A C     1 
ATOM   9923  O O     . SER A 1 2599 ? 130.455 175.500 174.766 1.00 28.31  ? 2599 SER A O     1 
ATOM   9924  C CB    . SER A 1 2599 ? 133.136 174.121 175.064 1.00 28.31  ? 2599 SER A CB    1 
ATOM   9925  O OG    . SER A 1 2599 ? 133.978 175.153 174.583 1.00 28.31  ? 2599 SER A OG    1 
ATOM   9926  N N     . GLY A 1 2600 ? 131.285 175.722 172.689 1.00 27.68  ? 2600 GLY A N     1 
ATOM   9927  C CA    . GLY A 1 2600 ? 130.504 176.910 172.413 1.00 27.68  ? 2600 GLY A CA    1 
ATOM   9928  C C     . GLY A 1 2600 ? 131.289 178.198 172.531 1.00 27.68  ? 2600 GLY A C     1 
ATOM   9929  O O     . GLY A 1 2600 ? 130.804 179.175 173.108 1.00 27.68  ? 2600 GLY A O     1 
ATOM   9930  N N     . LYS A 1 2601 ? 132.509 178.213 171.994 1.00 29.09  ? 2601 LYS A N     1 
ATOM   9931  C CA    . LYS A 1 2601 ? 133.354 179.400 172.045 1.00 29.09  ? 2601 LYS A CA    1 
ATOM   9932  C C     . LYS A 1 2601 ? 133.219 180.254 170.789 1.00 29.09  ? 2601 LYS A C     1 
ATOM   9933  O O     . LYS A 1 2601 ? 132.876 181.436 170.874 1.00 29.09  ? 2601 LYS A O     1 
ATOM   9934  C CB    . LYS A 1 2601 ? 134.818 178.999 172.233 1.00 29.09  ? 2601 LYS A CB    1 
ATOM   9935  C CG    . LYS A 1 2601 ? 135.064 178.047 173.378 1.00 29.09  ? 2601 LYS A CG    1 
ATOM   9936  C CD    . LYS A 1 2601 ? 136.534 177.692 173.466 1.00 29.09  ? 2601 LYS A CD    1 
ATOM   9937  C CE    . LYS A 1 2601 ? 136.968 176.865 172.272 1.00 29.09  ? 2601 LYS A CE    1 
ATOM   9938  N NZ    . LYS A 1 2601 ? 136.204 175.594 172.175 1.00 29.09  ? 2601 LYS A NZ    1 
ATOM   9939  N N     . THR A 1 2602 ? 133.492 179.664 169.623 1.00 34.08  ? 2602 THR A N     1 
ATOM   9940  C CA    . THR A 1 2602 ? 133.508 180.424 168.377 1.00 34.08  ? 2602 THR A CA    1 
ATOM   9941  C C     . THR A 1 2602 ? 132.148 181.038 168.074 1.00 34.08  ? 2602 THR A C     1 
ATOM   9942  O O     . THR A 1 2602 ? 132.053 182.223 167.733 1.00 34.08  ? 2602 THR A O     1 
ATOM   9943  C CB    . THR A 1 2602 ? 133.948 179.518 167.227 1.00 34.08  ? 2602 THR A CB    1 
ATOM   9944  O OG1   . THR A 1 2602 ? 135.269 179.024 167.481 1.00 34.08  ? 2602 THR A OG1   1 
ATOM   9945  C CG2   . THR A 1 2602 ? 133.926 180.269 165.910 1.00 34.08  ? 2602 THR A CG2   1 
ATOM   9946  N N     . MET A 1 2603 ? 131.082 180.247 168.187 1.00 38.29  ? 2603 MET A N     1 
ATOM   9947  C CA    . MET A 1 2603 ? 129.757 180.731 167.819 1.00 38.29  ? 2603 MET A CA    1 
ATOM   9948  C C     . MET A 1 2603 ? 129.259 181.780 168.809 1.00 38.29  ? 2603 MET A C     1 
ATOM   9949  O O     . MET A 1 2603 ? 128.666 182.792 168.416 1.00 38.29  ? 2603 MET A O     1 
ATOM   9950  C CB    . MET A 1 2603 ? 128.796 179.546 167.720 1.00 38.29  ? 2603 MET A CB    1 
ATOM   9951  C CG    . MET A 1 2603 ? 127.387 179.875 167.280 1.00 38.29  ? 2603 MET A CG    1 
ATOM   9952  S SD    . MET A 1 2603 ? 126.387 180.473 168.645 1.00 38.29  ? 2603 MET A SD    1 
ATOM   9953  C CE    . MET A 1 2603 ? 126.170 178.956 169.551 1.00 38.29  ? 2603 MET A CE    1 
ATOM   9954  N N     . THR A 1 2604 ? 129.480 181.548 170.106 1.00 33.93  ? 2604 THR A N     1 
ATOM   9955  C CA    . THR A 1 2604 ? 129.095 182.537 171.109 1.00 33.93  ? 2604 THR A CA    1 
ATOM   9956  C C     . THR A 1 2604 ? 129.872 183.832 170.917 1.00 33.93  ? 2604 THR A C     1 
ATOM   9957  O O     . THR A 1 2604 ? 129.333 184.930 171.109 1.00 33.93  ? 2604 THR A O     1 
ATOM   9958  C CB    . THR A 1 2604 ? 129.326 181.976 172.512 1.00 33.93  ? 2604 THR A CB    1 
ATOM   9959  O OG1   . THR A 1 2604 ? 128.488 180.831 172.711 1.00 33.93  ? 2604 THR A OG1   1 
ATOM   9960  C CG2   . THR A 1 2604 ? 129.005 183.018 173.572 1.00 33.93  ? 2604 THR A CG2   1 
ATOM   9961  N N     . LEU A 1 2605 ? 131.142 183.719 170.535 1.00 32.71  ? 2605 LEU A N     1 
ATOM   9962  C CA    . LEU A 1 2605 ? 131.956 184.898 170.269 1.00 32.71  ? 2605 LEU A CA    1 
ATOM   9963  C C     . LEU A 1 2605 ? 131.436 185.664 169.058 1.00 32.71  ? 2605 LEU A C     1 
ATOM   9964  O O     . LEU A 1 2605 ? 131.355 186.897 169.081 1.00 32.71  ? 2605 LEU A O     1 
ATOM   9965  C CB    . LEU A 1 2605 ? 133.410 184.463 170.098 1.00 32.71  ? 2605 LEU A CB    1 
ATOM   9966  C CG    . LEU A 1 2605 ? 134.548 185.463 169.966 1.00 32.71  ? 2605 LEU A CG    1 
ATOM   9967  C CD1   . LEU A 1 2605 ? 134.404 186.532 170.982 1.00 32.71  ? 2605 LEU A CD1   1 
ATOM   9968  C CD2   . LEU A 1 2605 ? 135.819 184.704 170.270 1.00 32.71  ? 2605 LEU A CD2   1 
ATOM   9969  N N     . PHE A 1 2606 ? 131.057 184.946 167.995 1.00 35.34  ? 2606 PHE A N     1 
ATOM   9970  C CA    . PHE A 1 2606 ? 130.372 185.590 166.874 1.00 35.34  ? 2606 PHE A CA    1 
ATOM   9971  C C     . PHE A 1 2606 ? 129.123 186.330 167.329 1.00 35.34  ? 2606 PHE A C     1 
ATOM   9972  O O     . PHE A 1 2606 ? 128.898 187.479 166.933 1.00 35.34  ? 2606 PHE A O     1 
ATOM   9973  C CB    . PHE A 1 2606 ? 130.001 184.571 165.797 1.00 35.34  ? 2606 PHE A CB    1 
ATOM   9974  C CG    . PHE A 1 2606 ? 131.170 184.001 165.063 1.00 35.34  ? 2606 PHE A CG    1 
ATOM   9975  C CD1   . PHE A 1 2606 ? 132.411 184.599 165.144 1.00 35.34  ? 2606 PHE A CD1   1 
ATOM   9976  C CD2   . PHE A 1 2606 ? 131.022 182.874 164.273 1.00 35.34  ? 2606 PHE A CD2   1 
ATOM   9977  C CE1   . PHE A 1 2606 ? 133.482 184.084 164.455 1.00 35.34  ? 2606 PHE A CE1   1 
ATOM   9978  C CE2   . PHE A 1 2606 ? 132.095 182.350 163.584 1.00 35.34  ? 2606 PHE A CE2   1 
ATOM   9979  C CZ    . PHE A 1 2606 ? 133.327 182.955 163.676 1.00 35.34  ? 2606 PHE A CZ    1 
ATOM   9980  N N     . SER A 1 2607 ? 128.288 185.679 168.140 1.00 35.77  ? 2607 SER A N     1 
ATOM   9981  C CA    . SER A 1 2607 ? 127.039 186.307 168.561 1.00 35.77  ? 2607 SER A CA    1 
ATOM   9982  C C     . SER A 1 2607 ? 127.299 187.574 169.362 1.00 35.77  ? 2607 SER A C     1 
ATOM   9983  O O     . SER A 1 2607 ? 126.694 188.621 169.098 1.00 35.77  ? 2607 SER A O     1 
ATOM   9984  C CB    . SER A 1 2607 ? 126.209 185.326 169.383 1.00 35.77  ? 2607 SER A CB    1 
ATOM   9985  O OG    . SER A 1 2607 ? 126.817 185.075 170.638 1.00 35.77  ? 2607 SER A OG    1 
ATOM   9986  N N     . ALA A 1 2608 ? 128.205 187.502 170.338 1.00 34.34  ? 2608 ALA A N     1 
ATOM   9987  C CA    . ALA A 1 2608 ? 128.491 188.668 171.165 1.00 34.34  ? 2608 ALA A CA    1 
ATOM   9988  C C     . ALA A 1 2608 ? 129.103 189.794 170.342 1.00 34.34  ? 2608 ALA A C     1 
ATOM   9989  O O     . ALA A 1 2608 ? 128.757 190.966 170.532 1.00 34.34  ? 2608 ALA A O     1 
ATOM   9990  C CB    . ALA A 1 2608 ? 129.413 188.281 172.320 1.00 34.34  ? 2608 ALA A CB    1 
ATOM   9991  N N     . LEU A 1 2609 ? 130.013 189.463 169.422 1.00 36.67  ? 2609 LEU A N     1 
ATOM   9992  C CA    . LEU A 1 2609 ? 130.659 190.493 168.618 1.00 36.67  ? 2609 LEU A CA    1 
ATOM   9993  C C     . LEU A 1 2609 ? 129.675 191.156 167.661 1.00 36.67  ? 2609 LEU A C     1 
ATOM   9994  O O     . LEU A 1 2609 ? 129.706 192.379 167.484 1.00 36.67  ? 2609 LEU A O     1 
ATOM   9995  C CB    . LEU A 1 2609 ? 131.833 189.887 167.853 1.00 36.67  ? 2609 LEU A CB    1 
ATOM   9996  C CG    . LEU A 1 2609 ? 133.103 189.645 168.666 1.00 36.67  ? 2609 LEU A CG    1 
ATOM   9997  C CD1   . LEU A 1 2609 ? 134.109 188.850 167.855 1.00 36.67  ? 2609 LEU A CD1   1 
ATOM   9998  C CD2   . LEU A 1 2609 ? 133.700 190.964 169.116 1.00 36.67  ? 2609 LEU A CD2   1 
ATOM   9999  N N     . ARG A 1 2610 ? 128.796 190.371 167.033 1.00 42.33  ? 2610 ARG A N     1 
ATOM   10000 C CA    . ARG A 1 2610 ? 127.829 190.930 166.098 1.00 42.33  ? 2610 ARG A CA    1 
ATOM   10001 C C     . ARG A 1 2610 ? 126.661 191.611 166.797 1.00 42.33  ? 2610 ARG A C     1 
ATOM   10002 O O     . ARG A 1 2610 ? 125.931 192.371 166.152 1.00 42.33  ? 2610 ARG A O     1 
ATOM   10003 C CB    . ARG A 1 2610 ? 127.301 189.837 165.166 1.00 42.33  ? 2610 ARG A CB    1 
ATOM   10004 C CG    . ARG A 1 2610 ? 128.336 189.285 164.198 1.00 42.33  ? 2610 ARG A CG    1 
ATOM   10005 C CD    . ARG A 1 2610 ? 127.679 188.468 163.097 1.00 42.33  ? 2610 ARG A CD    1 
ATOM   10006 N NE    . ARG A 1 2610 ? 128.655 187.930 162.156 1.00 42.33  ? 2610 ARG A NE    1 
ATOM   10007 C CZ    . ARG A 1 2610 ? 128.802 186.640 161.886 1.00 42.33  ? 2610 ARG A CZ    1 
ATOM   10008 N NH1   . ARG A 1 2610 ? 128.048 185.722 162.468 1.00 42.33  ? 2610 ARG A NH1   1 
ATOM   10009 N NH2   . ARG A 1 2610 ? 129.728 186.262 161.010 1.00 42.33  ? 2610 ARG A NH2   1 
ATOM   10010 N N     . ALA A 1 2611 ? 126.463 191.351 168.093 1.00 41.92  ? 2611 ALA A N     1 
ATOM   10011 C CA    . ALA A 1 2611 ? 125.397 192.027 168.824 1.00 41.92  ? 2611 ALA A CA    1 
ATOM   10012 C C     . ALA A 1 2611 ? 125.632 193.532 168.880 1.00 41.92  ? 2611 ALA A C     1 
ATOM   10013 O O     . ALA A 1 2611 ? 124.686 194.320 168.763 1.00 41.92  ? 2611 ALA A O     1 
ATOM   10014 C CB    . ALA A 1 2611 ? 125.278 191.448 170.233 1.00 41.92  ? 2611 ALA A CB    1 
ATOM   10015 N N     . LEU A 1 2612 ? 126.881 193.947 169.067 1.00 42.95  ? 2612 LEU A N     1 
ATOM   10016 C CA    . LEU A 1 2612 ? 127.195 195.367 169.112 1.00 42.95  ? 2612 LEU A CA    1 
ATOM   10017 C C     . LEU A 1 2612 ? 126.977 196.001 167.739 1.00 42.95  ? 2612 LEU A C     1 
ATOM   10018 O O     . LEU A 1 2612 ? 127.298 195.392 166.714 1.00 42.95  ? 2612 LEU A O     1 
ATOM   10019 C CB    . LEU A 1 2612 ? 128.635 195.580 169.572 1.00 42.95  ? 2612 LEU A CB    1 
ATOM   10020 C CG    . LEU A 1 2612 ? 128.889 195.152 171.017 1.00 42.95  ? 2612 LEU A CG    1 
ATOM   10021 C CD1   . LEU A 1 2612 ? 130.359 195.261 171.375 1.00 42.95  ? 2612 LEU A CD1   1 
ATOM   10022 C CD2   . LEU A 1 2612 ? 128.040 195.979 171.969 1.00 42.95  ? 2612 LEU A CD2   1 
ATOM   10023 N N     . PRO A 1 2613 ? 126.437 197.219 167.686 1.00 49.30  ? 2613 PRO A N     1 
ATOM   10024 C CA    . PRO A 1 2613 ? 126.087 197.816 166.391 1.00 49.30  ? 2613 PRO A CA    1 
ATOM   10025 C C     . PRO A 1 2613 ? 127.254 198.502 165.697 1.00 49.30  ? 2613 PRO A C     1 
ATOM   10026 O O     . PRO A 1 2613 ? 127.268 198.618 164.468 1.00 49.30  ? 2613 PRO A O     1 
ATOM   10027 C CB    . PRO A 1 2613 ? 124.995 198.823 166.766 1.00 49.30  ? 2613 PRO A CB    1 
ATOM   10028 C CG    . PRO A 1 2613 ? 125.357 199.247 168.156 1.00 49.30  ? 2613 PRO A CG    1 
ATOM   10029 C CD    . PRO A 1 2613 ? 126.039 198.072 168.820 1.00 49.30  ? 2613 PRO A CD    1 
ATOM   10030 N N     . ASP A 1 2614 ? 128.236 198.962 166.469 1.00 50.33  ? 2614 ASP A N     1 
ATOM   10031 C CA    . ASP A 1 2614 ? 129.355 199.725 165.935 1.00 50.33  ? 2614 ASP A CA    1 
ATOM   10032 C C     . ASP A 1 2614 ? 130.592 198.871 165.693 1.00 50.33  ? 2614 ASP A C     1 
ATOM   10033 O O     . ASP A 1 2614 ? 131.665 199.418 165.423 1.00 50.33  ? 2614 ASP A O     1 
ATOM   10034 C CB    . ASP A 1 2614 ? 129.702 200.880 166.875 1.00 50.33  ? 2614 ASP A CB    1 
ATOM   10035 C CG    . ASP A 1 2614 ? 129.883 200.427 168.310 1.00 50.33  ? 2614 ASP A CG    1 
ATOM   10036 O OD1   . ASP A 1 2614 ? 129.614 199.243 168.599 1.00 50.33  ? 2614 ASP A OD1   1 
ATOM   10037 O OD2   . ASP A 1 2614 ? 130.297 201.255 169.148 1.00 50.33  ? 2614 ASP A OD2   1 
ATOM   10038 N N     . MET A 1 2615 ? 130.470 197.551 165.782 1.00 43.55  ? 2615 MET A N     1 
ATOM   10039 C CA    . MET A 1 2615 ? 131.603 196.646 165.649 1.00 43.55  ? 2615 MET A CA    1 
ATOM   10040 C C     . MET A 1 2615 ? 131.457 195.805 164.389 1.00 43.55  ? 2615 MET A C     1 
ATOM   10041 O O     . MET A 1 2615 ? 130.420 195.168 164.177 1.00 43.55  ? 2615 MET A O     1 
ATOM   10042 C CB    . MET A 1 2615 ? 131.723 195.747 166.880 1.00 43.55  ? 2615 MET A CB    1 
ATOM   10043 C CG    . MET A 1 2615 ? 133.145 195.348 167.209 1.00 43.55  ? 2615 MET A CG    1 
ATOM   10044 S SD    . MET A 1 2615 ? 133.366 194.937 168.948 1.00 43.55  ? 2615 MET A SD    1 
ATOM   10045 C CE    . MET A 1 2615 ? 133.261 196.567 169.681 1.00 43.55  ? 2615 MET A CE    1 
ATOM   10046 N N     . GLU A 1 2616 ? 132.498 195.805 163.562 1.00 42.90  ? 2616 GLU A N     1 
ATOM   10047 C CA    . GLU A 1 2616 ? 132.560 195.002 162.346 1.00 42.90  ? 2616 GLU A CA    1 
ATOM   10048 C C     . GLU A 1 2616 ? 133.448 193.798 162.632 1.00 42.90  ? 2616 GLU A C     1 
ATOM   10049 O O     . GLU A 1 2616 ? 134.578 193.954 163.105 1.00 42.90  ? 2616 GLU A O     1 
ATOM   10050 C CB    . GLU A 1 2616 ? 133.097 195.820 161.175 1.00 42.90  ? 2616 GLU A CB    1 
ATOM   10051 C CG    . GLU A 1 2616 ? 133.401 194.999 159.935 1.00 42.90  ? 2616 GLU A CG    1 
ATOM   10052 C CD    . GLU A 1 2616 ? 133.709 195.861 158.729 1.00 42.90  ? 2616 GLU A CD    1 
ATOM   10053 O OE1   . GLU A 1 2616 ? 134.641 196.688 158.812 1.00 42.90  ? 2616 GLU A OE1   1 
ATOM   10054 O OE2   . GLU A 1 2616 ? 133.022 195.711 157.697 1.00 42.90  ? 2616 GLU A OE2   1 
ATOM   10055 N N     . VAL A 1 2617 ? 132.940 192.603 162.345 1.00 34.32  ? 2617 VAL A N     1 
ATOM   10056 C CA    . VAL A 1 2617 ? 133.605 191.358 162.709 1.00 34.32  ? 2617 VAL A CA    1 
ATOM   10057 C C     . VAL A 1 2617 ? 134.154 190.701 161.452 1.00 34.32  ? 2617 VAL A C     1 
ATOM   10058 O O     . VAL A 1 2617 ? 133.435 190.545 160.458 1.00 34.32  ? 2617 VAL A O     1 
ATOM   10059 C CB    . VAL A 1 2617 ? 132.641 190.412 163.443 1.00 34.32  ? 2617 VAL A CB    1 
ATOM   10060 C CG1   . VAL A 1 2617 ? 133.388 189.194 163.962 1.00 34.32  ? 2617 VAL A CG1   1 
ATOM   10061 C CG2   . VAL A 1 2617 ? 131.940 191.148 164.566 1.00 34.32  ? 2617 VAL A CG2   1 
ATOM   10062 N N     . VAL A 1 2618 ? 135.426 190.318 161.496 1.00 33.30  ? 2618 VAL A N     1 
ATOM   10063 C CA    . VAL A 1 2618 ? 136.076 189.582 160.419 1.00 33.30  ? 2618 VAL A CA    1 
ATOM   10064 C C     . VAL A 1 2618 ? 136.633 188.294 161.005 1.00 33.30  ? 2618 VAL A C     1 
ATOM   10065 O O     . VAL A 1 2618 ? 137.448 188.332 161.935 1.00 33.30  ? 2618 VAL A O     1 
ATOM   10066 C CB    . VAL A 1 2618 ? 137.188 190.404 159.751 1.00 33.30  ? 2618 VAL A CB    1 
ATOM   10067 C CG1   . VAL A 1 2618 ? 137.927 189.557 158.729 1.00 33.30  ? 2618 VAL A CG1   1 
ATOM   10068 C CG2   . VAL A 1 2618 ? 136.605 191.641 159.099 1.00 33.30  ? 2618 VAL A CG2   1 
ATOM   10069 N N     . GLY A 1 2619 ? 136.199 187.161 160.464 1.00 33.82  ? 2619 GLY A N     1 
ATOM   10070 C CA    . GLY A 1 2619 ? 136.652 185.876 160.956 1.00 33.82  ? 2619 GLY A CA    1 
ATOM   10071 C C     . GLY A 1 2619 ? 137.842 185.334 160.195 1.00 33.82  ? 2619 GLY A C     1 
ATOM   10072 O O     . GLY A 1 2619 ? 137.770 185.129 158.980 1.00 33.82  ? 2619 GLY A O     1 
ATOM   10073 N N     . LEU A 1 2620 ? 138.947 185.101 160.899 1.00 35.14  ? 2620 LEU A N     1 
ATOM   10074 C CA    . LEU A 1 2620 ? 140.153 184.529 160.313 1.00 35.14  ? 2620 LEU A CA    1 
ATOM   10075 C C     . LEU A 1 2620 ? 140.432 183.193 160.981 1.00 35.14  ? 2620 LEU A C     1 
ATOM   10076 O O     . LEU A 1 2620 ? 140.581 183.127 162.206 1.00 35.14  ? 2620 LEU A O     1 
ATOM   10077 C CB    . LEU A 1 2620 ? 141.349 185.469 160.476 1.00 35.14  ? 2620 LEU A CB    1 
ATOM   10078 C CG    . LEU A 1 2620 ? 141.205 186.874 159.895 1.00 35.14  ? 2620 LEU A CG    1 
ATOM   10079 C CD1   . LEU A 1 2620 ? 142.484 187.665 160.100 1.00 35.14  ? 2620 LEU A CD1   1 
ATOM   10080 C CD2   . LEU A 1 2620 ? 140.848 186.804 158.421 1.00 35.14  ? 2620 LEU A CD2   1 
ATOM   10081 N N     . ASN A 1 2621 ? 140.506 182.136 160.180 1.00 40.63  ? 2621 ASN A N     1 
ATOM   10082 C CA    . ASN A 1 2621 ? 140.837 180.809 160.678 1.00 40.63  ? 2621 ASN A CA    1 
ATOM   10083 C C     . ASN A 1 2621 ? 142.344 180.613 160.587 1.00 40.63  ? 2621 ASN A C     1 
ATOM   10084 O O     . ASN A 1 2621 ? 142.893 180.484 159.487 1.00 40.63  ? 2621 ASN A O     1 
ATOM   10085 C CB    . ASN A 1 2621 ? 140.102 179.731 159.883 1.00 40.63  ? 2621 ASN A CB    1 
ATOM   10086 C CG    . ASN A 1 2621 ? 138.611 179.728 160.149 1.00 40.63  ? 2621 ASN A CG    1 
ATOM   10087 O OD1   . ASN A 1 2621 ? 137.806 179.580 159.231 1.00 40.63  ? 2621 ASN A OD1   1 
ATOM   10088 N ND2   . ASN A 1 2621 ? 138.235 179.891 161.412 1.00 40.63  ? 2621 ASN A ND2   1 
ATOM   10089 N N     . PHE A 1 2622 ? 143.010 180.593 161.737 1.00 36.89  ? 2622 PHE A N     1 
ATOM   10090 C CA    . PHE A 1 2622 ? 144.459 180.436 161.791 1.00 36.89  ? 2622 PHE A CA    1 
ATOM   10091 C C     . PHE A 1 2622 ? 144.793 178.967 161.571 1.00 36.89  ? 2622 PHE A C     1 
ATOM   10092 O O     . PHE A 1 2622 ? 144.462 178.117 162.402 1.00 36.89  ? 2622 PHE A O     1 
ATOM   10093 C CB    . PHE A 1 2622 ? 145.010 180.934 163.124 1.00 36.89  ? 2622 PHE A CB    1 
ATOM   10094 C CG    . PHE A 1 2622 ? 145.315 182.403 163.142 1.00 36.89  ? 2622 PHE A CG    1 
ATOM   10095 C CD1   . PHE A 1 2622 ? 144.920 183.218 162.096 1.00 36.89  ? 2622 PHE A CD1   1 
ATOM   10096 C CD2   . PHE A 1 2622 ? 145.997 182.968 164.204 1.00 36.89  ? 2622 PHE A CD2   1 
ATOM   10097 C CE1   . PHE A 1 2622 ? 145.198 184.569 162.110 1.00 36.89  ? 2622 PHE A CE1   1 
ATOM   10098 C CE2   . PHE A 1 2622 ? 146.278 184.319 164.223 1.00 36.89  ? 2622 PHE A CE2   1 
ATOM   10099 C CZ    . PHE A 1 2622 ? 145.877 185.120 163.175 1.00 36.89  ? 2622 PHE A CZ    1 
ATOM   10100 N N     . SER A 1 2623 ? 145.441 178.670 160.449 1.00 35.92  ? 2623 SER A N     1 
ATOM   10101 C CA    . SER A 1 2623 ? 145.821 177.308 160.116 1.00 35.92  ? 2623 SER A CA    1 
ATOM   10102 C C     . SER A 1 2623 ? 147.216 177.010 160.660 1.00 35.92  ? 2623 SER A C     1 
ATOM   10103 O O     . SER A 1 2623 ? 147.862 177.851 161.289 1.00 35.92  ? 2623 SER A O     1 
ATOM   10104 C CB    . SER A 1 2623 ? 145.756 177.092 158.605 1.00 35.92  ? 2623 SER A CB    1 
ATOM   10105 O OG    . SER A 1 2623 ? 146.157 175.779 158.258 1.00 35.92  ? 2623 SER A OG    1 
ATOM   10106 N N     . SER A 1 2624 ? 147.692 175.789 160.412 1.00 33.98  ? 2624 SER A N     1 
ATOM   10107 C CA    . SER A 1 2624 ? 149.016 175.396 160.873 1.00 33.98  ? 2624 SER A CA    1 
ATOM   10108 C C     . SER A 1 2624 ? 150.136 176.057 160.083 1.00 33.98  ? 2624 SER A C     1 
ATOM   10109 O O     . SER A 1 2624 ? 151.298 175.949 160.485 1.00 33.98  ? 2624 SER A O     1 
ATOM   10110 C CB    . SER A 1 2624 ? 149.167 173.876 160.805 1.00 33.98  ? 2624 SER A CB    1 
ATOM   10111 O OG    . SER A 1 2624 ? 150.529 173.498 160.898 1.00 33.98  ? 2624 SER A OG    1 
ATOM   10112 N N     . ALA A 1 2625 ? 149.822 176.728 158.976 1.00 34.76  ? 2625 ALA A N     1 
ATOM   10113 C CA    . ALA A 1 2625 ? 150.811 177.442 158.179 1.00 34.76  ? 2625 ALA A CA    1 
ATOM   10114 C C     . ALA A 1 2625 ? 150.497 178.933 158.119 1.00 34.76  ? 2625 ALA A C     1 
ATOM   10115 O O     . ALA A 1 2625 ? 150.851 179.612 157.154 1.00 34.76  ? 2625 ALA A O     1 
ATOM   10116 C CB    . ALA A 1 2625 ? 150.899 176.855 156.771 1.00 34.76  ? 2625 ALA A CB    1 
ATOM   10117 N N     . THR A 1 2626 ? 149.827 179.448 159.146 1.00 38.33  ? 2626 THR A N     1 
ATOM   10118 C CA    . THR A 1 2626 ? 149.429 180.848 159.155 1.00 38.33  ? 2626 THR A CA    1 
ATOM   10119 C C     . THR A 1 2626 ? 150.646 181.752 159.307 1.00 38.33  ? 2626 THR A C     1 
ATOM   10120 O O     . THR A 1 2626 ? 151.539 181.493 160.118 1.00 38.33  ? 2626 THR A O     1 
ATOM   10121 C CB    . THR A 1 2626 ? 148.434 181.107 160.286 1.00 38.33  ? 2626 THR A CB    1 
ATOM   10122 O OG1   . THR A 1 2626 ? 147.276 180.285 160.097 1.00 38.33  ? 2626 THR A OG1   1 
ATOM   10123 C CG2   . THR A 1 2626 ? 148.007 182.566 160.301 1.00 38.33  ? 2626 THR A CG2   1 
ATOM   10124 N N     . THR A 1 2627 ? 150.674 182.815 158.518 1.00 41.92  ? 2627 THR A N     1 
ATOM   10125 C CA    . THR A 1 2627 ? 151.758 183.781 158.477 1.00 41.92  ? 2627 THR A CA    1 
ATOM   10126 C C     . THR A 1 2627 ? 151.171 185.182 158.529 1.00 41.92  ? 2627 THR A C     1 
ATOM   10127 O O     . THR A 1 2627 ? 150.010 185.390 158.161 1.00 41.92  ? 2627 THR A O     1 
ATOM   10128 C CB    . THR A 1 2627 ? 152.601 183.598 157.204 1.00 41.92  ? 2627 THR A CB    1 
ATOM   10129 O OG1   . THR A 1 2627 ? 153.726 184.485 157.222 1.00 41.92  ? 2627 THR A OG1   1 
ATOM   10130 C CG2   . THR A 1 2627 ? 151.765 183.859 155.961 1.00 41.92  ? 2627 THR A CG2   1 
ATOM   10131 N N     . PRO A 1 2628 ? 151.940 186.166 159.006 1.00 40.66  ? 2628 PRO A N     1 
ATOM   10132 C CA    . PRO A 1 2628 ? 151.433 187.549 159.030 1.00 40.66  ? 2628 PRO A CA    1 
ATOM   10133 C C     . PRO A 1 2628 ? 151.004 188.081 157.674 1.00 40.66  ? 2628 PRO A C     1 
ATOM   10134 O O     . PRO A 1 2628 ? 150.334 189.121 157.621 1.00 40.66  ? 2628 PRO A O     1 
ATOM   10135 C CB    . PRO A 1 2628 ? 152.620 188.341 159.590 1.00 40.66  ? 2628 PRO A CB    1 
ATOM   10136 C CG    . PRO A 1 2628 ? 153.321 187.369 160.458 1.00 40.66  ? 2628 PRO A CG    1 
ATOM   10137 C CD    . PRO A 1 2628 ? 153.175 186.025 159.796 1.00 40.66  ? 2628 PRO A CD    1 
ATOM   10138 N N     . GLU A 1 2629 ? 151.377 187.418 156.577 1.00 48.47  ? 2629 GLU A N     1 
ATOM   10139 C CA    . GLU A 1 2629 ? 150.861 187.818 155.273 1.00 48.47  ? 2629 GLU A CA    1 
ATOM   10140 C C     . GLU A 1 2629 ? 149.342 187.726 155.227 1.00 48.47  ? 2629 GLU A C     1 
ATOM   10141 O O     . GLU A 1 2629 ? 148.696 188.517 154.535 1.00 48.47  ? 2629 GLU A O     1 
ATOM   10142 C CB    . GLU A 1 2629 ? 151.482 186.960 154.172 1.00 48.47  ? 2629 GLU A CB    1 
ATOM   10143 C CG    . GLU A 1 2629 ? 152.972 187.180 153.981 1.00 48.47  ? 2629 GLU A CG    1 
ATOM   10144 C CD    . GLU A 1 2629 ? 153.560 186.276 152.918 1.00 48.47  ? 2629 GLU A CD    1 
ATOM   10145 O OE1   . GLU A 1 2629 ? 152.835 185.385 152.427 1.00 48.47  ? 2629 GLU A OE1   1 
ATOM   10146 O OE2   . GLU A 1 2629 ? 154.747 186.454 152.574 1.00 48.47  ? 2629 GLU A OE2   1 
ATOM   10147 N N     . LEU A 1 2630 ? 148.754 186.774 155.957 1.00 46.03  ? 2630 LEU A N     1 
ATOM   10148 C CA    . LEU A 1 2630 ? 147.299 186.705 156.049 1.00 46.03  ? 2630 LEU A CA    1 
ATOM   10149 C C     . LEU A 1 2630 ? 146.728 187.956 156.704 1.00 46.03  ? 2630 LEU A C     1 
ATOM   10150 O O     . LEU A 1 2630 ? 145.732 188.519 156.230 1.00 46.03  ? 2630 LEU A O     1 
ATOM   10151 C CB    . LEU A 1 2630 ? 146.884 185.456 156.825 1.00 46.03  ? 2630 LEU A CB    1 
ATOM   10152 C CG    . LEU A 1 2630 ? 145.455 185.436 157.370 1.00 46.03  ? 2630 LEU A CG    1 
ATOM   10153 C CD1   . LEU A 1 2630 ? 144.450 185.289 156.239 1.00 46.03  ? 2630 LEU A CD1   1 
ATOM   10154 C CD2   . LEU A 1 2630 ? 145.288 184.324 158.391 1.00 46.03  ? 2630 LEU A CD2   1 
ATOM   10155 N N     . LEU A 1 2631 ? 147.347 188.410 157.796 1.00 43.82  ? 2631 LEU A N     1 
ATOM   10156 C CA    . LEU A 1 2631 ? 146.896 189.636 158.444 1.00 43.82  ? 2631 LEU A CA    1 
ATOM   10157 C C     . LEU A 1 2631 ? 147.060 190.836 157.522 1.00 43.82  ? 2631 LEU A C     1 
ATOM   10158 O O     . LEU A 1 2631 ? 146.193 191.715 157.475 1.00 43.82  ? 2631 LEU A O     1 
ATOM   10159 C CB    . LEU A 1 2631 ? 147.661 189.854 159.749 1.00 43.82  ? 2631 LEU A CB    1 
ATOM   10160 C CG    . LEU A 1 2631 ? 147.182 189.057 160.961 1.00 43.82  ? 2631 LEU A CG    1 
ATOM   10161 C CD1   . LEU A 1 2631 ? 148.307 188.888 161.965 1.00 43.82  ? 2631 LEU A CD1   1 
ATOM   10162 C CD2   . LEU A 1 2631 ? 145.986 189.734 161.604 1.00 43.82  ? 2631 LEU A CD2   1 
ATOM   10163 N N     . LEU A 1 2632 ? 148.172 190.893 156.786 1.00 47.31  ? 2632 LEU A N     1 
ATOM   10164 C CA    . LEU A 1 2632 ? 148.382 191.996 155.853 1.00 47.31  ? 2632 LEU A CA    1 
ATOM   10165 C C     . LEU A 1 2632 ? 147.333 191.990 154.746 1.00 47.31  ? 2632 LEU A C     1 
ATOM   10166 O O     . LEU A 1 2632 ? 146.828 193.048 154.354 1.00 47.31  ? 2632 LEU A O     1 
ATOM   10167 C CB    . LEU A 1 2632 ? 149.790 191.923 155.265 1.00 47.31  ? 2632 LEU A CB    1 
ATOM   10168 C CG    . LEU A 1 2632 ? 150.929 192.143 156.262 1.00 47.31  ? 2632 LEU A CG    1 
ATOM   10169 C CD1   . LEU A 1 2632 ? 152.279 191.912 155.601 1.00 47.31  ? 2632 LEU A CD1   1 
ATOM   10170 C CD2   . LEU A 1 2632 ? 150.853 193.535 156.864 1.00 47.31  ? 2632 LEU A CD2   1 
ATOM   10171 N N     . LYS A 1 2633 ? 146.996 190.806 154.231 1.00 47.34  ? 2633 LYS A N     1 
ATOM   10172 C CA    . LYS A 1 2633 ? 145.949 190.703 153.220 1.00 47.34  ? 2633 LYS A CA    1 
ATOM   10173 C C     . LYS A 1 2633 ? 144.604 191.147 153.777 1.00 47.34  ? 2633 LYS A C     1 
ATOM   10174 O O     . LYS A 1 2633 ? 143.833 191.827 153.090 1.00 47.34  ? 2633 LYS A O     1 
ATOM   10175 C CB    . LYS A 1 2633 ? 145.861 189.269 152.700 1.00 47.34  ? 2633 LYS A CB    1 
ATOM   10176 C CG    . LYS A 1 2633 ? 146.981 188.873 151.754 1.00 47.34  ? 2633 LYS A CG    1 
ATOM   10177 C CD    . LYS A 1 2633 ? 147.262 187.379 151.827 1.00 47.34  ? 2633 LYS A CD    1 
ATOM   10178 C CE    . LYS A 1 2633 ? 145.974 186.570 151.841 1.00 47.34  ? 2633 LYS A CE    1 
ATOM   10179 N NZ    . LYS A 1 2633 ? 146.229 185.121 152.070 1.00 47.34  ? 2633 LYS A NZ    1 
ATOM   10180 N N     . THR A 1 2634 ? 144.299 190.761 155.018 1.00 42.19  ? 2634 THR A N     1 
ATOM   10181 C CA    . THR A 1 2634 ? 143.047 191.188 155.635 1.00 42.19  ? 2634 THR A CA    1 
ATOM   10182 C C     . THR A 1 2634 ? 143.003 192.702 155.802 1.00 42.19  ? 2634 THR A C     1 
ATOM   10183 O O     . THR A 1 2634 ? 141.967 193.332 155.558 1.00 42.19  ? 2634 THR A O     1 
ATOM   10184 C CB    . THR A 1 2634 ? 142.862 190.494 156.983 1.00 42.19  ? 2634 THR A CB    1 
ATOM   10185 O OG1   . THR A 1 2634 ? 142.973 189.076 156.810 1.00 42.19  ? 2634 THR A OG1   1 
ATOM   10186 C CG2   . THR A 1 2634 ? 141.496 190.819 157.562 1.00 42.19  ? 2634 THR A CG2   1 
ATOM   10187 N N     . PHE A 1 2635 ? 144.121 193.303 156.217 1.00 45.72  ? 2635 PHE A N     1 
ATOM   10188 C CA    . PHE A 1 2635 ? 144.178 194.756 156.344 1.00 45.72  ? 2635 PHE A CA    1 
ATOM   10189 C C     . PHE A 1 2635 ? 144.001 195.434 154.993 1.00 45.72  ? 2635 PHE A C     1 
ATOM   10190 O O     . PHE A 1 2635 ? 143.313 196.456 154.887 1.00 45.72  ? 2635 PHE A O     1 
ATOM   10191 C CB    . PHE A 1 2635 ? 145.499 195.180 156.985 1.00 45.72  ? 2635 PHE A CB    1 
ATOM   10192 C CG    . PHE A 1 2635 ? 145.606 194.829 158.438 1.00 45.72  ? 2635 PHE A CG    1 
ATOM   10193 C CD1   . PHE A 1 2635 ? 144.525 194.999 159.283 1.00 45.72  ? 2635 PHE A CD1   1 
ATOM   10194 C CD2   . PHE A 1 2635 ? 146.787 194.335 158.961 1.00 45.72  ? 2635 PHE A CD2   1 
ATOM   10195 C CE1   . PHE A 1 2635 ? 144.618 194.680 160.621 1.00 45.72  ? 2635 PHE A CE1   1 
ATOM   10196 C CE2   . PHE A 1 2635 ? 146.885 194.012 160.298 1.00 45.72  ? 2635 PHE A CE2   1 
ATOM   10197 C CZ    . PHE A 1 2635 ? 145.799 194.185 161.128 1.00 45.72  ? 2635 PHE A CZ    1 
ATOM   10198 N N     . ASP A 1 2636 ? 144.622 194.886 153.948 1.00 51.32  ? 2636 ASP A N     1 
ATOM   10199 C CA    . ASP A 1 2636 ? 144.453 195.444 152.611 1.00 51.32  ? 2636 ASP A CA    1 
ATOM   10200 C C     . ASP A 1 2636 ? 143.002 195.347 152.154 1.00 51.32  ? 2636 ASP A C     1 
ATOM   10201 O O     . ASP A 1 2636 ? 142.470 196.299 151.573 1.00 51.32  ? 2636 ASP A O     1 
ATOM   10202 C CB    . ASP A 1 2636 ? 145.388 194.721 151.635 1.00 51.32  ? 2636 ASP A CB    1 
ATOM   10203 C CG    . ASP A 1 2636 ? 145.476 195.399 150.273 1.00 51.32  ? 2636 ASP A CG    1 
ATOM   10204 O OD1   . ASP A 1 2636 ? 146.589 195.428 149.707 1.00 51.32  ? 2636 ASP A OD1   1 
ATOM   10205 O OD2   . ASP A 1 2636 ? 144.452 195.888 149.754 1.00 51.32  ? 2636 ASP A OD2   1 
ATOM   10206 N N     . HIS A 1 2637 ? 142.345 194.218 152.426 1.00 53.01  ? 2637 HIS A N     1 
ATOM   10207 C CA    . HIS A 1 2637 ? 140.978 194.020 151.954 1.00 53.01  ? 2637 HIS A CA    1 
ATOM   10208 C C     . HIS A 1 2637 ? 139.983 194.885 152.721 1.00 53.01  ? 2637 HIS A C     1 
ATOM   10209 O O     . HIS A 1 2637 ? 139.033 195.412 152.132 1.00 53.01  ? 2637 HIS A O     1 
ATOM   10210 C CB    . HIS A 1 2637 ? 140.598 192.544 152.062 1.00 53.01  ? 2637 HIS A CB    1 
ATOM   10211 C CG    . HIS A 1 2637 ? 139.226 192.235 151.551 1.00 53.01  ? 2637 HIS A CG    1 
ATOM   10212 N ND1   . HIS A 1 2637 ? 138.171 191.937 152.386 1.00 53.01  ? 2637 HIS A ND1   1 
ATOM   10213 C CD2   . HIS A 1 2637 ? 138.735 192.180 150.290 1.00 53.01  ? 2637 HIS A CD2   1 
ATOM   10214 C CE1   . HIS A 1 2637 ? 137.089 191.710 151.662 1.00 53.01  ? 2637 HIS A CE1   1 
ATOM   10215 N NE2   . HIS A 1 2637 ? 137.405 191.852 150.387 1.00 53.01  ? 2637 HIS A NE2   1 
ATOM   10216 N N     . TYR A 1 2638 ? 140.178 195.045 154.030 1.00 48.74  ? 2638 TYR A N     1 
ATOM   10217 C CA    . TYR A 1 2638 ? 139.202 195.730 154.869 1.00 48.74  ? 2638 TYR A CA    1 
ATOM   10218 C C     . TYR A 1 2638 ? 139.596 197.142 155.273 1.00 48.74  ? 2638 TYR A C     1 
ATOM   10219 O O     . TYR A 1 2638 ? 138.711 197.954 155.548 1.00 48.74  ? 2638 TYR A O     1 
ATOM   10220 C CB    . TYR A 1 2638 ? 138.934 194.922 156.144 1.00 48.74  ? 2638 TYR A CB    1 
ATOM   10221 C CG    . TYR A 1 2638 ? 138.056 193.710 155.940 1.00 48.74  ? 2638 TYR A CG    1 
ATOM   10222 C CD1   . TYR A 1 2638 ? 136.673 193.824 155.938 1.00 48.74  ? 2638 TYR A CD1   1 
ATOM   10223 C CD2   . TYR A 1 2638 ? 138.610 192.450 155.761 1.00 48.74  ? 2638 TYR A CD2   1 
ATOM   10224 C CE1   . TYR A 1 2638 ? 135.866 192.718 155.756 1.00 48.74  ? 2638 TYR A CE1   1 
ATOM   10225 C CE2   . TYR A 1 2638 ? 137.811 191.338 155.579 1.00 48.74  ? 2638 TYR A CE2   1 
ATOM   10226 C CZ    . TYR A 1 2638 ? 136.440 191.478 155.577 1.00 48.74  ? 2638 TYR A CZ    1 
ATOM   10227 O OH    . TYR A 1 2638 ? 135.640 190.374 155.396 1.00 48.74  ? 2638 TYR A OH    1 
ATOM   10228 N N     . CYS A 1 2639 ? 140.886 197.460 155.319 1.00 52.24  ? 2639 CYS A N     1 
ATOM   10229 C CA    . CYS A 1 2639 ? 141.354 198.736 155.841 1.00 52.24  ? 2639 CYS A CA    1 
ATOM   10230 C C     . CYS A 1 2639 ? 142.099 199.515 154.763 1.00 52.24  ? 2639 CYS A C     1 
ATOM   10231 O O     . CYS A 1 2639 ? 142.387 199.008 153.677 1.00 52.24  ? 2639 CYS A O     1 
ATOM   10232 C CB    . CYS A 1 2639 ? 142.254 198.530 157.066 1.00 52.24  ? 2639 CYS A CB    1 
ATOM   10233 S SG    . CYS A 1 2639 ? 141.465 197.639 158.424 1.00 52.24  ? 2639 CYS A SG    1 
ATOM   10234 N N     . GLU A 1 2640 ? 142.408 200.771 155.086 1.00 57.77  ? 2640 GLU A N     1 
ATOM   10235 C CA    . GLU A 1 2640 ? 143.106 201.668 154.177 1.00 57.77  ? 2640 GLU A CA    1 
ATOM   10236 C C     . GLU A 1 2640 ? 144.203 202.404 154.932 1.00 57.77  ? 2640 GLU A C     1 
ATOM   10237 O O     . GLU A 1 2640 ? 144.131 202.574 156.152 1.00 57.77  ? 2640 GLU A O     1 
ATOM   10238 C CB    . GLU A 1 2640 ? 142.149 202.684 153.539 1.00 57.77  ? 2640 GLU A CB    1 
ATOM   10239 C CG    . GLU A 1 2640 ? 141.500 203.630 154.537 1.00 57.77  ? 2640 GLU A CG    1 
ATOM   10240 C CD    . GLU A 1 2640 ? 140.774 204.781 153.867 1.00 57.77  ? 2640 GLU A CD    1 
ATOM   10241 O OE1   . GLU A 1 2640 ? 141.421 205.530 153.104 1.00 57.77  ? 2640 GLU A OE1   1 
ATOM   10242 O OE2   . GLU A 1 2640 ? 139.558 204.937 154.103 1.00 57.77  ? 2640 GLU A OE2   1 
ATOM   10243 N N     . TYR A 1 2641 ? 145.217 202.843 154.193 1.00 54.80  ? 2641 TYR A N     1 
ATOM   10244 C CA    . TYR A 1 2641 ? 146.334 203.592 154.753 1.00 54.80  ? 2641 TYR A CA    1 
ATOM   10245 C C     . TYR A 1 2641 ? 146.114 205.080 154.517 1.00 54.80  ? 2641 TYR A C     1 
ATOM   10246 O O     . TYR A 1 2641 ? 145.814 205.497 153.394 1.00 54.80  ? 2641 TYR A O     1 
ATOM   10247 C CB    . TYR A 1 2641 ? 147.660 203.150 154.133 1.00 54.80  ? 2641 TYR A CB    1 
ATOM   10248 C CG    . TYR A 1 2641 ? 148.033 201.712 154.420 1.00 54.80  ? 2641 TYR A CG    1 
ATOM   10249 C CD1   . TYR A 1 2641 ? 147.433 200.667 153.730 1.00 54.80  ? 2641 TYR A CD1   1 
ATOM   10250 C CD2   . TYR A 1 2641 ? 148.985 201.401 155.379 1.00 54.80  ? 2641 TYR A CD2   1 
ATOM   10251 C CE1   . TYR A 1 2641 ? 147.772 199.353 153.988 1.00 54.80  ? 2641 TYR A CE1   1 
ATOM   10252 C CE2   . TYR A 1 2641 ? 149.329 200.090 155.644 1.00 54.80  ? 2641 TYR A CE2   1 
ATOM   10253 C CZ    . TYR A 1 2641 ? 148.720 199.071 154.946 1.00 54.80  ? 2641 TYR A CZ    1 
ATOM   10254 O OH    . TYR A 1 2641 ? 149.061 197.764 155.207 1.00 54.80  ? 2641 TYR A OH    1 
ATOM   10255 N N     . ARG A 1 2642 ? 146.265 205.875 155.574 1.00 57.75  ? 2642 ARG A N     1 
ATOM   10256 C CA    . ARG A 1 2642 ? 146.008 207.310 155.524 1.00 57.75  ? 2642 ARG A CA    1 
ATOM   10257 C C     . ARG A 1 2642 ? 147.227 208.051 156.050 1.00 57.75  ? 2642 ARG A C     1 
ATOM   10258 O O     . ARG A 1 2642 ? 147.754 207.707 157.113 1.00 57.75  ? 2642 ARG A O     1 
ATOM   10259 C CB    . ARG A 1 2642 ? 144.758 207.666 156.333 1.00 57.75  ? 2642 ARG A CB    1 
ATOM   10260 C CG    . ARG A 1 2642 ? 144.612 209.138 156.657 1.00 57.75  ? 2642 ARG A CG    1 
ATOM   10261 C CD    . ARG A 1 2642 ? 143.254 209.530 157.275 1.00 57.75  ? 2642 ARG A CD    1 
ATOM   10262 N NE    . ARG A 1 2642 ? 142.836 208.737 158.429 1.00 57.75  ? 2642 ARG A NE    1 
ATOM   10263 C CZ    . ARG A 1 2642 ? 142.246 207.549 158.373 1.00 57.75  ? 2642 ARG A CZ    1 
ATOM   10264 N NH1   . ARG A 1 2642 ? 141.889 207.005 157.221 1.00 57.75  ? 2642 ARG A NH1   1 
ATOM   10265 N NH2   . ARG A 1 2642 ? 141.980 206.905 159.504 1.00 57.75  ? 2642 ARG A NH2   1 
ATOM   10266 N N     . ARG A 1 2643 ? 147.672 209.063 155.306 1.00 68.15  ? 2643 ARG A N     1 
ATOM   10267 C CA    . ARG A 1 2643 ? 148.894 209.791 155.618 1.00 68.15  ? 2643 ARG A CA    1 
ATOM   10268 C C     . ARG A 1 2643 ? 148.639 211.137 156.293 1.00 68.15  ? 2643 ARG A C     1 
ATOM   10269 O O     . ARG A 1 2643 ? 149.572 211.712 156.865 1.00 68.15  ? 2643 ARG A O     1 
ATOM   10270 C CB    . ARG A 1 2643 ? 149.710 209.986 154.329 1.00 68.15  ? 2643 ARG A CB    1 
ATOM   10271 C CG    . ARG A 1 2643 ? 151.030 210.728 154.484 1.00 68.15  ? 2643 ARG A CG    1 
ATOM   10272 C CD    . ARG A 1 2643 ? 152.100 209.835 155.092 1.00 68.15  ? 2643 ARG A CD    1 
ATOM   10273 N NE    . ARG A 1 2643 ? 153.041 210.589 155.913 1.00 68.15  ? 2643 ARG A NE    1 
ATOM   10274 C CZ    . ARG A 1 2643 ? 152.766 211.075 157.116 1.00 68.15  ? 2643 ARG A CZ    1 
ATOM   10275 N NH1   . ARG A 1 2643 ? 151.585 210.894 157.684 1.00 68.15  ? 2643 ARG A NH1   1 
ATOM   10276 N NH2   . ARG A 1 2643 ? 153.703 211.759 157.769 1.00 68.15  ? 2643 ARG A NH2   1 
ATOM   10277 N N     . THR A 1 2644 ? 147.400 211.632 156.274 1.00 77.96  ? 2644 THR A N     1 
ATOM   10278 C CA    . THR A 1 2644 ? 147.120 212.953 156.837 1.00 77.96  ? 2644 THR A CA    1 
ATOM   10279 C C     . THR A 1 2644 ? 147.551 213.123 158.295 1.00 77.96  ? 2644 THR A C     1 
ATOM   10280 O O     . THR A 1 2644 ? 148.037 214.217 158.632 1.00 77.96  ? 2644 THR A O     1 
ATOM   10281 C CB    . THR A 1 2644 ? 145.632 213.297 156.664 1.00 77.96  ? 2644 THR A CB    1 
ATOM   10282 O OG1   . THR A 1 2644 ? 144.814 212.295 157.279 1.00 77.96  ? 2644 THR A OG1   1 
ATOM   10283 C CG2   . THR A 1 2644 ? 145.277 213.397 155.188 1.00 77.96  ? 2644 THR A CG2   1 
ATOM   10284 N N     . PRO A 1 2645 ? 147.410 212.131 159.203 1.00 75.76  ? 2645 PRO A N     1 
ATOM   10285 C CA    . PRO A 1 2645 ? 147.898 212.345 160.574 1.00 75.76  ? 2645 PRO A CA    1 
ATOM   10286 C C     . PRO A 1 2645 ? 149.415 212.429 160.651 1.00 75.76  ? 2645 PRO A C     1 
ATOM   10287 O O     . PRO A 1 2645 ? 150.097 212.448 159.620 1.00 75.76  ? 2645 PRO A O     1 
ATOM   10288 C CB    . PRO A 1 2645 ? 147.365 211.123 161.337 1.00 75.76  ? 2645 PRO A CB    1 
ATOM   10289 C CG    . PRO A 1 2645 ? 146.273 210.581 160.482 1.00 75.76  ? 2645 PRO A CG    1 
ATOM   10290 C CD    . PRO A 1 2645 ? 146.739 210.824 159.091 1.00 75.76  ? 2645 PRO A CD    1 
ATOM   10291 N N     . ASN A 1 2646 ? 149.947 212.501 161.875 1.00 71.28  ? 2646 ASN A N     1 
ATOM   10292 C CA    . ASN A 1 2646 ? 151.390 212.629 162.066 1.00 71.28  ? 2646 ASN A CA    1 
ATOM   10293 C C     . ASN A 1 2646 ? 152.150 211.520 161.348 1.00 71.28  ? 2646 ASN A C     1 
ATOM   10294 O O     . ASN A 1 2646 ? 153.195 211.768 160.736 1.00 71.28  ? 2646 ASN A O     1 
ATOM   10295 C CB    . ASN A 1 2646 ? 151.720 212.620 163.559 1.00 71.28  ? 2646 ASN A CB    1 
ATOM   10296 C CG    . ASN A 1 2646 ? 151.062 213.761 164.307 1.00 71.28  ? 2646 ASN A CG    1 
ATOM   10297 O OD1   . ASN A 1 2646 ? 150.222 213.543 165.180 1.00 71.28  ? 2646 ASN A OD1   1 
ATOM   10298 N ND2   . ASN A 1 2646 ? 151.438 214.988 163.966 1.00 71.28  ? 2646 ASN A ND2   1 
ATOM   10299 N N     . GLY A 1 2647 ? 151.640 210.290 161.411 1.00 64.71  ? 2647 GLY A N     1 
ATOM   10300 C CA    . GLY A 1 2647 ? 152.220 209.177 160.691 1.00 64.71  ? 2647 GLY A CA    1 
ATOM   10301 C C     . GLY A 1 2647 ? 151.171 208.460 159.861 1.00 64.71  ? 2647 GLY A C     1 
ATOM   10302 O O     . GLY A 1 2647 ? 149.978 208.764 159.934 1.00 64.71  ? 2647 GLY A O     1 
ATOM   10303 N N     . VAL A 1 2648 ? 151.650 207.506 159.060 1.00 52.40  ? 2648 VAL A N     1 
ATOM   10304 C CA    . VAL A 1 2648 ? 150.740 206.672 158.286 1.00 52.40  ? 2648 VAL A CA    1 
ATOM   10305 C C     . VAL A 1 2648 ? 149.834 205.911 159.241 1.00 52.40  ? 2648 VAL A C     1 
ATOM   10306 O O     . VAL A 1 2648 ? 150.278 205.394 160.273 1.00 52.40  ? 2648 VAL A O     1 
ATOM   10307 C CB    . VAL A 1 2648 ? 151.523 205.715 157.374 1.00 52.40  ? 2648 VAL A CB    1 
ATOM   10308 C CG1   . VAL A 1 2648 ? 150.588 205.048 156.381 1.00 52.40  ? 2648 VAL A CG1   1 
ATOM   10309 C CG2   . VAL A 1 2648 ? 152.629 206.463 156.648 1.00 52.40  ? 2648 VAL A CG2   1 
ATOM   10310 N N     . VAL A 1 2649 ? 148.547 205.857 158.912 1.00 50.42  ? 2649 VAL A N     1 
ATOM   10311 C CA    . VAL A 1 2649 ? 147.538 205.294 159.799 1.00 50.42  ? 2649 VAL A CA    1 
ATOM   10312 C C     . VAL A 1 2649 ? 146.737 204.250 159.036 1.00 50.42  ? 2649 VAL A C     1 
ATOM   10313 O O     . VAL A 1 2649 ? 146.288 204.503 157.913 1.00 50.42  ? 2649 VAL A O     1 
ATOM   10314 C CB    . VAL A 1 2649 ? 146.612 206.387 160.364 1.00 50.42  ? 2649 VAL A CB    1 
ATOM   10315 C CG1   . VAL A 1 2649 ? 145.348 205.775 160.918 1.00 50.42  ? 2649 VAL A CG1   1 
ATOM   10316 C CG2   . VAL A 1 2649 ? 147.332 207.185 161.437 1.00 50.42  ? 2649 VAL A CG2   1 
ATOM   10317 N N     . LEU A 1 2650 ? 146.561 203.079 159.645 1.00 48.51  ? 2650 LEU A N     1 
ATOM   10318 C CA    . LEU A 1 2650 ? 145.733 202.022 159.082 1.00 48.51  ? 2650 LEU A CA    1 
ATOM   10319 C C     . LEU A 1 2650 ? 144.405 201.985 159.828 1.00 48.51  ? 2650 LEU A C     1 
ATOM   10320 O O     . LEU A 1 2650 ? 144.378 201.782 161.047 1.00 48.51  ? 2650 LEU A O     1 
ATOM   10321 C CB    . LEU A 1 2650 ? 146.443 200.673 159.177 1.00 48.51  ? 2650 LEU A CB    1 
ATOM   10322 C CG    . LEU A 1 2650 ? 145.714 199.480 158.560 1.00 48.51  ? 2650 LEU A CG    1 
ATOM   10323 C CD1   . LEU A 1 2650 ? 145.914 199.456 157.056 1.00 48.51  ? 2650 LEU A CD1   1 
ATOM   10324 C CD2   . LEU A 1 2650 ? 146.191 198.185 159.186 1.00 48.51  ? 2650 LEU A CD2   1 
ATOM   10325 N N     . ALA A 1 2651 ? 143.310 202.184 159.102 1.00 53.65  ? 2651 ALA A N     1 
ATOM   10326 C CA    . ALA A 1 2651 ? 141.979 202.213 159.687 1.00 53.65  ? 2651 ALA A CA    1 
ATOM   10327 C C     . ALA A 1 2651 ? 140.994 201.544 158.743 1.00 53.65  ? 2651 ALA A C     1 
ATOM   10328 O O     . ALA A 1 2651 ? 141.218 201.515 157.527 1.00 53.65  ? 2651 ALA A O     1 
ATOM   10329 C CB    . ALA A 1 2651 ? 141.522 203.652 159.973 1.00 53.65  ? 2651 ALA A CB    1 
ATOM   10330 N N     . PRO A 1 2652 ? 139.895 201.002 159.270 1.00 52.94  ? 2652 PRO A N     1 
ATOM   10331 C CA    . PRO A 1 2652 ? 138.873 200.421 158.394 1.00 52.94  ? 2652 PRO A CA    1 
ATOM   10332 C C     . PRO A 1 2652 ? 138.259 201.478 157.490 1.00 52.94  ? 2652 PRO A C     1 
ATOM   10333 O O     . PRO A 1 2652 ? 138.184 202.658 157.837 1.00 52.94  ? 2652 PRO A O     1 
ATOM   10334 C CB    . PRO A 1 2652 ? 137.839 199.857 159.375 1.00 52.94  ? 2652 PRO A CB    1 
ATOM   10335 C CG    . PRO A 1 2652 ? 138.568 199.699 160.653 1.00 52.94  ? 2652 PRO A CG    1 
ATOM   10336 C CD    . PRO A 1 2652 ? 139.575 200.803 160.692 1.00 52.94  ? 2652 PRO A CD    1 
ATOM   10337 N N     . VAL A 1 2653 ? 137.824 201.036 156.309 1.00 55.92  ? 2653 VAL A N     1 
ATOM   10338 C CA    . VAL A 1 2653 ? 137.207 201.951 155.352 1.00 55.92  ? 2653 VAL A CA    1 
ATOM   10339 C C     . VAL A 1 2653 ? 135.925 202.536 155.933 1.00 55.92  ? 2653 VAL A C     1 
ATOM   10340 O O     . VAL A 1 2653 ? 135.659 203.738 155.812 1.00 55.92  ? 2653 VAL A O     1 
ATOM   10341 C CB    . VAL A 1 2653 ? 136.950 201.236 154.014 1.00 55.92  ? 2653 VAL A CB    1 
ATOM   10342 C CG1   . VAL A 1 2653 ? 136.219 202.157 153.050 1.00 55.92  ? 2653 VAL A CG1   1 
ATOM   10343 C CG2   . VAL A 1 2653 ? 138.261 200.758 153.413 1.00 55.92  ? 2653 VAL A CG2   1 
ATOM   10344 N N     . GLN A 1 2654 ? 135.115 201.696 156.572 1.00 54.65  ? 2654 GLN A N     1 
ATOM   10345 C CA    . GLN A 1 2654 ? 133.895 202.171 157.210 1.00 54.65  ? 2654 GLN A CA    1 
ATOM   10346 C C     . GLN A 1 2654 ? 134.233 203.110 158.361 1.00 54.65  ? 2654 GLN A C     1 
ATOM   10347 O O     . GLN A 1 2654 ? 135.143 202.840 159.151 1.00 54.65  ? 2654 GLN A O     1 
ATOM   10348 C CB    . GLN A 1 2654 ? 133.066 200.991 157.714 1.00 54.65  ? 2654 GLN A CB    1 
ATOM   10349 C CG    . GLN A 1 2654 ? 132.371 200.207 156.613 1.00 54.65  ? 2654 GLN A CG    1 
ATOM   10350 C CD    . GLN A 1 2654 ? 133.147 198.974 156.200 1.00 54.65  ? 2654 GLN A CD    1 
ATOM   10351 O OE1   . GLN A 1 2654 ? 134.159 198.631 156.809 1.00 54.65  ? 2654 GLN A OE1   1 
ATOM   10352 N NE2   . GLN A 1 2654 ? 132.676 198.300 155.157 1.00 54.65  ? 2654 GLN A NE2   1 
ATOM   10353 N N     . LEU A 1 2655 ? 133.502 204.217 158.452 1.00 53.77  ? 2655 LEU A N     1 
ATOM   10354 C CA    . LEU A 1 2655 ? 133.742 205.203 159.495 1.00 53.77  ? 2655 LEU A CA    1 
ATOM   10355 C C     . LEU A 1 2655 ? 132.952 204.859 160.752 1.00 53.77  ? 2655 LEU A C     1 
ATOM   10356 O O     . LEU A 1 2655 ? 131.794 204.441 160.681 1.00 53.77  ? 2655 LEU A O     1 
ATOM   10357 C CB    . LEU A 1 2655 ? 133.365 206.602 159.008 1.00 53.77  ? 2655 LEU A CB    1 
ATOM   10358 C CG    . LEU A 1 2655 ? 134.394 207.362 158.167 1.00 53.77  ? 2655 LEU A CG    1 
ATOM   10359 C CD1   . LEU A 1 2655 ? 134.478 206.808 156.751 1.00 53.77  ? 2655 LEU A CD1   1 
ATOM   10360 C CD2   . LEU A 1 2655 ? 134.069 208.847 158.145 1.00 53.77  ? 2655 LEU A CD2   1 
ATOM   10361 N N     . GLY A 1 2656 ? 133.591 205.036 161.906 1.00 48.45  ? 2656 GLY A N     1 
ATOM   10362 C CA    . GLY A 1 2656 ? 132.931 204.770 163.168 1.00 48.45  ? 2656 GLY A CA    1 
ATOM   10363 C C     . GLY A 1 2656 ? 132.781 203.308 163.511 1.00 48.45  ? 2656 GLY A C     1 
ATOM   10364 O O     . GLY A 1 2656 ? 132.057 202.974 164.452 1.00 48.45  ? 2656 GLY A O     1 
ATOM   10365 N N     . LYS A 1 2657 ? 133.446 202.422 162.776 1.00 48.82  ? 2657 LYS A N     1 
ATOM   10366 C CA    . LYS A 1 2657 ? 133.345 200.985 162.985 1.00 48.82  ? 2657 LYS A CA    1 
ATOM   10367 C C     . LYS A 1 2657 ? 134.675 200.452 163.499 1.00 48.82  ? 2657 LYS A C     1 
ATOM   10368 O O     . LYS A 1 2657 ? 135.723 200.699 162.894 1.00 48.82  ? 2657 LYS A O     1 
ATOM   10369 C CB    . LYS A 1 2657 ? 132.958 200.272 161.687 1.00 48.82  ? 2657 LYS A CB    1 
ATOM   10370 C CG    . LYS A 1 2657 ? 131.496 200.421 161.300 1.00 48.82  ? 2657 LYS A CG    1 
ATOM   10371 C CD    . LYS A 1 2657 ? 130.579 199.821 162.351 1.00 48.82  ? 2657 LYS A CD    1 
ATOM   10372 C CE    . LYS A 1 2657 ? 129.190 199.565 161.791 1.00 48.82  ? 2657 LYS A CE    1 
ATOM   10373 N NZ    . LYS A 1 2657 ? 129.219 198.598 160.659 1.00 48.82  ? 2657 LYS A NZ    1 
ATOM   10374 N N     . TRP A 1 2658 ? 134.629 199.724 164.613 1.00 38.18  ? 2658 TRP A N     1 
ATOM   10375 C CA    . TRP A 1 2658 ? 135.815 199.089 165.172 1.00 38.18  ? 2658 TRP A CA    1 
ATOM   10376 C C     . TRP A 1 2658 ? 135.943 197.687 164.592 1.00 38.18  ? 2658 TRP A C     1 
ATOM   10377 O O     . TRP A 1 2658 ? 135.092 196.826 164.839 1.00 38.18  ? 2658 TRP A O     1 
ATOM   10378 C CB    . TRP A 1 2658 ? 135.745 199.040 166.697 1.00 38.18  ? 2658 TRP A CB    1 
ATOM   10379 C CG    . TRP A 1 2658 ? 136.242 200.290 167.349 1.00 38.18  ? 2658 TRP A CG    1 
ATOM   10380 C CD1   . TRP A 1 2658 ? 135.534 201.433 167.574 1.00 38.18  ? 2658 TRP A CD1   1 
ATOM   10381 C CD2   . TRP A 1 2658 ? 137.567 200.536 167.834 1.00 38.18  ? 2658 TRP A CD2   1 
ATOM   10382 N NE1   . TRP A 1 2658 ? 136.331 202.372 168.182 1.00 38.18  ? 2658 TRP A NE1   1 
ATOM   10383 C CE2   . TRP A 1 2658 ? 137.585 201.846 168.351 1.00 38.18  ? 2658 TRP A CE2   1 
ATOM   10384 C CE3   . TRP A 1 2658 ? 138.736 199.773 167.889 1.00 38.18  ? 2658 TRP A CE3   1 
ATOM   10385 C CZ2   . TRP A 1 2658 ? 138.727 202.411 168.913 1.00 38.18  ? 2658 TRP A CZ2   1 
ATOM   10386 C CZ3   . TRP A 1 2658 ? 139.872 200.338 168.440 1.00 38.18  ? 2658 TRP A CZ3   1 
ATOM   10387 C CH2   . TRP A 1 2658 ? 139.858 201.642 168.950 1.00 38.18  ? 2658 TRP A CH2   1 
ATOM   10388 N N     . LEU A 1 2659 ? 137.004 197.459 163.824 1.00 34.57  ? 2659 LEU A N     1 
ATOM   10389 C CA    . LEU A 1 2659 ? 137.215 196.188 163.142 1.00 34.57  ? 2659 LEU A CA    1 
ATOM   10390 C C     . LEU A 1 2659 ? 137.784 195.183 164.133 1.00 34.57  ? 2659 LEU A C     1 
ATOM   10391 O O     . LEU A 1 2659 ? 138.879 195.380 164.669 1.00 34.57  ? 2659 LEU A O     1 
ATOM   10392 C CB    . LEU A 1 2659 ? 138.148 196.364 161.948 1.00 34.57  ? 2659 LEU A CB    1 
ATOM   10393 C CG    . LEU A 1 2659 ? 138.322 195.134 161.058 1.00 34.57  ? 2659 LEU A CG    1 
ATOM   10394 C CD1   . LEU A 1 2659 ? 137.246 195.104 159.991 1.00 34.57  ? 2659 LEU A CD1   1 
ATOM   10395 C CD2   . LEU A 1 2659 ? 139.704 195.114 160.429 1.00 34.57  ? 2659 LEU A CD2   1 
ATOM   10396 N N     . VAL A 1 2660 ? 137.045 194.106 164.374 1.00 29.34  ? 2660 VAL A N     1 
ATOM   10397 C CA    . VAL A 1 2660 ? 137.497 193.017 165.229 1.00 29.34  ? 2660 VAL A CA    1 
ATOM   10398 C C     . VAL A 1 2660 ? 138.005 191.901 164.331 1.00 29.34  ? 2660 VAL A C     1 
ATOM   10399 O O     . VAL A 1 2660 ? 137.246 191.343 163.529 1.00 29.34  ? 2660 VAL A O     1 
ATOM   10400 C CB    . VAL A 1 2660 ? 136.374 192.517 166.150 1.00 29.34  ? 2660 VAL A CB    1 
ATOM   10401 C CG1   . VAL A 1 2660 ? 136.681 191.116 166.642 1.00 29.34  ? 2660 VAL A CG1   1 
ATOM   10402 C CG2   . VAL A 1 2660 ? 136.202 193.457 167.319 1.00 29.34  ? 2660 VAL A CG2   1 
ATOM   10403 N N     . LEU A 1 2661 ? 139.290 191.580 164.451 1.00 27.07  ? 2661 LEU A N     1 
ATOM   10404 C CA    . LEU A 1 2661 ? 139.879 190.475 163.701 1.00 27.07  ? 2661 LEU A CA    1 
ATOM   10405 C C     . LEU A 1 2661 ? 139.783 189.229 164.567 1.00 27.07  ? 2661 LEU A C     1 
ATOM   10406 O O     . LEU A 1 2661 ? 140.695 188.896 165.323 1.00 27.07  ? 2661 LEU A O     1 
ATOM   10407 C CB    . LEU A 1 2661 ? 141.316 190.782 163.306 1.00 27.07  ? 2661 LEU A CB    1 
ATOM   10408 C CG    . LEU A 1 2661 ? 141.500 191.829 162.209 1.00 27.07  ? 2661 LEU A CG    1 
ATOM   10409 C CD1   . LEU A 1 2661 ? 142.937 191.833 161.728 1.00 27.07  ? 2661 LEU A CD1   1 
ATOM   10410 C CD2   . LEU A 1 2661 ? 140.551 191.566 161.056 1.00 27.07  ? 2661 LEU A CD2   1 
ATOM   10411 N N     . PHE A 1 2662 ? 138.653 188.540 164.463 1.00 30.09  ? 2662 PHE A N     1 
ATOM   10412 C CA    . PHE A 1 2662 ? 138.436 187.297 165.195 1.00 30.09  ? 2662 PHE A CA    1 
ATOM   10413 C C     . PHE A 1 2662 ? 139.374 186.242 164.626 1.00 30.09  ? 2662 PHE A C     1 
ATOM   10414 O O     . PHE A 1 2662 ? 139.247 185.837 163.469 1.00 30.09  ? 2662 PHE A O     1 
ATOM   10415 C CB    . PHE A 1 2662 ? 136.974 186.875 165.088 1.00 30.09  ? 2662 PHE A CB    1 
ATOM   10416 C CG    . PHE A 1 2662 ? 136.717 185.451 165.486 1.00 30.09  ? 2662 PHE A CG    1 
ATOM   10417 C CD1   . PHE A 1 2662 ? 136.820 184.425 164.563 1.00 30.09  ? 2662 PHE A CD1   1 
ATOM   10418 C CD2   . PHE A 1 2662 ? 136.358 185.138 166.781 1.00 30.09  ? 2662 PHE A CD2   1 
ATOM   10419 C CE1   . PHE A 1 2662 ? 136.586 183.123 164.930 1.00 30.09  ? 2662 PHE A CE1   1 
ATOM   10420 C CE2   . PHE A 1 2662 ? 136.119 183.834 167.143 1.00 30.09  ? 2662 PHE A CE2   1 
ATOM   10421 C CZ    . PHE A 1 2662 ? 136.230 182.831 166.222 1.00 30.09  ? 2662 PHE A CZ    1 
ATOM   10422 N N     . CYS A 1 2663 ? 140.335 185.803 165.433 1.00 30.04  ? 2663 CYS A N     1 
ATOM   10423 C CA    . CYS A 1 2663 ? 141.308 184.796 165.019 1.00 30.04  ? 2663 CYS A CA    1 
ATOM   10424 C C     . CYS A 1 2663 ? 141.141 183.569 165.906 1.00 30.04  ? 2663 CYS A C     1 
ATOM   10425 O O     . CYS A 1 2663 ? 141.806 183.442 166.936 1.00 30.04  ? 2663 CYS A O     1 
ATOM   10426 C CB    . CYS A 1 2663 ? 142.729 185.346 165.098 1.00 30.04  ? 2663 CYS A CB    1 
ATOM   10427 S SG    . CYS A 1 2663 ? 142.965 186.949 164.303 1.00 30.04  ? 2663 CYS A SG    1 
ATOM   10428 N N     . ASP A 1 2664 ? 140.252 182.665 165.508 1.00 33.11  ? 2664 ASP A N     1 
ATOM   10429 C CA    . ASP A 1 2664 ? 140.144 181.405 166.222 1.00 33.11  ? 2664 ASP A CA    1 
ATOM   10430 C C     . ASP A 1 2664 ? 141.316 180.500 165.865 1.00 33.11  ? 2664 ASP A C     1 
ATOM   10431 O O     . ASP A 1 2664 ? 142.027 180.720 164.880 1.00 33.11  ? 2664 ASP A O     1 
ATOM   10432 C CB    . ASP A 1 2664 ? 138.824 180.700 165.915 1.00 33.11  ? 2664 ASP A CB    1 
ATOM   10433 C CG    . ASP A 1 2664 ? 138.607 180.483 164.436 1.00 33.11  ? 2664 ASP A CG    1 
ATOM   10434 O OD1   . ASP A 1 2664 ? 139.396 181.017 163.631 1.00 33.11  ? 2664 ASP A OD1   1 
ATOM   10435 O OD2   . ASP A 1 2664 ? 137.640 179.778 164.078 1.00 33.11  ? 2664 ASP A OD2   1 
ATOM   10436 N N     . GLU A 1 2665 ? 141.506 179.466 166.684 1.00 37.40  ? 2665 GLU A N     1 
ATOM   10437 C CA    . GLU A 1 2665 ? 142.636 178.552 166.553 1.00 37.40  ? 2665 GLU A CA    1 
ATOM   10438 C C     . GLU A 1 2665 ? 143.949 179.336 166.595 1.00 37.40  ? 2665 GLU A C     1 
ATOM   10439 O O     . GLU A 1 2665 ? 144.872 179.114 165.810 1.00 37.40  ? 2665 GLU A O     1 
ATOM   10440 C CB    . GLU A 1 2665 ? 142.520 177.724 165.269 1.00 37.40  ? 2665 GLU A CB    1 
ATOM   10441 C CG    . GLU A 1 2665 ? 141.190 177.002 165.122 1.00 37.40  ? 2665 GLU A CG    1 
ATOM   10442 C CD    . GLU A 1 2665 ? 140.969 175.955 166.189 1.00 37.40  ? 2665 GLU A CD    1 
ATOM   10443 O OE1   . GLU A 1 2665 ? 141.962 175.350 166.639 1.00 37.40  ? 2665 GLU A OE1   1 
ATOM   10444 O OE2   . GLU A 1 2665 ? 139.804 175.739 166.581 1.00 37.40  ? 2665 GLU A OE2   1 
ATOM   10445 N N     . ILE A 1 2666 ? 144.003 180.282 167.536 1.00 32.39  ? 2666 ILE A N     1 
ATOM   10446 C CA    . ILE A 1 2666 ? 145.107 181.236 167.579 1.00 32.39  ? 2666 ILE A CA    1 
ATOM   10447 C C     . ILE A 1 2666 ? 146.422 180.547 167.925 1.00 32.39  ? 2666 ILE A C     1 
ATOM   10448 O O     . ILE A 1 2666 ? 147.493 181.000 167.504 1.00 32.39  ? 2666 ILE A O     1 
ATOM   10449 C CB    . ILE A 1 2666 ? 144.778 182.378 168.560 1.00 32.39  ? 2666 ILE A CB    1 
ATOM   10450 C CG1   . ILE A 1 2666 ? 145.741 183.550 168.363 1.00 32.39  ? 2666 ILE A CG1   1 
ATOM   10451 C CG2   . ILE A 1 2666 ? 144.796 181.888 170.000 1.00 32.39  ? 2666 ILE A CG2   1 
ATOM   10452 C CD1   . ILE A 1 2666 ? 145.298 184.822 169.045 1.00 32.39  ? 2666 ILE A CD1   1 
ATOM   10453 N N     . ASN A 1 2667 ? 146.376 179.454 168.680 1.00 33.37  ? 2667 ASN A N     1 
ATOM   10454 C CA    . ASN A 1 2667 ? 147.581 178.724 169.046 1.00 33.37  ? 2667 ASN A CA    1 
ATOM   10455 C C     . ASN A 1 2667 ? 147.987 177.692 168.004 1.00 33.37  ? 2667 ASN A C     1 
ATOM   10456 O O     . ASN A 1 2667 ? 149.064 177.101 168.125 1.00 33.37  ? 2667 ASN A O     1 
ATOM   10457 C CB    . ASN A 1 2667 ? 147.388 178.037 170.400 1.00 33.37  ? 2667 ASN A CB    1 
ATOM   10458 C CG    . ASN A 1 2667 ? 146.150 177.168 170.439 1.00 33.37  ? 2667 ASN A CG    1 
ATOM   10459 O OD1   . ASN A 1 2667 ? 145.412 177.076 169.460 1.00 33.37  ? 2667 ASN A OD1   1 
ATOM   10460 N ND2   . ASN A 1 2667 ? 145.916 176.523 171.575 1.00 33.37  ? 2667 ASN A ND2   1 
ATOM   10461 N N     . LEU A 1 2668 ? 147.151 177.460 166.995 1.00 36.29  ? 2668 LEU A N     1 
ATOM   10462 C CA    . LEU A 1 2668 ? 147.466 176.456 165.982 1.00 36.29  ? 2668 LEU A CA    1 
ATOM   10463 C C     . LEU A 1 2668 ? 148.723 176.754 165.165 1.00 36.29  ? 2668 LEU A C     1 
ATOM   10464 O O     . LEU A 1 2668 ? 149.462 175.798 164.872 1.00 36.29  ? 2668 LEU A O     1 
ATOM   10465 C CB    . LEU A 1 2668 ? 146.254 176.254 165.063 1.00 36.29  ? 2668 LEU A CB    1 
ATOM   10466 C CG    . LEU A 1 2668 ? 146.420 175.175 163.992 1.00 36.29  ? 2668 LEU A CG    1 
ATOM   10467 C CD1   . LEU A 1 2668 ? 146.623 173.823 164.652 1.00 36.29  ? 2668 LEU A CD1   1 
ATOM   10468 C CD2   . LEU A 1 2668 ? 145.216 175.134 163.073 1.00 36.29  ? 2668 LEU A CD2   1 
ATOM   10469 N N     . PRO A 1 2669 ? 149.017 177.994 164.747 1.00 35.92  ? 2669 PRO A N     1 
ATOM   10470 C CA    . PRO A 1 2669 ? 150.185 178.217 163.881 1.00 35.92  ? 2669 PRO A CA    1 
ATOM   10471 C C     . PRO A 1 2669 ? 151.467 177.642 164.469 1.00 35.92  ? 2669 PRO A C     1 
ATOM   10472 O O     . PRO A 1 2669 ? 151.726 177.739 165.669 1.00 35.92  ? 2669 PRO A O     1 
ATOM   10473 C CB    . PRO A 1 2669 ? 150.255 179.742 163.774 1.00 35.92  ? 2669 PRO A CB    1 
ATOM   10474 C CG    . PRO A 1 2669 ? 148.864 180.182 163.923 1.00 35.92  ? 2669 PRO A CG    1 
ATOM   10475 C CD    . PRO A 1 2669 ? 148.203 179.219 164.866 1.00 35.92  ? 2669 PRO A CD    1 
ATOM   10476 N N     . ASP A 1 2670 ? 152.270 177.036 163.597 1.00 42.19  ? 2670 ASP A N     1 
ATOM   10477 C CA    . ASP A 1 2670 ? 153.420 176.260 164.033 1.00 42.19  ? 2670 ASP A CA    1 
ATOM   10478 C C     . ASP A 1 2670 ? 154.542 177.154 164.546 1.00 42.19  ? 2670 ASP A C     1 
ATOM   10479 O O     . ASP A 1 2670 ? 154.772 178.258 164.046 1.00 42.19  ? 2670 ASP A O     1 
ATOM   10480 C CB    . ASP A 1 2670 ? 153.942 175.389 162.889 1.00 42.19  ? 2670 ASP A CB    1 
ATOM   10481 C CG    . ASP A 1 2670 ? 154.036 176.143 161.574 1.00 42.19  ? 2670 ASP A CG    1 
ATOM   10482 O OD1   . ASP A 1 2670 ? 153.923 177.386 161.581 1.00 42.19  ? 2670 ASP A OD1   1 
ATOM   10483 O OD2   . ASP A 1 2670 ? 154.225 175.488 160.527 1.00 42.19  ? 2670 ASP A OD2   1 
ATOM   10484 N N     . MET A 1 2671 ? 155.241 176.660 165.563 1.00 46.73  ? 2671 MET A N     1 
ATOM   10485 C CA    . MET A 1 2671 ? 156.474 177.285 166.010 1.00 46.73  ? 2671 MET A CA    1 
ATOM   10486 C C     . MET A 1 2671 ? 157.600 176.946 165.044 1.00 46.73  ? 2671 MET A C     1 
ATOM   10487 O O     . MET A 1 2671 ? 157.661 175.837 164.506 1.00 46.73  ? 2671 MET A O     1 
ATOM   10488 C CB    . MET A 1 2671 ? 156.836 176.816 167.419 1.00 46.73  ? 2671 MET A CB    1 
ATOM   10489 C CG    . MET A 1 2671 ? 156.409 177.766 168.524 1.00 46.73  ? 2671 MET A CG    1 
ATOM   10490 S SD    . MET A 1 2671 ? 156.420 176.981 170.147 1.00 46.73  ? 2671 MET A SD    1 
ATOM   10491 C CE    . MET A 1 2671 ? 155.604 178.231 171.136 1.00 46.73  ? 2671 MET A CE    1 
ATOM   10492 N N     . ASP A 1 2672 ? 158.493 177.904 164.826 1.00 48.89  ? 2672 ASP A N     1 
ATOM   10493 C CA    . ASP A 1 2672 ? 159.632 177.686 163.945 1.00 48.89  ? 2672 ASP A CA    1 
ATOM   10494 C C     . ASP A 1 2672 ? 160.677 176.846 164.678 1.00 48.89  ? 2672 ASP A C     1 
ATOM   10495 O O     . ASP A 1 2672 ? 160.429 176.299 165.756 1.00 48.89  ? 2672 ASP A O     1 
ATOM   10496 C CB    . ASP A 1 2672 ? 160.192 179.019 163.457 1.00 48.89  ? 2672 ASP A CB    1 
ATOM   10497 C CG    . ASP A 1 2672 ? 160.708 179.885 164.588 1.00 48.89  ? 2672 ASP A CG    1 
ATOM   10498 O OD1   . ASP A 1 2672 ? 160.415 179.575 165.761 1.00 48.89  ? 2672 ASP A OD1   1 
ATOM   10499 O OD2   . ASP A 1 2672 ? 161.408 180.878 164.302 1.00 48.89  ? 2672 ASP A OD2   1 
ATOM   10500 N N     . LYS A 1 2673 ? 161.869 176.729 164.091 1.00 50.88  ? 2673 LYS A N     1 
ATOM   10501 C CA    . LYS A 1 2673 ? 162.932 175.937 164.696 1.00 50.88  ? 2673 LYS A CA    1 
ATOM   10502 C C     . LYS A 1 2673 ? 163.398 176.491 166.037 1.00 50.88  ? 2673 LYS A C     1 
ATOM   10503 O O     . LYS A 1 2673 ? 164.026 175.755 166.805 1.00 50.88  ? 2673 LYS A O     1 
ATOM   10504 C CB    . LYS A 1 2673 ? 164.118 175.842 163.732 1.00 50.88  ? 2673 LYS A CB    1 
ATOM   10505 C CG    . LYS A 1 2673 ? 165.000 174.620 163.936 1.00 50.88  ? 2673 LYS A CG    1 
ATOM   10506 C CD    . LYS A 1 2673 ? 166.272 174.975 164.690 1.00 50.88  ? 2673 LYS A CD    1 
ATOM   10507 C CE    . LYS A 1 2673 ? 167.269 173.830 164.665 1.00 50.88  ? 2673 LYS A CE    1 
ATOM   10508 N NZ    . LYS A 1 2673 ? 168.641 174.284 165.026 1.00 50.88  ? 2673 LYS A NZ    1 
ATOM   10509 N N     . TYR A 1 2674 ? 163.095 177.752 166.347 1.00 46.74  ? 2674 TYR A N     1 
ATOM   10510 C CA    . TYR A 1 2674 ? 163.593 178.405 167.551 1.00 46.74  ? 2674 TYR A CA    1 
ATOM   10511 C C     . TYR A 1 2674 ? 162.465 178.784 168.505 1.00 46.74  ? 2674 TYR A C     1 
ATOM   10512 O O     . TYR A 1 2674 ? 162.578 179.753 169.259 1.00 46.74  ? 2674 TYR A O     1 
ATOM   10513 C CB    . TYR A 1 2674 ? 164.432 179.626 167.180 1.00 46.74  ? 2674 TYR A CB    1 
ATOM   10514 C CG    . TYR A 1 2674 ? 165.434 179.328 166.092 1.00 46.74  ? 2674 TYR A CG    1 
ATOM   10515 C CD1   . TYR A 1 2674 ? 166.637 178.701 166.384 1.00 46.74  ? 2674 TYR A CD1   1 
ATOM   10516 C CD2   . TYR A 1 2674 ? 165.168 179.649 164.769 1.00 46.74  ? 2674 TYR A CD2   1 
ATOM   10517 C CE1   . TYR A 1 2674 ? 167.554 178.416 165.393 1.00 46.74  ? 2674 TYR A CE1   1 
ATOM   10518 C CE2   . TYR A 1 2674 ? 166.076 179.365 163.770 1.00 46.74  ? 2674 TYR A CE2   1 
ATOM   10519 C CZ    . TYR A 1 2674 ? 167.268 178.751 164.087 1.00 46.74  ? 2674 TYR A CZ    1 
ATOM   10520 O OH    . TYR A 1 2674 ? 168.179 178.467 163.096 1.00 46.74  ? 2674 TYR A OH    1 
ATOM   10521 N N     . GLY A 1 2675 ? 161.373 178.023 168.484 1.00 44.48  ? 2675 GLY A N     1 
ATOM   10522 C CA    . GLY A 1 2675 ? 160.323 178.160 169.474 1.00 44.48  ? 2675 GLY A CA    1 
ATOM   10523 C C     . GLY A 1 2675 ? 159.585 179.482 169.495 1.00 44.48  ? 2675 GLY A C     1 
ATOM   10524 O O     . GLY A 1 2675 ? 159.392 180.066 170.566 1.00 44.48  ? 2675 GLY A O     1 
ATOM   10525 N N     . THR A 1 2676 ? 159.170 179.975 168.330 1.00 40.62  ? 2676 THR A N     1 
ATOM   10526 C CA    . THR A 1 2676 ? 158.338 181.167 168.277 1.00 40.62  ? 2676 THR A CA    1 
ATOM   10527 C C     . THR A 1 2676 ? 157.385 181.063 167.097 1.00 40.62  ? 2676 THR A C     1 
ATOM   10528 O O     . THR A 1 2676 ? 157.650 180.351 166.125 1.00 40.62  ? 2676 THR A O     1 
ATOM   10529 C CB    . THR A 1 2676 ? 159.172 182.449 168.166 1.00 40.62  ? 2676 THR A CB    1 
ATOM   10530 O OG1   . THR A 1 2676 ? 158.317 183.589 168.322 1.00 40.62  ? 2676 THR A OG1   1 
ATOM   10531 C CG2   . THR A 1 2676 ? 159.846 182.528 166.814 1.00 40.62  ? 2676 THR A CG2   1 
ATOM   10532 N N     . GLN A 1 2677 ? 156.268 181.777 167.198 1.00 34.84  ? 2677 GLN A N     1 
ATOM   10533 C CA    . GLN A 1 2677 ? 155.259 181.831 166.149 1.00 34.84  ? 2677 GLN A CA    1 
ATOM   10534 C C     . GLN A 1 2677 ? 155.260 183.232 165.555 1.00 34.84  ? 2677 GLN A C     1 
ATOM   10535 O O     . GLN A 1 2677 ? 155.098 184.217 166.282 1.00 34.84  ? 2677 GLN A O     1 
ATOM   10536 C CB    . GLN A 1 2677 ? 153.880 181.469 166.696 1.00 34.84  ? 2677 GLN A CB    1 
ATOM   10537 C CG    . GLN A 1 2677 ? 153.875 180.222 167.562 1.00 34.84  ? 2677 GLN A CG    1 
ATOM   10538 C CD    . GLN A 1 2677 ? 152.514 179.929 168.155 1.00 34.84  ? 2677 GLN A CD    1 
ATOM   10539 O OE1   . GLN A 1 2677 ? 151.493 180.043 167.480 1.00 34.84  ? 2677 GLN A OE1   1 
ATOM   10540 N NE2   . GLN A 1 2677 ? 152.494 179.547 169.425 1.00 34.84  ? 2677 GLN A NE2   1 
ATOM   10541 N N     . ARG A 1 2678 ? 155.445 183.314 164.237 1.00 28.03  ? 2678 ARG A N     1 
ATOM   10542 C CA    . ARG A 1 2678 ? 155.594 184.612 163.588 1.00 28.03  ? 2678 ARG A CA    1 
ATOM   10543 C C     . ARG A 1 2678 ? 154.325 185.448 163.708 1.00 28.03  ? 2678 ARG A C     1 
ATOM   10544 O O     . ARG A 1 2678 ? 154.388 186.648 164.003 1.00 28.03  ? 2678 ARG A O     1 
ATOM   10545 C CB    . ARG A 1 2678 ? 155.978 184.410 162.123 1.00 28.03  ? 2678 ARG A CB    1 
ATOM   10546 C CG    . ARG A 1 2678 ? 156.320 185.684 161.381 1.00 28.03  ? 2678 ARG A CG    1 
ATOM   10547 C CD    . ARG A 1 2678 ? 157.007 185.431 160.036 1.00 28.03  ? 2678 ARG A CD    1 
ATOM   10548 N NE    . ARG A 1 2678 ? 158.410 185.048 160.162 1.00 28.03  ? 2678 ARG A NE    1 
ATOM   10549 C CZ    . ARG A 1 2678 ? 158.851 183.816 160.385 1.00 28.03  ? 2678 ARG A CZ    1 
ATOM   10550 N NH1   . ARG A 1 2678 ? 158.027 182.784 160.445 1.00 28.03  ? 2678 ARG A NH1   1 
ATOM   10551 N NH2   . ARG A 1 2678 ? 160.157 183.613 160.532 1.00 28.03  ? 2678 ARG A NH2   1 
ATOM   10552 N N     . VAL A 1 2679 ? 153.162 184.831 163.496 1.00 29.57  ? 2679 VAL A N     1 
ATOM   10553 C CA    . VAL A 1 2679 ? 151.908 185.574 163.568 1.00 29.57  ? 2679 VAL A CA    1 
ATOM   10554 C C     . VAL A 1 2679 ? 151.623 186.011 165.001 1.00 29.57  ? 2679 VAL A C     1 
ATOM   10555 O O     . VAL A 1 2679 ? 151.106 187.110 165.237 1.00 29.57  ? 2679 VAL A O     1 
ATOM   10556 C CB    . VAL A 1 2679 ? 150.756 184.740 162.977 1.00 29.57  ? 2679 VAL A CB    1 
ATOM   10557 C CG1   . VAL A 1 2679 ? 150.584 183.432 163.734 1.00 29.57  ? 2679 VAL A CG1   1 
ATOM   10558 C CG2   . VAL A 1 2679 ? 149.465 185.539 162.985 1.00 29.57  ? 2679 VAL A CG2   1 
ATOM   10559 N N     . ILE A 1 2680 ? 151.957 185.167 165.979 1.00 27.58  ? 2680 ILE A N     1 
ATOM   10560 C CA    . ILE A 1 2680 ? 151.751 185.535 167.376 1.00 27.58  ? 2680 ILE A CA    1 
ATOM   10561 C C     . ILE A 1 2680 ? 152.616 186.734 167.741 1.00 27.58  ? 2680 ILE A C     1 
ATOM   10562 O O     . ILE A 1 2680 ? 152.161 187.664 168.417 1.00 27.58  ? 2680 ILE A O     1 
ATOM   10563 C CB    . ILE A 1 2680 ? 152.030 184.330 168.293 1.00 27.58  ? 2680 ILE A CB    1 
ATOM   10564 C CG1   . ILE A 1 2680 ? 150.963 183.253 168.095 1.00 27.58  ? 2680 ILE A CG1   1 
ATOM   10565 C CG2   . ILE A 1 2680 ? 152.080 184.765 169.748 1.00 27.58  ? 2680 ILE A CG2   1 
ATOM   10566 C CD1   . ILE A 1 2680 ? 149.549 183.782 168.125 1.00 27.58  ? 2680 ILE A CD1   1 
ATOM   10567 N N     . SER A 1 2681 ? 153.873 186.736 167.293 1.00 27.47  ? 2681 SER A N     1 
ATOM   10568 C CA    . SER A 1 2681 ? 154.745 187.878 167.543 1.00 27.47  ? 2681 SER A CA    1 
ATOM   10569 C C     . SER A 1 2681 ? 154.229 189.128 166.843 1.00 27.47  ? 2681 SER A C     1 
ATOM   10570 O O     . SER A 1 2681 ? 154.322 190.235 167.385 1.00 27.47  ? 2681 SER A O     1 
ATOM   10571 C CB    . SER A 1 2681 ? 156.171 187.562 167.096 1.00 27.47  ? 2681 SER A CB    1 
ATOM   10572 O OG    . SER A 1 2681 ? 156.752 186.564 167.916 1.00 27.47  ? 2681 SER A OG    1 
ATOM   10573 N N     . PHE A 1 2682 ? 153.687 188.973 165.633 1.00 28.70  ? 2682 PHE A N     1 
ATOM   10574 C CA    . PHE A 1 2682 ? 153.124 190.116 164.920 1.00 28.70  ? 2682 PHE A CA    1 
ATOM   10575 C C     . PHE A 1 2682 ? 151.957 190.721 165.695 1.00 28.70  ? 2682 PHE A C     1 
ATOM   10576 O O     . PHE A 1 2682 ? 151.867 191.946 165.858 1.00 28.70  ? 2682 PHE A O     1 
ATOM   10577 C CB    . PHE A 1 2682 ? 152.681 189.681 163.523 1.00 28.70  ? 2682 PHE A CB    1 
ATOM   10578 C CG    . PHE A 1 2682 ? 152.471 190.818 162.569 1.00 28.70  ? 2682 PHE A CG    1 
ATOM   10579 C CD1   . PHE A 1 2682 ? 153.341 191.891 162.549 1.00 28.70  ? 2682 PHE A CD1   1 
ATOM   10580 C CD2   . PHE A 1 2682 ? 151.406 190.810 161.687 1.00 28.70  ? 2682 PHE A CD2   1 
ATOM   10581 C CE1   . PHE A 1 2682 ? 153.154 192.936 161.667 1.00 28.70  ? 2682 PHE A CE1   1 
ATOM   10582 C CE2   . PHE A 1 2682 ? 151.214 191.851 160.802 1.00 28.70  ? 2682 PHE A CE2   1 
ATOM   10583 C CZ    . PHE A 1 2682 ? 152.089 192.915 160.792 1.00 28.70  ? 2682 PHE A CZ    1 
ATOM   10584 N N     . ILE A 1 2683 ? 151.055 189.869 166.188 1.00 26.63  ? 2683 ILE A N     1 
ATOM   10585 C CA    . ILE A 1 2683 ? 149.922 190.352 166.975 1.00 26.63  ? 2683 ILE A CA    1 
ATOM   10586 C C     . ILE A 1 2683 ? 150.404 191.009 168.261 1.00 26.63  ? 2683 ILE A C     1 
ATOM   10587 O O     . ILE A 1 2683 ? 149.877 192.046 168.678 1.00 26.63  ? 2683 ILE A O     1 
ATOM   10588 C CB    . ILE A 1 2683 ? 148.932 189.208 167.264 1.00 26.63  ? 2683 ILE A CB    1 
ATOM   10589 C CG1   . ILE A 1 2683 ? 148.461 188.561 165.963 1.00 26.63  ? 2683 ILE A CG1   1 
ATOM   10590 C CG2   . ILE A 1 2683 ? 147.745 189.716 168.065 1.00 26.63  ? 2683 ILE A CG2   1 
ATOM   10591 C CD1   . ILE A 1 2683 ? 147.625 187.322 166.174 1.00 26.63  ? 2683 ILE A CD1   1 
ATOM   10592 N N     . ARG A 1 2684 ? 151.405 190.414 168.914 1.00 24.77  ? 2684 ARG A N     1 
ATOM   10593 C CA    . ARG A 1 2684 ? 151.934 190.999 170.141 1.00 24.77  ? 2684 ARG A CA    1 
ATOM   10594 C C     . ARG A 1 2684 ? 152.515 192.383 169.884 1.00 24.77  ? 2684 ARG A C     1 
ATOM   10595 O O     . ARG A 1 2684 ? 152.292 193.315 170.667 1.00 24.77  ? 2684 ARG A O     1 
ATOM   10596 C CB    . ARG A 1 2684 ? 152.985 190.069 170.748 1.00 24.77  ? 2684 ARG A CB    1 
ATOM   10597 C CG    . ARG A 1 2684 ? 153.596 190.562 172.048 1.00 24.77  ? 2684 ARG A CG    1 
ATOM   10598 C CD    . ARG A 1 2684 ? 154.946 191.217 171.806 1.00 24.77  ? 2684 ARG A CD    1 
ATOM   10599 N NE    . ARG A 1 2684 ? 155.619 191.568 173.049 1.00 24.77  ? 2684 ARG A NE    1 
ATOM   10600 C CZ    . ARG A 1 2684 ? 156.734 192.283 173.115 1.00 24.77  ? 2684 ARG A CZ    1 
ATOM   10601 N NH1   . ARG A 1 2684 ? 157.334 192.728 172.024 1.00 24.77  ? 2684 ARG A NH1   1 
ATOM   10602 N NH2   . ARG A 1 2684 ? 157.256 192.560 174.305 1.00 24.77  ? 2684 ARG A NH2   1 
ATOM   10603 N N     . GLN A 1 2685 ? 153.263 192.536 168.789 1.00 27.75  ? 2685 GLN A N     1 
ATOM   10604 C CA    . GLN A 1 2685 ? 153.829 193.837 168.450 1.00 27.75  ? 2685 GLN A CA    1 
ATOM   10605 C C     . GLN A 1 2685 ? 152.733 194.854 168.164 1.00 27.75  ? 2685 GLN A C     1 
ATOM   10606 O O     . GLN A 1 2685 ? 152.790 195.995 168.636 1.00 27.75  ? 2685 GLN A O     1 
ATOM   10607 C CB    . GLN A 1 2685 ? 154.765 193.708 167.249 1.00 27.75  ? 2685 GLN A CB    1 
ATOM   10608 C CG    . GLN A 1 2685 ? 155.016 195.022 166.528 1.00 27.75  ? 2685 GLN A CG    1 
ATOM   10609 C CD    . GLN A 1 2685 ? 155.600 194.829 165.145 1.00 27.75  ? 2685 GLN A CD    1 
ATOM   10610 O OE1   . GLN A 1 2685 ? 155.009 194.162 164.297 1.00 27.75  ? 2685 GLN A OE1   1 
ATOM   10611 N NE2   . GLN A 1 2685 ? 156.764 195.420 164.907 1.00 27.75  ? 2685 GLN A NE2   1 
ATOM   10612 N N     . MET A 1 2686 ? 151.719 194.457 167.396 1.00 30.20  ? 2686 MET A N     1 
ATOM   10613 C CA    . MET A 1 2686 ? 150.660 195.393 167.041 1.00 30.20  ? 2686 MET A CA    1 
ATOM   10614 C C     . MET A 1 2686 ? 149.707 195.685 168.192 1.00 30.20  ? 2686 MET A C     1 
ATOM   10615 O O     . MET A 1 2686 ? 148.959 196.665 168.120 1.00 30.20  ? 2686 MET A O     1 
ATOM   10616 C CB    . MET A 1 2686 ? 149.880 194.872 165.834 1.00 30.20  ? 2686 MET A CB    1 
ATOM   10617 C CG    . MET A 1 2686 ? 150.603 195.106 164.519 1.00 30.20  ? 2686 MET A CG    1 
ATOM   10618 S SD    . MET A 1 2686 ? 149.939 194.158 163.143 1.00 30.20  ? 2686 MET A SD    1 
ATOM   10619 C CE    . MET A 1 2686 ? 148.243 193.971 163.660 1.00 30.20  ? 2686 MET A CE    1 
ATOM   10620 N N     . VAL A 1 2687 ? 149.711 194.870 169.241 1.00 25.12  ? 2687 VAL A N     1 
ATOM   10621 C CA    . VAL A 1 2687 ? 148.879 195.136 170.411 1.00 25.12  ? 2687 VAL A CA    1 
ATOM   10622 C C     . VAL A 1 2687 ? 149.619 195.983 171.437 1.00 25.12  ? 2687 VAL A C     1 
ATOM   10623 O O     . VAL A 1 2687 ? 149.090 196.985 171.926 1.00 25.12  ? 2687 VAL A O     1 
ATOM   10624 C CB    . VAL A 1 2687 ? 148.387 193.809 171.025 1.00 25.12  ? 2687 VAL A CB    1 
ATOM   10625 C CG1   . VAL A 1 2687 ? 147.862 194.037 172.431 1.00 25.12  ? 2687 VAL A CG1   1 
ATOM   10626 C CG2   . VAL A 1 2687 ? 147.308 193.194 170.154 1.00 25.12  ? 2687 VAL A CG2   1 
ATOM   10627 N N     . GLU A 1 2688 ? 150.851 195.601 171.784 1.00 24.94  ? 2688 GLU A N     1 
ATOM   10628 C CA    . GLU A 1 2688 ? 151.585 196.342 172.804 1.00 24.94  ? 2688 GLU A CA    1 
ATOM   10629 C C     . GLU A 1 2688 ? 151.982 197.728 172.308 1.00 24.94  ? 2688 GLU A C     1 
ATOM   10630 O O     . GLU A 1 2688 ? 151.757 198.731 172.995 1.00 24.94  ? 2688 GLU A O     1 
ATOM   10631 C CB    . GLU A 1 2688 ? 152.821 195.558 173.243 1.00 24.94  ? 2688 GLU A CB    1 
ATOM   10632 C CG    . GLU A 1 2688 ? 153.867 196.416 173.936 1.00 24.94  ? 2688 GLU A CG    1 
ATOM   10633 C CD    . GLU A 1 2688 ? 154.758 195.620 174.866 1.00 24.94  ? 2688 GLU A CD    1 
ATOM   10634 O OE1   . GLU A 1 2688 ? 155.133 194.485 174.507 1.00 24.94  ? 2688 GLU A OE1   1 
ATOM   10635 O OE2   . GLU A 1 2688 ? 155.085 196.131 175.958 1.00 24.94  ? 2688 GLU A OE2   1 
ATOM   10636 N N     . HIS A 1 2689 ? 152.570 197.805 171.116 1.00 27.32  ? 2689 HIS A N     1 
ATOM   10637 C CA    . HIS A 1 2689 ? 153.050 199.078 170.593 1.00 27.32  ? 2689 HIS A CA    1 
ATOM   10638 C C     . HIS A 1 2689 ? 151.963 199.886 169.901 1.00 27.32  ? 2689 HIS A C     1 
ATOM   10639 O O     . HIS A 1 2689 ? 152.040 201.120 169.881 1.00 27.32  ? 2689 HIS A O     1 
ATOM   10640 C CB    . HIS A 1 2689 ? 154.211 198.844 169.623 1.00 27.32  ? 2689 HIS A CB    1 
ATOM   10641 C CG    . HIS A 1 2689 ? 155.360 198.102 170.228 1.00 27.32  ? 2689 HIS A CG    1 
ATOM   10642 N ND1   . HIS A 1 2689 ? 155.896 196.967 169.660 1.00 27.32  ? 2689 HIS A ND1   1 
ATOM   10643 C CD2   . HIS A 1 2689 ? 156.076 198.333 171.353 1.00 27.32  ? 2689 HIS A CD2   1 
ATOM   10644 C CE1   . HIS A 1 2689 ? 156.892 196.530 170.409 1.00 27.32  ? 2689 HIS A CE1   1 
ATOM   10645 N NE2   . HIS A 1 2689 ? 157.022 197.341 171.443 1.00 27.32  ? 2689 HIS A NE2   1 
ATOM   10646 N N     . GLY A 1 2690 ? 150.957 199.228 169.337 1.00 30.76  ? 2690 GLY A N     1 
ATOM   10647 C CA    . GLY A 1 2690 ? 149.884 199.913 168.651 1.00 30.76  ? 2690 GLY A CA    1 
ATOM   10648 C C     . GLY A 1 2690 ? 150.067 200.080 167.161 1.00 30.76  ? 2690 GLY A C     1 
ATOM   10649 O O     . GLY A 1 2690 ? 149.275 200.795 166.537 1.00 30.76  ? 2690 GLY A O     1 
ATOM   10650 N N     . GLY A 1 2691 ? 151.075 199.452 166.574 1.00 31.91  ? 2691 GLY A N     1 
ATOM   10651 C CA    . GLY A 1 2691 ? 151.296 199.578 165.150 1.00 31.91  ? 2691 GLY A CA    1 
ATOM   10652 C C     . GLY A 1 2691 ? 152.324 198.578 164.676 1.00 31.91  ? 2691 GLY A C     1 
ATOM   10653 O O     . GLY A 1 2691 ? 152.709 197.660 165.403 1.00 31.91  ? 2691 GLY A O     1 
ATOM   10654 N N     . PHE A 1 2692 ? 152.767 198.767 163.436 1.00 36.16  ? 2692 PHE A N     1 
ATOM   10655 C CA    . PHE A 1 2692 ? 153.769 197.892 162.847 1.00 36.16  ? 2692 PHE A CA    1 
ATOM   10656 C C     . PHE A 1 2692 ? 154.478 198.632 161.723 1.00 36.16  ? 2692 PHE A C     1 
ATOM   10657 O O     . PHE A 1 2692 ? 154.088 199.734 161.330 1.00 36.16  ? 2692 PHE A O     1 
ATOM   10658 C CB    . PHE A 1 2692 ? 153.145 196.584 162.342 1.00 36.16  ? 2692 PHE A CB    1 
ATOM   10659 C CG    . PHE A 1 2692 ? 152.183 196.764 161.200 1.00 36.16  ? 2692 PHE A CG    1 
ATOM   10660 C CD1   . PHE A 1 2692 ? 152.607 196.634 159.888 1.00 36.16  ? 2692 PHE A CD1   1 
ATOM   10661 C CD2   . PHE A 1 2692 ? 150.852 197.055 161.440 1.00 36.16  ? 2692 PHE A CD2   1 
ATOM   10662 C CE1   . PHE A 1 2692 ? 151.722 196.795 158.840 1.00 36.16  ? 2692 PHE A CE1   1 
ATOM   10663 C CE2   . PHE A 1 2692 ? 149.963 197.217 160.396 1.00 36.16  ? 2692 PHE A CE2   1 
ATOM   10664 C CZ    . PHE A 1 2692 ? 150.399 197.087 159.095 1.00 36.16  ? 2692 PHE A CZ    1 
ATOM   10665 N N     . TYR A 1 2693 ? 155.542 198.015 161.219 1.00 37.19  ? 2693 TYR A N     1 
ATOM   10666 C CA    . TYR A 1 2693 ? 156.308 198.562 160.109 1.00 37.19  ? 2693 TYR A CA    1 
ATOM   10667 C C     . TYR A 1 2693 ? 155.872 197.892 158.813 1.00 37.19  ? 2693 TYR A C     1 
ATOM   10668 O O     . TYR A 1 2693 ? 155.941 196.665 158.691 1.00 37.19  ? 2693 TYR A O     1 
ATOM   10669 C CB    . TYR A 1 2693 ? 157.807 198.346 160.329 1.00 37.19  ? 2693 TYR A CB    1 
ATOM   10670 C CG    . TYR A 1 2693 ? 158.464 199.372 161.223 1.00 37.19  ? 2693 TYR A CG    1 
ATOM   10671 C CD1   . TYR A 1 2693 ? 158.553 200.702 160.840 1.00 37.19  ? 2693 TYR A CD1   1 
ATOM   10672 C CD2   . TYR A 1 2693 ? 159.002 199.007 162.449 1.00 37.19  ? 2693 TYR A CD2   1 
ATOM   10673 C CE1   . TYR A 1 2693 ? 159.156 201.640 161.653 1.00 37.19  ? 2693 TYR A CE1   1 
ATOM   10674 C CE2   . TYR A 1 2693 ? 159.607 199.938 163.269 1.00 37.19  ? 2693 TYR A CE2   1 
ATOM   10675 C CZ    . TYR A 1 2693 ? 159.681 201.253 162.866 1.00 37.19  ? 2693 TYR A CZ    1 
ATOM   10676 O OH    . TYR A 1 2693 ? 160.282 202.185 163.680 1.00 37.19  ? 2693 TYR A OH    1 
ATOM   10677 N N     . ARG A 1 2694 ? 155.423 198.694 157.851 1.00 50.15  ? 2694 ARG A N     1 
ATOM   10678 C CA    . ARG A 1 2694 ? 155.060 198.162 156.544 1.00 50.15  ? 2694 ARG A CA    1 
ATOM   10679 C C     . ARG A 1 2694 ? 156.325 197.990 155.710 1.00 50.15  ? 2694 ARG A C     1 
ATOM   10680 O O     . ARG A 1 2694 ? 157.190 198.871 155.690 1.00 50.15  ? 2694 ARG A O     1 
ATOM   10681 C CB    . ARG A 1 2694 ? 154.050 199.069 155.842 1.00 50.15  ? 2694 ARG A CB    1 
ATOM   10682 C CG    . ARG A 1 2694 ? 154.566 200.440 155.443 1.00 50.15  ? 2694 ARG A CG    1 
ATOM   10683 C CD    . ARG A 1 2694 ? 153.469 201.263 154.785 1.00 50.15  ? 2694 ARG A CD    1 
ATOM   10684 N NE    . ARG A 1 2694 ? 153.966 202.537 154.283 1.00 50.15  ? 2694 ARG A NE    1 
ATOM   10685 C CZ    . ARG A 1 2694 ? 153.209 203.472 153.727 1.00 50.15  ? 2694 ARG A CZ    1 
ATOM   10686 N NH1   . ARG A 1 2694 ? 151.905 203.306 153.575 1.00 50.15  ? 2694 ARG A NH1   1 
ATOM   10687 N NH2   . ARG A 1 2694 ? 153.773 204.603 153.313 1.00 50.15  ? 2694 ARG A NH2   1 
ATOM   10688 N N     . THR A 1 2695 ? 156.442 196.843 155.041 1.00 54.09  ? 2695 THR A N     1 
ATOM   10689 C CA    . THR A 1 2695 ? 157.650 196.533 154.287 1.00 54.09  ? 2695 THR A CA    1 
ATOM   10690 C C     . THR A 1 2695 ? 157.734 197.279 152.963 1.00 54.09  ? 2695 THR A C     1 
ATOM   10691 O O     . THR A 1 2695 ? 158.770 197.196 152.294 1.00 54.09  ? 2695 THR A O     1 
ATOM   10692 C CB    . THR A 1 2695 ? 157.738 195.027 154.035 1.00 54.09  ? 2695 THR A CB    1 
ATOM   10693 O OG1   . THR A 1 2695 ? 156.558 194.587 153.351 1.00 54.09  ? 2695 THR A OG1   1 
ATOM   10694 C CG2   . THR A 1 2695 ? 157.865 194.276 155.351 1.00 54.09  ? 2695 THR A CG2   1 
ATOM   10695 N N     . SER A 1 2696 ? 156.680 197.993 152.566 1.00 55.10  ? 2696 SER A N     1 
ATOM   10696 C CA    . SER A 1 2696 ? 156.700 198.694 151.286 1.00 55.10  ? 2696 SER A CA    1 
ATOM   10697 C C     . SER A 1 2696 ? 157.729 199.819 151.285 1.00 55.10  ? 2696 SER A C     1 
ATOM   10698 O O     . SER A 1 2696 ? 158.557 199.915 150.372 1.00 55.10  ? 2696 SER A O     1 
ATOM   10699 C CB    . SER A 1 2696 ? 155.308 199.238 150.966 1.00 55.10  ? 2696 SER A CB    1 
ATOM   10700 O OG    . SER A 1 2696 ? 155.064 200.447 151.662 1.00 55.10  ? 2696 SER A OG    1 
ATOM   10701 N N     . ASP A 1 2697 ? 157.696 200.680 152.305 1.00 54.98  ? 2697 ASP A N     1 
ATOM   10702 C CA    . ASP A 1 2697 ? 158.622 201.802 152.393 1.00 54.98  ? 2697 ASP A CA    1 
ATOM   10703 C C     . ASP A 1 2697 ? 159.260 201.937 153.771 1.00 54.98  ? 2697 ASP A C     1 
ATOM   10704 O O     . ASP A 1 2697 ? 159.919 202.949 154.035 1.00 54.98  ? 2697 ASP A O     1 
ATOM   10705 C CB    . ASP A 1 2697 ? 157.922 203.112 152.014 1.00 54.98  ? 2697 ASP A CB    1 
ATOM   10706 C CG    . ASP A 1 2697 ? 156.703 203.393 152.869 1.00 54.98  ? 2697 ASP A CG    1 
ATOM   10707 O OD1   . ASP A 1 2697 ? 156.326 202.521 153.679 1.00 54.98  ? 2697 ASP A OD1   1 
ATOM   10708 O OD2   . ASP A 1 2697 ? 156.121 204.489 152.734 1.00 54.98  ? 2697 ASP A OD2   1 
ATOM   10709 N N     . GLN A 1 2698 ? 159.076 200.951 154.651 1.00 50.49  ? 2698 GLN A N     1 
ATOM   10710 C CA    . GLN A 1 2698 ? 159.722 200.923 155.964 1.00 50.49  ? 2698 GLN A CA    1 
ATOM   10711 C C     . GLN A 1 2698 ? 159.376 202.159 156.792 1.00 50.49  ? 2698 GLN A C     1 
ATOM   10712 O O     . GLN A 1 2698 ? 160.254 202.926 157.192 1.00 50.49  ? 2698 GLN A O     1 
ATOM   10713 C CB    . GLN A 1 2698 ? 161.238 200.766 155.829 1.00 50.49  ? 2698 GLN A CB    1 
ATOM   10714 C CG    . GLN A 1 2698 ? 161.667 199.422 155.269 1.00 50.49  ? 2698 GLN A CG    1 
ATOM   10715 C CD    . GLN A 1 2698 ? 161.908 199.462 153.774 1.00 50.49  ? 2698 GLN A CD    1 
ATOM   10716 O OE1   . GLN A 1 2698 ? 161.897 200.528 153.160 1.00 50.49  ? 2698 GLN A OE1   1 
ATOM   10717 N NE2   . GLN A 1 2698 ? 162.128 198.296 153.180 1.00 50.49  ? 2698 GLN A NE2   1 
ATOM   10718 N N     . THR A 1 2699 ? 158.088 202.355 157.051 1.00 45.33  ? 2699 THR A N     1 
ATOM   10719 C CA    . THR A 1 2699 ? 157.617 203.412 157.930 1.00 45.33  ? 2699 THR A CA    1 
ATOM   10720 C C     . THR A 1 2699 ? 156.651 202.834 158.955 1.00 45.33  ? 2699 THR A C     1 
ATOM   10721 O O     . THR A 1 2699 ? 156.049 201.778 158.742 1.00 45.33  ? 2699 THR A O     1 
ATOM   10722 C CB    . THR A 1 2699 ? 156.937 204.539 157.145 1.00 45.33  ? 2699 THR A CB    1 
ATOM   10723 O OG1   . THR A 1 2699 ? 156.735 205.666 158.007 1.00 45.33  ? 2699 THR A OG1   1 
ATOM   10724 C CG2   . THR A 1 2699 ? 155.597 204.082 156.607 1.00 45.33  ? 2699 THR A CG2   1 
ATOM   10725 N N     . TRP A 1 2700 ? 156.515 203.533 160.078 1.00 37.88  ? 2700 TRP A N     1 
ATOM   10726 C CA    . TRP A 1 2700 ? 155.717 203.054 161.201 1.00 37.88  ? 2700 TRP A CA    1 
ATOM   10727 C C     . TRP A 1 2700 ? 154.267 203.477 160.999 1.00 37.88  ? 2700 TRP A C     1 
ATOM   10728 O O     . TRP A 1 2700 ? 153.933 204.658 161.137 1.00 37.88  ? 2700 TRP A O     1 
ATOM   10729 C CB    . TRP A 1 2700 ? 156.267 203.596 162.517 1.00 37.88  ? 2700 TRP A CB    1 
ATOM   10730 C CG    . TRP A 1 2700 ? 155.467 203.191 163.710 1.00 37.88  ? 2700 TRP A CG    1 
ATOM   10731 C CD1   . TRP A 1 2700 ? 154.544 203.943 164.373 1.00 37.88  ? 2700 TRP A CD1   1 
ATOM   10732 C CD2   . TRP A 1 2700 ? 155.519 201.931 164.388 1.00 37.88  ? 2700 TRP A CD2   1 
ATOM   10733 N NE1   . TRP A 1 2700 ? 154.017 203.230 165.422 1.00 37.88  ? 2700 TRP A NE1   1 
ATOM   10734 C CE2   . TRP A 1 2700 ? 154.600 201.991 165.452 1.00 37.88  ? 2700 TRP A CE2   1 
ATOM   10735 C CE3   . TRP A 1 2700 ? 156.255 200.758 164.198 1.00 37.88  ? 2700 TRP A CE3   1 
ATOM   10736 C CZ2   . TRP A 1 2700 ? 154.397 200.925 166.323 1.00 37.88  ? 2700 TRP A CZ2   1 
ATOM   10737 C CZ3   . TRP A 1 2700 ? 156.052 199.701 165.063 1.00 37.88  ? 2700 TRP A CZ3   1 
ATOM   10738 C CH2   . TRP A 1 2700 ? 155.132 199.791 166.112 1.00 37.88  ? 2700 TRP A CH2   1 
ATOM   10739 N N     . VAL A 1 2701 ? 153.410 202.517 160.674 1.00 38.87  ? 2701 VAL A N     1 
ATOM   10740 C CA    . VAL A 1 2701 ? 151.979 202.766 160.548 1.00 38.87  ? 2701 VAL A CA    1 
ATOM   10741 C C     . VAL A 1 2701 ? 151.319 202.502 161.893 1.00 38.87  ? 2701 VAL A C     1 
ATOM   10742 O O     . VAL A 1 2701 ? 151.718 201.593 162.631 1.00 38.87  ? 2701 VAL A O     1 
ATOM   10743 C CB    . VAL A 1 2701 ? 151.361 201.903 159.430 1.00 38.87  ? 2701 VAL A CB    1 
ATOM   10744 C CG1   . VAL A 1 2701 ? 152.093 202.137 158.120 1.00 38.87  ? 2701 VAL A CG1   1 
ATOM   10745 C CG2   . VAL A 1 2701 ? 151.389 200.432 159.795 1.00 38.87  ? 2701 VAL A CG2   1 
ATOM   10746 N N     . LYS A 1 2702 ? 150.322 203.312 162.230 1.00 37.89  ? 2702 LYS A N     1 
ATOM   10747 C CA    . LYS A 1 2702 ? 149.650 203.237 163.520 1.00 37.89  ? 2702 LYS A CA    1 
ATOM   10748 C C     . LYS A 1 2702 ? 148.226 202.736 163.331 1.00 37.89  ? 2702 LYS A C     1 
ATOM   10749 O O     . LYS A 1 2702 ? 147.490 203.247 162.481 1.00 37.89  ? 2702 LYS A O     1 
ATOM   10750 C CB    . LYS A 1 2702 ? 149.644 204.600 164.215 1.00 37.89  ? 2702 LYS A CB    1 
ATOM   10751 C CG    . LYS A 1 2702 ? 149.002 204.586 165.592 1.00 37.89  ? 2702 LYS A CG    1 
ATOM   10752 C CD    . LYS A 1 2702 ? 149.253 205.886 166.335 1.00 37.89  ? 2702 LYS A CD    1 
ATOM   10753 C CE    . LYS A 1 2702 ? 148.012 206.763 166.344 1.00 37.89  ? 2702 LYS A CE    1 
ATOM   10754 N NZ    . LYS A 1 2702 ? 146.949 206.208 167.226 1.00 37.89  ? 2702 LYS A NZ    1 
ATOM   10755 N N     . LEU A 1 2703 ? 147.847 201.736 164.120 1.00 37.25  ? 2703 LEU A N     1 
ATOM   10756 C CA    . LEU A 1 2703 ? 146.500 201.187 164.047 1.00 37.25  ? 2703 LEU A CA    1 
ATOM   10757 C C     . LEU A 1 2703 ? 145.518 202.067 164.809 1.00 37.25  ? 2703 LEU A C     1 
ATOM   10758 O O     . LEU A 1 2703 ? 145.788 202.486 165.938 1.00 37.25  ? 2703 LEU A O     1 
ATOM   10759 C CB    . LEU A 1 2703 ? 146.474 199.770 164.618 1.00 37.25  ? 2703 LEU A CB    1 
ATOM   10760 C CG    . LEU A 1 2703 ? 146.719 198.596 163.671 1.00 37.25  ? 2703 LEU A CG    1 
ATOM   10761 C CD1   . LEU A 1 2703 ? 148.155 198.576 163.190 1.00 37.25  ? 2703 LEU A CD1   1 
ATOM   10762 C CD2   . LEU A 1 2703 ? 146.374 197.292 164.367 1.00 37.25  ? 2703 LEU A CD2   1 
ATOM   10763 N N     . GLU A 1 2704 ? 144.377 202.354 164.186 1.00 46.12  ? 2704 GLU A N     1 
ATOM   10764 C CA    . GLU A 1 2704 ? 143.235 202.926 164.884 1.00 46.12  ? 2704 GLU A CA    1 
ATOM   10765 C C     . GLU A 1 2704 ? 141.987 202.176 164.446 1.00 46.12  ? 2704 GLU A C     1 
ATOM   10766 O O     . GLU A 1 2704 ? 141.894 201.738 163.295 1.00 46.12  ? 2704 GLU A O     1 
ATOM   10767 C CB    . GLU A 1 2704 ? 143.080 204.429 164.617 1.00 46.12  ? 2704 GLU A CB    1 
ATOM   10768 C CG    . GLU A 1 2704 ? 142.747 204.796 163.184 1.00 46.12  ? 2704 GLU A CG    1 
ATOM   10769 C CD    . GLU A 1 2704 ? 142.669 206.297 162.972 1.00 46.12  ? 2704 GLU A CD    1 
ATOM   10770 O OE1   . GLU A 1 2704 ? 142.899 207.051 163.941 1.00 46.12  ? 2704 GLU A OE1   1 
ATOM   10771 O OE2   . GLU A 1 2704 ? 142.369 206.723 161.837 1.00 46.12  ? 2704 GLU A OE2   1 
ATOM   10772 N N     . ARG A 1 2705 ? 141.042 202.019 165.372 1.00 43.55  ? 2705 ARG A N     1 
ATOM   10773 C CA    . ARG A 1 2705 ? 139.782 201.322 165.115 1.00 43.55  ? 2705 ARG A CA    1 
ATOM   10774 C C     . ARG A 1 2705 ? 140.014 199.897 164.614 1.00 43.55  ? 2705 ARG A C     1 
ATOM   10775 O O     . ARG A 1 2705 ? 139.318 199.414 163.720 1.00 43.55  ? 2705 ARG A O     1 
ATOM   10776 C CB    . ARG A 1 2705 ? 138.898 202.107 164.144 1.00 43.55  ? 2705 ARG A CB    1 
ATOM   10777 C CG    . ARG A 1 2705 ? 138.370 203.408 164.721 1.00 43.55  ? 2705 ARG A CG    1 
ATOM   10778 C CD    . ARG A 1 2705 ? 137.530 204.161 163.709 1.00 43.55  ? 2705 ARG A CD    1 
ATOM   10779 N NE    . ARG A 1 2705 ? 138.326 204.635 162.584 1.00 43.55  ? 2705 ARG A NE    1 
ATOM   10780 C CZ    . ARG A 1 2705 ? 137.836 205.319 161.560 1.00 43.55  ? 2705 ARG A CZ    1 
ATOM   10781 N NH1   . ARG A 1 2705 ? 136.551 205.623 161.484 1.00 43.55  ? 2705 ARG A NH1   1 
ATOM   10782 N NH2   . ARG A 1 2705 ? 138.656 205.707 160.588 1.00 43.55  ? 2705 ARG A NH2   1 
ATOM   10783 N N     . ILE A 1 2706 ? 140.997 199.215 165.195 1.00 34.46  ? 2706 ILE A N     1 
ATOM   10784 C CA    . ILE A 1 2706 ? 141.254 197.806 164.921 1.00 34.46  ? 2706 ILE A CA    1 
ATOM   10785 C C     . ILE A 1 2706 ? 141.421 197.083 166.250 1.00 34.46  ? 2706 ILE A C     1 
ATOM   10786 O O     . ILE A 1 2706 ? 142.214 197.509 167.097 1.00 34.46  ? 2706 ILE A O     1 
ATOM   10787 C CB    . ILE A 1 2706 ? 142.496 197.611 164.033 1.00 34.46  ? 2706 ILE A CB    1 
ATOM   10788 C CG1   . ILE A 1 2706 ? 142.235 198.152 162.628 1.00 34.46  ? 2706 ILE A CG1   1 
ATOM   10789 C CG2   . ILE A 1 2706 ? 142.873 196.141 163.965 1.00 34.46  ? 2706 ILE A CG2   1 
ATOM   10790 C CD1   . ILE A 1 2706 ? 143.364 197.896 161.657 1.00 34.46  ? 2706 ILE A CD1   1 
ATOM   10791 N N     . GLN A 1 2707 ? 140.677 195.993 166.429 1.00 29.42  ? 2707 GLN A N     1 
ATOM   10792 C CA    . GLN A 1 2707 ? 140.763 195.183 167.634 1.00 29.42  ? 2707 GLN A CA    1 
ATOM   10793 C C     . GLN A 1 2707 ? 141.222 193.784 167.262 1.00 29.42  ? 2707 GLN A C     1 
ATOM   10794 O O     . GLN A 1 2707 ? 141.351 193.449 166.082 1.00 29.42  ? 2707 GLN A O     1 
ATOM   10795 C CB    . GLN A 1 2707 ? 139.421 195.085 168.371 1.00 29.42  ? 2707 GLN A CB    1 
ATOM   10796 C CG    . GLN A 1 2707 ? 138.839 196.404 168.827 1.00 29.42  ? 2707 GLN A CG    1 
ATOM   10797 C CD    . GLN A 1 2707 ? 137.545 196.222 169.594 1.00 29.42  ? 2707 GLN A CD    1 
ATOM   10798 O OE1   . GLN A 1 2707 ? 137.137 195.098 169.882 1.00 29.42  ? 2707 GLN A OE1   1 
ATOM   10799 N NE2   . GLN A 1 2707 ? 136.880 197.326 169.907 1.00 29.42  ? 2707 GLN A NE2   1 
ATOM   10800 N N     . PHE A 1 2708 ? 141.472 192.970 168.282 1.00 22.86  ? 2708 PHE A N     1 
ATOM   10801 C CA    . PHE A 1 2708 ? 141.792 191.562 168.106 1.00 22.86  ? 2708 PHE A CA    1 
ATOM   10802 C C     . PHE A 1 2708 ? 141.042 190.728 169.131 1.00 22.86  ? 2708 PHE A C     1 
ATOM   10803 O O     . PHE A 1 2708 ? 140.940 191.108 170.300 1.00 22.86  ? 2708 PHE A O     1 
ATOM   10804 C CB    . PHE A 1 2708 ? 143.293 191.313 168.225 1.00 22.86  ? 2708 PHE A CB    1 
ATOM   10805 C CG    . PHE A 1 2708 ? 144.059 191.685 166.996 1.00 22.86  ? 2708 PHE A CG    1 
ATOM   10806 C CD1   . PHE A 1 2708 ? 144.141 190.805 165.934 1.00 22.86  ? 2708 PHE A CD1   1 
ATOM   10807 C CD2   . PHE A 1 2708 ? 144.683 192.913 166.893 1.00 22.86  ? 2708 PHE A CD2   1 
ATOM   10808 C CE1   . PHE A 1 2708 ? 144.838 191.137 164.797 1.00 22.86  ? 2708 PHE A CE1   1 
ATOM   10809 C CE2   . PHE A 1 2708 ? 145.382 193.251 165.756 1.00 22.86  ? 2708 PHE A CE2   1 
ATOM   10810 C CZ    . PHE A 1 2708 ? 145.456 192.360 164.707 1.00 22.86  ? 2708 PHE A CZ    1 
ATOM   10811 N N     . VAL A 1 2709 ? 140.501 189.602 168.678 1.00 19.87  ? 2709 VAL A N     1 
ATOM   10812 C CA    . VAL A 1 2709 ? 139.815 188.646 169.538 1.00 19.87  ? 2709 VAL A CA    1 
ATOM   10813 C C     . VAL A 1 2709 ? 140.200 187.248 169.078 1.00 19.87  ? 2709 VAL A C     1 
ATOM   10814 O O     . VAL A 1 2709 ? 140.268 186.979 167.874 1.00 19.87  ? 2709 VAL A O     1 
ATOM   10815 C CB    . VAL A 1 2709 ? 138.284 188.838 169.501 1.00 19.87  ? 2709 VAL A CB    1 
ATOM   10816 C CG1   . VAL A 1 2709 ? 137.607 187.742 170.273 1.00 19.87  ? 2709 VAL A CG1   1 
ATOM   10817 C CG2   . VAL A 1 2709 ? 137.891 190.192 170.067 1.00 19.87  ? 2709 VAL A CG2   1 
ATOM   10818 N N     . GLY A 1 2710 ? 140.456 186.351 170.035 1.00 19.02  ? 2710 GLY A N     1 
ATOM   10819 C CA    . GLY A 1 2710 ? 140.924 185.021 169.721 1.00 19.02  ? 2710 GLY A CA    1 
ATOM   10820 C C     . GLY A 1 2710 ? 140.083 183.948 170.389 1.00 19.02  ? 2710 GLY A C     1 
ATOM   10821 O O     . GLY A 1 2710 ? 139.254 184.220 171.259 1.00 19.02  ? 2710 GLY A O     1 
ATOM   10822 N N     . ALA A 1 2711 ? 140.317 182.713 169.950 1.00 22.25  ? 2711 ALA A N     1 
ATOM   10823 C CA    . ALA A 1 2711 ? 139.672 181.534 170.509 1.00 22.25  ? 2711 ALA A CA    1 
ATOM   10824 C C     . ALA A 1 2711 ? 140.510 180.322 170.131 1.00 22.25  ? 2711 ALA A C     1 
ATOM   10825 O O     . ALA A 1 2711 ? 141.020 180.247 169.012 1.00 22.25  ? 2711 ALA A O     1 
ATOM   10826 C CB    . ALA A 1 2711 ? 138.237 181.378 169.997 1.00 22.25  ? 2711 ALA A CB    1 
ATOM   10827 N N     . CYS A 1 2712 ? 140.657 179.382 171.061 1.00 27.49  ? 2712 CYS A N     1 
ATOM   10828 C CA    . CYS A 1 2712 ? 141.549 178.259 170.810 1.00 27.49  ? 2712 CYS A CA    1 
ATOM   10829 C C     . CYS A 1 2712 ? 141.157 177.073 171.677 1.00 27.49  ? 2712 CYS A C     1 
ATOM   10830 O O     . CYS A 1 2712 ? 140.507 177.221 172.713 1.00 27.49  ? 2712 CYS A O     1 
ATOM   10831 C CB    . CYS A 1 2712 ? 143.008 178.643 171.075 1.00 27.49  ? 2712 CYS A CB    1 
ATOM   10832 S SG    . CYS A 1 2712 ? 143.402 178.868 172.823 1.00 27.49  ? 2712 CYS A SG    1 
ATOM   10833 N N     . ASN A 1 2713 ? 141.564 175.892 171.226 1.00 33.29  ? 2713 ASN A N     1 
ATOM   10834 C CA    . ASN A 1 2713 ? 141.486 174.676 172.014 1.00 33.29  ? 2713 ASN A CA    1 
ATOM   10835 C C     . ASN A 1 2713 ? 142.627 174.645 173.027 1.00 33.29  ? 2713 ASN A C     1 
ATOM   10836 O O     . ASN A 1 2713 ? 143.593 175.403 172.903 1.00 33.29  ? 2713 ASN A O     1 
ATOM   10837 C CB    . ASN A 1 2713 ? 141.542 173.459 171.095 1.00 33.29  ? 2713 ASN A CB    1 
ATOM   10838 C CG    . ASN A 1 2713 ? 140.391 173.421 170.110 1.00 33.29  ? 2713 ASN A CG    1 
ATOM   10839 O OD1   . ASN A 1 2713 ? 140.528 172.919 168.995 1.00 33.29  ? 2713 ASN A OD1   1 
ATOM   10840 N ND2   . ASN A 1 2713 ? 139.248 173.957 170.518 1.00 33.29  ? 2713 ASN A ND2   1 
ATOM   10841 N N     . PRO A 1 2714 ? 142.535 173.800 174.054 1.00 35.95  ? 2714 PRO A N     1 
ATOM   10842 C CA    . PRO A 1 2714 ? 143.600 173.754 175.050 1.00 35.95  ? 2714 PRO A CA    1 
ATOM   10843 C C     . PRO A 1 2714 ? 144.926 173.405 174.403 1.00 35.95  ? 2714 PRO A C     1 
ATOM   10844 O O     . PRO A 1 2714 ? 144.977 172.630 173.430 1.00 35.95  ? 2714 PRO A O     1 
ATOM   10845 C CB    . PRO A 1 2714 ? 143.138 172.651 176.012 1.00 35.95  ? 2714 PRO A CB    1 
ATOM   10846 C CG    . PRO A 1 2714 ? 141.676 172.589 175.846 1.00 35.95  ? 2714 PRO A CG    1 
ATOM   10847 C CD    . PRO A 1 2714 ? 141.407 172.923 174.416 1.00 35.95  ? 2714 PRO A CD    1 
ATOM   10848 N N     . PRO A 1 2715 ? 146.027 173.971 174.901 1.00 38.69  ? 2715 PRO A N     1 
ATOM   10849 C CA    . PRO A 1 2715 ? 147.339 173.670 174.305 1.00 38.69  ? 2715 PRO A CA    1 
ATOM   10850 C C     . PRO A 1 2715 ? 147.739 172.211 174.421 1.00 38.69  ? 2715 PRO A C     1 
ATOM   10851 O O     . PRO A 1 2715 ? 148.563 171.746 173.624 1.00 38.69  ? 2715 PRO A O     1 
ATOM   10852 C CB    . PRO A 1 2715 ? 148.295 174.579 175.088 1.00 38.69  ? 2715 PRO A CB    1 
ATOM   10853 C CG    . PRO A 1 2715 ? 147.605 174.812 176.390 1.00 38.69  ? 2715 PRO A CG    1 
ATOM   10854 C CD    . PRO A 1 2715 ? 146.139 174.851 176.076 1.00 38.69  ? 2715 PRO A CD    1 
ATOM   10855 N N     . THR A 1 2716 ? 147.186 171.475 175.387 1.00 40.78  ? 2716 THR A N     1 
ATOM   10856 C CA    . THR A 1 2716 ? 147.514 170.063 175.537 1.00 40.78  ? 2716 THR A CA    1 
ATOM   10857 C C     . THR A 1 2716 ? 146.975 169.216 174.392 1.00 40.78  ? 2716 THR A C     1 
ATOM   10858 O O     . THR A 1 2716 ? 147.462 168.101 174.182 1.00 40.78  ? 2716 THR A O     1 
ATOM   10859 C CB    . THR A 1 2716 ? 146.974 169.534 176.866 1.00 40.78  ? 2716 THR A CB    1 
ATOM   10860 O OG1   . THR A 1 2716 ? 145.560 169.332 176.762 1.00 40.78  ? 2716 THR A OG1   1 
ATOM   10861 C CG2   . THR A 1 2716 ? 147.256 170.525 177.983 1.00 40.78  ? 2716 THR A CG2   1 
ATOM   10862 N N     . ASP A 1 2717 ? 145.985 169.714 173.656 1.00 41.53  ? 2717 ASP A N     1 
ATOM   10863 C CA    . ASP A 1 2717 ? 145.437 168.967 172.538 1.00 41.53  ? 2717 ASP A CA    1 
ATOM   10864 C C     . ASP A 1 2717 ? 146.475 168.843 171.423 1.00 41.53  ? 2717 ASP A C     1 
ATOM   10865 O O     . ASP A 1 2717 ? 147.368 169.686 171.299 1.00 41.53  ? 2717 ASP A O     1 
ATOM   10866 C CB    . ASP A 1 2717 ? 144.178 169.648 172.010 1.00 41.53  ? 2717 ASP A CB    1 
ATOM   10867 C CG    . ASP A 1 2717 ? 142.966 169.383 172.881 1.00 41.53  ? 2717 ASP A CG    1 
ATOM   10868 O OD1   . ASP A 1 2717 ? 143.147 168.901 174.019 1.00 41.53  ? 2717 ASP A OD1   1 
ATOM   10869 O OD2   . ASP A 1 2717 ? 141.835 169.654 172.428 1.00 41.53  ? 2717 ASP A OD2   1 
ATOM   10870 N N     . PRO A 1 2718 ? 146.392 167.788 170.611 1.00 41.93  ? 2718 PRO A N     1 
ATOM   10871 C CA    . PRO A 1 2718 ? 147.386 167.597 169.547 1.00 41.93  ? 2718 PRO A CA    1 
ATOM   10872 C C     . PRO A 1 2718 ? 147.403 168.763 168.571 1.00 41.93  ? 2718 PRO A C     1 
ATOM   10873 O O     . PRO A 1 2718 ? 146.363 169.326 168.225 1.00 41.93  ? 2718 PRO A O     1 
ATOM   10874 C CB    . PRO A 1 2718 ? 146.931 166.301 168.866 1.00 41.93  ? 2718 PRO A CB    1 
ATOM   10875 C CG    . PRO A 1 2718 ? 146.126 165.592 169.900 1.00 41.93  ? 2718 PRO A CG    1 
ATOM   10876 C CD    . PRO A 1 2718 ? 145.442 166.665 170.686 1.00 41.93  ? 2718 PRO A CD    1 
ATOM   10877 N N     . GLY A 1 2719 ? 148.608 169.124 168.129 1.00 42.81  ? 2719 GLY A N     1 
ATOM   10878 C CA    . GLY A 1 2719 ? 148.795 170.193 167.174 1.00 42.81  ? 2719 GLY A CA    1 
ATOM   10879 C C     . GLY A 1 2719 ? 148.701 171.591 167.744 1.00 42.81  ? 2719 GLY A C     1 
ATOM   10880 O O     . GLY A 1 2719 ? 148.736 172.559 166.973 1.00 42.81  ? 2719 GLY A O     1 
ATOM   10881 N N     . ARG A 1 2720 ? 148.585 171.733 169.061 1.00 40.52  ? 2720 ARG A N     1 
ATOM   10882 C CA    . ARG A 1 2720 ? 148.398 173.030 169.698 1.00 40.52  ? 2720 ARG A CA    1 
ATOM   10883 C C     . ARG A 1 2720 ? 149.682 173.429 170.412 1.00 40.52  ? 2720 ARG A C     1 
ATOM   10884 O O     . ARG A 1 2720 ? 150.192 172.678 171.250 1.00 40.52  ? 2720 ARG A O     1 
ATOM   10885 C CB    . ARG A 1 2720 ? 147.225 172.990 170.677 1.00 40.52  ? 2720 ARG A CB    1 
ATOM   10886 C CG    . ARG A 1 2720 ? 145.965 172.355 170.111 1.00 40.52  ? 2720 ARG A CG    1 
ATOM   10887 C CD    . ARG A 1 2720 ? 145.643 172.904 168.733 1.00 40.52  ? 2720 ARG A CD    1 
ATOM   10888 N NE    . ARG A 1 2720 ? 144.454 172.286 168.162 1.00 40.52  ? 2720 ARG A NE    1 
ATOM   10889 C CZ    . ARG A 1 2720 ? 143.349 172.947 167.852 1.00 40.52  ? 2720 ARG A CZ    1 
ATOM   10890 N NH1   . ARG A 1 2720 ? 143.242 174.249 168.060 1.00 40.52  ? 2720 ARG A NH1   1 
ATOM   10891 N NH2   . ARG A 1 2720 ? 142.323 172.286 167.324 1.00 40.52  ? 2720 ARG A NH2   1 
ATOM   10892 N N     . LYS A 1 2721 ? 150.195 174.608 170.081 1.00 37.41  ? 2721 LYS A N     1 
ATOM   10893 C CA    . LYS A 1 2721 ? 151.418 175.141 170.664 1.00 37.41  ? 2721 LYS A CA    1 
ATOM   10894 C C     . LYS A 1 2721 ? 151.078 176.178 171.718 1.00 37.41  ? 2721 LYS A C     1 
ATOM   10895 O O     . LYS A 1 2721 ? 150.300 177.100 171.435 1.00 37.41  ? 2721 LYS A O     1 
ATOM   10896 C CB    . LYS A 1 2721 ? 152.294 175.769 169.585 1.00 37.41  ? 2721 LYS A CB    1 
ATOM   10897 C CG    . LYS A 1 2721 ? 153.238 174.795 168.901 1.00 37.41  ? 2721 LYS A CG    1 
ATOM   10898 C CD    . LYS A 1 2721 ? 152.492 173.893 167.935 1.00 37.41  ? 2721 LYS A CD    1 
ATOM   10899 C CE    . LYS A 1 2721 ? 151.863 174.694 166.812 1.00 37.41  ? 2721 LYS A CE    1 
ATOM   10900 N NZ    . LYS A 1 2721 ? 151.257 173.820 165.772 1.00 37.41  ? 2721 LYS A NZ    1 
ATOM   10901 N N     . PRO A 1 2722 ? 151.618 176.065 172.931 1.00 30.54  ? 2722 PRO A N     1 
ATOM   10902 C CA    . PRO A 1 2722 ? 151.310 177.059 173.966 1.00 30.54  ? 2722 PRO A CA    1 
ATOM   10903 C C     . PRO A 1 2722 ? 151.755 178.451 173.544 1.00 30.54  ? 2722 PRO A C     1 
ATOM   10904 O O     . PRO A 1 2722 ? 152.814 178.629 172.938 1.00 30.54  ? 2722 PRO A O     1 
ATOM   10905 C CB    . PRO A 1 2722 ? 152.092 176.558 175.185 1.00 30.54  ? 2722 PRO A CB    1 
ATOM   10906 C CG    . PRO A 1 2722 ? 153.169 175.695 174.619 1.00 30.54  ? 2722 PRO A CG    1 
ATOM   10907 C CD    . PRO A 1 2722 ? 152.578 175.054 173.401 1.00 30.54  ? 2722 PRO A CD    1 
ATOM   10908 N N     . LEU A 1 2723 ? 150.931 179.441 173.873 1.00 23.44  ? 2723 LEU A N     1 
ATOM   10909 C CA    . LEU A 1 2723 ? 151.211 180.812 173.478 1.00 23.44  ? 2723 LEU A CA    1 
ATOM   10910 C C     . LEU A 1 2723 ? 152.353 181.391 174.306 1.00 23.44  ? 2723 LEU A C     1 
ATOM   10911 O O     . LEU A 1 2723 ? 152.560 181.025 175.466 1.00 23.44  ? 2723 LEU A O     1 
ATOM   10912 C CB    . LEU A 1 2723 ? 149.959 181.674 173.630 1.00 23.44  ? 2723 LEU A CB    1 
ATOM   10913 C CG    . LEU A 1 2723 ? 148.834 181.385 172.636 1.00 23.44  ? 2723 LEU A CG    1 
ATOM   10914 C CD1   . LEU A 1 2723 ? 147.665 182.327 172.862 1.00 23.44  ? 2723 LEU A CD1   1 
ATOM   10915 C CD2   . LEU A 1 2723 ? 149.344 181.494 171.211 1.00 23.44  ? 2723 LEU A CD2   1 
ATOM   10916 N N     . SER A 1 2724 ? 153.101 182.304 173.692 1.00 19.19  ? 2724 SER A N     1 
ATOM   10917 C CA    . SER A 1 2724 ? 154.229 182.929 174.364 1.00 19.19  ? 2724 SER A CA    1 
ATOM   10918 C C     . SER A 1 2724 ? 153.754 183.794 175.525 1.00 19.19  ? 2724 SER A C     1 
ATOM   10919 O O     . SER A 1 2724 ? 152.695 184.424 175.468 1.00 19.19  ? 2724 SER A O     1 
ATOM   10920 C CB    . SER A 1 2724 ? 155.035 183.774 173.380 1.00 19.19  ? 2724 SER A CB    1 
ATOM   10921 O OG    . SER A 1 2724 ? 154.186 184.616 172.622 1.00 19.19  ? 2724 SER A OG    1 
ATOM   10922 N N     . HIS A 1 2725 ? 154.556 183.816 176.592 1.00 20.87  ? 2725 HIS A N     1 
ATOM   10923 C CA    . HIS A 1 2725 ? 154.194 184.590 177.775 1.00 20.87  ? 2725 HIS A CA    1 
ATOM   10924 C C     . HIS A 1 2725 ? 154.137 186.079 177.466 1.00 20.87  ? 2725 HIS A C     1 
ATOM   10925 O O     . HIS A 1 2725 ? 153.287 186.799 178.002 1.00 20.87  ? 2725 HIS A O     1 
ATOM   10926 C CB    . HIS A 1 2725 ? 155.183 184.314 178.906 1.00 20.87  ? 2725 HIS A CB    1 
ATOM   10927 C CG    . HIS A 1 2725 ? 154.955 183.009 179.601 1.00 20.87  ? 2725 HIS A CG    1 
ATOM   10928 N ND1   . HIS A 1 2725 ? 154.940 181.804 178.933 1.00 20.87  ? 2725 HIS A ND1   1 
ATOM   10929 C CD2   . HIS A 1 2725 ? 154.734 182.720 180.904 1.00 20.87  ? 2725 HIS A CD2   1 
ATOM   10930 C CE1   . HIS A 1 2725 ? 154.718 180.828 179.796 1.00 20.87  ? 2725 HIS A CE1   1 
ATOM   10931 N NE2   . HIS A 1 2725 ? 154.590 181.358 180.999 1.00 20.87  ? 2725 HIS A NE2   1 
ATOM   10932 N N     . ARG A 1 2726 ? 155.037 186.562 176.606 1.00 18.70  ? 2726 ARG A N     1 
ATOM   10933 C CA    . ARG A 1 2726 ? 155.035 187.977 176.254 1.00 18.70  ? 2726 ARG A CA    1 
ATOM   10934 C C     . ARG A 1 2726 ? 153.745 188.376 175.552 1.00 18.70  ? 2726 ARG A C     1 
ATOM   10935 O O     . ARG A 1 2726 ? 153.298 189.521 175.680 1.00 18.70  ? 2726 ARG A O     1 
ATOM   10936 C CB    . ARG A 1 2726 ? 156.242 188.304 175.378 1.00 18.70  ? 2726 ARG A CB    1 
ATOM   10937 C CG    . ARG A 1 2726 ? 157.572 187.895 175.986 1.00 18.70  ? 2726 ARG A CG    1 
ATOM   10938 C CD    . ARG A 1 2726 ? 158.738 188.479 175.210 1.00 18.70  ? 2726 ARG A CD    1 
ATOM   10939 N NE    . ARG A 1 2726 ? 158.949 189.886 175.522 1.00 18.70  ? 2726 ARG A NE    1 
ATOM   10940 C CZ    . ARG A 1 2726 ? 159.853 190.655 174.931 1.00 18.70  ? 2726 ARG A CZ    1 
ATOM   10941 N NH1   . ARG A 1 2726 ? 160.641 190.186 173.979 1.00 18.70  ? 2726 ARG A NH1   1 
ATOM   10942 N NH2   . ARG A 1 2726 ? 159.970 191.925 175.306 1.00 18.70  ? 2726 ARG A NH2   1 
ATOM   10943 N N     . PHE A 1 2727 ? 153.138 187.455 174.805 1.00 16.82  ? 2727 PHE A N     1 
ATOM   10944 C CA    . PHE A 1 2727 ? 151.840 187.711 174.193 1.00 16.82  ? 2727 PHE A CA    1 
ATOM   10945 C C     . PHE A 1 2727 ? 150.693 187.432 175.153 1.00 16.82  ? 2727 PHE A C     1 
ATOM   10946 O O     . PHE A 1 2727 ? 149.707 188.176 175.169 1.00 16.82  ? 2727 PHE A O     1 
ATOM   10947 C CB    . PHE A 1 2727 ? 151.672 186.866 172.929 1.00 16.82  ? 2727 PHE A CB    1 
ATOM   10948 C CG    . PHE A 1 2727 ? 150.272 186.865 172.387 1.00 16.82  ? 2727 PHE A CG    1 
ATOM   10949 C CD1   . PHE A 1 2727 ? 149.680 188.041 171.962 1.00 16.82  ? 2727 PHE A CD1   1 
ATOM   10950 C CD2   . PHE A 1 2727 ? 149.546 185.690 172.307 1.00 16.82  ? 2727 PHE A CD2   1 
ATOM   10951 C CE1   . PHE A 1 2727 ? 148.393 188.043 171.464 1.00 16.82  ? 2727 PHE A CE1   1 
ATOM   10952 C CE2   . PHE A 1 2727 ? 148.260 185.687 171.811 1.00 16.82  ? 2727 PHE A CE2   1 
ATOM   10953 C CZ    . PHE A 1 2727 ? 147.683 186.864 171.390 1.00 16.82  ? 2727 PHE A CZ    1 
ATOM   10954 N N     . LEU A 1 2728 ? 150.805 186.373 175.957 1.00 17.56  ? 2728 LEU A N     1 
ATOM   10955 C CA    . LEU A 1 2728 ? 149.756 186.047 176.917 1.00 17.56  ? 2728 LEU A CA    1 
ATOM   10956 C C     . LEU A 1 2728 ? 149.577 187.132 177.966 1.00 17.56  ? 2728 LEU A C     1 
ATOM   10957 O O     . LEU A 1 2728 ? 148.490 187.247 178.541 1.00 17.56  ? 2728 LEU A O     1 
ATOM   10958 C CB    . LEU A 1 2728 ? 150.062 184.715 177.601 1.00 17.56  ? 2728 LEU A CB    1 
ATOM   10959 C CG    . LEU A 1 2728 ? 149.546 183.458 176.904 1.00 17.56  ? 2728 LEU A CG    1 
ATOM   10960 C CD1   . LEU A 1 2728 ? 149.765 182.242 177.784 1.00 17.56  ? 2728 LEU A CD1   1 
ATOM   10961 C CD2   . LEU A 1 2728 ? 148.079 183.610 176.550 1.00 17.56  ? 2728 LEU A CD2   1 
ATOM   10962 N N     . ARG A 1 2729 ? 150.616 187.926 178.230 1.00 12.23  ? 2729 ARG A N     1 
ATOM   10963 C CA    . ARG A 1 2729 ? 150.504 188.991 179.220 1.00 12.23  ? 2729 ARG A CA    1 
ATOM   10964 C C     . ARG A 1 2729 ? 149.416 189.990 178.849 1.00 12.23  ? 2729 ARG A C     1 
ATOM   10965 O O     . ARG A 1 2729 ? 148.757 190.549 179.733 1.00 12.23  ? 2729 ARG A O     1 
ATOM   10966 C CB    . ARG A 1 2729 ? 151.855 189.691 179.377 1.00 12.23  ? 2729 ARG A CB    1 
ATOM   10967 C CG    . ARG A 1 2729 ? 151.787 191.074 179.990 1.00 12.23  ? 2729 ARG A CG    1 
ATOM   10968 C CD    . ARG A 1 2729 ? 153.138 191.761 179.957 1.00 12.23  ? 2729 ARG A CD    1 
ATOM   10969 N NE    . ARG A 1 2729 ? 153.014 193.195 180.184 1.00 12.23  ? 2729 ARG A NE    1 
ATOM   10970 C CZ    . ARG A 1 2729 ? 153.381 194.123 179.313 1.00 12.23  ? 2729 ARG A CZ    1 
ATOM   10971 N NH1   . ARG A 1 2729 ? 153.919 193.803 178.148 1.00 12.23  ? 2729 ARG A NH1   1 
ATOM   10972 N NH2   . ARG A 1 2729 ? 153.205 195.405 179.618 1.00 12.23  ? 2729 ARG A NH2   1 
ATOM   10973 N N     . HIS A 1 2730 ? 149.195 190.210 177.555 1.00 16.90  ? 2730 HIS A N     1 
ATOM   10974 C CA    . HIS A 1 2730 ? 148.203 191.179 177.108 1.00 16.90  ? 2730 HIS A CA    1 
ATOM   10975 C C     . HIS A 1 2730 ? 146.799 190.602 177.003 1.00 16.90  ? 2730 HIS A C     1 
ATOM   10976 O O     . HIS A 1 2730 ? 145.825 191.337 177.199 1.00 16.90  ? 2730 HIS A O     1 
ATOM   10977 C CB    . HIS A 1 2730 ? 148.602 191.757 175.749 1.00 16.90  ? 2730 HIS A CB    1 
ATOM   10978 C CG    . HIS A 1 2730 ? 149.962 192.378 175.731 1.00 16.90  ? 2730 HIS A CG    1 
ATOM   10979 N ND1   . HIS A 1 2730 ? 150.232 193.593 176.322 1.00 16.90  ? 2730 HIS A ND1   1 
ATOM   10980 C CD2   . HIS A 1 2730 ? 151.129 191.954 175.190 1.00 16.90  ? 2730 HIS A CD2   1 
ATOM   10981 C CE1   . HIS A 1 2730 ? 151.507 193.890 176.147 1.00 16.90  ? 2730 HIS A CE1   1 
ATOM   10982 N NE2   . HIS A 1 2730 ? 152.074 192.912 175.465 1.00 16.90  ? 2730 HIS A NE2   1 
ATOM   10983 N N     . VAL A 1 2731 ? 146.662 189.314 176.701 1.00 15.77  ? 2731 VAL A N     1 
ATOM   10984 C CA    . VAL A 1 2731 ? 145.373 188.723 176.353 1.00 15.77  ? 2731 VAL A CA    1 
ATOM   10985 C C     . VAL A 1 2731 ? 144.860 187.936 177.558 1.00 15.77  ? 2731 VAL A C     1 
ATOM   10986 O O     . VAL A 1 2731 ? 145.461 186.910 177.917 1.00 15.77  ? 2731 VAL A O     1 
ATOM   10987 C CB    . VAL A 1 2731 ? 145.475 187.837 175.103 1.00 15.77  ? 2731 VAL A CB    1 
ATOM   10988 C CG1   . VAL A 1 2731 ? 145.598 188.699 173.866 1.00 15.77  ? 2731 VAL A CG1   1 
ATOM   10989 C CG2   . VAL A 1 2731 ? 146.671 186.908 175.186 1.00 15.77  ? 2731 VAL A CG2   1 
ATOM   10990 N N     . PRO A 1 2732 ? 143.791 188.377 178.216 1.00 15.95  ? 2732 PRO A N     1 
ATOM   10991 C CA    . PRO A 1 2732 ? 143.114 187.506 179.180 1.00 15.95  ? 2732 PRO A CA    1 
ATOM   10992 C C     . PRO A 1 2732 ? 142.445 186.339 178.474 1.00 15.95  ? 2732 PRO A C     1 
ATOM   10993 O O     . PRO A 1 2732 ? 142.017 186.443 177.322 1.00 15.95  ? 2732 PRO A O     1 
ATOM   10994 C CB    . PRO A 1 2732 ? 142.078 188.430 179.829 1.00 15.95  ? 2732 PRO A CB    1 
ATOM   10995 C CG    . PRO A 1 2732 ? 141.869 189.517 178.829 1.00 15.95  ? 2732 PRO A CG    1 
ATOM   10996 C CD    . PRO A 1 2732 ? 143.203 189.725 178.189 1.00 15.95  ? 2732 PRO A CD    1 
ATOM   10997 N N     . VAL A 1 2733 ? 142.357 185.213 179.178 1.00 17.55  ? 2733 VAL A N     1 
ATOM   10998 C CA    . VAL A 1 2733 ? 141.771 183.996 178.629 1.00 17.55  ? 2733 VAL A CA    1 
ATOM   10999 C C     . VAL A 1 2733 ? 140.663 183.519 179.556 1.00 17.55  ? 2733 VAL A C     1 
ATOM   11000 O O     . VAL A 1 2733 ? 140.783 183.619 180.782 1.00 17.55  ? 2733 VAL A O     1 
ATOM   11001 C CB    . VAL A 1 2733 ? 142.824 182.890 178.417 1.00 17.55  ? 2733 VAL A CB    1 
ATOM   11002 C CG1   . VAL A 1 2733 ? 143.818 183.308 177.351 1.00 17.55  ? 2733 VAL A CG1   1 
ATOM   11003 C CG2   . VAL A 1 2733 ? 143.543 182.579 179.709 1.00 17.55  ? 2733 VAL A CG2   1 
ATOM   11004 N N     . VAL A 1 2734 ? 139.580 183.021 178.968 1.00 20.99  ? 2734 VAL A N     1 
ATOM   11005 C CA    . VAL A 1 2734 ? 138.445 182.485 179.707 1.00 20.99  ? 2734 VAL A CA    1 
ATOM   11006 C C     . VAL A 1 2734 ? 138.257 181.029 179.313 1.00 20.99  ? 2734 VAL A C     1 
ATOM   11007 O O     . VAL A 1 2734 ? 138.282 180.677 178.129 1.00 20.99  ? 2734 VAL A O     1 
ATOM   11008 C CB    . VAL A 1 2734 ? 137.154 183.286 179.441 1.00 20.99  ? 2734 VAL A CB    1 
ATOM   11009 C CG1   . VAL A 1 2734 ? 136.024 182.783 180.321 1.00 20.99  ? 2734 VAL A CG1   1 
ATOM   11010 C CG2   . VAL A 1 2734 ? 137.393 184.758 179.667 1.00 20.99  ? 2734 VAL A CG2   1 
ATOM   11011 N N     . TYR A 1 2735 ? 138.070 180.177 180.316 1.00 28.33  ? 2735 TYR A N     1 
ATOM   11012 C CA    . TYR A 1 2735 ? 137.831 178.757 180.093 1.00 28.33  ? 2735 TYR A CA    1 
ATOM   11013 C C     . TYR A 1 2735 ? 136.341 178.549 179.862 1.00 28.33  ? 2735 TYR A C     1 
ATOM   11014 O O     . TYR A 1 2735 ? 135.556 178.520 180.815 1.00 28.33  ? 2735 TYR A O     1 
ATOM   11015 C CB    . TYR A 1 2735 ? 138.320 177.918 181.270 1.00 28.33  ? 2735 TYR A CB    1 
ATOM   11016 C CG    . TYR A 1 2735 ? 138.285 176.435 180.993 1.00 28.33  ? 2735 TYR A CG    1 
ATOM   11017 C CD1   . TYR A 1 2735 ? 138.641 175.935 179.748 1.00 28.33  ? 2735 TYR A CD1   1 
ATOM   11018 C CD2   . TYR A 1 2735 ? 137.889 175.534 181.969 1.00 28.33  ? 2735 TYR A CD2   1 
ATOM   11019 C CE1   . TYR A 1 2735 ? 138.607 174.581 179.485 1.00 28.33  ? 2735 TYR A CE1   1 
ATOM   11020 C CE2   . TYR A 1 2735 ? 137.852 174.178 181.716 1.00 28.33  ? 2735 TYR A CE2   1 
ATOM   11021 C CZ    . TYR A 1 2735 ? 138.214 173.707 180.473 1.00 28.33  ? 2735 TYR A CZ    1 
ATOM   11022 O OH    . TYR A 1 2735 ? 138.180 172.357 180.215 1.00 28.33  ? 2735 TYR A OH    1 
ATOM   11023 N N     . VAL A 1 2736 ? 135.953 178.406 178.597 1.00 25.99  ? 2736 VAL A N     1 
ATOM   11024 C CA    . VAL A 1 2736 ? 134.568 178.104 178.240 1.00 25.99  ? 2736 VAL A CA    1 
ATOM   11025 C C     . VAL A 1 2736 ? 134.479 176.581 178.201 1.00 25.99  ? 2736 VAL A C     1 
ATOM   11026 O O     . VAL A 1 2736 ? 134.816 175.935 177.207 1.00 25.99  ? 2736 VAL A O     1 
ATOM   11027 C CB    . VAL A 1 2736 ? 134.158 178.756 176.922 1.00 25.99  ? 2736 VAL A CB    1 
ATOM   11028 C CG1   . VAL A 1 2736 ? 132.871 178.141 176.390 1.00 25.99  ? 2736 VAL A CG1   1 
ATOM   11029 C CG2   . VAL A 1 2736 ? 133.998 180.255 177.103 1.00 25.99  ? 2736 VAL A CG2   1 
ATOM   11030 N N     . ASP A 1 2737 ? 134.051 175.999 179.315 1.00 28.91  ? 2737 ASP A N     1 
ATOM   11031 C CA    . ASP A 1 2737 ? 133.959 174.554 179.420 1.00 28.91  ? 2737 ASP A CA    1 
ATOM   11032 C C     . ASP A 1 2737 ? 132.644 174.066 178.820 1.00 28.91  ? 2737 ASP A C     1 
ATOM   11033 O O     . ASP A 1 2737 ? 131.813 174.852 178.359 1.00 28.91  ? 2737 ASP A O     1 
ATOM   11034 C CB    . ASP A 1 2737 ? 134.076 174.114 180.880 1.00 28.91  ? 2737 ASP A CB    1 
ATOM   11035 C CG    . ASP A 1 2737 ? 134.573 172.690 181.022 1.00 28.91  ? 2737 ASP A CG    1 
ATOM   11036 O OD1   . ASP A 1 2737 ? 134.892 172.066 179.989 1.00 28.91  ? 2737 ASP A OD1   1 
ATOM   11037 O OD2   . ASP A 1 2737 ? 134.645 172.195 182.166 1.00 28.91  ? 2737 ASP A OD2   1 
ATOM   11038 N N     . TYR A 1 2738 ? 132.466 172.747 178.824 1.00 30.79  ? 2738 TYR A N     1 
ATOM   11039 C CA    . TYR A 1 2738 ? 131.248 172.141 178.304 1.00 30.79  ? 2738 TYR A CA    1 
ATOM   11040 C C     . TYR A 1 2738 ? 130.053 172.629 179.111 1.00 30.79  ? 2738 TYR A C     1 
ATOM   11041 O O     . TYR A 1 2738 ? 130.130 172.707 180.343 1.00 30.79  ? 2738 TYR A O     1 
ATOM   11042 C CB    . TYR A 1 2738 ? 131.336 170.615 178.349 1.00 30.79  ? 2738 TYR A CB    1 
ATOM   11043 C CG    . TYR A 1 2738 ? 132.202 170.017 177.266 1.00 30.79  ? 2738 TYR A CG    1 
ATOM   11044 C CD1   . TYR A 1 2738 ? 131.961 170.292 175.928 1.00 30.79  ? 2738 TYR A CD1   1 
ATOM   11045 C CD2   . TYR A 1 2738 ? 133.255 169.172 177.581 1.00 30.79  ? 2738 TYR A CD2   1 
ATOM   11046 C CE1   . TYR A 1 2738 ? 132.748 169.746 174.934 1.00 30.79  ? 2738 TYR A CE1   1 
ATOM   11047 C CE2   . TYR A 1 2738 ? 134.047 168.621 176.594 1.00 30.79  ? 2738 TYR A CE2   1 
ATOM   11048 C CZ    . TYR A 1 2738 ? 133.789 168.911 175.273 1.00 30.79  ? 2738 TYR A CZ    1 
ATOM   11049 O OH    . TYR A 1 2738 ? 134.575 168.365 174.286 1.00 30.79  ? 2738 TYR A OH    1 
ATOM   11050 N N     . PRO A 1 2739 ? 128.949 172.986 178.458 1.00 31.25  ? 2739 PRO A N     1 
ATOM   11051 C CA    . PRO A 1 2739 ? 127.777 173.467 179.196 1.00 31.25  ? 2739 PRO A CA    1 
ATOM   11052 C C     . PRO A 1 2739 ? 127.293 172.436 180.202 1.00 31.25  ? 2739 PRO A C     1 
ATOM   11053 O O     . PRO A 1 2739 ? 127.267 171.234 179.927 1.00 31.25  ? 2739 PRO A O     1 
ATOM   11054 C CB    . PRO A 1 2739 ? 126.744 173.711 178.092 1.00 31.25  ? 2739 PRO A CB    1 
ATOM   11055 C CG    . PRO A 1 2739 ? 127.557 173.960 176.870 1.00 31.25  ? 2739 PRO A CG    1 
ATOM   11056 C CD    . PRO A 1 2739 ? 128.760 173.074 177.001 1.00 31.25  ? 2739 PRO A CD    1 
ATOM   11057 N N     . GLY A 1 2740 ? 126.908 172.915 181.381 1.00 34.48  ? 2740 GLY A N     1 
ATOM   11058 C CA    . GLY A 1 2740 ? 126.482 172.049 182.452 1.00 34.48  ? 2740 GLY A CA    1 
ATOM   11059 C C     . GLY A 1 2740 ? 125.128 171.433 182.178 1.00 34.48  ? 2740 GLY A C     1 
ATOM   11060 O O     . GLY A 1 2740 ? 124.438 171.793 181.220 1.00 34.48  ? 2740 GLY A O     1 
ATOM   11061 N N     . PRO A 1 2741 ? 124.730 170.470 183.013 1.00 34.84  ? 2741 PRO A N     1 
ATOM   11062 C CA    . PRO A 1 2741 ? 123.404 169.855 182.833 1.00 34.84  ? 2741 PRO A CA    1 
ATOM   11063 C C     . PRO A 1 2741 ? 122.264 170.860 182.843 1.00 34.84  ? 2741 PRO A C     1 
ATOM   11064 O O     . PRO A 1 2741 ? 121.310 170.709 182.075 1.00 34.84  ? 2741 PRO A O     1 
ATOM   11065 C CB    . PRO A 1 2741 ? 123.324 168.875 184.009 1.00 34.84  ? 2741 PRO A CB    1 
ATOM   11066 C CG    . PRO A 1 2741 ? 124.742 168.517 184.286 1.00 34.84  ? 2741 PRO A CG    1 
ATOM   11067 C CD    . PRO A 1 2741 ? 125.535 169.768 184.027 1.00 34.84  ? 2741 PRO A CD    1 
ATOM   11068 N N     . ALA A 1 2742 ? 122.342 171.893 183.684 1.00 37.42  ? 2742 ALA A N     1 
ATOM   11069 C CA    . ALA A 1 2742 ? 121.281 172.896 183.721 1.00 37.42  ? 2742 ALA A CA    1 
ATOM   11070 C C     . ALA A 1 2742 ? 121.203 173.665 182.407 1.00 37.42  ? 2742 ALA A C     1 
ATOM   11071 O O     . ALA A 1 2742 ? 120.119 173.834 181.833 1.00 37.42  ? 2742 ALA A O     1 
ATOM   11072 C CB    . ALA A 1 2742 ? 121.505 173.851 184.894 1.00 37.42  ? 2742 ALA A CB    1 
ATOM   11073 N N     . SER A 1 2743 ? 122.350 174.143 181.917 1.00 37.93  ? 2743 SER A N     1 
ATOM   11074 C CA    . SER A 1 2743 ? 122.366 174.878 180.657 1.00 37.93  ? 2743 SER A CA    1 
ATOM   11075 C C     . SER A 1 2743 ? 121.932 173.993 179.497 1.00 37.93  ? 2743 SER A C     1 
ATOM   11076 O O     . SER A 1 2743 ? 121.187 174.435 178.615 1.00 37.93  ? 2743 SER A O     1 
ATOM   11077 C CB    . SER A 1 2743 ? 123.758 175.453 180.400 1.00 37.93  ? 2743 SER A CB    1 
ATOM   11078 O OG    . SER A 1 2743 ? 124.100 176.420 181.377 1.00 37.93  ? 2743 SER A OG    1 
ATOM   11079 N N     . LEU A 1 2744 ? 122.397 172.741 179.478 1.00 37.61  ? 2744 LEU A N     1 
ATOM   11080 C CA    . LEU A 1 2744 ? 122.000 171.815 178.422 1.00 37.61  ? 2744 LEU A CA    1 
ATOM   11081 C C     . LEU A 1 2744 ? 120.496 171.578 178.442 1.00 37.61  ? 2744 LEU A C     1 
ATOM   11082 O O     . LEU A 1 2744 ? 119.834 171.617 177.397 1.00 37.61  ? 2744 LEU A O     1 
ATOM   11083 C CB    . LEU A 1 2744 ? 122.753 170.494 178.573 1.00 37.61  ? 2744 LEU A CB    1 
ATOM   11084 C CG    . LEU A 1 2744 ? 124.218 170.470 178.139 1.00 37.61  ? 2744 LEU A CG    1 
ATOM   11085 C CD1   . LEU A 1 2744 ? 124.795 169.077 178.310 1.00 37.61  ? 2744 LEU A CD1   1 
ATOM   11086 C CD2   . LEU A 1 2744 ? 124.354 170.931 176.699 1.00 37.61  ? 2744 LEU A CD2   1 
ATOM   11087 N N     . THR A 1 2745 ? 119.937 171.341 179.631 1.00 38.78  ? 2745 THR A N     1 
ATOM   11088 C CA    . THR A 1 2745 ? 118.499 171.131 179.737 1.00 38.78  ? 2745 THR A CA    1 
ATOM   11089 C C     . THR A 1 2745 ? 117.734 172.350 179.255 1.00 38.78  ? 2745 THR A C     1 
ATOM   11090 O O     . THR A 1 2745 ? 116.785 172.219 178.482 1.00 38.78  ? 2745 THR A O     1 
ATOM   11091 C CB    . THR A 1 2745 ? 118.104 170.793 181.175 1.00 38.78  ? 2745 THR A CB    1 
ATOM   11092 O OG1   . THR A 1 2745 ? 118.700 171.736 182.074 1.00 38.78  ? 2745 THR A OG1   1 
ATOM   11093 C CG2   . THR A 1 2745 ? 118.538 169.383 181.539 1.00 38.78  ? 2745 THR A CG2   1 
ATOM   11094 N N     . GLN A 1 2746 ? 118.153 173.548 179.667 1.00 40.14  ? 2746 GLN A N     1 
ATOM   11095 C CA    . GLN A 1 2746 ? 117.442 174.752 179.246 1.00 40.14  ? 2746 GLN A CA    1 
ATOM   11096 C C     . GLN A 1 2746 ? 117.495 174.928 177.732 1.00 40.14  ? 2746 GLN A C     1 
ATOM   11097 O O     . GLN A 1 2746 ? 116.454 175.087 177.076 1.00 40.14  ? 2746 GLN A O     1 
ATOM   11098 C CB    . GLN A 1 2746 ? 118.023 175.977 179.952 1.00 40.14  ? 2746 GLN A CB    1 
ATOM   11099 C CG    . GLN A 1 2746 ? 117.512 177.299 179.409 1.00 40.14  ? 2746 GLN A CG    1 
ATOM   11100 C CD    . GLN A 1 2746 ? 118.159 178.493 180.078 1.00 40.14  ? 2746 GLN A CD    1 
ATOM   11101 O OE1   . GLN A 1 2746 ? 117.898 179.638 179.712 1.00 40.14  ? 2746 GLN A OE1   1 
ATOM   11102 N NE2   . GLN A 1 2746 ? 119.005 178.232 181.067 1.00 40.14  ? 2746 GLN A NE2   1 
ATOM   11103 N N     . ILE A 1 2747 ? 118.699 174.875 177.155 1.00 40.39  ? 2747 ILE A N     1 
ATOM   11104 C CA    . ILE A 1 2747 ? 118.850 175.127 175.725 1.00 40.39  ? 2747 ILE A CA    1 
ATOM   11105 C C     . ILE A 1 2747 ? 118.094 174.089 174.904 1.00 40.39  ? 2747 ILE A C     1 
ATOM   11106 O O     . ILE A 1 2747 ? 117.360 174.431 173.966 1.00 40.39  ? 2747 ILE A O     1 
ATOM   11107 C CB    . ILE A 1 2747 ? 120.343 175.190 175.342 1.00 40.39  ? 2747 ILE A CB    1 
ATOM   11108 C CG1   . ILE A 1 2747 ? 120.504 175.651 173.899 1.00 40.39  ? 2747 ILE A CG1   1 
ATOM   11109 C CG2   . ILE A 1 2747 ? 121.061 173.869 175.562 1.00 40.39  ? 2747 ILE A CG2   1 
ATOM   11110 C CD1   . ILE A 1 2747 ? 121.909 175.997 173.559 1.00 40.39  ? 2747 ILE A CD1   1 
ATOM   11111 N N     . TYR A 1 2748 ? 118.228 172.812 175.249 1.00 40.47  ? 2748 TYR A N     1 
ATOM   11112 C CA    . TYR A 1 2748 ? 117.642 171.812 174.374 1.00 40.47  ? 2748 TYR A CA    1 
ATOM   11113 C C     . TYR A 1 2748 ? 116.174 171.568 174.698 1.00 40.47  ? 2748 TYR A C     1 
ATOM   11114 O O     . TYR A 1 2748 ? 115.432 171.075 173.849 1.00 40.47  ? 2748 TYR A O     1 
ATOM   11115 C CB    . TYR A 1 2748 ? 118.478 170.533 174.427 1.00 40.47  ? 2748 TYR A CB    1 
ATOM   11116 C CG    . TYR A 1 2748 ? 119.822 170.741 173.760 1.00 40.47  ? 2748 TYR A CG    1 
ATOM   11117 C CD1   . TYR A 1 2748 ? 119.898 171.173 172.442 1.00 40.47  ? 2748 TYR A CD1   1 
ATOM   11118 C CD2   . TYR A 1 2748 ? 121.007 170.555 174.455 1.00 40.47  ? 2748 TYR A CD2   1 
ATOM   11119 C CE1   . TYR A 1 2748 ? 121.116 171.382 171.827 1.00 40.47  ? 2748 TYR A CE1   1 
ATOM   11120 C CE2   . TYR A 1 2748 ? 122.232 170.761 173.845 1.00 40.47  ? 2748 TYR A CE2   1 
ATOM   11121 C CZ    . TYR A 1 2748 ? 122.279 171.176 172.532 1.00 40.47  ? 2748 TYR A CZ    1 
ATOM   11122 O OH    . TYR A 1 2748 ? 123.493 171.385 171.921 1.00 40.47  ? 2748 TYR A OH    1 
ATOM   11123 N N     . GLY A 1 2749 ? 115.714 171.983 175.879 1.00 46.22  ? 2749 GLY A N     1 
ATOM   11124 C CA    . GLY A 1 2749 ? 114.287 172.067 176.108 1.00 46.22  ? 2749 GLY A CA    1 
ATOM   11125 C C     . GLY A 1 2749 ? 113.648 173.154 175.275 1.00 46.22  ? 2749 GLY A C     1 
ATOM   11126 O O     . GLY A 1 2749 ? 112.566 172.966 174.718 1.00 46.22  ? 2749 GLY A O     1 
ATOM   11127 N N     . THR A 1 2750 ? 114.318 174.304 175.162 1.00 47.88  ? 2750 THR A N     1 
ATOM   11128 C CA    . THR A 1 2750 ? 113.837 175.342 174.255 1.00 47.88  ? 2750 THR A CA    1 
ATOM   11129 C C     . THR A 1 2750 ? 113.807 174.834 172.818 1.00 47.88  ? 2750 THR A C     1 
ATOM   11130 O O     . THR A 1 2750 ? 112.822 175.032 172.093 1.00 47.88  ? 2750 THR A O     1 
ATOM   11131 C CB    . THR A 1 2750 ? 114.718 176.587 174.367 1.00 47.88  ? 2750 THR A CB    1 
ATOM   11132 O OG1   . THR A 1 2750 ? 114.635 177.117 175.696 1.00 47.88  ? 2750 THR A OG1   1 
ATOM   11133 C CG2   . THR A 1 2750 ? 114.279 177.647 173.368 1.00 47.88  ? 2750 THR A CG2   1 
ATOM   11134 N N     . PHE A 1 2751 ? 114.877 174.157 172.396 1.00 45.66  ? 2751 PHE A N     1 
ATOM   11135 C CA    . PHE A 1 2751 ? 114.935 173.647 171.030 1.00 45.66  ? 2751 PHE A CA    1 
ATOM   11136 C C     . PHE A 1 2751 ? 113.857 172.596 170.773 1.00 45.66  ? 2751 PHE A C     1 
ATOM   11137 O O     . PHE A 1 2751 ? 113.220 172.601 169.714 1.00 45.66  ? 2751 PHE A O     1 
ATOM   11138 C CB    . PHE A 1 2751 ? 116.325 173.085 170.738 1.00 45.66  ? 2751 PHE A CB    1 
ATOM   11139 C CG    . PHE A 1 2751 ? 117.313 174.125 170.291 1.00 45.66  ? 2751 PHE A CG    1 
ATOM   11140 C CD1   . PHE A 1 2751 ? 117.029 174.947 169.214 1.00 45.66  ? 2751 PHE A CD1   1 
ATOM   11141 C CD2   . PHE A 1 2751 ? 118.523 174.280 170.943 1.00 45.66  ? 2751 PHE A CD2   1 
ATOM   11142 C CE1   . PHE A 1 2751 ? 117.932 175.906 168.799 1.00 45.66  ? 2751 PHE A CE1   1 
ATOM   11143 C CE2   . PHE A 1 2751 ? 119.430 175.237 170.530 1.00 45.66  ? 2751 PHE A CE2   1 
ATOM   11144 C CZ    . PHE A 1 2751 ? 119.134 176.050 169.457 1.00 45.66  ? 2751 PHE A CZ    1 
ATOM   11145 N N     . ASN A 1 2752 ? 113.636 171.688 171.727 1.00 47.25  ? 2752 ASN A N     1 
ATOM   11146 C CA    . ASN A 1 2752 ? 112.599 170.675 171.563 1.00 47.25  ? 2752 ASN A CA    1 
ATOM   11147 C C     . ASN A 1 2752 ? 111.210 171.293 171.556 1.00 47.25  ? 2752 ASN A C     1 
ATOM   11148 O O     . ASN A 1 2752 ? 110.339 170.863 170.792 1.00 47.25  ? 2752 ASN A O     1 
ATOM   11149 C CB    . ASN A 1 2752 ? 112.698 169.637 172.676 1.00 47.25  ? 2752 ASN A CB    1 
ATOM   11150 C CG    . ASN A 1 2752 ? 113.918 168.766 172.548 1.00 47.25  ? 2752 ASN A CG    1 
ATOM   11151 O OD1   . ASN A 1 2752 ? 114.395 168.211 173.533 1.00 47.25  ? 2752 ASN A OD1   1 
ATOM   11152 N ND2   . ASN A 1 2752 ? 114.432 168.634 171.331 1.00 47.25  ? 2752 ASN A ND2   1 
ATOM   11153 N N     . ARG A 1 2753 ? 110.972 172.280 172.420 1.00 48.59  ? 2753 ARG A N     1 
ATOM   11154 C CA    . ARG A 1 2753 ? 109.674 172.940 172.443 1.00 48.59  ? 2753 ARG A CA    1 
ATOM   11155 C C     . ARG A 1 2753 ? 109.412 173.666 171.133 1.00 48.59  ? 2753 ARG A C     1 
ATOM   11156 O O     . ARG A 1 2753 ? 108.269 173.731 170.669 1.00 48.59  ? 2753 ARG A O     1 
ATOM   11157 C CB    . ARG A 1 2753 ? 109.603 173.904 173.625 1.00 48.59  ? 2753 ARG A CB    1 
ATOM   11158 C CG    . ARG A 1 2753 ? 108.942 173.312 174.856 1.00 48.59  ? 2753 ARG A CG    1 
ATOM   11159 C CD    . ARG A 1 2753 ? 108.649 174.381 175.887 1.00 48.59  ? 2753 ARG A CD    1 
ATOM   11160 N NE    . ARG A 1 2753 ? 109.814 175.219 176.138 1.00 48.59  ? 2753 ARG A NE    1 
ATOM   11161 C CZ    . ARG A 1 2753 ? 110.736 174.959 177.054 1.00 48.59  ? 2753 ARG A CZ    1 
ATOM   11162 N NH1   . ARG A 1 2753 ? 110.662 173.885 177.823 1.00 48.59  ? 2753 ARG A NH1   1 
ATOM   11163 N NH2   . ARG A 1 2753 ? 111.759 175.796 177.202 1.00 48.59  ? 2753 ARG A NH2   1 
ATOM   11164 N N     . ALA A 1 2754 ? 110.460 174.220 170.522 1.00 52.29  ? 2754 ALA A N     1 
ATOM   11165 C CA    . ALA A 1 2754 ? 110.290 174.842 169.214 1.00 52.29  ? 2754 ALA A CA    1 
ATOM   11166 C C     . ALA A 1 2754 ? 110.055 173.801 168.125 1.00 52.29  ? 2754 ALA A C     1 
ATOM   11167 O O     . ALA A 1 2754 ? 109.218 174.001 167.239 1.00 52.29  ? 2754 ALA A O     1 
ATOM   11168 C CB    . ALA A 1 2754 ? 111.507 175.700 168.883 1.00 52.29  ? 2754 ALA A CB    1 
ATOM   11169 N N     . MET A 1 2755 ? 110.782 172.682 168.173 1.00 52.48  ? 2755 MET A N     1 
ATOM   11170 C CA    . MET A 1 2755 ? 110.691 171.692 167.104 1.00 52.48  ? 2755 MET A CA    1 
ATOM   11171 C C     . MET A 1 2755 ? 109.359 170.949 167.133 1.00 52.48  ? 2755 MET A C     1 
ATOM   11172 O O     . MET A 1 2755 ? 108.749 170.720 166.082 1.00 52.48  ? 2755 MET A O     1 
ATOM   11173 C CB    . MET A 1 2755 ? 111.860 170.710 167.203 1.00 52.48  ? 2755 MET A CB    1 
ATOM   11174 C CG    . MET A 1 2755 ? 111.556 169.310 166.693 1.00 52.48  ? 2755 MET A CG    1 
ATOM   11175 S SD    . MET A 1 2755 ? 112.872 168.140 167.073 1.00 52.48  ? 2755 MET A SD    1 
ATOM   11176 C CE    . MET A 1 2755 ? 112.354 167.563 168.686 1.00 52.48  ? 2755 MET A CE    1 
ATOM   11177 N N     . LEU A 1 2756 ? 108.887 170.571 168.322 1.00 50.98  ? 2756 LEU A N     1 
ATOM   11178 C CA    . LEU A 1 2756 ? 107.671 169.778 168.440 1.00 50.98  ? 2756 LEU A CA    1 
ATOM   11179 C C     . LEU A 1 2756 ? 106.404 170.586 168.200 1.00 50.98  ? 2756 LEU A C     1 
ATOM   11180 O O     . LEU A 1 2756 ? 105.319 169.998 168.162 1.00 50.98  ? 2756 LEU A O     1 
ATOM   11181 C CB    . LEU A 1 2756 ? 107.606 169.117 169.816 1.00 50.98  ? 2756 LEU A CB    1 
ATOM   11182 C CG    . LEU A 1 2756 ? 108.671 168.058 170.093 1.00 50.98  ? 2756 LEU A CG    1 
ATOM   11183 C CD1   . LEU A 1 2756 ? 108.528 167.518 171.503 1.00 50.98  ? 2756 LEU A CD1   1 
ATOM   11184 C CD2   . LEU A 1 2756 ? 108.585 166.935 169.077 1.00 50.98  ? 2756 LEU A CD2   1 
ATOM   11185 N N     . ARG A 1 2757 ? 106.506 171.909 168.050 1.00 57.22  ? 2757 ARG A N     1 
ATOM   11186 C CA    . ARG A 1 2757 ? 105.328 172.707 167.732 1.00 57.22  ? 2757 ARG A CA    1 
ATOM   11187 C C     . ARG A 1 2757 ? 104.784 172.406 166.342 1.00 57.22  ? 2757 ARG A C     1 
ATOM   11188 O O     . ARG A 1 2757 ? 103.661 172.816 166.029 1.00 57.22  ? 2757 ARG A O     1 
ATOM   11189 C CB    . ARG A 1 2757 ? 105.646 174.198 167.863 1.00 57.22  ? 2757 ARG A CB    1 
ATOM   11190 C CG    . ARG A 1 2757 ? 105.652 174.691 169.301 1.00 57.22  ? 2757 ARG A CG    1 
ATOM   11191 C CD    . ARG A 1 2757 ? 105.528 176.204 169.401 1.00 57.22  ? 2757 ARG A CD    1 
ATOM   11192 N NE    . ARG A 1 2757 ? 106.663 176.899 168.807 1.00 57.22  ? 2757 ARG A NE    1 
ATOM   11193 C CZ    . ARG A 1 2757 ? 106.595 177.654 167.720 1.00 57.22  ? 2757 ARG A CZ    1 
ATOM   11194 N NH1   . ARG A 1 2757 ? 105.457 177.828 167.069 1.00 57.22  ? 2757 ARG A NH1   1 
ATOM   11195 N NH2   . ARG A 1 2757 ? 107.698 178.252 167.275 1.00 57.22  ? 2757 ARG A NH2   1 
ATOM   11196 N N     . LEU A 1 2758 ? 105.553 171.707 165.503 1.00 56.31  ? 2758 LEU A N     1 
ATOM   11197 C CA    . LEU A 1 2758 ? 105.035 171.279 164.208 1.00 56.31  ? 2758 LEU A CA    1 
ATOM   11198 C C     . LEU A 1 2758 ? 103.862 170.321 164.374 1.00 56.31  ? 2758 LEU A C     1 
ATOM   11199 O O     . LEU A 1 2758 ? 102.840 170.453 163.691 1.00 56.31  ? 2758 LEU A O     1 
ATOM   11200 C CB    . LEU A 1 2758 ? 106.148 170.626 163.388 1.00 56.31  ? 2758 LEU A CB    1 
ATOM   11201 C CG    . LEU A 1 2758 ? 107.149 171.552 162.693 1.00 56.31  ? 2758 LEU A CG    1 
ATOM   11202 C CD1   . LEU A 1 2758 ? 107.977 170.778 161.679 1.00 56.31  ? 2758 LEU A CD1   1 
ATOM   11203 C CD2   . LEU A 1 2758 ? 106.436 172.719 162.028 1.00 56.31  ? 2758 LEU A CD2   1 
ATOM   11204 N N     . ILE A 1 2759 ? 103.989 169.354 165.277 1.00 57.15  ? 2759 ILE A N     1 
ATOM   11205 C CA    . ILE A 1 2759 ? 102.927 168.386 165.541 1.00 57.15  ? 2759 ILE A CA    1 
ATOM   11206 C C     . ILE A 1 2759 ? 102.388 168.598 166.953 1.00 57.15  ? 2759 ILE A C     1 
ATOM   11207 O O     . ILE A 1 2759 ? 103.079 168.308 167.941 1.00 57.15  ? 2759 ILE A O     1 
ATOM   11208 C CB    . ILE A 1 2759 ? 103.420 166.948 165.305 1.00 57.15  ? 2759 ILE A CB    1 
ATOM   11209 C CG1   . ILE A 1 2759 ? 104.732 166.682 166.047 1.00 57.15  ? 2759 ILE A CG1   1 
ATOM   11210 C CG2   . ILE A 1 2759 ? 103.600 166.689 163.819 1.00 57.15  ? 2759 ILE A CG2   1 
ATOM   11211 C CD1   . ILE A 1 2759 ? 105.158 165.239 166.014 1.00 57.15  ? 2759 ILE A CD1   1 
ATOM   11212 N N     . PRO A 1 2760 ? 101.164 169.111 167.094 1.00 61.04  ? 2760 PRO A N     1 
ATOM   11213 C CA    . PRO A 1 2760 ? 100.665 169.463 168.435 1.00 61.04  ? 2760 PRO A CA    1 
ATOM   11214 C C     . PRO A 1 2760 ? 100.418 168.268 169.339 1.00 61.04  ? 2760 PRO A C     1 
ATOM   11215 O O     . PRO A 1 2760 ? 100.189 168.454 170.540 1.00 61.04  ? 2760 PRO A O     1 
ATOM   11216 C CB    . PRO A 1 2760 ? 99.360  170.215 168.133 1.00 61.04  ? 2760 PRO A CB    1 
ATOM   11217 C CG    . PRO A 1 2760 ? 98.950  169.734 166.779 1.00 61.04  ? 2760 PRO A CG    1 
ATOM   11218 C CD    . PRO A 1 2760 ? 100.222 169.493 166.030 1.00 61.04  ? 2760 PRO A CD    1 
ATOM   11219 N N     . SER A 1 2761 ? 100.446 167.047 168.803 1.00 61.51  ? 2761 SER A N     1 
ATOM   11220 C CA    . SER A 1 2761 ? 100.109 165.881 169.610 1.00 61.51  ? 2761 SER A CA    1 
ATOM   11221 C C     . SER A 1 2761 ? 101.167 165.563 170.660 1.00 61.51  ? 2761 SER A C     1 
ATOM   11222 O O     . SER A 1 2761 ? 100.892 164.784 171.579 1.00 61.51  ? 2761 SER A O     1 
ATOM   11223 C CB    . SER A 1 2761 ? 99.893  164.664 168.708 1.00 61.51  ? 2761 SER A CB    1 
ATOM   11224 O OG    . SER A 1 2761 ? 98.800  164.867 167.828 1.00 61.51  ? 2761 SER A OG    1 
ATOM   11225 N N     . LEU A 1 2762 ? 102.364 166.140 170.553 1.00 64.93  ? 2762 LEU A N     1 
ATOM   11226 C CA    . LEU A 1 2762 ? 103.459 165.814 171.457 1.00 64.93  ? 2762 LEU A CA    1 
ATOM   11227 C C     . LEU A 1 2762 ? 104.101 167.037 172.098 1.00 64.93  ? 2762 LEU A C     1 
ATOM   11228 O O     . LEU A 1 2762 ? 105.298 167.007 172.399 1.00 64.93  ? 2762 LEU A O     1 
ATOM   11229 C CB    . LEU A 1 2762 ? 104.523 164.998 170.724 1.00 64.93  ? 2762 LEU A CB    1 
ATOM   11230 C CG    . LEU A 1 2762 ? 103.989 163.696 170.135 1.00 64.93  ? 2762 LEU A CG    1 
ATOM   11231 C CD1   . LEU A 1 2762 ? 104.800 163.247 168.931 1.00 64.93  ? 2762 LEU A CD1   1 
ATOM   11232 C CD2   . LEU A 1 2762 ? 103.954 162.638 171.206 1.00 64.93  ? 2762 LEU A CD2   1 
ATOM   11233 N N     . ARG A 1 2763 ? 103.340 168.112 172.310 1.00 64.84  ? 2763 ARG A N     1 
ATOM   11234 C CA    . ARG A 1 2763 ? 103.885 169.275 173.004 1.00 64.84  ? 2763 ARG A CA    1 
ATOM   11235 C C     . ARG A 1 2763 ? 104.250 168.932 174.443 1.00 64.84  ? 2763 ARG A C     1 
ATOM   11236 O O     . ARG A 1 2763 ? 105.282 169.375 174.959 1.00 64.84  ? 2763 ARG A O     1 
ATOM   11237 C CB    . ARG A 1 2763 ? 102.882 170.427 172.959 1.00 64.84  ? 2763 ARG A CB    1 
ATOM   11238 C CG    . ARG A 1 2763 ? 102.272 170.658 171.589 1.00 64.84  ? 2763 ARG A CG    1 
ATOM   11239 C CD    . ARG A 1 2763 ? 103.303 171.201 170.607 1.00 64.84  ? 2763 ARG A CD    1 
ATOM   11240 N NE    . ARG A 1 2763 ? 103.374 172.659 170.604 1.00 64.84  ? 2763 ARG A NE    1 
ATOM   11241 C CZ    . ARG A 1 2763 ? 102.366 173.475 170.316 1.00 64.84  ? 2763 ARG A CZ    1 
ATOM   11242 N NH1   . ARG A 1 2763 ? 101.186 173.014 169.931 1.00 64.84  ? 2763 ARG A NH1   1 
ATOM   11243 N NH2   . ARG A 1 2763 ? 102.553 174.789 170.398 1.00 64.84  ? 2763 ARG A NH2   1 
ATOM   11244 N N     . THR A 1 2764 ? 103.409 168.137 175.109 1.00 73.06  ? 2764 THR A N     1 
ATOM   11245 C CA    . THR A 1 2764 ? 103.626 167.820 176.517 1.00 73.06  ? 2764 THR A CA    1 
ATOM   11246 C C     . THR A 1 2764 ? 104.825 166.906 176.737 1.00 73.06  ? 2764 THR A C     1 
ATOM   11247 O O     . THR A 1 2764 ? 105.270 166.754 177.880 1.00 73.06  ? 2764 THR A O     1 
ATOM   11248 C CB    . THR A 1 2764 ? 102.373 167.171 177.108 1.00 73.06  ? 2764 THR A CB    1 
ATOM   11249 O OG1   . THR A 1 2764 ? 102.606 166.843 178.483 1.00 73.06  ? 2764 THR A OG1   1 
ATOM   11250 C CG2   . THR A 1 2764 ? 102.017 165.905 176.343 1.00 73.06  ? 2764 THR A CG2   1 
ATOM   11251 N N     . TYR A 1 2765 ? 105.354 166.294 175.682 1.00 70.96  ? 2765 TYR A N     1 
ATOM   11252 C CA    . TYR A 1 2765 ? 106.473 165.368 175.799 1.00 70.96  ? 2765 TYR A CA    1 
ATOM   11253 C C     . TYR A 1 2765 ? 107.826 166.027 175.562 1.00 70.96  ? 2765 TYR A C     1 
ATOM   11254 O O     . TYR A 1 2765 ? 108.842 165.326 175.539 1.00 70.96  ? 2765 TYR A O     1 
ATOM   11255 C CB    . TYR A 1 2765 ? 106.292 164.204 174.820 1.00 70.96  ? 2765 TYR A CB    1 
ATOM   11256 C CG    . TYR A 1 2765 ? 105.273 163.178 175.262 1.00 70.96  ? 2765 TYR A CG    1 
ATOM   11257 C CD1   . TYR A 1 2765 ? 105.548 162.301 176.303 1.00 70.96  ? 2765 TYR A CD1   1 
ATOM   11258 C CD2   . TYR A 1 2765 ? 104.036 163.088 174.641 1.00 70.96  ? 2765 TYR A CD2   1 
ATOM   11259 C CE1   . TYR A 1 2765 ? 104.620 161.361 176.709 1.00 70.96  ? 2765 TYR A CE1   1 
ATOM   11260 C CE2   . TYR A 1 2765 ? 103.101 162.152 175.039 1.00 70.96  ? 2765 TYR A CE2   1 
ATOM   11261 C CZ    . TYR A 1 2765 ? 103.398 161.292 176.074 1.00 70.96  ? 2765 TYR A CZ    1 
ATOM   11262 O OH    . TYR A 1 2765 ? 102.470 160.358 176.476 1.00 70.96  ? 2765 TYR A OH    1 
ATOM   11263 N N     . ALA A 1 2766 ? 107.865 167.350 175.383 1.00 66.45  ? 2766 ALA A N     1 
ATOM   11264 C CA    . ALA A 1 2766 ? 109.123 168.021 175.067 1.00 66.45  ? 2766 ALA A CA    1 
ATOM   11265 C C     . ALA A 1 2766 ? 110.110 167.932 176.225 1.00 66.45  ? 2766 ALA A C     1 
ATOM   11266 O O     . ALA A 1 2766 ? 111.279 167.579 176.033 1.00 66.45  ? 2766 ALA A O     1 
ATOM   11267 C CB    . ALA A 1 2766 ? 108.857 169.480 174.696 1.00 66.45  ? 2766 ALA A CB    1 
ATOM   11268 N N     . GLU A 1 2767 ? 109.659 168.256 177.437 1.00 67.65  ? 2767 GLU A N     1 
ATOM   11269 C CA    . GLU A 1 2767 ? 110.558 168.247 178.590 1.00 67.65  ? 2767 GLU A CA    1 
ATOM   11270 C C     . GLU A 1 2767 ? 111.130 166.866 178.893 1.00 67.65  ? 2767 GLU A C     1 
ATOM   11271 O O     . GLU A 1 2767 ? 112.357 166.759 179.073 1.00 67.65  ? 2767 GLU A O     1 
ATOM   11272 C CB    . GLU A 1 2767 ? 109.834 168.838 179.805 1.00 67.65  ? 2767 GLU A CB    1 
ATOM   11273 C CG    . GLU A 1 2767 ? 110.631 168.782 181.098 1.00 67.65  ? 2767 GLU A CG    1 
ATOM   11274 C CD    . GLU A 1 2767 ? 109.845 169.302 182.287 1.00 67.65  ? 2767 GLU A CD    1 
ATOM   11275 O OE1   . GLU A 1 2767 ? 109.113 170.301 182.128 1.00 67.65  ? 2767 GLU A OE1   1 
ATOM   11276 O OE2   . GLU A 1 2767 ? 109.960 168.710 183.380 1.00 67.65  ? 2767 GLU A OE2   1 
ATOM   11277 N N     . PRO A 1 2768 ? 110.336 165.789 178.979 1.00 63.49  ? 2768 PRO A N     1 
ATOM   11278 C CA    . PRO A 1 2768 ? 110.956 164.474 179.217 1.00 63.49  ? 2768 PRO A CA    1 
ATOM   11279 C C     . PRO A 1 2768 ? 111.913 164.063 178.115 1.00 63.49  ? 2768 PRO A C     1 
ATOM   11280 O O     . PRO A 1 2768 ? 112.918 163.401 178.393 1.00 63.49  ? 2768 PRO A O     1 
ATOM   11281 C CB    . PRO A 1 2768 ? 109.751 163.526 179.315 1.00 63.49  ? 2768 PRO A CB    1 
ATOM   11282 C CG    . PRO A 1 2768 ? 108.587 164.407 179.605 1.00 63.49  ? 2768 PRO A CG    1 
ATOM   11283 C CD    . PRO A 1 2768 ? 108.871 165.677 178.880 1.00 63.49  ? 2768 PRO A CD    1 
ATOM   11284 N N     . LEU A 1 2769 ? 111.631 164.444 176.867 1.00 56.40  ? 2769 LEU A N     1 
ATOM   11285 C CA    . LEU A 1 2769 ? 112.532 164.120 175.765 1.00 56.40  ? 2769 LEU A CA    1 
ATOM   11286 C C     . LEU A 1 2769 ? 113.883 164.804 175.943 1.00 56.40  ? 2769 LEU A C     1 
ATOM   11287 O O     . LEU A 1 2769 ? 114.941 164.186 175.765 1.00 56.40  ? 2769 LEU A O     1 
ATOM   11288 C CB    . LEU A 1 2769 ? 111.888 164.526 174.439 1.00 56.40  ? 2769 LEU A CB    1 
ATOM   11289 C CG    . LEU A 1 2769 ? 112.692 164.289 173.163 1.00 56.40  ? 2769 LEU A CG    1 
ATOM   11290 C CD1   . LEU A 1 2769 ? 112.486 162.867 172.679 1.00 56.40  ? 2769 LEU A CD1   1 
ATOM   11291 C CD2   . LEU A 1 2769 ? 112.296 165.285 172.089 1.00 56.40  ? 2769 LEU A CD2   1 
ATOM   11292 N N     . THR A 1 2770 ? 113.862 166.090 176.300 1.00 52.11  ? 2770 THR A N     1 
ATOM   11293 C CA    . THR A 1 2770 ? 115.100 166.822 176.542 1.00 52.11  ? 2770 THR A CA    1 
ATOM   11294 C C     . THR A 1 2770 ? 115.865 166.223 177.715 1.00 52.11  ? 2770 THR A C     1 
ATOM   11295 O O     . THR A 1 2770 ? 117.093 166.080 177.668 1.00 52.11  ? 2770 THR A O     1 
ATOM   11296 C CB    . THR A 1 2770 ? 114.792 168.297 176.801 1.00 52.11  ? 2770 THR A CB    1 
ATOM   11297 O OG1   . THR A 1 2770 ? 114.293 168.900 175.602 1.00 52.11  ? 2770 THR A OG1   1 
ATOM   11298 C CG2   . THR A 1 2770 ? 116.042 169.033 177.250 1.00 52.11  ? 2770 THR A CG2   1 
ATOM   11299 N N     . ALA A 1 2771 ? 115.148 165.867 178.782 1.00 51.75  ? 2771 ALA A N     1 
ATOM   11300 C CA    . ALA A 1 2771 ? 115.800 165.262 179.936 1.00 51.75  ? 2771 ALA A CA    1 
ATOM   11301 C C     . ALA A 1 2771 ? 116.444 163.932 179.562 1.00 51.75  ? 2771 ALA A C     1 
ATOM   11302 O O     . ALA A 1 2771 ? 117.560 163.621 179.994 1.00 51.75  ? 2771 ALA A O     1 
ATOM   11303 C CB    . ALA A 1 2771 ? 114.793 165.084 181.073 1.00 51.75  ? 2771 ALA A CB    1 
ATOM   11304 N N     . ALA A 1 2772 ? 115.755 163.136 178.742 1.00 50.00  ? 2772 ALA A N     1 
ATOM   11305 C CA    . ALA A 1 2772 ? 116.315 161.868 178.292 1.00 50.00  ? 2772 ALA A CA    1 
ATOM   11306 C C     . ALA A 1 2772 ? 117.573 162.086 177.462 1.00 50.00  ? 2772 ALA A C     1 
ATOM   11307 O O     . ALA A 1 2772 ? 118.578 161.383 177.637 1.00 50.00  ? 2772 ALA A O     1 
ATOM   11308 C CB    . ALA A 1 2772 ? 115.269 161.089 177.494 1.00 50.00  ? 2772 ALA A CB    1 
ATOM   11309 N N     . MET A 1 2773 ? 117.538 163.062 176.550 1.00 41.85  ? 2773 MET A N     1 
ATOM   11310 C CA    . MET A 1 2773 ? 118.713 163.324 175.726 1.00 41.85  ? 2773 MET A CA    1 
ATOM   11311 C C     . MET A 1 2773 ? 119.894 163.759 176.580 1.00 41.85  ? 2773 MET A C     1 
ATOM   11312 O O     . MET A 1 2773 ? 121.021 163.297 176.380 1.00 41.85  ? 2773 MET A O     1 
ATOM   11313 C CB    . MET A 1 2773 ? 118.432 164.382 174.658 1.00 41.85  ? 2773 MET A CB    1 
ATOM   11314 C CG    . MET A 1 2773 ? 117.680 163.881 173.449 1.00 41.85  ? 2773 MET A CG    1 
ATOM   11315 S SD    . MET A 1 2773 ? 117.546 165.146 172.177 1.00 41.85  ? 2773 MET A SD    1 
ATOM   11316 C CE    . MET A 1 2773 ? 116.883 166.495 173.131 1.00 41.85  ? 2773 MET A CE    1 
ATOM   11317 N N     . VAL A 1 2774 ? 119.658 164.662 177.535 1.00 45.32  ? 2774 VAL A N     1 
ATOM   11318 C CA    . VAL A 1 2774 ? 120.773 165.161 178.337 1.00 45.32  ? 2774 VAL A CA    1 
ATOM   11319 C C     . VAL A 1 2774 ? 121.315 164.062 179.242 1.00 45.32  ? 2774 VAL A C     1 
ATOM   11320 O O     . VAL A 1 2774 ? 122.527 163.975 179.471 1.00 45.32  ? 2774 VAL A O     1 
ATOM   11321 C CB    . VAL A 1 2774 ? 120.375 166.425 179.126 1.00 45.32  ? 2774 VAL A CB    1 
ATOM   11322 C CG1   . VAL A 1 2774 ? 119.874 167.505 178.180 1.00 45.32  ? 2774 VAL A CG1   1 
ATOM   11323 C CG2   . VAL A 1 2774 ? 119.341 166.119 180.188 1.00 45.32  ? 2774 VAL A CG2   1 
ATOM   11324 N N     . GLU A 1 2775 ? 120.441 163.186 179.747 1.00 52.48  ? 2775 GLU A N     1 
ATOM   11325 C CA    . GLU A 1 2775 ? 120.913 162.067 180.556 1.00 52.48  ? 2775 GLU A CA    1 
ATOM   11326 C C     . GLU A 1 2775 ? 121.780 161.122 179.733 1.00 52.48  ? 2775 GLU A C     1 
ATOM   11327 O O     . GLU A 1 2775 ? 122.864 160.710 180.173 1.00 52.48  ? 2775 GLU A O     1 
ATOM   11328 C CB    . GLU A 1 2775 ? 119.728 161.318 181.162 1.00 52.48  ? 2775 GLU A CB    1 
ATOM   11329 C CG    . GLU A 1 2775 ? 119.091 162.019 182.347 1.00 52.48  ? 2775 GLU A CG    1 
ATOM   11330 C CD    . GLU A 1 2775 ? 118.040 161.167 183.027 1.00 52.48  ? 2775 GLU A CD    1 
ATOM   11331 O OE1   . GLU A 1 2775 ? 117.707 160.089 182.490 1.00 52.48  ? 2775 GLU A OE1   1 
ATOM   11332 O OE2   . GLU A 1 2775 ? 117.544 161.575 184.098 1.00 52.48  ? 2775 GLU A OE2   1 
ATOM   11333 N N     . PHE A 1 2776 ? 121.322 160.769 178.529 1.00 45.89  ? 2776 PHE A N     1 
ATOM   11334 C CA    . PHE A 1 2776 ? 122.109 159.871 177.692 1.00 45.89  ? 2776 PHE A CA    1 
ATOM   11335 C C     . PHE A 1 2776 ? 123.427 160.515 177.284 1.00 45.89  ? 2776 PHE A C     1 
ATOM   11336 O O     . PHE A 1 2776 ? 124.464 159.848 177.236 1.00 45.89  ? 2776 PHE A O     1 
ATOM   11337 C CB    . PHE A 1 2776 ? 121.324 159.442 176.455 1.00 45.89  ? 2776 PHE A CB    1 
ATOM   11338 C CG    . PHE A 1 2776 ? 122.035 158.404 175.637 1.00 45.89  ? 2776 PHE A CG    1 
ATOM   11339 C CD1   . PHE A 1 2776 ? 122.665 157.337 176.254 1.00 45.89  ? 2776 PHE A CD1   1 
ATOM   11340 C CD2   . PHE A 1 2776 ? 122.108 158.513 174.261 1.00 45.89  ? 2776 PHE A CD2   1 
ATOM   11341 C CE1   . PHE A 1 2776 ? 123.334 156.387 175.512 1.00 45.89  ? 2776 PHE A CE1   1 
ATOM   11342 C CE2   . PHE A 1 2776 ? 122.778 157.564 173.514 1.00 45.89  ? 2776 PHE A CE2   1 
ATOM   11343 C CZ    . PHE A 1 2776 ? 123.394 156.502 174.142 1.00 45.89  ? 2776 PHE A CZ    1 
ATOM   11344 N N     . TYR A 1 2777 ? 123.404 161.812 176.974 1.00 42.15  ? 2777 TYR A N     1 
ATOM   11345 C CA    . TYR A 1 2777 ? 124.629 162.510 176.606 1.00 42.15  ? 2777 TYR A CA    1 
ATOM   11346 C C     . TYR A 1 2777 ? 125.616 162.528 177.766 1.00 42.15  ? 2777 TYR A C     1 
ATOM   11347 O O     . TYR A 1 2777 ? 126.814 162.291 177.582 1.00 42.15  ? 2777 TYR A O     1 
ATOM   11348 C CB    . TYR A 1 2777 ? 124.298 163.932 176.150 1.00 42.15  ? 2777 TYR A CB    1 
ATOM   11349 C CG    . TYR A 1 2777 ? 125.497 164.841 176.027 1.00 42.15  ? 2777 TYR A CG    1 
ATOM   11350 C CD1   . TYR A 1 2777 ? 126.300 164.817 174.896 1.00 42.15  ? 2777 TYR A CD1   1 
ATOM   11351 C CD2   . TYR A 1 2777 ? 125.821 165.732 177.041 1.00 42.15  ? 2777 TYR A CD2   1 
ATOM   11352 C CE1   . TYR A 1 2777 ? 127.395 165.650 174.782 1.00 42.15  ? 2777 TYR A CE1   1 
ATOM   11353 C CE2   . TYR A 1 2777 ? 126.913 166.567 176.935 1.00 42.15  ? 2777 TYR A CE2   1 
ATOM   11354 C CZ    . TYR A 1 2777 ? 127.696 166.523 175.804 1.00 42.15  ? 2777 TYR A CZ    1 
ATOM   11355 O OH    . TYR A 1 2777 ? 128.783 167.357 175.701 1.00 42.15  ? 2777 TYR A OH    1 
ATOM   11356 N N     . THR A 1 2778 ? 125.122 162.792 178.978 1.00 47.58  ? 2778 THR A N     1 
ATOM   11357 C CA    . THR A 1 2778 ? 125.991 162.798 180.149 1.00 47.58  ? 2778 THR A CA    1 
ATOM   11358 C C     . THR A 1 2778 ? 126.617 161.428 180.374 1.00 47.58  ? 2778 THR A C     1 
ATOM   11359 O O     . THR A 1 2778 ? 127.823 161.318 180.629 1.00 47.58  ? 2778 THR A O     1 
ATOM   11360 C CB    . THR A 1 2778 ? 125.199 163.236 181.381 1.00 47.58  ? 2778 THR A CB    1 
ATOM   11361 O OG1   . THR A 1 2778 ? 124.588 164.507 181.130 1.00 47.58  ? 2778 THR A OG1   1 
ATOM   11362 C CG2   . THR A 1 2778 ? 126.113 163.349 182.588 1.00 47.58  ? 2778 THR A CG2   1 
ATOM   11363 N N     . MET A 1 2779 ? 125.813 160.367 180.277 1.00 54.88  ? 2779 MET A N     1 
ATOM   11364 C CA    . MET A 1 2779 ? 126.349 159.028 180.512 1.00 54.88  ? 2779 MET A CA    1 
ATOM   11365 C C     . MET A 1 2779 ? 127.320 158.608 179.414 1.00 54.88  ? 2779 MET A C     1 
ATOM   11366 O O     . MET A 1 2779 ? 128.357 157.996 179.697 1.00 54.88  ? 2779 MET A O     1 
ATOM   11367 C CB    . MET A 1 2779 ? 125.212 158.022 180.653 1.00 54.88  ? 2779 MET A CB    1 
ATOM   11368 C CG    . MET A 1 2779 ? 124.378 158.252 181.895 1.00 54.88  ? 2779 MET A CG    1 
ATOM   11369 S SD    . MET A 1 2779 ? 123.083 157.025 182.082 1.00 54.88  ? 2779 MET A SD    1 
ATOM   11370 C CE    . MET A 1 2779 ? 121.974 157.598 180.811 1.00 54.88  ? 2779 MET A CE    1 
ATOM   11371 N N     . SER A 1 2780 ? 127.008 158.924 178.157 1.00 48.27  ? 2780 SER A N     1 
ATOM   11372 C CA    . SER A 1 2780 ? 127.917 158.616 177.062 1.00 48.27  ? 2780 SER A CA    1 
ATOM   11373 C C     . SER A 1 2780 ? 129.175 159.471 177.091 1.00 48.27  ? 2780 SER A C     1 
ATOM   11374 O O     . SER A 1 2780 ? 130.166 159.105 176.451 1.00 48.27  ? 2780 SER A O     1 
ATOM   11375 C CB    . SER A 1 2780 ? 127.203 158.790 175.722 1.00 48.27  ? 2780 SER A CB    1 
ATOM   11376 O OG    . SER A 1 2780 ? 126.253 157.760 175.515 1.00 48.27  ? 2780 SER A OG    1 
ATOM   11377 N N     . GLN A 1 2781 ? 129.153 160.602 177.794 1.00 45.04  ? 2781 GLN A N     1 
ATOM   11378 C CA    . GLN A 1 2781 ? 130.364 161.376 178.023 1.00 45.04  ? 2781 GLN A CA    1 
ATOM   11379 C C     . GLN A 1 2781 ? 131.177 160.848 179.195 1.00 45.04  ? 2781 GLN A C     1 
ATOM   11380 O O     . GLN A 1 2781 ? 132.408 160.960 179.184 1.00 45.04  ? 2781 GLN A O     1 
ATOM   11381 C CB    . GLN A 1 2781 ? 130.014 162.846 178.265 1.00 45.04  ? 2781 GLN A CB    1 
ATOM   11382 C CG    . GLN A 1 2781 ? 131.156 163.806 177.988 1.00 45.04  ? 2781 GLN A CG    1 
ATOM   11383 C CD    . GLN A 1 2781 ? 130.728 165.256 178.069 1.00 45.04  ? 2781 GLN A CD    1 
ATOM   11384 O OE1   . GLN A 1 2781 ? 129.576 165.560 178.375 1.00 45.04  ? 2781 GLN A OE1   1 
ATOM   11385 N NE2   . GLN A 1 2781 ? 131.658 166.163 177.796 1.00 45.04  ? 2781 GLN A NE2   1 
ATOM   11386 N N     . GLU A 1 2782 ? 130.515 160.282 180.208 1.00 51.34  ? 2782 GLU A N     1 
ATOM   11387 C CA    . GLU A 1 2782 ? 131.243 159.694 181.329 1.00 51.34  ? 2782 GLU A CA    1 
ATOM   11388 C C     . GLU A 1 2782 ? 132.111 158.530 180.866 1.00 51.34  ? 2782 GLU A C     1 
ATOM   11389 O O     . GLU A 1 2782 ? 133.310 158.480 181.164 1.00 51.34  ? 2782 GLU A O     1 
ATOM   11390 C CB    . GLU A 1 2782 ? 130.266 159.244 182.415 1.00 51.34  ? 2782 GLU A CB    1 
ATOM   11391 C CG    . GLU A 1 2782 ? 129.601 160.390 183.160 1.00 51.34  ? 2782 GLU A CG    1 
ATOM   11392 C CD    . GLU A 1 2782 ? 128.603 159.911 184.195 1.00 51.34  ? 2782 GLU A CD    1 
ATOM   11393 O OE1   . GLU A 1 2782 ? 128.424 158.683 184.329 1.00 51.34  ? 2782 GLU A OE1   1 
ATOM   11394 O OE2   . GLU A 1 2782 ? 127.998 160.765 184.877 1.00 51.34  ? 2782 GLU A OE2   1 
ATOM   11395 N N     . ARG A 1 2783 ? 131.528 157.589 180.133 1.00 51.84  ? 2783 ARG A N     1 
ATOM   11396 C CA    . ARG A 1 2783 ? 132.306 156.545 179.489 1.00 51.84  ? 2783 ARG A CA    1 
ATOM   11397 C C     . ARG A 1 2783 ? 132.758 157.037 178.116 1.00 51.84  ? 2783 ARG A C     1 
ATOM   11398 O O     . ARG A 1 2783 ? 132.403 158.134 177.680 1.00 51.84  ? 2783 ARG A O     1 
ATOM   11399 C CB    . ARG A 1 2783 ? 131.491 155.251 179.373 1.00 51.84  ? 2783 ARG A CB    1 
ATOM   11400 C CG    . ARG A 1 2783 ? 132.323 153.996 179.108 1.00 51.84  ? 2783 ARG A CG    1 
ATOM   11401 C CD    . ARG A 1 2783 ? 131.463 152.796 178.750 1.00 51.84  ? 2783 ARG A CD    1 
ATOM   11402 N NE    . ARG A 1 2783 ? 132.091 151.539 179.139 1.00 51.84  ? 2783 ARG A NE    1 
ATOM   11403 C CZ    . ARG A 1 2783 ? 131.444 150.502 179.653 1.00 51.84  ? 2783 ARG A CZ    1 
ATOM   11404 N NH1   . ARG A 1 2783 ? 130.139 150.538 179.864 1.00 51.84  ? 2783 ARG A NH1   1 
ATOM   11405 N NH2   . ARG A 1 2783 ? 132.123 149.402 179.962 1.00 51.84  ? 2783 ARG A NH2   1 
ATOM   11406 N N     . PHE A 1 2784 ? 133.563 156.216 177.442 1.00 50.45  ? 2784 PHE A N     1 
ATOM   11407 C CA    . PHE A 1 2784 ? 134.165 156.565 176.156 1.00 50.45  ? 2784 PHE A CA    1 
ATOM   11408 C C     . PHE A 1 2784 ? 134.985 157.850 176.275 1.00 50.45  ? 2784 PHE A C     1 
ATOM   11409 O O     . PHE A 1 2784 ? 134.786 158.823 175.546 1.00 50.45  ? 2784 PHE A O     1 
ATOM   11410 C CB    . PHE A 1 2784 ? 133.108 156.688 175.054 1.00 50.45  ? 2784 PHE A CB    1 
ATOM   11411 C CG    . PHE A 1 2784 ? 132.198 155.506 174.959 1.00 50.45  ? 2784 PHE A CG    1 
ATOM   11412 C CD1   . PHE A 1 2784 ? 130.826 155.667 175.016 1.00 50.45  ? 2784 PHE A CD1   1 
ATOM   11413 C CD2   . PHE A 1 2784 ? 132.714 154.230 174.831 1.00 50.45  ? 2784 PHE A CD2   1 
ATOM   11414 C CE1   . PHE A 1 2784 ? 129.987 154.580 174.929 1.00 50.45  ? 2784 PHE A CE1   1 
ATOM   11415 C CE2   . PHE A 1 2784 ? 131.879 153.139 174.751 1.00 50.45  ? 2784 PHE A CE2   1 
ATOM   11416 C CZ    . PHE A 1 2784 ? 130.513 153.314 174.804 1.00 50.45  ? 2784 PHE A CZ    1 
ATOM   11417 N N     . THR A 1 2785 ? 135.906 157.840 177.230 1.00 51.57  ? 2785 THR A N     1 
ATOM   11418 C CA    . THR A 1 2785 ? 136.863 158.924 177.345 1.00 51.57  ? 2785 THR A CA    1 
ATOM   11419 C C     . THR A 1 2785 ? 137.863 158.856 176.196 1.00 51.57  ? 2785 THR A C     1 
ATOM   11420 O O     . THR A 1 2785 ? 137.998 157.836 175.515 1.00 51.57  ? 2785 THR A O     1 
ATOM   11421 C CB    . THR A 1 2785 ? 137.593 158.859 178.686 1.00 51.57  ? 2785 THR A CB    1 
ATOM   11422 O OG1   . THR A 1 2785 ? 138.318 157.627 178.777 1.00 51.57  ? 2785 THR A OG1   1 
ATOM   11423 C CG2   . THR A 1 2785 ? 136.598 158.940 179.835 1.00 51.57  ? 2785 THR A CG2   1 
ATOM   11424 N N     . GLN A 1 2786 ? 138.568 159.966 175.980 1.00 50.51  ? 2786 GLN A N     1 
ATOM   11425 C CA    . GLN A 1 2786 ? 139.550 160.010 174.903 1.00 50.51  ? 2786 GLN A CA    1 
ATOM   11426 C C     . GLN A 1 2786 ? 140.713 159.059 175.145 1.00 50.51  ? 2786 GLN A C     1 
ATOM   11427 O O     . GLN A 1 2786 ? 141.472 158.777 174.211 1.00 50.51  ? 2786 GLN A O     1 
ATOM   11428 C CB    . GLN A 1 2786 ? 140.065 161.437 174.721 1.00 50.51  ? 2786 GLN A CB    1 
ATOM   11429 C CG    . GLN A 1 2786 ? 139.011 162.406 174.217 1.00 50.51  ? 2786 GLN A CG    1 
ATOM   11430 C CD    . GLN A 1 2786 ? 139.543 163.815 174.063 1.00 50.51  ? 2786 GLN A CD    1 
ATOM   11431 O OE1   . GLN A 1 2786 ? 140.694 164.096 174.395 1.00 50.51  ? 2786 GLN A OE1   1 
ATOM   11432 N NE2   . GLN A 1 2786 ? 138.705 164.711 173.555 1.00 50.51  ? 2786 GLN A NE2   1 
ATOM   11433 N N     . ASP A 1 2787 ? 140.875 158.564 176.374 1.00 50.71  ? 2787 ASP A N     1 
ATOM   11434 C CA    . ASP A 1 2787 ? 141.925 157.588 176.647 1.00 50.71  ? 2787 ASP A CA    1 
ATOM   11435 C C     . ASP A 1 2787 ? 141.676 156.285 175.897 1.00 50.71  ? 2787 ASP A C     1 
ATOM   11436 O O     . ASP A 1 2787 ? 142.613 155.680 175.363 1.00 50.71  ? 2787 ASP A O     1 
ATOM   11437 C CB    . ASP A 1 2787 ? 142.022 157.331 178.150 1.00 50.71  ? 2787 ASP A CB    1 
ATOM   11438 C CG    . ASP A 1 2787 ? 142.090 158.611 178.958 1.00 50.71  ? 2787 ASP A CG    1 
ATOM   11439 O OD1   . ASP A 1 2787 ? 143.048 159.388 178.764 1.00 50.71  ? 2787 ASP A OD1   1 
ATOM   11440 O OD2   . ASP A 1 2787 ? 141.186 158.841 179.788 1.00 50.71  ? 2787 ASP A OD2   1 
ATOM   11441 N N     . THR A 1 2788 ? 140.420 155.832 175.855 1.00 52.35  ? 2788 THR A N     1 
ATOM   11442 C CA    . THR A 1 2788 ? 140.104 154.573 175.187 1.00 52.35  ? 2788 THR A CA    1 
ATOM   11443 C C     . THR A 1 2788 ? 140.371 154.659 173.688 1.00 52.35  ? 2788 THR A C     1 
ATOM   11444 O O     . THR A 1 2788 ? 141.081 153.820 173.123 1.00 52.35  ? 2788 THR A O     1 
ATOM   11445 C CB    . THR A 1 2788 ? 138.647 154.191 175.450 1.00 52.35  ? 2788 THR A CB    1 
ATOM   11446 O OG1   . THR A 1 2788 ? 138.356 154.340 176.844 1.00 52.35  ? 2788 THR A OG1   1 
ATOM   11447 C CG2   . THR A 1 2788 ? 138.393 152.752 175.035 1.00 52.35  ? 2788 THR A CG2   1 
ATOM   11448 N N     . GLN A 1 2789 ? 139.811 155.673 173.027 1.00 47.98  ? 2789 GLN A N     1 
ATOM   11449 C CA    . GLN A 1 2789 ? 139.989 155.865 171.597 1.00 47.98  ? 2789 GLN A CA    1 
ATOM   11450 C C     . GLN A 1 2789 ? 140.087 157.356 171.306 1.00 47.98  ? 2789 GLN A C     1 
ATOM   11451 O O     . GLN A 1 2789 ? 139.428 158.163 171.978 1.00 47.98  ? 2789 GLN A O     1 
ATOM   11452 C CB    . GLN A 1 2789 ? 138.832 155.251 170.795 1.00 47.98  ? 2789 GLN A CB    1 
ATOM   11453 C CG    . GLN A 1 2789 ? 138.875 153.730 170.674 1.00 47.98  ? 2789 GLN A CG    1 
ATOM   11454 C CD    . GLN A 1 2789 ? 139.850 153.235 169.617 1.00 47.98  ? 2789 GLN A CD    1 
ATOM   11455 O OE1   . GLN A 1 2789 ? 140.887 153.848 169.369 1.00 47.98  ? 2789 GLN A OE1   1 
ATOM   11456 N NE2   . GLN A 1 2789 ? 139.516 152.114 168.989 1.00 47.98  ? 2789 GLN A NE2   1 
ATOM   11457 N N     . PRO A 1 2790 ? 140.898 157.751 170.322 1.00 46.12  ? 2790 PRO A N     1 
ATOM   11458 C CA    . PRO A 1 2790 ? 141.056 159.186 170.034 1.00 46.12  ? 2790 PRO A CA    1 
ATOM   11459 C C     . PRO A 1 2790 ? 139.794 159.859 169.524 1.00 46.12  ? 2790 PRO A C     1 
ATOM   11460 O O     . PRO A 1 2790 ? 139.684 161.086 169.633 1.00 46.12  ? 2790 PRO A O     1 
ATOM   11461 C CB    . PRO A 1 2790 ? 142.169 159.212 168.977 1.00 46.12  ? 2790 PRO A CB    1 
ATOM   11462 C CG    . PRO A 1 2790 ? 142.147 157.852 168.367 1.00 46.12  ? 2790 PRO A CG    1 
ATOM   11463 C CD    . PRO A 1 2790 ? 141.757 156.916 169.468 1.00 46.12  ? 2790 PRO A CD    1 
ATOM   11464 N N     . HIS A 1 2791 ? 138.842 159.110 168.971 1.00 47.27  ? 2791 HIS A N     1 
ATOM   11465 C CA    . HIS A 1 2791 ? 137.627 159.689 168.414 1.00 47.27  ? 2791 HIS A CA    1 
ATOM   11466 C C     . HIS A 1 2791 ? 136.460 159.670 169.391 1.00 47.27  ? 2791 HIS A C     1 
ATOM   11467 O O     . HIS A 1 2791 ? 135.334 159.986 168.999 1.00 47.27  ? 2791 HIS A O     1 
ATOM   11468 C CB    . HIS A 1 2791 ? 137.237 158.973 167.118 1.00 47.27  ? 2791 HIS A CB    1 
ATOM   11469 C CG    . HIS A 1 2791 ? 136.998 157.504 167.276 1.00 47.27  ? 2791 HIS A CG    1 
ATOM   11470 N ND1   . HIS A 1 2791 ? 138.023 156.594 167.417 1.00 47.27  ? 2791 HIS A ND1   1 
ATOM   11471 C CD2   . HIS A 1 2791 ? 135.851 156.785 167.297 1.00 47.27  ? 2791 HIS A CD2   1 
ATOM   11472 C CE1   . HIS A 1 2791 ? 137.518 155.378 167.527 1.00 47.27  ? 2791 HIS A CE1   1 
ATOM   11473 N NE2   . HIS A 1 2791 ? 136.202 155.467 167.457 1.00 47.27  ? 2791 HIS A NE2   1 
ATOM   11474 N N     . TYR A 1 2792 ? 136.702 159.318 170.650 1.00 49.81  ? 2792 TYR A N     1 
ATOM   11475 C CA    . TYR A 1 2792 ? 135.637 159.252 171.650 1.00 49.81  ? 2792 TYR A CA    1 
ATOM   11476 C C     . TYR A 1 2792 ? 135.474 160.603 172.350 1.00 49.81  ? 2792 TYR A C     1 
ATOM   11477 O O     . TYR A 1 2792 ? 135.526 160.721 173.573 1.00 49.81  ? 2792 TYR A O     1 
ATOM   11478 C CB    . TYR A 1 2792 ? 135.926 158.138 172.649 1.00 49.81  ? 2792 TYR A CB    1 
ATOM   11479 C CG    . TYR A 1 2792 ? 135.608 156.752 172.138 1.00 49.81  ? 2792 TYR A CG    1 
ATOM   11480 C CD1   . TYR A 1 2792 ? 135.174 156.553 170.835 1.00 49.81  ? 2792 TYR A CD1   1 
ATOM   11481 C CD2   . TYR A 1 2792 ? 135.746 155.643 172.958 1.00 49.81  ? 2792 TYR A CD2   1 
ATOM   11482 C CE1   . TYR A 1 2792 ? 134.884 155.288 170.366 1.00 49.81  ? 2792 TYR A CE1   1 
ATOM   11483 C CE2   . TYR A 1 2792 ? 135.458 154.374 172.498 1.00 49.81  ? 2792 TYR A CE2   1 
ATOM   11484 C CZ    . TYR A 1 2792 ? 135.029 154.203 171.202 1.00 49.81  ? 2792 TYR A CZ    1 
ATOM   11485 O OH    . TYR A 1 2792 ? 134.742 152.940 170.741 1.00 49.81  ? 2792 TYR A OH    1 
ATOM   11486 N N     . ILE A 1 2793 ? 135.267 161.636 171.539 1.00 43.92  ? 2793 ILE A N     1 
ATOM   11487 C CA    . ILE A 1 2793 ? 135.090 163.001 172.019 1.00 43.92  ? 2793 ILE A CA    1 
ATOM   11488 C C     . ILE A 1 2793 ? 133.620 163.370 171.878 1.00 43.92  ? 2793 ILE A C     1 
ATOM   11489 O O     . ILE A 1 2793 ? 133.022 163.177 170.813 1.00 43.92  ? 2793 ILE A O     1 
ATOM   11490 C CB    . ILE A 1 2793 ? 135.993 163.994 171.262 1.00 43.92  ? 2793 ILE A CB    1 
ATOM   11491 C CG1   . ILE A 1 2793 ? 135.752 165.423 171.753 1.00 43.92  ? 2793 ILE A CG1   1 
ATOM   11492 C CG2   . ILE A 1 2793 ? 135.806 163.877 169.754 1.00 43.92  ? 2793 ILE A CG2   1 
ATOM   11493 C CD1   . ILE A 1 2793 ? 136.779 166.415 171.261 1.00 43.92  ? 2793 ILE A CD1   1 
ATOM   11494 N N     . TYR A 1 2794 ? 133.034 163.877 172.959 1.00 41.70  ? 2794 TYR A N     1 
ATOM   11495 C CA    . TYR A 1 2794 ? 131.620 164.219 172.997 1.00 41.70  ? 2794 TYR A CA    1 
ATOM   11496 C C     . TYR A 1 2794 ? 131.462 165.690 173.348 1.00 41.70  ? 2794 TYR A C     1 
ATOM   11497 O O     . TYR A 1 2794 ? 132.195 166.221 174.188 1.00 41.70  ? 2794 TYR A O     1 
ATOM   11498 C CB    . TYR A 1 2794 ? 130.861 163.352 174.009 1.00 41.70  ? 2794 TYR A CB    1 
ATOM   11499 C CG    . TYR A 1 2794 ? 130.642 161.924 173.559 1.00 41.70  ? 2794 TYR A CG    1 
ATOM   11500 C CD1   . TYR A 1 2794 ? 129.364 161.389 173.484 1.00 41.70  ? 2794 TYR A CD1   1 
ATOM   11501 C CD2   . TYR A 1 2794 ? 131.713 161.104 173.230 1.00 41.70  ? 2794 TYR A CD2   1 
ATOM   11502 C CE1   . TYR A 1 2794 ? 129.160 160.086 173.077 1.00 41.70  ? 2794 TYR A CE1   1 
ATOM   11503 C CE2   . TYR A 1 2794 ? 131.518 159.801 172.824 1.00 41.70  ? 2794 TYR A CE2   1 
ATOM   11504 C CZ    . TYR A 1 2794 ? 130.240 159.296 172.750 1.00 41.70  ? 2794 TYR A CZ    1 
ATOM   11505 O OH    . TYR A 1 2794 ? 130.041 157.996 172.347 1.00 41.70  ? 2794 TYR A OH    1 
ATOM   11506 N N     . SER A 1 2795 ? 130.505 166.342 172.703 1.00 35.36  ? 2795 SER A N     1 
ATOM   11507 C CA    . SER A 1 2795 ? 130.305 167.775 172.854 1.00 35.36  ? 2795 SER A CA    1 
ATOM   11508 C C     . SER A 1 2795 ? 128.838 168.075 172.607 1.00 35.36  ? 2795 SER A C     1 
ATOM   11509 O O     . SER A 1 2795 ? 128.111 167.246 172.047 1.00 35.36  ? 2795 SER A O     1 
ATOM   11510 C CB    . SER A 1 2795 ? 131.192 168.564 171.885 1.00 35.36  ? 2795 SER A CB    1 
ATOM   11511 O OG    . SER A 1 2795 ? 130.776 168.372 170.544 1.00 35.36  ? 2795 SER A OG    1 
ATOM   11512 N N     . PRO A 1 2796 ? 128.363 169.254 173.025 1.00 34.01  ? 2796 PRO A N     1 
ATOM   11513 C CA    . PRO A 1 2796 ? 126.987 169.651 172.681 1.00 34.01  ? 2796 PRO A CA    1 
ATOM   11514 C C     . PRO A 1 2796 ? 126.723 169.716 171.186 1.00 34.01  ? 2796 PRO A C     1 
ATOM   11515 O O     . PRO A 1 2796 ? 125.555 169.829 170.793 1.00 34.01  ? 2796 PRO A O     1 
ATOM   11516 C CB    . PRO A 1 2796 ? 126.836 171.032 173.337 1.00 34.01  ? 2796 PRO A CB    1 
ATOM   11517 C CG    . PRO A 1 2796 ? 128.208 171.435 173.761 1.00 34.01  ? 2796 PRO A CG    1 
ATOM   11518 C CD    . PRO A 1 2796 ? 128.962 170.174 174.002 1.00 34.01  ? 2796 PRO A CD    1 
ATOM   11519 N N     . ARG A 1 2797 ? 127.757 169.654 170.343 1.00 36.13  ? 2797 ARG A N     1 
ATOM   11520 C CA    . ARG A 1 2797 ? 127.527 169.464 168.915 1.00 36.13  ? 2797 ARG A CA    1 
ATOM   11521 C C     . ARG A 1 2797 ? 126.791 168.157 168.655 1.00 36.13  ? 2797 ARG A C     1 
ATOM   11522 O O     . ARG A 1 2797 ? 125.945 168.080 167.757 1.00 36.13  ? 2797 ARG A O     1 
ATOM   11523 C CB    . ARG A 1 2797 ? 128.852 169.484 168.156 1.00 36.13  ? 2797 ARG A CB    1 
ATOM   11524 C CG    . ARG A 1 2797 ? 129.465 170.856 167.993 1.00 36.13  ? 2797 ARG A CG    1 
ATOM   11525 C CD    . ARG A 1 2797 ? 130.801 170.765 167.282 1.00 36.13  ? 2797 ARG A CD    1 
ATOM   11526 N NE    . ARG A 1 2797 ? 131.400 172.076 167.071 1.00 36.13  ? 2797 ARG A NE    1 
ATOM   11527 C CZ    . ARG A 1 2797 ? 132.636 172.271 166.634 1.00 36.13  ? 2797 ARG A CZ    1 
ATOM   11528 N NH1   . ARG A 1 2797 ? 133.445 171.257 166.378 1.00 36.13  ? 2797 ARG A NH1   1 
ATOM   11529 N NH2   . ARG A 1 2797 ? 133.073 173.514 166.457 1.00 36.13  ? 2797 ARG A NH2   1 
ATOM   11530 N N     . GLU A 1 2798 ? 127.104 167.117 169.431 1.00 35.90  ? 2798 GLU A N     1 
ATOM   11531 C CA    . GLU A 1 2798 ? 126.402 165.848 169.278 1.00 35.90  ? 2798 GLU A CA    1 
ATOM   11532 C C     . GLU A 1 2798 ? 124.918 166.002 169.577 1.00 35.90  ? 2798 GLU A C     1 
ATOM   11533 O O     . GLU A 1 2798 ? 124.073 165.482 168.842 1.00 35.90  ? 2798 GLU A O     1 
ATOM   11534 C CB    . GLU A 1 2798 ? 127.024 164.788 170.186 1.00 35.90  ? 2798 GLU A CB    1 
ATOM   11535 C CG    . GLU A 1 2798 ? 128.513 164.564 169.963 1.00 35.90  ? 2798 GLU A CG    1 
ATOM   11536 C CD    . GLU A 1 2798 ? 128.849 164.178 168.535 1.00 35.90  ? 2798 GLU A CD    1 
ATOM   11537 O OE1   . GLU A 1 2798 ? 128.016 163.520 167.878 1.00 35.90  ? 2798 GLU A OE1   1 
ATOM   11538 O OE2   . GLU A 1 2798 ? 129.951 164.532 168.068 1.00 35.90  ? 2798 GLU A OE2   1 
ATOM   11539 N N     . MET A 1 2799 ? 124.576 166.732 170.641 1.00 31.66  ? 2799 MET A N     1 
ATOM   11540 C CA    . MET A 1 2799 ? 123.166 166.917 170.966 1.00 31.66  ? 2799 MET A CA    1 
ATOM   11541 C C     . MET A 1 2799 ? 122.488 167.840 169.961 1.00 31.66  ? 2799 MET A C     1 
ATOM   11542 O O     . MET A 1 2799 ? 121.290 167.699 169.688 1.00 31.66  ? 2799 MET A O     1 
ATOM   11543 C CB    . MET A 1 2799 ? 123.015 167.455 172.387 1.00 31.66  ? 2799 MET A CB    1 
ATOM   11544 C CG    . MET A 1 2799 ? 123.204 166.391 173.455 1.00 31.66  ? 2799 MET A CG    1 
ATOM   11545 S SD    . MET A 1 2799 ? 122.356 166.748 175.002 1.00 31.66  ? 2799 MET A SD    1 
ATOM   11546 C CE    . MET A 1 2799 ? 120.728 167.174 174.397 1.00 31.66  ? 2799 MET A CE    1 
ATOM   11547 N N     . THR A 1 2800 ? 123.237 168.790 169.397 1.00 34.55  ? 2800 THR A N     1 
ATOM   11548 C CA    . THR A 1 2800 ? 122.688 169.622 168.332 1.00 34.55  ? 2800 THR A CA    1 
ATOM   11549 C C     . THR A 1 2800 ? 122.339 168.784 167.108 1.00 34.55  ? 2800 THR A C     1 
ATOM   11550 O O     . THR A 1 2800 ? 121.262 168.948 166.523 1.00 34.55  ? 2800 THR A O     1 
ATOM   11551 C CB    . THR A 1 2800 ? 123.674 170.729 167.962 1.00 34.55  ? 2800 THR A CB    1 
ATOM   11552 O OG1   . THR A 1 2800 ? 123.833 171.618 169.075 1.00 34.55  ? 2800 THR A OG1   1 
ATOM   11553 C CG2   . THR A 1 2800 ? 123.170 171.515 166.763 1.00 34.55  ? 2800 THR A CG2   1 
ATOM   11554 N N     . ARG A 1 2801 ? 123.232 167.874 166.711 1.00 32.82  ? 2801 ARG A N     1 
ATOM   11555 C CA    . ARG A 1 2801 ? 122.915 166.958 165.618 1.00 32.82  ? 2801 ARG A CA    1 
ATOM   11556 C C     . ARG A 1 2801 ? 121.748 166.052 165.987 1.00 32.82  ? 2801 ARG A C     1 
ATOM   11557 O O     . ARG A 1 2801 ? 120.919 165.714 165.137 1.00 32.82  ? 2801 ARG A O     1 
ATOM   11558 C CB    . ARG A 1 2801 ? 124.136 166.119 165.240 1.00 32.82  ? 2801 ARG A CB    1 
ATOM   11559 C CG    . ARG A 1 2801 ? 125.395 166.900 164.939 1.00 32.82  ? 2801 ARG A CG    1 
ATOM   11560 C CD    . ARG A 1 2801 ? 126.394 166.020 164.209 1.00 32.82  ? 2801 ARG A CD    1 
ATOM   11561 N NE    . ARG A 1 2801 ? 127.771 166.434 164.445 1.00 32.82  ? 2801 ARG A NE    1 
ATOM   11562 C CZ    . ARG A 1 2801 ? 128.708 165.650 164.959 1.00 32.82  ? 2801 ARG A CZ    1 
ATOM   11563 N NH1   . ARG A 1 2801 ? 128.448 164.401 165.310 1.00 32.82  ? 2801 ARG A NH1   1 
ATOM   11564 N NH2   . ARG A 1 2801 ? 129.936 166.131 165.127 1.00 32.82  ? 2801 ARG A NH2   1 
ATOM   11565 N N     . TRP A 1 2802 ? 121.679 165.637 167.252 1.00 32.72  ? 2802 TRP A N     1 
ATOM   11566 C CA    . TRP A 1 2802 ? 120.572 164.813 167.722 1.00 32.72  ? 2802 TRP A CA    1 
ATOM   11567 C C     . TRP A 1 2802 ? 119.233 165.514 167.566 1.00 32.72  ? 2802 TRP A C     1 
ATOM   11568 O O     . TRP A 1 2802 ? 118.270 164.896 167.101 1.00 32.72  ? 2802 TRP A O     1 
ATOM   11569 C CB    . TRP A 1 2802 ? 120.807 164.444 169.186 1.00 32.72  ? 2802 TRP A CB    1 
ATOM   11570 C CG    . TRP A 1 2802 ? 120.028 163.273 169.669 1.00 32.72  ? 2802 TRP A CG    1 
ATOM   11571 C CD1   . TRP A 1 2802 ? 119.028 162.623 169.014 1.00 32.72  ? 2802 TRP A CD1   1 
ATOM   11572 C CD2   . TRP A 1 2802 ? 120.191 162.602 170.921 1.00 32.72  ? 2802 TRP A CD2   1 
ATOM   11573 N NE1   . TRP A 1 2802 ? 118.553 161.589 169.781 1.00 32.72  ? 2802 TRP A NE1   1 
ATOM   11574 C CE2   . TRP A 1 2802 ? 119.253 161.555 170.958 1.00 32.72  ? 2802 TRP A CE2   1 
ATOM   11575 C CE3   . TRP A 1 2802 ? 121.038 162.788 172.017 1.00 32.72  ? 2802 TRP A CE3   1 
ATOM   11576 C CZ2   . TRP A 1 2802 ? 119.139 160.696 172.046 1.00 32.72  ? 2802 TRP A CZ2   1 
ATOM   11577 C CZ3   . TRP A 1 2802 ? 120.924 161.934 173.094 1.00 32.72  ? 2802 TRP A CZ3   1 
ATOM   11578 C CH2   . TRP A 1 2802 ? 119.981 160.902 173.102 1.00 32.72  ? 2802 TRP A CH2   1 
ATOM   11579 N N     . VAL A 1 2803 ? 119.155 166.785 167.939 1.00 33.83  ? 2803 VAL A N     1 
ATOM   11580 C CA    . VAL A 1 2803 ? 117.932 167.559 167.759 1.00 33.83  ? 2803 VAL A CA    1 
ATOM   11581 C C     . VAL A 1 2803 ? 117.647 167.808 166.282 1.00 33.83  ? 2803 VAL A C     1 
ATOM   11582 O O     . VAL A 1 2803 ? 116.497 167.713 165.842 1.00 33.83  ? 2803 VAL A O     1 
ATOM   11583 C CB    . VAL A 1 2803 ? 118.030 168.879 168.548 1.00 33.83  ? 2803 VAL A CB    1 
ATOM   11584 C CG1   . VAL A 1 2803 ? 116.913 169.825 168.148 1.00 33.83  ? 2803 VAL A CG1   1 
ATOM   11585 C CG2   . VAL A 1 2803 ? 117.990 168.603 170.039 1.00 33.83  ? 2803 VAL A CG2   1 
ATOM   11586 N N     . ARG A 1 2804 ? 118.684 168.120 165.500 1.00 35.93  ? 2804 ARG A N     1 
ATOM   11587 C CA    . ARG A 1 2804 ? 118.489 168.424 164.087 1.00 35.93  ? 2804 ARG A CA    1 
ATOM   11588 C C     . ARG A 1 2804 ? 117.982 167.211 163.317 1.00 35.93  ? 2804 ARG A C     1 
ATOM   11589 O O     . ARG A 1 2804 ? 117.131 167.347 162.433 1.00 35.93  ? 2804 ARG A O     1 
ATOM   11590 C CB    . ARG A 1 2804 ? 119.791 168.938 163.476 1.00 35.93  ? 2804 ARG A CB    1 
ATOM   11591 C CG    . ARG A 1 2804 ? 119.675 169.318 162.010 1.00 35.93  ? 2804 ARG A CG    1 
ATOM   11592 C CD    . ARG A 1 2804 ? 120.981 169.884 161.481 1.00 35.93  ? 2804 ARG A CD    1 
ATOM   11593 N NE    . ARG A 1 2804 ? 121.295 171.177 162.076 1.00 35.93  ? 2804 ARG A NE    1 
ATOM   11594 C CZ    . ARG A 1 2804 ? 122.431 171.834 161.885 1.00 35.93  ? 2804 ARG A CZ    1 
ATOM   11595 N NH1   . ARG A 1 2804 ? 123.389 171.348 161.113 1.00 35.93  ? 2804 ARG A NH1   1 
ATOM   11596 N NH2   . ARG A 1 2804 ? 122.610 173.008 162.483 1.00 35.93  ? 2804 ARG A NH2   1 
ATOM   11597 N N     . GLY A 1 2805 ? 118.497 166.020 163.627 1.00 33.64  ? 2805 GLY A N     1 
ATOM   11598 C CA    . GLY A 1 2805 ? 118.026 164.824 162.947 1.00 33.64  ? 2805 GLY A CA    1 
ATOM   11599 C C     . GLY A 1 2805 ? 116.574 164.516 163.254 1.00 33.64  ? 2805 GLY A C     1 
ATOM   11600 O O     . GLY A 1 2805 ? 115.801 164.162 162.358 1.00 33.64  ? 2805 GLY A O     1 
ATOM   11601 N N     . ILE A 1 2806 ? 116.181 164.652 164.522 1.00 28.36  ? 2806 ILE A N     1 
ATOM   11602 C CA    . ILE A 1 2806 ? 114.786 164.442 164.893 1.00 28.36  ? 2806 ILE A CA    1 
ATOM   11603 C C     . ILE A 1 2806 ? 113.896 165.460 164.195 1.00 28.36  ? 2806 ILE A C     1 
ATOM   11604 O O     . ILE A 1 2806 ? 112.814 165.124 163.698 1.00 28.36  ? 2806 ILE A O     1 
ATOM   11605 C CB    . ILE A 1 2806 ? 114.626 164.500 166.422 1.00 28.36  ? 2806 ILE A CB    1 
ATOM   11606 C CG1   . ILE A 1 2806 ? 115.388 163.350 167.079 1.00 28.36  ? 2806 ILE A CG1   1 
ATOM   11607 C CG2   . ILE A 1 2806 ? 113.159 164.448 166.807 1.00 28.36  ? 2806 ILE A CG2   1 
ATOM   11608 C CD1   . ILE A 1 2806 ? 115.226 163.293 168.580 1.00 28.36  ? 2806 ILE A CD1   1 
ATOM   11609 N N     . PHE A 1 2807 ? 114.336 166.720 164.142 1.00 40.07  ? 2807 PHE A N     1 
ATOM   11610 C CA    . PHE A 1 2807 ? 113.554 167.742 163.454 1.00 40.07  ? 2807 PHE A CA    1 
ATOM   11611 C C     . PHE A 1 2807 ? 113.427 167.438 161.966 1.00 40.07  ? 2807 PHE A C     1 
ATOM   11612 O O     . PHE A 1 2807 ? 112.355 167.616 161.380 1.00 40.07  ? 2807 PHE A O     1 
ATOM   11613 C CB    . PHE A 1 2807 ? 114.180 169.118 163.662 1.00 40.07  ? 2807 PHE A CB    1 
ATOM   11614 C CG    . PHE A 1 2807 ? 113.577 170.185 162.801 1.00 40.07  ? 2807 PHE A CG    1 
ATOM   11615 C CD1   . PHE A 1 2807 ? 112.299 170.651 163.049 1.00 40.07  ? 2807 PHE A CD1   1 
ATOM   11616 C CD2   . PHE A 1 2807 ? 114.284 170.715 161.735 1.00 40.07  ? 2807 PHE A CD2   1 
ATOM   11617 C CE1   . PHE A 1 2807 ? 111.738 171.628 162.253 1.00 40.07  ? 2807 PHE A CE1   1 
ATOM   11618 C CE2   . PHE A 1 2807 ? 113.730 171.693 160.936 1.00 40.07  ? 2807 PHE A CE2   1 
ATOM   11619 C CZ    . PHE A 1 2807 ? 112.455 172.151 161.196 1.00 40.07  ? 2807 PHE A CZ    1 
ATOM   11620 N N     . GLU A 1 2808 ? 114.513 166.988 161.336 1.00 37.21  ? 2808 GLU A N     1 
ATOM   11621 C CA    . GLU A 1 2808 ? 114.461 166.653 159.917 1.00 37.21  ? 2808 GLU A CA    1 
ATOM   11622 C C     . GLU A 1 2808 ? 113.518 165.484 159.666 1.00 37.21  ? 2808 GLU A C     1 
ATOM   11623 O O     . GLU A 1 2808 ? 112.787 165.468 158.669 1.00 37.21  ? 2808 GLU A O     1 
ATOM   11624 C CB    . GLU A 1 2808 ? 115.863 166.332 159.402 1.00 37.21  ? 2808 GLU A CB    1 
ATOM   11625 C CG    . GLU A 1 2808 ? 115.925 166.008 157.918 1.00 37.21  ? 2808 GLU A CG    1 
ATOM   11626 C CD    . GLU A 1 2808 ? 115.647 167.214 157.042 1.00 37.21  ? 2808 GLU A CD    1 
ATOM   11627 O OE1   . GLU A 1 2808 ? 115.891 168.351 157.495 1.00 37.21  ? 2808 GLU A OE1   1 
ATOM   11628 O OE2   . GLU A 1 2808 ? 115.185 167.023 155.897 1.00 37.21  ? 2808 GLU A OE2   1 
ATOM   11629 N N     . ALA A 1 2809 ? 113.526 164.494 160.557 1.00 35.96  ? 2809 ALA A N     1 
ATOM   11630 C CA    . ALA A 1 2809 ? 112.644 163.346 160.388 1.00 35.96  ? 2809 ALA A CA    1 
ATOM   11631 C C     . ALA A 1 2809 ? 111.185 163.722 160.623 1.00 35.96  ? 2809 ALA A C     1 
ATOM   11632 O O     . ALA A 1 2809 ? 110.286 163.159 159.988 1.00 35.96  ? 2809 ALA A O     1 
ATOM   11633 C CB    . ALA A 1 2809 ? 113.074 162.218 161.323 1.00 35.96  ? 2809 ALA A CB    1 
ATOM   11634 N N     . LEU A 1 2810 ? 110.926 164.661 161.535 1.00 36.24  ? 2810 LEU A N     1 
ATOM   11635 C CA    . LEU A 1 2810 ? 109.560 165.088 161.820 1.00 36.24  ? 2810 LEU A CA    1 
ATOM   11636 C C     . LEU A 1 2810 ? 109.056 166.180 160.884 1.00 36.24  ? 2810 LEU A C     1 
ATOM   11637 O O     . LEU A 1 2810 ? 107.859 166.483 160.909 1.00 36.24  ? 2810 LEU A O     1 
ATOM   11638 C CB    . LEU A 1 2810 ? 109.452 165.582 163.265 1.00 36.24  ? 2810 LEU A CB    1 
ATOM   11639 C CG    . LEU A 1 2810 ? 109.058 164.573 164.344 1.00 36.24  ? 2810 LEU A CG    1 
ATOM   11640 C CD1   . LEU A 1 2810 ? 110.129 163.517 164.524 1.00 36.24  ? 2810 LEU A CD1   1 
ATOM   11641 C CD2   . LEU A 1 2810 ? 108.796 165.289 165.656 1.00 36.24  ? 2810 LEU A CD2   1 
ATOM   11642 N N     . ARG A 1 2811 ? 109.931 166.781 160.079 1.00 43.79  ? 2811 ARG A N     1 
ATOM   11643 C CA    . ARG A 1 2811 ? 109.514 167.896 159.229 1.00 43.79  ? 2811 ARG A CA    1 
ATOM   11644 C C     . ARG A 1 2811 ? 108.414 167.534 158.237 1.00 43.79  ? 2811 ARG A C     1 
ATOM   11645 O O     . ARG A 1 2811 ? 107.396 168.246 158.197 1.00 43.79  ? 2811 ARG A O     1 
ATOM   11646 C CB    . ARG A 1 2811 ? 110.740 168.473 158.514 1.00 43.79  ? 2811 ARG A CB    1 
ATOM   11647 C CG    . ARG A 1 2811 ? 110.412 169.367 157.334 1.00 43.79  ? 2811 ARG A CG    1 
ATOM   11648 C CD    . ARG A 1 2811 ? 110.493 170.835 157.716 1.00 43.79  ? 2811 ARG A CD    1 
ATOM   11649 N NE    . ARG A 1 2811 ? 111.848 171.228 158.085 1.00 43.79  ? 2811 ARG A NE    1 
ATOM   11650 C CZ    . ARG A 1 2811 ? 112.849 171.381 157.227 1.00 43.79  ? 2811 ARG A CZ    1 
ATOM   11651 N NH1   . ARG A 1 2811 ? 112.683 171.189 155.928 1.00 43.79  ? 2811 ARG A NH1   1 
ATOM   11652 N NH2   . ARG A 1 2811 ? 114.046 171.737 157.684 1.00 43.79  ? 2811 ARG A NH2   1 
ATOM   11653 N N     . PRO A 1 2812 ? 108.528 166.470 157.420 1.00 45.62  ? 2812 PRO A N     1 
ATOM   11654 C CA    . PRO A 1 2812 ? 107.458 166.200 156.450 1.00 45.62  ? 2812 PRO A CA    1 
ATOM   11655 C C     . PRO A 1 2812 ? 106.302 165.423 157.056 1.00 45.62  ? 2812 PRO A C     1 
ATOM   11656 O O     . PRO A 1 2812 ? 105.165 165.507 156.583 1.00 45.62  ? 2812 PRO A O     1 
ATOM   11657 C CB    . PRO A 1 2812 ? 108.174 165.389 155.366 1.00 45.62  ? 2812 PRO A CB    1 
ATOM   11658 C CG    . PRO A 1 2812 ? 109.232 164.650 156.108 1.00 45.62  ? 2812 PRO A CG    1 
ATOM   11659 C CD    . PRO A 1 2812 ? 109.627 165.492 157.299 1.00 45.62  ? 2812 PRO A CD    1 
ATOM   11660 N N     . LEU A 1 2813 ? 106.589 164.665 158.109 1.00 47.51  ? 2813 LEU A N     1 
ATOM   11661 C CA    . LEU A 1 2813 ? 105.609 163.782 158.717 1.00 47.51  ? 2813 LEU A CA    1 
ATOM   11662 C C     . LEU A 1 2813 ? 104.587 164.568 159.530 1.00 47.51  ? 2813 LEU A C     1 
ATOM   11663 O O     . LEU A 1 2813 ? 104.918 165.535 160.220 1.00 47.51  ? 2813 LEU A O     1 
ATOM   11664 C CB    . LEU A 1 2813 ? 106.318 162.754 159.598 1.00 47.51  ? 2813 LEU A CB    1 
ATOM   11665 C CG    . LEU A 1 2813 ? 105.477 161.687 160.286 1.00 47.51  ? 2813 LEU A CG    1 
ATOM   11666 C CD1   . LEU A 1 2813 ? 104.792 160.825 159.251 1.00 47.51  ? 2813 LEU A CD1   1 
ATOM   11667 C CD2   . LEU A 1 2813 ? 106.388 160.837 161.141 1.00 47.51  ? 2813 LEU A CD2   1 
ATOM   11668 N N     . GLU A 1 2814 ? 103.330 164.134 159.444 1.00 59.29  ? 2814 GLU A N     1 
ATOM   11669 C CA    . GLU A 1 2814 ? 102.225 164.781 160.134 1.00 59.29  ? 2814 GLU A CA    1 
ATOM   11670 C C     . GLU A 1 2814 ? 101.391 163.718 160.837 1.00 59.29  ? 2814 GLU A C     1 
ATOM   11671 O O     . GLU A 1 2814 ? 101.279 162.584 160.361 1.00 59.29  ? 2814 GLU A O     1 
ATOM   11672 C CB    . GLU A 1 2814 ? 101.369 165.604 159.147 1.00 59.29  ? 2814 GLU A CB    1 
ATOM   11673 C CG    . GLU A 1 2814 ? 99.982  166.000 159.635 1.00 59.29  ? 2814 GLU A CG    1 
ATOM   11674 C CD    . GLU A 1 2814 ? 100.024 166.951 160.817 1.00 59.29  ? 2814 GLU A CD    1 
ATOM   11675 O OE1   . GLU A 1 2814 ? 100.230 168.163 160.600 1.00 59.29  ? 2814 GLU A OE1   1 
ATOM   11676 O OE2   . GLU A 1 2814 ? 99.846  166.489 161.963 1.00 59.29  ? 2814 GLU A OE2   1 
ATOM   11677 N N     . THR A 1 2815 ? 100.818 164.094 161.983 1.00 63.02  ? 2815 THR A N     1 
ATOM   11678 C CA    . THR A 1 2815 ? 100.043 163.191 162.839 1.00 63.02  ? 2815 THR A CA    1 
ATOM   11679 C C     . THR A 1 2815 ? 100.891 161.997 163.283 1.00 63.02  ? 2815 THR A C     1 
ATOM   11680 O O     . THR A 1 2815 ? 100.629 160.843 162.936 1.00 63.02  ? 2815 THR A O     1 
ATOM   11681 C CB    . THR A 1 2815 ? 98.753  162.722 162.151 1.00 63.02  ? 2815 THR A CB    1 
ATOM   11682 O OG1   . THR A 1 2815 ? 99.071  161.885 161.032 1.00 63.02  ? 2815 THR A OG1   1 
ATOM   11683 C CG2   . THR A 1 2815 ? 97.930  163.908 161.678 1.00 63.02  ? 2815 THR A CG2   1 
ATOM   11684 N N     . LEU A 1 2816 ? 101.926 162.300 164.066 1.00 55.70  ? 2816 LEU A N     1 
ATOM   11685 C CA    . LEU A 1 2816 ? 102.826 161.289 164.608 1.00 55.70  ? 2816 LEU A CA    1 
ATOM   11686 C C     . LEU A 1 2816 ? 102.534 161.046 166.078 1.00 55.70  ? 2816 LEU A C     1 
ATOM   11687 O O     . LEU A 1 2816 ? 102.531 162.001 166.868 1.00 55.70  ? 2816 LEU A O     1 
ATOM   11688 C CB    . LEU A 1 2816 ? 104.279 161.718 164.446 1.00 55.70  ? 2816 LEU A CB    1 
ATOM   11689 C CG    . LEU A 1 2816 ? 105.292 160.685 164.937 1.00 55.70  ? 2816 LEU A CG    1 
ATOM   11690 C CD1   . LEU A 1 2816 ? 105.187 159.398 164.134 1.00 55.70  ? 2816 LEU A CD1   1 
ATOM   11691 C CD2   . LEU A 1 2816 ? 106.699 161.254 164.884 1.00 55.70  ? 2816 LEU A CD2   1 
ATOM   11692 N N     . PRO A 1 2817 ? 102.281 159.801 166.485 1.00 56.46  ? 2817 PRO A N     1 
ATOM   11693 C CA    . PRO A 1 2817 ? 102.123 159.513 167.916 1.00 56.46  ? 2817 PRO A CA    1 
ATOM   11694 C C     . PRO A 1 2817 ? 103.455 159.514 168.649 1.00 56.46  ? 2817 PRO A C     1 
ATOM   11695 O O     . PRO A 1 2817 ? 104.510 159.706 168.035 1.00 56.46  ? 2817 PRO A O     1 
ATOM   11696 C CB    . PRO A 1 2817 ? 101.478 158.123 167.923 1.00 56.46  ? 2817 PRO A CB    1 
ATOM   11697 C CG    . PRO A 1 2817 ? 101.942 157.499 166.656 1.00 56.46  ? 2817 PRO A CG    1 
ATOM   11698 C CD    . PRO A 1 2817 ? 102.018 158.616 165.650 1.00 56.46  ? 2817 PRO A CD    1 
ATOM   11699 N N     . VAL A 1 2818 ? 103.413 159.303 169.967 1.00 58.01  ? 2818 VAL A N     1 
ATOM   11700 C CA    . VAL A 1 2818 ? 104.636 159.277 170.767 1.00 58.01  ? 2818 VAL A CA    1 
ATOM   11701 C C     . VAL A 1 2818 ? 105.529 158.121 170.346 1.00 58.01  ? 2818 VAL A C     1 
ATOM   11702 O O     . VAL A 1 2818 ? 106.759 158.178 170.507 1.00 58.01  ? 2818 VAL A O     1 
ATOM   11703 C CB    . VAL A 1 2818 ? 104.278 159.211 172.266 1.00 58.01  ? 2818 VAL A CB    1 
ATOM   11704 C CG1   . VAL A 1 2818 ? 103.543 157.914 172.594 1.00 58.01  ? 2818 VAL A CG1   1 
ATOM   11705 C CG2   . VAL A 1 2818 ? 105.516 159.384 173.129 1.00 58.01  ? 2818 VAL A CG2   1 
ATOM   11706 N N     . GLU A 1 2819 ? 104.932 157.064 169.795 1.00 59.36  ? 2819 GLU A N     1 
ATOM   11707 C CA    . GLU A 1 2819 ? 105.705 155.907 169.365 1.00 59.36  ? 2819 GLU A CA    1 
ATOM   11708 C C     . GLU A 1 2819 ? 106.761 156.304 168.343 1.00 59.36  ? 2819 GLU A C     1 
ATOM   11709 O O     . GLU A 1 2819 ? 107.951 156.023 168.524 1.00 59.36  ? 2819 GLU A O     1 
ATOM   11710 C CB    . GLU A 1 2819 ? 104.765 154.848 168.789 1.00 59.36  ? 2819 GLU A CB    1 
ATOM   11711 C CG    . GLU A 1 2819 ? 104.061 153.998 169.834 1.00 59.36  ? 2819 GLU A CG    1 
ATOM   11712 C CD    . GLU A 1 2819 ? 102.890 154.711 170.480 1.00 59.36  ? 2819 GLU A CD    1 
ATOM   11713 O OE1   . GLU A 1 2819 ? 102.593 155.857 170.082 1.00 59.36  ? 2819 GLU A OE1   1 
ATOM   11714 O OE2   . GLU A 1 2819 ? 102.261 154.120 171.383 1.00 59.36  ? 2819 GLU A OE2   1 
ATOM   11715 N N     . GLY A 1 2820 ? 106.347 156.987 167.274 1.00 54.37  ? 2820 GLY A N     1 
ATOM   11716 C CA    . GLY A 1 2820 ? 107.300 157.396 166.257 1.00 54.37  ? 2820 GLY A CA    1 
ATOM   11717 C C     . GLY A 1 2820 ? 108.320 158.386 166.781 1.00 54.37  ? 2820 GLY A C     1 
ATOM   11718 O O     . GLY A 1 2820 ? 109.487 158.356 166.386 1.00 54.37  ? 2820 GLY A O     1 
ATOM   11719 N N     . LEU A 1 2821 ? 107.896 159.274 167.682 1.00 48.52  ? 2821 LEU A N     1 
ATOM   11720 C CA    . LEU A 1 2821 ? 108.821 160.236 168.272 1.00 48.52  ? 2821 LEU A CA    1 
ATOM   11721 C C     . LEU A 1 2821 ? 109.957 159.530 168.999 1.00 48.52  ? 2821 LEU A C     1 
ATOM   11722 O O     . LEU A 1 2821 ? 111.136 159.833 168.780 1.00 48.52  ? 2821 LEU A O     1 
ATOM   11723 C CB    . LEU A 1 2821 ? 108.071 161.164 169.227 1.00 48.52  ? 2821 LEU A CB    1 
ATOM   11724 C CG    . LEU A 1 2821 ? 108.908 162.235 169.927 1.00 48.52  ? 2821 LEU A CG    1 
ATOM   11725 C CD1   . LEU A 1 2821 ? 109.501 163.200 168.912 1.00 48.52  ? 2821 LEU A CD1   1 
ATOM   11726 C CD2   . LEU A 1 2821 ? 108.074 162.974 170.960 1.00 48.52  ? 2821 LEU A CD2   1 
ATOM   11727 N N     . ILE A 1 2822 ? 109.623 158.571 169.864 1.00 47.80  ? 2822 ILE A N     1 
ATOM   11728 C CA    . ILE A 1 2822 ? 110.665 157.895 170.630 1.00 47.80  ? 2822 ILE A CA    1 
ATOM   11729 C C     . ILE A 1 2822 ? 111.449 156.933 169.742 1.00 47.80  ? 2822 ILE A C     1 
ATOM   11730 O O     . ILE A 1 2822 ? 112.643 156.699 169.964 1.00 47.80  ? 2822 ILE A O     1 
ATOM   11731 C CB    . ILE A 1 2822 ? 110.050 157.201 171.857 1.00 47.80  ? 2822 ILE A CB    1 
ATOM   11732 C CG1   . ILE A 1 2822 ? 109.438 158.260 172.774 1.00 47.80  ? 2822 ILE A CG1   1 
ATOM   11733 C CG2   . ILE A 1 2822 ? 111.095 156.394 172.610 1.00 47.80  ? 2822 ILE A CG2   1 
ATOM   11734 C CD1   . ILE A 1 2822 ? 108.585 157.708 173.875 1.00 47.80  ? 2822 ILE A CD1   1 
ATOM   11735 N N     . ARG A 1 2823 ? 110.811 156.396 168.700 1.00 51.36  ? 2823 ARG A N     1 
ATOM   11736 C CA    . ARG A 1 2823 ? 111.534 155.596 167.715 1.00 51.36  ? 2823 ARG A CA    1 
ATOM   11737 C C     . ARG A 1 2823 ? 112.621 156.417 167.034 1.00 51.36  ? 2823 ARG A C     1 
ATOM   11738 O O     . ARG A 1 2823 ? 113.763 155.967 166.898 1.00 51.36  ? 2823 ARG A O     1 
ATOM   11739 C CB    . ARG A 1 2823 ? 110.554 155.042 166.680 1.00 51.36  ? 2823 ARG A CB    1 
ATOM   11740 C CG    . ARG A 1 2823 ? 110.993 153.779 165.936 1.00 51.36  ? 2823 ARG A CG    1 
ATOM   11741 C CD    . ARG A 1 2823 ? 110.765 152.512 166.727 1.00 51.36  ? 2823 ARG A CD    1 
ATOM   11742 N NE    . ARG A 1 2823 ? 111.572 151.390 166.263 1.00 51.36  ? 2823 ARG A NE    1 
ATOM   11743 C CZ    . ARG A 1 2823 ? 111.390 150.766 165.105 1.00 51.36  ? 2823 ARG A CZ    1 
ATOM   11744 N NH1   . ARG A 1 2823 ? 110.449 151.143 164.255 1.00 51.36  ? 2823 ARG A NH1   1 
ATOM   11745 N NH2   . ARG A 1 2823 ? 112.159 149.727 164.800 1.00 51.36  ? 2823 ARG A NH2   1 
ATOM   11746 N N     . ILE A 1 2824 ? 112.279 157.633 166.603 1.00 41.06  ? 2824 ILE A N     1 
ATOM   11747 C CA    . ILE A 1 2824 ? 113.250 158.502 165.947 1.00 41.06  ? 2824 ILE A CA    1 
ATOM   11748 C C     . ILE A 1 2824 ? 114.316 158.959 166.934 1.00 41.06  ? 2824 ILE A C     1 
ATOM   11749 O O     . ILE A 1 2824 ? 115.495 159.068 166.577 1.00 41.06  ? 2824 ILE A O     1 
ATOM   11750 C CB    . ILE A 1 2824 ? 112.523 159.690 165.295 1.00 41.06  ? 2824 ILE A CB    1 
ATOM   11751 C CG1   . ILE A 1 2824 ? 111.554 159.176 164.231 1.00 41.06  ? 2824 ILE A CG1   1 
ATOM   11752 C CG2   . ILE A 1 2824 ? 113.519 160.656 164.681 1.00 41.06  ? 2824 ILE A CG2   1 
ATOM   11753 C CD1   . ILE A 1 2824 ? 111.020 160.232 163.312 1.00 41.06  ? 2824 ILE A CD1   1 
ATOM   11754 N N     . TRP A 1 2825 ? 113.925 159.231 168.181 1.00 40.00  ? 2825 TRP A N     1 
ATOM   11755 C CA    . TRP A 1 2825 ? 114.899 159.549 169.222 1.00 40.00  ? 2825 TRP A CA    1 
ATOM   11756 C C     . TRP A 1 2825 ? 115.924 158.432 169.373 1.00 40.00  ? 2825 TRP A C     1 
ATOM   11757 O O     . TRP A 1 2825 ? 117.138 158.676 169.366 1.00 40.00  ? 2825 TRP A O     1 
ATOM   11758 C CB    . TRP A 1 2825 ? 114.165 159.799 170.542 1.00 40.00  ? 2825 TRP A CB    1 
ATOM   11759 C CG    . TRP A 1 2825 ? 115.047 160.042 171.732 1.00 40.00  ? 2825 TRP A CG    1 
ATOM   11760 C CD1   . TRP A 1 2825 ? 115.447 161.249 172.217 1.00 40.00  ? 2825 TRP A CD1   1 
ATOM   11761 C CD2   . TRP A 1 2825 ? 115.597 159.054 172.615 1.00 40.00  ? 2825 TRP A CD2   1 
ATOM   11762 N NE1   . TRP A 1 2825 ? 116.227 161.077 173.332 1.00 40.00  ? 2825 TRP A NE1   1 
ATOM   11763 C CE2   . TRP A 1 2825 ? 116.336 159.738 173.597 1.00 40.00  ? 2825 TRP A CE2   1 
ATOM   11764 C CE3   . TRP A 1 2825 ? 115.545 157.659 172.662 1.00 40.00  ? 2825 TRP A CE3   1 
ATOM   11765 C CZ2   . TRP A 1 2825 ? 117.019 159.077 174.614 1.00 40.00  ? 2825 TRP A CZ2   1 
ATOM   11766 C CZ3   . TRP A 1 2825 ? 116.224 157.004 173.673 1.00 40.00  ? 2825 TRP A CZ3   1 
ATOM   11767 C CH2   . TRP A 1 2825 ? 116.951 157.713 174.635 1.00 40.00  ? 2825 TRP A CH2   1 
ATOM   11768 N N     . ALA A 1 2826 ? 115.448 157.192 169.489 1.00 37.75  ? 2826 ALA A N     1 
ATOM   11769 C CA    . ALA A 1 2826 ? 116.353 156.061 169.647 1.00 37.75  ? 2826 ALA A CA    1 
ATOM   11770 C C     . ALA A 1 2826 ? 117.206 155.854 168.403 1.00 37.75  ? 2826 ALA A C     1 
ATOM   11771 O O     . ALA A 1 2826 ? 118.393 155.537 168.510 1.00 37.75  ? 2826 ALA A O     1 
ATOM   11772 C CB    . ALA A 1 2826 ? 115.559 154.799 169.977 1.00 37.75  ? 2826 ALA A CB    1 
ATOM   11773 N N     . HIS A 1 2827 ? 116.626 156.026 167.214 1.00 37.60  ? 2827 HIS A N     1 
ATOM   11774 C CA    . HIS A 1 2827 ? 117.393 155.835 165.987 1.00 37.60  ? 2827 HIS A CA    1 
ATOM   11775 C C     . HIS A 1 2827 ? 118.505 156.870 165.865 1.00 37.60  ? 2827 HIS A C     1 
ATOM   11776 O O     . HIS A 1 2827 ? 119.629 156.548 165.465 1.00 37.60  ? 2827 HIS A O     1 
ATOM   11777 C CB    . HIS A 1 2827 ? 116.471 155.891 164.772 1.00 37.60  ? 2827 HIS A CB    1 
ATOM   11778 C CG    . HIS A 1 2827 ? 117.201 155.895 163.466 1.00 37.60  ? 2827 HIS A CG    1 
ATOM   11779 N ND1   . HIS A 1 2827 ? 117.953 154.825 163.032 1.00 37.60  ? 2827 HIS A ND1   1 
ATOM   11780 C CD2   . HIS A 1 2827 ? 117.297 156.838 162.500 1.00 37.60  ? 2827 HIS A CD2   1 
ATOM   11781 C CE1   . HIS A 1 2827 ? 118.480 155.108 161.855 1.00 37.60  ? 2827 HIS A CE1   1 
ATOM   11782 N NE2   . HIS A 1 2827 ? 118.097 156.324 161.509 1.00 37.60  ? 2827 HIS A NE2   1 
ATOM   11783 N N     . GLU A 1 2828 ? 118.207 158.128 166.198 1.00 34.25  ? 2828 GLU A N     1 
ATOM   11784 C CA    . GLU A 1 2828 ? 119.241 159.157 166.168 1.00 34.25  ? 2828 GLU A CA    1 
ATOM   11785 C C     . GLU A 1 2828 ? 120.309 158.893 167.221 1.00 34.25  ? 2828 GLU A C     1 
ATOM   11786 O O     . GLU A 1 2828 ? 121.500 159.125 166.977 1.00 34.25  ? 2828 GLU A O     1 
ATOM   11787 C CB    . GLU A 1 2828 ? 118.616 160.535 166.362 1.00 34.25  ? 2828 GLU A CB    1 
ATOM   11788 C CG    . GLU A 1 2828 ? 117.888 161.053 165.137 1.00 34.25  ? 2828 GLU A CG    1 
ATOM   11789 C CD    . GLU A 1 2828 ? 118.728 160.958 163.881 1.00 34.25  ? 2828 GLU A CD    1 
ATOM   11790 O OE1   . GLU A 1 2828 ? 119.906 161.370 163.921 1.00 34.25  ? 2828 GLU A OE1   1 
ATOM   11791 O OE2   . GLU A 1 2828 ? 118.211 160.474 162.852 1.00 34.25  ? 2828 GLU A OE2   1 
ATOM   11792 N N     . ALA A 1 2829 ? 119.904 158.409 168.397 1.00 34.73  ? 2829 ALA A N     1 
ATOM   11793 C CA    . ALA A 1 2829 ? 120.888 158.024 169.402 1.00 34.73  ? 2829 ALA A CA    1 
ATOM   11794 C C     . ALA A 1 2829 ? 121.783 156.904 168.888 1.00 34.73  ? 2829 ALA A C     1 
ATOM   11795 O O     . ALA A 1 2829 ? 122.990 156.899 169.141 1.00 34.73  ? 2829 ALA A O     1 
ATOM   11796 C CB    . ALA A 1 2829 ? 120.186 157.609 170.693 1.00 34.73  ? 2829 ALA A CB    1 
ATOM   11797 N N     . LEU A 1 2830 ? 121.203 155.940 168.170 1.00 36.86  ? 2830 LEU A N     1 
ATOM   11798 C CA    . LEU A 1 2830 ? 121.999 154.881 167.556 1.00 36.86  ? 2830 LEU A CA    1 
ATOM   11799 C C     . LEU A 1 2830 ? 122.974 155.444 166.527 1.00 36.86  ? 2830 LEU A C     1 
ATOM   11800 O O     . LEU A 1 2830 ? 124.139 155.038 166.474 1.00 36.86  ? 2830 LEU A O     1 
ATOM   11801 C CB    . LEU A 1 2830 ? 121.083 153.844 166.902 1.00 36.86  ? 2830 LEU A CB    1 
ATOM   11802 C CG    . LEU A 1 2830 ? 120.607 152.588 167.646 1.00 36.86  ? 2830 LEU A CG    1 
ATOM   11803 C CD1   . LEU A 1 2830 ? 121.769 151.666 167.943 1.00 36.86  ? 2830 LEU A CD1   1 
ATOM   11804 C CD2   . LEU A 1 2830 ? 119.847 152.897 168.920 1.00 36.86  ? 2830 LEU A CD2   1 
ATOM   11805 N N     . ARG A 1 2831 ? 122.515 156.374 165.692 1.00 36.44  ? 2831 ARG A N     1 
ATOM   11806 C CA    . ARG A 1 2831 ? 123.368 156.858 164.613 1.00 36.44  ? 2831 ARG A CA    1 
ATOM   11807 C C     . ARG A 1 2831 ? 124.412 157.863 165.085 1.00 36.44  ? 2831 ARG A C     1 
ATOM   11808 O O     . ARG A 1 2831 ? 125.371 158.124 164.352 1.00 36.44  ? 2831 ARG A O     1 
ATOM   11809 C CB    . ARG A 1 2831 ? 122.518 157.466 163.497 1.00 36.44  ? 2831 ARG A CB    1 
ATOM   11810 C CG    . ARG A 1 2831 ? 121.511 156.496 162.902 1.00 36.44  ? 2831 ARG A CG    1 
ATOM   11811 C CD    . ARG A 1 2831 ? 122.137 155.655 161.791 1.00 36.44  ? 2831 ARG A CD    1 
ATOM   11812 N NE    . ARG A 1 2831 ? 122.933 154.536 162.289 1.00 36.44  ? 2831 ARG A NE    1 
ATOM   11813 C CZ    . ARG A 1 2831 ? 122.462 153.517 162.997 1.00 36.44  ? 2831 ARG A CZ    1 
ATOM   11814 N NH1   . ARG A 1 2831 ? 121.176 153.412 163.291 1.00 36.44  ? 2831 ARG A NH1   1 
ATOM   11815 N NH2   . ARG A 1 2831 ? 123.301 152.572 163.410 1.00 36.44  ? 2831 ARG A NH2   1 
ATOM   11816 N N     . LEU A 1 2832 ? 124.256 158.432 166.278 1.00 32.89  ? 2832 LEU A N     1 
ATOM   11817 C CA    . LEU A 1 2832 ? 125.223 159.407 166.771 1.00 32.89  ? 2832 LEU A CA    1 
ATOM   11818 C C     . LEU A 1 2832 ? 126.119 158.867 167.876 1.00 32.89  ? 2832 LEU A C     1 
ATOM   11819 O O     . LEU A 1 2832 ? 127.298 159.226 167.943 1.00 32.89  ? 2832 LEU A O     1 
ATOM   11820 C CB    . LEU A 1 2832 ? 124.495 160.652 167.283 1.00 32.89  ? 2832 LEU A CB    1 
ATOM   11821 C CG    . LEU A 1 2832 ? 123.974 161.612 166.217 1.00 32.89  ? 2832 LEU A CG    1 
ATOM   11822 C CD1   . LEU A 1 2832 ? 123.482 162.884 166.864 1.00 32.89  ? 2832 LEU A CD1   1 
ATOM   11823 C CD2   . LEU A 1 2832 ? 125.044 161.914 165.189 1.00 32.89  ? 2832 LEU A CD2   1 
ATOM   11824 N N     . PHE A 1 2833 ? 125.585 158.015 168.748 1.00 38.64  ? 2833 PHE A N     1 
ATOM   11825 C CA    . PHE A 1 2833 ? 126.297 157.533 169.920 1.00 38.64  ? 2833 PHE A CA    1 
ATOM   11826 C C     . PHE A 1 2833 ? 126.660 156.057 169.858 1.00 38.64  ? 2833 PHE A C     1 
ATOM   11827 O O     . PHE A 1 2833 ? 127.224 155.545 170.827 1.00 38.64  ? 2833 PHE A O     1 
ATOM   11828 C CB    . PHE A 1 2833 ? 125.462 157.775 171.188 1.00 38.64  ? 2833 PHE A CB    1 
ATOM   11829 C CG    . PHE A 1 2833 ? 125.145 159.221 171.449 1.00 38.64  ? 2833 PHE A CG    1 
ATOM   11830 C CD1   . PHE A 1 2833 ? 124.118 159.859 170.775 1.00 38.64  ? 2833 PHE A CD1   1 
ATOM   11831 C CD2   . PHE A 1 2833 ? 125.863 159.938 172.389 1.00 38.64  ? 2833 PHE A CD2   1 
ATOM   11832 C CE1   . PHE A 1 2833 ? 123.827 161.187 171.022 1.00 38.64  ? 2833 PHE A CE1   1 
ATOM   11833 C CE2   . PHE A 1 2833 ? 125.575 161.265 172.642 1.00 38.64  ? 2833 PHE A CE2   1 
ATOM   11834 C CZ    . PHE A 1 2833 ? 124.554 161.889 171.958 1.00 38.64  ? 2833 PHE A CZ    1 
ATOM   11835 N N     . GLN A 1 2834 ? 126.322 155.358 168.773 1.00 43.26  ? 2834 GLN A N     1 
ATOM   11836 C CA    . GLN A 1 2834 ? 126.527 153.916 168.685 1.00 43.26  ? 2834 GLN A CA    1 
ATOM   11837 C C     . GLN A 1 2834 ? 127.421 153.475 167.531 1.00 43.26  ? 2834 GLN A C     1 
ATOM   11838 O O     . GLN A 1 2834 ? 128.201 152.533 167.701 1.00 43.26  ? 2834 GLN A O     1 
ATOM   11839 C CB    . GLN A 1 2834 ? 125.173 153.207 168.575 1.00 43.26  ? 2834 GLN A CB    1 
ATOM   11840 C CG    . GLN A 1 2834 ? 125.168 151.764 169.004 1.00 43.26  ? 2834 GLN A CG    1 
ATOM   11841 C CD    . GLN A 1 2834 ? 125.324 150.832 167.822 1.00 43.26  ? 2834 GLN A CD    1 
ATOM   11842 O OE1   . GLN A 1 2834 ? 124.614 150.950 166.824 1.00 43.26  ? 2834 GLN A OE1   1 
ATOM   11843 N NE2   . GLN A 1 2834 ? 126.253 149.900 167.927 1.00 43.26  ? 2834 GLN A NE2   1 
ATOM   11844 N N     . ASP A 1 2835 ? 127.339 154.115 166.364 1.00 41.68  ? 2835 ASP A N     1 
ATOM   11845 C CA    . ASP A 1 2835 ? 128.092 153.641 165.207 1.00 41.68  ? 2835 ASP A CA    1 
ATOM   11846 C C     . ASP A 1 2835 ? 129.546 154.104 165.191 1.00 41.68  ? 2835 ASP A C     1 
ATOM   11847 O O     . ASP A 1 2835 ? 130.315 153.636 164.345 1.00 41.68  ? 2835 ASP A O     1 
ATOM   11848 C CB    . ASP A 1 2835 ? 127.396 154.068 163.911 1.00 41.68  ? 2835 ASP A CB    1 
ATOM   11849 C CG    . ASP A 1 2835 ? 127.226 155.570 163.797 1.00 41.68  ? 2835 ASP A CG    1 
ATOM   11850 O OD1   . ASP A 1 2835 ? 127.781 156.311 164.635 1.00 41.68  ? 2835 ASP A OD1   1 
ATOM   11851 O OD2   . ASP A 1 2835 ? 126.533 156.010 162.856 1.00 41.68  ? 2835 ASP A OD2   1 
ATOM   11852 N N     . ARG A 1 2836 ? 129.935 155.005 166.089 1.00 42.31  ? 2836 ARG A N     1 
ATOM   11853 C CA    . ARG A 1 2836 ? 131.312 155.471 166.198 1.00 42.31  ? 2836 ARG A CA    1 
ATOM   11854 C C     . ARG A 1 2836 ? 132.173 154.536 167.040 1.00 42.31  ? 2836 ARG A C     1 
ATOM   11855 O O     . ARG A 1 2836 ? 133.380 154.765 167.175 1.00 42.31  ? 2836 ARG A O     1 
ATOM   11856 C CB    . ARG A 1 2836 ? 131.318 156.887 166.791 1.00 42.31  ? 2836 ARG A CB    1 
ATOM   11857 C CG    . ARG A 1 2836 ? 132.623 157.654 166.676 1.00 42.31  ? 2836 ARG A CG    1 
ATOM   11858 C CD    . ARG A 1 2836 ? 132.690 158.765 167.713 1.00 42.31  ? 2836 ARG A CD    1 
ATOM   11859 N NE    . ARG A 1 2836 ? 131.645 159.762 167.515 1.00 42.31  ? 2836 ARG A NE    1 
ATOM   11860 C CZ    . ARG A 1 2836 ? 130.819 160.182 168.463 1.00 42.31  ? 2836 ARG A CZ    1 
ATOM   11861 N NH1   . ARG A 1 2836 ? 130.879 159.703 169.694 1.00 42.31  ? 2836 ARG A NH1   1 
ATOM   11862 N NH2   . ARG A 1 2836 ? 129.905 161.102 168.167 1.00 42.31  ? 2836 ARG A NH2   1 
ATOM   11863 N N     . LEU A 1 2837 ? 131.575 153.484 167.588 1.00 49.72  ? 2837 LEU A N     1 
ATOM   11864 C CA    . LEU A 1 2837 ? 132.193 152.604 168.564 1.00 49.72  ? 2837 LEU A CA    1 
ATOM   11865 C C     . LEU A 1 2837 ? 132.919 151.451 167.874 1.00 49.72  ? 2837 LEU A C     1 
ATOM   11866 O O     . LEU A 1 2837 ? 132.721 151.179 166.688 1.00 49.72  ? 2837 LEU A O     1 
ATOM   11867 C CB    . LEU A 1 2837 ? 131.123 152.081 169.520 1.00 49.72  ? 2837 LEU A CB    1 
ATOM   11868 C CG    . LEU A 1 2837 ? 130.661 153.062 170.600 1.00 49.72  ? 2837 LEU A CG    1 
ATOM   11869 C CD1   . LEU A 1 2837 ? 129.830 154.192 170.026 1.00 49.72  ? 2837 LEU A CD1   1 
ATOM   11870 C CD2   . LEU A 1 2837 ? 129.836 152.311 171.608 1.00 49.72  ? 2837 LEU A CD2   1 
ATOM   11871 N N     . VAL A 1 2838 ? 133.756 150.755 168.644 1.00 51.82  ? 2838 VAL A N     1 
ATOM   11872 C CA    . VAL A 1 2838 ? 134.626 149.718 168.098 1.00 51.82  ? 2838 VAL A CA    1 
ATOM   11873 C C     . VAL A 1 2838 ? 134.250 148.341 168.635 1.00 51.82  ? 2838 VAL A C     1 
ATOM   11874 O O     . VAL A 1 2838 ? 133.997 147.412 167.859 1.00 51.82  ? 2838 VAL A O     1 
ATOM   11875 C CB    . VAL A 1 2838 ? 136.103 150.033 168.393 1.00 51.82  ? 2838 VAL A CB    1 
ATOM   11876 C CG1   . VAL A 1 2838 ? 136.975 148.822 168.110 1.00 51.82  ? 2838 VAL A CG1   1 
ATOM   11877 C CG2   . VAL A 1 2838 ? 136.559 151.223 167.566 1.00 51.82  ? 2838 VAL A CG2   1 
ATOM   11878 N N     . GLU A 1 2839 ? 134.227 148.189 169.957 1.00 63.72  ? 2839 GLU A N     1 
ATOM   11879 C CA    . GLU A 1 2839 ? 133.957 146.893 170.563 1.00 63.72  ? 2839 GLU A CA    1 
ATOM   11880 C C     . GLU A 1 2839 ? 132.457 146.659 170.715 1.00 63.72  ? 2839 GLU A C     1 
ATOM   11881 O O     . GLU A 1 2839 ? 131.691 147.575 171.024 1.00 63.72  ? 2839 GLU A O     1 
ATOM   11882 C CB    . GLU A 1 2839 ? 134.644 146.784 171.925 1.00 63.72  ? 2839 GLU A CB    1 
ATOM   11883 C CG    . GLU A 1 2839 ? 134.497 145.425 172.594 1.00 63.72  ? 2839 GLU A CG    1 
ATOM   11884 C CD    . GLU A 1 2839 ? 135.248 145.336 173.908 1.00 63.72  ? 2839 GLU A CD    1 
ATOM   11885 O OE1   . GLU A 1 2839 ? 135.869 146.342 174.311 1.00 63.72  ? 2839 GLU A OE1   1 
ATOM   11886 O OE2   . GLU A 1 2839 ? 135.220 144.258 174.539 1.00 63.72  ? 2839 GLU A OE2   1 
ATOM   11887 N N     . ASP A 1 2840 ? 132.043 145.407 170.492 1.00 66.74  ? 2840 ASP A N     1 
ATOM   11888 C CA    . ASP A 1 2840 ? 130.626 145.060 170.566 1.00 66.74  ? 2840 ASP A CA    1 
ATOM   11889 C C     . ASP A 1 2840 ? 130.067 145.240 171.972 1.00 66.74  ? 2840 ASP A C     1 
ATOM   11890 O O     . ASP A 1 2840 ? 128.871 145.514 172.130 1.00 66.74  ? 2840 ASP A O     1 
ATOM   11891 C CB    . ASP A 1 2840 ? 130.412 143.623 170.090 1.00 66.74  ? 2840 ASP A CB    1 
ATOM   11892 C CG    . ASP A 1 2840 ? 130.658 143.460 168.602 1.00 66.74  ? 2840 ASP A CG    1 
ATOM   11893 O OD1   . ASP A 1 2840 ? 130.451 144.438 167.854 1.00 66.74  ? 2840 ASP A OD1   1 
ATOM   11894 O OD2   . ASP A 1 2840 ? 131.057 142.354 168.179 1.00 66.74  ? 2840 ASP A OD2   1 
ATOM   11895 N N     . GLU A 1 2841 ? 130.904 145.080 172.999 1.00 67.10  ? 2841 GLU A N     1 
ATOM   11896 C CA    . GLU A 1 2841 ? 130.451 145.321 174.366 1.00 67.10  ? 2841 GLU A CA    1 
ATOM   11897 C C     . GLU A 1 2841 ? 130.019 146.770 174.538 1.00 67.10  ? 2841 GLU A C     1 
ATOM   11898 O O     . GLU A 1 2841 ? 128.984 147.058 175.151 1.00 67.10  ? 2841 GLU A O     1 
ATOM   11899 C CB    . GLU A 1 2841 ? 131.560 144.960 175.356 1.00 67.10  ? 2841 GLU A CB    1 
ATOM   11900 C CG    . GLU A 1 2841 ? 131.262 145.334 176.801 1.00 67.10  ? 2841 GLU A CG    1 
ATOM   11901 C CD    . GLU A 1 2841 ? 129.882 144.895 177.249 1.00 67.10  ? 2841 GLU A CD    1 
ATOM   11902 O OE1   . GLU A 1 2841 ? 129.576 143.688 177.147 1.00 67.10  ? 2841 GLU A OE1   1 
ATOM   11903 O OE2   . GLU A 1 2841 ? 129.102 145.758 177.702 1.00 67.10  ? 2841 GLU A OE2   1 
ATOM   11904 N N     . GLU A 1 2842 ? 130.796 147.698 173.978 1.00 61.04  ? 2842 GLU A N     1 
ATOM   11905 C CA    . GLU A 1 2842 ? 130.419 149.105 174.013 1.00 61.04  ? 2842 GLU A CA    1 
ATOM   11906 C C     . GLU A 1 2842 ? 129.096 149.333 173.287 1.00 61.04  ? 2842 GLU A C     1 
ATOM   11907 O O     . GLU A 1 2842 ? 128.235 150.088 173.756 1.00 61.04  ? 2842 GLU A O     1 
ATOM   11908 C CB    . GLU A 1 2842 ? 131.532 149.948 173.392 1.00 61.04  ? 2842 GLU A CB    1 
ATOM   11909 C CG    . GLU A 1 2842 ? 132.930 149.620 173.881 1.00 61.04  ? 2842 GLU A CG    1 
ATOM   11910 C CD    . GLU A 1 2842 ? 134.004 150.295 173.048 1.00 61.04  ? 2842 GLU A CD    1 
ATOM   11911 O OE1   . GLU A 1 2842 ? 134.057 150.041 171.826 1.00 61.04  ? 2842 GLU A OE1   1 
ATOM   11912 O OE2   . GLU A 1 2842 ? 134.793 151.080 173.612 1.00 61.04  ? 2842 GLU A OE2   1 
ATOM   11913 N N     . ARG A 1 2843 ? 128.916 148.675 172.138 1.00 60.57  ? 2843 ARG A N     1 
ATOM   11914 C CA    . ARG A 1 2843 ? 127.693 148.848 171.360 1.00 60.57  ? 2843 ARG A CA    1 
ATOM   11915 C C     . ARG A 1 2843 ? 126.468 148.369 172.131 1.00 60.57  ? 2843 ARG A C     1 
ATOM   11916 O O     . ARG A 1 2843 ? 125.442 149.064 172.185 1.00 60.57  ? 2843 ARG A O     1 
ATOM   11917 C CB    . ARG A 1 2843 ? 127.811 148.097 170.034 1.00 60.57  ? 2843 ARG A CB    1 
ATOM   11918 C CG    . ARG A 1 2843 ? 128.968 148.541 169.151 1.00 60.57  ? 2843 ARG A CG    1 
ATOM   11919 C CD    . ARG A 1 2843 ? 128.795 148.003 167.736 1.00 60.57  ? 2843 ARG A CD    1 
ATOM   11920 N NE    . ARG A 1 2843 ? 129.912 148.324 166.856 1.00 60.57  ? 2843 ARG A NE    1 
ATOM   11921 C CZ    . ARG A 1 2843 ? 131.109 147.758 166.923 1.00 60.57  ? 2843 ARG A CZ    1 
ATOM   11922 N NH1   . ARG A 1 2843 ? 131.378 146.813 167.808 1.00 60.57  ? 2843 ARG A NH1   1 
ATOM   11923 N NH2   . ARG A 1 2843 ? 132.056 148.140 166.072 1.00 60.57  ? 2843 ARG A NH2   1 
ATOM   11924 N N     . ARG A 1 2844 ? 126.550 147.179 172.731 1.00 68.78  ? 2844 ARG A N     1 
ATOM   11925 C CA    . ARG A 1 2844 ? 125.411 146.673 173.487 1.00 68.78  ? 2844 ARG A CA    1 
ATOM   11926 C C     . ARG A 1 2844 ? 125.165 147.515 174.732 1.00 68.78  ? 2844 ARG A C     1 
ATOM   11927 O O     . ARG A 1 2844 ? 124.012 147.731 175.122 1.00 68.78  ? 2844 ARG A O     1 
ATOM   11928 C CB    . ARG A 1 2844 ? 125.610 145.200 173.853 1.00 68.78  ? 2844 ARG A CB    1 
ATOM   11929 C CG    . ARG A 1 2844 ? 126.857 144.892 174.654 1.00 68.78  ? 2844 ARG A CG    1 
ATOM   11930 C CD    . ARG A 1 2844 ? 126.612 143.753 175.633 1.00 68.78  ? 2844 ARG A CD    1 
ATOM   11931 N NE    . ARG A 1 2844 ? 125.530 144.048 176.566 1.00 68.78  ? 2844 ARG A NE    1 
ATOM   11932 C CZ    . ARG A 1 2844 ? 125.593 144.955 177.533 1.00 68.78  ? 2844 ARG A CZ    1 
ATOM   11933 N NH1   . ARG A 1 2844 ? 126.690 145.662 177.749 1.00 68.78  ? 2844 ARG A NH1   1 
ATOM   11934 N NH2   . ARG A 1 2844 ? 124.531 145.150 178.309 1.00 68.78  ? 2844 ARG A NH2   1 
ATOM   11935 N N     . TRP A 1 2845 ? 126.235 148.008 175.365 1.00 65.63  ? 2845 TRP A N     1 
ATOM   11936 C CA    . TRP A 1 2845 ? 126.071 148.920 176.491 1.00 65.63  ? 2845 TRP A CA    1 
ATOM   11937 C C     . TRP A 1 2845 ? 125.278 150.147 176.066 1.00 65.63  ? 2845 TRP A C     1 
ATOM   11938 O O     . TRP A 1 2845 ? 124.352 150.581 176.761 1.00 65.63  ? 2845 TRP A O     1 
ATOM   11939 C CB    . TRP A 1 2845 ? 127.440 149.337 177.030 1.00 65.63  ? 2845 TRP A CB    1 
ATOM   11940 C CG    . TRP A 1 2845 ? 127.364 150.252 178.216 1.00 65.63  ? 2845 TRP A CG    1 
ATOM   11941 C CD1   . TRP A 1 2845 ? 126.935 149.930 179.470 1.00 65.63  ? 2845 TRP A CD1   1 
ATOM   11942 C CD2   . TRP A 1 2845 ? 127.680 151.650 178.248 1.00 65.63  ? 2845 TRP A CD2   1 
ATOM   11943 N NE1   . TRP A 1 2845 ? 126.993 151.031 180.289 1.00 65.63  ? 2845 TRP A NE1   1 
ATOM   11944 C CE2   . TRP A 1 2845 ? 127.446 152.101 179.562 1.00 65.63  ? 2845 TRP A CE2   1 
ATOM   11945 C CE3   . TRP A 1 2845 ? 128.149 152.561 177.298 1.00 65.63  ? 2845 TRP A CE3   1 
ATOM   11946 C CZ2   . TRP A 1 2845 ? 127.657 153.421 179.947 1.00 65.63  ? 2845 TRP A CZ2   1 
ATOM   11947 C CZ3   . TRP A 1 2845 ? 128.359 153.871 177.684 1.00 65.63  ? 2845 TRP A CZ3   1 
ATOM   11948 C CH2   . TRP A 1 2845 ? 128.116 154.288 178.996 1.00 65.63  ? 2845 TRP A CH2   1 
ATOM   11949 N N     . THR A 1 2846 ? 125.627 150.707 174.905 1.00 63.23  ? 2846 THR A N     1 
ATOM   11950 C CA    . THR A 1 2846 ? 124.937 151.885 174.395 1.00 63.23  ? 2846 THR A CA    1 
ATOM   11951 C C     . THR A 1 2846 ? 123.462 151.595 174.140 1.00 63.23  ? 2846 THR A C     1 
ATOM   11952 O O     . THR A 1 2846 ? 122.587 152.380 174.518 1.00 63.23  ? 2846 THR A O     1 
ATOM   11953 C CB    . THR A 1 2846 ? 125.620 152.374 173.115 1.00 63.23  ? 2846 THR A CB    1 
ATOM   11954 O OG1   . THR A 1 2846 ? 126.927 152.871 173.429 1.00 63.23  ? 2846 THR A OG1   1 
ATOM   11955 C CG2   . THR A 1 2846 ? 124.807 153.481 172.465 1.00 63.23  ? 2846 THR A CG2   1 
ATOM   11956 N N     . ASP A 1 2847 ? 123.167 150.460 173.498 1.00 64.49  ? 2847 ASP A N     1 
ATOM   11957 C CA    . ASP A 1 2847 ? 121.773 150.139 173.189 1.00 64.49  ? 2847 ASP A CA    1 
ATOM   11958 C C     . ASP A 1 2847 ? 120.950 149.926 174.457 1.00 64.49  ? 2847 ASP A C     1 
ATOM   11959 O O     . ASP A 1 2847 ? 119.812 150.415 174.565 1.00 64.49  ? 2847 ASP A O     1 
ATOM   11960 C CB    . ASP A 1 2847 ? 121.702 148.906 172.289 1.00 64.49  ? 2847 ASP A CB    1 
ATOM   11961 C CG    . ASP A 1 2847 ? 122.419 149.106 170.971 1.00 64.49  ? 2847 ASP A CG    1 
ATOM   11962 O OD1   . ASP A 1 2847 ? 122.990 150.198 170.766 1.00 64.49  ? 2847 ASP A OD1   1 
ATOM   11963 O OD2   . ASP A 1 2847 ? 122.412 148.175 170.139 1.00 64.49  ? 2847 ASP A OD2   1 
ATOM   11964 N N     . GLU A 1 2848 ? 121.505 149.194 175.427 1.00 70.86  ? 2848 GLU A N     1 
ATOM   11965 C CA    . GLU A 1 2848 ? 120.795 148.976 176.682 1.00 70.86  ? 2848 GLU A CA    1 
ATOM   11966 C C     . GLU A 1 2848 ? 120.574 150.290 177.417 1.00 70.86  ? 2848 GLU A C     1 
ATOM   11967 O O     . GLU A 1 2848 ? 119.508 150.517 177.992 1.00 70.86  ? 2848 GLU A O     1 
ATOM   11968 C CB    . GLU A 1 2848 ? 121.552 147.979 177.562 1.00 70.86  ? 2848 GLU A CB    1 
ATOM   11969 C CG    . GLU A 1 2848 ? 121.826 146.625 176.913 1.00 70.86  ? 2848 GLU A CG    1 
ATOM   11970 C CD    . GLU A 1 2848 ? 120.567 145.825 176.617 1.00 70.86  ? 2848 GLU A CD    1 
ATOM   11971 O OE1   . GLU A 1 2848 ? 119.478 146.203 177.100 1.00 70.86  ? 2848 GLU A OE1   1 
ATOM   11972 O OE2   . GLU A 1 2848 ? 120.669 144.811 175.895 1.00 70.86  ? 2848 GLU A OE2   1 
ATOM   11973 N N     . ASN A 1 2849 ? 121.570 151.178 177.404 1.00 69.17  ? 2849 ASN A N     1 
ATOM   11974 C CA    . ASN A 1 2849 ? 121.388 152.478 178.039 1.00 69.17  ? 2849 ASN A CA    1 
ATOM   11975 C C     . ASN A 1 2849 ? 120.304 153.285 177.337 1.00 69.17  ? 2849 ASN A C     1 
ATOM   11976 O O     . ASN A 1 2849 ? 119.504 153.964 177.991 1.00 69.17  ? 2849 ASN A O     1 
ATOM   11977 C CB    . ASN A 1 2849 ? 122.708 153.241 178.048 1.00 69.17  ? 2849 ASN A CB    1 
ATOM   11978 C CG    . ASN A 1 2849 ? 123.646 152.746 179.118 1.00 69.17  ? 2849 ASN A CG    1 
ATOM   11979 O OD1   . ASN A 1 2849 ? 123.465 153.024 180.303 1.00 69.17  ? 2849 ASN A OD1   1 
ATOM   11980 N ND2   . ASN A 1 2849 ? 124.635 151.970 178.709 1.00 69.17  ? 2849 ASN A ND2   1 
ATOM   11981 N N     . ILE A 1 2850 ? 120.258 153.214 176.006 1.00 60.68  ? 2850 ILE A N     1 
ATOM   11982 C CA    . ILE A 1 2850 ? 119.258 153.962 175.248 1.00 60.68  ? 2850 ILE A CA    1 
ATOM   11983 C C     . ILE A 1 2850 ? 117.856 153.513 175.638 1.00 60.68  ? 2850 ILE A C     1 
ATOM   11984 O O     . ILE A 1 2850 ? 116.992 154.331 175.984 1.00 60.68  ? 2850 ILE A O     1 
ATOM   11985 C CB    . ILE A 1 2850 ? 119.497 153.797 173.738 1.00 60.68  ? 2850 ILE A CB    1 
ATOM   11986 C CG1   . ILE A 1 2850 ? 120.724 154.595 173.309 1.00 60.68  ? 2850 ILE A CG1   1 
ATOM   11987 C CG2   . ILE A 1 2850 ? 118.276 154.234 172.950 1.00 60.68  ? 2850 ILE A CG2   1 
ATOM   11988 C CD1   . ILE A 1 2850 ? 121.135 154.361 171.883 1.00 60.68  ? 2850 ILE A CD1   1 
ATOM   11989 N N     . ASP A 1 2851 ? 117.615 152.199 175.611 1.00 72.10  ? 2851 ASP A N     1 
ATOM   11990 C CA    . ASP A 1 2851 ? 116.267 151.727 175.923 1.00 72.10  ? 2851 ASP A CA    1 
ATOM   11991 C C     . ASP A 1 2851 ? 115.947 151.925 177.403 1.00 72.10  ? 2851 ASP A C     1 
ATOM   11992 O O     . ASP A 1 2851 ? 114.797 152.207 177.768 1.00 72.10  ? 2851 ASP A O     1 
ATOM   11993 C CB    . ASP A 1 2851 ? 116.077 150.272 175.459 1.00 72.10  ? 2851 ASP A CB    1 
ATOM   11994 C CG    . ASP A 1 2851 ? 116.723 149.228 176.374 1.00 72.10  ? 2851 ASP A CG    1 
ATOM   11995 O OD1   . ASP A 1 2851 ? 117.181 149.533 177.490 1.00 72.10  ? 2851 ASP A OD1   1 
ATOM   11996 O OD2   . ASP A 1 2851 ? 116.768 148.054 175.950 1.00 72.10  ? 2851 ASP A OD2   1 
ATOM   11997 N N     . THR A 1 2852 ? 116.962 151.822 178.266 1.00 70.04  ? 2852 THR A N     1 
ATOM   11998 C CA    . THR A 1 2852 ? 116.770 152.064 179.689 1.00 70.04  ? 2852 THR A CA    1 
ATOM   11999 C C     . THR A 1 2852 ? 116.307 153.492 179.943 1.00 70.04  ? 2852 THR A C     1 
ATOM   12000 O O     . THR A 1 2852 ? 115.354 153.722 180.689 1.00 70.04  ? 2852 THR A O     1 
ATOM   12001 C CB    . THR A 1 2852 ? 118.069 151.778 180.446 1.00 70.04  ? 2852 THR A CB    1 
ATOM   12002 O OG1   . THR A 1 2852 ? 118.517 150.450 180.145 1.00 70.04  ? 2852 THR A OG1   1 
ATOM   12003 C CG2   . THR A 1 2852 ? 117.853 151.909 181.945 1.00 70.04  ? 2852 THR A CG2   1 
ATOM   12004 N N     . VAL A 1 2853 ? 116.970 154.469 179.319 1.00 69.47  ? 2853 VAL A N     1 
ATOM   12005 C CA    . VAL A 1 2853 ? 116.579 155.865 179.506 1.00 69.47  ? 2853 VAL A CA    1 
ATOM   12006 C C     . VAL A 1 2853 ? 115.202 156.117 178.912 1.00 69.47  ? 2853 VAL A C     1 
ATOM   12007 O O     . VAL A 1 2853 ? 114.373 156.832 179.499 1.00 69.47  ? 2853 VAL A O     1 
ATOM   12008 C CB    . VAL A 1 2853 ? 117.635 156.803 178.896 1.00 69.47  ? 2853 VAL A CB    1 
ATOM   12009 C CG1   . VAL A 1 2853 ? 117.191 158.253 179.013 1.00 69.47  ? 2853 VAL A CG1   1 
ATOM   12010 C CG2   . VAL A 1 2853 ? 118.954 156.601 179.583 1.00 69.47  ? 2853 VAL A CG2   1 
ATOM   12011 N N     . ALA A 1 2854 ? 114.938 155.544 177.734 1.00 73.35  ? 2854 ALA A N     1 
ATOM   12012 C CA    . ALA A 1 2854 ? 113.625 155.684 177.117 1.00 73.35  ? 2854 ALA A CA    1 
ATOM   12013 C C     . ALA A 1 2854 ? 112.531 155.207 178.062 1.00 73.35  ? 2854 ALA A C     1 
ATOM   12014 O O     . ALA A 1 2854 ? 111.472 155.832 178.176 1.00 73.35  ? 2854 ALA A O     1 
ATOM   12015 C CB    . ALA A 1 2854 ? 113.583 154.912 175.797 1.00 73.35  ? 2854 ALA A CB    1 
ATOM   12016 N N     . LEU A 1 2855 ? 112.776 154.097 178.762 1.00 77.29  ? 2855 LEU A N     1 
ATOM   12017 C CA    . LEU A 1 2855 ? 111.802 153.627 179.742 1.00 77.29  ? 2855 LEU A CA    1 
ATOM   12018 C C     . LEU A 1 2855 ? 111.789 154.498 180.994 1.00 77.29  ? 2855 LEU A C     1 
ATOM   12019 O O     . LEU A 1 2855 ? 110.735 154.671 181.615 1.00 77.29  ? 2855 LEU A O     1 
ATOM   12020 C CB    . LEU A 1 2855 ? 112.085 152.171 180.107 1.00 77.29  ? 2855 LEU A CB    1 
ATOM   12021 C CG    . LEU A 1 2855 ? 111.808 151.159 178.995 1.00 77.29  ? 2855 LEU A CG    1 
ATOM   12022 C CD1   . LEU A 1 2855 ? 112.159 149.753 179.449 1.00 77.29  ? 2855 LEU A CD1   1 
ATOM   12023 C CD2   . LEU A 1 2855 ? 110.356 151.238 178.547 1.00 77.29  ? 2855 LEU A CD2   1 
ATOM   12024 N N     . LYS A 1 2856 ? 112.944 155.044 181.386 1.00 71.78  ? 2856 LYS A N     1 
ATOM   12025 C CA    . LYS A 1 2856 ? 113.013 155.856 182.598 1.00 71.78  ? 2856 LYS A CA    1 
ATOM   12026 C C     . LYS A 1 2856 ? 112.153 157.103 182.476 1.00 71.78  ? 2856 LYS A C     1 
ATOM   12027 O O     . LYS A 1 2856 ? 111.410 157.453 183.400 1.00 71.78  ? 2856 LYS A O     1 
ATOM   12028 C CB    . LYS A 1 2856 ? 114.462 156.243 182.902 1.00 71.78  ? 2856 LYS A CB    1 
ATOM   12029 C CG    . LYS A 1 2856 ? 115.336 155.107 183.400 1.00 71.78  ? 2856 LYS A CG    1 
ATOM   12030 C CD    . LYS A 1 2856 ? 114.704 154.392 184.577 1.00 71.78  ? 2856 LYS A CD    1 
ATOM   12031 C CE    . LYS A 1 2856 ? 115.097 152.927 184.590 1.00 71.78  ? 2856 LYS A CE    1 
ATOM   12032 N NZ    . LYS A 1 2856 ? 114.763 152.263 183.300 1.00 71.78  ? 2856 LYS A NZ    1 
ATOM   12033 N N     . HIS A 1 2857 ? 112.238 157.792 181.340 1.00 71.14  ? 2857 HIS A N     1 
ATOM   12034 C CA    . HIS A 1 2857 ? 111.439 158.997 181.155 1.00 71.14  ? 2857 HIS A CA    1 
ATOM   12035 C C     . HIS A 1 2857 ? 110.149 158.755 180.386 1.00 71.14  ? 2857 HIS A C     1 
ATOM   12036 O O     . HIS A 1 2857 ? 109.288 159.641 180.363 1.00 71.14  ? 2857 HIS A O     1 
ATOM   12037 C CB    . HIS A 1 2857 ? 112.262 160.085 180.457 1.00 71.14  ? 2857 HIS A CB    1 
ATOM   12038 C CG    . HIS A 1 2857 ? 113.387 160.608 181.292 1.00 71.14  ? 2857 HIS A CG    1 
ATOM   12039 N ND1   . HIS A 1 2857 ? 114.249 161.588 180.852 1.00 71.14  ? 2857 HIS A ND1   1 
ATOM   12040 C CD2   . HIS A 1 2857 ? 113.787 160.289 182.545 1.00 71.14  ? 2857 HIS A CD2   1 
ATOM   12041 C CE1   . HIS A 1 2857 ? 115.135 161.847 181.797 1.00 71.14  ? 2857 HIS A CE1   1 
ATOM   12042 N NE2   . HIS A 1 2857 ? 114.876 161.074 182.835 1.00 71.14  ? 2857 HIS A NE2   1 
ATOM   12043 N N     . PHE A 1 2858 ? 109.989 157.590 179.765 1.00 74.36  ? 2858 PHE A N     1 
ATOM   12044 C CA    . PHE A 1 2858 ? 108.738 157.209 179.108 1.00 74.36  ? 2858 PHE A CA    1 
ATOM   12045 C C     . PHE A 1 2858 ? 108.404 155.772 179.486 1.00 74.36  ? 2858 PHE A C     1 
ATOM   12046 O O     . PHE A 1 2858 ? 108.563 154.846 178.682 1.00 74.36  ? 2858 PHE A O     1 
ATOM   12047 C CB    . PHE A 1 2858 ? 108.846 157.376 177.591 1.00 74.36  ? 2858 PHE A CB    1 
ATOM   12048 C CG    . PHE A 1 2858 ? 109.224 158.764 177.159 1.00 74.36  ? 2858 PHE A CG    1 
ATOM   12049 C CD1   . PHE A 1 2858 ? 108.345 159.820 177.327 1.00 74.36  ? 2858 PHE A CD1   1 
ATOM   12050 C CD2   . PHE A 1 2858 ? 110.460 159.011 176.584 1.00 74.36  ? 2858 PHE A CD2   1 
ATOM   12051 C CE1   . PHE A 1 2858 ? 108.692 161.096 176.929 1.00 74.36  ? 2858 PHE A CE1   1 
ATOM   12052 C CE2   . PHE A 1 2858 ? 110.811 160.285 176.184 1.00 74.36  ? 2858 PHE A CE2   1 
ATOM   12053 C CZ    . PHE A 1 2858 ? 109.926 161.328 176.357 1.00 74.36  ? 2858 PHE A CZ    1 
ATOM   12054 N N     . PRO A 1 2859 ? 107.949 155.544 180.723 1.00 81.83  ? 2859 PRO A N     1 
ATOM   12055 C CA    . PRO A 1 2859 ? 107.578 154.181 181.125 1.00 81.83  ? 2859 PRO A CA    1 
ATOM   12056 C C     . PRO A 1 2859 ? 106.165 153.818 180.699 1.00 81.83  ? 2859 PRO A C     1 
ATOM   12057 O O     . PRO A 1 2859 ? 105.842 152.638 180.527 1.00 81.83  ? 2859 PRO A O     1 
ATOM   12058 C CB    . PRO A 1 2859 ? 107.715 154.222 182.650 1.00 81.83  ? 2859 PRO A CB    1 
ATOM   12059 C CG    . PRO A 1 2859 ? 107.392 155.637 183.005 1.00 81.83  ? 2859 PRO A CG    1 
ATOM   12060 C CD    . PRO A 1 2859 ? 107.808 156.505 181.834 1.00 81.83  ? 2859 PRO A CD    1 
ATOM   12061 N N     . ASN A 1 2860 ? 105.315 154.832 180.527 1.00 78.22  ? 2860 ASN A N     1 
ATOM   12062 C CA    . ASN A 1 2860 ? 103.922 154.581 180.175 1.00 78.22  ? 2860 ASN A CA    1 
ATOM   12063 C C     . ASN A 1 2860 ? 103.797 154.072 178.744 1.00 78.22  ? 2860 ASN A C     1 
ATOM   12064 O O     . ASN A 1 2860 ? 102.834 153.372 178.409 1.00 78.22  ? 2860 ASN A O     1 
ATOM   12065 C CB    . ASN A 1 2860 ? 103.100 155.855 180.369 1.00 78.22  ? 2860 ASN A CB    1 
ATOM   12066 C CG    . ASN A 1 2860 ? 101.609 155.585 180.433 1.00 78.22  ? 2860 ASN A CG    1 
ATOM   12067 O OD1   . ASN A 1 2860 ? 101.168 154.439 180.354 1.00 78.22  ? 2860 ASN A OD1   1 
ATOM   12068 N ND2   . ASN A 1 2860 ? 100.824 156.646 180.580 1.00 78.22  ? 2860 ASN A ND2   1 
ATOM   12069 N N     . ILE A 1 2861 ? 104.761 154.414 177.885 1.00 79.75  ? 2861 ILE A N     1 
ATOM   12070 C CA    . ILE A 1 2861 ? 104.700 153.984 176.494 1.00 79.75  ? 2861 ILE A CA    1 
ATOM   12071 C C     . ILE A 1 2861 ? 104.808 152.469 176.409 1.00 79.75  ? 2861 ILE A C     1 
ATOM   12072 O O     . ILE A 1 2861 ? 105.350 151.807 177.305 1.00 79.75  ? 2861 ILE A O     1 
ATOM   12073 C CB    . ILE A 1 2861 ? 105.811 154.650 175.665 1.00 79.75  ? 2861 ILE A CB    1 
ATOM   12074 C CG1   . ILE A 1 2861 ? 107.152 153.972 175.958 1.00 79.75  ? 2861 ILE A CG1   1 
ATOM   12075 C CG2   . ILE A 1 2861 ? 105.867 156.144 175.947 1.00 79.75  ? 2861 ILE A CG2   1 
ATOM   12076 C CD1   . ILE A 1 2861 ? 108.305 154.483 175.143 1.00 79.75  ? 2861 ILE A CD1   1 
ATOM   12077 N N     . ASP A 1 2862 ? 104.275 151.913 175.327 1.00 80.51  ? 2862 ASP A N     1 
ATOM   12078 C CA    . ASP A 1 2862 ? 104.431 150.491 175.062 1.00 80.51  ? 2862 ASP A CA    1 
ATOM   12079 C C     . ASP A 1 2862 ? 105.861 150.183 174.637 1.00 80.51  ? 2862 ASP A C     1 
ATOM   12080 O O     . ASP A 1 2862 ? 106.479 150.935 173.877 1.00 80.51  ? 2862 ASP A O     1 
ATOM   12081 C CB    . ASP A 1 2862 ? 103.449 150.048 173.978 1.00 80.51  ? 2862 ASP A CB    1 
ATOM   12082 C CG    . ASP A 1 2862 ? 103.458 150.969 172.773 1.00 80.51  ? 2862 ASP A CG    1 
ATOM   12083 O OD1   . ASP A 1 2862 ? 104.140 152.014 172.824 1.00 80.51  ? 2862 ASP A OD1   1 
ATOM   12084 O OD2   . ASP A 1 2862 ? 102.781 150.649 171.774 1.00 80.51  ? 2862 ASP A OD2   1 
ATOM   12085 N N     . ARG A 1 2863 ? 106.390 149.067 175.138 1.00 79.72  ? 2863 ARG A N     1 
ATOM   12086 C CA    . ARG A 1 2863 ? 107.730 148.617 174.766 1.00 79.72  ? 2863 ARG A CA    1 
ATOM   12087 C C     . ARG A 1 2863 ? 107.642 147.831 173.457 1.00 79.72  ? 2863 ARG A C     1 
ATOM   12088 O O     . ARG A 1 2863 ? 107.715 146.601 173.406 1.00 79.72  ? 2863 ARG A O     1 
ATOM   12089 C CB    . ARG A 1 2863 ? 108.357 147.794 175.882 1.00 79.72  ? 2863 ARG A CB    1 
ATOM   12090 C CG    . ARG A 1 2863 ? 109.773 147.338 175.568 1.00 79.72  ? 2863 ARG A CG    1 
ATOM   12091 C CD    . ARG A 1 2863 ? 110.736 148.507 175.482 1.00 79.72  ? 2863 ARG A CD    1 
ATOM   12092 N NE    . ARG A 1 2863 ? 112.051 148.081 175.016 1.00 79.72  ? 2863 ARG A NE    1 
ATOM   12093 C CZ    . ARG A 1 2863 ? 113.023 147.630 175.798 1.00 79.72  ? 2863 ARG A CZ    1 
ATOM   12094 N NH1   . ARG A 1 2863 ? 112.863 147.520 177.107 1.00 79.72  ? 2863 ARG A NH1   1 
ATOM   12095 N NH2   . ARG A 1 2863 ? 114.182 147.276 175.252 1.00 79.72  ? 2863 ARG A NH2   1 
ATOM   12096 N N     . GLU A 1 2864 ? 107.438 148.579 172.377 1.00 78.55  ? 2864 GLU A N     1 
ATOM   12097 C CA    . GLU A 1 2864 ? 107.435 148.012 171.036 1.00 78.55  ? 2864 GLU A CA    1 
ATOM   12098 C C     . GLU A 1 2864 ? 108.328 148.822 170.108 1.00 78.55  ? 2864 GLU A C     1 
ATOM   12099 O O     . GLU A 1 2864 ? 108.918 148.263 169.178 1.00 78.55  ? 2864 GLU A O     1 
ATOM   12100 C CB    . GLU A 1 2864 ? 105.994 147.929 170.513 1.00 78.55  ? 2864 GLU A CB    1 
ATOM   12101 C CG    . GLU A 1 2864 ? 105.830 147.117 169.236 1.00 78.55  ? 2864 GLU A CG    1 
ATOM   12102 C CD    . GLU A 1 2864 ? 105.975 147.946 167.983 1.00 78.55  ? 2864 GLU A CD    1 
ATOM   12103 O OE1   . GLU A 1 2864 ? 105.613 149.137 168.024 1.00 78.55  ? 2864 GLU A OE1   1 
ATOM   12104 O OE2   . GLU A 1 2864 ? 106.458 147.408 166.963 1.00 78.55  ? 2864 GLU A OE2   1 
ATOM   12105 N N     . LYS A 1 2865 ? 108.425 150.135 170.327 1.00 70.96  ? 2865 LYS A N     1 
ATOM   12106 C CA    . LYS A 1 2865 ? 109.383 150.955 169.593 1.00 70.96  ? 2865 LYS A CA    1 
ATOM   12107 C C     . LYS A 1 2865 ? 110.820 150.601 169.955 1.00 70.96  ? 2865 LYS A C     1 
ATOM   12108 O O     . LYS A 1 2865 ? 111.644 150.323 169.077 1.00 70.96  ? 2865 LYS A O     1 
ATOM   12109 C CB    . LYS A 1 2865 ? 109.113 152.432 169.871 1.00 70.96  ? 2865 LYS A CB    1 
ATOM   12110 C CG    . LYS A 1 2865 ? 107.738 152.932 169.454 1.00 70.96  ? 2865 LYS A CG    1 
ATOM   12111 C CD    . LYS A 1 2865 ? 107.592 153.017 167.935 1.00 70.96  ? 2865 LYS A CD    1 
ATOM   12112 C CE    . LYS A 1 2865 ? 106.987 151.792 167.293 1.00 70.96  ? 2865 LYS A CE    1 
ATOM   12113 N NZ    . LYS A 1 2865 ? 106.792 152.026 165.840 1.00 70.96  ? 2865 LYS A NZ    1 
ATOM   12114 N N     . ALA A 1 2866 ? 111.142 150.614 171.248 1.00 77.00  ? 2866 ALA A N     1 
ATOM   12115 C CA    . ALA A 1 2866 ? 112.502 150.285 171.662 1.00 77.00  ? 2866 ALA A CA    1 
ATOM   12116 C C     . ALA A 1 2866 ? 112.756 148.789 171.555 1.00 77.00  ? 2866 ALA A C     1 
ATOM   12117 O O     . ALA A 1 2866 ? 113.879 148.360 171.266 1.00 77.00  ? 2866 ALA A O     1 
ATOM   12118 C CB    . ALA A 1 2866 ? 112.750 150.778 173.086 1.00 77.00  ? 2866 ALA A CB    1 
ATOM   12119 N N     . MET A 1 2867 ? 111.719 147.980 171.784 1.00 79.70  ? 2867 MET A N     1 
ATOM   12120 C CA    . MET A 1 2867 ? 111.862 146.535 171.653 1.00 79.70  ? 2867 MET A CA    1 
ATOM   12121 C C     . MET A 1 2867 ? 112.195 146.136 170.221 1.00 79.70  ? 2867 MET A C     1 
ATOM   12122 O O     . MET A 1 2867 ? 112.904 145.147 170.001 1.00 79.70  ? 2867 MET A O     1 
ATOM   12123 C CB    . MET A 1 2867 ? 110.582 145.844 172.122 1.00 79.70  ? 2867 MET A CB    1 
ATOM   12124 C CG    . MET A 1 2867 ? 110.640 144.331 172.084 1.00 79.70  ? 2867 MET A CG    1 
ATOM   12125 S SD    . MET A 1 2867 ? 109.110 143.560 172.641 1.00 79.70  ? 2867 MET A SD    1 
ATOM   12126 C CE    . MET A 1 2867 ? 109.200 143.855 174.405 1.00 79.70  ? 2867 MET A CE    1 
ATOM   12127 N N     . SER A 1 2868 ? 111.698 146.889 169.241 1.00 72.72  ? 2868 SER A N     1 
ATOM   12128 C CA    . SER A 1 2868 ? 111.990 146.598 167.844 1.00 72.72  ? 2868 SER A CA    1 
ATOM   12129 C C     . SER A 1 2868 ? 113.487 146.699 167.581 1.00 72.72  ? 2868 SER A C     1 
ATOM   12130 O O     . SER A 1 2868 ? 114.119 147.719 167.867 1.00 72.72  ? 2868 SER A O     1 
ATOM   12131 C CB    . SER A 1 2868 ? 111.221 147.558 166.937 1.00 72.72  ? 2868 SER A CB    1 
ATOM   12132 O OG    . SER A 1 2868 ? 109.830 147.507 167.203 1.00 72.72  ? 2868 SER A OG    1 
ATOM   12133 N N     . ARG A 1 2869 ? 114.050 145.626 167.033 1.00 70.12  ? 2869 ARG A N     1 
ATOM   12134 C CA    . ARG A 1 2869 ? 115.493 145.480 166.874 1.00 70.12  ? 2869 ARG A CA    1 
ATOM   12135 C C     . ARG A 1 2869 ? 116.077 146.220 165.670 1.00 70.12  ? 2869 ARG A C     1 
ATOM   12136 O O     . ARG A 1 2869 ? 117.101 146.897 165.825 1.00 70.12  ? 2869 ARG A O     1 
ATOM   12137 C CB    . ARG A 1 2869 ? 115.855 143.993 166.804 1.00 70.12  ? 2869 ARG A CB    1 
ATOM   12138 C CG    . ARG A 1 2869 ? 115.563 143.228 168.089 1.00 70.12  ? 2869 ARG A CG    1 
ATOM   12139 C CD    . ARG A 1 2869 ? 116.382 143.771 169.255 1.00 70.12  ? 2869 ARG A CD    1 
ATOM   12140 N NE    . ARG A 1 2869 ? 115.697 144.846 169.964 1.00 70.12  ? 2869 ARG A NE    1 
ATOM   12141 C CZ    . ARG A 1 2869 ? 116.291 145.699 170.788 1.00 70.12  ? 2869 ARG A CZ    1 
ATOM   12142 N NH1   . ARG A 1 2869 ? 117.588 145.630 171.037 1.00 70.12  ? 2869 ARG A NH1   1 
ATOM   12143 N NH2   . ARG A 1 2869 ? 115.565 146.645 171.376 1.00 70.12  ? 2869 ARG A NH2   1 
ATOM   12144 N N     . PRO A 1 2870 ? 115.499 146.117 164.464 1.00 63.27  ? 2870 PRO A N     1 
ATOM   12145 C CA    . PRO A 1 2870 ? 116.138 146.788 163.314 1.00 63.27  ? 2870 PRO A CA    1 
ATOM   12146 C C     . PRO A 1 2870 ? 116.278 148.291 163.487 1.00 63.27  ? 2870 PRO A C     1 
ATOM   12147 O O     . PRO A 1 2870 ? 117.383 148.826 163.320 1.00 63.27  ? 2870 PRO A O     1 
ATOM   12148 C CB    . PRO A 1 2870 ? 115.216 146.424 162.140 1.00 63.27  ? 2870 PRO A CB    1 
ATOM   12149 C CG    . PRO A 1 2870 ? 113.918 146.063 162.764 1.00 63.27  ? 2870 PRO A CG    1 
ATOM   12150 C CD    . PRO A 1 2870 ? 114.277 145.401 164.053 1.00 63.27  ? 2870 PRO A CD    1 
ATOM   12151 N N     . ILE A 1 2871 ? 115.187 148.978 163.842 1.00 54.08  ? 2871 ILE A N     1 
ATOM   12152 C CA    . ILE A 1 2871 ? 115.102 150.431 163.999 1.00 54.08  ? 2871 ILE A CA    1 
ATOM   12153 C C     . ILE A 1 2871 ? 115.969 151.144 162.964 1.00 54.08  ? 2871 ILE A C     1 
ATOM   12154 O O     . ILE A 1 2871 ? 116.896 151.892 163.293 1.00 54.08  ? 2871 ILE A O     1 
ATOM   12155 C CB    . ILE A 1 2871 ? 115.422 150.855 165.453 1.00 54.08  ? 2871 ILE A CB    1 
ATOM   12156 C CG1   . ILE A 1 2871 ? 115.084 152.333 165.674 1.00 54.08  ? 2871 ILE A CG1   1 
ATOM   12157 C CG2   . ILE A 1 2871 ? 116.855 150.494 165.892 1.00 54.08  ? 2871 ILE A CG2   1 
ATOM   12158 C CD1   . ILE A 1 2871 ? 115.064 152.730 167.120 1.00 54.08  ? 2871 ILE A CD1   1 
ATOM   12159 N N     . LEU A 1 2872 ? 115.667 150.902 161.694 1.00 51.45  ? 2872 LEU A N     1 
ATOM   12160 C CA    . LEU A 1 2872 ? 116.366 151.527 160.584 1.00 51.45  ? 2872 LEU A CA    1 
ATOM   12161 C C     . LEU A 1 2872 ? 115.347 152.123 159.625 1.00 51.45  ? 2872 LEU A C     1 
ATOM   12162 O O     . LEU A 1 2872 ? 114.364 151.471 159.265 1.00 51.45  ? 2872 LEU A O     1 
ATOM   12163 C CB    . LEU A 1 2872 ? 117.292 150.508 159.887 1.00 51.45  ? 2872 LEU A CB    1 
ATOM   12164 C CG    . LEU A 1 2872 ? 116.743 149.233 159.230 1.00 51.45  ? 2872 LEU A CG    1 
ATOM   12165 C CD1   . LEU A 1 2872 ? 116.219 149.440 157.809 1.00 51.45  ? 2872 LEU A CD1   1 
ATOM   12166 C CD2   . LEU A 1 2872 ? 117.796 148.133 159.261 1.00 51.45  ? 2872 LEU A CD2   1 
ATOM   12167 N N     . TYR A 1 2873 ? 115.571 153.376 159.240 1.00 46.97  ? 2873 TYR A N     1 
ATOM   12168 C CA    . TYR A 1 2873 ? 114.672 154.093 158.350 1.00 46.97  ? 2873 TYR A CA    1 
ATOM   12169 C C     . TYR A 1 2873 ? 115.323 154.273 156.986 1.00 46.97  ? 2873 TYR A C     1 
ATOM   12170 O O     . TYR A 1 2873 ? 116.548 154.206 156.850 1.00 46.97  ? 2873 TYR A O     1 
ATOM   12171 C CB    . TYR A 1 2873 ? 114.292 155.472 158.902 1.00 46.97  ? 2873 TYR A CB    1 
ATOM   12172 C CG    . TYR A 1 2873 ? 113.470 155.505 160.178 1.00 46.97  ? 2873 TYR A CG    1 
ATOM   12173 C CD1   . TYR A 1 2873 ? 113.275 154.371 160.953 1.00 46.97  ? 2873 TYR A CD1   1 
ATOM   12174 C CD2   . TYR A 1 2873 ? 112.862 156.683 160.587 1.00 46.97  ? 2873 TYR A CD2   1 
ATOM   12175 C CE1   . TYR A 1 2873 ? 112.516 154.421 162.107 1.00 46.97  ? 2873 TYR A CE1   1 
ATOM   12176 C CE2   . TYR A 1 2873 ? 112.108 156.741 161.728 1.00 46.97  ? 2873 TYR A CE2   1 
ATOM   12177 C CZ    . TYR A 1 2873 ? 111.936 155.612 162.484 1.00 46.97  ? 2873 TYR A CZ    1 
ATOM   12178 O OH    . TYR A 1 2873 ? 111.175 155.692 163.620 1.00 46.97  ? 2873 TYR A OH    1 
ATOM   12179 N N     . SER A 1 2874 ? 114.489 154.513 155.976 1.00 49.66  ? 2874 SER A N     1 
ATOM   12180 C CA    . SER A 1 2874 ? 114.977 154.741 154.618 1.00 49.66  ? 2874 SER A CA    1 
ATOM   12181 C C     . SER A 1 2874 ? 113.887 155.446 153.826 1.00 49.66  ? 2874 SER A C     1 
ATOM   12182 O O     . SER A 1 2874 ? 112.773 154.929 153.707 1.00 49.66  ? 2874 SER A O     1 
ATOM   12183 C CB    . SER A 1 2874 ? 115.373 153.427 153.949 1.00 49.66  ? 2874 SER A CB    1 
ATOM   12184 O OG    . SER A 1 2874 ? 115.866 153.651 152.639 1.00 49.66  ? 2874 SER A OG    1 
ATOM   12185 N N     . ASN A 1 2875 ? 114.208 156.623 153.283 1.00 50.19  ? 2875 ASN A N     1 
ATOM   12186 C CA    . ASN A 1 2875 ? 113.266 157.309 152.406 1.00 50.19  ? 2875 ASN A CA    1 
ATOM   12187 C C     . ASN A 1 2875 ? 113.230 156.670 151.025 1.00 50.19  ? 2875 ASN A C     1 
ATOM   12188 O O     . ASN A 1 2875 ? 112.382 157.026 150.198 1.00 50.19  ? 2875 ASN A O     1 
ATOM   12189 C CB    . ASN A 1 2875 ? 113.629 158.788 152.294 1.00 50.19  ? 2875 ASN A CB    1 
ATOM   12190 C CG    . ASN A 1 2875 ? 114.900 159.015 151.506 1.00 50.19  ? 2875 ASN A CG    1 
ATOM   12191 O OD1   . ASN A 1 2875 ? 115.940 158.431 151.805 1.00 50.19  ? 2875 ASN A OD1   1 
ATOM   12192 N ND2   . ASN A 1 2875 ? 114.823 159.865 150.490 1.00 50.19  ? 2875 ASN A ND2   1 
ATOM   12193 N N     . TRP A 1 2876 ? 114.150 155.741 150.755 1.00 47.62  ? 2876 TRP A N     1 
ATOM   12194 C CA    . TRP A 1 2876 ? 114.187 155.063 149.464 1.00 47.62  ? 2876 TRP A CA    1 
ATOM   12195 C C     . TRP A 1 2876 ? 112.873 154.349 149.177 1.00 47.62  ? 2876 TRP A C     1 
ATOM   12196 O O     . TRP A 1 2876 ? 112.268 154.534 148.116 1.00 47.62  ? 2876 TRP A O     1 
ATOM   12197 C CB    . TRP A 1 2876 ? 115.351 154.076 149.442 1.00 47.62  ? 2876 TRP A CB    1 
ATOM   12198 C CG    . TRP A 1 2876 ? 116.679 154.742 149.399 1.00 47.62  ? 2876 TRP A CG    1 
ATOM   12199 C CD1   . TRP A 1 2876 ? 116.945 156.012 148.982 1.00 47.62  ? 2876 TRP A CD1   1 
ATOM   12200 C CD2   . TRP A 1 2876 ? 117.928 154.185 149.817 1.00 47.62  ? 2876 TRP A CD2   1 
ATOM   12201 N NE1   . TRP A 1 2876 ? 118.287 156.275 149.097 1.00 47.62  ? 2876 TRP A NE1   1 
ATOM   12202 C CE2   . TRP A 1 2876 ? 118.912 155.169 149.610 1.00 47.62  ? 2876 TRP A CE2   1 
ATOM   12203 C CE3   . TRP A 1 2876 ? 118.311 152.947 150.339 1.00 47.62  ? 2876 TRP A CE3   1 
ATOM   12204 C CZ2   . TRP A 1 2876 ? 120.252 154.955 149.905 1.00 47.62  ? 2876 TRP A CZ2   1 
ATOM   12205 C CZ3   . TRP A 1 2876 ? 119.642 152.737 150.633 1.00 47.62  ? 2876 TRP A CZ3   1 
ATOM   12206 C CH2   . TRP A 1 2876 ? 120.596 153.736 150.418 1.00 47.62  ? 2876 TRP A CH2   1 
ATOM   12207 N N     . LEU A 1 2877 ? 112.417 153.526 150.115 1.00 52.61  ? 2877 LEU A N     1 
ATOM   12208 C CA    . LEU A 1 2877 ? 111.089 152.944 150.019 1.00 52.61  ? 2877 LEU A CA    1 
ATOM   12209 C C     . LEU A 1 2877 ? 110.057 153.972 150.459 1.00 52.61  ? 2877 LEU A C     1 
ATOM   12210 O O     . LEU A 1 2877 ? 110.313 154.778 151.359 1.00 52.61  ? 2877 LEU A O     1 
ATOM   12211 C CB    . LEU A 1 2877 ? 110.991 151.678 150.867 1.00 52.61  ? 2877 LEU A CB    1 
ATOM   12212 C CG    . LEU A 1 2877 ? 111.448 150.423 150.121 1.00 52.61  ? 2877 LEU A CG    1 
ATOM   12213 C CD1   . LEU A 1 2877 ? 111.428 149.201 151.020 1.00 52.61  ? 2877 LEU A CD1   1 
ATOM   12214 C CD2   . LEU A 1 2877 ? 110.582 150.200 148.894 1.00 52.61  ? 2877 LEU A CD2   1 
ATOM   12215 N N     . SER A 1 2878 ? 108.897 153.953 149.799 1.00 52.44  ? 2878 SER A N     1 
ATOM   12216 C CA    . SER A 1 2878 ? 107.874 154.981 149.961 1.00 52.44  ? 2878 SER A CA    1 
ATOM   12217 C C     . SER A 1 2878 ? 108.423 156.329 149.512 1.00 52.44  ? 2878 SER A C     1 
ATOM   12218 O O     . SER A 1 2878 ? 109.363 156.385 148.712 1.00 52.44  ? 2878 SER A O     1 
ATOM   12219 C CB    . SER A 1 2878 ? 107.370 155.049 151.405 1.00 52.44  ? 2878 SER A CB    1 
ATOM   12220 O OG    . SER A 1 2878 ? 108.176 155.918 152.182 1.00 52.44  ? 2878 SER A OG    1 
ATOM   12221 N N     . LYS A 1 2879 ? 107.847 157.420 150.014 1.00 57.97  ? 2879 LYS A N     1 
ATOM   12222 C CA    . LYS A 1 2879 ? 108.213 158.756 149.565 1.00 57.97  ? 2879 LYS A CA    1 
ATOM   12223 C C     . LYS A 1 2879 ? 108.886 159.608 150.631 1.00 57.97  ? 2879 LYS A C     1 
ATOM   12224 O O     . LYS A 1 2879 ? 109.214 160.767 150.351 1.00 57.97  ? 2879 LYS A O     1 
ATOM   12225 C CB    . LYS A 1 2879 ? 106.974 159.496 149.045 1.00 57.97  ? 2879 LYS A CB    1 
ATOM   12226 C CG    . LYS A 1 2879 ? 105.959 159.826 150.125 1.00 57.97  ? 2879 LYS A CG    1 
ATOM   12227 C CD    . LYS A 1 2879 ? 104.747 160.538 149.551 1.00 57.97  ? 2879 LYS A CD    1 
ATOM   12228 C CE    . LYS A 1 2879 ? 103.718 160.826 150.631 1.00 57.97  ? 2879 LYS A CE    1 
ATOM   12229 N NZ    . LYS A 1 2879 ? 104.219 161.817 151.621 1.00 57.97  ? 2879 LYS A NZ    1 
ATOM   12230 N N     . ASP A 1 2880 ? 109.105 159.086 151.836 1.00 53.47  ? 2880 ASP A N     1 
ATOM   12231 C CA    . ASP A 1 2880 ? 109.645 159.919 152.901 1.00 53.47  ? 2880 ASP A CA    1 
ATOM   12232 C C     . ASP A 1 2880 ? 110.338 159.055 153.944 1.00 53.47  ? 2880 ASP A C     1 
ATOM   12233 O O     . ASP A 1 2880 ? 110.296 157.823 153.895 1.00 53.47  ? 2880 ASP A O     1 
ATOM   12234 C CB    . ASP A 1 2880 ? 108.551 160.773 153.549 1.00 53.47  ? 2880 ASP A CB    1 
ATOM   12235 C CG    . ASP A 1 2880 ? 107.282 159.992 153.812 1.00 53.47  ? 2880 ASP A CG    1 
ATOM   12236 O OD1   . ASP A 1 2880 ? 107.226 158.803 153.435 1.00 53.47  ? 2880 ASP A OD1   1 
ATOM   12237 O OD2   . ASP A 1 2880 ? 106.340 160.568 154.394 1.00 53.47  ? 2880 ASP A OD2   1 
ATOM   12238 N N     . TYR A 1 2881 ? 110.975 159.736 154.892 1.00 45.04  ? 2881 TYR A N     1 
ATOM   12239 C CA    . TYR A 1 2881 ? 111.772 159.091 155.927 1.00 45.04  ? 2881 TYR A CA    1 
ATOM   12240 C C     . TYR A 1 2881 ? 110.872 158.393 156.940 1.00 45.04  ? 2881 TYR A C     1 
ATOM   12241 O O     . TYR A 1 2881 ? 110.358 159.025 157.868 1.00 45.04  ? 2881 TYR A O     1 
ATOM   12242 C CB    . TYR A 1 2881 ? 112.641 160.156 156.596 1.00 45.04  ? 2881 TYR A CB    1 
ATOM   12243 C CG    . TYR A 1 2881 ? 113.898 159.671 157.276 1.00 45.04  ? 2881 TYR A CG    1 
ATOM   12244 C CD1   . TYR A 1 2881 ? 113.864 159.152 158.559 1.00 45.04  ? 2881 TYR A CD1   1 
ATOM   12245 C CD2   . TYR A 1 2881 ? 115.121 159.722 156.625 1.00 45.04  ? 2881 TYR A CD2   1 
ATOM   12246 C CE1   . TYR A 1 2881 ? 115.019 158.723 159.185 1.00 45.04  ? 2881 TYR A CE1   1 
ATOM   12247 C CE2   . TYR A 1 2881 ? 116.276 159.283 157.239 1.00 45.04  ? 2881 TYR A CE2   1 
ATOM   12248 C CZ    . TYR A 1 2881 ? 116.219 158.782 158.518 1.00 45.04  ? 2881 TYR A CZ    1 
ATOM   12249 O OH    . TYR A 1 2881 ? 117.366 158.343 159.136 1.00 45.04  ? 2881 TYR A OH    1 
ATOM   12250 N N     . ILE A 1 2882 ? 110.683 157.087 156.760 1.00 47.01  ? 2882 ILE A N     1 
ATOM   12251 C CA    . ILE A 1 2882 ? 109.782 156.294 157.597 1.00 47.01  ? 2882 ILE A CA    1 
ATOM   12252 C C     . ILE A 1 2882 ? 110.475 154.998 158.004 1.00 47.01  ? 2882 ILE A C     1 
ATOM   12253 O O     . ILE A 1 2882 ? 111.456 154.596 157.362 1.00 47.01  ? 2882 ILE A O     1 
ATOM   12254 C CB    . ILE A 1 2882 ? 108.458 155.986 156.876 1.00 47.01  ? 2882 ILE A CB    1 
ATOM   12255 C CG1   . ILE A 1 2882 ? 108.653 154.852 155.867 1.00 47.01  ? 2882 ILE A CG1   1 
ATOM   12256 C CG2   . ILE A 1 2882 ? 107.895 157.227 156.197 1.00 47.01  ? 2882 ILE A CG2   1 
ATOM   12257 C CD1   . ILE A 1 2882 ? 107.426 154.551 155.041 1.00 47.01  ? 2882 ILE A CD1   1 
ATOM   12258 N N     . PRO A 1 2883 ? 110.025 154.331 159.066 1.00 47.95  ? 2883 PRO A N     1 
ATOM   12259 C CA    . PRO A 1 2883 ? 110.567 153.006 159.387 1.00 47.95  ? 2883 PRO A CA    1 
ATOM   12260 C C     . PRO A 1 2883 ? 110.321 152.020 158.256 1.00 47.95  ? 2883 PRO A C     1 
ATOM   12261 O O     . PRO A 1 2883 ? 109.275 152.042 157.603 1.00 47.95  ? 2883 PRO A O     1 
ATOM   12262 C CB    . PRO A 1 2883 ? 109.805 152.605 160.658 1.00 47.95  ? 2883 PRO A CB    1 
ATOM   12263 C CG    . PRO A 1 2883 ? 108.679 153.586 160.784 1.00 47.95  ? 2883 PRO A CG    1 
ATOM   12264 C CD    . PRO A 1 2883 ? 109.154 154.838 160.137 1.00 47.95  ? 2883 PRO A CD    1 
ATOM   12265 N N     . VAL A 1 2884 ? 111.295 151.147 158.026 1.00 52.47  ? 2884 VAL A N     1 
ATOM   12266 C CA    . VAL A 1 2884 ? 111.216 150.141 156.976 1.00 52.47  ? 2884 VAL A CA    1 
ATOM   12267 C C     . VAL A 1 2884 ? 111.846 148.850 157.479 1.00 52.47  ? 2884 VAL A C     1 
ATOM   12268 O O     . VAL A 1 2884 ? 112.839 148.875 158.216 1.00 52.47  ? 2884 VAL A O     1 
ATOM   12269 C CB    . VAL A 1 2884 ? 111.893 150.631 155.678 1.00 52.47  ? 2884 VAL A CB    1 
ATOM   12270 C CG1   . VAL A 1 2884 ? 113.382 150.825 155.889 1.00 52.47  ? 2884 VAL A CG1   1 
ATOM   12271 C CG2   . VAL A 1 2884 ? 111.631 149.661 154.544 1.00 52.47  ? 2884 VAL A CG2   1 
ATOM   12272 N N     . ASP A 1 2885 ? 111.252 147.721 157.098 1.00 56.93  ? 2885 ASP A N     1 
ATOM   12273 C CA    . ASP A 1 2885 ? 111.773 146.421 157.497 1.00 56.93  ? 2885 ASP A CA    1 
ATOM   12274 C C     . ASP A 1 2885 ? 113.056 146.098 156.741 1.00 56.93  ? 2885 ASP A C     1 
ATOM   12275 O O     . ASP A 1 2885 ? 113.304 146.620 155.651 1.00 56.93  ? 2885 ASP A O     1 
ATOM   12276 C CB    . ASP A 1 2885 ? 110.731 145.329 157.255 1.00 56.93  ? 2885 ASP A CB    1 
ATOM   12277 C CG    . ASP A 1 2885 ? 109.515 145.477 158.146 1.00 56.93  ? 2885 ASP A CG    1 
ATOM   12278 O OD1   . ASP A 1 2885 ? 109.646 146.066 159.240 1.00 56.93  ? 2885 ASP A OD1   1 
ATOM   12279 O OD2   . ASP A 1 2885 ? 108.430 144.995 157.760 1.00 56.93  ? 2885 ASP A OD2   1 
ATOM   12280 N N     . GLN A 1 2886 ? 113.874 145.226 157.333 1.00 59.69  ? 2886 GLN A N     1 
ATOM   12281 C CA    . GLN A 1 2886 ? 115.198 144.964 156.779 1.00 59.69  ? 2886 GLN A CA    1 
ATOM   12282 C C     . GLN A 1 2886 ? 115.122 144.155 155.489 1.00 59.69  ? 2886 GLN A C     1 
ATOM   12283 O O     . GLN A 1 2886 ? 115.955 144.328 154.595 1.00 59.69  ? 2886 GLN A O     1 
ATOM   12284 C CB    . GLN A 1 2886 ? 116.066 144.250 157.816 1.00 59.69  ? 2886 GLN A CB    1 
ATOM   12285 C CG    . GLN A 1 2886 ? 117.518 144.081 157.394 1.00 59.69  ? 2886 GLN A CG    1 
ATOM   12286 C CD    . GLN A 1 2886 ? 118.421 143.674 158.543 1.00 59.69  ? 2886 GLN A CD    1 
ATOM   12287 O OE1   . GLN A 1 2886 ? 117.957 143.437 159.657 1.00 59.69  ? 2886 GLN A OE1   1 
ATOM   12288 N NE2   . GLN A 1 2886 ? 119.720 143.599 158.277 1.00 59.69  ? 2886 GLN A NE2   1 
ATOM   12289 N N     . GLU A 1 2887 ? 114.132 143.267 155.368 1.00 63.63  ? 2887 GLU A N     1 
ATOM   12290 C CA    . GLU A 1 2887 ? 114.083 142.362 154.220 1.00 63.63  ? 2887 GLU A CA    1 
ATOM   12291 C C     . GLU A 1 2887 ? 113.697 143.095 152.938 1.00 63.63  ? 2887 GLU A C     1 
ATOM   12292 O O     . GLU A 1 2887 ? 114.313 142.892 151.883 1.00 63.63  ? 2887 GLU A O     1 
ATOM   12293 C CB    . GLU A 1 2887 ? 113.111 141.216 154.502 1.00 63.63  ? 2887 GLU A CB    1 
ATOM   12294 C CG    . GLU A 1 2887 ? 113.566 140.256 155.598 1.00 63.63  ? 2887 GLU A CG    1 
ATOM   12295 C CD    . GLU A 1 2887 ? 115.040 139.899 155.506 1.00 63.63  ? 2887 GLU A CD    1 
ATOM   12296 O OE1   . GLU A 1 2887 ? 115.718 139.902 156.555 1.00 63.63  ? 2887 GLU A OE1   1 
ATOM   12297 O OE2   . GLU A 1 2887 ? 115.518 139.590 154.394 1.00 63.63  ? 2887 GLU A OE2   1 
ATOM   12298 N N     . GLU A 1 2888 ? 112.661 143.935 153.002 1.00 62.53  ? 2888 GLU A N     1 
ATOM   12299 C CA    . GLU A 1 2888 ? 112.249 144.690 151.821 1.00 62.53  ? 2888 GLU A CA    1 
ATOM   12300 C C     . GLU A 1 2888 ? 113.340 145.655 151.378 1.00 62.53  ? 2888 GLU A C     1 
ATOM   12301 O O     . GLU A 1 2888 ? 113.633 145.773 150.180 1.00 62.53  ? 2888 GLU A O     1 
ATOM   12302 C CB    . GLU A 1 2888 ? 110.941 145.443 152.094 1.00 62.53  ? 2888 GLU A CB    1 
ATOM   12303 C CG    . GLU A 1 2888 ? 109.722 144.589 152.494 1.00 62.53  ? 2888 GLU A CG    1 
ATOM   12304 C CD    . GLU A 1 2888 ? 109.842 143.877 153.838 1.00 62.53  ? 2888 GLU A CD    1 
ATOM   12305 O OE1   . GLU A 1 2888 ? 110.940 143.855 154.431 1.00 62.53  ? 2888 GLU A OE1   1 
ATOM   12306 O OE2   . GLU A 1 2888 ? 108.821 143.327 154.302 1.00 62.53  ? 2888 GLU A OE2   1 
ATOM   12307 N N     . LEU A 1 2889 ? 113.959 146.348 152.335 1.00 54.46  ? 2889 LEU A N     1 
ATOM   12308 C CA    . LEU A 1 2889 ? 115.082 147.219 152.014 1.00 54.46  ? 2889 LEU A CA    1 
ATOM   12309 C C     . LEU A 1 2889 ? 116.227 146.423 151.407 1.00 54.46  ? 2889 LEU A C     1 
ATOM   12310 O O     . LEU A 1 2889 ? 116.892 146.886 150.476 1.00 54.46  ? 2889 LEU A O     1 
ATOM   12311 C CB    . LEU A 1 2889 ? 115.550 147.956 153.265 1.00 54.46  ? 2889 LEU A CB    1 
ATOM   12312 C CG    . LEU A 1 2889 ? 116.748 148.877 153.046 1.00 54.46  ? 2889 LEU A CG    1 
ATOM   12313 C CD1   . LEU A 1 2889 ? 116.349 150.096 152.234 1.00 54.46  ? 2889 LEU A CD1   1 
ATOM   12314 C CD2   . LEU A 1 2889 ? 117.339 149.280 154.375 1.00 54.46  ? 2889 LEU A CD2   1 
ATOM   12315 N N     . ARG A 1 2890 ? 116.476 145.224 151.936 1.00 53.91  ? 2890 ARG A N     1 
ATOM   12316 C CA    . ARG A 1 2890 ? 117.528 144.364 151.411 1.00 53.91  ? 2890 ARG A CA    1 
ATOM   12317 C C     . ARG A 1 2890 ? 117.269 144.017 149.955 1.00 53.91  ? 2890 ARG A C     1 
ATOM   12318 O O     . ARG A 1 2890 ? 118.166 144.107 149.115 1.00 53.91  ? 2890 ARG A O     1 
ATOM   12319 C CB    . ARG A 1 2890 ? 117.628 143.090 152.253 1.00 53.91  ? 2890 ARG A CB    1 
ATOM   12320 C CG    . ARG A 1 2890 ? 118.610 142.062 151.713 1.00 53.91  ? 2890 ARG A CG    1 
ATOM   12321 C CD    . ARG A 1 2890 ? 118.696 140.842 152.621 1.00 53.91  ? 2890 ARG A CD    1 
ATOM   12322 N NE    . ARG A 1 2890 ? 119.282 141.148 153.921 1.00 53.91  ? 2890 ARG A NE    1 
ATOM   12323 C CZ    . ARG A 1 2890 ? 120.562 141.432 154.122 1.00 53.91  ? 2890 ARG A CZ    1 
ATOM   12324 N NH1   . ARG A 1 2890 ? 121.432 141.454 153.126 1.00 53.91  ? 2890 ARG A NH1   1 
ATOM   12325 N NH2   . ARG A 1 2890 ? 120.981 141.695 155.357 1.00 53.91  ? 2890 ARG A NH2   1 
ATOM   12326 N N     . ASP A 1 2891 ? 116.035 143.630 149.636 1.00 56.87  ? 2891 ASP A N     1 
ATOM   12327 C CA    . ASP A 1 2891 ? 115.704 143.303 148.252 1.00 56.87  ? 2891 ASP A CA    1 
ATOM   12328 C C     . ASP A 1 2891 ? 115.865 144.522 147.349 1.00 56.87  ? 2891 ASP A C     1 
ATOM   12329 O O     . ASP A 1 2891 ? 116.413 144.424 146.240 1.00 56.87  ? 2891 ASP A O     1 
ATOM   12330 C CB    . ASP A 1 2891 ? 114.281 142.751 148.167 1.00 56.87  ? 2891 ASP A CB    1 
ATOM   12331 C CG    . ASP A 1 2891 ? 113.947 142.207 146.791 1.00 56.87  ? 2891 ASP A CG    1 
ATOM   12332 O OD1   . ASP A 1 2891 ? 114.879 142.008 145.984 1.00 56.87  ? 2891 ASP A OD1   1 
ATOM   12333 O OD2   . ASP A 1 2891 ? 112.751 141.978 146.516 1.00 56.87  ? 2891 ASP A OD2   1 
ATOM   12334 N N     . TYR A 1 2892 ? 115.404 145.685 147.816 1.00 53.68  ? 2892 TYR A N     1 
ATOM   12335 C CA    . TYR A 1 2892 ? 115.502 146.895 147.006 1.00 53.68  ? 2892 TYR A CA    1 
ATOM   12336 C C     . TYR A 1 2892 ? 116.958 147.254 146.729 1.00 53.68  ? 2892 TYR A C     1 
ATOM   12337 O O     . TYR A 1 2892 ? 117.328 147.570 145.591 1.00 53.68  ? 2892 TYR A O     1 
ATOM   12338 C CB    . TYR A 1 2892 ? 114.786 148.051 147.705 1.00 53.68  ? 2892 TYR A CB    1 
ATOM   12339 C CG    . TYR A 1 2892 ? 115.123 149.409 147.136 1.00 53.68  ? 2892 TYR A CG    1 
ATOM   12340 C CD1   . TYR A 1 2892 ? 114.603 149.818 145.917 1.00 53.68  ? 2892 TYR A CD1   1 
ATOM   12341 C CD2   . TYR A 1 2892 ? 115.967 150.278 147.812 1.00 53.68  ? 2892 TYR A CD2   1 
ATOM   12342 C CE1   . TYR A 1 2892 ? 114.907 151.057 145.390 1.00 53.68  ? 2892 TYR A CE1   1 
ATOM   12343 C CE2   . TYR A 1 2892 ? 116.280 151.517 147.291 1.00 53.68  ? 2892 TYR A CE2   1 
ATOM   12344 C CZ    . TYR A 1 2892 ? 115.746 151.902 146.081 1.00 53.68  ? 2892 TYR A CZ    1 
ATOM   12345 O OH    . TYR A 1 2892 ? 116.054 153.137 145.558 1.00 53.68  ? 2892 TYR A OH    1 
ATOM   12346 N N     . VAL A 1 2893 ? 117.804 147.205 147.762 1.00 52.76  ? 2893 VAL A N     1 
ATOM   12347 C CA    . VAL A 1 2893 ? 119.205 147.570 147.579 1.00 52.76  ? 2893 VAL A CA    1 
ATOM   12348 C C     . VAL A 1 2893 ? 119.933 146.518 146.752 1.00 52.76  ? 2893 VAL A C     1 
ATOM   12349 O O     . VAL A 1 2893 ? 120.859 146.847 146.007 1.00 52.76  ? 2893 VAL A O     1 
ATOM   12350 C CB    . VAL A 1 2893 ? 119.897 147.818 148.938 1.00 52.76  ? 2893 VAL A CB    1 
ATOM   12351 C CG1   . VAL A 1 2893 ? 119.848 146.591 149.810 1.00 52.76  ? 2893 VAL A CG1   1 
ATOM   12352 C CG2   . VAL A 1 2893 ? 121.336 148.269 148.737 1.00 52.76  ? 2893 VAL A CG2   1 
ATOM   12353 N N     . LYS A 1 2894 ? 119.529 145.248 146.849 1.00 55.51  ? 2894 LYS A N     1 
ATOM   12354 C CA    . LYS A 1 2894 ? 120.112 144.230 145.979 1.00 55.51  ? 2894 LYS A CA    1 
ATOM   12355 C C     . LYS A 1 2894 ? 119.794 144.511 144.517 1.00 55.51  ? 2894 LYS A C     1 
ATOM   12356 O O     . LYS A 1 2894 ? 120.667 144.393 143.652 1.00 55.51  ? 2894 LYS A O     1 
ATOM   12357 C CB    . LYS A 1 2894 ? 119.627 142.836 146.382 1.00 55.51  ? 2894 LYS A CB    1 
ATOM   12358 C CG    . LYS A 1 2894 ? 120.174 142.350 147.715 1.00 55.51  ? 2894 LYS A CG    1 
ATOM   12359 C CD    . LYS A 1 2894 ? 119.548 141.028 148.129 1.00 55.51  ? 2894 LYS A CD    1 
ATOM   12360 C CE    . LYS A 1 2894 ? 120.023 139.883 147.254 1.00 55.51  ? 2894 LYS A CE    1 
ATOM   12361 N NZ    . LYS A 1 2894 ? 119.497 138.575 147.735 1.00 55.51  ? 2894 LYS A NZ    1 
ATOM   12362 N N     . ALA A 1 2895 ? 118.551 144.897 144.219 1.00 60.32  ? 2895 ALA A N     1 
ATOM   12363 C CA    . ALA A 1 2895 ? 118.213 145.251 142.840 1.00 60.32  ? 2895 ALA A CA    1 
ATOM   12364 C C     . ALA A 1 2895 ? 118.987 146.483 142.375 1.00 60.32  ? 2895 ALA A C     1 
ATOM   12365 O O     . ALA A 1 2895 ? 119.525 146.514 141.255 1.00 60.32  ? 2895 ALA A O     1 
ATOM   12366 C CB    . ALA A 1 2895 ? 116.708 145.481 142.711 1.00 60.32  ? 2895 ALA A CB    1 
ATOM   12367 N N     . ARG A 1 2896 ? 119.060 147.509 143.227 1.00 59.09  ? 2896 ARG A N     1 
ATOM   12368 C CA    . ARG A 1 2896 ? 119.775 148.726 142.854 1.00 59.09  ? 2896 ARG A CA    1 
ATOM   12369 C C     . ARG A 1 2896 ? 121.256 148.451 142.633 1.00 59.09  ? 2896 ARG A C     1 
ATOM   12370 O O     . ARG A 1 2896 ? 121.864 148.994 141.706 1.00 59.09  ? 2896 ARG A O     1 
ATOM   12371 C CB    . ARG A 1 2896 ? 119.578 149.804 143.917 1.00 59.09  ? 2896 ARG A CB    1 
ATOM   12372 C CG    . ARG A 1 2896 ? 118.137 150.247 144.075 1.00 59.09  ? 2896 ARG A CG    1 
ATOM   12373 C CD    . ARG A 1 2896 ? 117.640 150.937 142.817 1.00 59.09  ? 2896 ARG A CD    1 
ATOM   12374 N NE    . ARG A 1 2896 ? 118.345 152.188 142.569 1.00 59.09  ? 2896 ARG A NE    1 
ATOM   12375 C CZ    . ARG A 1 2896 ? 118.344 152.831 141.410 1.00 59.09  ? 2896 ARG A CZ    1 
ATOM   12376 N NH1   . ARG A 1 2896 ? 117.685 152.366 140.362 1.00 59.09  ? 2896 ARG A NH1   1 
ATOM   12377 N NH2   . ARG A 1 2896 ? 119.022 153.970 141.300 1.00 59.09  ? 2896 ARG A NH2   1 
ATOM   12378 N N     . LEU A 1 2897 ? 121.856 147.600 143.466 1.00 57.09  ? 2897 LEU A N     1 
ATOM   12379 C CA    . LEU A 1 2897 ? 123.260 147.257 143.282 1.00 57.09  ? 2897 LEU A CA    1 
ATOM   12380 C C     . LEU A 1 2897 ? 123.465 146.345 142.084 1.00 57.09  ? 2897 LEU A C     1 
ATOM   12381 O O     . LEU A 1 2897 ? 124.538 146.365 141.476 1.00 57.09  ? 2897 LEU A O     1 
ATOM   12382 C CB    . LEU A 1 2897 ? 123.817 146.604 144.542 1.00 57.09  ? 2897 LEU A CB    1 
ATOM   12383 C CG    . LEU A 1 2897 ? 125.305 146.269 144.455 1.00 57.09  ? 2897 LEU A CG    1 
ATOM   12384 C CD1   . LEU A 1 2897 ? 126.150 147.516 144.278 1.00 57.09  ? 2897 LEU A CD1   1 
ATOM   12385 C CD2   . LEU A 1 2897 ? 125.720 145.528 145.683 1.00 57.09  ? 2897 LEU A CD2   1 
ATOM   12386 N N     . LYS A 1 2898 ? 122.467 145.535 141.732 1.00 64.62  ? 2898 LYS A N     1 
ATOM   12387 C CA    . LYS A 1 2898 ? 122.532 144.815 140.468 1.00 64.62  ? 2898 LYS A CA    1 
ATOM   12388 C C     . LYS A 1 2898 ? 122.681 145.799 139.319 1.00 64.62  ? 2898 LYS A C     1 
ATOM   12389 O O     . LYS A 1 2898 ? 123.599 145.690 138.495 1.00 64.62  ? 2898 LYS A O     1 
ATOM   12390 C CB    . LYS A 1 2898 ? 121.287 143.945 140.289 1.00 64.62  ? 2898 LYS A CB    1 
ATOM   12391 C CG    . LYS A 1 2898 ? 121.350 143.014 139.091 1.00 64.62  ? 2898 LYS A CG    1 
ATOM   12392 C CD    . LYS A 1 2898 ? 120.209 142.012 139.110 1.00 64.62  ? 2898 LYS A CD    1 
ATOM   12393 C CE    . LYS A 1 2898 ? 120.340 141.007 137.978 1.00 64.62  ? 2898 LYS A CE    1 
ATOM   12394 N NZ    . LYS A 1 2898 ? 119.275 139.968 138.028 1.00 64.62  ? 2898 LYS A NZ    1 
ATOM   12395 N N     . VAL A 1 2899 ? 121.810 146.810 139.291 1.00 62.66  ? 2899 VAL A N     1 
ATOM   12396 C CA    . VAL A 1 2899 ? 121.924 147.862 138.281 1.00 62.66  ? 2899 VAL A CA    1 
ATOM   12397 C C     . VAL A 1 2899 ? 123.284 148.547 138.355 1.00 62.66  ? 2899 VAL A C     1 
ATOM   12398 O O     . VAL A 1 2899 ? 123.921 148.809 137.324 1.00 62.66  ? 2899 VAL A O     1 
ATOM   12399 C CB    . VAL A 1 2899 ? 120.773 148.877 138.440 1.00 62.66  ? 2899 VAL A CB    1 
ATOM   12400 C CG1   . VAL A 1 2899 ? 120.937 150.028 137.460 1.00 62.66  ? 2899 VAL A CG1   1 
ATOM   12401 C CG2   . VAL A 1 2899 ? 119.432 148.189 138.242 1.00 62.66  ? 2899 VAL A CG2   1 
ATOM   12402 N N     . PHE A 1 2900 ? 123.758 148.832 139.567 1.00 59.44  ? 2900 PHE A N     1 
ATOM   12403 C CA    . PHE A 1 2900 ? 125.010 149.551 139.763 1.00 59.44  ? 2900 PHE A CA    1 
ATOM   12404 C C     . PHE A 1 2900 ? 126.218 148.780 139.247 1.00 59.44  ? 2900 PHE A C     1 
ATOM   12405 O O     . PHE A 1 2900 ? 127.012 149.327 138.483 1.00 59.44  ? 2900 PHE A O     1 
ATOM   12406 C CB    . PHE A 1 2900 ? 125.214 149.895 141.239 1.00 59.44  ? 2900 PHE A CB    1 
ATOM   12407 C CG    . PHE A 1 2900 ? 126.452 150.705 141.499 1.00 59.44  ? 2900 PHE A CG    1 
ATOM   12408 C CD1   . PHE A 1 2900 ? 126.694 151.866 140.788 1.00 59.44  ? 2900 PHE A CD1   1 
ATOM   12409 C CD2   . PHE A 1 2900 ? 127.369 150.309 142.454 1.00 59.44  ? 2900 PHE A CD2   1 
ATOM   12410 C CE1   . PHE A 1 2900 ? 127.830 152.613 141.021 1.00 59.44  ? 2900 PHE A CE1   1 
ATOM   12411 C CE2   . PHE A 1 2900 ? 128.501 151.056 142.695 1.00 59.44  ? 2900 PHE A CE2   1 
ATOM   12412 C CZ    . PHE A 1 2900 ? 128.734 152.207 141.976 1.00 59.44  ? 2900 PHE A CZ    1 
ATOM   12413 N N     . TYR A 1 2901 ? 126.389 147.521 139.652 1.00 68.68  ? 2901 TYR A N     1 
ATOM   12414 C CA    . TYR A 1 2901 ? 127.548 146.787 139.160 1.00 68.68  ? 2901 TYR A CA    1 
ATOM   12415 C C     . TYR A 1 2901 ? 127.332 146.322 137.728 1.00 68.68  ? 2901 TYR A C     1 
ATOM   12416 O O     . TYR A 1 2901 ? 128.262 145.787 137.113 1.00 68.68  ? 2901 TYR A O     1 
ATOM   12417 C CB    . TYR A 1 2901 ? 127.907 145.607 140.075 1.00 68.68  ? 2901 TYR A CB    1 
ATOM   12418 C CG    . TYR A 1 2901 ? 127.225 144.287 139.789 1.00 68.68  ? 2901 TYR A CG    1 
ATOM   12419 C CD1   . TYR A 1 2901 ? 125.873 144.106 140.019 1.00 68.68  ? 2901 TYR A CD1   1 
ATOM   12420 C CD2   . TYR A 1 2901 ? 127.957 143.206 139.316 1.00 68.68  ? 2901 TYR A CD2   1 
ATOM   12421 C CE1   . TYR A 1 2901 ? 125.262 142.889 139.767 1.00 68.68  ? 2901 TYR A CE1   1 
ATOM   12422 C CE2   . TYR A 1 2901 ? 127.357 141.989 139.061 1.00 68.68  ? 2901 TYR A CE2   1 
ATOM   12423 C CZ    . TYR A 1 2901 ? 126.009 141.836 139.288 1.00 68.68  ? 2901 TYR A CZ    1 
ATOM   12424 O OH    . TYR A 1 2901 ? 125.405 140.625 139.037 1.00 68.68  ? 2901 TYR A OH    1 
ATOM   12425 N N     . GLU A 1 2902 ? 126.125 146.510 137.185 1.00 70.62  ? 2902 GLU A N     1 
ATOM   12426 C CA    . GLU A 1 2902 ? 125.966 146.464 135.736 1.00 70.62  ? 2902 GLU A CA    1 
ATOM   12427 C C     . GLU A 1 2902 ? 126.548 147.713 135.082 1.00 70.62  ? 2902 GLU A C     1 
ATOM   12428 O O     . GLU A 1 2902 ? 127.139 147.636 133.998 1.00 70.62  ? 2902 GLU A O     1 
ATOM   12429 C CB    . GLU A 1 2902 ? 124.489 146.303 135.376 1.00 70.62  ? 2902 GLU A CB    1 
ATOM   12430 C CG    . GLU A 1 2902 ? 123.983 144.873 135.460 1.00 70.62  ? 2902 GLU A CG    1 
ATOM   12431 C CD    . GLU A 1 2902 ? 122.545 144.737 135.002 1.00 70.62  ? 2902 GLU A CD    1 
ATOM   12432 O OE1   . GLU A 1 2902 ? 121.690 145.508 135.488 1.00 70.62  ? 2902 GLU A OE1   1 
ATOM   12433 O OE2   . GLU A 1 2902 ? 122.268 143.856 134.163 1.00 70.62  ? 2902 GLU A OE2   1 
ATOM   12434 N N     . GLU A 1 2903 ? 126.395 148.873 135.723 1.00 69.66  ? 2903 GLU A N     1 
ATOM   12435 C CA    . GLU A 1 2903 ? 126.888 150.145 135.186 1.00 69.66  ? 2903 GLU A CA    1 
ATOM   12436 C C     . GLU A 1 2903 ? 128.035 150.639 136.066 1.00 69.66  ? 2903 GLU A C     1 
ATOM   12437 O O     . GLU A 1 2903 ? 127.803 151.303 137.081 1.00 69.66  ? 2903 GLU A O     1 
ATOM   12438 C CB    . GLU A 1 2903 ? 125.759 151.172 135.109 1.00 69.66  ? 2903 GLU A CB    1 
ATOM   12439 C CG    . GLU A 1 2903 ? 126.160 152.521 134.517 1.00 69.66  ? 2903 GLU A CG    1 
ATOM   12440 C CD    . GLU A 1 2903 ? 126.584 153.529 135.570 1.00 69.66  ? 2903 GLU A CD    1 
ATOM   12441 O OE1   . GLU A 1 2903 ? 127.678 154.115 135.428 1.00 69.66  ? 2903 GLU A OE1   1 
ATOM   12442 O OE2   . GLU A 1 2903 ? 125.828 153.730 136.543 1.00 69.66  ? 2903 GLU A OE2   1 
ATOM   12443 N N     . GLU A 1 2904 ? 129.271 150.324 135.657 1.00 74.43  ? 2904 GLU A N     1 
ATOM   12444 C CA    . GLU A 1 2904 ? 130.500 150.620 136.398 1.00 74.43  ? 2904 GLU A CA    1 
ATOM   12445 C C     . GLU A 1 2904 ? 130.662 149.708 137.609 1.00 74.43  ? 2904 GLU A C     1 
ATOM   12446 O O     . GLU A 1 2904 ? 129.702 149.067 138.047 1.00 74.43  ? 2904 GLU A O     1 
ATOM   12447 C CB    . GLU A 1 2904 ? 130.556 152.091 136.834 1.00 74.43  ? 2904 GLU A CB    1 
ATOM   12448 C CG    . GLU A 1 2904 ? 130.883 153.075 135.722 1.00 74.43  ? 2904 GLU A CG    1 
ATOM   12449 C CD    . GLU A 1 2904 ? 132.359 153.096 135.368 1.00 74.43  ? 2904 GLU A CD    1 
ATOM   12450 O OE1   . GLU A 1 2904 ? 133.151 152.417 136.055 1.00 74.43  ? 2904 GLU A OE1   1 
ATOM   12451 O OE2   . GLU A 1 2904 ? 132.727 153.789 134.397 1.00 74.43  ? 2904 GLU A OE2   1 
ATOM   12452 N N     . LEU A 1 2905 ? 131.882 149.648 138.145 1.00 72.17  ? 2905 LEU A N     1 
ATOM   12453 C CA    . LEU A 1 2905 ? 132.228 148.790 139.280 1.00 72.17  ? 2905 LEU A CA    1 
ATOM   12454 C C     . LEU A 1 2905 ? 131.807 147.346 139.000 1.00 72.17  ? 2905 LEU A C     1 
ATOM   12455 O O     . LEU A 1 2905 ? 130.892 146.799 139.619 1.00 72.17  ? 2905 LEU A O     1 
ATOM   12456 C CB    . LEU A 1 2905 ? 131.609 149.316 140.578 1.00 72.17  ? 2905 LEU A CB    1 
ATOM   12457 C CG    . LEU A 1 2905 ? 131.967 148.588 141.878 1.00 72.17  ? 2905 LEU A CG    1 
ATOM   12458 C CD1   . LEU A 1 2905 ? 133.479 148.505 142.013 1.00 72.17  ? 2905 LEU A CD1   1 
ATOM   12459 C CD2   . LEU A 1 2905 ? 131.357 149.265 143.087 1.00 72.17  ? 2905 LEU A CD2   1 
ATOM   12460 N N     . ASP A 1 2906 ? 132.471 146.742 138.010 1.00 72.31  ? 2906 ASP A N     1 
ATOM   12461 C CA    . ASP A 1 2906 ? 132.052 145.440 137.499 1.00 72.31  ? 2906 ASP A CA    1 
ATOM   12462 C C     . ASP A 1 2906 ? 132.233 144.311 138.510 1.00 72.31  ? 2906 ASP A C     1 
ATOM   12463 O O     . ASP A 1 2906 ? 131.622 143.246 138.359 1.00 72.31  ? 2906 ASP A O     1 
ATOM   12464 C CB    . ASP A 1 2906 ? 132.812 145.134 136.204 1.00 72.31  ? 2906 ASP A CB    1 
ATOM   12465 C CG    . ASP A 1 2906 ? 134.321 145.169 136.384 1.00 72.31  ? 2906 ASP A CG    1 
ATOM   12466 O OD1   . ASP A 1 2906 ? 134.788 145.507 137.493 1.00 72.31  ? 2906 ASP A OD1   1 
ATOM   12467 O OD2   . ASP A 1 2906 ? 135.040 144.863 135.410 1.00 72.31  ? 2906 ASP A OD2   1 
ATOM   12468 N N     . VAL A 1 2907 ? 133.057 144.509 139.534 1.00 63.27  ? 2907 VAL A N     1 
ATOM   12469 C CA    . VAL A 1 2907 ? 133.293 143.458 140.525 1.00 63.27  ? 2907 VAL A CA    1 
ATOM   12470 C C     . VAL A 1 2907 ? 132.007 143.233 141.315 1.00 63.27  ? 2907 VAL A C     1 
ATOM   12471 O O     . VAL A 1 2907 ? 131.344 144.201 141.713 1.00 63.27  ? 2907 VAL A O     1 
ATOM   12472 C CB    . VAL A 1 2907 ? 134.488 143.800 141.435 1.00 63.27  ? 2907 VAL A CB    1 
ATOM   12473 C CG1   . VAL A 1 2907 ? 134.207 145.022 142.276 1.00 63.27  ? 2907 VAL A CG1   1 
ATOM   12474 C CG2   . VAL A 1 2907 ? 134.855 142.622 142.328 1.00 63.27  ? 2907 VAL A CG2   1 
ATOM   12475 N N     . PRO A 1 2908 ? 131.594 141.984 141.525 1.00 50.04  ? 2908 PRO A N     1 
ATOM   12476 C CA    . PRO A 1 2908 ? 130.356 141.732 142.270 1.00 50.04  ? 2908 PRO A CA    1 
ATOM   12477 C C     . PRO A 1 2908 ? 130.485 142.112 143.734 1.00 50.04  ? 2908 PRO A C     1 
ATOM   12478 O O     . PRO A 1 2908 ? 131.585 142.216 144.283 1.00 50.04  ? 2908 PRO A O     1 
ATOM   12479 C CB    . PRO A 1 2908 ? 130.144 140.221 142.112 1.00 50.04  ? 2908 PRO A CB    1 
ATOM   12480 C CG    . PRO A 1 2908 ? 131.015 139.821 140.969 1.00 50.04  ? 2908 PRO A CG    1 
ATOM   12481 C CD    . PRO A 1 2908 ? 132.184 140.742 141.005 1.00 50.04  ? 2908 PRO A CD    1 
ATOM   12482 N N     . LEU A 1 2909 ? 129.332 142.320 144.365 1.00 37.44  ? 2909 LEU A N     1 
ATOM   12483 C CA    . LEU A 1 2909 ? 129.253 142.688 145.771 1.00 37.44  ? 2909 LEU A CA    1 
ATOM   12484 C C     . LEU A 1 2909 ? 128.218 141.808 146.455 1.00 37.44  ? 2909 LEU A C     1 
ATOM   12485 O O     . LEU A 1 2909 ? 127.172 141.509 145.870 1.00 37.44  ? 2909 LEU A O     1 
ATOM   12486 C CB    . LEU A 1 2909 ? 128.877 144.162 145.931 1.00 37.44  ? 2909 LEU A CB    1 
ATOM   12487 C CG    . LEU A 1 2909 ? 129.938 145.242 145.717 1.00 37.44  ? 2909 LEU A CG    1 
ATOM   12488 C CD1   . LEU A 1 2909 ? 129.396 146.603 146.122 1.00 37.44  ? 2909 LEU A CD1   1 
ATOM   12489 C CD2   . LEU A 1 2909 ? 131.201 144.924 146.481 1.00 37.44  ? 2909 LEU A CD2   1 
ATOM   12490 N N     . VAL A 1 2910 ? 128.505 141.397 147.685 1.00 33.24  ? 2910 VAL A N     1 
ATOM   12491 C CA    . VAL A 1 2910 ? 127.568 140.611 148.480 1.00 33.24  ? 2910 VAL A CA    1 
ATOM   12492 C C     . VAL A 1 2910 ? 127.061 141.467 149.634 1.00 33.24  ? 2910 VAL A C     1 
ATOM   12493 O O     . VAL A 1 2910 ? 127.833 142.195 150.269 1.00 33.24  ? 2910 VAL A O     1 
ATOM   12494 C CB    . VAL A 1 2910 ? 128.224 139.316 148.986 1.00 33.24  ? 2910 VAL A CB    1 
ATOM   12495 C CG1   . VAL A 1 2910 ? 129.495 139.627 149.715 1.00 33.24  ? 2910 VAL A CG1   1 
ATOM   12496 C CG2   . VAL A 1 2910 ? 127.272 138.548 149.891 1.00 33.24  ? 2910 VAL A CG2   1 
ATOM   12497 N N     . LEU A 1 2911 ? 125.754 141.402 149.888 1.00 35.73  ? 2911 LEU A N     1 
ATOM   12498 C CA    . LEU A 1 2911 ? 125.108 142.269 150.874 1.00 35.73  ? 2911 LEU A CA    1 
ATOM   12499 C C     . LEU A 1 2911 ? 124.851 141.506 152.167 1.00 35.73  ? 2911 LEU A C     1 
ATOM   12500 O O     . LEU A 1 2911 ? 123.767 140.976 152.417 1.00 35.73  ? 2911 LEU A O     1 
ATOM   12501 C CB    . LEU A 1 2911 ? 123.824 142.853 150.302 1.00 35.73  ? 2911 LEU A CB    1 
ATOM   12502 C CG    . LEU A 1 2911 ? 123.978 144.275 149.774 1.00 35.73  ? 2911 LEU A CG    1 
ATOM   12503 C CD1   . LEU A 1 2911 ? 125.123 144.343 148.806 1.00 35.73  ? 2911 LEU A CD1   1 
ATOM   12504 C CD2   . LEU A 1 2911 ? 122.705 144.699 149.084 1.00 35.73  ? 2911 LEU A CD2   1 
ATOM   12505 N N     . PHE A 1 2912 ? 125.878 141.457 153.009 1.00 34.32  ? 2912 PHE A N     1 
ATOM   12506 C CA    . PHE A 1 2912 ? 125.643 141.064 154.386 1.00 34.32  ? 2912 PHE A CA    1 
ATOM   12507 C C     . PHE A 1 2912 ? 125.153 142.269 155.186 1.00 34.32  ? 2912 PHE A C     1 
ATOM   12508 O O     . PHE A 1 2912 ? 125.269 143.420 154.757 1.00 34.32  ? 2912 PHE A O     1 
ATOM   12509 C CB    . PHE A 1 2912 ? 126.900 140.447 155.005 1.00 34.32  ? 2912 PHE A CB    1 
ATOM   12510 C CG    . PHE A 1 2912 ? 128.158 141.240 154.793 1.00 34.32  ? 2912 PHE A CG    1 
ATOM   12511 C CD1   . PHE A 1 2912 ? 128.507 142.262 155.659 1.00 34.32  ? 2912 PHE A CD1   1 
ATOM   12512 C CD2   . PHE A 1 2912 ? 129.009 140.942 153.742 1.00 34.32  ? 2912 PHE A CD2   1 
ATOM   12513 C CE1   . PHE A 1 2912 ? 129.674 142.977 155.475 1.00 34.32  ? 2912 PHE A CE1   1 
ATOM   12514 C CE2   . PHE A 1 2912 ? 130.172 141.657 153.548 1.00 34.32  ? 2912 PHE A CE2   1 
ATOM   12515 C CZ    . PHE A 1 2912 ? 130.508 142.673 154.417 1.00 34.32  ? 2912 PHE A CZ    1 
ATOM   12516 N N     . ASN A 1 2913 ? 124.586 141.984 156.361 1.00 37.75  ? 2913 ASN A N     1 
ATOM   12517 C CA    . ASN A 1 2913 ? 123.844 142.988 157.120 1.00 37.75  ? 2913 ASN A CA    1 
ATOM   12518 C C     . ASN A 1 2913 ? 124.664 144.246 157.386 1.00 37.75  ? 2913 ASN A C     1 
ATOM   12519 O O     . ASN A 1 2913 ? 124.139 145.366 157.360 1.00 37.75  ? 2913 ASN A O     1 
ATOM   12520 C CB    . ASN A 1 2913 ? 123.366 142.373 158.435 1.00 37.75  ? 2913 ASN A CB    1 
ATOM   12521 C CG    . ASN A 1 2913 ? 122.808 140.978 158.252 1.00 37.75  ? 2913 ASN A CG    1 
ATOM   12522 O OD1   . ASN A 1 2913 ? 121.835 140.777 157.526 1.00 37.75  ? 2913 ASN A OD1   1 
ATOM   12523 N ND2   . ASN A 1 2913 ? 123.429 140.003 158.904 1.00 37.75  ? 2913 ASN A ND2   1 
ATOM   12524 N N     . GLU A 1 2914 ? 125.963 144.074 157.640 1.00 35.47  ? 2914 GLU A N     1 
ATOM   12525 C CA    . GLU A 1 2914 ? 126.824 145.225 157.882 1.00 35.47  ? 2914 GLU A CA    1 
ATOM   12526 C C     . GLU A 1 2914 ? 126.860 146.150 156.673 1.00 35.47  ? 2914 GLU A C     1 
ATOM   12527 O O     . GLU A 1 2914 ? 126.827 147.376 156.823 1.00 35.47  ? 2914 GLU A O     1 
ATOM   12528 C CB    . GLU A 1 2914 ? 128.231 144.757 158.253 1.00 35.47  ? 2914 GLU A CB    1 
ATOM   12529 C CG    . GLU A 1 2914 ? 128.281 143.846 159.473 1.00 35.47  ? 2914 GLU A CG    1 
ATOM   12530 C CD    . GLU A 1 2914 ? 128.102 142.380 159.125 1.00 35.47  ? 2914 GLU A CD    1 
ATOM   12531 O OE1   . GLU A 1 2914 ? 127.072 142.035 158.508 1.00 35.47  ? 2914 GLU A OE1   1 
ATOM   12532 O OE2   . GLU A 1 2914 ? 128.989 141.571 159.470 1.00 35.47  ? 2914 GLU A OE2   1 
ATOM   12533 N N     . VAL A 1 2915 ? 126.911 145.583 155.464 1.00 36.23  ? 2915 VAL A N     1 
ATOM   12534 C CA    . VAL A 1 2915 ? 126.875 146.409 154.259 1.00 36.23  ? 2915 VAL A CA    1 
ATOM   12535 C C     . VAL A 1 2915 ? 125.606 147.245 154.230 1.00 36.23  ? 2915 VAL A C     1 
ATOM   12536 O O     . VAL A 1 2915 ? 125.638 148.439 153.919 1.00 36.23  ? 2915 VAL A O     1 
ATOM   12537 C CB    . VAL A 1 2915 ? 126.998 145.540 152.996 1.00 36.23  ? 2915 VAL A CB    1 
ATOM   12538 C CG1   . VAL A 1 2915 ? 126.845 146.395 151.754 1.00 36.23  ? 2915 VAL A CG1   1 
ATOM   12539 C CG2   . VAL A 1 2915 ? 128.336 144.856 152.964 1.00 36.23  ? 2915 VAL A CG2   1 
ATOM   12540 N N     . LEU A 1 2916 ? 124.468 146.631 154.554 1.00 38.77  ? 2916 LEU A N     1 
ATOM   12541 C CA    . LEU A 1 2916 ? 123.204 147.358 154.520 1.00 38.77  ? 2916 LEU A CA    1 
ATOM   12542 C C     . LEU A 1 2916 ? 123.192 148.488 155.544 1.00 38.77  ? 2916 LEU A C     1 
ATOM   12543 O O     . LEU A 1 2916 ? 122.755 149.608 155.247 1.00 38.77  ? 2916 LEU A O     1 
ATOM   12544 C CB    . LEU A 1 2916 ? 122.045 146.393 154.760 1.00 38.77  ? 2916 LEU A CB    1 
ATOM   12545 C CG    . LEU A 1 2916 ? 120.646 146.996 154.688 1.00 38.77  ? 2916 LEU A CG    1 
ATOM   12546 C CD1   . LEU A 1 2916 ? 120.384 147.536 153.295 1.00 38.77  ? 2916 LEU A CD1   1 
ATOM   12547 C CD2   . LEU A 1 2916 ? 119.612 145.956 155.063 1.00 38.77  ? 2916 LEU A CD2   1 
ATOM   12548 N N     . ASP A 1 2917 ? 123.681 148.215 156.757 1.00 36.88  ? 2917 ASP A N     1 
ATOM   12549 C CA    . ASP A 1 2917 ? 123.732 149.252 157.784 1.00 36.88  ? 2917 ASP A CA    1 
ATOM   12550 C C     . ASP A 1 2917 ? 124.615 150.414 157.346 1.00 36.88  ? 2917 ASP A C     1 
ATOM   12551 O O     . ASP A 1 2917 ? 124.262 151.586 157.520 1.00 36.88  ? 2917 ASP A O     1 
ATOM   12552 C CB    . ASP A 1 2917 ? 124.236 148.668 159.107 1.00 36.88  ? 2917 ASP A CB    1 
ATOM   12553 C CG    . ASP A 1 2917 ? 123.357 147.551 159.627 1.00 36.88  ? 2917 ASP A CG    1 
ATOM   12554 O OD1   . ASP A 1 2917 ? 122.139 147.776 159.783 1.00 36.88  ? 2917 ASP A OD1   1 
ATOM   12555 O OD2   . ASP A 1 2917 ? 123.886 146.454 159.901 1.00 36.88  ? 2917 ASP A OD2   1 
ATOM   12556 N N     . HIS A 1 2918 ? 125.778 150.101 156.773 1.00 37.86  ? 2918 HIS A N     1 
ATOM   12557 C CA    . HIS A 1 2918 ? 126.694 151.155 156.351 1.00 37.86  ? 2918 HIS A CA    1 
ATOM   12558 C C     . HIS A 1 2918 ? 126.137 151.949 155.175 1.00 37.86  ? 2918 HIS A C     1 
ATOM   12559 O O     . HIS A 1 2918 ? 126.326 153.169 155.109 1.00 37.86  ? 2918 HIS A O     1 
ATOM   12560 C CB    . HIS A 1 2918 ? 128.056 150.548 156.022 1.00 37.86  ? 2918 HIS A CB    1 
ATOM   12561 C CG    . HIS A 1 2918 ? 128.775 150.016 157.223 1.00 37.86  ? 2918 HIS A CG    1 
ATOM   12562 N ND1   . HIS A 1 2918 ? 129.163 150.821 158.272 1.00 37.86  ? 2918 HIS A ND1   1 
ATOM   12563 C CD2   . HIS A 1 2918 ? 129.151 148.759 157.557 1.00 37.86  ? 2918 HIS A CD2   1 
ATOM   12564 C CE1   . HIS A 1 2918 ? 129.764 150.087 159.191 1.00 37.86  ? 2918 HIS A CE1   1 
ATOM   12565 N NE2   . HIS A 1 2918 ? 129.769 148.831 158.781 1.00 37.86  ? 2918 HIS A NE2   1 
ATOM   12566 N N     . VAL A 1 2919 ? 125.434 151.286 154.255 1.00 36.81  ? 2919 VAL A N     1 
ATOM   12567 C CA    . VAL A 1 2919 ? 124.750 151.994 153.176 1.00 36.81  ? 2919 VAL A CA    1 
ATOM   12568 C C     . VAL A 1 2919 ? 123.715 152.956 153.745 1.00 36.81  ? 2919 VAL A C     1 
ATOM   12569 O O     . VAL A 1 2919 ? 123.616 154.112 153.316 1.00 36.81  ? 2919 VAL A O     1 
ATOM   12570 C CB    . VAL A 1 2919 ? 124.113 150.997 152.191 1.00 36.81  ? 2919 VAL A CB    1 
ATOM   12571 C CG1   . VAL A 1 2919 ? 123.309 151.728 151.147 1.00 36.81  ? 2919 VAL A CG1   1 
ATOM   12572 C CG2   . VAL A 1 2919 ? 125.192 150.198 151.490 1.00 36.81  ? 2919 VAL A CG2   1 
ATOM   12573 N N     . LEU A 1 2920 ? 122.937 152.495 154.727 1.00 37.11  ? 2920 LEU A N     1 
ATOM   12574 C CA    . LEU A 1 2920 ? 121.926 153.357 155.333 1.00 37.11  ? 2920 LEU A CA    1 
ATOM   12575 C C     . LEU A 1 2920 ? 122.557 154.568 156.009 1.00 37.11  ? 2920 LEU A C     1 
ATOM   12576 O O     . LEU A 1 2920 ? 122.079 155.699 155.861 1.00 37.11  ? 2920 LEU A O     1 
ATOM   12577 C CB    . LEU A 1 2920 ? 121.098 152.563 156.338 1.00 37.11  ? 2920 LEU A CB    1 
ATOM   12578 C CG    . LEU A 1 2920 ? 120.077 151.601 155.747 1.00 37.11  ? 2920 LEU A CG    1 
ATOM   12579 C CD1   . LEU A 1 2920 ? 119.082 151.242 156.818 1.00 37.11  ? 2920 LEU A CD1   1 
ATOM   12580 C CD2   . LEU A 1 2920 ? 119.385 152.236 154.553 1.00 37.11  ? 2920 LEU A CD2   1 
ATOM   12581 N N     . ARG A 1 2921 ? 123.636 154.346 156.761 1.00 35.91  ? 2921 ARG A N     1 
ATOM   12582 C CA    . ARG A 1 2921 ? 124.302 155.444 157.453 1.00 35.91  ? 2921 ARG A CA    1 
ATOM   12583 C C     . ARG A 1 2921 ? 124.872 156.451 156.461 1.00 35.91  ? 2921 ARG A C     1 
ATOM   12584 O O     . ARG A 1 2921 ? 124.729 157.670 156.630 1.00 35.91  ? 2921 ARG A O     1 
ATOM   12585 C CB    . ARG A 1 2921 ? 125.401 154.887 158.359 1.00 35.91  ? 2921 ARG A CB    1 
ATOM   12586 C CG    . ARG A 1 2921 ? 124.881 153.977 159.456 1.00 35.91  ? 2921 ARG A CG    1 
ATOM   12587 C CD    . ARG A 1 2921 ? 126.011 153.237 160.146 1.00 35.91  ? 2921 ARG A CD    1 
ATOM   12588 N NE    . ARG A 1 2921 ? 125.516 152.298 161.145 1.00 35.91  ? 2921 ARG A NE    1 
ATOM   12589 C CZ    . ARG A 1 2921 ? 126.282 151.453 161.820 1.00 35.91  ? 2921 ARG A CZ    1 
ATOM   12590 N NH1   . ARG A 1 2921 ? 127.588 151.398 161.624 1.00 35.91  ? 2921 ARG A NH1   1 
ATOM   12591 N NH2   . ARG A 1 2921 ? 125.722 150.638 162.709 1.00 35.91  ? 2921 ARG A NH2   1 
ATOM   12592 N N     . ILE A 1 2922 ? 125.516 155.951 155.403 1.00 38.30  ? 2922 ILE A N     1 
ATOM   12593 C CA    . ILE A 1 2922 ? 126.137 156.842 154.429 1.00 38.30  ? 2922 ILE A CA    1 
ATOM   12594 C C     . ILE A 1 2922 ? 125.061 157.641 153.704 1.00 38.30  ? 2922 ILE A C     1 
ATOM   12595 O O     . ILE A 1 2922 ? 125.230 158.835 153.421 1.00 38.30  ? 2922 ILE A O     1 
ATOM   12596 C CB    . ILE A 1 2922 ? 127.008 156.032 153.451 1.00 38.30  ? 2922 ILE A CB    1 
ATOM   12597 C CG1   . ILE A 1 2922 ? 128.370 155.732 154.069 1.00 38.30  ? 2922 ILE A CG1   1 
ATOM   12598 C CG2   . ILE A 1 2922 ? 127.283 156.838 152.209 1.00 38.30  ? 2922 ILE A CG2   1 
ATOM   12599 C CD1   . ILE A 1 2922 ? 129.249 154.861 153.197 1.00 38.30  ? 2922 ILE A CD1   1 
ATOM   12600 N N     . ASP A 1 2923 ? 123.925 157.000 153.414 1.00 39.54  ? 2923 ASP A N     1 
ATOM   12601 C CA    . ASP A 1 2923 ? 122.800 157.696 152.796 1.00 39.54  ? 2923 ASP A CA    1 
ATOM   12602 C C     . ASP A 1 2923 ? 122.256 158.782 153.712 1.00 39.54  ? 2923 ASP A C     1 
ATOM   12603 O O     . ASP A 1 2923 ? 121.939 159.892 153.266 1.00 39.54  ? 2923 ASP A O     1 
ATOM   12604 C CB    . ASP A 1 2923 ? 121.700 156.696 152.445 1.00 39.54  ? 2923 ASP A CB    1 
ATOM   12605 C CG    . ASP A 1 2923 ? 120.373 157.369 152.150 1.00 39.54  ? 2923 ASP A CG    1 
ATOM   12606 O OD1   . ASP A 1 2923 ? 120.316 158.182 151.204 1.00 39.54  ? 2923 ASP A OD1   1 
ATOM   12607 O OD2   . ASP A 1 2923 ? 119.387 157.084 152.862 1.00 39.54  ? 2923 ASP A OD2   1 
ATOM   12608 N N     . ARG A 1 2924 ? 122.126 158.471 155.003 1.00 38.09  ? 2924 ARG A N     1 
ATOM   12609 C CA    . ARG A 1 2924 ? 121.634 159.449 155.965 1.00 38.09  ? 2924 ARG A CA    1 
ATOM   12610 C C     . ARG A 1 2924 ? 122.543 160.666 156.008 1.00 38.09  ? 2924 ARG A C     1 
ATOM   12611 O O     . ARG A 1 2924 ? 122.075 161.807 156.091 1.00 38.09  ? 2924 ARG A O     1 
ATOM   12612 C CB    . ARG A 1 2924 ? 121.523 158.811 157.352 1.00 38.09  ? 2924 ARG A CB    1 
ATOM   12613 C CG    . ARG A 1 2924 ? 121.119 159.785 158.442 1.00 38.09  ? 2924 ARG A CG    1 
ATOM   12614 C CD    . ARG A 1 2924 ? 120.897 159.082 159.772 1.00 38.09  ? 2924 ARG A CD    1 
ATOM   12615 N NE    . ARG A 1 2924 ? 120.771 160.026 160.877 1.00 38.09  ? 2924 ARG A NE    1 
ATOM   12616 C CZ    . ARG A 1 2924 ? 121.755 160.789 161.335 1.00 38.09  ? 2924 ARG A CZ    1 
ATOM   12617 N NH1   . ARG A 1 2924 ? 122.976 160.722 160.831 1.00 38.09  ? 2924 ARG A NH1   1 
ATOM   12618 N NH2   . ARG A 1 2924 ? 121.509 161.636 162.330 1.00 38.09  ? 2924 ARG A NH2   1 
ATOM   12619 N N     . ILE A 1 2925 ? 123.855 160.438 155.952 1.00 39.93  ? 2925 ILE A N     1 
ATOM   12620 C CA    . ILE A 1 2925 ? 124.791 161.561 155.974 1.00 39.93  ? 2925 ILE A CA    1 
ATOM   12621 C C     . ILE A 1 2925 ? 124.703 162.363 154.680 1.00 39.93  ? 2925 ILE A C     1 
ATOM   12622 O O     . ILE A 1 2925 ? 124.734 163.600 154.694 1.00 39.93  ? 2925 ILE A O     1 
ATOM   12623 C CB    . ILE A 1 2925 ? 126.225 161.073 156.240 1.00 39.93  ? 2925 ILE A CB    1 
ATOM   12624 C CG1   . ILE A 1 2925 ? 126.273 160.212 157.502 1.00 39.93  ? 2925 ILE A CG1   1 
ATOM   12625 C CG2   . ILE A 1 2925 ? 127.150 162.260 156.389 1.00 39.93  ? 2925 ILE A CG2   1 
ATOM   12626 C CD1   . ILE A 1 2925 ? 125.528 160.799 158.681 1.00 39.93  ? 2925 ILE A CD1   1 
ATOM   12627 N N     . PHE A 1 2926 ? 124.603 161.675 153.538 1.00 42.76  ? 2926 PHE A N     1 
ATOM   12628 C CA    . PHE A 1 2926 ? 124.531 162.378 152.258 1.00 42.76  ? 2926 PHE A CA    1 
ATOM   12629 C C     . PHE A 1 2926 ? 123.275 163.234 152.148 1.00 42.76  ? 2926 PHE A C     1 
ATOM   12630 O O     . PHE A 1 2926 ? 123.327 164.359 151.638 1.00 42.76  ? 2926 PHE A O     1 
ATOM   12631 C CB    . PHE A 1 2926 ? 124.597 161.386 151.097 1.00 42.76  ? 2926 PHE A CB    1 
ATOM   12632 C CG    . PHE A 1 2926 ? 125.987 160.937 150.759 1.00 42.76  ? 2926 PHE A CG    1 
ATOM   12633 C CD1   . PHE A 1 2926 ? 127.085 161.625 151.241 1.00 42.76  ? 2926 PHE A CD1   1 
ATOM   12634 C CD2   . PHE A 1 2926 ? 126.196 159.839 149.945 1.00 42.76  ? 2926 PHE A CD2   1 
ATOM   12635 C CE1   . PHE A 1 2926 ? 128.365 161.222 150.924 1.00 42.76  ? 2926 PHE A CE1   1 
ATOM   12636 C CE2   . PHE A 1 2926 ? 127.475 159.430 149.627 1.00 42.76  ? 2926 PHE A CE2   1 
ATOM   12637 C CZ    . PHE A 1 2926 ? 128.560 160.123 150.117 1.00 42.76  ? 2926 PHE A CZ    1 
ATOM   12638 N N     . ARG A 1 2927 ? 122.134 162.715 152.608 1.00 43.09  ? 2927 ARG A N     1 
ATOM   12639 C CA    . ARG A 1 2927 ? 120.871 163.422 152.420 1.00 43.09  ? 2927 ARG A CA    1 
ATOM   12640 C C     . ARG A 1 2927 ? 120.870 164.763 153.144 1.00 43.09  ? 2927 ARG A C     1 
ATOM   12641 O O     . ARG A 1 2927 ? 120.439 165.781 152.590 1.00 43.09  ? 2927 ARG A O     1 
ATOM   12642 C CB    . ARG A 1 2927 ? 119.711 162.560 152.909 1.00 43.09  ? 2927 ARG A CB    1 
ATOM   12643 C CG    . ARG A 1 2927 ? 118.991 161.783 151.825 1.00 43.09  ? 2927 ARG A CG    1 
ATOM   12644 C CD    . ARG A 1 2927 ? 117.927 160.880 152.431 1.00 43.09  ? 2927 ARG A CD    1 
ATOM   12645 N NE    . ARG A 1 2927 ? 117.051 161.608 153.343 1.00 43.09  ? 2927 ARG A NE    1 
ATOM   12646 C CZ    . ARG A 1 2927 ? 117.155 161.588 154.665 1.00 43.09  ? 2927 ARG A CZ    1 
ATOM   12647 N NH1   . ARG A 1 2927 ? 118.094 160.882 155.273 1.00 43.09  ? 2927 ARG A NH1   1 
ATOM   12648 N NH2   . ARG A 1 2927 ? 116.308 162.310 155.393 1.00 43.09  ? 2927 ARG A NH2   1 
ATOM   12649 N N     . GLN A 1 2928 ? 121.341 164.779 154.387 1.00 46.72  ? 2928 GLN A N     1 
ATOM   12650 C CA    . GLN A 1 2928 ? 121.315 166.003 155.172 1.00 46.72  ? 2928 GLN A CA    1 
ATOM   12651 C C     . GLN A 1 2928 ? 122.282 167.030 154.586 1.00 46.72  ? 2928 GLN A C     1 
ATOM   12652 O O     . GLN A 1 2928 ? 123.344 166.663 154.075 1.00 46.72  ? 2928 GLN A O     1 
ATOM   12653 C CB    . GLN A 1 2928 ? 121.678 165.716 156.627 1.00 46.72  ? 2928 GLN A CB    1 
ATOM   12654 C CG    . GLN A 1 2928 ? 120.712 164.785 157.334 1.00 46.72  ? 2928 GLN A CG    1 
ATOM   12655 C CD    . GLN A 1 2928 ? 121.190 164.393 158.715 1.00 46.72  ? 2928 GLN A CD    1 
ATOM   12656 O OE1   . GLN A 1 2928 ? 122.272 164.789 159.145 1.00 46.72  ? 2928 GLN A OE1   1 
ATOM   12657 N NE2   . GLN A 1 2928 ? 120.381 163.612 159.421 1.00 46.72  ? 2928 GLN A NE2   1 
ATOM   12658 N N     . PRO A 1 2929 ? 121.947 168.320 154.648 1.00 56.63  ? 2929 PRO A N     1 
ATOM   12659 C CA    . PRO A 1 2929 ? 122.869 169.345 154.144 1.00 56.63  ? 2929 PRO A CA    1 
ATOM   12660 C C     . PRO A 1 2929 ? 124.084 169.506 155.043 1.00 56.63  ? 2929 PRO A C     1 
ATOM   12661 O O     . PRO A 1 2929 ? 124.236 170.526 155.723 1.00 56.63  ? 2929 PRO A O     1 
ATOM   12662 C CB    . PRO A 1 2929 ? 122.007 170.613 154.126 1.00 56.63  ? 2929 PRO A CB    1 
ATOM   12663 C CG    . PRO A 1 2929 ? 120.973 170.375 155.172 1.00 56.63  ? 2929 PRO A CG    1 
ATOM   12664 C CD    . PRO A 1 2929 ? 120.687 168.900 155.146 1.00 56.63  ? 2929 PRO A CD    1 
ATOM   12665 N N     . GLN A 1 2930 ? 124.951 168.496 155.057 1.00 57.06  ? 2930 GLN A N     1 
ATOM   12666 C CA    . GLN A 1 2930 ? 126.137 168.469 155.891 1.00 57.06  ? 2930 GLN A CA    1 
ATOM   12667 C C     . GLN A 1 2930 ? 127.367 168.705 155.006 1.00 57.06  ? 2930 GLN A C     1 
ATOM   12668 O O     . GLN A 1 2930 ? 127.240 168.937 153.796 1.00 57.06  ? 2930 GLN A O     1 
ATOM   12669 C CB    . GLN A 1 2930 ? 126.172 167.139 156.654 1.00 57.06  ? 2930 GLN A CB    1 
ATOM   12670 C CG    . GLN A 1 2930 ? 127.180 167.075 157.791 1.00 57.06  ? 2930 GLN A CG    1 
ATOM   12671 C CD    . GLN A 1 2930 ? 127.163 165.747 158.511 1.00 57.06  ? 2930 GLN A CD    1 
ATOM   12672 O OE1   . GLN A 1 2930 ? 126.387 164.854 158.174 1.00 57.06  ? 2930 GLN A OE1   1 
ATOM   12673 N NE2   . GLN A 1 2930 ? 128.026 165.608 159.508 1.00 57.06  ? 2930 GLN A NE2   1 
ATOM   12674 N N     . GLY A 1 2931 ? 128.554 168.652 155.607 1.00 54.87  ? 2931 GLY A N     1 
ATOM   12675 C CA    . GLY A 1 2931 ? 129.769 168.962 154.884 1.00 54.87  ? 2931 GLY A CA    1 
ATOM   12676 C C     . GLY A 1 2931 ? 130.823 167.874 154.840 1.00 54.87  ? 2931 GLY A C     1 
ATOM   12677 O O     . GLY A 1 2931 ? 131.848 168.058 154.181 1.00 54.87  ? 2931 GLY A O     1 
ATOM   12678 N N     . HIS A 1 2932 ? 130.607 166.749 155.521 1.00 55.07  ? 2932 HIS A N     1 
ATOM   12679 C CA    . HIS A 1 2932 ? 131.615 165.693 155.542 1.00 55.07  ? 2932 HIS A CA    1 
ATOM   12680 C C     . HIS A 1 2932 ? 130.981 164.390 156.006 1.00 55.07  ? 2932 HIS A C     1 
ATOM   12681 O O     . HIS A 1 2932 ? 129.962 164.385 156.703 1.00 55.07  ? 2932 HIS A O     1 
ATOM   12682 C CB    . HIS A 1 2932 ? 132.788 166.053 156.461 1.00 55.07  ? 2932 HIS A CB    1 
ATOM   12683 C CG    . HIS A 1 2932 ? 134.058 165.308 156.168 1.00 55.07  ? 2932 HIS A CG    1 
ATOM   12684 N ND1   . HIS A 1 2932 ? 135.232 165.948 155.834 1.00 55.07  ? 2932 HIS A ND1   1 
ATOM   12685 C CD2   . HIS A 1 2932 ? 134.344 163.985 156.176 1.00 55.07  ? 2932 HIS A CD2   1 
ATOM   12686 C CE1   . HIS A 1 2932 ? 136.183 165.052 155.639 1.00 55.07  ? 2932 HIS A CE1   1 
ATOM   12687 N NE2   . HIS A 1 2932 ? 135.670 163.852 155.840 1.00 55.07  ? 2932 HIS A NE2   1 
ATOM   12688 N N     . LEU A 1 2933 ? 131.607 163.284 155.604 1.00 47.20  ? 2933 LEU A N     1 
ATOM   12689 C CA    . LEU A 1 2933 ? 131.341 161.957 156.160 1.00 47.20  ? 2933 LEU A CA    1 
ATOM   12690 C C     . LEU A 1 2933 ? 132.671 161.211 156.200 1.00 47.20  ? 2933 LEU A C     1 
ATOM   12691 O O     . LEU A 1 2933 ? 133.141 160.714 155.173 1.00 47.20  ? 2933 LEU A O     1 
ATOM   12692 C CB    . LEU A 1 2933 ? 130.305 161.201 155.342 1.00 47.20  ? 2933 LEU A CB    1 
ATOM   12693 C CG    . LEU A 1 2933 ? 130.166 159.713 155.662 1.00 47.20  ? 2933 LEU A CG    1 
ATOM   12694 C CD1   . LEU A 1 2933 ? 129.757 159.494 157.109 1.00 47.20  ? 2933 LEU A CD1   1 
ATOM   12695 C CD2   . LEU A 1 2933 ? 129.156 159.094 154.723 1.00 47.20  ? 2933 LEU A CD2   1 
ATOM   12696 N N     . LEU A 1 2934 ? 133.274 161.140 157.382 1.00 48.17  ? 2934 LEU A N     1 
ATOM   12697 C CA    . LEU A 1 2934 ? 134.585 160.523 157.527 1.00 48.17  ? 2934 LEU A CA    1 
ATOM   12698 C C     . LEU A 1 2934 ? 134.430 159.052 157.891 1.00 48.17  ? 2934 LEU A C     1 
ATOM   12699 O O     . LEU A 1 2934 ? 133.716 158.710 158.839 1.00 48.17  ? 2934 LEU A O     1 
ATOM   12700 C CB    . LEU A 1 2934 ? 135.397 161.252 158.594 1.00 48.17  ? 2934 LEU A CB    1 
ATOM   12701 C CG    . LEU A 1 2934 ? 136.648 160.555 159.119 1.00 48.17  ? 2934 LEU A CG    1 
ATOM   12702 C CD1   . LEU A 1 2934 ? 137.739 160.646 158.079 1.00 48.17  ? 2934 LEU A CD1   1 
ATOM   12703 C CD2   . LEU A 1 2934 ? 137.102 161.172 160.427 1.00 48.17  ? 2934 LEU A CD2   1 
ATOM   12704 N N     . LEU A 1 2935 ? 135.104 158.185 157.140 1.00 43.93  ? 2935 LEU A N     1 
ATOM   12705 C CA    . LEU A 1 2935 ? 134.990 156.742 157.297 1.00 43.93  ? 2935 LEU A CA    1 
ATOM   12706 C C     . LEU A 1 2935 ? 136.334 156.174 157.725 1.00 43.93  ? 2935 LEU A C     1 
ATOM   12707 O O     . LEU A 1 2935 ? 137.358 156.460 157.101 1.00 43.93  ? 2935 LEU A O     1 
ATOM   12708 C CB    . LEU A 1 2935 ? 134.532 156.088 155.991 1.00 43.93  ? 2935 LEU A CB    1 
ATOM   12709 C CG    . LEU A 1 2935 ? 133.037 155.798 155.861 1.00 43.93  ? 2935 LEU A CG    1 
ATOM   12710 C CD1   . LEU A 1 2935 ? 132.700 155.377 154.442 1.00 43.93  ? 2935 LEU A CD1   1 
ATOM   12711 C CD2   . LEU A 1 2935 ? 132.615 154.732 156.854 1.00 43.93  ? 2935 LEU A CD2   1 
ATOM   12712 N N     . ILE A 1 2936 ? 136.332 155.371 158.785 1.00 46.75  ? 2936 ILE A N     1 
ATOM   12713 C CA    . ILE A 1 2936 ? 137.548 154.766 159.316 1.00 46.75  ? 2936 ILE A CA    1 
ATOM   12714 C C     . ILE A 1 2936 ? 137.353 153.258 159.386 1.00 46.75  ? 2936 ILE A C     1 
ATOM   12715 O O     . ILE A 1 2936 ? 136.349 152.780 159.926 1.00 46.75  ? 2936 ILE A O     1 
ATOM   12716 C CB    . ILE A 1 2936 ? 137.916 155.347 160.694 1.00 46.75  ? 2936 ILE A CB    1 
ATOM   12717 C CG1   . ILE A 1 2936 ? 136.676 155.460 161.583 1.00 46.75  ? 2936 ILE A CG1   1 
ATOM   12718 C CG2   . ILE A 1 2936 ? 138.599 156.697 160.539 1.00 46.75  ? 2936 ILE A CG2   1 
ATOM   12719 C CD1   . ILE A 1 2936 ? 136.990 155.690 163.044 1.00 46.75  ? 2936 ILE A CD1   1 
ATOM   12720 N N     . GLY A 1 2937 ? 138.308 152.516 158.836 1.00 44.89  ? 2937 GLY A N     1 
ATOM   12721 C CA    . GLY A 1 2937 ? 138.236 151.068 158.839 1.00 44.89  ? 2937 GLY A CA    1 
ATOM   12722 C C     . GLY A 1 2937 ? 139.462 150.467 158.192 1.00 44.89  ? 2937 GLY A C     1 
ATOM   12723 O O     . GLY A 1 2937 ? 140.312 151.177 157.646 1.00 44.89  ? 2937 GLY A O     1 
ATOM   12724 N N     . VAL A 1 2938 ? 139.541 149.136 158.265 1.00 39.57  ? 2938 VAL A N     1 
ATOM   12725 C CA    . VAL A 1 2938 ? 140.686 148.427 157.707 1.00 39.57  ? 2938 VAL A CA    1 
ATOM   12726 C C     . VAL A 1 2938 ? 140.656 148.515 156.185 1.00 39.57  ? 2938 VAL A C     1 
ATOM   12727 O O     . VAL A 1 2938 ? 139.587 148.585 155.566 1.00 39.57  ? 2938 VAL A O     1 
ATOM   12728 C CB    . VAL A 1 2938 ? 140.702 146.969 158.199 1.00 39.57  ? 2938 VAL A CB    1 
ATOM   12729 C CG1   . VAL A 1 2938 ? 139.529 146.189 157.628 1.00 39.57  ? 2938 VAL A CG1   1 
ATOM   12730 C CG2   . VAL A 1 2938 ? 142.024 146.299 157.855 1.00 39.57  ? 2938 VAL A CG2   1 
ATOM   12731 N N     . SER A 1 2939 ? 141.841 148.531 155.577 1.00 41.45  ? 2939 SER A N     1 
ATOM   12732 C CA    . SER A 1 2939 ? 141.949 148.757 154.141 1.00 41.45  ? 2939 SER A CA    1 
ATOM   12733 C C     . SER A 1 2939 ? 141.316 147.615 153.357 1.00 41.45  ? 2939 SER A C     1 
ATOM   12734 O O     . SER A 1 2939 ? 141.429 146.445 153.727 1.00 41.45  ? 2939 SER A O     1 
ATOM   12735 C CB    . SER A 1 2939 ? 143.416 148.918 153.739 1.00 41.45  ? 2939 SER A CB    1 
ATOM   12736 O OG    . SER A 1 2939 ? 143.988 150.069 154.335 1.00 41.45  ? 2939 SER A OG    1 
ATOM   12737 N N     . GLY A 1 2940 ? 140.635 147.964 152.269 1.00 33.42  ? 2940 GLY A N     1 
ATOM   12738 C CA    . GLY A 1 2940 ? 140.015 146.982 151.409 1.00 33.42  ? 2940 GLY A CA    1 
ATOM   12739 C C     . GLY A 1 2940 ? 138.707 146.425 151.918 1.00 33.42  ? 2940 GLY A C     1 
ATOM   12740 O O     . GLY A 1 2940 ? 138.097 145.594 151.234 1.00 33.42  ? 2940 GLY A O     1 
ATOM   12741 N N     . ALA A 1 2941 ? 138.249 146.860 153.092 1.00 33.25  ? 2941 ALA A N     1 
ATOM   12742 C CA    . ALA A 1 2941 ? 137.012 146.324 153.642 1.00 33.25  ? 2941 ALA A CA    1 
ATOM   12743 C C     . ALA A 1 2941 ? 135.791 146.808 152.869 1.00 33.25  ? 2941 ALA A C     1 
ATOM   12744 O O     . ALA A 1 2941 ? 134.760 146.128 152.862 1.00 33.25  ? 2941 ALA A O     1 
ATOM   12745 C CB    . ALA A 1 2941 ? 136.900 146.687 155.120 1.00 33.25  ? 2941 ALA A CB    1 
ATOM   12746 N N     . GLY A 1 2942 ? 135.875 147.968 152.223 1.00 35.77  ? 2942 GLY A N     1 
ATOM   12747 C CA    . GLY A 1 2942 ? 134.784 148.455 151.393 1.00 35.77  ? 2942 GLY A CA    1 
ATOM   12748 C C     . GLY A 1 2942 ? 134.233 149.820 151.757 1.00 35.77  ? 2942 GLY A C     1 
ATOM   12749 O O     . GLY A 1 2942 ? 133.061 150.088 151.456 1.00 35.77  ? 2942 GLY A O     1 
ATOM   12750 N N     . LYS A 1 2943 ? 134.999 150.700 152.405 1.00 41.08  ? 2943 LYS A N     1 
ATOM   12751 C CA    . LYS A 1 2943 ? 134.494 152.036 152.709 1.00 41.08  ? 2943 LYS A CA    1 
ATOM   12752 C C     . LYS A 1 2943 ? 134.245 152.838 151.435 1.00 41.08  ? 2943 LYS A C     1 
ATOM   12753 O O     . LYS A 1 2943 ? 133.144 153.361 151.215 1.00 41.08  ? 2943 LYS A O     1 
ATOM   12754 C CB    . LYS A 1 2943 ? 135.479 152.767 153.625 1.00 41.08  ? 2943 LYS A CB    1 
ATOM   12755 C CG    . LYS A 1 2943 ? 136.146 151.867 154.654 1.00 41.08  ? 2943 LYS A CG    1 
ATOM   12756 C CD    . LYS A 1 2943 ? 137.273 152.560 155.400 1.00 41.08  ? 2943 LYS A CD    1 
ATOM   12757 C CE    . LYS A 1 2943 ? 138.384 152.986 154.462 1.00 41.08  ? 2943 LYS A CE    1 
ATOM   12758 N NZ    . LYS A 1 2943 ? 139.518 153.609 155.200 1.00 41.08  ? 2943 LYS A NZ    1 
ATOM   12759 N N     . THR A 1 2944 ? 135.259 152.925 150.570 1.00 39.57  ? 2944 THR A N     1 
ATOM   12760 C CA    . THR A 1 2944 ? 135.135 153.723 149.354 1.00 39.57  ? 2944 THR A CA    1 
ATOM   12761 C C     . THR A 1 2944 ? 134.086 153.135 148.418 1.00 39.57  ? 2944 THR A C     1 
ATOM   12762 O O     . THR A 1 2944 ? 133.323 153.871 147.781 1.00 39.57  ? 2944 THR A O     1 
ATOM   12763 C CB    . THR A 1 2944 ? 136.489 153.825 148.650 1.00 39.57  ? 2944 THR A CB    1 
ATOM   12764 O OG1   . THR A 1 2944 ? 137.410 154.540 149.483 1.00 39.57  ? 2944 THR A OG1   1 
ATOM   12765 C CG2   . THR A 1 2944 ? 136.350 154.556 147.323 1.00 39.57  ? 2944 THR A CG2   1 
ATOM   12766 N N     . THR A 1 2945 ? 134.036 151.805 148.324 1.00 38.72  ? 2945 THR A N     1 
ATOM   12767 C CA    . THR A 1 2945 ? 133.068 151.158 147.444 1.00 38.72  ? 2945 THR A CA    1 
ATOM   12768 C C     . THR A 1 2945 ? 131.640 151.505 147.847 1.00 38.72  ? 2945 THR A C     1 
ATOM   12769 O O     . THR A 1 2945 ? 130.818 151.883 147.004 1.00 38.72  ? 2945 THR A O     1 
ATOM   12770 C CB    . THR A 1 2945 ? 133.278 149.645 147.463 1.00 38.72  ? 2945 THR A CB    1 
ATOM   12771 O OG1   . THR A 1 2945 ? 134.625 149.342 147.081 1.00 38.72  ? 2945 THR A OG1   1 
ATOM   12772 C CG2   . THR A 1 2945 ? 132.317 148.962 146.510 1.00 38.72  ? 2945 THR A CG2   1 
ATOM   12773 N N     . LEU A 1 2946 ? 131.330 151.401 149.141 1.00 41.02  ? 2946 LEU A N     1 
ATOM   12774 C CA    . LEU A 1 2946 ? 129.975 151.699 149.591 1.00 41.02  ? 2946 LEU A CA    1 
ATOM   12775 C C     . LEU A 1 2946 ? 129.674 153.189 149.494 1.00 41.02  ? 2946 LEU A C     1 
ATOM   12776 O O     . LEU A 1 2946 ? 128.536 153.580 149.202 1.00 41.02  ? 2946 LEU A O     1 
ATOM   12777 C CB    . LEU A 1 2946 ? 129.769 151.195 151.017 1.00 41.02  ? 2946 LEU A CB    1 
ATOM   12778 C CG    . LEU A 1 2946 ? 129.738 149.672 151.120 1.00 41.02  ? 2946 LEU A CG    1 
ATOM   12779 C CD1   . LEU A 1 2946 ? 129.555 149.227 152.560 1.00 41.02  ? 2946 LEU A CD1   1 
ATOM   12780 C CD2   . LEU A 1 2946 ? 128.645 149.113 150.227 1.00 41.02  ? 2946 LEU A CD2   1 
ATOM   12781 N N     . SER A 1 2947 ? 130.678 154.039 149.727 1.00 40.37  ? 2947 SER A N     1 
ATOM   12782 C CA    . SER A 1 2947 ? 130.467 155.471 149.544 1.00 40.37  ? 2947 SER A CA    1 
ATOM   12783 C C     . SER A 1 2947 ? 130.093 155.781 148.099 1.00 40.37  ? 2947 SER A C     1 
ATOM   12784 O O     . SER A 1 2947 ? 129.145 156.531 147.837 1.00 40.37  ? 2947 SER A O     1 
ATOM   12785 C CB    . SER A 1 2947 ? 131.716 156.247 149.962 1.00 40.37  ? 2947 SER A CB    1 
ATOM   12786 O OG    . SER A 1 2947 ? 132.737 156.134 148.989 1.00 40.37  ? 2947 SER A OG    1 
ATOM   12787 N N     . ARG A 1 2948 ? 130.813 155.183 147.145 1.00 43.00  ? 2948 ARG A N     1 
ATOM   12788 C CA    . ARG A 1 2948 ? 130.496 155.387 145.735 1.00 43.00  ? 2948 ARG A CA    1 
ATOM   12789 C C     . ARG A 1 2948 ? 129.123 154.829 145.390 1.00 43.00  ? 2948 ARG A C     1 
ATOM   12790 O O     . ARG A 1 2948 ? 128.381 155.424 144.603 1.00 43.00  ? 2948 ARG A O     1 
ATOM   12791 C CB    . ARG A 1 2948 ? 131.565 154.740 144.855 1.00 43.00  ? 2948 ARG A CB    1 
ATOM   12792 C CG    . ARG A 1 2948 ? 132.929 155.383 144.966 1.00 43.00  ? 2948 ARG A CG    1 
ATOM   12793 C CD    . ARG A 1 2948 ? 133.933 154.705 144.056 1.00 43.00  ? 2948 ARG A CD    1 
ATOM   12794 N NE    . ARG A 1 2948 ? 133.468 154.653 142.676 1.00 43.00  ? 2948 ARG A NE    1 
ATOM   12795 C CZ    . ARG A 1 2948 ? 134.133 154.080 141.684 1.00 43.00  ? 2948 ARG A CZ    1 
ATOM   12796 N NH1   . ARG A 1 2948 ? 135.304 153.497 141.883 1.00 43.00  ? 2948 ARG A NH1   1 
ATOM   12797 N NH2   . ARG A 1 2948 ? 133.613 154.095 140.460 1.00 43.00  ? 2948 ARG A NH2   1 
ATOM   12798 N N     . PHE A 1 2949 ? 128.773 153.678 145.963 1.00 44.21  ? 2949 PHE A N     1 
ATOM   12799 C CA    . PHE A 1 2949 ? 127.480 153.062 145.683 1.00 44.21  ? 2949 PHE A CA    1 
ATOM   12800 C C     . PHE A 1 2949 ? 126.331 153.951 146.152 1.00 44.21  ? 2949 PHE A C     1 
ATOM   12801 O O     . PHE A 1 2949 ? 125.353 154.172 145.422 1.00 44.21  ? 2949 PHE A O     1 
ATOM   12802 C CB    . PHE A 1 2949 ? 127.436 151.686 146.347 1.00 44.21  ? 2949 PHE A CB    1 
ATOM   12803 C CG    . PHE A 1 2949 ? 126.104 151.010 146.285 1.00 44.21  ? 2949 PHE A CG    1 
ATOM   12804 C CD1   . PHE A 1 2949 ? 125.418 150.904 145.092 1.00 44.21  ? 2949 PHE A CD1   1 
ATOM   12805 C CD2   . PHE A 1 2949 ? 125.564 150.431 147.417 1.00 44.21  ? 2949 PHE A CD2   1 
ATOM   12806 C CE1   . PHE A 1 2949 ? 124.200 150.266 145.037 1.00 44.21  ? 2949 PHE A CE1   1 
ATOM   12807 C CE2   . PHE A 1 2949 ? 124.350 149.787 147.367 1.00 44.21  ? 2949 PHE A CE2   1 
ATOM   12808 C CZ    . PHE A 1 2949 ? 123.672 149.698 146.173 1.00 44.21  ? 2949 PHE A CZ    1 
ATOM   12809 N N     . VAL A 1 2950 ? 126.444 154.493 147.365 1.00 42.22  ? 2950 VAL A N     1 
ATOM   12810 C CA    . VAL A 1 2950 ? 125.389 155.362 147.874 1.00 42.22  ? 2950 VAL A CA    1 
ATOM   12811 C C     . VAL A 1 2950 ? 125.358 156.673 147.100 1.00 42.22  ? 2950 VAL A C     1 
ATOM   12812 O O     . VAL A 1 2950 ? 124.284 157.229 146.838 1.00 42.22  ? 2950 VAL A O     1 
ATOM   12813 C CB    . VAL A 1 2950 ? 125.570 155.599 149.381 1.00 42.22  ? 2950 VAL A CB    1 
ATOM   12814 C CG1   . VAL A 1 2950 ? 124.540 156.594 149.881 1.00 42.22  ? 2950 VAL A CG1   1 
ATOM   12815 C CG2   . VAL A 1 2950 ? 125.480 154.293 150.135 1.00 42.22  ? 2950 VAL A CG2   1 
ATOM   12816 N N     . ALA A 1 2951 ? 126.530 157.191 146.723 1.00 44.01  ? 2951 ALA A N     1 
ATOM   12817 C CA    . ALA A 1 2951 ? 126.572 158.390 145.893 1.00 44.01  ? 2951 ALA A CA    1 
ATOM   12818 C C     . ALA A 1 2951 ? 125.871 158.155 144.563 1.00 44.01  ? 2951 ALA A C     1 
ATOM   12819 O O     . ALA A 1 2951 ? 125.193 159.049 144.042 1.00 44.01  ? 2951 ALA A O     1 
ATOM   12820 C CB    . ALA A 1 2951 ? 128.021 158.821 145.668 1.00 44.01  ? 2951 ALA A CB    1 
ATOM   12821 N N     . TRP A 1 2952 ? 126.031 156.960 143.995 1.00 50.19  ? 2952 TRP A N     1 
ATOM   12822 C CA    . TRP A 1 2952 ? 125.332 156.627 142.760 1.00 50.19  ? 2952 TRP A CA    1 
ATOM   12823 C C     . TRP A 1 2952 ? 123.827 156.578 142.981 1.00 50.19  ? 2952 TRP A C     1 
ATOM   12824 O O     . TRP A 1 2952 ? 123.052 157.057 142.145 1.00 50.19  ? 2952 TRP A O     1 
ATOM   12825 C CB    . TRP A 1 2952 ? 125.830 155.295 142.208 1.00 50.19  ? 2952 TRP A CB    1 
ATOM   12826 C CG    . TRP A 1 2952 ? 124.979 154.788 141.090 1.00 50.19  ? 2952 TRP A CG    1 
ATOM   12827 C CD1   . TRP A 1 2952 ? 124.989 155.218 139.797 1.00 50.19  ? 2952 TRP A CD1   1 
ATOM   12828 C CD2   . TRP A 1 2952 ? 123.971 153.775 141.169 1.00 50.19  ? 2952 TRP A CD2   1 
ATOM   12829 N NE1   . TRP A 1 2952 ? 124.060 154.526 139.061 1.00 50.19  ? 2952 TRP A NE1   1 
ATOM   12830 C CE2   . TRP A 1 2952 ? 123.420 153.633 139.880 1.00 50.19  ? 2952 TRP A CE2   1 
ATOM   12831 C CE3   . TRP A 1 2952 ? 123.486 152.968 142.202 1.00 50.19  ? 2952 TRP A CE3   1 
ATOM   12832 C CZ2   . TRP A 1 2952 ? 122.409 152.720 139.598 1.00 50.19  ? 2952 TRP A CZ2   1 
ATOM   12833 C CZ3   . TRP A 1 2952 ? 122.481 152.062 141.919 1.00 50.19  ? 2952 TRP A CZ3   1 
ATOM   12834 C CH2   . TRP A 1 2952 ? 121.954 151.945 140.628 1.00 50.19  ? 2952 TRP A CH2   1 
ATOM   12835 N N     . MET A 1 2953 ? 123.388 155.984 144.098 1.00 48.93  ? 2953 MET A N     1 
ATOM   12836 C CA    . MET A 1 2953 ? 121.952 155.988 144.378 1.00 48.93  ? 2953 MET A CA    1 
ATOM   12837 C C     . MET A 1 2953 ? 121.397 157.400 144.508 1.00 48.93  ? 2953 MET A C     1 
ATOM   12838 O O     . MET A 1 2953 ? 120.373 157.721 143.897 1.00 48.93  ? 2953 MET A O     1 
ATOM   12839 C CB    . MET A 1 2953 ? 121.605 155.223 145.654 1.00 48.93  ? 2953 MET A CB    1 
ATOM   12840 C CG    . MET A 1 2953 ? 121.394 153.737 145.509 1.00 48.93  ? 2953 MET A CG    1 
ATOM   12841 S SD    . MET A 1 2953 ? 120.551 153.195 147.009 1.00 48.93  ? 2953 MET A SD    1 
ATOM   12842 C CE    . MET A 1 2953 ? 121.201 151.560 147.257 1.00 48.93  ? 2953 MET A CE    1 
ATOM   12843 N N     . ASN A 1 2954 ? 122.054 158.252 145.292 1.00 43.04  ? 2954 ASN A N     1 
ATOM   12844 C CA    . ASN A 1 2954 ? 121.513 159.555 145.649 1.00 43.04  ? 2954 ASN A CA    1 
ATOM   12845 C C     . ASN A 1 2954 ? 121.872 160.634 144.634 1.00 43.04  ? 2954 ASN A C     1 
ATOM   12846 O O     . ASN A 1 2954 ? 121.663 161.822 144.902 1.00 43.04  ? 2954 ASN A O     1 
ATOM   12847 C CB    . ASN A 1 2954 ? 121.987 159.952 147.047 1.00 43.04  ? 2954 ASN A CB    1 
ATOM   12848 C CG    . ASN A 1 2954 ? 121.139 159.339 148.144 1.00 43.04  ? 2954 ASN A CG    1 
ATOM   12849 O OD1   . ASN A 1 2954 ? 120.058 159.836 148.460 1.00 43.04  ? 2954 ASN A OD1   1 
ATOM   12850 N ND2   . ASN A 1 2954 ? 121.627 158.254 148.733 1.00 43.04  ? 2954 ASN A ND2   1 
ATOM   12851 N N     . GLY A 1 2955 ? 122.397 160.247 143.478 1.00 42.30  ? 2955 GLY A N     1 
ATOM   12852 C CA    . GLY A 1 2955 ? 122.724 161.228 142.451 1.00 42.30  ? 2955 GLY A CA    1 
ATOM   12853 C C     . GLY A 1 2955 ? 123.846 162.164 142.839 1.00 42.30  ? 2955 GLY A C     1 
ATOM   12854 O O     . GLY A 1 2955 ? 123.794 163.362 142.533 1.00 42.30  ? 2955 GLY A O     1 
ATOM   12855 N N     . LEU A 1 2956 ? 124.870 161.640 143.503 1.00 44.93  ? 2956 LEU A N     1 
ATOM   12856 C CA    . LEU A 1 2956 ? 126.040 162.414 143.891 1.00 44.93  ? 2956 LEU A CA    1 
ATOM   12857 C C     . LEU A 1 2956 ? 127.173 162.153 142.911 1.00 44.93  ? 2956 LEU A C     1 
ATOM   12858 O O     . LEU A 1 2956 ? 127.527 160.997 142.658 1.00 44.93  ? 2956 LEU A O     1 
ATOM   12859 C CB    . LEU A 1 2956 ? 126.490 162.059 145.310 1.00 44.93  ? 2956 LEU A CB    1 
ATOM   12860 C CG    . LEU A 1 2956 ? 125.853 162.736 146.526 1.00 44.93  ? 2956 LEU A CG    1 
ATOM   12861 C CD1   . LEU A 1 2956 ? 126.169 164.219 146.523 1.00 44.93  ? 2956 LEU A CD1   1 
ATOM   12862 C CD2   . LEU A 1 2956 ? 124.355 162.513 146.573 1.00 44.93  ? 2956 LEU A CD2   1 
ATOM   12863 N N     . SER A 1 2957 ? 127.740 163.225 142.365 1.00 50.21  ? 2957 SER A N     1 
ATOM   12864 C CA    . SER A 1 2957 ? 128.922 163.085 141.536 1.00 50.21  ? 2957 SER A CA    1 
ATOM   12865 C C     . SER A 1 2957 ? 130.113 162.679 142.402 1.00 50.21  ? 2957 SER A C     1 
ATOM   12866 O O     . SER A 1 2957 ? 130.137 162.890 143.615 1.00 50.21  ? 2957 SER A O     1 
ATOM   12867 C CB    . SER A 1 2957 ? 129.214 164.386 140.791 1.00 50.21  ? 2957 SER A CB    1 
ATOM   12868 O OG    . SER A 1 2957 ? 128.103 164.782 140.005 1.00 50.21  ? 2957 SER A OG    1 
ATOM   12869 N N     . VAL A 1 2958 ? 131.115 162.085 141.759 1.00 48.95  ? 2958 VAL A N     1 
ATOM   12870 C CA    . VAL A 1 2958 ? 132.280 161.555 142.458 1.00 48.95  ? 2958 VAL A CA    1 
ATOM   12871 C C     . VAL A 1 2958 ? 133.516 162.286 141.959 1.00 48.95  ? 2958 VAL A C     1 
ATOM   12872 O O     . VAL A 1 2958 ? 133.776 162.319 140.752 1.00 48.95  ? 2958 VAL A O     1 
ATOM   12873 C CB    . VAL A 1 2958 ? 132.436 160.038 142.256 1.00 48.95  ? 2958 VAL A CB    1 
ATOM   12874 C CG1   . VAL A 1 2958 ? 133.856 159.602 142.573 1.00 48.95  ? 2958 VAL A CG1   1 
ATOM   12875 C CG2   . VAL A 1 2958 ? 131.440 159.288 143.126 1.00 48.95  ? 2958 VAL A CG2   1 
ATOM   12876 N N     . TYR A 1 2959 ? 134.273 162.873 142.881 1.00 58.05  ? 2959 TYR A N     1 
ATOM   12877 C CA    . TYR A 1 2959 ? 135.543 163.515 142.574 1.00 58.05  ? 2959 TYR A CA    1 
ATOM   12878 C C     . TYR A 1 2959 ? 136.612 162.917 143.477 1.00 58.05  ? 2959 TYR A C     1 
ATOM   12879 O O     . TYR A 1 2959 ? 136.484 162.958 144.705 1.00 58.05  ? 2959 TYR A O     1 
ATOM   12880 C CB    . TYR A 1 2959 ? 135.454 165.030 142.767 1.00 58.05  ? 2959 TYR A CB    1 
ATOM   12881 C CG    . TYR A 1 2959 ? 136.609 165.800 142.165 1.00 58.05  ? 2959 TYR A CG    1 
ATOM   12882 C CD1   . TYR A 1 2959 ? 136.452 166.514 140.986 1.00 58.05  ? 2959 TYR A CD1   1 
ATOM   12883 C CD2   . TYR A 1 2959 ? 137.855 165.814 142.776 1.00 58.05  ? 2959 TYR A CD2   1 
ATOM   12884 C CE1   . TYR A 1 2959 ? 137.503 167.219 140.433 1.00 58.05  ? 2959 TYR A CE1   1 
ATOM   12885 C CE2   . TYR A 1 2959 ? 138.911 166.515 142.231 1.00 58.05  ? 2959 TYR A CE2   1 
ATOM   12886 C CZ    . TYR A 1 2959 ? 138.731 167.215 141.060 1.00 58.05  ? 2959 TYR A CZ    1 
ATOM   12887 O OH    . TYR A 1 2959 ? 139.783 167.914 140.514 1.00 58.05  ? 2959 TYR A OH    1 
ATOM   12888 N N     . GLN A 1 2960 ? 137.660 162.364 142.871 1.00 60.35  ? 2960 GLN A N     1 
ATOM   12889 C CA    . GLN A 1 2960 ? 138.781 161.782 143.598 1.00 60.35  ? 2960 GLN A CA    1 
ATOM   12890 C C     . GLN A 1 2960 ? 140.069 162.414 143.092 1.00 60.35  ? 2960 GLN A C     1 
ATOM   12891 O O     . GLN A 1 2960 ? 140.346 162.383 141.889 1.00 60.35  ? 2960 GLN A O     1 
ATOM   12892 C CB    . GLN A 1 2960 ? 138.827 160.263 143.420 1.00 60.35  ? 2960 GLN A CB    1 
ATOM   12893 C CG    . GLN A 1 2960 ? 137.507 159.558 143.684 1.00 60.35  ? 2960 GLN A CG    1 
ATOM   12894 C CD    . GLN A 1 2960 ? 137.656 158.051 143.755 1.00 60.35  ? 2960 GLN A CD    1 
ATOM   12895 O OE1   . GLN A 1 2960 ? 138.757 157.518 143.625 1.00 60.35  ? 2960 GLN A OE1   1 
ATOM   12896 N NE2   . GLN A 1 2960 ? 136.544 157.355 143.962 1.00 60.35  ? 2960 GLN A NE2   1 
ATOM   12897 N N     . ILE A 1 2961 ? 140.853 162.982 144.006 1.00 71.53  ? 2961 ILE A N     1 
ATOM   12898 C CA    . ILE A 1 2961 ? 142.147 163.541 143.631 1.00 71.53  ? 2961 ILE A CA    1 
ATOM   12899 C C     . ILE A 1 2961 ? 143.140 162.401 143.453 1.00 71.53  ? 2961 ILE A C     1 
ATOM   12900 O O     . ILE A 1 2961 ? 143.353 161.594 144.365 1.00 71.53  ? 2961 ILE A O     1 
ATOM   12901 C CB    . ILE A 1 2961 ? 142.643 164.547 144.676 1.00 71.53  ? 2961 ILE A CB    1 
ATOM   12902 C CG1   . ILE A 1 2961 ? 141.794 165.818 144.652 1.00 71.53  ? 2961 ILE A CG1   1 
ATOM   12903 C CG2   . ILE A 1 2961 ? 144.104 164.884 144.436 1.00 71.53  ? 2961 ILE A CG2   1 
ATOM   12904 C CD1   . ILE A 1 2961 ? 142.294 166.888 145.599 1.00 71.53  ? 2961 ILE A CD1   1 
ATOM   12905 N N     . LYS A 1 2962 ? 143.749 162.326 142.270 1.00 71.67  ? 2962 LYS A N     1 
ATOM   12906 C CA    . LYS A 1 2962 ? 144.739 161.293 141.974 1.00 71.67  ? 2962 LYS A CA    1 
ATOM   12907 C C     . LYS A 1 2962 ? 146.123 161.862 142.278 1.00 71.67  ? 2962 LYS A C     1 
ATOM   12908 O O     . LYS A 1 2962 ? 146.848 162.338 141.402 1.00 71.67  ? 2962 LYS A O     1 
ATOM   12909 C CB    . LYS A 1 2962 ? 144.622 160.832 140.527 1.00 71.67  ? 2962 LYS A CB    1 
ATOM   12910 C CG    . LYS A 1 2962 ? 143.272 160.219 140.115 1.00 71.67  ? 2962 LYS A CG    1 
ATOM   12911 C CD    . LYS A 1 2962 ? 143.014 158.841 140.728 1.00 71.67  ? 2962 LYS A CD    1 
ATOM   12912 C CE    . LYS A 1 2962 ? 142.216 158.922 142.025 1.00 71.67  ? 2962 LYS A CE    1 
ATOM   12913 N NZ    . LYS A 1 2962 ? 141.877 157.574 142.558 1.00 71.67  ? 2962 LYS A NZ    1 
ATOM   12914 N N     . VAL A 1 2963 ? 146.490 161.819 143.561 1.00 74.86  ? 2963 VAL A N     1 
ATOM   12915 C CA    . VAL A 1 2963 ? 147.772 162.371 143.977 1.00 74.86  ? 2963 VAL A CA    1 
ATOM   12916 C C     . VAL A 1 2963 ? 148.901 161.543 143.385 1.00 74.86  ? 2963 VAL A C     1 
ATOM   12917 O O     . VAL A 1 2963 ? 148.787 160.321 143.222 1.00 74.86  ? 2963 VAL A O     1 
ATOM   12918 C CB    . VAL A 1 2963 ? 147.885 162.407 145.509 1.00 74.86  ? 2963 VAL A CB    1 
ATOM   12919 C CG1   . VAL A 1 2963 ? 146.947 163.452 146.104 1.00 74.86  ? 2963 VAL A CG1   1 
ATOM   12920 C CG2   . VAL A 1 2963 ? 147.630 161.028 146.079 1.00 74.86  ? 2963 VAL A CG2   1 
ATOM   12921 N N     . HIS A 1 2964 ? 149.995 162.214 143.046 1.00 80.36  ? 2964 HIS A N     1 
ATOM   12922 C CA    . HIS A 1 2964 ? 151.224 161.574 142.608 1.00 80.36  ? 2964 HIS A CA    1 
ATOM   12923 C C     . HIS A 1 2964 ? 152.343 161.947 143.568 1.00 80.36  ? 2964 HIS A C     1 
ATOM   12924 O O     . HIS A 1 2964 ? 152.126 162.616 144.582 1.00 80.36  ? 2964 HIS A O     1 
ATOM   12925 C CB    . HIS A 1 2964 ? 151.577 161.977 141.171 1.00 80.36  ? 2964 HIS A CB    1 
ATOM   12926 C CG    . HIS A 1 2964 ? 151.209 163.388 140.836 1.00 80.36  ? 2964 HIS A CG    1 
ATOM   12927 N ND1   . HIS A 1 2964 ? 151.808 164.477 141.430 1.00 80.36  ? 2964 HIS A ND1   1 
ATOM   12928 C CD2   . HIS A 1 2964 ? 150.285 163.887 139.981 1.00 80.36  ? 2964 HIS A CD2   1 
ATOM   12929 C CE1   . HIS A 1 2964 ? 151.276 165.587 140.948 1.00 80.36  ? 2964 HIS A CE1   1 
ATOM   12930 N NE2   . HIS A 1 2964 ? 150.349 165.256 140.067 1.00 80.36  ? 2964 HIS A NE2   1 
ATOM   12931 N N     . ARG A 1 2965 ? 153.556 161.500 143.241 1.00 82.47  ? 2965 ARG A N     1 
ATOM   12932 C CA    . ARG A 1 2965 ? 154.705 161.821 144.076 1.00 82.47  ? 2965 ARG A CA    1 
ATOM   12933 C C     . ARG A 1 2965 ? 155.027 163.308 144.060 1.00 82.47  ? 2965 ARG A C     1 
ATOM   12934 O O     . ARG A 1 2965 ? 155.643 163.809 145.007 1.00 82.47  ? 2965 ARG A O     1 
ATOM   12935 C CB    . ARG A 1 2965 ? 155.924 161.017 143.622 1.00 82.47  ? 2965 ARG A CB    1 
ATOM   12936 C CG    . ARG A 1 2965 ? 157.078 161.013 144.613 1.00 82.47  ? 2965 ARG A CG    1 
ATOM   12937 C CD    . ARG A 1 2965 ? 156.726 160.222 145.865 1.00 82.47  ? 2965 ARG A CD    1 
ATOM   12938 N NE    . ARG A 1 2965 ? 156.819 158.783 145.647 1.00 82.47  ? 2965 ARG A NE    1 
ATOM   12939 C CZ    . ARG A 1 2965 ? 157.954 158.120 145.465 1.00 82.47  ? 2965 ARG A CZ    1 
ATOM   12940 N NH1   . ARG A 1 2965 ? 159.128 158.728 145.519 1.00 82.47  ? 2965 ARG A NH1   1 
ATOM   12941 N NH2   . ARG A 1 2965 ? 157.909 156.812 145.230 1.00 82.47  ? 2965 ARG A NH2   1 
ATOM   12942 N N     . LYS A 1 2966 ? 154.614 164.026 143.019 1.00 85.39  ? 2966 LYS A N     1 
ATOM   12943 C CA    . LYS A 1 2966 ? 154.958 165.429 142.833 1.00 85.39  ? 2966 LYS A CA    1 
ATOM   12944 C C     . LYS A 1 2966 ? 153.741 166.329 143.020 1.00 85.39  ? 2966 LYS A C     1 
ATOM   12945 O O     . LYS A 1 2966 ? 153.574 167.332 142.323 1.00 85.39  ? 2966 LYS A O     1 
ATOM   12946 C CB    . LYS A 1 2966 ? 155.584 165.651 141.458 1.00 85.39  ? 2966 LYS A CB    1 
ATOM   12947 C CG    . LYS A 1 2966 ? 156.692 164.667 141.115 1.00 85.39  ? 2966 LYS A CG    1 
ATOM   12948 C CD    . LYS A 1 2966 ? 157.748 164.613 142.207 1.00 85.39  ? 2966 LYS A CD    1 
ATOM   12949 C CE    . LYS A 1 2966 ? 158.843 163.616 141.867 1.00 85.39  ? 2966 LYS A CE    1 
ATOM   12950 N NZ    . LYS A 1 2966 ? 158.299 162.253 141.613 1.00 85.39  ? 2966 LYS A NZ    1 
ATOM   12951 N N     . TYR A 1 2967 ? 152.871 165.980 143.965 1.00 83.51  ? 2967 TYR A N     1 
ATOM   12952 C CA    . TYR A 1 2967 ? 151.714 166.814 144.246 1.00 83.51  ? 2967 TYR A CA    1 
ATOM   12953 C C     . TYR A 1 2967 ? 152.131 168.036 145.064 1.00 83.51  ? 2967 TYR A C     1 
ATOM   12954 O O     . TYR A 1 2967 ? 153.259 168.138 145.554 1.00 83.51  ? 2967 TYR A O     1 
ATOM   12955 C CB    . TYR A 1 2967 ? 150.639 166.017 144.982 1.00 83.51  ? 2967 TYR A CB    1 
ATOM   12956 C CG    . TYR A 1 2967 ? 149.234 166.523 144.740 1.00 83.51  ? 2967 TYR A CG    1 
ATOM   12957 C CD1   . TYR A 1 2967 ? 148.660 166.458 143.478 1.00 83.51  ? 2967 TYR A CD1   1 
ATOM   12958 C CD2   . TYR A 1 2967 ? 148.485 167.070 145.772 1.00 83.51  ? 2967 TYR A CD2   1 
ATOM   12959 C CE1   . TYR A 1 2967 ? 147.377 166.921 143.251 1.00 83.51  ? 2967 TYR A CE1   1 
ATOM   12960 C CE2   . TYR A 1 2967 ? 147.202 167.536 145.556 1.00 83.51  ? 2967 TYR A CE2   1 
ATOM   12961 C CZ    . TYR A 1 2967 ? 146.653 167.459 144.293 1.00 83.51  ? 2967 TYR A CZ    1 
ATOM   12962 O OH    . TYR A 1 2967 ? 145.377 167.922 144.073 1.00 83.51  ? 2967 TYR A OH    1 
ATOM   12963 N N     . THR A 1 2968 ? 151.200 168.976 145.209 1.00 85.93  ? 2968 THR A N     1 
ATOM   12964 C CA    . THR A 1 2968 ? 151.479 170.212 145.925 1.00 85.93  ? 2968 THR A CA    1 
ATOM   12965 C C     . THR A 1 2968 ? 150.190 170.757 146.523 1.00 85.93  ? 2968 THR A C     1 
ATOM   12966 O O     . THR A 1 2968 ? 149.086 170.370 146.132 1.00 85.93  ? 2968 THR A O     1 
ATOM   12967 C CB    . THR A 1 2968 ? 152.131 171.258 145.011 1.00 85.93  ? 2968 THR A CB    1 
ATOM   12968 O OG1   . THR A 1 2968 ? 152.709 172.300 145.807 1.00 85.93  ? 2968 THR A OG1   1 
ATOM   12969 C CG2   . THR A 1 2968 ? 151.105 171.856 144.062 1.00 85.93  ? 2968 THR A CG2   1 
ATOM   12970 N N     . GLY A 1 2969 ? 150.352 171.664 147.490 1.00 83.28  ? 2969 GLY A N     1 
ATOM   12971 C CA    . GLY A 1 2969 ? 149.194 172.247 148.151 1.00 83.28  ? 2969 GLY A CA    1 
ATOM   12972 C C     . GLY A 1 2969 ? 148.349 173.096 147.222 1.00 83.28  ? 2969 GLY A C     1 
ATOM   12973 O O     . GLY A 1 2969 ? 147.125 173.167 147.372 1.00 83.28  ? 2969 GLY A O     1 
ATOM   12974 N N     . GLU A 1 2970 ? 148.989 173.763 146.260 1.00 89.06  ? 2970 GLU A N     1 
ATOM   12975 C CA    . GLU A 1 2970 ? 148.259 174.600 145.315 1.00 89.06  ? 2970 GLU A CA    1 
ATOM   12976 C C     . GLU A 1 2970 ? 147.272 173.773 144.500 1.00 89.06  ? 2970 GLU A C     1 
ATOM   12977 O O     . GLU A 1 2970 ? 146.126 174.180 144.286 1.00 89.06  ? 2970 GLU A O     1 
ATOM   12978 C CB    . GLU A 1 2970 ? 149.243 175.334 144.398 1.00 89.06  ? 2970 GLU A CB    1 
ATOM   12979 C CG    . GLU A 1 2970 ? 150.104 176.380 145.097 1.00 89.06  ? 2970 GLU A CG    1 
ATOM   12980 C CD    . GLU A 1 2970 ? 151.281 175.782 145.847 1.00 89.06  ? 2970 GLU A CD    1 
ATOM   12981 O OE1   . GLU A 1 2970 ? 151.456 174.546 145.802 1.00 89.06  ? 2970 GLU A OE1   1 
ATOM   12982 O OE2   . GLU A 1 2970 ? 152.033 176.550 146.483 1.00 89.06  ? 2970 GLU A OE2   1 
ATOM   12983 N N     . ASP A 1 2971 ? 147.706 172.597 144.041 1.00 82.91  ? 2971 ASP A N     1 
ATOM   12984 C CA    . ASP A 1 2971 ? 146.818 171.723 143.281 1.00 82.91  ? 2971 ASP A CA    1 
ATOM   12985 C C     . ASP A 1 2971 ? 145.645 171.256 144.134 1.00 82.91  ? 2971 ASP A C     1 
ATOM   12986 O O     . ASP A 1 2971 ? 144.503 171.201 143.664 1.00 82.91  ? 2971 ASP A O     1 
ATOM   12987 C CB    . ASP A 1 2971 ? 147.598 170.528 142.734 1.00 82.91  ? 2971 ASP A CB    1 
ATOM   12988 C CG    . ASP A 1 2971 ? 148.691 170.937 141.767 1.00 82.91  ? 2971 ASP A CG    1 
ATOM   12989 O OD1   . ASP A 1 2971 ? 148.814 172.147 141.486 1.00 82.91  ? 2971 ASP A OD1   1 
ATOM   12990 O OD2   . ASP A 1 2971 ? 149.428 170.049 141.291 1.00 82.91  ? 2971 ASP A OD2   1 
ATOM   12991 N N     . PHE A 1 2972 ? 145.911 170.908 145.396 1.00 79.67  ? 2972 PHE A N     1 
ATOM   12992 C CA    . PHE A 1 2972 ? 144.842 170.454 146.280 1.00 79.67  ? 2972 PHE A CA    1 
ATOM   12993 C C     . PHE A 1 2972 ? 143.823 171.561 146.524 1.00 79.67  ? 2972 PHE A C     1 
ATOM   12994 O O     . PHE A 1 2972 ? 142.611 171.324 146.493 1.00 79.67  ? 2972 PHE A O     1 
ATOM   12995 C CB    . PHE A 1 2972 ? 145.432 169.958 147.601 1.00 79.67  ? 2972 PHE A CB    1 
ATOM   12996 C CG    . PHE A 1 2972 ? 144.398 169.578 148.622 1.00 79.67  ? 2972 PHE A CG    1 
ATOM   12997 C CD1   . PHE A 1 2972 ? 143.685 168.399 148.497 1.00 79.67  ? 2972 PHE A CD1   1 
ATOM   12998 C CD2   . PHE A 1 2972 ? 144.147 170.393 149.711 1.00 79.67  ? 2972 PHE A CD2   1 
ATOM   12999 C CE1   . PHE A 1 2972 ? 142.735 168.045 149.435 1.00 79.67  ? 2972 PHE A CE1   1 
ATOM   13000 C CE2   . PHE A 1 2972 ? 143.201 170.040 150.654 1.00 79.67  ? 2972 PHE A CE2   1 
ATOM   13001 C CZ    . PHE A 1 2972 ? 142.493 168.867 150.515 1.00 79.67  ? 2972 PHE A CZ    1 
ATOM   13002 N N     . ASP A 1 2973 ? 144.300 172.786 146.761 1.00 85.71  ? 2973 ASP A N     1 
ATOM   13003 C CA    . ASP A 1 2973 ? 143.385 173.905 146.962 1.00 85.71  ? 2973 ASP A CA    1 
ATOM   13004 C C     . ASP A 1 2973 ? 142.600 174.213 145.692 1.00 85.71  ? 2973 ASP A C     1 
ATOM   13005 O O     . ASP A 1 2973 ? 141.410 174.550 145.753 1.00 85.71  ? 2973 ASP A O     1 
ATOM   13006 C CB    . ASP A 1 2973 ? 144.159 175.136 147.433 1.00 85.71  ? 2973 ASP A CB    1 
ATOM   13007 C CG    . ASP A 1 2973 ? 144.918 174.887 148.723 1.00 85.71  ? 2973 ASP A CG    1 
ATOM   13008 O OD1   . ASP A 1 2973 ? 144.811 173.770 149.270 1.00 85.71  ? 2973 ASP A OD1   1 
ATOM   13009 O OD2   . ASP A 1 2973 ? 145.620 175.809 149.189 1.00 85.71  ? 2973 ASP A OD2   1 
ATOM   13010 N N     . GLU A 1 2974 ? 143.249 174.104 144.530 1.00 83.99  ? 2974 GLU A N     1 
ATOM   13011 C CA    . GLU A 1 2974 ? 142.548 174.318 143.270 1.00 83.99  ? 2974 GLU A CA    1 
ATOM   13012 C C     . GLU A 1 2974 ? 141.450 173.282 143.072 1.00 83.99  ? 2974 GLU A C     1 
ATOM   13013 O O     . GLU A 1 2974 ? 140.349 173.612 142.620 1.00 83.99  ? 2974 GLU A O     1 
ATOM   13014 C CB    . GLU A 1 2974 ? 143.538 174.283 142.106 1.00 83.99  ? 2974 GLU A CB    1 
ATOM   13015 C CG    . GLU A 1 2974 ? 142.888 174.380 140.738 1.00 83.99  ? 2974 GLU A CG    1 
ATOM   13016 C CD    . GLU A 1 2974 ? 142.008 175.608 140.601 1.00 83.99  ? 2974 GLU A CD    1 
ATOM   13017 O OE1   . GLU A 1 2974 ? 142.533 176.733 140.733 1.00 83.99  ? 2974 GLU A OE1   1 
ATOM   13018 O OE2   . GLU A 1 2974 ? 140.792 175.447 140.363 1.00 83.99  ? 2974 GLU A OE2   1 
ATOM   13019 N N     . ASP A 1 2975 ? 141.731 172.022 143.410 1.00 81.56  ? 2975 ASP A N     1 
ATOM   13020 C CA    . ASP A 1 2975 ? 140.714 170.981 143.296 1.00 81.56  ? 2975 ASP A CA    1 
ATOM   13021 C C     . ASP A 1 2975 ? 139.580 171.209 144.290 1.00 81.56  ? 2975 ASP A C     1 
ATOM   13022 O O     . ASP A 1 2975 ? 138.410 170.948 143.984 1.00 81.56  ? 2975 ASP A O     1 
ATOM   13023 C CB    . ASP A 1 2975 ? 141.346 169.604 143.497 1.00 81.56  ? 2975 ASP A CB    1 
ATOM   13024 C CG    . ASP A 1 2975 ? 142.460 169.326 142.507 1.00 81.56  ? 2975 ASP A CG    1 
ATOM   13025 O OD1   . ASP A 1 2975 ? 142.698 170.177 141.624 1.00 81.56  ? 2975 ASP A OD1   1 
ATOM   13026 O OD2   . ASP A 1 2975 ? 143.099 168.258 142.612 1.00 81.56  ? 2975 ASP A OD2   1 
ATOM   13027 N N     . LEU A 1 2976 ? 139.908 171.690 145.490 1.00 81.27  ? 2976 LEU A N     1 
ATOM   13028 C CA    . LEU A 1 2976 ? 138.878 172.048 146.461 1.00 81.27  ? 2976 LEU A CA    1 
ATOM   13029 C C     . LEU A 1 2976 ? 137.953 173.112 145.890 1.00 81.27  ? 2976 LEU A C     1 
ATOM   13030 O O     . LEU A 1 2976 ? 136.727 172.978 145.952 1.00 81.27  ? 2976 LEU A O     1 
ATOM   13031 C CB    . LEU A 1 2976 ? 139.493 172.559 147.765 1.00 81.27  ? 2976 LEU A CB    1 
ATOM   13032 C CG    . LEU A 1 2976 ? 140.288 171.607 148.653 1.00 81.27  ? 2976 LEU A CG    1 
ATOM   13033 C CD1   . LEU A 1 2976 ? 140.809 172.364 149.862 1.00 81.27  ? 2976 LEU A CD1   1 
ATOM   13034 C CD2   . LEU A 1 2976 ? 139.430 170.430 149.079 1.00 81.27  ? 2976 LEU A CD2   1 
ATOM   13035 N N     . ARG A 1 2977 ? 138.539 174.174 145.333 1.00 85.77  ? 2977 ARG A N     1 
ATOM   13036 C CA    . ARG A 1 2977 ? 137.727 175.250 144.771 1.00 85.77  ? 2977 ARG A CA    1 
ATOM   13037 C C     . ARG A 1 2977 ? 136.927 174.762 143.568 1.00 85.77  ? 2977 ARG A C     1 
ATOM   13038 O O     . ARG A 1 2977 ? 135.796 175.205 143.346 1.00 85.77  ? 2977 ARG A O     1 
ATOM   13039 C CB    . ARG A 1 2977 ? 138.615 176.440 144.401 1.00 85.77  ? 2977 ARG A CB    1 
ATOM   13040 C CG    . ARG A 1 2977 ? 137.999 177.409 143.400 1.00 85.77  ? 2977 ARG A CG    1 
ATOM   13041 C CD    . ARG A 1 2977 ? 138.838 178.670 143.257 1.00 85.77  ? 2977 ARG A CD    1 
ATOM   13042 N NE    . ARG A 1 2977 ? 140.125 178.411 142.624 1.00 85.77  ? 2977 ARG A NE    1 
ATOM   13043 C CZ    . ARG A 1 2977 ? 141.299 178.606 143.210 1.00 85.77  ? 2977 ARG A CZ    1 
ATOM   13044 N NH1   . ARG A 1 2977 ? 141.386 179.060 144.449 1.00 85.77  ? 2977 ARG A NH1   1 
ATOM   13045 N NH2   . ARG A 1 2977 ? 142.413 178.337 142.535 1.00 85.77  ? 2977 ARG A NH2   1 
ATOM   13046 N N     . THR A 1 2978 ? 137.495 173.842 142.785 1.00 76.32  ? 2978 THR A N     1 
ATOM   13047 C CA    . THR A 1 2978 ? 136.769 173.266 141.658 1.00 76.32  ? 2978 THR A CA    1 
ATOM   13048 C C     . THR A 1 2978 ? 135.546 172.488 142.133 1.00 76.32  ? 2978 THR A C     1 
ATOM   13049 O O     . THR A 1 2978 ? 134.452 172.615 141.572 1.00 76.32  ? 2978 THR A O     1 
ATOM   13050 C CB    . THR A 1 2978 ? 137.700 172.363 140.846 1.00 76.32  ? 2978 THR A CB    1 
ATOM   13051 O OG1   . THR A 1 2978 ? 138.736 173.155 140.250 1.00 76.32  ? 2978 THR A OG1   1 
ATOM   13052 C CG2   . THR A 1 2978 ? 136.928 171.644 139.750 1.00 76.32  ? 2978 THR A CG2   1 
ATOM   13053 N N     . VAL A 1 2979 ? 135.715 171.680 143.178 1.00 74.50  ? 2979 VAL A N     1 
ATOM   13054 C CA    . VAL A 1 2979 ? 134.587 170.921 143.711 1.00 74.50  ? 2979 VAL A CA    1 
ATOM   13055 C C     . VAL A 1 2979 ? 133.541 171.871 144.287 1.00 74.50  ? 2979 VAL A C     1 
ATOM   13056 O O     . VAL A 1 2979 ? 132.332 171.668 144.124 1.00 74.50  ? 2979 VAL A O     1 
ATOM   13057 C CB    . VAL A 1 2979 ? 135.074 169.899 144.755 1.00 74.50  ? 2979 VAL A CB    1 
ATOM   13058 C CG1   . VAL A 1 2979 ? 133.902 169.303 145.509 1.00 74.50  ? 2979 VAL A CG1   1 
ATOM   13059 C CG2   . VAL A 1 2979 ? 135.885 168.805 144.079 1.00 74.50  ? 2979 VAL A CG2   1 
ATOM   13060 N N     . LEU A 1 2980 ? 133.995 172.937 144.952 1.00 78.02  ? 2980 LEU A N     1 
ATOM   13061 C CA    . LEU A 1 2980 ? 133.061 173.927 145.484 1.00 78.02  ? 2980 LEU A CA    1 
ATOM   13062 C C     . LEU A 1 2980 ? 132.269 174.602 144.370 1.00 78.02  ? 2980 LEU A C     1 
ATOM   13063 O O     . LEU A 1 2980 ? 131.051 174.777 144.487 1.00 78.02  ? 2980 LEU A O     1 
ATOM   13064 C CB    . LEU A 1 2980 ? 133.808 174.972 146.314 1.00 78.02  ? 2980 LEU A CB    1 
ATOM   13065 C CG    . LEU A 1 2980 ? 134.545 174.515 147.574 1.00 78.02  ? 2980 LEU A CG    1 
ATOM   13066 C CD1   . LEU A 1 2980 ? 135.410 175.639 148.122 1.00 78.02  ? 2980 LEU A CD1   1 
ATOM   13067 C CD2   . LEU A 1 2980 ? 133.563 174.042 148.627 1.00 78.02  ? 2980 LEU A CD2   1 
ATOM   13068 N N     . ARG A 1 2981 ? 132.941 174.994 143.283 1.00 76.05  ? 2981 ARG A N     1 
ATOM   13069 C CA    . ARG A 1 2981 ? 132.242 175.668 142.193 1.00 76.05  ? 2981 ARG A CA    1 
ATOM   13070 C C     . ARG A 1 2981 ? 131.273 174.719 141.498 1.00 76.05  ? 2981 ARG A C     1 
ATOM   13071 O O     . ARG A 1 2981 ? 130.192 175.133 141.064 1.00 76.05  ? 2981 ARG A O     1 
ATOM   13072 C CB    . ARG A 1 2981 ? 133.241 176.271 141.198 1.00 76.05  ? 2981 ARG A CB    1 
ATOM   13073 C CG    . ARG A 1 2981 ? 133.929 175.276 140.282 1.00 76.05  ? 2981 ARG A CG    1 
ATOM   13074 C CD    . ARG A 1 2981 ? 135.229 175.815 139.707 1.00 76.05  ? 2981 ARG A CD    1 
ATOM   13075 N NE    . ARG A 1 2981 ? 135.082 177.137 139.114 1.00 76.05  ? 2981 ARG A NE    1 
ATOM   13076 C CZ    . ARG A 1 2981 ? 135.802 177.579 138.092 1.00 76.05  ? 2981 ARG A CZ    1 
ATOM   13077 N NH1   . ARG A 1 2981 ? 136.728 176.825 137.522 1.00 76.05  ? 2981 ARG A NH1   1 
ATOM   13078 N NH2   . ARG A 1 2981 ? 135.588 178.807 137.630 1.00 76.05  ? 2981 ARG A NH2   1 
ATOM   13079 N N     . ARG A 1 2982 ? 131.635 173.439 141.384 1.00 70.14  ? 2982 ARG A N     1 
ATOM   13080 C CA    . ARG A 1 2982 ? 130.674 172.455 140.905 1.00 70.14  ? 2982 ARG A CA    1 
ATOM   13081 C C     . ARG A 1 2982 ? 129.537 172.221 141.889 1.00 70.14  ? 2982 ARG A C     1 
ATOM   13082 O O     . ARG A 1 2982 ? 128.477 171.735 141.481 1.00 70.14  ? 2982 ARG A O     1 
ATOM   13083 C CB    . ARG A 1 2982 ? 131.372 171.128 140.596 1.00 70.14  ? 2982 ARG A CB    1 
ATOM   13084 C CG    . ARG A 1 2982 ? 132.501 171.241 139.586 1.00 70.14  ? 2982 ARG A CG    1 
ATOM   13085 C CD    . ARG A 1 2982 ? 132.122 170.600 138.262 1.00 70.14  ? 2982 ARG A CD    1 
ATOM   13086 N NE    . ARG A 1 2982 ? 132.252 169.149 138.300 1.00 70.14  ? 2982 ARG A NE    1 
ATOM   13087 C CZ    . ARG A 1 2982 ? 133.400 168.495 138.178 1.00 70.14  ? 2982 ARG A CZ    1 
ATOM   13088 N NH1   . ARG A 1 2982 ? 134.544 169.135 138.003 1.00 70.14  ? 2982 ARG A NH1   1 
ATOM   13089 N NH2   . ARG A 1 2982 ? 133.399 167.167 138.233 1.00 70.14  ? 2982 ARG A NH2   1 
ATOM   13090 N N     . SER A 1 2983 ? 129.728 172.552 143.168 1.00 70.91  ? 2983 SER A N     1 
ATOM   13091 C CA    . SER A 1 2983 ? 128.669 172.445 144.161 1.00 70.91  ? 2983 SER A CA    1 
ATOM   13092 C C     . SER A 1 2983 ? 128.029 173.777 144.523 1.00 70.91  ? 2983 SER A C     1 
ATOM   13093 O O     . SER A 1 2983 ? 126.862 173.788 144.925 1.00 70.91  ? 2983 SER A O     1 
ATOM   13094 C CB    . SER A 1 2983 ? 129.203 171.788 145.444 1.00 70.91  ? 2983 SER A CB    1 
ATOM   13095 O OG    . SER A 1 2983 ? 128.231 171.815 146.473 1.00 70.91  ? 2983 SER A OG    1 
ATOM   13096 N N     . GLY A 1 2984 ? 128.754 174.887 144.400 1.00 76.33  ? 2984 GLY A N     1 
ATOM   13097 C CA    . GLY A 1 2984 ? 128.199 176.190 144.714 1.00 76.33  ? 2984 GLY A CA    1 
ATOM   13098 C C     . GLY A 1 2984 ? 127.705 176.960 143.506 1.00 76.33  ? 2984 GLY A C     1 
ATOM   13099 O O     . GLY A 1 2984 ? 126.570 177.444 143.495 1.00 76.33  ? 2984 GLY A O     1 
ATOM   13100 N N     . CYS A 1 2985 ? 128.550 177.079 142.477 1.00 82.85  ? 2985 CYS A N     1 
ATOM   13101 C CA    . CYS A 1 2985 ? 128.137 177.781 141.265 1.00 82.85  ? 2985 CYS A CA    1 
ATOM   13102 C C     . CYS A 1 2985 ? 127.092 176.980 140.501 1.00 82.85  ? 2985 CYS A C     1 
ATOM   13103 O O     . CYS A 1 2985 ? 126.187 177.553 139.883 1.00 82.85  ? 2985 CYS A O     1 
ATOM   13104 C CB    . CYS A 1 2985 ? 129.351 178.067 140.381 1.00 82.85  ? 2985 CYS A CB    1 
ATOM   13105 S SG    . CYS A 1 2985 ? 130.609 179.110 141.150 1.00 82.85  ? 2985 CYS A SG    1 
ATOM   13106 N N     . LYS A 1 2986 ? 127.205 175.656 140.528 1.00 72.33  ? 2986 LYS A N     1 
ATOM   13107 C CA    . LYS A 1 2986 ? 126.213 174.760 139.955 1.00 72.33  ? 2986 LYS A CA    1 
ATOM   13108 C C     . LYS A 1 2986 ? 125.542 173.989 141.081 1.00 72.33  ? 2986 LYS A C     1 
ATOM   13109 O O     . LYS A 1 2986 ? 126.205 173.559 142.030 1.00 72.33  ? 2986 LYS A O     1 
ATOM   13110 C CB    . LYS A 1 2986 ? 126.846 173.783 138.957 1.00 72.33  ? 2986 LYS A CB    1 
ATOM   13111 C CG    . LYS A 1 2986 ? 126.883 174.283 137.522 1.00 72.33  ? 2986 LYS A CG    1 
ATOM   13112 C CD    . LYS A 1 2986 ? 127.899 175.399 137.344 1.00 72.33  ? 2986 LYS A CD    1 
ATOM   13113 C CE    . LYS A 1 2986 ? 129.319 174.871 137.471 1.00 72.33  ? 2986 LYS A CE    1 
ATOM   13114 N NZ    . LYS A 1 2986 ? 130.333 175.936 137.243 1.00 72.33  ? 2986 LYS A NZ    1 
ATOM   13115 N N     . ASN A 1 2987 ? 124.225 173.817 140.977 1.00 67.77  ? 2987 ASN A N     1 
ATOM   13116 C CA    . ASN A 1 2987 ? 123.487 173.101 142.011 1.00 67.77  ? 2987 ASN A CA    1 
ATOM   13117 C C     . ASN A 1 2987 ? 123.787 171.607 142.030 1.00 67.77  ? 2987 ASN A C     1 
ATOM   13118 O O     . ASN A 1 2987 ? 123.200 170.891 142.848 1.00 67.77  ? 2987 ASN A O     1 
ATOM   13119 C CB    . ASN A 1 2987 ? 121.984 173.327 141.837 1.00 67.77  ? 2987 ASN A CB    1 
ATOM   13120 C CG    . ASN A 1 2987 ? 121.213 173.141 143.130 1.00 67.77  ? 2987 ASN A CG    1 
ATOM   13121 O OD1   . ASN A 1 2987 ? 121.419 173.870 144.100 1.00 67.77  ? 2987 ASN A OD1   1 
ATOM   13122 N ND2   . ASN A 1 2987 ? 120.318 172.160 143.150 1.00 67.77  ? 2987 ASN A ND2   1 
ATOM   13123 N N     . GLU A 1 2988 ? 124.670 171.124 141.156 1.00 63.08  ? 2988 GLU A N     1 
ATOM   13124 C CA    . GLU A 1 2988 ? 125.047 169.718 141.164 1.00 63.08  ? 2988 GLU A CA    1 
ATOM   13125 C C     . GLU A 1 2988 ? 125.685 169.344 142.496 1.00 63.08  ? 2988 GLU A C     1 
ATOM   13126 O O     . GLU A 1 2988 ? 126.562 170.047 143.004 1.00 63.08  ? 2988 GLU A O     1 
ATOM   13127 C CB    . GLU A 1 2988 ? 126.015 169.424 140.017 1.00 63.08  ? 2988 GLU A CB    1 
ATOM   13128 C CG    . GLU A 1 2988 ? 126.672 168.056 140.097 1.00 63.08  ? 2988 GLU A CG    1 
ATOM   13129 C CD    . GLU A 1 2988 ? 127.596 167.782 138.929 1.00 63.08  ? 2988 GLU A CD    1 
ATOM   13130 O OE1   . GLU A 1 2988 ? 128.522 168.589 138.701 1.00 63.08  ? 2988 GLU A OE1   1 
ATOM   13131 O OE2   . GLU A 1 2988 ? 127.399 166.758 138.243 1.00 63.08  ? 2988 GLU A OE2   1 
ATOM   13132 N N     . LYS A 1 2989 ? 125.237 168.225 143.057 1.00 54.53  ? 2989 LYS A N     1 
ATOM   13133 C CA    . LYS A 1 2989 ? 125.710 167.755 144.354 1.00 54.53  ? 2989 LYS A CA    1 
ATOM   13134 C C     . LYS A 1 2989 ? 126.934 166.871 144.137 1.00 54.53  ? 2989 LYS A C     1 
ATOM   13135 O O     . LYS A 1 2989 ? 126.856 165.848 143.451 1.00 54.53  ? 2989 LYS A O     1 
ATOM   13136 C CB    . LYS A 1 2989 ? 124.601 167.002 145.082 1.00 54.53  ? 2989 LYS A CB    1 
ATOM   13137 C CG    . LYS A 1 2989 ? 123.309 167.786 145.223 1.00 54.53  ? 2989 LYS A CG    1 
ATOM   13138 C CD    . LYS A 1 2989 ? 122.222 166.947 145.877 1.00 54.53  ? 2989 LYS A CD    1 
ATOM   13139 C CE    . LYS A 1 2989 ? 122.644 166.457 147.253 1.00 54.53  ? 2989 LYS A CE    1 
ATOM   13140 N NZ    . LYS A 1 2989 ? 122.955 167.580 148.177 1.00 54.53  ? 2989 LYS A NZ    1 
ATOM   13141 N N     . ILE A 1 2990 ? 128.061 167.267 144.720 1.00 52.29  ? 2990 ILE A N     1 
ATOM   13142 C CA    . ILE A 1 2990 ? 129.308 166.533 144.568 1.00 52.29  ? 2990 ILE A CA    1 
ATOM   13143 C C     . ILE A 1 2990 ? 129.567 165.713 145.827 1.00 52.29  ? 2990 ILE A C     1 
ATOM   13144 O O     . ILE A 1 2990 ? 129.122 166.052 146.926 1.00 52.29  ? 2990 ILE A O     1 
ATOM   13145 C CB    . ILE A 1 2990 ? 130.486 167.484 144.270 1.00 52.29  ? 2990 ILE A CB    1 
ATOM   13146 C CG1   . ILE A 1 2990 ? 130.077 168.530 143.235 1.00 52.29  ? 2990 ILE A CG1   1 
ATOM   13147 C CG2   . ILE A 1 2990 ? 131.694 166.712 143.764 1.00 52.29  ? 2990 ILE A CG2   1 
ATOM   13148 C CD1   . ILE A 1 2990 ? 129.821 167.956 141.863 1.00 52.29  ? 2990 ILE A CD1   1 
ATOM   13149 N N     . ALA A 1 2991 ? 130.294 164.605 145.658 1.00 52.47  ? 2991 ALA A N     1 
ATOM   13150 C CA    . ALA A 1 2991 ? 130.745 163.761 146.766 1.00 52.47  ? 2991 ALA A CA    1 
ATOM   13151 C C     . ALA A 1 2991 ? 132.249 163.561 146.596 1.00 52.47  ? 2991 ALA A C     1 
ATOM   13152 O O     . ALA A 1 2991 ? 132.697 162.630 145.924 1.00 52.47  ? 2991 ALA A O     1 
ATOM   13153 C CB    . ALA A 1 2991 ? 129.988 162.436 146.801 1.00 52.47  ? 2991 ALA A CB    1 
ATOM   13154 N N     . PHE A 1 2992 ? 133.028 164.450 147.207 1.00 56.45  ? 2992 PHE A N     1 
ATOM   13155 C CA    . PHE A 1 2992 ? 134.480 164.373 147.119 1.00 56.45  ? 2992 PHE A CA    1 
ATOM   13156 C C     . PHE A 1 2992 ? 134.990 163.157 147.882 1.00 56.45  ? 2992 PHE A C     1 
ATOM   13157 O O     . PHE A 1 2992 ? 134.726 163.005 149.077 1.00 56.45  ? 2992 PHE A O     1 
ATOM   13158 C CB    . PHE A 1 2992 ? 135.098 165.652 147.688 1.00 56.45  ? 2992 PHE A CB    1 
ATOM   13159 C CG    . PHE A 1 2992 ? 136.575 165.779 147.449 1.00 56.45  ? 2992 PHE A CG    1 
ATOM   13160 C CD1   . PHE A 1 2992 ? 137.059 166.224 146.233 1.00 56.45  ? 2992 PHE A CD1   1 
ATOM   13161 C CD2   . PHE A 1 2992 ? 137.481 165.445 148.438 1.00 56.45  ? 2992 PHE A CD2   1 
ATOM   13162 C CE1   . PHE A 1 2992 ? 138.416 166.344 146.020 1.00 56.45  ? 2992 PHE A CE1   1 
ATOM   13163 C CE2   . PHE A 1 2992 ? 138.834 165.561 148.228 1.00 56.45  ? 2992 PHE A CE2   1 
ATOM   13164 C CZ    . PHE A 1 2992 ? 139.301 166.009 147.020 1.00 56.45  ? 2992 PHE A CZ    1 
ATOM   13165 N N     . ILE A 1 2993 ? 135.732 162.296 147.187 1.00 56.61  ? 2993 ILE A N     1 
ATOM   13166 C CA    . ILE A 1 2993 ? 136.234 161.064 147.788 1.00 56.61  ? 2993 ILE A CA    1 
ATOM   13167 C C     . ILE A 1 2993 ? 137.751 161.128 147.901 1.00 56.61  ? 2993 ILE A C     1 
ATOM   13168 O O     . ILE A 1 2993 ? 138.460 161.202 146.892 1.00 56.61  ? 2993 ILE A O     1 
ATOM   13169 C CB    . ILE A 1 2993 ? 135.797 159.828 146.983 1.00 56.61  ? 2993 ILE A CB    1 
ATOM   13170 C CG1   . ILE A 1 2993 ? 134.275 159.701 146.992 1.00 56.61  ? 2993 ILE A CG1   1 
ATOM   13171 C CG2   . ILE A 1 2993 ? 136.435 158.572 147.547 1.00 56.61  ? 2993 ILE A CG2   1 
ATOM   13172 C CD1   . ILE A 1 2993 ? 133.744 158.681 146.030 1.00 56.61  ? 2993 ILE A CD1   1 
ATOM   13173 N N     . MET A 1 2994 ? 138.252 161.102 149.130 1.00 67.24  ? 2994 MET A N     1 
ATOM   13174 C CA    . MET A 1 2994 ? 139.677 161.175 149.402 1.00 67.24  ? 2994 MET A CA    1 
ATOM   13175 C C     . MET A 1 2994 ? 140.059 160.168 150.487 1.00 67.24  ? 2994 MET A C     1 
ATOM   13176 O O     . MET A 1 2994 ? 139.235 159.759 151.306 1.00 67.24  ? 2994 MET A O     1 
ATOM   13177 C CB    . MET A 1 2994 ? 140.050 162.601 149.811 1.00 67.24  ? 2994 MET A CB    1 
ATOM   13178 C CG    . MET A 1 2994 ? 141.509 162.949 149.635 1.00 67.24  ? 2994 MET A CG    1 
ATOM   13179 S SD    . MET A 1 2994 ? 141.851 164.714 149.710 1.00 67.24  ? 2994 MET A SD    1 
ATOM   13180 C CE    . MET A 1 2994 ? 141.206 165.118 151.329 1.00 67.24  ? 2994 MET A CE    1 
ATOM   13181 N N     . ASP A 1 2995 ? 141.328 159.757 150.487 1.00 70.64  ? 2995 ASP A N     1 
ATOM   13182 C CA    . ASP A 1 2995 ? 141.826 158.845 151.508 1.00 70.64  ? 2995 ASP A CA    1 
ATOM   13183 C C     . ASP A 1 2995 ? 143.070 159.434 152.158 1.00 70.64  ? 2995 ASP A C     1 
ATOM   13184 O O     . ASP A 1 2995 ? 143.599 160.460 151.723 1.00 70.64  ? 2995 ASP A O     1 
ATOM   13185 C CB    . ASP A 1 2995 ? 142.123 157.440 150.947 1.00 70.64  ? 2995 ASP A CB    1 
ATOM   13186 C CG    . ASP A 1 2995 ? 143.223 157.433 149.899 1.00 70.64  ? 2995 ASP A CG    1 
ATOM   13187 O OD1   . ASP A 1 2995 ? 143.735 158.510 149.547 1.00 70.64  ? 2995 ASP A OD1   1 
ATOM   13188 O OD2   . ASP A 1 2995 ? 143.585 156.334 149.428 1.00 70.64  ? 2995 ASP A OD2   1 
ATOM   13189 N N     . GLU A 1 2996 ? 143.528 158.764 153.220 1.00 67.09  ? 2996 GLU A N     1 
ATOM   13190 C CA    . GLU A 1 2996 ? 144.719 159.215 153.933 1.00 67.09  ? 2996 GLU A CA    1 
ATOM   13191 C C     . GLU A 1 2996 ? 145.935 159.244 153.015 1.00 67.09  ? 2996 GLU A C     1 
ATOM   13192 O O     . GLU A 1 2996 ? 146.885 160.000 153.250 1.00 67.09  ? 2996 GLU A O     1 
ATOM   13193 C CB    . GLU A 1 2996 ? 144.975 158.313 155.142 1.00 67.09  ? 2996 GLU A CB    1 
ATOM   13194 C CG    . GLU A 1 2996 ? 146.148 158.741 156.007 1.00 67.09  ? 2996 GLU A CG    1 
ATOM   13195 C CD    . GLU A 1 2996 ? 146.339 157.853 157.219 1.00 67.09  ? 2996 GLU A CD    1 
ATOM   13196 O OE1   . GLU A 1 2996 ? 145.567 156.883 157.380 1.00 67.09  ? 2996 GLU A OE1   1 
ATOM   13197 O OE2   . GLU A 1 2996 ? 147.264 158.125 158.013 1.00 67.09  ? 2996 GLU A OE2   1 
ATOM   13198 N N     . SER A 1 2997 ? 145.918 158.432 151.956 1.00 69.53  ? 2997 SER A N     1 
ATOM   13199 C CA    . SER A 1 2997 ? 147.020 158.434 151.001 1.00 69.53  ? 2997 SER A CA    1 
ATOM   13200 C C     . SER A 1 2997 ? 147.139 159.778 150.289 1.00 69.53  ? 2997 SER A C     1 
ATOM   13201 O O     . SER A 1 2997 ? 148.251 160.252 150.030 1.00 69.53  ? 2997 SER A O     1 
ATOM   13202 C CB    . SER A 1 2997 ? 146.844 157.299 149.991 1.00 69.53  ? 2997 SER A CB    1 
ATOM   13203 O OG    . SER A 1 2997 ? 146.634 156.057 150.642 1.00 69.53  ? 2997 SER A OG    1 
ATOM   13204 N N     . ASN A 1 2998 ? 146.007 160.410 149.960 1.00 75.49  ? 2998 ASN A N     1 
ATOM   13205 C CA    . ASN A 1 2998 ? 146.065 161.672 149.224 1.00 75.49  ? 2998 ASN A CA    1 
ATOM   13206 C C     . ASN A 1 2998 ? 146.599 162.804 150.094 1.00 75.49  ? 2998 ASN A C     1 
ATOM   13207 O O     . ASN A 1 2998 ? 147.256 163.725 149.591 1.00 75.49  ? 2998 ASN A O     1 
ATOM   13208 C CB    . ASN A 1 2998 ? 144.690 162.044 148.668 1.00 75.49  ? 2998 ASN A CB    1 
ATOM   13209 C CG    . ASN A 1 2998 ? 144.015 160.900 147.935 1.00 75.49  ? 2998 ASN A CG    1 
ATOM   13210 O OD1   . ASN A 1 2998 ? 142.832 160.631 148.142 1.00 75.49  ? 2998 ASN A OD1   1 
ATOM   13211 N ND2   . ASN A 1 2998 ? 144.763 160.213 147.088 1.00 75.49  ? 2998 ASN A ND2   1 
ATOM   13212 N N     . VAL A 1 2999 ? 146.323 162.763 151.393 1.00 75.24  ? 2999 VAL A N     1 
ATOM   13213 C CA    . VAL A 1 2999 ? 146.776 163.810 152.303 1.00 75.24  ? 2999 VAL A CA    1 
ATOM   13214 C C     . VAL A 1 2999 ? 148.212 163.537 152.725 1.00 75.24  ? 2999 VAL A C     1 
ATOM   13215 O O     . VAL A 1 2999 ? 148.532 162.454 153.228 1.00 75.24  ? 2999 VAL A O     1 
ATOM   13216 C CB    . VAL A 1 2999 ? 145.851 163.910 153.525 1.00 75.24  ? 2999 VAL A CB    1 
ATOM   13217 C CG1   . VAL A 1 2999 ? 146.400 164.923 154.512 1.00 75.24  ? 2999 VAL A CG1   1 
ATOM   13218 C CG2   . VAL A 1 2999 ? 144.464 164.322 153.083 1.00 75.24  ? 2999 VAL A CG2   1 
ATOM   13219 N N     . LEU A 1 3000 ? 149.078 164.531 152.534 1.00 77.45  ? 3000 LEU A N     1 
ATOM   13220 C CA    . LEU A 1 3000 ? 150.482 164.421 152.906 1.00 77.45  ? 3000 LEU A CA    1 
ATOM   13221 C C     . LEU A 1 3000 ? 150.817 165.373 154.047 1.00 77.45  ? 3000 LEU A C     1 
ATOM   13222 O O     . LEU A 1 3000 ? 151.359 164.954 155.075 1.00 77.45  ? 3000 LEU A O     1 
ATOM   13223 C CB    . LEU A 1 3000 ? 151.373 164.707 151.695 1.00 77.45  ? 3000 LEU A CB    1 
ATOM   13224 C CG    . LEU A 1 3000 ? 152.886 164.581 151.877 1.00 77.45  ? 3000 LEU A CG    1 
ATOM   13225 C CD1   . LEU A 1 3000 ? 153.267 163.153 152.228 1.00 77.45  ? 3000 LEU A CD1   1 
ATOM   13226 C CD2   . LEU A 1 3000 ? 153.622 165.049 150.628 1.00 77.45  ? 3000 LEU A CD2   1 
ATOM   13227 N N     . ASP A 1 3001 ? 150.502 166.655 153.877 1.00 73.55  ? 3001 ASP A N     1 
ATOM   13228 C CA    . ASP A 1 3001 ? 150.820 167.645 154.895 1.00 73.55  ? 3001 ASP A CA    1 
ATOM   13229 C C     . ASP A 1 3001 ? 149.562 168.118 155.617 1.00 73.55  ? 3001 ASP A C     1 
ATOM   13230 O O     . ASP A 1 3001 ? 148.434 167.854 155.190 1.00 73.55  ? 3001 ASP A O     1 
ATOM   13231 C CB    . ASP A 1 3001 ? 151.563 168.832 154.273 1.00 73.55  ? 3001 ASP A CB    1 
ATOM   13232 C CG    . ASP A 1 3001 ? 150.681 169.685 153.368 1.00 73.55  ? 3001 ASP A CG    1 
ATOM   13233 O OD1   . ASP A 1 3001 ? 149.557 169.261 153.026 1.00 73.55  ? 3001 ASP A OD1   1 
ATOM   13234 O OD2   . ASP A 1 3001 ? 151.120 170.792 152.993 1.00 73.55  ? 3001 ASP A OD2   1 
ATOM   13235 N N     . SER A 1 3002 ? 149.769 168.825 156.731 1.00 68.37  ? 3002 SER A N     1 
ATOM   13236 C CA    . SER A 1 3002 ? 148.648 169.392 157.471 1.00 68.37  ? 3002 SER A CA    1 
ATOM   13237 C C     . SER A 1 3002 ? 147.979 170.534 156.720 1.00 68.37  ? 3002 SER A C     1 
ATOM   13238 O O     . SER A 1 3002 ? 146.890 170.961 157.115 1.00 68.37  ? 3002 SER A O     1 
ATOM   13239 C CB    . SER A 1 3002 ? 149.110 169.873 158.848 1.00 68.37  ? 3002 SER A CB    1 
ATOM   13240 O OG    . SER A 1 3002 ? 149.133 168.804 159.777 1.00 68.37  ? 3002 SER A OG    1 
ATOM   13241 N N     . GLY A 1 3003 ? 148.608 171.046 155.660 1.00 69.89  ? 3003 GLY A N     1 
ATOM   13242 C CA    . GLY A 1 3003 ? 147.940 172.022 154.818 1.00 69.89  ? 3003 GLY A CA    1 
ATOM   13243 C C     . GLY A 1 3003 ? 146.725 171.451 154.118 1.00 69.89  ? 3003 GLY A C     1 
ATOM   13244 O O     . GLY A 1 3003 ? 145.722 172.147 153.937 1.00 69.89  ? 3003 GLY A O     1 
ATOM   13245 N N     . PHE A 1 3004 ? 146.795 170.180 153.714 1.00 73.56  ? 3004 PHE A N     1 
ATOM   13246 C CA    . PHE A 1 3004 ? 145.620 169.514 153.162 1.00 73.56  ? 3004 PHE A CA    1 
ATOM   13247 C C     . PHE A 1 3004 ? 144.534 169.347 154.215 1.00 73.56  ? 3004 PHE A C     1 
ATOM   13248 O O     . PHE A 1 3004 ? 143.365 169.138 153.873 1.00 73.56  ? 3004 PHE A O     1 
ATOM   13249 C CB    . PHE A 1 3004 ? 146.003 168.153 152.579 1.00 73.56  ? 3004 PHE A CB    1 
ATOM   13250 C CG    . PHE A 1 3004 ? 147.078 168.218 151.530 1.00 73.56  ? 3004 PHE A CG    1 
ATOM   13251 C CD1   . PHE A 1 3004 ? 147.220 169.335 150.727 1.00 73.56  ? 3004 PHE A CD1   1 
ATOM   13252 C CD2   . PHE A 1 3004 ? 147.941 167.154 151.343 1.00 73.56  ? 3004 PHE A CD2   1 
ATOM   13253 C CE1   . PHE A 1 3004 ? 148.206 169.390 149.763 1.00 73.56  ? 3004 PHE A CE1   1 
ATOM   13254 C CE2   . PHE A 1 3004 ? 148.930 167.203 150.380 1.00 73.56  ? 3004 PHE A CE2   1 
ATOM   13255 C CZ    . PHE A 1 3004 ? 149.063 168.323 149.589 1.00 73.56  ? 3004 PHE A CZ    1 
ATOM   13256 N N     . LEU A 1 3005 ? 144.898 169.428 155.491 1.00 71.43  ? 3005 LEU A N     1 
ATOM   13257 C CA    . LEU A 1 3005 ? 143.955 169.330 156.591 1.00 71.43  ? 3005 LEU A CA    1 
ATOM   13258 C C     . LEU A 1 3005 ? 143.668 170.725 157.146 1.00 71.43  ? 3005 LEU A C     1 
ATOM   13259 O O     . LEU A 1 3005 ? 144.329 171.709 156.791 1.00 71.43  ? 3005 LEU A O     1 
ATOM   13260 C CB    . LEU A 1 3005 ? 144.494 168.379 157.664 1.00 71.43  ? 3005 LEU A CB    1 
ATOM   13261 C CG    . LEU A 1 3005 ? 143.448 167.770 158.601 1.00 71.43  ? 3005 LEU A CG    1 
ATOM   13262 C CD1   . LEU A 1 3005 ? 142.670 166.682 157.880 1.00 71.43  ? 3005 LEU A CD1   1 
ATOM   13263 C CD2   . LEU A 1 3005 ? 144.095 167.226 159.864 1.00 71.43  ? 3005 LEU A CD2   1 
ATOM   13264 N N     . GLU A 1 3006 ? 142.626 170.807 157.974 1.00 67.89  ? 3006 GLU A N     1 
ATOM   13265 C CA    . GLU A 1 3006 ? 142.094 172.019 158.594 1.00 67.89  ? 3006 GLU A CA    1 
ATOM   13266 C C     . GLU A 1 3006 ? 141.411 172.887 157.544 1.00 67.89  ? 3006 GLU A C     1 
ATOM   13267 O O     . GLU A 1 3006 ? 140.495 173.653 157.866 1.00 67.89  ? 3006 GLU A O     1 
ATOM   13268 C CB    . GLU A 1 3006 ? 143.201 172.805 159.306 1.00 67.89  ? 3006 GLU A CB    1 
ATOM   13269 C CG    . GLU A 1 3006 ? 142.735 173.645 160.483 1.00 67.89  ? 3006 GLU A CG    1 
ATOM   13270 C CD    . GLU A 1 3006 ? 142.337 172.803 161.678 1.00 67.89  ? 3006 GLU A CD    1 
ATOM   13271 O OE1   . GLU A 1 3006 ? 143.173 172.002 162.145 1.00 67.89  ? 3006 GLU A OE1   1 
ATOM   13272 O OE2   . GLU A 1 3006 ? 141.193 172.948 162.157 1.00 67.89  ? 3006 GLU A OE2   1 
ATOM   13273 N N     . ARG A 1 3007 ? 141.738 172.643 156.271 1.00 69.41  ? 3007 ARG A N     1 
ATOM   13274 C CA    . ARG A 1 3007 ? 140.927 173.154 155.177 1.00 69.41  ? 3007 ARG A CA    1 
ATOM   13275 C C     . ARG A 1 3007 ? 139.629 172.380 155.112 1.00 69.41  ? 3007 ARG A C     1 
ATOM   13276 O O     . ARG A 1 3007 ? 138.585 172.928 154.740 1.00 69.41  ? 3007 ARG A O     1 
ATOM   13277 C CB    . ARG A 1 3007 ? 141.687 173.045 153.854 1.00 69.41  ? 3007 ARG A CB    1 
ATOM   13278 C CG    . ARG A 1 3007 ? 142.788 174.077 153.672 1.00 69.41  ? 3007 ARG A CG    1 
ATOM   13279 C CD    . ARG A 1 3007 ? 142.282 175.292 152.914 1.00 69.41  ? 3007 ARG A CD    1 
ATOM   13280 N NE    . ARG A 1 3007 ? 143.369 176.155 152.467 1.00 69.41  ? 3007 ARG A NE    1 
ATOM   13281 C CZ    . ARG A 1 3007 ? 143.455 177.451 152.734 1.00 69.41  ? 3007 ARG A CZ    1 
ATOM   13282 N NH1   . ARG A 1 3007 ? 142.533 178.073 153.451 1.00 69.41  ? 3007 ARG A NH1   1 
ATOM   13283 N NH2   . ARG A 1 3007 ? 144.492 178.142 152.269 1.00 69.41  ? 3007 ARG A NH2   1 
ATOM   13284 N N     . MET A 1 3008 ? 139.682 171.098 155.466 1.00 69.51  ? 3008 MET A N     1 
ATOM   13285 C CA    . MET A 1 3008 ? 138.485 170.355 155.817 1.00 69.51  ? 3008 MET A CA    1 
ATOM   13286 C C     . MET A 1 3008 ? 137.777 171.002 156.999 1.00 69.51  ? 3008 MET A C     1 
ATOM   13287 O O     . MET A 1 3008 ? 136.679 171.528 156.833 1.00 69.51  ? 3008 MET A O     1 
ATOM   13288 C CB    . MET A 1 3008 ? 138.836 168.898 156.133 1.00 69.51  ? 3008 MET A CB    1 
ATOM   13289 C CG    . MET A 1 3008 ? 139.373 168.104 154.952 1.00 69.51  ? 3008 MET A CG    1 
ATOM   13290 S SD    . MET A 1 3008 ? 138.198 167.962 153.590 1.00 69.51  ? 3008 MET A SD    1 
ATOM   13291 C CE    . MET A 1 3008 ? 138.843 169.178 152.445 1.00 69.51  ? 3008 MET A CE    1 
ATOM   13292 N N     . ASN A 1 3009 ? 138.426 171.048 158.167 1.00 63.38  ? 3009 ASN A N     1 
ATOM   13293 C CA    . ASN A 1 3009 ? 137.759 171.458 159.403 1.00 63.38  ? 3009 ASN A CA    1 
ATOM   13294 C C     . ASN A 1 3009 ? 137.020 172.789 159.275 1.00 63.38  ? 3009 ASN A C     1 
ATOM   13295 O O     . ASN A 1 3009 ? 135.891 172.932 159.763 1.00 63.38  ? 3009 ASN A O     1 
ATOM   13296 C CB    . ASN A 1 3009 ? 138.780 171.531 160.542 1.00 63.38  ? 3009 ASN A CB    1 
ATOM   13297 C CG    . ASN A 1 3009 ? 139.487 170.212 160.777 1.00 63.38  ? 3009 ASN A CG    1 
ATOM   13298 O OD1   . ASN A 1 3009 ? 139.243 169.232 160.077 1.00 63.38  ? 3009 ASN A OD1   1 
ATOM   13299 N ND2   . ASN A 1 3009 ? 140.365 170.180 161.772 1.00 63.38  ? 3009 ASN A ND2   1 
ATOM   13300 N N     . THR A 1 3010 ? 137.635 173.776 158.616 1.00 68.50  ? 3010 THR A N     1 
ATOM   13301 C CA    . THR A 1 3010 ? 136.960 175.060 158.444 1.00 68.50  ? 3010 THR A CA    1 
ATOM   13302 C C     . THR A 1 3010 ? 135.699 174.912 157.595 1.00 68.50  ? 3010 THR A C     1 
ATOM   13303 O O     . THR A 1 3010 ? 134.664 175.519 157.892 1.00 68.50  ? 3010 THR A O     1 
ATOM   13304 C CB    . THR A 1 3010 ? 137.921 176.097 157.848 1.00 68.50  ? 3010 THR A CB    1 
ATOM   13305 O OG1   . THR A 1 3010 ? 137.280 177.378 157.806 1.00 68.50  ? 3010 THR A OG1   1 
ATOM   13306 C CG2   . THR A 1 3010 ? 138.383 175.709 156.447 1.00 68.50  ? 3010 THR A CG2   1 
ATOM   13307 N N     . LEU A 1 3011 ? 135.758 174.088 156.545 1.00 68.35  ? 3011 LEU A N     1 
ATOM   13308 C CA    . LEU A 1 3011 ? 134.581 173.850 155.712 1.00 68.35  ? 3011 LEU A CA    1 
ATOM   13309 C C     . LEU A 1 3011 ? 133.526 173.053 156.471 1.00 68.35  ? 3011 LEU A C     1 
ATOM   13310 O O     . LEU A 1 3011 ? 132.325 173.310 156.348 1.00 68.35  ? 3011 LEU A O     1 
ATOM   13311 C CB    . LEU A 1 3011 ? 135.004 173.124 154.433 1.00 68.35  ? 3011 LEU A CB    1 
ATOM   13312 C CG    . LEU A 1 3011 ? 134.017 172.892 153.287 1.00 68.35  ? 3011 LEU A CG    1 
ATOM   13313 C CD1   . LEU A 1 3011 ? 134.773 172.831 151.972 1.00 68.35  ? 3011 LEU A CD1   1 
ATOM   13314 C CD2   . LEU A 1 3011 ? 133.227 171.609 153.488 1.00 68.35  ? 3011 LEU A CD2   1 
ATOM   13315 N N     . LEU A 1 3012 ? 133.966 172.075 157.254 1.00 64.14  ? 3012 LEU A N     1 
ATOM   13316 C CA    . LEU A 1 3012 ? 133.055 171.232 158.016 1.00 64.14  ? 3012 LEU A CA    1 
ATOM   13317 C C     . LEU A 1 3012 ? 132.268 172.040 159.036 1.00 64.14  ? 3012 LEU A C     1 
ATOM   13318 O O     . LEU A 1 3012 ? 131.057 171.847 159.192 1.00 64.14  ? 3012 LEU A O     1 
ATOM   13319 C CB    . LEU A 1 3012 ? 133.844 170.121 158.699 1.00 64.14  ? 3012 LEU A CB    1 
ATOM   13320 C CG    . LEU A 1 3012 ? 134.114 168.854 157.893 1.00 64.14  ? 3012 LEU A CG    1 
ATOM   13321 C CD1   . LEU A 1 3012 ? 134.951 169.082 156.655 1.00 64.14  ? 3012 LEU A CD1   1 
ATOM   13322 C CD2   . LEU A 1 3012 ? 134.832 167.895 158.797 1.00 64.14  ? 3012 LEU A CD2   1 
ATOM   13323 N N     . ALA A 1 3013 ? 132.936 172.948 159.745 1.00 69.32  ? 3013 ALA A N     1 
ATOM   13324 C CA    . ALA A 1 3013 ? 132.259 173.805 160.707 1.00 69.32  ? 3013 ALA A CA    1 
ATOM   13325 C C     . ALA A 1 3013 ? 131.550 174.981 160.047 1.00 69.32  ? 3013 ALA A C     1 
ATOM   13326 O O     . ALA A 1 3013 ? 130.642 175.561 160.651 1.00 69.32  ? 3013 ALA A O     1 
ATOM   13327 C CB    . ALA A 1 3013 ? 133.248 174.313 161.756 1.00 69.32  ? 3013 ALA A CB    1 
ATOM   13328 N N     . ASN A 1 3014 ? 131.934 175.344 158.824 1.00 76.83  ? 3014 ASN A N     1 
ATOM   13329 C CA    . ASN A 1 3014 ? 131.404 176.549 158.199 1.00 76.83  ? 3014 ASN A CA    1 
ATOM   13330 C C     . ASN A 1 3014 ? 130.695 176.256 156.882 1.00 76.83  ? 3014 ASN A C     1 
ATOM   13331 O O     . ASN A 1 3014 ? 129.575 176.725 156.657 1.00 76.83  ? 3014 ASN A O     1 
ATOM   13332 C CB    . ASN A 1 3014 ? 132.536 177.553 157.973 1.00 76.83  ? 3014 ASN A CB    1 
ATOM   13333 C CG    . ASN A 1 3014 ? 133.124 178.067 159.272 1.00 76.83  ? 3014 ASN A CG    1 
ATOM   13334 O OD1   . ASN A 1 3014 ? 132.397 178.396 160.209 1.00 76.83  ? 3014 ASN A OD1   1 
ATOM   13335 N ND2   . ASN A 1 3014 ? 134.449 178.132 159.336 1.00 76.83  ? 3014 ASN A ND2   1 
ATOM   13336 N N     . GLY A 1 3015 ? 131.333 175.483 156.011 1.00 75.49  ? 3015 GLY A N     1 
ATOM   13337 C CA    . GLY A 1 3015 ? 130.840 175.275 154.667 1.00 75.49  ? 3015 GLY A CA    1 
ATOM   13338 C C     . GLY A 1 3015 ? 131.495 176.122 153.602 1.00 75.49  ? 3015 GLY A C     1 
ATOM   13339 O O     . GLY A 1 3015 ? 130.970 176.194 152.486 1.00 75.49  ? 3015 GLY A O     1 
ATOM   13340 N N     . GLU A 1 3016 ? 132.613 176.772 153.910 1.00 82.12  ? 3016 GLU A N     1 
ATOM   13341 C CA    . GLU A 1 3016 ? 133.318 177.594 152.939 1.00 82.12  ? 3016 GLU A CA    1 
ATOM   13342 C C     . GLU A 1 3016 ? 134.748 177.788 153.414 1.00 82.12  ? 3016 GLU A C     1 
ATOM   13343 O O     . GLU A 1 3016 ? 135.042 177.709 154.610 1.00 82.12  ? 3016 GLU A O     1 
ATOM   13344 C CB    . GLU A 1 3016 ? 132.621 178.945 152.736 1.00 82.12  ? 3016 GLU A CB    1 
ATOM   13345 C CG    . GLU A 1 3016 ? 132.968 179.988 153.788 1.00 82.12  ? 3016 GLU A CG    1 
ATOM   13346 C CD    . GLU A 1 3016 ? 132.331 179.700 155.136 1.00 82.12  ? 3016 GLU A CD    1 
ATOM   13347 O OE1   . GLU A 1 3016 ? 131.462 178.805 155.211 1.00 82.12  ? 3016 GLU A OE1   1 
ATOM   13348 O OE2   . GLU A 1 3016 ? 132.703 180.365 156.125 1.00 82.12  ? 3016 GLU A OE2   1 
ATOM   13349 N N     . VAL A 1 3017 ? 135.636 178.032 152.460 1.00 88.81  ? 3017 VAL A N     1 
ATOM   13350 C CA    . VAL A 1 3017 ? 137.040 178.301 152.729 1.00 88.81  ? 3017 VAL A CA    1 
ATOM   13351 C C     . VAL A 1 3017 ? 137.397 179.640 152.094 1.00 88.81  ? 3017 VAL A C     1 
ATOM   13352 O O     . VAL A 1 3017 ? 137.676 179.717 150.897 1.00 88.81  ? 3017 VAL A O     1 
ATOM   13353 C CB    . VAL A 1 3017 ? 137.946 177.175 152.198 1.00 88.81  ? 3017 VAL A CB    1 
ATOM   13354 C CG1   . VAL A 1 3017 ? 139.376 177.407 152.646 1.00 88.81  ? 3017 VAL A CG1   1 
ATOM   13355 C CG2   . VAL A 1 3017 ? 137.448 175.819 152.675 1.00 88.81  ? 3017 VAL A CG2   1 
ATOM   13356 N N     . PRO A 1 3018 ? 137.385 180.726 152.872 1.00 89.47  ? 3018 PRO A N     1 
ATOM   13357 C CA    . PRO A 1 3018 ? 137.640 182.053 152.278 1.00 89.47  ? 3018 PRO A CA    1 
ATOM   13358 C C     . PRO A 1 3018 ? 139.011 182.189 151.637 1.00 89.47  ? 3018 PRO A C     1 
ATOM   13359 O O     . PRO A 1 3018 ? 139.178 182.977 150.697 1.00 89.47  ? 3018 PRO A O     1 
ATOM   13360 C CB    . PRO A 1 3018 ? 137.469 183.001 153.475 1.00 89.47  ? 3018 PRO A CB    1 
ATOM   13361 C CG    . PRO A 1 3018 ? 136.630 182.242 154.455 1.00 89.47  ? 3018 PRO A CG    1 
ATOM   13362 C CD    . PRO A 1 3018 ? 137.038 180.812 154.300 1.00 89.47  ? 3018 PRO A CD    1 
ATOM   13363 N N     . GLY A 1 3019 ? 140.002 181.443 152.118 1.00 85.43  ? 3019 GLY A N     1 
ATOM   13364 C CA    . GLY A 1 3019 ? 141.363 181.603 151.643 1.00 85.43  ? 3019 GLY A CA    1 
ATOM   13365 C C     . GLY A 1 3019 ? 141.603 181.123 150.226 1.00 85.43  ? 3019 GLY A C     1 
ATOM   13366 O O     . GLY A 1 3019 ? 142.648 181.418 149.638 1.00 85.43  ? 3019 GLY A O     1 
ATOM   13367 N N     . LEU A 1 3020 ? 140.648 180.385 149.662 1.00 91.85  ? 3020 LEU A N     1 
ATOM   13368 C CA    . LEU A 1 3020 ? 140.787 179.833 148.320 1.00 91.85  ? 3020 LEU A CA    1 
ATOM   13369 C C     . LEU A 1 3020 ? 140.412 180.816 147.221 1.00 91.85  ? 3020 LEU A C     1 
ATOM   13370 O O     . LEU A 1 3020 ? 140.891 180.684 146.091 1.00 91.85  ? 3020 LEU A O     1 
ATOM   13371 C CB    . LEU A 1 3020 ? 139.931 178.572 148.173 1.00 91.85  ? 3020 LEU A CB    1 
ATOM   13372 C CG    . LEU A 1 3020 ? 140.195 177.445 149.169 1.00 91.85  ? 3020 LEU A CG    1 
ATOM   13373 C CD1   . LEU A 1 3020 ? 139.307 176.248 148.870 1.00 91.85  ? 3020 LEU A CD1   1 
ATOM   13374 C CD2   . LEU A 1 3020 ? 141.660 177.051 149.160 1.00 91.85  ? 3020 LEU A CD2   1 
ATOM   13375 N N     . PHE A 1 3021 ? 139.567 181.798 147.521 1.00 95.23  ? 3021 PHE A N     1 
ATOM   13376 C CA    . PHE A 1 3021 ? 139.030 182.708 146.515 1.00 95.23  ? 3021 PHE A CA    1 
ATOM   13377 C C     . PHE A 1 3021 ? 139.743 184.051 146.624 1.00 95.23  ? 3021 PHE A C     1 
ATOM   13378 O O     . PHE A 1 3021 ? 139.616 184.750 147.635 1.00 95.23  ? 3021 PHE A O     1 
ATOM   13379 C CB    . PHE A 1 3021 ? 137.522 182.859 146.689 1.00 95.23  ? 3021 PHE A CB    1 
ATOM   13380 C CG    . PHE A 1 3021 ? 136.791 181.551 146.714 1.00 95.23  ? 3021 PHE A CG    1 
ATOM   13381 C CD1   . PHE A 1 3021 ? 136.718 180.766 145.575 1.00 95.23  ? 3021 PHE A CD1   1 
ATOM   13382 C CD2   . PHE A 1 3021 ? 136.197 181.096 147.878 1.00 95.23  ? 3021 PHE A CD2   1 
ATOM   13383 C CE1   . PHE A 1 3021 ? 136.053 179.557 145.593 1.00 95.23  ? 3021 PHE A CE1   1 
ATOM   13384 C CE2   . PHE A 1 3021 ? 135.532 179.887 147.902 1.00 95.23  ? 3021 PHE A CE2   1 
ATOM   13385 C CZ    . PHE A 1 3021 ? 135.462 179.116 146.757 1.00 95.23  ? 3021 PHE A CZ    1 
ATOM   13386 N N     . GLU A 1 3022 ? 140.490 184.406 145.582 1.00 96.19  ? 3022 GLU A N     1 
ATOM   13387 C CA    . GLU A 1 3022 ? 141.248 185.647 145.554 1.00 96.19  ? 3022 GLU A CA    1 
ATOM   13388 C C     . GLU A 1 3022 ? 141.435 186.096 144.113 1.00 96.19  ? 3022 GLU A C     1 
ATOM   13389 O O     . GLU A 1 3022 ? 141.459 185.277 143.189 1.00 96.19  ? 3022 GLU A O     1 
ATOM   13390 C CB    . GLU A 1 3022 ? 142.614 185.482 146.241 1.00 96.19  ? 3022 GLU A CB    1 
ATOM   13391 C CG    . GLU A 1 3022 ? 143.727 184.958 145.334 1.00 96.19  ? 3022 GLU A CG    1 
ATOM   13392 C CD    . GLU A 1 3022 ? 143.430 183.586 144.748 1.00 96.19  ? 3022 GLU A CD    1 
ATOM   13393 O OE1   . GLU A 1 3022 ? 144.010 183.256 143.692 1.00 96.19  ? 3022 GLU A OE1   1 
ATOM   13394 O OE2   . GLU A 1 3022 ? 142.630 182.834 145.344 1.00 96.19  ? 3022 GLU A OE2   1 
ATOM   13395 N N     . GLY A 1 3023 ? 141.559 187.408 143.933 1.00 90.55  ? 3023 GLY A N     1 
ATOM   13396 C CA    . GLY A 1 3023 ? 141.884 187.954 142.624 1.00 90.55  ? 3023 GLY A CA    1 
ATOM   13397 C C     . GLY A 1 3023 ? 140.884 187.556 141.560 1.00 90.55  ? 3023 GLY A C     1 
ATOM   13398 O O     . GLY A 1 3023 ? 139.665 187.656 141.747 1.00 90.55  ? 3023 GLY A O     1 
ATOM   13399 N N     . ASP A 1 3024 ? 141.406 187.098 140.420 1.00 93.51  ? 3024 ASP A N     1 
ATOM   13400 C CA    . ASP A 1 3024 ? 140.543 186.711 139.309 1.00 93.51  ? 3024 ASP A CA    1 
ATOM   13401 C C     . ASP A 1 3024 ? 139.736 185.462 139.637 1.00 93.51  ? 3024 ASP A C     1 
ATOM   13402 O O     . ASP A 1 3024 ? 138.655 185.249 139.076 1.00 93.51  ? 3024 ASP A O     1 
ATOM   13403 C CB    . ASP A 1 3024 ? 141.379 186.502 138.045 1.00 93.51  ? 3024 ASP A CB    1 
ATOM   13404 C CG    . ASP A 1 3024 ? 142.454 185.447 138.220 1.00 93.51  ? 3024 ASP A CG    1 
ATOM   13405 O OD1   . ASP A 1 3024 ? 142.633 184.951 139.353 1.00 93.51  ? 3024 ASP A OD1   1 
ATOM   13406 O OD2   . ASP A 1 3024 ? 143.126 185.115 137.221 1.00 93.51  ? 3024 ASP A OD2   1 
ATOM   13407 N N     . GLU A 1 3025 ? 140.250 184.614 140.531 1.00 94.39  ? 3025 GLU A N     1 
ATOM   13408 C CA    . GLU A 1 3025 ? 139.499 183.430 140.935 1.00 94.39  ? 3025 GLU A CA    1 
ATOM   13409 C C     . GLU A 1 3025 ? 138.222 183.819 141.670 1.00 94.39  ? 3025 GLU A C     1 
ATOM   13410 O O     . GLU A 1 3025 ? 137.154 183.247 141.431 1.00 94.39  ? 3025 GLU A O     1 
ATOM   13411 C CB    . GLU A 1 3025 ? 140.371 182.523 141.803 1.00 94.39  ? 3025 GLU A CB    1 
ATOM   13412 C CG    . GLU A 1 3025 ? 141.710 182.170 141.175 1.00 94.39  ? 3025 GLU A CG    1 
ATOM   13413 C CD    . GLU A 1 3025 ? 141.584 181.209 140.006 1.00 94.39  ? 3025 GLU A CD    1 
ATOM   13414 O OE1   . GLU A 1 3025 ? 140.480 180.667 139.784 1.00 94.39  ? 3025 GLU A OE1   1 
ATOM   13415 O OE2   . GLU A 1 3025 ? 142.594 180.998 139.303 1.00 94.39  ? 3025 GLU A OE2   1 
ATOM   13416 N N     . TYR A 1 3026 ? 138.314 184.805 142.565 1.00 94.13  ? 3026 TYR A N     1 
ATOM   13417 C CA    . TYR A 1 3026 ? 137.131 185.265 143.285 1.00 94.13  ? 3026 TYR A CA    1 
ATOM   13418 C C     . TYR A 1 3026 ? 136.130 185.915 142.334 1.00 94.13  ? 3026 TYR A C     1 
ATOM   13419 O O     . TYR A 1 3026 ? 134.915 185.715 142.464 1.00 94.13  ? 3026 TYR A O     1 
ATOM   13420 C CB    . TYR A 1 3026 ? 137.554 186.229 144.397 1.00 94.13  ? 3026 TYR A CB    1 
ATOM   13421 C CG    . TYR A 1 3026 ? 136.433 186.711 145.291 1.00 94.13  ? 3026 TYR A CG    1 
ATOM   13422 C CD1   . TYR A 1 3026 ? 135.738 185.825 146.104 1.00 94.13  ? 3026 TYR A CD1   1 
ATOM   13423 C CD2   . TYR A 1 3026 ? 136.098 188.056 145.356 1.00 94.13  ? 3026 TYR A CD2   1 
ATOM   13424 C CE1   . TYR A 1 3026 ? 134.721 186.259 146.934 1.00 94.13  ? 3026 TYR A CE1   1 
ATOM   13425 C CE2   . TYR A 1 3026 ? 135.083 188.501 146.184 1.00 94.13  ? 3026 TYR A CE2   1 
ATOM   13426 C CZ    . TYR A 1 3026 ? 134.399 187.598 146.970 1.00 94.13  ? 3026 TYR A CZ    1 
ATOM   13427 O OH    . TYR A 1 3026 ? 133.390 188.038 147.795 1.00 94.13  ? 3026 TYR A OH    1 
ATOM   13428 N N     . ALA A 1 3027 ? 136.628 186.684 141.360 1.00 92.70  ? 3027 ALA A N     1 
ATOM   13429 C CA    . ALA A 1 3027 ? 135.756 187.316 140.375 1.00 92.70  ? 3027 ALA A CA    1 
ATOM   13430 C C     . ALA A 1 3027 ? 135.046 186.275 139.516 1.00 92.70  ? 3027 ALA A C     1 
ATOM   13431 O O     . ALA A 1 3027 ? 133.849 186.397 139.229 1.00 92.70  ? 3027 ALA A O     1 
ATOM   13432 C CB    . ALA A 1 3027 ? 136.567 188.274 139.502 1.00 92.70  ? 3027 ALA A CB    1 
ATOM   13433 N N     . THR A 1 3028 ? 135.770 185.232 139.101 1.00 94.18  ? 3028 THR A N     1 
ATOM   13434 C CA    . THR A 1 3028 ? 135.145 184.169 138.323 1.00 94.18  ? 3028 THR A CA    1 
ATOM   13435 C C     . THR A 1 3028 ? 134.139 183.397 139.165 1.00 94.18  ? 3028 THR A C     1 
ATOM   13436 O O     . THR A 1 3028 ? 133.097 182.969 138.658 1.00 94.18  ? 3028 THR A O     1 
ATOM   13437 C CB    . THR A 1 3028 ? 136.206 183.223 137.762 1.00 94.18  ? 3028 THR A CB    1 
ATOM   13438 O OG1   . THR A 1 3028 ? 137.120 182.858 138.800 1.00 94.18  ? 3028 THR A OG1   1 
ATOM   13439 C CG2   . THR A 1 3028 ? 136.966 183.882 136.618 1.00 94.18  ? 3028 THR A CG2   1 
ATOM   13440 N N     . LEU A 1 3029 ? 134.439 183.196 140.451 1.00 93.56  ? 3029 LEU A N     1 
ATOM   13441 C CA    . LEU A 1 3029 ? 133.478 182.553 141.340 1.00 93.56  ? 3029 LEU A CA    1 
ATOM   13442 C C     . LEU A 1 3029 ? 132.191 183.360 141.416 1.00 93.56  ? 3029 LEU A C     1 
ATOM   13443 O O     . LEU A 1 3029 ? 131.092 182.808 141.316 1.00 93.56  ? 3029 LEU A O     1 
ATOM   13444 C CB    . LEU A 1 3029 ? 134.081 182.371 142.734 1.00 93.56  ? 3029 LEU A CB    1 
ATOM   13445 C CG    . LEU A 1 3029 ? 133.089 181.901 143.805 1.00 93.56  ? 3029 LEU A CG    1 
ATOM   13446 C CD1   . LEU A 1 3029 ? 132.911 180.393 143.744 1.00 93.56  ? 3029 LEU A CD1   1 
ATOM   13447 C CD2   . LEU A 1 3029 ? 133.522 182.333 145.197 1.00 93.56  ? 3029 LEU A CD2   1 
ATOM   13448 N N     . MET A 1 3030 ? 132.312 184.680 141.574 1.00 93.90  ? 3030 MET A N     1 
ATOM   13449 C CA    . MET A 1 3030 ? 131.120 185.523 141.628 1.00 93.90  ? 3030 MET A CA    1 
ATOM   13450 C C     . MET A 1 3030 ? 130.355 185.495 140.309 1.00 93.90  ? 3030 MET A C     1 
ATOM   13451 O O     . MET A 1 3030 ? 129.121 185.471 140.306 1.00 93.90  ? 3030 MET A O     1 
ATOM   13452 C CB    . MET A 1 3030 ? 131.491 186.954 142.003 1.00 93.90  ? 3030 MET A CB    1 
ATOM   13453 C CG    . MET A 1 3030 ? 132.028 187.102 143.409 1.00 93.90  ? 3030 MET A CG    1 
ATOM   13454 S SD    . MET A 1 3030 ? 132.373 188.825 143.788 1.00 93.90  ? 3030 MET A SD    1 
ATOM   13455 C CE    . MET A 1 3030 ? 133.859 189.082 142.829 1.00 93.90  ? 3030 MET A CE    1 
ATOM   13456 N N     . THR A 1 3031 ? 131.067 185.508 139.180 1.00 87.54  ? 3031 THR A N     1 
ATOM   13457 C CA    . THR A 1 3031 ? 130.398 185.499 137.880 1.00 87.54  ? 3031 THR A CA    1 
ATOM   13458 C C     . THR A 1 3031 ? 129.646 184.190 137.649 1.00 87.54  ? 3031 THR A C     1 
ATOM   13459 O O     . THR A 1 3031 ? 128.481 184.190 137.225 1.00 87.54  ? 3031 THR A O     1 
ATOM   13460 C CB    . THR A 1 3031 ? 131.425 185.734 136.771 1.00 87.54  ? 3031 THR A CB    1 
ATOM   13461 O OG1   . THR A 1 3031 ? 132.104 186.973 137.004 1.00 87.54  ? 3031 THR A OG1   1 
ATOM   13462 C CG2   . THR A 1 3031 ? 130.751 185.780 135.404 1.00 87.54  ? 3031 THR A CG2   1 
ATOM   13463 N N     . GLN A 1 3032 ? 130.301 183.059 137.921 1.00 89.60  ? 3032 GLN A N     1 
ATOM   13464 C CA    . GLN A 1 3032 ? 129.638 181.770 137.755 1.00 89.60  ? 3032 GLN A CA    1 
ATOM   13465 C C     . GLN A 1 3032 ? 128.509 181.604 138.763 1.00 89.60  ? 3032 GLN A C     1 
ATOM   13466 O O     . GLN A 1 3032 ? 127.500 180.953 138.471 1.00 89.60  ? 3032 GLN A O     1 
ATOM   13467 C CB    . GLN A 1 3032 ? 130.651 180.632 137.879 1.00 89.60  ? 3032 GLN A CB    1 
ATOM   13468 C CG    . GLN A 1 3032 ? 131.821 180.724 136.909 1.00 89.60  ? 3032 GLN A CG    1 
ATOM   13469 C CD    . GLN A 1 3032 ? 131.386 180.655 135.458 1.00 89.60  ? 3032 GLN A CD    1 
ATOM   13470 O OE1   . GLN A 1 3032 ? 131.420 181.655 134.740 1.00 89.60  ? 3032 GLN A OE1   1 
ATOM   13471 N NE2   . GLN A 1 3032 ? 130.965 179.474 135.021 1.00 89.60  ? 3032 GLN A NE2   1 
ATOM   13472 N N     . CYS A 1 3033 ? 128.649 182.199 139.950 1.00 87.90  ? 3033 CYS A N     1 
ATOM   13473 C CA    . CYS A 1 3033 ? 127.552 182.192 140.910 1.00 87.90  ? 3033 CYS A CA    1 
ATOM   13474 C C     . CYS A 1 3033 ? 126.382 183.025 140.408 1.00 87.90  ? 3033 CYS A C     1 
ATOM   13475 O O     . CYS A 1 3033 ? 125.222 182.675 140.633 1.00 87.90  ? 3033 CYS A O     1 
ATOM   13476 C CB    . CYS A 1 3033 ? 128.038 182.702 142.265 1.00 87.90  ? 3033 CYS A CB    1 
ATOM   13477 S SG    . CYS A 1 3033 ? 128.869 181.452 143.260 1.00 87.90  ? 3033 CYS A SG    1 
ATOM   13478 N N     . LYS A 1 3034 ? 126.668 184.137 139.729 1.00 86.08  ? 3034 LYS A N     1 
ATOM   13479 C CA    . LYS A 1 3034 ? 125.604 184.929 139.121 1.00 86.08  ? 3034 LYS A CA    1 
ATOM   13480 C C     . LYS A 1 3034 ? 124.874 184.126 138.052 1.00 86.08  ? 3034 LYS A C     1 
ATOM   13481 O O     . LYS A 1 3034 ? 123.641 184.150 137.971 1.00 86.08  ? 3034 LYS A O     1 
ATOM   13482 C CB    . LYS A 1 3034 ? 126.182 186.216 138.531 1.00 86.08  ? 3034 LYS A CB    1 
ATOM   13483 C CG    . LYS A 1 3034 ? 125.302 186.861 137.470 1.00 86.08  ? 3034 LYS A CG    1 
ATOM   13484 C CD    . LYS A 1 3034 ? 126.064 187.901 136.663 1.00 86.08  ? 3034 LYS A CD    1 
ATOM   13485 C CE    . LYS A 1 3034 ? 127.356 187.333 136.098 1.00 86.08  ? 3034 LYS A CE    1 
ATOM   13486 N NZ    . LYS A 1 3034 ? 128.160 188.378 135.407 1.00 86.08  ? 3034 LYS A NZ    1 
ATOM   13487 N N     . GLU A 1 3035 ? 125.627 183.405 137.219 1.00 84.49  ? 3035 GLU A N     1 
ATOM   13488 C CA    . GLU A 1 3035 ? 124.999 182.565 136.200 1.00 84.49  ? 3035 GLU A CA    1 
ATOM   13489 C C     . GLU A 1 3035 ? 124.158 181.463 136.841 1.00 84.49  ? 3035 GLU A C     1 
ATOM   13490 O O     . GLU A 1 3035 ? 123.031 181.188 136.406 1.00 84.49  ? 3035 GLU A O     1 
ATOM   13491 C CB    . GLU A 1 3035 ? 126.061 181.970 135.274 1.00 84.49  ? 3035 GLU A CB    1 
ATOM   13492 C CG    . GLU A 1 3035 ? 126.984 183.000 134.642 1.00 84.49  ? 3035 GLU A CG    1 
ATOM   13493 C CD    . GLU A 1 3035 ? 128.315 182.408 134.220 1.00 84.49  ? 3035 GLU A CD    1 
ATOM   13494 O OE1   . GLU A 1 3035 ? 128.514 181.191 134.418 1.00 84.49  ? 3035 GLU A OE1   1 
ATOM   13495 O OE2   . GLU A 1 3035 ? 129.161 183.159 133.690 1.00 84.49  ? 3035 GLU A OE2   1 
ATOM   13496 N N     . GLY A 1 3036 ? 124.688 180.825 137.885 1.00 81.94  ? 3036 GLY A N     1 
ATOM   13497 C CA    . GLY A 1 3036 ? 123.910 179.831 138.604 1.00 81.94  ? 3036 GLY A CA    1 
ATOM   13498 C C     . GLY A 1 3036 ? 122.666 180.423 139.237 1.00 81.94  ? 3036 GLY A C     1 
ATOM   13499 O O     . GLY A 1 3036 ? 121.633 179.761 139.334 1.00 81.94  ? 3036 GLY A O     1 
ATOM   13500 N N     . ALA A 1 3037 ? 122.753 181.677 139.681 1.00 81.63  ? 3037 ALA A N     1 
ATOM   13501 C CA    . ALA A 1 3037 ? 121.584 182.375 140.202 1.00 81.63  ? 3037 ALA A CA    1 
ATOM   13502 C C     . ALA A 1 3037 ? 120.545 182.591 139.110 1.00 81.63  ? 3037 ALA A C     1 
ATOM   13503 O O     . ALA A 1 3037 ? 119.340 182.457 139.353 1.00 81.63  ? 3037 ALA A O     1 
ATOM   13504 C CB    . ALA A 1 3037 ? 122.009 183.708 140.817 1.00 81.63  ? 3037 ALA A CB    1 
ATOM   13505 N N     . GLN A 1 3038 ? 120.995 182.940 137.902 1.00 83.86  ? 3038 GLN A N     1 
ATOM   13506 C CA    . GLN A 1 3038 ? 120.077 183.028 136.769 1.00 83.86  ? 3038 GLN A CA    1 
ATOM   13507 C C     . GLN A 1 3038 ? 119.390 181.690 136.533 1.00 83.86  ? 3038 GLN A C     1 
ATOM   13508 O O     . GLN A 1 3038 ? 118.190 181.635 136.239 1.00 83.86  ? 3038 GLN A O     1 
ATOM   13509 C CB    . GLN A 1 3038 ? 120.812 183.476 135.503 1.00 83.86  ? 3038 GLN A CB    1 
ATOM   13510 C CG    . GLN A 1 3038 ? 121.727 184.675 135.666 1.00 83.86  ? 3038 GLN A CG    1 
ATOM   13511 C CD    . GLN A 1 3038 ? 121.086 185.806 136.441 1.00 83.86  ? 3038 GLN A CD    1 
ATOM   13512 O OE1   . GLN A 1 3038 ? 121.638 186.281 137.432 1.00 83.86  ? 3038 GLN A OE1   1 
ATOM   13513 N NE2   . GLN A 1 3038 ? 119.919 186.250 135.988 1.00 83.86  ? 3038 GLN A NE2   1 
ATOM   13514 N N     . LYS A 1 3039 ? 120.145 180.595 136.649 1.00 79.93  ? 3039 LYS A N     1 
ATOM   13515 C CA    . LYS A 1 3039 ? 119.536 179.270 136.556 1.00 79.93  ? 3039 LYS A CA    1 
ATOM   13516 C C     . LYS A 1 3039 ? 118.502 179.054 137.658 1.00 79.93  ? 3039 LYS A C     1 
ATOM   13517 O O     . LYS A 1 3039 ? 117.418 178.515 137.403 1.00 79.93  ? 3039 LYS A O     1 
ATOM   13518 C CB    . LYS A 1 3039 ? 120.607 178.179 136.604 1.00 79.93  ? 3039 LYS A CB    1 
ATOM   13519 C CG    . LYS A 1 3039 ? 121.157 177.776 135.243 1.00 79.93  ? 3039 LYS A CG    1 
ATOM   13520 C CD    . LYS A 1 3039 ? 122.166 178.772 134.711 1.00 79.93  ? 3039 LYS A CD    1 
ATOM   13521 C CE    . LYS A 1 3039 ? 122.315 178.655 133.204 1.00 79.93  ? 3039 LYS A CE    1 
ATOM   13522 N NZ    . LYS A 1 3039 ? 122.971 179.857 132.620 1.00 79.93  ? 3039 LYS A NZ    1 
ATOM   13523 N N     . GLU A 1 3040 ? 118.817 179.466 138.888 1.00 81.32  ? 3040 GLU A N     1 
ATOM   13524 C CA    . GLU A 1 3040 ? 117.871 179.366 139.994 1.00 81.32  ? 3040 GLU A CA    1 
ATOM   13525 C C     . GLU A 1 3040 ? 116.803 180.449 139.957 1.00 81.32  ? 3040 GLU A C     1 
ATOM   13526 O O     . GLU A 1 3040 ? 115.825 180.354 140.706 1.00 81.32  ? 3040 GLU A O     1 
ATOM   13527 C CB    . GLU A 1 3040 ? 118.604 179.430 141.337 1.00 81.32  ? 3040 GLU A CB    1 
ATOM   13528 C CG    . GLU A 1 3040 ? 119.794 178.492 141.470 1.00 81.32  ? 3040 GLU A CG    1 
ATOM   13529 C CD    . GLU A 1 3040 ? 119.390 177.057 141.744 1.00 81.32  ? 3040 GLU A CD    1 
ATOM   13530 O OE1   . GLU A 1 3040 ? 118.179 176.792 141.895 1.00 81.32  ? 3040 GLU A OE1   1 
ATOM   13531 O OE2   . GLU A 1 3040 ? 120.288 176.192 141.813 1.00 81.32  ? 3040 GLU A OE2   1 
ATOM   13532 N N     . GLY A 1 3041 ? 116.961 181.467 139.114 1.00 79.40  ? 3041 GLY A N     1 
ATOM   13533 C CA    . GLY A 1 3041 ? 116.011 182.553 139.035 1.00 79.40  ? 3041 GLY A CA    1 
ATOM   13534 C C     . GLY A 1 3041 ? 116.418 183.823 139.748 1.00 79.40  ? 3041 GLY A C     1 
ATOM   13535 O O     . GLY A 1 3041 ? 115.647 184.791 139.740 1.00 79.40  ? 3041 GLY A O     1 
ATOM   13536 N N     . LEU A 1 3042 ? 117.597 183.856 140.364 1.00 83.17  ? 3042 LEU A N     1 
ATOM   13537 C CA    . LEU A 1 3042 ? 118.078 185.053 141.031 1.00 83.17  ? 3042 LEU A CA    1 
ATOM   13538 C C     . LEU A 1 3042 ? 118.824 185.938 140.031 1.00 83.17  ? 3042 LEU A C     1 
ATOM   13539 O O     . LEU A 1 3042 ? 118.831 185.688 138.824 1.00 83.17  ? 3042 LEU A O     1 
ATOM   13540 C CB    . LEU A 1 3042 ? 118.960 184.681 142.222 1.00 83.17  ? 3042 LEU A CB    1 
ATOM   13541 C CG    . LEU A 1 3042 ? 118.289 183.906 143.358 1.00 83.17  ? 3042 LEU A CG    1 
ATOM   13542 C CD1   . LEU A 1 3042 ? 119.320 183.459 144.384 1.00 83.17  ? 3042 LEU A CD1   1 
ATOM   13543 C CD2   . LEU A 1 3042 ? 117.201 184.743 144.015 1.00 83.17  ? 3042 LEU A CD2   1 
ATOM   13544 N N     . MET A 1 3043 ? 119.463 186.985 140.540 1.00 95.94  ? 3043 MET A N     1 
ATOM   13545 C CA    . MET A 1 3043 ? 120.122 187.976 139.696 1.00 95.94  ? 3043 MET A CA    1 
ATOM   13546 C C     . MET A 1 3043 ? 121.503 188.231 140.303 1.00 95.94  ? 3043 MET A C     1 
ATOM   13547 O O     . MET A 1 3043 ? 121.914 187.577 141.271 1.00 95.94  ? 3043 MET A O     1 
ATOM   13548 C CB    . MET A 1 3043 ? 119.192 189.196 139.574 1.00 95.94  ? 3043 MET A CB    1 
ATOM   13549 C CG    . MET A 1 3043 ? 119.644 190.343 138.672 1.00 95.94  ? 3043 MET A CG    1 
ATOM   13550 S SD    . MET A 1 3043 ? 120.804 191.478 139.452 1.00 95.94  ? 3043 MET A SD    1 
ATOM   13551 C CE    . MET A 1 3043 ? 119.724 192.334 140.596 1.00 95.94  ? 3043 MET A CE    1 
ATOM   13552 N N     . LEU A 1 3044 ? 122.252 189.174 139.722 1.00 97.07  ? 3044 LEU A N     1 
ATOM   13553 C CA    . LEU A 1 3044 ? 123.576 189.506 140.245 1.00 97.07  ? 3044 LEU A CA    1 
ATOM   13554 C C     . LEU A 1 3044 ? 123.503 189.916 141.709 1.00 97.07  ? 3044 LEU A C     1 
ATOM   13555 O O     . LEU A 1 3044 ? 124.315 189.466 142.527 1.00 97.07  ? 3044 LEU A O     1 
ATOM   13556 C CB    . LEU A 1 3044 ? 124.204 190.624 139.409 1.00 97.07  ? 3044 LEU A CB    1 
ATOM   13557 C CG    . LEU A 1 3044 ? 125.620 191.086 139.760 1.00 97.07  ? 3044 LEU A CG    1 
ATOM   13558 C CD1   . LEU A 1 3044 ? 126.626 189.967 139.571 1.00 97.07  ? 3044 LEU A CD1   1 
ATOM   13559 C CD2   . LEU A 1 3044 ? 126.009 192.303 138.933 1.00 97.07  ? 3044 LEU A CD2   1 
ATOM   13560 N N     . ASP A 1 3045 ? 122.528 190.758 142.057 1.00 97.77  ? 3045 ASP A N     1 
ATOM   13561 C CA    . ASP A 1 3045 ? 122.260 191.187 143.436 1.00 97.77  ? 3045 ASP A CA    1 
ATOM   13562 C C     . ASP A 1 3045 ? 123.553 191.767 144.011 1.00 97.77  ? 3045 ASP A C     1 
ATOM   13563 O O     . ASP A 1 3045 ? 124.152 192.652 143.383 1.00 97.77  ? 3045 ASP A O     1 
ATOM   13564 C CB    . ASP A 1 3045 ? 121.661 190.018 144.207 1.00 97.77  ? 3045 ASP A CB    1 
ATOM   13565 C CG    . ASP A 1 3045 ? 120.803 190.465 145.374 1.00 97.77  ? 3045 ASP A CG    1 
ATOM   13566 O OD1   . ASP A 1 3045 ? 120.690 191.688 145.597 1.00 97.77  ? 3045 ASP A OD1   1 
ATOM   13567 O OD2   . ASP A 1 3045 ? 120.238 189.591 146.066 1.00 97.77  ? 3045 ASP A OD2   1 
ATOM   13568 N N     . SER A 1 3046 ? 124.014 191.313 145.172 1.00 95.67  ? 3046 SER A N     1 
ATOM   13569 C CA    . SER A 1 3046 ? 125.264 191.785 145.747 1.00 95.67  ? 3046 SER A CA    1 
ATOM   13570 C C     . SER A 1 3046 ? 126.358 190.745 145.550 1.00 95.67  ? 3046 SER A C     1 
ATOM   13571 O O     . SER A 1 3046 ? 126.109 189.538 145.632 1.00 95.67  ? 3046 SER A O     1 
ATOM   13572 C CB    . SER A 1 3046 ? 125.090 192.094 147.235 1.00 95.67  ? 3046 SER A CB    1 
ATOM   13573 O OG    . SER A 1 3046 ? 126.345 192.269 147.869 1.00 95.67  ? 3046 SER A OG    1 
ATOM   13574 N N     . HIS A 1 3047 ? 127.573 191.224 145.276 1.00 98.65  ? 3047 HIS A N     1 
ATOM   13575 C CA    . HIS A 1 3047 ? 128.704 190.325 145.072 1.00 98.65  ? 3047 HIS A CA    1 
ATOM   13576 C C     . HIS A 1 3047 ? 128.990 189.518 146.335 1.00 98.65  ? 3047 HIS A C     1 
ATOM   13577 O O     . HIS A 1 3047 ? 129.205 188.298 146.282 1.00 98.65  ? 3047 HIS A O     1 
ATOM   13578 C CB    . HIS A 1 3047 ? 129.929 191.138 144.654 1.00 98.65  ? 3047 HIS A CB    1 
ATOM   13579 C CG    . HIS A 1 3047 ? 129.771 191.827 143.333 1.00 98.65  ? 3047 HIS A CG    1 
ATOM   13580 N ND1   . HIS A 1 3047 ? 129.840 191.160 142.130 1.00 98.65  ? 3047 HIS A ND1   1 
ATOM   13581 C CD2   . HIS A 1 3047 ? 129.543 193.127 143.029 1.00 98.65  ? 3047 HIS A CD2   1 
ATOM   13582 C CE1   . HIS A 1 3047 ? 129.662 192.018 141.141 1.00 98.65  ? 3047 HIS A CE1   1 
ATOM   13583 N NE2   . HIS A 1 3047 ? 129.480 193.219 141.660 1.00 98.65  ? 3047 HIS A NE2   1 
ATOM   13584 N N     . GLU A 1 3048 ? 128.981 190.188 147.488 1.00 97.37  ? 3048 GLU A N     1 
ATOM   13585 C CA    . GLU A 1 3048 ? 129.087 189.479 148.757 1.00 97.37  ? 3048 GLU A CA    1 
ATOM   13586 C C     . GLU A 1 3048 ? 127.914 188.525 148.935 1.00 97.37  ? 3048 GLU A C     1 
ATOM   13587 O O     . GLU A 1 3048 ? 128.067 187.424 149.475 1.00 97.37  ? 3048 GLU A O     1 
ATOM   13588 C CB    . GLU A 1 3048 ? 129.161 190.479 149.912 1.00 97.37  ? 3048 GLU A CB    1 
ATOM   13589 C CG    . GLU A 1 3048 ? 129.618 189.879 151.232 1.00 97.37  ? 3048 GLU A CG    1 
ATOM   13590 C CD    . GLU A 1 3048 ? 128.490 189.216 151.998 1.00 97.37  ? 3048 GLU A CD    1 
ATOM   13591 O OE1   . GLU A 1 3048 ? 127.330 189.651 151.846 1.00 97.37  ? 3048 GLU A OE1   1 
ATOM   13592 O OE2   . GLU A 1 3048 ? 128.765 188.257 152.750 1.00 97.37  ? 3048 GLU A OE2   1 
ATOM   13593 N N     . GLU A 1 3049 ? 126.727 188.928 148.475 1.00 92.49  ? 3049 GLU A N     1 
ATOM   13594 C CA    . GLU A 1 3049 ? 125.589 188.017 148.513 1.00 92.49  ? 3049 GLU A CA    1 
ATOM   13595 C C     . GLU A 1 3049 ? 125.759 186.871 147.524 1.00 92.49  ? 3049 GLU A C     1 
ATOM   13596 O O     . GLU A 1 3049 ? 125.238 185.775 147.754 1.00 92.49  ? 3049 GLU A O     1 
ATOM   13597 C CB    . GLU A 1 3049 ? 124.289 188.774 148.241 1.00 92.49  ? 3049 GLU A CB    1 
ATOM   13598 C CG    . GLU A 1 3049 ? 123.594 189.281 149.499 1.00 92.49  ? 3049 GLU A CG    1 
ATOM   13599 C CD    . GLU A 1 3049 ? 123.057 188.164 150.381 1.00 92.49  ? 3049 GLU A CD    1 
ATOM   13600 O OE1   . GLU A 1 3049 ? 123.049 186.994 149.944 1.00 92.49  ? 3049 GLU A OE1   1 
ATOM   13601 O OE2   . GLU A 1 3049 ? 122.644 188.459 151.521 1.00 92.49  ? 3049 GLU A OE2   1 
ATOM   13602 N N     . LEU A 1 3050 ? 126.486 187.093 146.427 1.00 92.21  ? 3050 LEU A N     1 
ATOM   13603 C CA    . LEU A 1 3050 ? 126.837 185.984 145.544 1.00 92.21  ? 3050 LEU A CA    1 
ATOM   13604 C C     . LEU A 1 3050 ? 127.706 184.970 146.276 1.00 92.21  ? 3050 LEU A C     1 
ATOM   13605 O O     . LEU A 1 3050 ? 127.487 183.755 146.178 1.00 92.21  ? 3050 LEU A O     1 
ATOM   13606 C CB    . LEU A 1 3050 ? 127.556 186.505 144.300 1.00 92.21  ? 3050 LEU A CB    1 
ATOM   13607 C CG    . LEU A 1 3050 ? 126.727 187.218 143.234 1.00 92.21  ? 3050 LEU A CG    1 
ATOM   13608 C CD1   . LEU A 1 3050 ? 127.636 187.687 142.117 1.00 92.21  ? 3050 LEU A CD1   1 
ATOM   13609 C CD2   . LEU A 1 3050 ? 125.639 186.304 142.695 1.00 92.21  ? 3050 LEU A CD2   1 
ATOM   13610 N N     . TYR A 1 3051 ? 128.697 185.456 147.028 1.00 88.47  ? 3051 TYR A N     1 
ATOM   13611 C CA    . TYR A 1 3051 ? 129.522 184.549 147.822 1.00 88.47  ? 3051 TYR A CA    1 
ATOM   13612 C C     . TYR A 1 3051 ? 128.690 183.841 148.887 1.00 88.47  ? 3051 TYR A C     1 
ATOM   13613 O O     . TYR A 1 3051 ? 128.906 182.656 149.171 1.00 88.47  ? 3051 TYR A O     1 
ATOM   13614 C CB    . TYR A 1 3051 ? 130.685 185.313 148.458 1.00 88.47  ? 3051 TYR A CB    1 
ATOM   13615 C CG    . TYR A 1 3051 ? 131.646 184.441 149.240 1.00 88.47  ? 3051 TYR A CG    1 
ATOM   13616 C CD1   . TYR A 1 3051 ? 131.396 184.105 150.565 1.00 88.47  ? 3051 TYR A CD1   1 
ATOM   13617 C CD2   . TYR A 1 3051 ? 132.800 183.946 148.647 1.00 88.47  ? 3051 TYR A CD2   1 
ATOM   13618 C CE1   . TYR A 1 3051 ? 132.269 183.306 151.277 1.00 88.47  ? 3051 TYR A CE1   1 
ATOM   13619 C CE2   . TYR A 1 3051 ? 133.680 183.146 149.352 1.00 88.47  ? 3051 TYR A CE2   1 
ATOM   13620 C CZ    . TYR A 1 3051 ? 133.409 182.830 150.667 1.00 88.47  ? 3051 TYR A CZ    1 
ATOM   13621 O OH    . TYR A 1 3051 ? 134.281 182.034 151.373 1.00 88.47  ? 3051 TYR A OH    1 
ATOM   13622 N N     . LYS A 1 3052 ? 127.742 184.556 149.495 1.00 84.59  ? 3052 LYS A N     1 
ATOM   13623 C CA    . LYS A 1 3052 ? 126.869 183.945 150.495 1.00 84.59  ? 3052 LYS A CA    1 
ATOM   13624 C C     . LYS A 1 3052 ? 126.012 182.840 149.885 1.00 84.59  ? 3052 LYS A C     1 
ATOM   13625 O O     . LYS A 1 3052 ? 125.820 181.780 150.496 1.00 84.59  ? 3052 LYS A O     1 
ATOM   13626 C CB    . LYS A 1 3052 ? 125.989 185.018 151.137 1.00 84.59  ? 3052 LYS A CB    1 
ATOM   13627 C CG    . LYS A 1 3052 ? 125.121 184.523 152.280 1.00 84.59  ? 3052 LYS A CG    1 
ATOM   13628 C CD    . LYS A 1 3052 ? 125.905 183.644 153.239 1.00 84.59  ? 3052 LYS A CD    1 
ATOM   13629 C CE    . LYS A 1 3052 ? 125.006 183.109 154.338 1.00 84.59  ? 3052 LYS A CE    1 
ATOM   13630 N NZ    . LYS A 1 3052 ? 123.614 182.901 153.853 1.00 84.59  ? 3052 LYS A NZ    1 
ATOM   13631 N N     . TRP A 1 3053 ? 125.474 183.078 148.687 1.00 84.50  ? 3053 TRP A N     1 
ATOM   13632 C CA    . TRP A 1 3053 ? 124.710 182.045 147.996 1.00 84.50  ? 3053 TRP A CA    1 
ATOM   13633 C C     . TRP A 1 3053 ? 125.588 180.844 147.671 1.00 84.50  ? 3053 TRP A C     1 
ATOM   13634 O O     . TRP A 1 3053 ? 125.152 179.693 147.799 1.00 84.50  ? 3053 TRP A O     1 
ATOM   13635 C CB    . TRP A 1 3053 ? 124.086 182.616 146.723 1.00 84.50  ? 3053 TRP A CB    1 
ATOM   13636 C CG    . TRP A 1 3053 ? 123.372 181.593 145.899 1.00 84.50  ? 3053 TRP A CG    1 
ATOM   13637 C CD1   . TRP A 1 3053 ? 122.159 181.029 146.164 1.00 84.50  ? 3053 TRP A CD1   1 
ATOM   13638 C CD2   . TRP A 1 3053 ? 123.829 181.005 144.676 1.00 84.50  ? 3053 TRP A CD2   1 
ATOM   13639 N NE1   . TRP A 1 3053 ? 121.830 180.129 145.181 1.00 84.50  ? 3053 TRP A NE1   1 
ATOM   13640 C CE2   . TRP A 1 3053 ? 122.840 180.095 144.255 1.00 84.50  ? 3053 TRP A CE2   1 
ATOM   13641 C CE3   . TRP A 1 3053 ? 124.978 181.161 143.895 1.00 84.50  ? 3053 TRP A CE3   1 
ATOM   13642 C CZ2   . TRP A 1 3053 ? 122.964 179.344 143.089 1.00 84.50  ? 3053 TRP A CZ2   1 
ATOM   13643 C CZ3   . TRP A 1 3053 ? 125.100 180.413 142.738 1.00 84.50  ? 3053 TRP A CZ3   1 
ATOM   13644 C CH2   . TRP A 1 3053 ? 124.099 179.517 142.345 1.00 84.50  ? 3053 TRP A CH2   1 
ATOM   13645 N N     . PHE A 1 3054 ? 126.826 181.097 147.240 1.00 82.26  ? 3054 PHE A N     1 
ATOM   13646 C CA    . PHE A 1 3054 ? 127.786 180.016 147.038 1.00 82.26  ? 3054 PHE A CA    1 
ATOM   13647 C C     . PHE A 1 3054 ? 127.957 179.192 148.307 1.00 82.26  ? 3054 PHE A C     1 
ATOM   13648 O O     . PHE A 1 3054 ? 127.952 177.955 148.271 1.00 82.26  ? 3054 PHE A O     1 
ATOM   13649 C CB    . PHE A 1 3054 ? 129.132 180.594 146.602 1.00 82.26  ? 3054 PHE A CB    1 
ATOM   13650 C CG    . PHE A 1 3054 ? 130.307 179.764 147.020 1.00 82.26  ? 3054 PHE A CG    1 
ATOM   13651 C CD1   . PHE A 1 3054 ? 130.643 178.616 146.326 1.00 82.26  ? 3054 PHE A CD1   1 
ATOM   13652 C CD2   . PHE A 1 3054 ? 131.068 180.123 148.121 1.00 82.26  ? 3054 PHE A CD2   1 
ATOM   13653 C CE1   . PHE A 1 3054 ? 131.723 177.850 146.712 1.00 82.26  ? 3054 PHE A CE1   1 
ATOM   13654 C CE2   . PHE A 1 3054 ? 132.144 179.357 148.515 1.00 82.26  ? 3054 PHE A CE2   1 
ATOM   13655 C CZ    . PHE A 1 3054 ? 132.470 178.217 147.811 1.00 82.26  ? 3054 PHE A CZ    1 
ATOM   13656 N N     . THR A 1 3055 ? 128.127 179.873 149.440 1.00 79.61  ? 3055 THR A N     1 
ATOM   13657 C CA    . THR A 1 3055 ? 128.337 179.179 150.706 1.00 79.61  ? 3055 THR A CA    1 
ATOM   13658 C C     . THR A 1 3055 ? 127.125 178.333 151.076 1.00 79.61  ? 3055 THR A C     1 
ATOM   13659 O O     . THR A 1 3055 ? 127.266 177.194 151.531 1.00 79.61  ? 3055 THR A O     1 
ATOM   13660 C CB    . THR A 1 3055 ? 128.651 180.189 151.810 1.00 79.61  ? 3055 THR A CB    1 
ATOM   13661 O OG1   . THR A 1 3055 ? 129.896 180.839 151.524 1.00 79.61  ? 3055 THR A OG1   1 
ATOM   13662 C CG2   . THR A 1 3055 ? 128.749 179.495 153.161 1.00 79.61  ? 3055 THR A CG2   1 
ATOM   13663 N N     . SER A 1 3056 ? 125.921 178.880 150.889 1.00 77.12  ? 3056 SER A N     1 
ATOM   13664 C CA    . SER A 1 3056 ? 124.714 178.116 151.196 1.00 77.12  ? 3056 SER A CA    1 
ATOM   13665 C C     . SER A 1 3056 ? 124.593 176.888 150.299 1.00 77.12  ? 3056 SER A C     1 
ATOM   13666 O O     . SER A 1 3056 ? 124.253 175.792 150.768 1.00 77.12  ? 3056 SER A O     1 
ATOM   13667 C CB    . SER A 1 3056 ? 123.478 179.004 151.061 1.00 77.12  ? 3056 SER A CB    1 
ATOM   13668 O OG    . SER A 1 3056 ? 123.523 179.761 149.865 1.00 77.12  ? 3056 SER A OG    1 
ATOM   13669 N N     . GLN A 1 3057 ? 124.878 177.049 149.005 1.00 73.25  ? 3057 GLN A N     1 
ATOM   13670 C CA    . GLN A 1 3057 ? 124.829 175.910 148.094 1.00 73.25  ? 3057 GLN A CA    1 
ATOM   13671 C C     . GLN A 1 3057 ? 125.831 174.840 148.506 1.00 73.25  ? 3057 GLN A C     1 
ATOM   13672 O O     . GLN A 1 3057 ? 125.536 173.642 148.448 1.00 73.25  ? 3057 GLN A O     1 
ATOM   13673 C CB    . GLN A 1 3057 ? 125.087 176.369 146.658 1.00 73.25  ? 3057 GLN A CB    1 
ATOM   13674 C CG    . GLN A 1 3057 ? 124.007 177.275 146.100 1.00 73.25  ? 3057 GLN A CG    1 
ATOM   13675 C CD    . GLN A 1 3057 ? 122.625 176.672 146.232 1.00 73.25  ? 3057 GLN A CD    1 
ATOM   13676 O OE1   . GLN A 1 3057 ? 121.750 177.235 146.889 1.00 73.25  ? 3057 GLN A OE1   1 
ATOM   13677 N NE2   . GLN A 1 3057 ? 122.421 175.517 145.610 1.00 73.25  ? 3057 GLN A NE2   1 
ATOM   13678 N N     . VAL A 1 3058 ? 127.027 175.256 148.929 1.00 67.70  ? 3058 VAL A N     1 
ATOM   13679 C CA    . VAL A 1 3058 ? 128.034 174.284 149.346 1.00 67.70  ? 3058 VAL A CA    1 
ATOM   13680 C C     . VAL A 1 3058 ? 127.595 173.561 150.614 1.00 67.70  ? 3058 VAL A C     1 
ATOM   13681 O O     . VAL A 1 3058 ? 127.701 172.333 150.709 1.00 67.70  ? 3058 VAL A O     1 
ATOM   13682 C CB    . VAL A 1 3058 ? 129.402 174.964 149.526 1.00 67.70  ? 3058 VAL A CB    1 
ATOM   13683 C CG1   . VAL A 1 3058 ? 130.346 174.045 150.274 1.00 67.70  ? 3058 VAL A CG1   1 
ATOM   13684 C CG2   . VAL A 1 3058 ? 129.980 175.320 148.176 1.00 67.70  ? 3058 VAL A CG2   1 
ATOM   13685 N N     . ILE A 1 3059 ? 127.089 174.301 151.606 1.00 69.04  ? 3059 ILE A N     1 
ATOM   13686 C CA    . ILE A 1 3059 ? 126.646 173.654 152.838 1.00 69.04  ? 3059 ILE A CA    1 
ATOM   13687 C C     . ILE A 1 3059 ? 125.430 172.772 152.623 1.00 69.04  ? 3059 ILE A C     1 
ATOM   13688 O O     . ILE A 1 3059 ? 125.150 171.912 153.465 1.00 69.04  ? 3059 ILE A O     1 
ATOM   13689 C CB    . ILE A 1 3059 ? 126.316 174.652 153.971 1.00 69.04  ? 3059 ILE A CB    1 
ATOM   13690 C CG1   . ILE A 1 3059 ? 124.991 175.369 153.710 1.00 69.04  ? 3059 ILE A CG1   1 
ATOM   13691 C CG2   . ILE A 1 3059 ? 127.438 175.645 154.172 1.00 69.04  ? 3059 ILE A CG2   1 
ATOM   13692 C CD1   . ILE A 1 3059 ? 124.467 176.131 154.907 1.00 69.04  ? 3059 ILE A CD1   1 
ATOM   13693 N N     . ARG A 1 3060 ? 124.699 172.954 151.524 1.00 70.20  ? 3060 ARG A N     1 
ATOM   13694 C CA    . ARG A 1 3060 ? 123.562 172.090 151.238 1.00 70.20  ? 3060 ARG A CA    1 
ATOM   13695 C C     . ARG A 1 3060 ? 123.871 170.964 150.258 1.00 70.20  ? 3060 ARG A C     1 
ATOM   13696 O O     . ARG A 1 3060 ? 123.258 169.899 150.359 1.00 70.20  ? 3060 ARG A O     1 
ATOM   13697 C CB    . ARG A 1 3060 ? 122.380 172.920 150.706 1.00 70.20  ? 3060 ARG A CB    1 
ATOM   13698 C CG    . ARG A 1 3060 ? 121.132 172.106 150.394 1.00 70.20  ? 3060 ARG A CG    1 
ATOM   13699 C CD    . ARG A 1 3060 ? 119.917 172.993 150.175 1.00 70.20  ? 3060 ARG A CD    1 
ATOM   13700 N NE    . ARG A 1 3060 ? 120.238 174.203 149.429 1.00 70.20  ? 3060 ARG A NE    1 
ATOM   13701 C CZ    . ARG A 1 3060 ? 119.687 174.533 148.269 1.00 70.20  ? 3060 ARG A CZ    1 
ATOM   13702 N NH1   . ARG A 1 3060 ? 118.785 173.759 147.687 1.00 70.20  ? 3060 ARG A NH1   1 
ATOM   13703 N NH2   . ARG A 1 3060 ? 120.048 175.669 147.679 1.00 70.20  ? 3060 ARG A NH2   1 
ATOM   13704 N N     . ASN A 1 3061 ? 124.818 171.151 149.338 1.00 65.18  ? 3061 ASN A N     1 
ATOM   13705 C CA    . ASN A 1 3061 ? 125.082 170.165 148.293 1.00 65.18  ? 3061 ASN A CA    1 
ATOM   13706 C C     . ASN A 1 3061 ? 126.324 169.323 148.569 1.00 65.18  ? 3061 ASN A C     1 
ATOM   13707 O O     . ASN A 1 3061 ? 126.256 168.091 148.541 1.00 65.18  ? 3061 ASN A O     1 
ATOM   13708 C CB    . ASN A 1 3061 ? 125.211 170.864 146.933 1.00 65.18  ? 3061 ASN A CB    1 
ATOM   13709 C CG    . ASN A 1 3061 ? 123.959 171.625 146.550 1.00 65.18  ? 3061 ASN A CG    1 
ATOM   13710 O OD1   . ASN A 1 3061 ? 122.987 171.661 147.303 1.00 65.18  ? 3061 ASN A OD1   1 
ATOM   13711 N ND2   . ASN A 1 3061 ? 123.976 172.236 145.372 1.00 65.18  ? 3061 ASN A ND2   1 
ATOM   13712 N N     . LEU A 1 3062 ? 127.463 169.964 148.826 1.00 58.29  ? 3062 LEU A N     1 
ATOM   13713 C CA    . LEU A 1 3062 ? 128.732 169.246 148.895 1.00 58.29  ? 3062 LEU A CA    1 
ATOM   13714 C C     . LEU A 1 3062 ? 128.757 168.279 150.073 1.00 58.29  ? 3062 LEU A C     1 
ATOM   13715 O O     . LEU A 1 3062 ? 128.287 168.598 151.167 1.00 58.29  ? 3062 LEU A O     1 
ATOM   13716 C CB    . LEU A 1 3062 ? 129.890 170.241 149.002 1.00 58.29  ? 3062 LEU A CB    1 
ATOM   13717 C CG    . LEU A 1 3062 ? 131.321 169.699 149.078 1.00 58.29  ? 3062 LEU A CG    1 
ATOM   13718 C CD1   . LEU A 1 3062 ? 132.256 170.633 148.344 1.00 58.29  ? 3062 LEU A CD1   1 
ATOM   13719 C CD2   . LEU A 1 3062 ? 131.783 169.529 150.517 1.00 58.29  ? 3062 LEU A CD2   1 
ATOM   13720 N N     . HIS A 1 3063 ? 129.319 167.079 149.838 1.00 56.04  ? 3063 HIS A N     1 
ATOM   13721 C CA    . HIS A 1 3063 ? 129.554 166.086 150.883 1.00 56.04  ? 3063 HIS A CA    1 
ATOM   13722 C C     . HIS A 1 3063 ? 130.895 165.398 150.611 1.00 56.04  ? 3063 HIS A C     1 
ATOM   13723 O O     . HIS A 1 3063 ? 130.987 164.410 149.887 1.00 56.04  ? 3063 HIS A O     1 
ATOM   13724 C CB    . HIS A 1 3063 ? 128.422 165.059 150.961 1.00 56.04  ? 3063 HIS A CB    1 
ATOM   13725 C CG    . HIS A 1 3063 ? 127.058 165.665 151.030 1.00 56.04  ? 3063 HIS A CG    1 
ATOM   13726 N ND1   . HIS A 1 3063 ? 126.625 166.402 152.111 1.00 56.04  ? 3063 HIS A ND1   1 
ATOM   13727 C CD2   . HIS A 1 3063 ? 126.024 165.634 150.157 1.00 56.04  ? 3063 HIS A CD2   1 
ATOM   13728 C CE1   . HIS A 1 3063 ? 125.386 166.806 151.896 1.00 56.04  ? 3063 HIS A CE1   1 
ATOM   13729 N NE2   . HIS A 1 3063 ? 124.998 166.353 150.718 1.00 56.04  ? 3063 HIS A NE2   1 
ATOM   13730 N N     . VAL A 1 3064 ? 131.959 165.927 151.215 1.00 53.79  ? 3064 VAL A N     1 
ATOM   13731 C CA    . VAL A 1 3064 ? 133.261 165.277 151.127 1.00 53.79  ? 3064 VAL A CA    1 
ATOM   13732 C C     . VAL A 1 3064 ? 133.285 164.053 152.032 1.00 53.79  ? 3064 VAL A C     1 
ATOM   13733 O O     . VAL A 1 3064 ? 132.836 164.097 153.183 1.00 53.79  ? 3064 VAL A O     1 
ATOM   13734 C CB    . VAL A 1 3064 ? 134.381 166.273 151.467 1.00 53.79  ? 3064 VAL A CB    1 
ATOM   13735 C CG1   . VAL A 1 3064 ? 134.284 166.734 152.897 1.00 53.79  ? 3064 VAL A CG1   1 
ATOM   13736 C CG2   . VAL A 1 3064 ? 135.725 165.621 151.269 1.00 53.79  ? 3064 VAL A CG2   1 
ATOM   13737 N N     . VAL A 1 3065 ? 133.778 162.938 151.500 1.00 54.50  ? 3065 VAL A N     1 
ATOM   13738 C CA    . VAL A 1 3065 ? 133.972 161.718 152.275 1.00 54.50  ? 3065 VAL A CA    1 
ATOM   13739 C C     . VAL A 1 3065 ? 135.453 161.374 152.259 1.00 54.50  ? 3065 VAL A C     1 
ATOM   13740 O O     . VAL A 1 3065 ? 136.096 161.403 151.203 1.00 54.50  ? 3065 VAL A O     1 
ATOM   13741 C CB    . VAL A 1 3065 ? 133.121 160.550 151.746 1.00 54.50  ? 3065 VAL A CB    1 
ATOM   13742 C CG1   . VAL A 1 3065 ? 131.654 160.812 152.014 1.00 54.50  ? 3065 VAL A CG1   1 
ATOM   13743 C CG2   . VAL A 1 3065 ? 133.346 160.355 150.271 1.00 54.50  ? 3065 VAL A CG2   1 
ATOM   13744 N N     . PHE A 1 3066 ? 135.994 161.068 153.432 1.00 62.52  ? 3066 PHE A N     1 
ATOM   13745 C CA    . PHE A 1 3066 ? 137.424 160.894 153.609 1.00 62.52  ? 3066 PHE A CA    1 
ATOM   13746 C C     . PHE A 1 3066 ? 137.662 159.685 154.503 1.00 62.52  ? 3066 PHE A C     1 
ATOM   13747 O O     . PHE A 1 3066 ? 136.861 159.390 155.393 1.00 62.52  ? 3066 PHE A O     1 
ATOM   13748 C CB    . PHE A 1 3066 ? 138.029 162.181 154.185 1.00 62.52  ? 3066 PHE A CB    1 
ATOM   13749 C CG    . PHE A 1 3066 ? 139.509 162.139 154.366 1.00 62.52  ? 3066 PHE A CG    1 
ATOM   13750 C CD1   . PHE A 1 3066 ? 140.343 162.249 153.272 1.00 62.52  ? 3066 PHE A CD1   1 
ATOM   13751 C CD2   . PHE A 1 3066 ? 140.072 162.072 155.626 1.00 62.52  ? 3066 PHE A CD2   1 
ATOM   13752 C CE1   . PHE A 1 3066 ? 141.710 162.234 153.424 1.00 62.52  ? 3066 PHE A CE1   1 
ATOM   13753 C CE2   . PHE A 1 3066 ? 141.445 162.070 155.781 1.00 62.52  ? 3066 PHE A CE2   1 
ATOM   13754 C CZ    . PHE A 1 3066 ? 142.262 162.143 154.682 1.00 62.52  ? 3066 PHE A CZ    1 
ATOM   13755 N N     . THR A 1 3067 ? 138.750 158.961 154.239 1.00 58.31  ? 3067 THR A N     1 
ATOM   13756 C CA    . THR A 1 3067 ? 138.969 157.662 154.862 1.00 58.31  ? 3067 THR A CA    1 
ATOM   13757 C C     . THR A 1 3067 ? 140.368 157.552 155.454 1.00 58.31  ? 3067 THR A C     1 
ATOM   13758 O O     . THR A 1 3067 ? 141.321 158.136 154.931 1.00 58.31  ? 3067 THR A O     1 
ATOM   13759 C CB    . THR A 1 3067 ? 138.756 156.522 153.854 1.00 58.31  ? 3067 THR A CB    1 
ATOM   13760 O OG1   . THR A 1 3067 ? 139.688 156.651 152.777 1.00 58.31  ? 3067 THR A OG1   1 
ATOM   13761 C CG2   . THR A 1 3067 ? 137.336 156.539 153.299 1.00 58.31  ? 3067 THR A CG2   1 
ATOM   13762 N N     . MET A 1 3068 ? 140.482 156.795 156.548 1.00 58.20  ? 3068 MET A N     1 
ATOM   13763 C CA    . MET A 1 3068 ? 141.777 156.390 157.079 1.00 58.20  ? 3068 MET A CA    1 
ATOM   13764 C C     . MET A 1 3068 ? 141.693 154.932 157.497 1.00 58.20  ? 3068 MET A C     1 
ATOM   13765 O O     . MET A 1 3068 ? 140.611 154.340 157.529 1.00 58.20  ? 3068 MET A O     1 
ATOM   13766 C CB    . MET A 1 3068 ? 142.234 157.186 158.308 1.00 58.20  ? 3068 MET A CB    1 
ATOM   13767 C CG    . MET A 1 3068 ? 142.727 158.584 158.068 1.00 58.20  ? 3068 MET A CG    1 
ATOM   13768 S SD    . MET A 1 3068 ? 141.308 159.653 157.862 1.00 58.20  ? 3068 MET A SD    1 
ATOM   13769 C CE    . MET A 1 3068 ? 140.767 159.748 159.567 1.00 58.20  ? 3068 MET A CE    1 
ATOM   13770 N N     . ASN A 1 3069 ? 142.847 154.368 157.817 1.00 50.50  ? 3069 ASN A N     1 
ATOM   13771 C CA    . ASN A 1 3069 ? 142.921 153.180 158.648 1.00 50.50  ? 3069 ASN A CA    1 
ATOM   13772 C C     . ASN A 1 3069 ? 142.971 153.585 160.114 1.00 50.50  ? 3069 ASN A C     1 
ATOM   13773 O O     . ASN A 1 3069 ? 143.424 154.683 160.449 1.00 50.50  ? 3069 ASN A O     1 
ATOM   13774 C CB    . ASN A 1 3069 ? 144.154 152.360 158.283 1.00 50.50  ? 3069 ASN A CB    1 
ATOM   13775 C CG    . ASN A 1 3069 ? 144.084 151.803 156.881 1.00 50.50  ? 3069 ASN A CG    1 
ATOM   13776 O OD1   . ASN A 1 3069 ? 144.865 152.181 156.010 1.00 50.50  ? 3069 ASN A OD1   1 
ATOM   13777 N ND2   . ASN A 1 3069 ? 143.138 150.903 156.651 1.00 50.50  ? 3069 ASN A ND2   1 
ATOM   13778 N N     . PRO A 1 3070 ? 142.504 152.722 161.026 1.00 46.00  ? 3070 PRO A N     1 
ATOM   13779 C CA    . PRO A 1 3070 ? 142.530 153.086 162.447 1.00 46.00  ? 3070 PRO A CA    1 
ATOM   13780 C C     . PRO A 1 3070 ? 143.946 153.202 163.004 1.00 46.00  ? 3070 PRO A C     1 
ATOM   13781 O O     . PRO A 1 3070 ? 144.198 154.108 163.798 1.00 46.00  ? 3070 PRO A O     1 
ATOM   13782 C CB    . PRO A 1 3070 ? 141.776 151.936 163.117 1.00 46.00  ? 3070 PRO A CB    1 
ATOM   13783 C CG    . PRO A 1 3070 ? 141.931 150.790 162.179 1.00 46.00  ? 3070 PRO A CG    1 
ATOM   13784 C CD    . PRO A 1 3070 ? 141.906 151.394 160.809 1.00 46.00  ? 3070 PRO A CD    1 
ATOM   13785 N N     . SER A 1 3082 ? 143.204 163.850 165.180 1.00 40.15  ? 3082 SER A N     1 
ATOM   13786 C CA    . SER A 1 3082 ? 142.838 165.233 165.460 1.00 40.15  ? 3082 SER A CA    1 
ATOM   13787 C C     . SER A 1 3082 ? 141.516 165.305 166.216 1.00 40.15  ? 3082 SER A C     1 
ATOM   13788 O O     . SER A 1 3082 ? 140.501 164.791 165.748 1.00 40.15  ? 3082 SER A O     1 
ATOM   13789 C CB    . SER A 1 3082 ? 142.748 166.037 164.162 1.00 40.15  ? 3082 SER A CB    1 
ATOM   13790 O OG    . SER A 1 3082 ? 142.421 167.391 164.422 1.00 40.15  ? 3082 SER A OG    1 
ATOM   13791 N N     . PRO A 1 3083 ? 141.527 165.943 167.386 1.00 40.82  ? 3083 PRO A N     1 
ATOM   13792 C CA    . PRO A 1 3083 ? 140.307 166.062 168.195 1.00 40.82  ? 3083 PRO A CA    1 
ATOM   13793 C C     . PRO A 1 3083 ? 139.237 166.966 167.602 1.00 40.82  ? 3083 PRO A C     1 
ATOM   13794 O O     . PRO A 1 3083 ? 138.092 166.915 168.063 1.00 40.82  ? 3083 PRO A O     1 
ATOM   13795 C CB    . PRO A 1 3083 ? 140.834 166.652 169.511 1.00 40.82  ? 3083 PRO A CB    1 
ATOM   13796 C CG    . PRO A 1 3083 ? 142.056 167.399 169.124 1.00 40.82  ? 3083 PRO A CG    1 
ATOM   13797 C CD    . PRO A 1 3083 ? 142.678 166.621 168.006 1.00 40.82  ? 3083 PRO A CD    1 
ATOM   13798 N N     . ALA A 1 3084 ? 139.574 167.783 166.606 1.00 44.72  ? 3084 ALA A N     1 
ATOM   13799 C CA    . ALA A 1 3084 ? 138.614 168.654 165.944 1.00 44.72  ? 3084 ALA A CA    1 
ATOM   13800 C C     . ALA A 1 3084 ? 137.956 167.988 164.747 1.00 44.72  ? 3084 ALA A C     1 
ATOM   13801 O O     . ALA A 1 3084 ? 136.727 167.901 164.691 1.00 44.72  ? 3084 ALA A O     1 
ATOM   13802 C CB    . ALA A 1 3084 ? 139.297 169.958 165.505 1.00 44.72  ? 3084 ALA A CB    1 
ATOM   13803 N N     . LEU A 1 3085 ? 138.751 167.489 163.796 1.00 44.27  ? 3085 LEU A N     1 
ATOM   13804 C CA    . LEU A 1 3085 ? 138.204 166.765 162.653 1.00 44.27  ? 3085 LEU A CA    1 
ATOM   13805 C C     . LEU A 1 3085 ? 137.335 165.592 163.077 1.00 44.27  ? 3085 LEU A C     1 
ATOM   13806 O O     . LEU A 1 3085 ? 136.395 165.234 162.359 1.00 44.27  ? 3085 LEU A O     1 
ATOM   13807 C CB    . LEU A 1 3085 ? 139.340 166.267 161.757 1.00 44.27  ? 3085 LEU A CB    1 
ATOM   13808 C CG    . LEU A 1 3085 ? 138.949 165.464 160.515 1.00 44.27  ? 3085 LEU A CG    1 
ATOM   13809 C CD1   . LEU A 1 3085 ? 138.120 166.299 159.555 1.00 44.27  ? 3085 LEU A CD1   1 
ATOM   13810 C CD2   . LEU A 1 3085 ? 140.184 164.909 159.826 1.00 44.27  ? 3085 LEU A CD2   1 
ATOM   13811 N N     . PHE A 1 3086 ? 137.615 164.999 164.232 1.00 44.13  ? 3086 PHE A N     1 
ATOM   13812 C CA    . PHE A 1 3086 ? 136.855 163.869 164.740 1.00 44.13  ? 3086 PHE A CA    1 
ATOM   13813 C C     . PHE A 1 3086 ? 135.578 164.304 165.447 1.00 44.13  ? 3086 PHE A C     1 
ATOM   13814 O O     . PHE A 1 3086 ? 134.824 163.452 165.927 1.00 44.13  ? 3086 PHE A O     1 
ATOM   13815 C CB    . PHE A 1 3086 ? 137.735 163.036 165.676 1.00 44.13  ? 3086 PHE A CB    1 
ATOM   13816 C CG    . PHE A 1 3086 ? 138.737 162.168 164.956 1.00 44.13  ? 3086 PHE A CG    1 
ATOM   13817 C CD1   . PHE A 1 3086 ? 139.308 161.080 165.587 1.00 44.13  ? 3086 PHE A CD1   1 
ATOM   13818 C CD2   . PHE A 1 3086 ? 139.095 162.432 163.643 1.00 44.13  ? 3086 PHE A CD2   1 
ATOM   13819 C CE1   . PHE A 1 3086 ? 140.222 160.278 164.932 1.00 44.13  ? 3086 PHE A CE1   1 
ATOM   13820 C CE2   . PHE A 1 3086 ? 140.009 161.636 162.982 1.00 44.13  ? 3086 PHE A CE2   1 
ATOM   13821 C CZ    . PHE A 1 3086 ? 140.573 160.557 163.628 1.00 44.13  ? 3086 PHE A CZ    1 
ATOM   13822 N N     . ASN A 1 3087 ? 135.326 165.611 165.526 1.00 43.09  ? 3087 ASN A N     1 
ATOM   13823 C CA    . ASN A 1 3087 ? 134.056 166.141 166.006 1.00 43.09  ? 3087 ASN A CA    1 
ATOM   13824 C C     . ASN A 1 3087 ? 133.279 166.908 164.947 1.00 43.09  ? 3087 ASN A C     1 
ATOM   13825 O O     . ASN A 1 3087 ? 132.054 167.020 165.072 1.00 43.09  ? 3087 ASN A O     1 
ATOM   13826 C CB    . ASN A 1 3087 ? 134.275 167.058 167.219 1.00 43.09  ? 3087 ASN A CB    1 
ATOM   13827 C CG    . ASN A 1 3087 ? 133.016 167.247 168.043 1.00 43.09  ? 3087 ASN A CG    1 
ATOM   13828 O OD1   . ASN A 1 3087 ? 132.001 166.593 167.807 1.00 43.09  ? 3087 ASN A OD1   1 
ATOM   13829 N ND2   . ASN A 1 3087 ? 133.075 168.149 169.014 1.00 43.09  ? 3087 ASN A ND2   1 
ATOM   13830 N N     . ARG A 1 3088 ? 133.937 167.435 163.915 1.00 48.63  ? 3088 ARG A N     1 
ATOM   13831 C CA    . ARG A 1 3088 ? 133.255 168.064 162.793 1.00 48.63  ? 3088 ARG A CA    1 
ATOM   13832 C C     . ARG A 1 3088 ? 132.709 167.051 161.797 1.00 48.63  ? 3088 ARG A C     1 
ATOM   13833 O O     . ARG A 1 3088 ? 132.008 167.442 160.858 1.00 48.63  ? 3088 ARG A O     1 
ATOM   13834 C CB    . ARG A 1 3088 ? 134.207 169.023 162.069 1.00 48.63  ? 3088 ARG A CB    1 
ATOM   13835 C CG    . ARG A 1 3088 ? 135.117 169.816 162.984 1.00 48.63  ? 3088 ARG A CG    1 
ATOM   13836 C CD    . ARG A 1 3088 ? 134.555 171.181 163.319 1.00 48.63  ? 3088 ARG A CD    1 
ATOM   13837 N NE    . ARG A 1 3088 ? 135.458 171.926 164.188 1.00 48.63  ? 3088 ARG A NE    1 
ATOM   13838 C CZ    . ARG A 1 3088 ? 136.211 172.945 163.797 1.00 48.63  ? 3088 ARG A CZ    1 
ATOM   13839 N NH1   . ARG A 1 3088 ? 136.230 173.346 162.537 1.00 48.63  ? 3088 ARG A NH1   1 
ATOM   13840 N NH2   . ARG A 1 3088 ? 136.971 173.570 164.691 1.00 48.63  ? 3088 ARG A NH2   1 
ATOM   13841 N N     . CYS A 1 3089 ? 133.017 165.769 161.978 1.00 45.44  ? 3089 CYS A N     1 
ATOM   13842 C CA    . CYS A 1 3089 ? 132.577 164.699 161.097 1.00 45.44  ? 3089 CYS A CA    1 
ATOM   13843 C C     . CYS A 1 3089 ? 131.605 163.793 161.835 1.00 45.44  ? 3089 CYS A C     1 
ATOM   13844 O O     . CYS A 1 3089 ? 131.653 163.689 163.064 1.00 45.44  ? 3089 CYS A O     1 
ATOM   13845 C CB    . CYS A 1 3089 ? 133.757 163.851 160.612 1.00 45.44  ? 3089 CYS A CB    1 
ATOM   13846 S SG    . CYS A 1 3089 ? 134.836 164.608 159.398 1.00 45.44  ? 3089 CYS A SG    1 
ATOM   13847 N N     . VAL A 1 3090 ? 130.724 163.138 161.083 1.00 47.28  ? 3090 VAL A N     1 
ATOM   13848 C CA    . VAL A 1 3090 ? 130.012 161.987 161.623 1.00 47.28  ? 3090 VAL A CA    1 
ATOM   13849 C C     . VAL A 1 3090 ? 130.855 160.749 161.352 1.00 47.28  ? 3090 VAL A C     1 
ATOM   13850 O O     . VAL A 1 3090 ? 130.924 160.262 160.217 1.00 47.28  ? 3090 VAL A O     1 
ATOM   13851 C CB    . VAL A 1 3090 ? 128.612 161.858 161.012 1.00 47.28  ? 3090 VAL A CB    1 
ATOM   13852 C CG1   . VAL A 1 3090 ? 127.970 160.551 161.447 1.00 47.28  ? 3090 VAL A CG1   1 
ATOM   13853 C CG2   . VAL A 1 3090 ? 127.745 163.028 161.431 1.00 47.28  ? 3090 VAL A CG2   1 
ATOM   13854 N N     . LEU A 1 3091 ? 131.513 160.243 162.389 1.00 45.49  ? 3091 LEU A N     1 
ATOM   13855 C CA    . LEU A 1 3091 ? 132.450 159.139 162.249 1.00 45.49  ? 3091 LEU A CA    1 
ATOM   13856 C C     . LEU A 1 3091 ? 131.701 157.819 162.329 1.00 45.49  ? 3091 LEU A C     1 
ATOM   13857 O O     . LEU A 1 3091 ? 131.002 157.552 163.312 1.00 45.49  ? 3091 LEU A O     1 
ATOM   13858 C CB    . LEU A 1 3091 ? 133.538 159.190 163.322 1.00 45.49  ? 3091 LEU A CB    1 
ATOM   13859 C CG    . LEU A 1 3091 ? 134.725 160.107 163.026 1.00 45.49  ? 3091 LEU A CG    1 
ATOM   13860 C CD1   . LEU A 1 3091 ? 134.368 161.555 163.299 1.00 45.49  ? 3091 LEU A CD1   1 
ATOM   13861 C CD2   . LEU A 1 3091 ? 135.945 159.688 163.824 1.00 45.49  ? 3091 LEU A CD2   1 
ATOM   13862 N N     . ASN A 1 3092 ? 131.850 157.004 161.294 1.00 43.76  ? 3092 ASN A N     1 
ATOM   13863 C CA    . ASN A 1 3092 ? 131.257 155.680 161.238 1.00 43.76  ? 3092 ASN A CA    1 
ATOM   13864 C C     . ASN A 1 3092 ? 132.368 154.641 161.235 1.00 43.76  ? 3092 ASN A C     1 
ATOM   13865 O O     . ASN A 1 3092 ? 133.244 154.658 160.364 1.00 43.76  ? 3092 ASN A O     1 
ATOM   13866 C CB    . ASN A 1 3092 ? 130.376 155.530 159.996 1.00 43.76  ? 3092 ASN A CB    1 
ATOM   13867 C CG    . ASN A 1 3092 ? 129.835 154.130 159.833 1.00 43.76  ? 3092 ASN A CG    1 
ATOM   13868 O OD1   . ASN A 1 3092 ? 129.178 153.596 160.725 1.00 43.76  ? 3092 ASN A OD1   1 
ATOM   13869 N ND2   . ASN A 1 3092 ? 130.108 153.524 158.685 1.00 43.76  ? 3092 ASN A ND2   1 
ATOM   13870 N N     . TRP A 1 3093 ? 132.329 153.740 162.214 1.00 46.64  ? 3093 TRP A N     1 
ATOM   13871 C CA    . TRP A 1 3093 ? 133.338 152.695 162.361 1.00 46.64  ? 3093 TRP A CA    1 
ATOM   13872 C C     . TRP A 1 3093 ? 132.988 151.566 161.402 1.00 46.64  ? 3093 TRP A C     1 
ATOM   13873 O O     . TRP A 1 3093 ? 132.048 150.804 161.638 1.00 46.64  ? 3093 TRP A O     1 
ATOM   13874 C CB    . TRP A 1 3093 ? 133.408 152.195 163.799 1.00 46.64  ? 3093 TRP A CB    1 
ATOM   13875 C CG    . TRP A 1 3093 ? 134.434 151.121 164.005 1.00 46.64  ? 3093 TRP A CG    1 
ATOM   13876 C CD1   . TRP A 1 3093 ? 134.216 149.864 164.487 1.00 46.64  ? 3093 TRP A CD1   1 
ATOM   13877 C CD2   . TRP A 1 3093 ? 135.839 151.210 163.740 1.00 46.64  ? 3093 TRP A CD2   1 
ATOM   13878 N NE1   . TRP A 1 3093 ? 135.396 149.164 164.537 1.00 46.64  ? 3093 TRP A NE1   1 
ATOM   13879 C CE2   . TRP A 1 3093 ? 136.407 149.968 164.084 1.00 46.64  ? 3093 TRP A CE2   1 
ATOM   13880 C CE3   . TRP A 1 3093 ? 136.671 152.217 163.245 1.00 46.64  ? 3093 TRP A CE3   1 
ATOM   13881 C CZ2   . TRP A 1 3093 ? 137.767 149.708 163.948 1.00 46.64  ? 3093 TRP A CZ2   1 
ATOM   13882 C CZ3   . TRP A 1 3093 ? 138.019 151.957 163.112 1.00 46.64  ? 3093 TRP A CZ3   1 
ATOM   13883 C CH2   . TRP A 1 3093 ? 138.554 150.713 163.462 1.00 46.64  ? 3093 TRP A CH2   1 
ATOM   13884 N N     . PHE A 1 3094 ? 133.748 151.462 160.313 1.00 41.73  ? 3094 PHE A N     1 
ATOM   13885 C CA    . PHE A 1 3094 ? 133.513 150.425 159.315 1.00 41.73  ? 3094 PHE A CA    1 
ATOM   13886 C C     . PHE A 1 3094 ? 134.548 149.330 159.556 1.00 41.73  ? 3094 PHE A C     1 
ATOM   13887 O O     . PHE A 1 3094 ? 135.570 149.227 158.875 1.00 41.73  ? 3094 PHE A O     1 
ATOM   13888 C CB    . PHE A 1 3094 ? 133.602 151.003 157.909 1.00 41.73  ? 3094 PHE A CB    1 
ATOM   13889 C CG    . PHE A 1 3094 ? 133.314 150.010 156.828 1.00 41.73  ? 3094 PHE A CG    1 
ATOM   13890 C CD1   . PHE A 1 3094 ? 132.015 149.627 156.568 1.00 41.73  ? 3094 PHE A CD1   1 
ATOM   13891 C CD2   . PHE A 1 3094 ? 134.331 149.443 156.088 1.00 41.73  ? 3094 PHE A CD2   1 
ATOM   13892 C CE1   . PHE A 1 3094 ? 131.728 148.714 155.580 1.00 41.73  ? 3094 PHE A CE1   1 
ATOM   13893 C CE2   . PHE A 1 3094 ? 134.049 148.531 155.097 1.00 41.73  ? 3094 PHE A CE2   1 
ATOM   13894 C CZ    . PHE A 1 3094 ? 132.747 148.162 154.846 1.00 41.73  ? 3094 PHE A CZ    1 
ATOM   13895 N N     . GLY A 1 3095 ? 134.274 148.501 160.557 1.00 37.08  ? 3095 GLY A N     1 
ATOM   13896 C CA    . GLY A 1 3095 ? 135.249 147.530 161.006 1.00 37.08  ? 3095 GLY A CA    1 
ATOM   13897 C C     . GLY A 1 3095 ? 135.483 146.418 160.002 1.00 37.08  ? 3095 GLY A C     1 
ATOM   13898 O O     . GLY A 1 3095 ? 134.828 146.311 158.965 1.00 37.08  ? 3095 GLY A O     1 
ATOM   13899 N N     . ASP A 1 3096 ? 136.459 145.574 160.328 1.00 32.44  ? 3096 ASP A N     1 
ATOM   13900 C CA    . ASP A 1 3096 ? 136.754 144.416 159.498 1.00 32.44  ? 3096 ASP A CA    1 
ATOM   13901 C C     . ASP A 1 3096 ? 135.556 143.475 159.475 1.00 32.44  ? 3096 ASP A C     1 
ATOM   13902 O O     . ASP A 1 3096 ? 134.774 143.405 160.427 1.00 32.44  ? 3096 ASP A O     1 
ATOM   13903 C CB    . ASP A 1 3096 ? 137.995 143.688 160.021 1.00 32.44  ? 3096 ASP A CB    1 
ATOM   13904 C CG    . ASP A 1 3096 ? 138.446 142.557 159.109 1.00 32.44  ? 3096 ASP A CG    1 
ATOM   13905 O OD1   . ASP A 1 3096 ? 137.819 142.343 158.051 1.00 32.44  ? 3096 ASP A OD1   1 
ATOM   13906 O OD2   . ASP A 1 3096 ? 139.435 141.876 159.456 1.00 32.44  ? 3096 ASP A OD2   1 
ATOM   13907 N N     . TRP A 1 3097 ? 135.414 142.754 158.364 1.00 28.80  ? 3097 TRP A N     1 
ATOM   13908 C CA    . TRP A 1 3097 ? 134.269 141.875 158.176 1.00 28.80  ? 3097 TRP A CA    1 
ATOM   13909 C C     . TRP A 1 3097 ? 134.210 140.816 159.267 1.00 28.80  ? 3097 TRP A C     1 
ATOM   13910 O O     . TRP A 1 3097 ? 135.215 140.181 159.596 1.00 28.80  ? 3097 TRP A O     1 
ATOM   13911 C CB    . TRP A 1 3097 ? 134.339 141.205 156.805 1.00 28.80  ? 3097 TRP A CB    1 
ATOM   13912 C CG    . TRP A 1 3097 ? 134.254 142.160 155.663 1.00 28.80  ? 3097 TRP A CG    1 
ATOM   13913 C CD1   . TRP A 1 3097 ? 133.997 143.496 155.728 1.00 28.80  ? 3097 TRP A CD1   1 
ATOM   13914 C CD2   . TRP A 1 3097 ? 134.426 141.851 154.279 1.00 28.80  ? 3097 TRP A CD2   1 
ATOM   13915 N NE1   . TRP A 1 3097 ? 133.999 144.040 154.468 1.00 28.80  ? 3097 TRP A NE1   1 
ATOM   13916 C CE2   . TRP A 1 3097 ? 134.260 143.048 153.560 1.00 28.80  ? 3097 TRP A CE2   1 
ATOM   13917 C CE3   . TRP A 1 3097 ? 134.705 140.676 153.577 1.00 28.80  ? 3097 TRP A CE3   1 
ATOM   13918 C CZ2   . TRP A 1 3097 ? 134.363 143.105 152.176 1.00 28.80  ? 3097 TRP A CZ2   1 
ATOM   13919 C CZ3   . TRP A 1 3097 ? 134.806 140.735 152.206 1.00 28.80  ? 3097 TRP A CZ3   1 
ATOM   13920 C CH2   . TRP A 1 3097 ? 134.636 141.940 151.518 1.00 28.80  ? 3097 TRP A CH2   1 
ATOM   13921 N N     . SER A 1 3098 ? 133.021 140.630 159.826 1.00 29.61  ? 3098 SER A N     1 
ATOM   13922 C CA    . SER A 1 3098 ? 132.806 139.628 160.855 1.00 29.61  ? 3098 SER A CA    1 
ATOM   13923 C C     . SER A 1 3098 ? 132.731 138.239 160.231 1.00 29.61  ? 3098 SER A C     1 
ATOM   13924 O O     . SER A 1 3098 ? 132.842 138.069 159.015 1.00 29.61  ? 3098 SER A O     1 
ATOM   13925 C CB    . SER A 1 3098 ? 131.528 139.923 161.639 1.00 29.61  ? 3098 SER A CB    1 
ATOM   13926 O OG    . SER A 1 3098 ? 131.351 138.994 162.694 1.00 29.61  ? 3098 SER A OG    1 
ATOM   13927 N N     . THR A 1 3099 ? 132.541 137.238 161.089 1.00 30.78  ? 3099 THR A N     1 
ATOM   13928 C CA    . THR A 1 3099 ? 132.482 135.851 160.647 1.00 30.78  ? 3099 THR A CA    1 
ATOM   13929 C C     . THR A 1 3099 ? 131.315 135.634 159.692 1.00 30.78  ? 3099 THR A C     1 
ATOM   13930 O O     . THR A 1 3099 ? 131.456 134.947 158.676 1.00 30.78  ? 3099 THR A O     1 
ATOM   13931 C CB    . THR A 1 3099 ? 132.366 134.915 161.850 1.00 30.78  ? 3099 THR A CB    1 
ATOM   13932 O OG1   . THR A 1 3099 ? 133.479 135.125 162.728 1.00 30.78  ? 3099 THR A OG1   1 
ATOM   13933 C CG2   . THR A 1 3099 ? 132.361 133.469 161.398 1.00 30.78  ? 3099 THR A CG2   1 
ATOM   13934 N N     . GLU A 1 3100 ? 130.159 136.221 160.010 1.00 29.92  ? 3100 GLU A N     1 
ATOM   13935 C CA    . GLU A 1 3100 ? 128.993 136.093 159.140 1.00 29.92  ? 3100 GLU A CA    1 
ATOM   13936 C C     . GLU A 1 3100 ? 129.248 136.741 157.784 1.00 29.92  ? 3100 GLU A C     1 
ATOM   13937 O O     . GLU A 1 3100 ? 128.849 136.209 156.740 1.00 29.92  ? 3100 GLU A O     1 
ATOM   13938 C CB    . GLU A 1 3100 ? 127.770 136.712 159.817 1.00 29.92  ? 3100 GLU A CB    1 
ATOM   13939 C CG    . GLU A 1 3100 ? 126.456 136.442 159.105 1.00 29.92  ? 3100 GLU A CG    1 
ATOM   13940 C CD    . GLU A 1 3100 ? 126.287 134.985 158.721 1.00 29.92  ? 3100 GLU A CD    1 
ATOM   13941 O OE1   . GLU A 1 3100 ? 126.352 134.121 159.620 1.00 29.92  ? 3100 GLU A OE1   1 
ATOM   13942 O OE2   . GLU A 1 3100 ? 126.085 134.705 157.521 1.00 29.92  ? 3100 GLU A OE2   1 
ATOM   13943 N N     . ALA A 1 3101 ? 129.905 137.902 157.784 1.00 29.12  ? 3101 ALA A N     1 
ATOM   13944 C CA    . ALA A 1 3101 ? 130.217 138.580 156.531 1.00 29.12  ? 3101 ALA A CA    1 
ATOM   13945 C C     . ALA A 1 3101 ? 131.137 137.732 155.664 1.00 29.12  ? 3101 ALA A C     1 
ATOM   13946 O O     . ALA A 1 3101 ? 130.911 137.582 154.458 1.00 29.12  ? 3101 ALA A O     1 
ATOM   13947 C CB    . ALA A 1 3101 ? 130.852 139.939 156.818 1.00 29.12  ? 3101 ALA A CB    1 
ATOM   13948 N N     . LEU A 1 3102 ? 132.182 137.161 156.269 1.00 28.00  ? 3102 LEU A N     1 
ATOM   13949 C CA    . LEU A 1 3102 ? 133.089 136.297 155.523 1.00 28.00  ? 3102 LEU A CA    1 
ATOM   13950 C C     . LEU A 1 3102 ? 132.364 135.064 155.003 1.00 28.00  ? 3102 LEU A C     1 
ATOM   13951 O O     . LEU A 1 3102 ? 132.618 134.609 153.882 1.00 28.00  ? 3102 LEU A O     1 
ATOM   13952 C CB    . LEU A 1 3102 ? 134.270 135.894 156.405 1.00 28.00  ? 3102 LEU A CB    1 
ATOM   13953 C CG    . LEU A 1 3102 ? 135.215 137.015 156.835 1.00 28.00  ? 3102 LEU A CG    1 
ATOM   13954 C CD1   . LEU A 1 3102 ? 136.418 136.447 157.565 1.00 28.00  ? 3102 LEU A CD1   1 
ATOM   13955 C CD2   . LEU A 1 3102 ? 135.651 137.833 155.635 1.00 28.00  ? 3102 LEU A CD2   1 
ATOM   13956 N N     . TYR A 1 3103 ? 131.457 134.509 155.809 1.00 34.07  ? 3103 TYR A N     1 
ATOM   13957 C CA    . TYR A 1 3103 ? 130.680 133.351 155.380 1.00 34.07  ? 3103 TYR A CA    1 
ATOM   13958 C C     . TYR A 1 3103 ? 129.835 133.677 154.155 1.00 34.07  ? 3103 TYR A C     1 
ATOM   13959 O O     . TYR A 1 3103 ? 129.792 132.904 153.192 1.00 34.07  ? 3103 TYR A O     1 
ATOM   13960 C CB    . TYR A 1 3103 ? 129.801 132.870 156.532 1.00 34.07  ? 3103 TYR A CB    1 
ATOM   13961 C CG    . TYR A 1 3103 ? 129.094 131.562 156.276 1.00 34.07  ? 3103 TYR A CG    1 
ATOM   13962 C CD1   . TYR A 1 3103 ? 129.808 130.401 156.027 1.00 34.07  ? 3103 TYR A CD1   1 
ATOM   13963 C CD2   . TYR A 1 3103 ? 127.709 131.487 156.301 1.00 34.07  ? 3103 TYR A CD2   1 
ATOM   13964 C CE1   . TYR A 1 3103 ? 129.163 129.204 155.797 1.00 34.07  ? 3103 TYR A CE1   1 
ATOM   13965 C CE2   . TYR A 1 3103 ? 127.057 130.295 156.076 1.00 34.07  ? 3103 TYR A CE2   1 
ATOM   13966 C CZ    . TYR A 1 3103 ? 127.788 129.158 155.823 1.00 34.07  ? 3103 TYR A CZ    1 
ATOM   13967 O OH    . TYR A 1 3103 ? 127.138 127.969 155.597 1.00 34.07  ? 3103 TYR A OH    1 
ATOM   13968 N N     . GLN A 1 3104 ? 129.159 134.826 154.171 1.00 31.64  ? 3104 GLN A N     1 
ATOM   13969 C CA    . GLN A 1 3104 ? 128.325 135.211 153.035 1.00 31.64  ? 3104 GLN A CA    1 
ATOM   13970 C C     . GLN A 1 3104 ? 129.174 135.489 151.798 1.00 31.64  ? 3104 GLN A C     1 
ATOM   13971 O O     . GLN A 1 3104 ? 128.801 135.123 150.673 1.00 31.64  ? 3104 GLN A O     1 
ATOM   13972 C CB    . GLN A 1 3104 ? 127.470 136.424 153.404 1.00 31.64  ? 3104 GLN A CB    1 
ATOM   13973 C CG    . GLN A 1 3104 ? 126.423 136.122 154.466 1.00 31.64  ? 3104 GLN A CG    1 
ATOM   13974 C CD    . GLN A 1 3104 ? 125.525 137.306 154.762 1.00 31.64  ? 3104 GLN A CD    1 
ATOM   13975 O OE1   . GLN A 1 3104 ? 125.457 137.777 155.897 1.00 31.64  ? 3104 GLN A OE1   1 
ATOM   13976 N NE2   . GLN A 1 3104 ? 124.833 137.796 153.741 1.00 31.64  ? 3104 GLN A NE2   1 
ATOM   13977 N N     . VAL A 1 3105 ? 130.326 136.141 151.990 1.00 29.30  ? 3105 VAL A N     1 
ATOM   13978 C CA    . VAL A 1 3105 ? 131.237 136.394 150.876 1.00 29.30  ? 3105 VAL A CA    1 
ATOM   13979 C C     . VAL A 1 3105 ? 131.667 135.080 150.243 1.00 29.30  ? 3105 VAL A C     1 
ATOM   13980 O O     . VAL A 1 3105 ? 131.628 134.916 149.016 1.00 29.30  ? 3105 VAL A O     1 
ATOM   13981 C CB    . VAL A 1 3105 ? 132.458 137.205 151.352 1.00 29.30  ? 3105 VAL A CB    1 
ATOM   13982 C CG1   . VAL A 1 3105 ? 133.522 137.247 150.269 1.00 29.30  ? 3105 VAL A CG1   1 
ATOM   13983 C CG2   . VAL A 1 3105 ? 132.057 138.606 151.758 1.00 29.30  ? 3105 VAL A CG2   1 
ATOM   13984 N N     . GLY A 1 3106 ? 132.074 134.119 151.074 1.00 29.66  ? 3106 GLY A N     1 
ATOM   13985 C CA    . GLY A 1 3106 ? 132.495 132.831 150.550 1.00 29.66  ? 3106 GLY A CA    1 
ATOM   13986 C C     . GLY A 1 3106 ? 131.370 132.094 149.851 1.00 29.66  ? 3106 GLY A C     1 
ATOM   13987 O O     . GLY A 1 3106 ? 131.575 131.477 148.803 1.00 29.66  ? 3106 GLY A O     1 
ATOM   13988 N N     . LYS A 1 3107 ? 130.163 132.150 150.420 1.00 32.77  ? 3107 LYS A N     1 
ATOM   13989 C CA    . LYS A 1 3107 ? 129.044 131.430 149.825 1.00 32.77  ? 3107 LYS A CA    1 
ATOM   13990 C C     . LYS A 1 3107 ? 128.690 131.982 148.452 1.00 32.77  ? 3107 LYS A C     1 
ATOM   13991 O O     . LYS A 1 3107 ? 128.517 131.215 147.498 1.00 32.77  ? 3107 LYS A O     1 
ATOM   13992 C CB    . LYS A 1 3107 ? 127.828 131.474 150.747 1.00 32.77  ? 3107 LYS A CB    1 
ATOM   13993 C CG    . LYS A 1 3107 ? 127.922 130.539 151.935 1.00 32.77  ? 3107 LYS A CG    1 
ATOM   13994 C CD    . LYS A 1 3107 ? 126.599 130.467 152.671 1.00 32.77  ? 3107 LYS A CD    1 
ATOM   13995 C CE    . LYS A 1 3107 ? 125.568 129.696 151.866 1.00 32.77  ? 3107 LYS A CE    1 
ATOM   13996 N NZ    . LYS A 1 3107 ? 125.932 128.258 151.736 1.00 32.77  ? 3107 LYS A NZ    1 
ATOM   13997 N N     . GLU A 1 3108 ? 128.577 133.305 148.321 1.00 33.60  ? 3108 GLU A N     1 
ATOM   13998 C CA    . GLU A 1 3108 ? 128.196 133.824 147.012 1.00 33.60  ? 3108 GLU A CA    1 
ATOM   13999 C C     . GLU A 1 3108 ? 129.342 133.814 146.007 1.00 33.60  ? 3108 GLU A C     1 
ATOM   14000 O O     . GLU A 1 3108 ? 129.093 133.598 144.815 1.00 33.60  ? 3108 GLU A O     1 
ATOM   14001 C CB    . GLU A 1 3108 ? 127.618 135.239 147.117 1.00 33.60  ? 3108 GLU A CB    1 
ATOM   14002 C CG    . GLU A 1 3108 ? 127.136 135.768 145.765 1.00 33.60  ? 3108 GLU A CG    1 
ATOM   14003 C CD    . GLU A 1 3108 ? 126.508 137.142 145.836 1.00 33.60  ? 3108 GLU A CD    1 
ATOM   14004 O OE1   . GLU A 1 3108 ? 126.451 137.718 146.938 1.00 33.60  ? 3108 GLU A OE1   1 
ATOM   14005 O OE2   . GLU A 1 3108 ? 126.070 137.649 144.782 1.00 33.60  ? 3108 GLU A OE2   1 
ATOM   14006 N N     . PHE A 1 3109 ? 130.586 134.013 146.442 1.00 33.26  ? 3109 PHE A N     1 
ATOM   14007 C CA    . PHE A 1 3109 ? 131.704 134.042 145.509 1.00 33.26  ? 3109 PHE A CA    1 
ATOM   14008 C C     . PHE A 1 3109 ? 132.219 132.660 145.132 1.00 33.26  ? 3109 PHE A C     1 
ATOM   14009 O O     . PHE A 1 3109 ? 133.079 132.559 144.250 1.00 33.26  ? 3109 PHE A O     1 
ATOM   14010 C CB    . PHE A 1 3109 ? 132.851 134.879 146.084 1.00 33.26  ? 3109 PHE A CB    1 
ATOM   14011 C CG    . PHE A 1 3109 ? 132.713 136.348 145.817 1.00 33.26  ? 3109 PHE A CG    1 
ATOM   14012 C CD1   . PHE A 1 3109 ? 132.619 136.821 144.521 1.00 33.26  ? 3109 PHE A CD1   1 
ATOM   14013 C CD2   . PHE A 1 3109 ? 132.662 137.255 146.860 1.00 33.26  ? 3109 PHE A CD2   1 
ATOM   14014 C CE1   . PHE A 1 3109 ? 132.488 138.170 144.268 1.00 33.26  ? 3109 PHE A CE1   1 
ATOM   14015 C CE2   . PHE A 1 3109 ? 132.529 138.607 146.613 1.00 33.26  ? 3109 PHE A CE2   1 
ATOM   14016 C CZ    . PHE A 1 3109 ? 132.443 139.064 145.316 1.00 33.26  ? 3109 PHE A CZ    1 
ATOM   14017 N N     . THR A 1 3110 ? 131.722 131.602 145.771 1.00 31.25  ? 3110 THR A N     1 
ATOM   14018 C CA    . THR A 1 3110 ? 132.010 130.233 145.363 1.00 31.25  ? 3110 THR A CA    1 
ATOM   14019 C C     . THR A 1 3110 ? 130.760 129.495 144.904 1.00 31.25  ? 3110 THR A C     1 
ATOM   14020 O O     . THR A 1 3110 ? 130.774 128.262 144.824 1.00 31.25  ? 3110 THR A O     1 
ATOM   14021 C CB    . THR A 1 3110 ? 132.681 129.462 146.502 1.00 31.25  ? 3110 THR A CB    1 
ATOM   14022 O OG1   . THR A 1 3110 ? 131.771 129.343 147.602 1.00 31.25  ? 3110 THR A OG1   1 
ATOM   14023 C CG2   . THR A 1 3110 ? 133.938 130.178 146.963 1.00 31.25  ? 3110 THR A CG2   1 
ATOM   14024 N N     . SER A 1 3111 ? 129.677 130.218 144.611 1.00 36.96  ? 3111 SER A N     1 
ATOM   14025 C CA    . SER A 1 3111 ? 128.431 129.571 144.213 1.00 36.96  ? 3111 SER A CA    1 
ATOM   14026 C C     . SER A 1 3111 ? 128.581 128.850 142.878 1.00 36.96  ? 3111 SER A C     1 
ATOM   14027 O O     . SER A 1 3111 ? 128.083 127.732 142.704 1.00 36.96  ? 3111 SER A O     1 
ATOM   14028 C CB    . SER A 1 3111 ? 127.307 130.604 144.145 1.00 36.96  ? 3111 SER A CB    1 
ATOM   14029 O OG    . SER A 1 3111 ? 127.660 131.682 143.297 1.00 36.96  ? 3111 SER A OG    1 
ATOM   14030 N N     . LYS A 1 3112 ? 129.263 129.480 141.917 1.00 39.55  ? 3112 LYS A N     1 
ATOM   14031 C CA    . LYS A 1 3112 ? 129.447 128.856 140.610 1.00 39.55  ? 3112 LYS A CA    1 
ATOM   14032 C C     . LYS A 1 3112 ? 130.270 127.579 140.710 1.00 39.55  ? 3112 LYS A C     1 
ATOM   14033 O O     . LYS A 1 3112 ? 130.165 126.702 139.845 1.00 39.55  ? 3112 LYS A O     1 
ATOM   14034 C CB    . LYS A 1 3112 ? 130.110 129.840 139.645 1.00 39.55  ? 3112 LYS A CB    1 
ATOM   14035 C CG    . LYS A 1 3112 ? 131.608 130.000 139.855 1.00 39.55  ? 3112 LYS A CG    1 
ATOM   14036 C CD    . LYS A 1 3112 ? 132.107 131.345 139.360 1.00 39.55  ? 3112 LYS A CD    1 
ATOM   14037 C CE    . LYS A 1 3112 ? 133.562 131.564 139.747 1.00 39.55  ? 3112 LYS A CE    1 
ATOM   14038 N NZ    . LYS A 1 3112 ? 133.696 132.127 141.119 1.00 39.55  ? 3112 LYS A NZ    1 
ATOM   14039 N N     . MET A 1 3113 ? 131.091 127.460 141.749 1.00 39.92  ? 3113 MET A N     1 
ATOM   14040 C CA    . MET A 1 3113 ? 131.908 126.271 141.941 1.00 39.92  ? 3113 MET A CA    1 
ATOM   14041 C C     . MET A 1 3113 ? 131.035 125.061 142.252 1.00 39.92  ? 3113 MET A C     1 
ATOM   14042 O O     . MET A 1 3113 ? 130.037 125.161 142.972 1.00 39.92  ? 3113 MET A O     1 
ATOM   14043 C CB    . MET A 1 3113 ? 132.903 126.511 143.074 1.00 39.92  ? 3113 MET A CB    1 
ATOM   14044 C CG    . MET A 1 3113 ? 133.959 127.556 142.779 1.00 39.92  ? 3113 MET A CG    1 
ATOM   14045 S SD    . MET A 1 3113 ? 135.026 127.832 144.204 1.00 39.92  ? 3113 MET A SD    1 
ATOM   14046 C CE    . MET A 1 3113 ? 135.943 126.300 144.245 1.00 39.92  ? 3113 MET A CE    1 
ATOM   14047 N N     . ASP A 1 3114 ? 131.418 123.909 141.705 1.00 50.67  ? 3114 ASP A N     1 
ATOM   14048 C CA    . ASP A 1 3114 ? 130.677 122.668 141.915 1.00 50.67  ? 3114 ASP A CA    1 
ATOM   14049 C C     . ASP A 1 3114 ? 131.282 121.911 143.091 1.00 50.67  ? 3114 ASP A C     1 
ATOM   14050 O O     . ASP A 1 3114 ? 132.359 121.319 142.972 1.00 50.67  ? 3114 ASP A O     1 
ATOM   14051 C CB    . ASP A 1 3114 ? 130.696 121.813 140.653 1.00 50.67  ? 3114 ASP A CB    1 
ATOM   14052 C CG    . ASP A 1 3114 ? 129.853 120.561 140.789 1.00 50.67  ? 3114 ASP A CG    1 
ATOM   14053 O OD1   . ASP A 1 3114 ? 128.610 120.672 140.750 1.00 50.67  ? 3114 ASP A OD1   1 
ATOM   14054 O OD2   . ASP A 1 3114 ? 130.435 119.467 140.942 1.00 50.67  ? 3114 ASP A OD2   1 
ATOM   14055 N N     . LEU A 1 3115 ? 130.586 121.926 144.231 1.00 50.86  ? 3115 LEU A N     1 
ATOM   14056 C CA    . LEU A 1 3115 ? 131.044 121.241 145.435 1.00 50.86  ? 3115 LEU A CA    1 
ATOM   14057 C C     . LEU A 1 3115 ? 129.954 120.371 146.048 1.00 50.86  ? 3115 LEU A C     1 
ATOM   14058 O O     . LEU A 1 3115 ? 130.025 120.046 147.237 1.00 50.86  ? 3115 LEU A O     1 
ATOM   14059 C CB    . LEU A 1 3115 ? 131.552 122.241 146.477 1.00 50.86  ? 3115 LEU A CB    1 
ATOM   14060 C CG    . LEU A 1 3115 ? 132.952 122.836 146.320 1.00 50.86  ? 3115 LEU A CG    1 
ATOM   14061 C CD1   . LEU A 1 3115 ? 133.031 123.811 145.180 1.00 50.86  ? 3115 LEU A CD1   1 
ATOM   14062 C CD2   . LEU A 1 3115 ? 133.343 123.526 147.598 1.00 50.86  ? 3115 LEU A CD2   1 
ATOM   14063 N N     . GLU A 1 3116 ? 128.948 119.987 145.269 1.00 60.01  ? 3116 GLU A N     1 
ATOM   14064 C CA    . GLU A 1 3116 ? 127.854 119.162 145.767 1.00 60.01  ? 3116 GLU A CA    1 
ATOM   14065 C C     . GLU A 1 3116 ? 128.330 117.717 145.845 1.00 60.01  ? 3116 GLU A C     1 
ATOM   14066 O O     . GLU A 1 3116 ? 128.481 117.048 144.817 1.00 60.01  ? 3116 GLU A O     1 
ATOM   14067 C CB    . GLU A 1 3116 ? 126.625 119.295 144.872 1.00 60.01  ? 3116 GLU A CB    1 
ATOM   14068 C CG    . GLU A 1 3116 ? 125.945 120.652 144.957 1.00 60.01  ? 3116 GLU A CG    1 
ATOM   14069 C CD    . GLU A 1 3116 ? 126.376 121.592 143.849 1.00 60.01  ? 3116 GLU A CD    1 
ATOM   14070 O OE1   . GLU A 1 3116 ? 126.551 122.798 144.126 1.00 60.01  ? 3116 GLU A OE1   1 
ATOM   14071 O OE2   . GLU A 1 3116 ? 126.540 121.127 142.701 1.00 60.01  ? 3116 GLU A OE2   1 
ATOM   14072 N N     . LYS A 1 3117 ? 128.569 117.238 147.064 1.00 66.74  ? 3117 LYS A N     1 
ATOM   14073 C CA    . LYS A 1 3117 ? 128.976 115.857 147.301 1.00 66.74  ? 3117 LYS A CA    1 
ATOM   14074 C C     . LYS A 1 3117 ? 127.897 115.161 148.119 1.00 66.74  ? 3117 LYS A C     1 
ATOM   14075 O O     . LYS A 1 3117 ? 127.853 115.319 149.349 1.00 66.74  ? 3117 LYS A O     1 
ATOM   14076 C CB    . LYS A 1 3117 ? 130.323 115.806 148.027 1.00 66.74  ? 3117 LYS A CB    1 
ATOM   14077 C CG    . LYS A 1 3117 ? 131.120 114.541 147.767 1.00 66.74  ? 3117 LYS A CG    1 
ATOM   14078 C CD    . LYS A 1 3117 ? 132.588 114.727 148.118 1.00 66.74  ? 3117 LYS A CD    1 
ATOM   14079 C CE    . LYS A 1 3117 ? 133.330 113.401 148.107 1.00 66.74  ? 3117 LYS A CE    1 
ATOM   14080 N NZ    . LYS A 1 3117 ? 132.913 112.537 146.968 1.00 66.74  ? 3117 LYS A NZ    1 
ATOM   14081 N N     . PRO A 1 3118 ? 127.002 114.394 147.491 1.00 66.44  ? 3118 PRO A N     1 
ATOM   14082 C CA    . PRO A 1 3118 ? 125.889 113.789 148.243 1.00 66.44  ? 3118 PRO A CA    1 
ATOM   14083 C C     . PRO A 1 3118 ? 126.326 112.833 149.339 1.00 66.44  ? 3118 PRO A C     1 
ATOM   14084 O O     . PRO A 1 3118 ? 125.616 112.706 150.344 1.00 66.44  ? 3118 PRO A O     1 
ATOM   14085 C CB    . PRO A 1 3118 ? 125.085 113.063 147.156 1.00 66.44  ? 3118 PRO A CB    1 
ATOM   14086 C CG    . PRO A 1 3118 ? 126.054 112.853 146.037 1.00 66.44  ? 3118 PRO A CG    1 
ATOM   14087 C CD    . PRO A 1 3118 ? 126.969 114.037 146.064 1.00 66.44  ? 3118 PRO A CD    1 
ATOM   14088 N N     . ASN A 1 3119 ? 127.464 112.157 149.186 1.00 69.23  ? 3119 ASN A N     1 
ATOM   14089 C CA    . ASN A 1 3119 ? 127.936 111.197 150.174 1.00 69.23  ? 3119 ASN A CA    1 
ATOM   14090 C C     . ASN A 1 3119 ? 128.811 111.833 151.250 1.00 69.23  ? 3119 ASN A C     1 
ATOM   14091 O O     . ASN A 1 3119 ? 129.632 111.138 151.859 1.00 69.23  ? 3119 ASN A O     1 
ATOM   14092 C CB    . ASN A 1 3119 ? 128.679 110.049 149.482 1.00 69.23  ? 3119 ASN A CB    1 
ATOM   14093 C CG    . ASN A 1 3119 ? 129.939 110.504 148.763 1.00 69.23  ? 3119 ASN A CG    1 
ATOM   14094 O OD1   . ASN A 1 3119 ? 130.353 111.657 148.863 1.00 69.23  ? 3119 ASN A OD1   1 
ATOM   14095 N ND2   . ASN A 1 3119 ? 130.557 109.586 148.030 1.00 69.23  ? 3119 ASN A ND2   1 
ATOM   14096 N N     . TYR A 1 3120 ? 128.656 113.132 151.493 1.00 62.37  ? 3120 TYR A N     1 
ATOM   14097 C CA    . TYR A 1 3120 ? 129.425 113.804 152.532 1.00 62.37  ? 3120 TYR A CA    1 
ATOM   14098 C C     . TYR A 1 3120 ? 128.973 113.320 153.904 1.00 62.37  ? 3120 TYR A C     1 
ATOM   14099 O O     . TYR A 1 3120 ? 127.788 113.409 154.243 1.00 62.37  ? 3120 TYR A O     1 
ATOM   14100 C CB    . TYR A 1 3120 ? 129.259 115.317 152.414 1.00 62.37  ? 3120 TYR A CB    1 
ATOM   14101 C CG    . TYR A 1 3120 ? 130.030 116.107 153.448 1.00 62.37  ? 3120 TYR A CG    1 
ATOM   14102 C CD1   . TYR A 1 3120 ? 131.401 116.287 153.332 1.00 62.37  ? 3120 TYR A CD1   1 
ATOM   14103 C CD2   . TYR A 1 3120 ? 129.385 116.673 154.540 1.00 62.37  ? 3120 TYR A CD2   1 
ATOM   14104 C CE1   . TYR A 1 3120 ? 132.109 117.008 154.275 1.00 62.37  ? 3120 TYR A CE1   1 
ATOM   14105 C CE2   . TYR A 1 3120 ? 130.085 117.395 155.487 1.00 62.37  ? 3120 TYR A CE2   1 
ATOM   14106 C CZ    . TYR A 1 3120 ? 131.446 117.560 155.350 1.00 62.37  ? 3120 TYR A CZ    1 
ATOM   14107 O OH    . TYR A 1 3120 ? 132.147 118.278 156.290 1.00 62.37  ? 3120 TYR A OH    1 
ATOM   14108 N N     . ILE A 1 3121 ? 129.914 112.809 154.694 1.00 65.73  ? 3121 ILE A N     1 
ATOM   14109 C CA    . ILE A 1 3121 ? 129.629 112.329 156.042 1.00 65.73  ? 3121 ILE A CA    1 
ATOM   14110 C C     . ILE A 1 3121 ? 129.792 113.522 156.978 1.00 65.73  ? 3121 ILE A C     1 
ATOM   14111 O O     . ILE A 1 3121 ? 130.855 114.141 157.037 1.00 65.73  ? 3121 ILE A O     1 
ATOM   14112 C CB    . ILE A 1 3121 ? 130.539 111.165 156.435 1.00 65.73  ? 3121 ILE A CB    1 
ATOM   14113 C CG1   . ILE A 1 3121 ? 130.368 110.003 155.455 1.00 65.73  ? 3121 ILE A CG1   1 
ATOM   14114 C CG2   . ILE A 1 3121 ? 130.243 110.716 157.858 1.00 65.73  ? 3121 ILE A CG2   1 
ATOM   14115 C CD1   . ILE A 1 3121 ? 128.965 109.439 155.415 1.00 65.73  ? 3121 ILE A CD1   1 
ATOM   14116 N N     . VAL A 1 3122 ? 128.733 113.844 157.714 1.00 67.77  ? 3122 VAL A N     1 
ATOM   14117 C CA    . VAL A 1 3122 ? 128.722 115.025 158.574 1.00 67.77  ? 3122 VAL A CA    1 
ATOM   14118 C C     . VAL A 1 3122 ? 129.684 114.818 159.737 1.00 67.77  ? 3122 VAL A C     1 
ATOM   14119 O O     . VAL A 1 3122 ? 129.522 113.872 160.520 1.00 67.77  ? 3122 VAL A O     1 
ATOM   14120 C CB    . VAL A 1 3122 ? 127.304 115.333 159.078 1.00 67.77  ? 3122 VAL A CB    1 
ATOM   14121 C CG1   . VAL A 1 3122 ? 127.337 116.473 160.082 1.00 67.77  ? 3122 VAL A CG1   1 
ATOM   14122 C CG2   . VAL A 1 3122 ? 126.392 115.671 157.910 1.00 67.77  ? 3122 VAL A CG2   1 
ATOM   14123 N N     . PRO A 1 3123 ? 130.690 115.675 159.889 1.00 68.82  ? 3123 PRO A N     1 
ATOM   14124 C CA    . PRO A 1 3123 ? 131.636 115.522 161.000 1.00 68.82  ? 3123 PRO A CA    1 
ATOM   14125 C C     . PRO A 1 3123 ? 131.139 116.169 162.282 1.00 68.82  ? 3123 PRO A C     1 
ATOM   14126 O O     . PRO A 1 3123 ? 130.001 116.643 162.351 1.00 68.82  ? 3123 PRO A O     1 
ATOM   14127 C CB    . PRO A 1 3123 ? 132.891 116.223 160.475 1.00 68.82  ? 3123 PRO A CB    1 
ATOM   14128 C CG    . PRO A 1 3123 ? 132.338 117.317 159.619 1.00 68.82  ? 3123 PRO A CG    1 
ATOM   14129 C CD    . PRO A 1 3123 ? 131.085 116.763 158.977 1.00 68.82  ? 3123 PRO A CD    1 
ATOM   14130 N N     . ASP A 1 3124 ? 131.991 116.188 163.304 1.00 82.40  ? 3124 ASP A N     1 
ATOM   14131 C CA    . ASP A 1 3124 ? 131.685 116.876 164.548 1.00 82.40  ? 3124 ASP A CA    1 
ATOM   14132 C C     . ASP A 1 3124 ? 132.647 118.047 164.698 1.00 82.40  ? 3124 ASP A C     1 
ATOM   14133 O O     . ASP A 1 3124 ? 133.644 118.149 163.979 1.00 82.40  ? 3124 ASP A O     1 
ATOM   14134 C CB    . ASP A 1 3124 ? 131.778 115.929 165.752 1.00 82.40  ? 3124 ASP A CB    1 
ATOM   14135 C CG    . ASP A 1 3124 ? 131.168 116.520 167.009 1.00 82.40  ? 3124 ASP A CG    1 
ATOM   14136 O OD1   . ASP A 1 3124 ? 129.964 116.852 166.987 1.00 82.40  ? 3124 ASP A OD1   1 
ATOM   14137 O OD2   . ASP A 1 3124 ? 131.891 116.655 168.017 1.00 82.40  ? 3124 ASP A OD2   1 
ATOM   14138 N N     . TYR A 1 3125 ? 132.317 118.944 165.630 1.00 87.94  ? 3125 TYR A N     1 
ATOM   14139 C CA    . TYR A 1 3125 ? 133.132 120.115 165.939 1.00 87.94  ? 3125 TYR A CA    1 
ATOM   14140 C C     . TYR A 1 3125 ? 133.251 121.053 164.745 1.00 87.94  ? 3125 TYR A C     1 
ATOM   14141 O O     . TYR A 1 3125 ? 132.241 121.451 164.155 1.00 87.94  ? 3125 TYR A O     1 
ATOM   14142 C CB    . TYR A 1 3125 ? 134.528 119.707 166.420 1.00 87.94  ? 3125 TYR A CB    1 
ATOM   14143 C CG    . TYR A 1 3125 ? 134.529 118.701 167.546 1.00 87.94  ? 3125 TYR A CG    1 
ATOM   14144 C CD1   . TYR A 1 3125 ? 134.022 119.031 168.796 1.00 87.94  ? 3125 TYR A CD1   1 
ATOM   14145 C CD2   . TYR A 1 3125 ? 135.043 117.425 167.362 1.00 87.94  ? 3125 TYR A CD2   1 
ATOM   14146 C CE1   . TYR A 1 3125 ? 134.025 118.116 169.831 1.00 87.94  ? 3125 TYR A CE1   1 
ATOM   14147 C CE2   . TYR A 1 3125 ? 135.050 116.503 168.390 1.00 87.94  ? 3125 TYR A CE2   1 
ATOM   14148 C CZ    . TYR A 1 3125 ? 134.539 116.854 169.622 1.00 87.94  ? 3125 TYR A CZ    1 
ATOM   14149 O OH    . TYR A 1 3125 ? 134.543 115.938 170.649 1.00 87.94  ? 3125 TYR A OH    1 
ATOM   14150 N N     . MET A 1 3126 ? 134.494 121.408 164.393 1.00 72.31  ? 3126 MET A N     1 
ATOM   14151 C CA    . MET A 1 3126 ? 134.863 122.390 163.373 1.00 72.31  ? 3126 MET A CA    1 
ATOM   14152 C C     . MET A 1 3126 ? 133.955 123.621 163.341 1.00 72.31  ? 3126 MET A C     1 
ATOM   14153 O O     . MET A 1 3126 ? 133.590 124.091 162.257 1.00 72.31  ? 3126 MET A O     1 
ATOM   14154 C CB    . MET A 1 3126 ? 134.946 121.688 162.004 1.00 72.31  ? 3126 MET A CB    1 
ATOM   14155 C CG    . MET A 1 3126 ? 133.675 121.006 161.450 1.00 72.31  ? 3126 MET A CG    1 
ATOM   14156 S SD    . MET A 1 3126 ? 132.383 121.992 160.666 1.00 72.31  ? 3126 MET A SD    1 
ATOM   14157 C CE    . MET A 1 3126 ? 133.194 122.466 159.141 1.00 72.31  ? 3126 MET A CE    1 
ATOM   14158 N N     . PRO A 1 3127 ? 133.631 124.231 164.499 1.00 67.74  ? 3127 PRO A N     1 
ATOM   14159 C CA    . PRO A 1 3127 ? 132.724 125.383 164.477 1.00 67.74  ? 3127 PRO A CA    1 
ATOM   14160 C C     . PRO A 1 3127 ? 133.449 126.702 164.253 1.00 67.74  ? 3127 PRO A C     1 
ATOM   14161 O O     . PRO A 1 3127 ? 134.355 127.059 165.012 1.00 67.74  ? 3127 PRO A O     1 
ATOM   14162 C CB    . PRO A 1 3127 ? 132.078 125.329 165.865 1.00 67.74  ? 3127 PRO A CB    1 
ATOM   14163 C CG    . PRO A 1 3127 ? 133.148 124.701 166.750 1.00 67.74  ? 3127 PRO A CG    1 
ATOM   14164 C CD    . PRO A 1 3127 ? 134.179 124.031 165.853 1.00 67.74  ? 3127 PRO A CD    1 
ATOM   14165 N N     . VAL A 1 3128 ? 133.060 127.438 163.211 1.00 47.11  ? 3128 VAL A N     1 
ATOM   14166 C CA    . VAL A 1 3128 ? 133.580 128.773 162.944 1.00 47.11  ? 3128 VAL A CA    1 
ATOM   14167 C C     . VAL A 1 3128 ? 132.452 129.782 162.770 1.00 47.11  ? 3128 VAL A C     1 
ATOM   14168 O O     . VAL A 1 3128 ? 132.432 130.829 163.424 1.00 47.11  ? 3128 VAL A O     1 
ATOM   14169 C CB    . VAL A 1 3128 ? 134.512 128.781 161.714 1.00 47.11  ? 3128 VAL A CB    1 
ATOM   14170 C CG1   . VAL A 1 3128 ? 135.162 130.143 161.560 1.00 47.11  ? 3128 VAL A CG1   1 
ATOM   14171 C CG2   . VAL A 1 3128 ? 135.560 127.695 161.835 1.00 47.11  ? 3128 VAL A CG2   1 
ATOM   14172 N N     . VAL A 1 3129 ? 131.506 129.485 161.887 1.00 50.27  ? 3129 VAL A N     1 
ATOM   14173 C CA    . VAL A 1 3129 ? 130.306 130.299 161.716 1.00 50.27  ? 3129 VAL A CA    1 
ATOM   14174 C C     . VAL A 1 3129 ? 129.276 129.716 162.676 1.00 50.27  ? 3129 VAL A C     1 
ATOM   14175 O O     . VAL A 1 3129 ? 128.802 128.591 162.507 1.00 50.27  ? 3129 VAL A O     1 
ATOM   14176 C CB    . VAL A 1 3129 ? 129.816 130.301 160.271 1.00 50.27  ? 3129 VAL A CB    1 
ATOM   14177 C CG1   . VAL A 1 3129 ? 128.511 131.077 160.154 1.00 50.27  ? 3129 VAL A CG1   1 
ATOM   14178 C CG2   . VAL A 1 3129 ? 130.875 130.882 159.355 1.00 50.27  ? 3129 VAL A CG2   1 
ATOM   14179 N N     . TYR A 1 3130 ? 128.931 130.491 163.706 1.00 64.67  ? 3130 TYR A N     1 
ATOM   14180 C CA    . TYR A 1 3130 ? 127.974 130.036 164.706 1.00 64.67  ? 3130 TYR A CA    1 
ATOM   14181 C C     . TYR A 1 3130 ? 126.609 129.769 164.081 1.00 64.67  ? 3130 TYR A C     1 
ATOM   14182 O O     . TYR A 1 3130 ? 125.917 128.811 164.444 1.00 64.67  ? 3130 TYR A O     1 
ATOM   14183 C CB    . TYR A 1 3130 ? 127.873 131.067 165.837 1.00 64.67  ? 3130 TYR A CB    1 
ATOM   14184 C CG    . TYR A 1 3130 ? 127.337 132.416 165.411 1.00 64.67  ? 3130 TYR A CG    1 
ATOM   14185 C CD1   . TYR A 1 3130 ? 128.193 133.415 164.967 1.00 64.67  ? 3130 TYR A CD1   1 
ATOM   14186 C CD2   . TYR A 1 3130 ? 125.977 132.698 165.471 1.00 64.67  ? 3130 TYR A CD2   1 
ATOM   14187 C CE1   . TYR A 1 3130 ? 127.709 134.651 164.580 1.00 64.67  ? 3130 TYR A CE1   1 
ATOM   14188 C CE2   . TYR A 1 3130 ? 125.485 133.929 165.086 1.00 64.67  ? 3130 TYR A CE2   1 
ATOM   14189 C CZ    . TYR A 1 3130 ? 126.355 134.902 164.643 1.00 64.67  ? 3130 TYR A CZ    1 
ATOM   14190 O OH    . TYR A 1 3130 ? 125.869 136.132 164.261 1.00 64.67  ? 3130 TYR A OH    1 
ATOM   14191 N N     . ASP A 1 3131 ? 126.209 130.616 163.134 1.00 63.21  ? 3131 ASP A N     1 
ATOM   14192 C CA    . ASP A 1 3131 ? 124.945 130.435 162.434 1.00 63.21  ? 3131 ASP A CA    1 
ATOM   14193 C C     . ASP A 1 3131 ? 125.147 129.633 161.155 1.00 63.21  ? 3131 ASP A C     1 
ATOM   14194 O O     . ASP A 1 3131 ? 124.971 130.161 160.053 1.00 63.21  ? 3131 ASP A O     1 
ATOM   14195 C CB    . ASP A 1 3131 ? 124.307 131.790 162.120 1.00 63.21  ? 3131 ASP A CB    1 
ATOM   14196 C CG    . ASP A 1 3131 ? 122.855 131.668 161.699 1.00 63.21  ? 3131 ASP A CG    1 
ATOM   14197 O OD1   . ASP A 1 3131 ? 122.319 130.541 161.714 1.00 63.21  ? 3131 ASP A OD1   1 
ATOM   14198 O OD2   . ASP A 1 3131 ? 122.248 132.703 161.351 1.00 63.21  ? 3131 ASP A OD2   1 
ATOM   14199 N N     . LYS A 1 3132 ? 125.532 128.366 161.291 1.00 60.96  ? 3132 LYS A N     1 
ATOM   14200 C CA    . LYS A 1 3132 ? 125.599 127.481 160.137 1.00 60.96  ? 3132 LYS A CA    1 
ATOM   14201 C C     . LYS A 1 3132 ? 124.212 127.347 159.523 1.00 60.96  ? 3132 LYS A C     1 
ATOM   14202 O O     . LYS A 1 3132 ? 123.224 127.160 160.239 1.00 60.96  ? 3132 LYS A O     1 
ATOM   14203 C CB    . LYS A 1 3132 ? 126.132 126.109 160.551 1.00 60.96  ? 3132 LYS A CB    1 
ATOM   14204 C CG    . LYS A 1 3132 ? 127.633 126.059 160.788 1.00 60.96  ? 3132 LYS A CG    1 
ATOM   14205 C CD    . LYS A 1 3132 ? 128.420 126.550 159.586 1.00 60.96  ? 3132 LYS A CD    1 
ATOM   14206 C CE    . LYS A 1 3132 ? 128.242 125.633 158.389 1.00 60.96  ? 3132 LYS A CE    1 
ATOM   14207 N NZ    . LYS A 1 3132 ? 129.133 126.034 157.267 1.00 60.96  ? 3132 LYS A NZ    1 
ATOM   14208 N N     . LEU A 1 3133 ? 124.134 127.460 158.195 1.00 72.68  ? 3133 LEU A N     1 
ATOM   14209 C CA    . LEU A 1 3133 ? 122.826 127.459 157.542 1.00 72.68  ? 3133 LEU A CA    1 
ATOM   14210 C C     . LEU A 1 3133 ? 122.043 126.181 157.819 1.00 72.68  ? 3133 LEU A C     1 
ATOM   14211 O O     . LEU A 1 3133 ? 120.874 126.281 158.229 1.00 72.68  ? 3133 LEU A O     1 
ATOM   14212 C CB    . LEU A 1 3133 ? 122.995 127.723 156.041 1.00 72.68  ? 3133 LEU A CB    1 
ATOM   14213 C CG    . LEU A 1 3133 ? 121.716 128.039 155.261 1.00 72.68  ? 3133 LEU A CG    1 
ATOM   14214 C CD1   . LEU A 1 3133 ? 121.305 129.489 155.469 1.00 72.68  ? 3133 LEU A CD1   1 
ATOM   14215 C CD2   . LEU A 1 3133 ? 121.898 127.734 153.782 1.00 72.68  ? 3133 LEU A CD2   1 
ATOM   14216 N N     . PRO A 1 3134 ? 122.593 124.969 157.628 1.00 73.19  ? 3134 PRO A N     1 
ATOM   14217 C CA    . PRO A 1 3134 ? 121.939 123.789 158.203 1.00 73.19  ? 3134 PRO A CA    1 
ATOM   14218 C C     . PRO A 1 3134 ? 122.564 123.397 159.532 1.00 73.19  ? 3134 PRO A C     1 
ATOM   14219 O O     . PRO A 1 3134 ? 123.745 123.671 159.766 1.00 73.19  ? 3134 PRO A O     1 
ATOM   14220 C CB    . PRO A 1 3134 ? 122.161 122.717 157.132 1.00 73.19  ? 3134 PRO A CB    1 
ATOM   14221 C CG    . PRO A 1 3134 ? 123.456 123.118 156.464 1.00 73.19  ? 3134 PRO A CG    1 
ATOM   14222 C CD    . PRO A 1 3134 ? 123.739 124.575 156.787 1.00 73.19  ? 3134 PRO A CD    1 
ATOM   14223 N N     . GLN A 1 3135 ? 121.793 122.768 160.419 1.00 80.36  ? 3135 GLN A N     1 
ATOM   14224 C CA    . GLN A 1 3135 ? 122.405 122.178 161.607 1.00 80.36  ? 3135 GLN A CA    1 
ATOM   14225 C C     . GLN A 1 3135 ? 123.377 121.062 161.244 1.00 80.36  ? 3135 GLN A C     1 
ATOM   14226 O O     . GLN A 1 3135 ? 124.511 121.075 161.753 1.00 80.36  ? 3135 GLN A O     1 
ATOM   14227 C CB    . GLN A 1 3135 ? 121.318 121.714 162.584 1.00 80.36  ? 3135 GLN A CB    1 
ATOM   14228 C CG    . GLN A 1 3135 ? 120.444 122.839 163.116 1.00 80.36  ? 3135 GLN A CG    1 
ATOM   14229 C CD    . GLN A 1 3135 ? 121.244 123.901 163.845 1.00 80.36  ? 3135 GLN A CD    1 
ATOM   14230 O OE1   . GLN A 1 3135 ? 121.901 123.621 164.848 1.00 80.36  ? 3135 GLN A OE1   1 
ATOM   14231 N NE2   . GLN A 1 3135 ? 121.192 125.130 163.344 1.00 80.36  ? 3135 GLN A NE2   1 
ATOM   14232 N N     . PRO A 1 3136 ? 123.029 120.085 160.404 1.00 74.50  ? 3136 PRO A N     1 
ATOM   14233 C CA    . PRO A 1 3136 ? 124.060 119.237 159.806 1.00 74.50  ? 3136 PRO A CA    1 
ATOM   14234 C C     . PRO A 1 3136 ? 124.597 119.869 158.534 1.00 74.50  ? 3136 PRO A C     1 
ATOM   14235 O O     . PRO A 1 3136 ? 123.874 119.979 157.533 1.00 74.50  ? 3136 PRO A O     1 
ATOM   14236 C CB    . PRO A 1 3136 ? 123.317 117.926 159.516 1.00 74.50  ? 3136 PRO A CB    1 
ATOM   14237 C CG    . PRO A 1 3136 ? 121.887 118.321 159.347 1.00 74.50  ? 3136 PRO A CG    1 
ATOM   14238 C CD    . PRO A 1 3136 ? 121.683 119.692 159.945 1.00 74.50  ? 3136 PRO A CD    1 
ATOM   14239 N N     . PRO A 1 3137 ? 125.857 120.295 158.528 1.00 66.69  ? 3137 PRO A N     1 
ATOM   14240 C CA    . PRO A 1 3137 ? 126.392 120.977 157.347 1.00 66.69  ? 3137 PRO A CA    1 
ATOM   14241 C C     . PRO A 1 3137 ? 126.584 120.026 156.177 1.00 66.69  ? 3137 PRO A C     1 
ATOM   14242 O O     . PRO A 1 3137 ? 126.852 118.834 156.348 1.00 66.69  ? 3137 PRO A O     1 
ATOM   14243 C CB    . PRO A 1 3137 ? 127.735 121.530 157.837 1.00 66.69  ? 3137 PRO A CB    1 
ATOM   14244 C CG    . PRO A 1 3137 ? 128.137 120.600 158.928 1.00 66.69  ? 3137 PRO A CG    1 
ATOM   14245 C CD    . PRO A 1 3137 ? 126.862 120.161 159.597 1.00 66.69  ? 3137 PRO A CD    1 
ATOM   14246 N N     . SER A 1 3138 ? 126.439 120.572 154.974 1.00 55.46  ? 3138 SER A N     1 
ATOM   14247 C CA    . SER A 1 3138 ? 126.739 119.853 153.748 1.00 55.46  ? 3138 SER A CA    1 
ATOM   14248 C C     . SER A 1 3138 ? 128.161 120.185 153.305 1.00 55.46  ? 3138 SER A C     1 
ATOM   14249 O O     . SER A 1 3138 ? 128.927 120.835 154.021 1.00 55.46  ? 3138 SER A O     1 
ATOM   14250 C CB    . SER A 1 3138 ? 125.720 120.192 152.658 1.00 55.46  ? 3138 SER A CB    1 
ATOM   14251 O OG    . SER A 1 3138 ? 126.095 119.622 151.417 1.00 55.46  ? 3138 SER A OG    1 
ATOM   14252 N N     . HIS A 1 3139 ? 128.523 119.726 152.105 1.00 51.58  ? 3139 HIS A N     1 
ATOM   14253 C CA    . HIS A 1 3139 ? 129.881 119.952 151.619 1.00 51.58  ? 3139 HIS A CA    1 
ATOM   14254 C C     . HIS A 1 3139 ? 130.143 121.429 151.351 1.00 51.58  ? 3139 HIS A C     1 
ATOM   14255 O O     . HIS A 1 3139 ? 131.203 121.951 151.715 1.00 51.58  ? 3139 HIS A O     1 
ATOM   14256 C CB    . HIS A 1 3139 ? 130.134 119.125 150.360 1.00 51.58  ? 3139 HIS A CB    1 
ATOM   14257 C CG    . HIS A 1 3139 ? 131.584 118.881 150.084 1.00 51.58  ? 3139 HIS A CG    1 
ATOM   14258 N ND1   . HIS A 1 3139 ? 132.496 118.619 151.084 1.00 51.58  ? 3139 HIS A ND1   1 
ATOM   14259 C CD2   . HIS A 1 3139 ? 132.282 118.861 148.924 1.00 51.58  ? 3139 HIS A CD2   1 
ATOM   14260 C CE1   . HIS A 1 3139 ? 133.693 118.447 150.551 1.00 51.58  ? 3139 HIS A CE1   1 
ATOM   14261 N NE2   . HIS A 1 3139 ? 133.590 118.589 149.242 1.00 51.58  ? 3139 HIS A NE2   1 
ATOM   14262 N N     . ARG A 1 3140 ? 129.191 122.121 150.719 1.00 45.42  ? 3140 ARG A N     1 
ATOM   14263 C CA    . ARG A 1 3140 ? 129.390 123.533 150.401 1.00 45.42  ? 3140 ARG A CA    1 
ATOM   14264 C C     . ARG A 1 3140 ? 129.549 124.368 151.665 1.00 45.42  ? 3140 ARG A C     1 
ATOM   14265 O O     . ARG A 1 3140 ? 130.481 125.179 151.773 1.00 45.42  ? 3140 ARG A O     1 
ATOM   14266 C CB    . ARG A 1 3140 ? 128.220 124.049 149.564 1.00 45.42  ? 3140 ARG A CB    1 
ATOM   14267 C CG    . ARG A 1 3140 ? 128.266 125.543 149.299 1.00 45.42  ? 3140 ARG A CG    1 
ATOM   14268 C CD    . ARG A 1 3140 ? 127.799 125.877 147.894 1.00 45.42  ? 3140 ARG A CD    1 
ATOM   14269 N NE    . ARG A 1 3140 ? 128.379 124.991 146.893 1.00 45.42  ? 3140 ARG A NE    1 
ATOM   14270 C CZ    . ARG A 1 3140 ? 128.140 125.078 145.592 1.00 45.42  ? 3140 ARG A CZ    1 
ATOM   14271 N NH1   . ARG A 1 3140 ? 127.338 126.007 145.098 1.00 45.42  ? 3140 ARG A NH1   1 
ATOM   14272 N NH2   . ARG A 1 3140 ? 128.721 124.214 144.766 1.00 45.42  ? 3140 ARG A NH2   1 
ATOM   14273 N N     . GLU A 1 3141 ? 128.650 124.184 152.632 1.00 48.60  ? 3141 GLU A N     1 
ATOM   14274 C CA    . GLU A 1 3141 ? 128.748 124.910 153.889 1.00 48.60  ? 3141 GLU A CA    1 
ATOM   14275 C C     . GLU A 1 3141 ? 130.029 124.571 154.637 1.00 48.60  ? 3141 GLU A C     1 
ATOM   14276 O O     . GLU A 1 3141 ? 130.657 125.465 155.214 1.00 48.60  ? 3141 GLU A O     1 
ATOM   14277 C CB    . GLU A 1 3141 ? 127.530 124.615 154.766 1.00 48.60  ? 3141 GLU A CB    1 
ATOM   14278 C CG    . GLU A 1 3141 ? 126.234 125.234 154.267 1.00 48.60  ? 3141 GLU A CG    1 
ATOM   14279 C CD    . GLU A 1 3141 ? 125.529 124.377 153.238 1.00 48.60  ? 3141 GLU A CD    1 
ATOM   14280 O OE1   . GLU A 1 3141 ? 126.059 123.301 152.896 1.00 48.60  ? 3141 GLU A OE1   1 
ATOM   14281 O OE2   . GLU A 1 3141 ? 124.441 124.778 152.773 1.00 48.60  ? 3141 GLU A OE2   1 
ATOM   14282 N N     . ALA A 1 3142 ? 130.435 123.300 154.630 1.00 44.00  ? 3142 ALA A N     1 
ATOM   14283 C CA    . ALA A 1 3142 ? 131.677 122.918 155.291 1.00 44.00  ? 3142 ALA A CA    1 
ATOM   14284 C C     . ALA A 1 3142 ? 132.879 123.596 154.647 1.00 44.00  ? 3142 ALA A C     1 
ATOM   14285 O O     . ALA A 1 3142 ? 133.792 124.045 155.346 1.00 44.00  ? 3142 ALA A O     1 
ATOM   14286 C CB    . ALA A 1 3142 ? 131.841 121.400 155.271 1.00 44.00  ? 3142 ALA A CB    1 
ATOM   14287 N N     . ILE A 1 3143 ? 132.897 123.688 153.316 1.00 37.80  ? 3143 ILE A N     1 
ATOM   14288 C CA    . ILE A 1 3143 ? 134.037 124.299 152.637 1.00 37.80  ? 3143 ILE A CA    1 
ATOM   14289 C C     . ILE A 1 3143 ? 134.082 125.800 152.903 1.00 37.80  ? 3143 ILE A C     1 
ATOM   14290 O O     . ILE A 1 3143 ? 135.154 126.375 153.129 1.00 37.80  ? 3143 ILE A O     1 
ATOM   14291 C CB    . ILE A 1 3143 ? 133.997 123.991 151.131 1.00 37.80  ? 3143 ILE A CB    1 
ATOM   14292 C CG1   . ILE A 1 3143 ? 134.217 122.496 150.900 1.00 37.80  ? 3143 ILE A CG1   1 
ATOM   14293 C CG2   . ILE A 1 3143 ? 135.048 124.806 150.397 1.00 37.80  ? 3143 ILE A CG2   1 
ATOM   14294 C CD1   . ILE A 1 3143 ? 135.645 122.052 151.103 1.00 37.80  ? 3143 ILE A CD1   1 
ATOM   14295 N N     . VAL A 1 3144 ? 132.922 126.463 152.875 1.00 33.40  ? 3144 VAL A N     1 
ATOM   14296 C CA    . VAL A 1 3144 ? 132.918 127.891 153.189 1.00 33.40  ? 3144 VAL A CA    1 
ATOM   14297 C C     . VAL A 1 3144 ? 133.319 128.138 154.640 1.00 33.40  ? 3144 VAL A C     1 
ATOM   14298 O O     . VAL A 1 3144 ? 134.028 129.115 154.934 1.00 33.40  ? 3144 VAL A O     1 
ATOM   14299 C CB    . VAL A 1 3144 ? 131.549 128.521 152.877 1.00 33.40  ? 3144 VAL A CB    1 
ATOM   14300 C CG1   . VAL A 1 3144 ? 131.613 130.024 153.057 1.00 33.40  ? 3144 VAL A CG1   1 
ATOM   14301 C CG2   . VAL A 1 3144 ? 131.134 128.197 151.455 1.00 33.40  ? 3144 VAL A CG2   1 
ATOM   14302 N N     . ASN A 1 3145 ? 132.898 127.264 155.556 1.00 37.67  ? 3145 ASN A N     1 
ATOM   14303 C CA    . ASN A 1 3145 ? 133.341 127.356 156.940 1.00 37.67  ? 3145 ASN A CA    1 
ATOM   14304 C C     . ASN A 1 3145 ? 134.848 127.160 157.050 1.00 37.67  ? 3145 ASN A C     1 
ATOM   14305 O O     . ASN A 1 3145 ? 135.509 127.839 157.839 1.00 37.67  ? 3145 ASN A O     1 
ATOM   14306 C CB    . ASN A 1 3145 ? 132.603 126.325 157.793 1.00 37.67  ? 3145 ASN A CB    1 
ATOM   14307 C CG    . ASN A 1 3145 ? 132.740 126.592 159.274 1.00 37.67  ? 3145 ASN A CG    1 
ATOM   14308 O OD1   . ASN A 1 3145 ? 132.273 127.614 159.775 1.00 37.67  ? 3145 ASN A OD1   1 
ATOM   14309 N ND2   . ASN A 1 3145 ? 133.387 125.678 159.985 1.00 37.67  ? 3145 ASN A ND2   1 
ATOM   14310 N N     . SER A 1 3146 ? 135.407 126.241 156.262 1.00 31.84  ? 3146 SER A N     1 
ATOM   14311 C CA    . SER A 1 3146 ? 136.855 126.056 156.258 1.00 31.84  ? 3146 SER A CA    1 
ATOM   14312 C C     . SER A 1 3146 ? 137.568 127.295 155.730 1.00 31.84  ? 3146 SER A C     1 
ATOM   14313 O O     . SER A 1 3146 ? 138.645 127.652 156.216 1.00 31.84  ? 3146 SER A O     1 
ATOM   14314 C CB    . SER A 1 3146 ? 137.224 124.827 155.430 1.00 31.84  ? 3146 SER A CB    1 
ATOM   14315 O OG    . SER A 1 3146 ? 136.513 123.686 155.873 1.00 31.84  ? 3146 SER A OG    1 
ATOM   14316 N N     . CYS A 1 3147 ? 136.988 127.959 154.729 1.00 27.51  ? 3147 CYS A N     1 
ATOM   14317 C CA    . CYS A 1 3147 ? 137.597 129.177 154.195 1.00 27.51  ? 3147 CYS A CA    1 
ATOM   14318 C C     . CYS A 1 3147 ? 137.615 130.290 155.240 1.00 27.51  ? 3147 CYS A C     1 
ATOM   14319 O O     . CYS A 1 3147 ? 138.640 130.963 155.444 1.00 27.51  ? 3147 CYS A O     1 
ATOM   14320 C CB    . CYS A 1 3147 ? 136.846 129.629 152.943 1.00 27.51  ? 3147 CYS A CB    1 
ATOM   14321 S SG    . CYS A 1 3147 ? 137.037 128.537 151.519 1.00 27.51  ? 3147 CYS A SG    1 
ATOM   14322 N N     . VAL A 1 3148 ? 136.483 130.503 155.916 1.00 27.55  ? 3148 VAL A N     1 
ATOM   14323 C CA    . VAL A 1 3148 ? 136.468 131.536 156.948 1.00 27.55  ? 3148 VAL A CA    1 
ATOM   14324 C C     . VAL A 1 3148 ? 137.369 131.134 158.111 1.00 27.55  ? 3148 VAL A C     1 
ATOM   14325 O O     . VAL A 1 3148 ? 137.967 131.995 158.770 1.00 27.55  ? 3148 VAL A O     1 
ATOM   14326 C CB    . VAL A 1 3148 ? 135.029 131.847 157.404 1.00 27.55  ? 3148 VAL A CB    1 
ATOM   14327 C CG1   . VAL A 1 3148 ? 134.185 132.282 156.219 1.00 27.55  ? 3148 VAL A CG1   1 
ATOM   14328 C CG2   . VAL A 1 3148 ? 134.402 130.664 158.094 1.00 27.55  ? 3148 VAL A CG2   1 
ATOM   14329 N N     . PHE A 1 3149 ? 137.514 129.829 158.363 1.00 27.37  ? 3149 PHE A N     1 
ATOM   14330 C CA    . PHE A 1 3149 ? 138.468 129.369 159.366 1.00 27.37  ? 3149 PHE A CA    1 
ATOM   14331 C C     . PHE A 1 3149 ? 139.896 129.692 158.954 1.00 27.37  ? 3149 PHE A C     1 
ATOM   14332 O O     . PHE A 1 3149 ? 140.727 130.032 159.798 1.00 27.37  ? 3149 PHE A O     1 
ATOM   14333 C CB    . PHE A 1 3149 ? 138.313 127.868 159.596 1.00 27.37  ? 3149 PHE A CB    1 
ATOM   14334 C CG    . PHE A 1 3149 ? 139.300 127.301 160.575 1.00 27.37  ? 3149 PHE A CG    1 
ATOM   14335 C CD1   . PHE A 1 3149 ? 139.060 127.371 161.936 1.00 27.37  ? 3149 PHE A CD1   1 
ATOM   14336 C CD2   . PHE A 1 3149 ? 140.467 126.698 160.138 1.00 27.37  ? 3149 PHE A CD2   1 
ATOM   14337 C CE1   . PHE A 1 3149 ? 139.963 126.851 162.842 1.00 27.37  ? 3149 PHE A CE1   1 
ATOM   14338 C CE2   . PHE A 1 3149 ? 141.373 126.178 161.039 1.00 27.37  ? 3149 PHE A CE2   1 
ATOM   14339 C CZ    . PHE A 1 3149 ? 141.120 126.253 162.392 1.00 27.37  ? 3149 PHE A CZ    1 
ATOM   14340 N N     . VAL A 1 3150 ? 140.205 129.558 157.665 1.00 24.23  ? 3150 VAL A N     1 
ATOM   14341 C CA    . VAL A 1 3150 ? 141.535 129.913 157.178 1.00 24.23  ? 3150 VAL A CA    1 
ATOM   14342 C C     . VAL A 1 3150 ? 141.805 131.392 157.418 1.00 24.23  ? 3150 VAL A C     1 
ATOM   14343 O O     . VAL A 1 3150 ? 142.881 131.779 157.897 1.00 24.23  ? 3150 VAL A O     1 
ATOM   14344 C CB    . VAL A 1 3150 ? 141.677 129.544 155.690 1.00 24.23  ? 3150 VAL A CB    1 
ATOM   14345 C CG1   . VAL A 1 3150 ? 142.886 130.232 155.087 1.00 24.23  ? 3150 VAL A CG1   1 
ATOM   14346 C CG2   . VAL A 1 3150 ? 141.784 128.039 155.526 1.00 24.23  ? 3150 VAL A CG2   1 
ATOM   14347 N N     . HIS A 1 3151 ? 140.827 132.242 157.102 1.00 23.47  ? 3151 HIS A N     1 
ATOM   14348 C CA    . HIS A 1 3151 ? 141.003 133.673 157.350 1.00 23.47  ? 3151 HIS A CA    1 
ATOM   14349 C C     . HIS A 1 3151 ? 141.211 133.954 158.838 1.00 23.47  ? 3151 HIS A C     1 
ATOM   14350 O O     . HIS A 1 3151 ? 142.098 134.734 159.221 1.00 23.47  ? 3151 HIS A O     1 
ATOM   14351 C CB    . HIS A 1 3151 ? 139.801 134.449 156.814 1.00 23.47  ? 3151 HIS A CB    1 
ATOM   14352 C CG    . HIS A 1 3151 ? 140.039 135.921 156.688 1.00 23.47  ? 3151 HIS A CG    1 
ATOM   14353 N ND1   . HIS A 1 3151 ? 140.286 136.535 155.479 1.00 23.47  ? 3151 HIS A ND1   1 
ATOM   14354 C CD2   . HIS A 1 3151 ? 140.060 136.903 157.618 1.00 23.47  ? 3151 HIS A CD2   1 
ATOM   14355 C CE1   . HIS A 1 3151 ? 140.454 137.830 155.671 1.00 23.47  ? 3151 HIS A CE1   1 
ATOM   14356 N NE2   . HIS A 1 3151 ? 140.322 138.080 156.961 1.00 23.47  ? 3151 HIS A NE2   1 
ATOM   14357 N N     . GLN A 1 3152 ? 140.418 133.306 159.694 1.00 24.66  ? 3152 GLN A N     1 
ATOM   14358 C CA    . GLN A 1 3152 ? 140.565 133.512 161.131 1.00 24.66  ? 3152 GLN A CA    1 
ATOM   14359 C C     . GLN A 1 3152 ? 141.914 133.009 161.631 1.00 24.66  ? 3152 GLN A C     1 
ATOM   14360 O O     . GLN A 1 3152 ? 142.495 133.587 162.556 1.00 24.66  ? 3152 GLN A O     1 
ATOM   14361 C CB    . GLN A 1 3152 ? 139.420 132.830 161.879 1.00 24.66  ? 3152 GLN A CB    1 
ATOM   14362 C CG    . GLN A 1 3152 ? 138.099 133.574 161.782 1.00 24.66  ? 3152 GLN A CG    1 
ATOM   14363 C CD    . GLN A 1 3152 ? 137.014 132.948 162.632 1.00 24.66  ? 3152 GLN A CD    1 
ATOM   14364 O OE1   . GLN A 1 3152 ? 137.256 131.981 163.353 1.00 24.66  ? 3152 GLN A OE1   1 
ATOM   14365 N NE2   . GLN A 1 3152 ? 135.809 133.501 162.555 1.00 24.66  ? 3152 GLN A NE2   1 
ATOM   14366 N N     . THR A 1 3153 ? 142.431 131.931 161.037 1.00 24.89  ? 3153 THR A N     1 
ATOM   14367 C CA    . THR A 1 3153 ? 143.735 131.427 161.451 1.00 24.89  ? 3153 THR A CA    1 
ATOM   14368 C C     . THR A 1 3153 ? 144.855 132.360 161.030 1.00 24.89  ? 3153 THR A C     1 
ATOM   14369 O O     . THR A 1 3153 ? 145.845 132.488 161.751 1.00 24.89  ? 3153 THR A O     1 
ATOM   14370 C CB    . THR A 1 3153 ? 143.989 130.030 160.890 1.00 24.89  ? 3153 THR A CB    1 
ATOM   14371 O OG1   . THR A 1 3153 ? 143.660 130.001 159.497 1.00 24.89  ? 3153 THR A OG1   1 
ATOM   14372 C CG2   . THR A 1 3153 ? 143.166 129.007 161.637 1.00 24.89  ? 3153 THR A CG2   1 
ATOM   14373 N N     . LEU A 1 3154 ? 144.733 133.009 159.871 1.00 25.07  ? 3154 LEU A N     1 
ATOM   14374 C CA    . LEU A 1 3154 ? 145.702 134.052 159.541 1.00 25.07  ? 3154 LEU A CA    1 
ATOM   14375 C C     . LEU A 1 3154 ? 145.632 135.207 160.532 1.00 25.07  ? 3154 LEU A C     1 
ATOM   14376 O O     . LEU A 1 3154 ? 146.671 135.743 160.941 1.00 25.07  ? 3154 LEU A O     1 
ATOM   14377 C CB    . LEU A 1 3154 ? 145.518 134.555 158.111 1.00 25.07  ? 3154 LEU A CB    1 
ATOM   14378 C CG    . LEU A 1 3154 ? 146.187 133.738 157.002 1.00 25.07  ? 3154 LEU A CG    1 
ATOM   14379 C CD1   . LEU A 1 3154 ? 147.696 133.787 157.187 1.00 25.07  ? 3154 LEU A CD1   1 
ATOM   14380 C CD2   . LEU A 1 3154 ? 145.716 132.304 156.926 1.00 25.07  ? 3154 LEU A CD2   1 
ATOM   14381 N N     . HIS A 1 3155 ? 144.423 135.601 160.939 1.00 25.32  ? 3155 HIS A N     1 
ATOM   14382 C CA    . HIS A 1 3155 ? 144.312 136.636 161.968 1.00 25.32  ? 3155 HIS A CA    1 
ATOM   14383 C C     . HIS A 1 3155 ? 145.006 136.210 163.260 1.00 25.32  ? 3155 HIS A C     1 
ATOM   14384 O O     . HIS A 1 3155 ? 145.769 136.982 163.857 1.00 25.32  ? 3155 HIS A O     1 
ATOM   14385 C CB    . HIS A 1 3155 ? 142.846 136.973 162.239 1.00 25.32  ? 3155 HIS A CB    1 
ATOM   14386 C CG    . HIS A 1 3155 ? 142.270 137.973 161.289 1.00 25.32  ? 3155 HIS A CG    1 
ATOM   14387 N ND1   . HIS A 1 3155 ? 142.681 139.288 161.254 1.00 25.32  ? 3155 HIS A ND1   1 
ATOM   14388 C CD2   . HIS A 1 3155 ? 141.302 137.858 160.350 1.00 25.32  ? 3155 HIS A CD2   1 
ATOM   14389 C CE1   . HIS A 1 3155 ? 141.998 139.937 160.327 1.00 25.32  ? 3155 HIS A CE1   1 
ATOM   14390 N NE2   . HIS A 1 3155 ? 141.154 139.091 159.764 1.00 25.32  ? 3155 HIS A NE2   1 
ATOM   14391 N N     . GLN A 1 3156 ? 144.754 134.977 163.704 1.00 28.25  ? 3156 GLN A N     1 
ATOM   14392 C CA    . GLN A 1 3156 ? 145.360 134.493 164.941 1.00 28.25  ? 3156 GLN A CA    1 
ATOM   14393 C C     . GLN A 1 3156 ? 146.872 134.363 164.821 1.00 28.25  ? 3156 GLN A C     1 
ATOM   14394 O O     . GLN A 1 3156 ? 147.592 134.645 165.783 1.00 28.25  ? 3156 GLN A O     1 
ATOM   14395 C CB    . GLN A 1 3156 ? 144.747 133.152 165.347 1.00 28.25  ? 3156 GLN A CB    1 
ATOM   14396 C CG    . GLN A 1 3156 ? 143.256 133.204 165.630 1.00 28.25  ? 3156 GLN A CG    1 
ATOM   14397 C CD    . GLN A 1 3156 ? 142.620 131.827 165.654 1.00 28.25  ? 3156 GLN A CD    1 
ATOM   14398 O OE1   . GLN A 1 3156 ? 143.314 130.811 165.655 1.00 28.25  ? 3156 GLN A OE1   1 
ATOM   14399 N NE2   . GLN A 1 3156 ? 141.293 131.788 165.671 1.00 28.25  ? 3156 GLN A NE2   1 
ATOM   14400 N N     . ALA A 1 3157 ? 147.371 133.926 163.663 1.00 29.85  ? 3157 ALA A N     1 
ATOM   14401 C CA    . ALA A 1 3157 ? 148.811 133.828 163.461 1.00 29.85  ? 3157 ALA A CA    1 
ATOM   14402 C C     . ALA A 1 3157 ? 149.464 135.201 163.489 1.00 29.85  ? 3157 ALA A C     1 
ATOM   14403 O O     . ALA A 1 3157 ? 150.545 135.365 164.063 1.00 29.85  ? 3157 ALA A O     1 
ATOM   14404 C CB    . ALA A 1 3157 ? 149.111 133.117 162.143 1.00 29.85  ? 3157 ALA A CB    1 
ATOM   14405 N N     . ASN A 1 3158 ? 148.825 136.200 162.874 1.00 35.25  ? 3158 ASN A N     1 
ATOM   14406 C CA    . ASN A 1 3158 ? 149.350 137.559 162.950 1.00 35.25  ? 3158 ASN A CA    1 
ATOM   14407 C C     . ASN A 1 3158 ? 149.366 138.061 164.388 1.00 35.25  ? 3158 ASN A C     1 
ATOM   14408 O O     . ASN A 1 3158 ? 150.342 138.684 164.825 1.00 35.25  ? 3158 ASN A O     1 
ATOM   14409 C CB    . ASN A 1 3158 ? 148.527 138.494 162.066 1.00 35.25  ? 3158 ASN A CB    1 
ATOM   14410 C CG    . ASN A 1 3158 ? 149.150 138.700 160.703 1.00 35.25  ? 3158 ASN A CG    1 
ATOM   14411 O OD1   . ASN A 1 3158 ? 150.079 137.993 160.319 1.00 35.25  ? 3158 ASN A OD1   1 
ATOM   14412 N ND2   . ASN A 1 3158 ? 148.644 139.679 159.965 1.00 35.25  ? 3158 ASN A ND2   1 
ATOM   14413 N N     . ALA A 1 3159 ? 148.298 137.792 165.143 1.00 36.64  ? 3159 ALA A N     1 
ATOM   14414 C CA    . ALA A 1 3159 ? 148.260 138.216 166.540 1.00 36.64  ? 3159 ALA A CA    1 
ATOM   14415 C C     . ALA A 1 3159 ? 149.355 137.540 167.358 1.00 36.64  ? 3159 ALA A C     1 
ATOM   14416 O O     . ALA A 1 3159 ? 150.025 138.189 168.171 1.00 36.64  ? 3159 ALA A O     1 
ATOM   14417 C CB    . ALA A 1 3159 ? 146.885 137.925 167.140 1.00 36.64  ? 3159 ALA A CB    1 
ATOM   14418 N N     . ARG A 1 3160 ? 149.553 136.236 167.156 1.00 39.94  ? 3160 ARG A N     1 
ATOM   14419 C CA    . ARG A 1 3160 ? 150.590 135.514 167.887 1.00 39.94  ? 3160 ARG A CA    1 
ATOM   14420 C C     . ARG A 1 3160 ? 151.980 136.018 167.519 1.00 39.94  ? 3160 ARG A C     1 
ATOM   14421 O O     . ARG A 1 3160 ? 152.837 136.184 168.394 1.00 39.94  ? 3160 ARG A O     1 
ATOM   14422 C CB    . ARG A 1 3160 ? 150.472 134.015 167.614 1.00 39.94  ? 3160 ARG A CB    1 
ATOM   14423 C CG    . ARG A 1 3160 ? 151.713 133.215 167.974 1.00 39.94  ? 3160 ARG A CG    1 
ATOM   14424 C CD    . ARG A 1 3160 ? 151.759 131.899 167.214 1.00 39.94  ? 3160 ARG A CD    1 
ATOM   14425 N NE    . ARG A 1 3160 ? 150.503 131.165 167.316 1.00 39.94  ? 3160 ARG A NE    1 
ATOM   14426 C CZ    . ARG A 1 3160 ? 150.350 130.037 167.995 1.00 39.94  ? 3160 ARG A CZ    1 
ATOM   14427 N NH1   . ARG A 1 3160 ? 151.358 129.479 168.646 1.00 39.94  ? 3160 ARG A NH1   1 
ATOM   14428 N NH2   . ARG A 1 3160 ? 149.155 129.453 168.023 1.00 39.94  ? 3160 ARG A NH2   1 
ATOM   14429 N N     . LEU A 1 3161 ? 152.220 136.268 166.230 1.00 41.16  ? 3161 LEU A N     1 
ATOM   14430 C CA    . LEU A 1 3161 ? 153.513 136.789 165.802 1.00 41.16  ? 3161 LEU A CA    1 
ATOM   14431 C C     . LEU A 1 3161 ? 153.762 138.176 166.379 1.00 41.16  ? 3161 LEU A C     1 
ATOM   14432 O O     . LEU A 1 3161 ? 154.900 138.520 166.718 1.00 41.16  ? 3161 LEU A O     1 
ATOM   14433 C CB    . LEU A 1 3161 ? 153.581 136.816 164.276 1.00 41.16  ? 3161 LEU A CB    1 
ATOM   14434 C CG    . LEU A 1 3161 ? 154.937 136.559 163.621 1.00 41.16  ? 3161 LEU A CG    1 
ATOM   14435 C CD1   . LEU A 1 3161 ? 155.440 135.171 163.965 1.00 41.16  ? 3161 LEU A CD1   1 
ATOM   14436 C CD2   . LEU A 1 3161 ? 154.839 136.736 162.114 1.00 41.16  ? 3161 LEU A CD2   1 
ATOM   14437 N N     . ALA A 1 3162 ? 152.711 138.991 166.489 1.00 45.10  ? 3162 ALA A N     1 
ATOM   14438 C CA    . ALA A 1 3162 ? 152.848 140.279 167.159 1.00 45.10  ? 3162 ALA A CA    1 
ATOM   14439 C C     . ALA A 1 3162 ? 153.170 140.098 168.637 1.00 45.10  ? 3162 ALA A C     1 
ATOM   14440 O O     . ALA A 1 3162 ? 153.962 140.860 169.204 1.00 45.10  ? 3162 ALA A O     1 
ATOM   14441 C CB    . ALA A 1 3162 ? 151.574 141.104 166.983 1.00 45.10  ? 3162 ALA A CB    1 
ATOM   14442 N N     . LYS A 1 3163 ? 152.559 139.099 169.280 1.00 46.69  ? 3163 LYS A N     1 
ATOM   14443 C CA    . LYS A 1 3163 ? 152.820 138.855 170.695 1.00 46.69  ? 3163 LYS A CA    1 
ATOM   14444 C C     . LYS A 1 3163 ? 154.272 138.455 170.929 1.00 46.69  ? 3163 LYS A C     1 
ATOM   14445 O O     . LYS A 1 3163 ? 154.947 139.006 171.807 1.00 46.69  ? 3163 LYS A O     1 
ATOM   14446 C CB    . LYS A 1 3163 ? 151.876 137.777 171.225 1.00 46.69  ? 3163 LYS A CB    1 
ATOM   14447 C CG    . LYS A 1 3163 ? 152.237 137.267 172.610 1.00 46.69  ? 3163 LYS A CG    1 
ATOM   14448 C CD    . LYS A 1 3163 ? 151.246 136.219 173.090 1.00 46.69  ? 3163 LYS A CD    1 
ATOM   14449 C CE    . LYS A 1 3163 ? 151.683 135.613 174.414 1.00 46.69  ? 3163 LYS A CE    1 
ATOM   14450 N NZ    . LYS A 1 3163 ? 150.776 134.515 174.846 1.00 46.69  ? 3163 LYS A NZ    1 
ATOM   14451 N N     . ARG A 1 3164 ? 154.774 137.495 170.152 1.00 49.50  ? 3164 ARG A N     1 
ATOM   14452 C CA    . ARG A 1 3164 ? 156.153 137.029 170.288 1.00 49.50  ? 3164 ARG A CA    1 
ATOM   14453 C C     . ARG A 1 3164 ? 156.998 137.826 169.297 1.00 49.50  ? 3164 ARG A C     1 
ATOM   14454 O O     . ARG A 1 3164 ? 157.098 137.508 168.113 1.00 49.50  ? 3164 ARG A O     1 
ATOM   14455 C CB    . ARG A 1 3164 ? 156.239 135.518 170.063 1.00 49.50  ? 3164 ARG A CB    1 
ATOM   14456 C CG    . ARG A 1 3164 ? 157.642 134.969 169.807 1.00 49.50  ? 3164 ARG A CG    1 
ATOM   14457 C CD    . ARG A 1 3164 ? 157.844 134.516 168.367 1.00 49.50  ? 3164 ARG A CD    1 
ATOM   14458 N NE    . ARG A 1 3164 ? 157.075 133.319 168.051 1.00 49.50  ? 3164 ARG A NE    1 
ATOM   14459 C CZ    . ARG A 1 3164 ? 156.933 132.822 166.829 1.00 49.50  ? 3164 ARG A CZ    1 
ATOM   14460 N NH1   . ARG A 1 3164 ? 157.518 133.382 165.784 1.00 49.50  ? 3164 ARG A NH1   1 
ATOM   14461 N NH2   . ARG A 1 3164 ? 156.191 131.732 166.654 1.00 49.50  ? 3164 ARG A NH2   1 
ATOM   14462 N N     . GLY A 1 3165 ? 157.591 138.897 169.796 1.00 49.38  ? 3165 GLY A N     1 
ATOM   14463 C CA    . GLY A 1 3165 ? 158.356 139.805 168.940 1.00 49.38  ? 3165 GLY A CA    1 
ATOM   14464 C C     . GLY A 1 3165 ? 157.440 140.782 168.200 1.00 49.38  ? 3165 GLY A C     1 
ATOM   14465 O O     . GLY A 1 3165 ? 156.944 141.734 168.793 1.00 49.38  ? 3165 GLY A O     1 
ATOM   14466 N N     . GLY A 1 3166 ? 157.232 140.530 166.910 1.00 50.12  ? 3166 GLY A N     1 
ATOM   14467 C CA    . GLY A 1 3166 ? 156.355 141.352 166.101 1.00 50.12  ? 3166 GLY A CA    1 
ATOM   14468 C C     . GLY A 1 3166 ? 156.559 141.126 164.618 1.00 50.12  ? 3166 GLY A C     1 
ATOM   14469 O O     . GLY A 1 3166 ? 156.597 139.980 164.159 1.00 50.12  ? 3166 GLY A O     1 
ATOM   14470 N N     . ARG A 1 3167 ? 156.691 142.218 163.864 1.00 48.53  ? 3167 ARG A N     1 
ATOM   14471 C CA    . ARG A 1 3167 ? 157.010 142.177 162.438 1.00 48.53  ? 3167 ARG A CA    1 
ATOM   14472 C C     . ARG A 1 3167 ? 155.933 141.413 161.660 1.00 48.53  ? 3167 ARG A C     1 
ATOM   14473 O O     . ARG A 1 3167 ? 156.160 140.331 161.114 1.00 48.53  ? 3167 ARG A O     1 
ATOM   14474 C CB    . ARG A 1 3167 ? 158.406 141.577 162.219 1.00 48.53  ? 3167 ARG A CB    1 
ATOM   14475 C CG    . ARG A 1 3167 ? 158.940 141.557 160.782 1.00 48.53  ? 3167 ARG A CG    1 
ATOM   14476 C CD    . ARG A 1 3167 ? 159.314 142.945 160.255 1.00 48.53  ? 3167 ARG A CD    1 
ATOM   14477 N NE    . ARG A 1 3167 ? 158.205 143.891 160.241 1.00 48.53  ? 3167 ARG A NE    1 
ATOM   14478 C CZ    . ARG A 1 3167 ? 158.241 145.076 159.650 1.00 48.53  ? 3167 ARG A CZ    1 
ATOM   14479 N NH1   . ARG A 1 3167 ? 159.332 145.512 159.046 1.00 48.53  ? 3167 ARG A NH1   1 
ATOM   14480 N NH2   . ARG A 1 3167 ? 157.157 145.845 159.675 1.00 48.53  ? 3167 ARG A NH2   1 
ATOM   14481 N N     . THR A 1 3168 ? 154.736 141.993 161.640 1.00 44.58  ? 3168 THR A N     1 
ATOM   14482 C CA    . THR A 1 3168 ? 153.573 141.392 161.005 1.00 44.58  ? 3168 THR A CA    1 
ATOM   14483 C C     . THR A 1 3168 ? 152.991 142.336 159.960 1.00 44.58  ? 3168 THR A C     1 
ATOM   14484 O O     . THR A 1 3168 ? 153.142 143.558 160.035 1.00 44.58  ? 3168 THR A O     1 
ATOM   14485 C CB    . THR A 1 3168 ? 152.495 141.045 162.038 1.00 44.58  ? 3168 THR A CB    1 
ATOM   14486 O OG1   . THR A 1 3168 ? 152.057 142.243 162.689 1.00 44.58  ? 3168 THR A OG1   1 
ATOM   14487 C CG2   . THR A 1 3168 ? 153.047 140.096 163.077 1.00 44.58  ? 3168 THR A CG2   1 
ATOM   14488 N N     . MET A 1 3169 ? 152.311 141.747 158.980 1.00 40.13  ? 3169 MET A N     1 
ATOM   14489 C CA    . MET A 1 3169 ? 151.578 142.487 157.964 1.00 40.13  ? 3169 MET A CA    1 
ATOM   14490 C C     . MET A 1 3169 ? 150.086 142.266 158.161 1.00 40.13  ? 3169 MET A C     1 
ATOM   14491 O O     . MET A 1 3169 ? 149.647 141.145 158.432 1.00 40.13  ? 3169 MET A O     1 
ATOM   14492 C CB    . MET A 1 3169 ? 151.991 142.062 156.553 1.00 40.13  ? 3169 MET A CB    1 
ATOM   14493 C CG    . MET A 1 3169 ? 153.439 142.367 156.216 1.00 40.13  ? 3169 MET A CG    1 
ATOM   14494 S SD    . MET A 1 3169 ? 153.999 143.922 156.932 1.00 40.13  ? 3169 MET A SD    1 
ATOM   14495 C CE    . MET A 1 3169 ? 155.701 143.956 156.382 1.00 40.13  ? 3169 MET A CE    1 
ATOM   14496 N N     . ALA A 1 3170 ? 149.314 143.341 158.025 1.00 32.71  ? 3170 ALA A N     1 
ATOM   14497 C CA    . ALA A 1 3170 ? 147.888 143.281 158.316 1.00 32.71  ? 3170 ALA A CA    1 
ATOM   14498 C C     . ALA A 1 3170 ? 147.157 142.396 157.315 1.00 32.71  ? 3170 ALA A C     1 
ATOM   14499 O O     . ALA A 1 3170 ? 147.462 142.394 156.120 1.00 32.71  ? 3170 ALA A O     1 
ATOM   14500 C CB    . ALA A 1 3170 ? 147.289 144.687 158.306 1.00 32.71  ? 3170 ALA A CB    1 
ATOM   14501 N N     . ILE A 1 3171 ? 146.183 141.640 157.817 1.00 27.11  ? 3171 ILE A N     1 
ATOM   14502 C CA    . ILE A 1 3171 ? 145.307 140.819 156.990 1.00 27.11  ? 3171 ILE A CA    1 
ATOM   14503 C C     . ILE A 1 3171 ? 144.006 141.576 156.779 1.00 27.11  ? 3171 ILE A C     1 
ATOM   14504 O O     . ILE A 1 3171 ? 143.376 142.027 157.743 1.00 27.11  ? 3171 ILE A O     1 
ATOM   14505 C CB    . ILE A 1 3171 ? 145.051 139.447 157.635 1.00 27.11  ? 3171 ILE A CB    1 
ATOM   14506 C CG1   . ILE A 1 3171 ? 146.365 138.682 157.797 1.00 27.11  ? 3171 ILE A CG1   1 
ATOM   14507 C CG2   . ILE A 1 3171 ? 144.065 138.645 156.804 1.00 27.11  ? 3171 ILE A CG2   1 
ATOM   14508 C CD1   . ILE A 1 3171 ? 147.114 138.476 156.500 1.00 27.11  ? 3171 ILE A CD1   1 
ATOM   14509 N N     . THR A 1 3172 ? 143.601 141.711 155.526 1.00 26.94  ? 3172 THR A N     1 
ATOM   14510 C CA    . THR A 1 3172 ? 142.478 142.538 155.120 1.00 26.94  ? 3172 THR A CA    1 
ATOM   14511 C C     . THR A 1 3172 ? 141.463 141.691 154.373 1.00 26.94  ? 3172 THR A C     1 
ATOM   14512 O O     . THR A 1 3172 ? 141.789 140.600 153.892 1.00 26.94  ? 3172 THR A O     1 
ATOM   14513 C CB    . THR A 1 3172 ? 142.952 143.693 154.226 1.00 26.94  ? 3172 THR A CB    1 
ATOM   14514 O OG1   . THR A 1 3172 ? 143.706 143.168 153.127 1.00 26.94  ? 3172 THR A OG1   1 
ATOM   14515 C CG2   . THR A 1 3172 ? 143.828 144.648 155.015 1.00 26.94  ? 3172 THR A CG2   1 
ATOM   14516 N N     . PRO A 1 3173 ? 140.215 142.154 154.271 1.00 26.36  ? 3173 PRO A N     1 
ATOM   14517 C CA    . PRO A 1 3173 ? 139.234 141.427 153.450 1.00 26.36  ? 3173 PRO A CA    1 
ATOM   14518 C C     . PRO A 1 3173 ? 139.653 141.281 151.999 1.00 26.36  ? 3173 PRO A C     1 
ATOM   14519 O O     . PRO A 1 3173 ? 139.195 140.345 151.330 1.00 26.36  ? 3173 PRO A O     1 
ATOM   14520 C CB    . PRO A 1 3173 ? 137.966 142.277 153.583 1.00 26.36  ? 3173 PRO A CB    1 
ATOM   14521 C CG    . PRO A 1 3173 ? 138.119 142.963 154.888 1.00 26.36  ? 3173 PRO A CG    1 
ATOM   14522 C CD    . PRO A 1 3173 ? 139.586 143.237 155.046 1.00 26.36  ? 3173 PRO A CD    1 
ATOM   14523 N N     . ARG A 1 3174 ? 140.501 142.177 151.489 1.00 29.54  ? 3174 ARG A N     1 
ATOM   14524 C CA    . ARG A 1 3174 ? 141.044 141.995 150.148 1.00 29.54  ? 3174 ARG A CA    1 
ATOM   14525 C C     . ARG A 1 3174 ? 141.804 140.679 150.048 1.00 29.54  ? 3174 ARG A C     1 
ATOM   14526 O O     . ARG A 1 3174 ? 141.776 140.015 149.006 1.00 29.54  ? 3174 ARG A O     1 
ATOM   14527 C CB    . ARG A 1 3174 ? 141.952 143.167 149.784 1.00 29.54  ? 3174 ARG A CB    1 
ATOM   14528 C CG    . ARG A 1 3174 ? 141.839 143.620 148.339 1.00 29.54  ? 3174 ARG A CG    1 
ATOM   14529 C CD    . ARG A 1 3174 ? 142.910 144.644 148.010 1.00 29.54  ? 3174 ARG A CD    1 
ATOM   14530 N NE    . ARG A 1 3174 ? 142.411 146.014 148.010 1.00 29.54  ? 3174 ARG A NE    1 
ATOM   14531 C CZ    . ARG A 1 3174 ? 141.691 146.551 147.035 1.00 29.54  ? 3174 ARG A CZ    1 
ATOM   14532 N NH1   . ARG A 1 3174 ? 141.344 145.853 145.966 1.00 29.54  ? 3174 ARG A NH1   1 
ATOM   14533 N NH2   . ARG A 1 3174 ? 141.319 147.824 147.130 1.00 29.54  ? 3174 ARG A NH2   1 
ATOM   14534 N N     . HIS A 1 3175 ? 142.479 140.280 151.129 1.00 25.18  ? 3175 HIS A N     1 
ATOM   14535 C CA    . HIS A 1 3175 ? 143.121 138.971 151.157 1.00 25.18  ? 3175 HIS A CA    1 
ATOM   14536 C C     . HIS A 1 3175 ? 142.094 137.853 151.044 1.00 25.18  ? 3175 HIS A C     1 
ATOM   14537 O O     . HIS A 1 3175 ? 142.339 136.843 150.377 1.00 25.18  ? 3175 HIS A O     1 
ATOM   14538 C CB    . HIS A 1 3175 ? 143.942 138.810 152.436 1.00 25.18  ? 3175 HIS A CB    1 
ATOM   14539 C CG    . HIS A 1 3175 ? 145.212 139.601 152.446 1.00 25.18  ? 3175 HIS A CG    1 
ATOM   14540 N ND1   . HIS A 1 3175 ? 145.380 140.728 153.219 1.00 25.18  ? 3175 HIS A ND1   1 
ATOM   14541 C CD2   . HIS A 1 3175 ? 146.381 139.418 151.788 1.00 25.18  ? 3175 HIS A CD2   1 
ATOM   14542 C CE1   . HIS A 1 3175 ? 146.595 141.212 153.031 1.00 25.18  ? 3175 HIS A CE1   1 
ATOM   14543 N NE2   . HIS A 1 3175 ? 147.222 140.436 152.166 1.00 25.18  ? 3175 HIS A NE2   1 
ATOM   14544 N N     . TYR A 1 3176 ? 140.941 138.008 151.698 1.00 24.13  ? 3176 TYR A N     1 
ATOM   14545 C CA    . TYR A 1 3176 ? 139.898 136.992 151.599 1.00 24.13  ? 3176 TYR A CA    1 
ATOM   14546 C C     . TYR A 1 3176 ? 139.357 136.893 150.180 1.00 24.13  ? 3176 TYR A C     1 
ATOM   14547 O O     . TYR A 1 3176 ? 139.133 135.790 149.667 1.00 24.13  ? 3176 TYR A O     1 
ATOM   14548 C CB    . TYR A 1 3176 ? 138.772 137.296 152.583 1.00 24.13  ? 3176 TYR A CB    1 
ATOM   14549 C CG    . TYR A 1 3176 ? 137.769 136.176 152.720 1.00 24.13  ? 3176 TYR A CG    1 
ATOM   14550 C CD1   . TYR A 1 3176 ? 138.162 134.916 153.143 1.00 24.13  ? 3176 TYR A CD1   1 
ATOM   14551 C CD2   . TYR A 1 3176 ? 136.431 136.379 152.426 1.00 24.13  ? 3176 TYR A CD2   1 
ATOM   14552 C CE1   . TYR A 1 3176 ? 137.250 133.891 153.270 1.00 24.13  ? 3176 TYR A CE1   1 
ATOM   14553 C CE2   . TYR A 1 3176 ? 135.512 135.360 152.551 1.00 24.13  ? 3176 TYR A CE2   1 
ATOM   14554 C CZ    . TYR A 1 3176 ? 135.926 134.119 152.972 1.00 24.13  ? 3176 TYR A CZ    1 
ATOM   14555 O OH    . TYR A 1 3176 ? 135.009 133.103 153.094 1.00 24.13  ? 3176 TYR A OH    1 
ATOM   14556 N N     . LEU A 1 3177 ? 139.135 138.037 149.529 1.00 25.02  ? 3177 LEU A N     1 
ATOM   14557 C CA    . LEU A 1 3177 ? 138.705 138.015 148.134 1.00 25.02  ? 3177 LEU A CA    1 
ATOM   14558 C C     . LEU A 1 3177 ? 139.754 137.361 147.245 1.00 25.02  ? 3177 LEU A C     1 
ATOM   14559 O O     . LEU A 1 3177 ? 139.416 136.584 146.345 1.00 25.02  ? 3177 LEU A O     1 
ATOM   14560 C CB    . LEU A 1 3177 ? 138.399 139.429 147.642 1.00 25.02  ? 3177 LEU A CB    1 
ATOM   14561 C CG    . LEU A 1 3177 ? 137.008 140.007 147.914 1.00 25.02  ? 3177 LEU A CG    1 
ATOM   14562 C CD1   . LEU A 1 3177 ? 135.959 139.190 147.183 1.00 25.02  ? 3177 LEU A CD1   1 
ATOM   14563 C CD2   . LEU A 1 3177 ? 136.696 140.069 149.391 1.00 25.02  ? 3177 LEU A CD2   1 
ATOM   14564 N N     . ASP A 1 3178 ? 141.032 137.664 147.484 1.00 26.30  ? 3178 ASP A N     1 
ATOM   14565 C CA    . ASP A 1 3178 ? 142.097 137.045 146.705 1.00 26.30  ? 3178 ASP A CA    1 
ATOM   14566 C C     . ASP A 1 3178 ? 142.118 135.535 146.903 1.00 26.30  ? 3178 ASP A C     1 
ATOM   14567 O O     . ASP A 1 3178 ? 142.289 134.778 145.941 1.00 26.30  ? 3178 ASP A O     1 
ATOM   14568 C CB    . ASP A 1 3178 ? 143.446 137.647 147.090 1.00 26.30  ? 3178 ASP A CB    1 
ATOM   14569 C CG    . ASP A 1 3178 ? 144.476 137.488 146.002 1.00 26.30  ? 3178 ASP A CG    1 
ATOM   14570 O OD1   . ASP A 1 3178 ? 144.086 137.072 144.894 1.00 26.30  ? 3178 ASP A OD1   1 
ATOM   14571 O OD2   . ASP A 1 3178 ? 145.667 137.764 146.252 1.00 26.30  ? 3178 ASP A OD2   1 
ATOM   14572 N N     . PHE A 1 3179 ? 141.953 135.082 148.143 1.00 22.68  ? 3179 PHE A N     1 
ATOM   14573 C CA    . PHE A 1 3179 ? 141.946 133.661 148.458 1.00 22.68  ? 3179 PHE A CA    1 
ATOM   14574 C C     . PHE A 1 3179 ? 140.780 132.971 147.766 1.00 22.68  ? 3179 PHE A C     1 
ATOM   14575 O O     . PHE A 1 3179 ? 140.948 131.892 147.193 1.00 22.68  ? 3179 PHE A O     1 
ATOM   14576 C CB    . PHE A 1 3179 ? 141.879 133.455 149.971 1.00 22.68  ? 3179 PHE A CB    1 
ATOM   14577 C CG    . PHE A 1 3179 ? 141.419 132.085 150.385 1.00 22.68  ? 3179 PHE A CG    1 
ATOM   14578 C CD1   . PHE A 1 3179 ? 142.044 130.948 149.904 1.00 22.68  ? 3179 PHE A CD1   1 
ATOM   14579 C CD2   . PHE A 1 3179 ? 140.368 131.938 151.270 1.00 22.68  ? 3179 PHE A CD2   1 
ATOM   14580 C CE1   . PHE A 1 3179 ? 141.620 129.693 150.288 1.00 22.68  ? 3179 PHE A CE1   1 
ATOM   14581 C CE2   . PHE A 1 3179 ? 139.944 130.686 151.659 1.00 22.68  ? 3179 PHE A CE2   1 
ATOM   14582 C CZ    . PHE A 1 3179 ? 140.570 129.563 151.167 1.00 22.68  ? 3179 PHE A CZ    1 
ATOM   14583 N N     . ILE A 1 3180 ? 139.597 133.587 147.805 1.00 22.54  ? 3180 ILE A N     1 
ATOM   14584 C CA    . ILE A 1 3180 ? 138.436 132.987 147.153 1.00 22.54  ? 3180 ILE A CA    1 
ATOM   14585 C C     . ILE A 1 3180 ? 138.625 132.931 145.643 1.00 22.54  ? 3180 ILE A C     1 
ATOM   14586 O O     . ILE A 1 3180 ? 138.277 131.930 145.002 1.00 22.54  ? 3180 ILE A O     1 
ATOM   14587 C CB    . ILE A 1 3180 ? 137.154 133.749 147.538 1.00 22.54  ? 3180 ILE A CB    1 
ATOM   14588 C CG1   . ILE A 1 3180 ? 136.827 133.520 149.014 1.00 22.54  ? 3180 ILE A CG1   1 
ATOM   14589 C CG2   . ILE A 1 3180 ? 135.994 133.304 146.674 1.00 22.54  ? 3180 ILE A CG2   1 
ATOM   14590 C CD1   . ILE A 1 3180 ? 136.448 132.095 149.339 1.00 22.54  ? 3180 ILE A CD1   1 
ATOM   14591 N N     . ASN A 1 3181 ? 139.172 133.992 145.050 1.00 26.40  ? 3181 ASN A N     1 
ATOM   14592 C CA    . ASN A 1 3181 ? 139.415 134.013 143.612 1.00 26.40  ? 3181 ASN A CA    1 
ATOM   14593 C C     . ASN A 1 3181 ? 140.416 132.939 143.208 1.00 26.40  ? 3181 ASN A C     1 
ATOM   14594 O O     . ASN A 1 3181 ? 140.209 132.236 142.213 1.00 26.40  ? 3181 ASN A O     1 
ATOM   14595 C CB    . ASN A 1 3181 ? 139.911 135.392 143.171 1.00 26.40  ? 3181 ASN A CB    1 
ATOM   14596 C CG    . ASN A 1 3181 ? 138.827 136.449 143.240 1.00 26.40  ? 3181 ASN A CG    1 
ATOM   14597 O OD1   . ASN A 1 3181 ? 137.694 136.168 143.631 1.00 26.40  ? 3181 ASN A OD1   1 
ATOM   14598 N ND2   . ASN A 1 3181 ? 139.170 137.673 142.857 1.00 26.40  ? 3181 ASN A ND2   1 
ATOM   14599 N N     . HIS A 1 3182 ? 141.502 132.803 143.971 1.00 26.40  ? 3182 HIS A N     1 
ATOM   14600 C CA    . HIS A 1 3182 ? 142.486 131.760 143.710 1.00 26.40  ? 3182 HIS A CA    1 
ATOM   14601 C C     . HIS A 1 3182 ? 141.862 130.381 143.852 1.00 26.40  ? 3182 HIS A C     1 
ATOM   14602 O O     . HIS A 1 3182 ? 142.130 129.492 143.041 1.00 26.40  ? 3182 HIS A O     1 
ATOM   14603 C CB    . HIS A 1 3182 ? 143.688 131.888 144.647 1.00 26.40  ? 3182 HIS A CB    1 
ATOM   14604 C CG    . HIS A 1 3182 ? 144.711 132.878 144.188 1.00 26.40  ? 3182 HIS A CG    1 
ATOM   14605 N ND1   . HIS A 1 3182 ? 144.746 134.180 144.638 1.00 26.40  ? 3182 HIS A ND1   1 
ATOM   14606 C CD2   . HIS A 1 3182 ? 145.736 132.755 143.313 1.00 26.40  ? 3182 HIS A CD2   1 
ATOM   14607 C CE1   . HIS A 1 3182 ? 145.753 134.814 144.065 1.00 26.40  ? 3182 HIS A CE1   1 
ATOM   14608 N NE2   . HIS A 1 3182 ? 146.368 133.973 143.255 1.00 26.40  ? 3182 HIS A NE2   1 
ATOM   14609 N N     . TYR A 1 3183 ? 141.034 130.193 144.882 1.00 27.58  ? 3183 TYR A N     1 
ATOM   14610 C CA    . TYR A 1 3183 ? 140.366 128.912 145.076 1.00 27.58  ? 3183 TYR A CA    1 
ATOM   14611 C C     . TYR A 1 3183 ? 139.505 128.563 143.871 1.00 27.58  ? 3183 TYR A C     1 
ATOM   14612 O O     . TYR A 1 3183 ? 139.598 127.457 143.327 1.00 27.58  ? 3183 TYR A O     1 
ATOM   14613 C CB    . TYR A 1 3183 ? 139.525 128.962 146.352 1.00 27.58  ? 3183 TYR A CB    1 
ATOM   14614 C CG    . TYR A 1 3183 ? 138.888 127.650 146.749 1.00 27.58  ? 3183 TYR A CG    1 
ATOM   14615 C CD1   . TYR A 1 3183 ? 139.429 126.439 146.346 1.00 27.58  ? 3183 TYR A CD1   1 
ATOM   14616 C CD2   . TYR A 1 3183 ? 137.747 127.627 147.536 1.00 27.58  ? 3183 TYR A CD2   1 
ATOM   14617 C CE1   . TYR A 1 3183 ? 138.847 125.242 146.712 1.00 27.58  ? 3183 TYR A CE1   1 
ATOM   14618 C CE2   . TYR A 1 3183 ? 137.161 126.437 147.907 1.00 27.58  ? 3183 TYR A CE2   1 
ATOM   14619 C CZ    . TYR A 1 3183 ? 137.714 125.248 147.493 1.00 27.58  ? 3183 TYR A CZ    1 
ATOM   14620 O OH    . TYR A 1 3183 ? 137.130 124.059 147.863 1.00 27.58  ? 3183 TYR A OH    1 
ATOM   14621 N N     . ALA A 1 3184 ? 138.676 129.508 143.425 1.00 29.43  ? 3184 ALA A N     1 
ATOM   14622 C CA    . ALA A 1 3184 ? 137.796 129.247 142.292 1.00 29.43  ? 3184 ALA A CA    1 
ATOM   14623 C C     . ALA A 1 3184 ? 138.596 128.960 141.028 1.00 29.43  ? 3184 ALA A C     1 
ATOM   14624 O O     . ALA A 1 3184 ? 138.317 127.992 140.309 1.00 29.43  ? 3184 ALA A O     1 
ATOM   14625 C CB    . ALA A 1 3184 ? 136.852 130.429 142.079 1.00 29.43  ? 3184 ALA A CB    1 
ATOM   14626 N N     . ASN A 1 3185 ? 139.609 129.786 140.747 1.00 30.98  ? 3185 ASN A N     1 
ATOM   14627 C CA    . ASN A 1 3185 ? 140.388 129.609 139.525 1.00 30.98  ? 3185 ASN A CA    1 
ATOM   14628 C C     . ASN A 1 3185 ? 141.131 128.280 139.527 1.00 30.98  ? 3185 ASN A C     1 
ATOM   14629 O O     . ASN A 1 3185 ? 141.104 127.543 138.533 1.00 30.98  ? 3185 ASN A O     1 
ATOM   14630 C CB    . ASN A 1 3185 ? 141.369 130.768 139.361 1.00 30.98  ? 3185 ASN A CB    1 
ATOM   14631 C CG    . ASN A 1 3185 ? 140.676 132.074 139.036 1.00 30.98  ? 3185 ASN A CG    1 
ATOM   14632 O OD1   . ASN A 1 3185 ? 139.741 132.112 138.237 1.00 30.98  ? 3185 ASN A OD1   1 
ATOM   14633 N ND2   . ASN A 1 3185 ? 141.130 133.156 139.658 1.00 30.98  ? 3185 ASN A ND2   1 
ATOM   14634 N N     . LEU A 1 3186 ? 141.797 127.953 140.637 1.00 33.88  ? 3186 LEU A N     1 
ATOM   14635 C CA    . LEU A 1 3186 ? 142.547 126.707 140.720 1.00 33.88  ? 3186 LEU A CA    1 
ATOM   14636 C C     . LEU A 1 3186 ? 141.626 125.498 140.640 1.00 33.88  ? 3186 LEU A C     1 
ATOM   14637 O O     . LEU A 1 3186 ? 141.945 124.514 139.963 1.00 33.88  ? 3186 LEU A O     1 
ATOM   14638 C CB    . LEU A 1 3186 ? 143.359 126.679 142.012 1.00 33.88  ? 3186 LEU A CB    1 
ATOM   14639 C CG    . LEU A 1 3186 ? 144.271 125.474 142.217 1.00 33.88  ? 3186 LEU A CG    1 
ATOM   14640 C CD1   . LEU A 1 3186 ? 145.415 125.499 141.218 1.00 33.88  ? 3186 LEU A CD1   1 
ATOM   14641 C CD2   . LEU A 1 3186 ? 144.793 125.457 143.637 1.00 33.88  ? 3186 LEU A CD2   1 
ATOM   14642 N N     . PHE A 1 3187 ? 140.483 125.545 141.332 1.00 34.91  ? 3187 PHE A N     1 
ATOM   14643 C CA    . PHE A 1 3187 ? 139.544 124.433 141.277 1.00 34.91  ? 3187 PHE A CA    1 
ATOM   14644 C C     . PHE A 1 3187 ? 139.027 124.229 139.861 1.00 34.91  ? 3187 PHE A C     1 
ATOM   14645 O O     . PHE A 1 3187 ? 138.960 123.096 139.372 1.00 34.91  ? 3187 PHE A O     1 
ATOM   14646 C CB    . PHE A 1 3187 ? 138.390 124.678 142.247 1.00 34.91  ? 3187 PHE A CB    1 
ATOM   14647 C CG    . PHE A 1 3187 ? 137.394 123.556 142.306 1.00 34.91  ? 3187 PHE A CG    1 
ATOM   14648 C CD1   . PHE A 1 3187 ? 136.280 123.556 141.485 1.00 34.91  ? 3187 PHE A CD1   1 
ATOM   14649 C CD2   . PHE A 1 3187 ? 137.571 122.504 143.185 1.00 34.91  ? 3187 PHE A CD2   1 
ATOM   14650 C CE1   . PHE A 1 3187 ? 135.364 122.527 141.539 1.00 34.91  ? 3187 PHE A CE1   1 
ATOM   14651 C CE2   . PHE A 1 3187 ? 136.657 121.472 143.243 1.00 34.91  ? 3187 PHE A CE2   1 
ATOM   14652 C CZ    . PHE A 1 3187 ? 135.553 121.484 142.419 1.00 34.91  ? 3187 PHE A CZ    1 
ATOM   14653 N N     . HIS A 1 3188 ? 138.666 125.320 139.181 1.00 41.20  ? 3188 HIS A N     1 
ATOM   14654 C CA    . HIS A 1 3188 ? 138.185 125.196 137.810 1.00 41.20  ? 3188 HIS A CA    1 
ATOM   14655 C C     . HIS A 1 3188 ? 139.264 124.630 136.898 1.00 41.20  ? 3188 HIS A C     1 
ATOM   14656 O O     . HIS A 1 3188 ? 138.989 123.750 136.074 1.00 41.20  ? 3188 HIS A O     1 
ATOM   14657 C CB    . HIS A 1 3188 ? 137.706 126.550 137.292 1.00 41.20  ? 3188 HIS A CB    1 
ATOM   14658 C CG    . HIS A 1 3188 ? 137.450 126.572 135.818 1.00 41.20  ? 3188 HIS A CG    1 
ATOM   14659 N ND1   . HIS A 1 3188 ? 136.526 125.750 135.212 1.00 41.20  ? 3188 HIS A ND1   1 
ATOM   14660 C CD2   . HIS A 1 3188 ? 138.001 127.313 134.828 1.00 41.20  ? 3188 HIS A CD2   1 
ATOM   14661 C CE1   . HIS A 1 3188 ? 136.516 125.985 133.912 1.00 41.20  ? 3188 HIS A CE1   1 
ATOM   14662 N NE2   . HIS A 1 3188 ? 137.402 126.929 133.653 1.00 41.20  ? 3188 HIS A NE2   1 
ATOM   14663 N N     . GLU A 1 3189 ? 140.501 125.110 137.041 1.00 44.32  ? 3189 GLU A N     1 
ATOM   14664 C CA    . GLU A 1 3189 ? 141.583 124.634 136.186 1.00 44.32  ? 3189 GLU A CA    1 
ATOM   14665 C C     . GLU A 1 3189 ? 141.846 123.148 136.402 1.00 44.32  ? 3189 GLU A C     1 
ATOM   14666 O O     . GLU A 1 3189 ? 141.956 122.379 135.440 1.00 44.32  ? 3189 GLU A O     1 
ATOM   14667 C CB    . GLU A 1 3189 ? 142.846 125.456 136.446 1.00 44.32  ? 3189 GLU A CB    1 
ATOM   14668 C CG    . GLU A 1 3189 ? 144.146 124.726 136.170 1.00 44.32  ? 3189 GLU A CG    1 
ATOM   14669 C CD    . GLU A 1 3189 ? 145.357 125.622 136.342 1.00 44.32  ? 3189 GLU A CD    1 
ATOM   14670 O OE1   . GLU A 1 3189 ? 145.201 126.857 136.253 1.00 44.32  ? 3189 GLU A OE1   1 
ATOM   14671 O OE2   . GLU A 1 3189 ? 146.466 125.092 136.565 1.00 44.32  ? 3189 GLU A OE2   1 
ATOM   14672 N N     . LYS A 1 3190 ? 141.939 122.721 137.665 1.00 44.50  ? 3190 LYS A N     1 
ATOM   14673 C CA    . LYS A 1 3190 ? 142.215 121.316 137.950 1.00 44.50  ? 3190 LYS A CA    1 
ATOM   14674 C C     . LYS A 1 3190 ? 141.065 120.423 137.500 1.00 44.50  ? 3190 LYS A C     1 
ATOM   14675 O O     . LYS A 1 3190 ? 141.292 119.350 136.922 1.00 44.50  ? 3190 LYS A O     1 
ATOM   14676 C CB    . LYS A 1 3190 ? 142.493 121.125 139.440 1.00 44.50  ? 3190 LYS A CB    1 
ATOM   14677 C CG    . LYS A 1 3190 ? 143.726 121.856 139.947 1.00 44.50  ? 3190 LYS A CG    1 
ATOM   14678 C CD    . LYS A 1 3190 ? 144.855 121.830 138.931 1.00 44.50  ? 3190 LYS A CD    1 
ATOM   14679 C CE    . LYS A 1 3190 ? 146.205 121.694 139.611 1.00 44.50  ? 3190 LYS A CE    1 
ATOM   14680 N NZ    . LYS A 1 3190 ? 147.308 121.506 138.628 1.00 44.50  ? 3190 LYS A NZ    1 
ATOM   14681 N N     . ARG A 1 3191 ? 139.823 120.850 137.754 1.00 49.58  ? 3191 ARG A N     1 
ATOM   14682 C CA    . ARG A 1 3191 ? 138.665 120.085 137.311 1.00 49.58  ? 3191 ARG A CA    1 
ATOM   14683 C C     . ARG A 1 3191 ? 138.663 119.934 135.797 1.00 49.58  ? 3191 ARG A C     1 
ATOM   14684 O O     . ARG A 1 3191 ? 138.452 118.831 135.279 1.00 49.58  ? 3191 ARG A O     1 
ATOM   14685 C CB    . ARG A 1 3191 ? 137.385 120.781 137.771 1.00 49.58  ? 3191 ARG A CB    1 
ATOM   14686 C CG    . ARG A 1 3191 ? 136.100 120.160 137.256 1.00 49.58  ? 3191 ARG A CG    1 
ATOM   14687 C CD    . ARG A 1 3191 ? 134.880 120.787 137.928 1.00 49.58  ? 3191 ARG A CD    1 
ATOM   14688 N NE    . ARG A 1 3191 ? 133.755 119.867 138.063 1.00 49.58  ? 3191 ARG A NE    1 
ATOM   14689 C CZ    . ARG A 1 3191 ? 133.633 118.958 139.020 1.00 49.58  ? 3191 ARG A CZ    1 
ATOM   14690 N NH1   . ARG A 1 3191 ? 134.488 118.895 140.026 1.00 49.58  ? 3191 ARG A NH1   1 
ATOM   14691 N NH2   . ARG A 1 3191 ? 132.606 118.114 138.986 1.00 49.58  ? 3191 ARG A NH2   1 
ATOM   14692 N N     . SER A 1 3192 ? 138.912 121.029 135.073 1.00 58.47  ? 3192 SER A N     1 
ATOM   14693 C CA    . SER A 1 3192 ? 138.917 120.971 133.617 1.00 58.47  ? 3192 SER A CA    1 
ATOM   14694 C C     . SER A 1 3192 ? 140.025 120.063 133.103 1.00 58.47  ? 3192 SER A C     1 
ATOM   14695 O O     . SER A 1 3192 ? 139.807 119.277 132.174 1.00 58.47  ? 3192 SER A O     1 
ATOM   14696 C CB    . SER A 1 3192 ? 139.064 122.376 133.036 1.00 58.47  ? 3192 SER A CB    1 
ATOM   14697 O OG    . SER A 1 3192 ? 139.129 122.333 131.621 1.00 58.47  ? 3192 SER A OG    1 
ATOM   14698 N N     . GLU A 1 3193 ? 141.221 120.153 133.691 1.00 60.32  ? 3193 GLU A N     1 
ATOM   14699 C CA    . GLU A 1 3193 ? 142.318 119.301 133.243 1.00 60.32  ? 3193 GLU A CA    1 
ATOM   14700 C C     . GLU A 1 3193 ? 142.002 117.829 133.468 1.00 60.32  ? 3193 GLU A C     1 
ATOM   14701 O O     . GLU A 1 3193 ? 142.246 116.991 132.588 1.00 60.32  ? 3193 GLU A O     1 
ATOM   14702 C CB    . GLU A 1 3193 ? 143.617 119.687 133.952 1.00 60.32  ? 3193 GLU A CB    1 
ATOM   14703 C CG    . GLU A 1 3193 ? 144.137 121.068 133.588 1.00 60.32  ? 3193 GLU A CG    1 
ATOM   14704 C CD    . GLU A 1 3193 ? 145.614 121.229 133.885 1.00 60.32  ? 3193 GLU A CD    1 
ATOM   14705 O OE1   . GLU A 1 3193 ? 146.062 120.754 134.949 1.00 60.32  ? 3193 GLU A OE1   1 
ATOM   14706 O OE2   . GLU A 1 3193 ? 146.327 121.832 133.056 1.00 60.32  ? 3193 GLU A OE2   1 
ATOM   14707 N N     . LEU A 1 3194 ? 141.445 117.489 134.633 1.00 62.64  ? 3194 LEU A N     1 
ATOM   14708 C CA    . LEU A 1 3194 ? 141.168 116.084 134.905 1.00 62.64  ? 3194 LEU A CA    1 
ATOM   14709 C C     . LEU A 1 3194 ? 140.035 115.572 134.020 1.00 62.64  ? 3194 LEU A C     1 
ATOM   14710 O O     . LEU A 1 3194 ? 140.071 114.425 133.559 1.00 62.64  ? 3194 LEU A O     1 
ATOM   14711 C CB    . LEU A 1 3194 ? 140.849 115.884 136.389 1.00 62.64  ? 3194 LEU A CB    1 
ATOM   14712 C CG    . LEU A 1 3194 ? 140.716 114.448 136.916 1.00 62.64  ? 3194 LEU A CG    1 
ATOM   14713 C CD1   . LEU A 1 3194 ? 141.058 114.409 138.400 1.00 62.64  ? 3194 LEU A CD1   1 
ATOM   14714 C CD2   . LEU A 1 3194 ? 139.349 113.826 136.669 1.00 62.64  ? 3194 LEU A CD2   1 
ATOM   14715 N N     . GLU A 1 3195 ? 139.023 116.407 133.760 1.00 68.11  ? 3195 GLU A N     1 
ATOM   14716 C CA    . GLU A 1 3195 ? 137.957 115.997 132.849 1.00 68.11  ? 3195 GLU A CA    1 
ATOM   14717 C C     . GLU A 1 3195 ? 138.486 115.797 131.434 1.00 68.11  ? 3195 GLU A C     1 
ATOM   14718 O O     . GLU A 1 3195 ? 138.073 114.863 130.735 1.00 68.11  ? 3195 GLU A O     1 
ATOM   14719 C CB    . GLU A 1 3195 ? 136.818 117.020 132.856 1.00 68.11  ? 3195 GLU A CB    1 
ATOM   14720 C CG    . GLU A 1 3195 ? 136.110 117.198 134.201 1.00 68.11  ? 3195 GLU A CG    1 
ATOM   14721 C CD    . GLU A 1 3195 ? 135.137 116.077 134.538 1.00 68.11  ? 3195 GLU A CD    1 
ATOM   14722 O OE1   . GLU A 1 3195 ? 135.345 114.931 134.091 1.00 68.11  ? 3195 GLU A OE1   1 
ATOM   14723 O OE2   . GLU A 1 3195 ? 134.157 116.347 135.265 1.00 68.11  ? 3195 GLU A OE2   1 
ATOM   14724 N N     . GLU A 1 3196 ? 139.398 116.667 130.991 1.00 74.49  ? 3196 GLU A N     1 
ATOM   14725 C CA    . GLU A 1 3196 ? 140.005 116.493 129.675 1.00 74.49  ? 3196 GLU A CA    1 
ATOM   14726 C C     . GLU A 1 3196 ? 140.790 115.190 129.606 1.00 74.49  ? 3196 GLU A C     1 
ATOM   14727 O O     . GLU A 1 3196 ? 140.723 114.467 128.604 1.00 74.49  ? 3196 GLU A O     1 
ATOM   14728 C CB    . GLU A 1 3196 ? 140.910 117.681 129.351 1.00 74.49  ? 3196 GLU A CB    1 
ATOM   14729 C CG    . GLU A 1 3196 ? 140.164 118.957 129.001 1.00 74.49  ? 3196 GLU A CG    1 
ATOM   14730 C CD    . GLU A 1 3196 ? 140.981 120.204 129.281 1.00 74.49  ? 3196 GLU A CD    1 
ATOM   14731 O OE1   . GLU A 1 3196 ? 142.222 120.143 129.155 1.00 74.49  ? 3196 GLU A OE1   1 
ATOM   14732 O OE2   . GLU A 1 3196 ? 140.383 121.244 129.627 1.00 74.49  ? 3196 GLU A OE2   1 
ATOM   14733 N N     . GLN A 1 3197 ? 141.537 114.874 130.665 1.00 74.32  ? 3197 GLN A N     1 
ATOM   14734 C CA    . GLN A 1 3197 ? 142.268 113.610 130.699 1.00 74.32  ? 3197 GLN A CA    1 
ATOM   14735 C C     . GLN A 1 3197 ? 141.316 112.420 130.662 1.00 74.32  ? 3197 GLN A C     1 
ATOM   14736 O O     . GLN A 1 3197 ? 141.576 111.426 129.973 1.00 74.32  ? 3197 GLN A O     1 
ATOM   14737 C CB    . GLN A 1 3197 ? 143.156 113.553 131.940 1.00 74.32  ? 3197 GLN A CB    1 
ATOM   14738 C CG    . GLN A 1 3197 ? 144.436 114.361 131.825 1.00 74.32  ? 3197 GLN A CG    1 
ATOM   14739 C CD    . GLN A 1 3197 ? 145.230 114.379 133.115 1.00 74.32  ? 3197 GLN A CD    1 
ATOM   14740 O OE1   . GLN A 1 3197 ? 144.752 113.933 134.157 1.00 74.32  ? 3197 GLN A OE1   1 
ATOM   14741 N NE2   . GLN A 1 3197 ? 146.450 114.897 133.052 1.00 74.32  ? 3197 GLN A NE2   1 
ATOM   14742 N N     . GLN A 1 3198 ? 140.203 112.504 131.396 1.00 75.44  ? 3198 GLN A N     1 
ATOM   14743 C CA    . GLN A 1 3198 ? 139.222 111.422 131.387 1.00 75.44  ? 3198 GLN A CA    1 
ATOM   14744 C C     . GLN A 1 3198 ? 138.615 111.231 130.003 1.00 75.44  ? 3198 GLN A C     1 
ATOM   14745 O O     . GLN A 1 3198 ? 138.412 110.095 129.557 1.00 75.44  ? 3198 GLN A O     1 
ATOM   14746 C CB    . GLN A 1 3198 ? 138.123 111.697 132.413 1.00 75.44  ? 3198 GLN A CB    1 
ATOM   14747 C CG    . GLN A 1 3198 ? 138.320 110.997 133.745 1.00 75.44  ? 3198 GLN A CG    1 
ATOM   14748 C CD    . GLN A 1 3198 ? 137.289 111.415 134.776 1.00 75.44  ? 3198 GLN A CD    1 
ATOM   14749 O OE1   . GLN A 1 3198 ? 136.533 112.363 134.567 1.00 75.44  ? 3198 GLN A OE1   1 
ATOM   14750 N NE2   . GLN A 1 3198 ? 137.253 110.704 135.898 1.00 75.44  ? 3198 GLN A NE2   1 
ATOM   14751 N N     . MET A 1 3199 ? 138.308 112.330 129.310 1.00 85.53  ? 3199 MET A N     1 
ATOM   14752 C CA    . MET A 1 3199 ? 137.707 112.206 127.987 1.00 85.53  ? 3199 MET A CA    1 
ATOM   14753 C C     . MET A 1 3199 ? 138.731 111.682 126.983 1.00 85.53  ? 3199 MET A C     1 
ATOM   14754 O O     . MET A 1 3199 ? 138.385 110.915 126.075 1.00 85.53  ? 3199 MET A O     1 
ATOM   14755 C CB    . MET A 1 3199 ? 137.094 113.551 127.571 1.00 85.53  ? 3199 MET A CB    1 
ATOM   14756 C CG    . MET A 1 3199 ? 136.574 113.705 126.127 1.00 85.53  ? 3199 MET A CG    1 
ATOM   14757 S SD    . MET A 1 3199 ? 137.711 113.643 124.728 1.00 85.53  ? 3199 MET A SD    1 
ATOM   14758 C CE    . MET A 1 3199 ? 138.909 114.867 125.233 1.00 85.53  ? 3199 MET A CE    1 
ATOM   14759 N N     . HIS A 1 3200 ? 140.006 112.047 127.158 1.00 85.07  ? 3200 HIS A N     1 
ATOM   14760 C CA    . HIS A 1 3200 ? 141.070 111.434 126.365 1.00 85.07  ? 3200 HIS A CA    1 
ATOM   14761 C C     . HIS A 1 3200 ? 141.127 109.929 126.599 1.00 85.07  ? 3200 HIS A C     1 
ATOM   14762 O O     . HIS A 1 3200 ? 141.295 109.148 125.654 1.00 85.07  ? 3200 HIS A O     1 
ATOM   14763 C CB    . HIS A 1 3200 ? 142.422 112.060 126.710 1.00 85.07  ? 3200 HIS A CB    1 
ATOM   14764 C CG    . HIS A 1 3200 ? 142.754 113.283 125.914 1.00 85.07  ? 3200 HIS A CG    1 
ATOM   14765 N ND1   . HIS A 1 3200 ? 141.940 114.393 125.878 1.00 85.07  ? 3200 HIS A ND1   1 
ATOM   14766 C CD2   . HIS A 1 3200 ? 143.817 113.571 125.126 1.00 85.07  ? 3200 HIS A CD2   1 
ATOM   14767 C CE1   . HIS A 1 3200 ? 142.485 115.312 125.101 1.00 85.07  ? 3200 HIS A CE1   1 
ATOM   14768 N NE2   . HIS A 1 3200 ? 143.625 114.839 124.633 1.00 85.07  ? 3200 HIS A NE2   1 
ATOM   14769 N N     . LEU A 1 3201 ? 141.006 109.509 127.860 1.00 84.17  ? 3201 LEU A N     1 
ATOM   14770 C CA    . LEU A 1 3201 ? 141.020 108.085 128.182 1.00 84.17  ? 3201 LEU A CA    1 
ATOM   14771 C C     . LEU A 1 3201 ? 139.844 107.362 127.535 1.00 84.17  ? 3201 LEU A C     1 
ATOM   14772 O O     . LEU A 1 3201 ? 139.998 106.250 127.016 1.00 84.17  ? 3201 LEU A O     1 
ATOM   14773 C CB    . LEU A 1 3201 ? 141.008 107.901 129.701 1.00 84.17  ? 3201 LEU A CB    1 
ATOM   14774 C CG    . LEU A 1 3201 ? 141.207 106.510 130.308 1.00 84.17  ? 3201 LEU A CG    1 
ATOM   14775 C CD1   . LEU A 1 3201 ? 141.870 106.638 131.663 1.00 84.17  ? 3201 LEU A CD1   1 
ATOM   14776 C CD2   . LEU A 1 3201 ? 139.885 105.770 130.449 1.00 84.17  ? 3201 LEU A CD2   1 
ATOM   14777 N N     . ASN A 1 3202 ? 138.659 107.975 127.567 1.00 83.94  ? 3202 ASN A N     1 
ATOM   14778 C CA    . ASN A 1 3202 ? 137.492 107.366 126.931 1.00 83.94  ? 3202 ASN A CA    1 
ATOM   14779 C C     . ASN A 1 3202 ? 137.679 107.258 125.421 1.00 83.94  ? 3202 ASN A C     1 
ATOM   14780 O O     . ASN A 1 3202 ? 137.305 106.247 124.809 1.00 83.94  ? 3202 ASN A O     1 
ATOM   14781 C CB    . ASN A 1 3202 ? 136.233 108.168 127.256 1.00 83.94  ? 3202 ASN A CB    1 
ATOM   14782 C CG    . ASN A 1 3202 ? 135.832 108.061 128.713 1.00 83.94  ? 3202 ASN A CG    1 
ATOM   14783 O OD1   . ASN A 1 3202 ? 135.796 109.058 129.433 1.00 83.94  ? 3202 ASN A OD1   1 
ATOM   14784 N ND2   . ASN A 1 3202 ? 135.524 106.847 129.155 1.00 83.94  ? 3202 ASN A ND2   1 
ATOM   14785 N N     . VAL A 1 3203 ? 138.249 108.296 124.804 1.00 84.26  ? 3203 VAL A N     1 
ATOM   14786 C CA    . VAL A 1 3203 ? 138.525 108.255 123.371 1.00 84.26  ? 3203 VAL A CA    1 
ATOM   14787 C C     . VAL A 1 3203 ? 139.501 107.128 123.052 1.00 84.26  ? 3203 VAL A C     1 
ATOM   14788 O O     . VAL A 1 3203 ? 139.325 106.393 122.072 1.00 84.26  ? 3203 VAL A O     1 
ATOM   14789 C CB    . VAL A 1 3203 ? 139.051 109.622 122.893 1.00 84.26  ? 3203 VAL A CB    1 
ATOM   14790 C CG1   . VAL A 1 3203 ? 139.746 109.497 121.545 1.00 84.26  ? 3203 VAL A CG1   1 
ATOM   14791 C CG2   . VAL A 1 3203 ? 137.914 110.628 122.815 1.00 84.26  ? 3203 VAL A CG2   1 
ATOM   14792 N N     . GLY A 1 3204 ? 140.540 106.973 123.876 1.00 86.04  ? 3204 GLY A N     1 
ATOM   14793 C CA    . GLY A 1 3204 ? 141.480 105.880 123.673 1.00 86.04  ? 3204 GLY A CA    1 
ATOM   14794 C C     . GLY A 1 3204 ? 140.833 104.515 123.819 1.00 86.04  ? 3204 GLY A C     1 
ATOM   14795 O O     . GLY A 1 3204 ? 141.124 103.593 123.051 1.00 86.04  ? 3204 GLY A O     1 
ATOM   14796 N N     . LEU A 1 3205 ? 139.946 104.371 124.808 1.00 87.21  ? 3205 LEU A N     1 
ATOM   14797 C CA    . LEU A 1 3205 ? 139.186 103.133 124.966 1.00 87.21  ? 3205 LEU A CA    1 
ATOM   14798 C C     . LEU A 1 3205 ? 138.363 102.816 123.721 1.00 87.21  ? 3205 LEU A C     1 
ATOM   14799 O O     . LEU A 1 3205 ? 138.386 101.682 123.229 1.00 87.21  ? 3205 LEU A O     1 
ATOM   14800 C CB    . LEU A 1 3205 ? 138.275 103.234 126.191 1.00 87.21  ? 3205 LEU A CB    1 
ATOM   14801 C CG    . LEU A 1 3205 ? 138.722 102.625 127.521 1.00 87.21  ? 3205 LEU A CG    1 
ATOM   14802 C CD1   . LEU A 1 3205 ? 137.576 102.643 128.520 1.00 87.21  ? 3205 LEU A CD1   1 
ATOM   14803 C CD2   . LEU A 1 3205 ? 139.187 101.196 127.298 1.00 87.21  ? 3205 LEU A CD2   1 
ATOM   14804 N N     . ARG A 1 3206 ? 137.627 103.800 123.200 1.00 88.31  ? 3206 ARG A N     1 
ATOM   14805 C CA    . ARG A 1 3206 ? 136.812 103.552 122.012 1.00 88.31  ? 3206 ARG A CA    1 
ATOM   14806 C C     . ARG A 1 3206 ? 137.682 103.204 120.809 1.00 88.31  ? 3206 ARG A C     1 
ATOM   14807 O O     . ARG A 1 3206 ? 137.369 102.280 120.045 1.00 88.31  ? 3206 ARG A O     1 
ATOM   14808 C CB    . ARG A 1 3206 ? 135.938 104.767 121.710 1.00 88.31  ? 3206 ARG A CB    1 
ATOM   14809 C CG    . ARG A 1 3206 ? 134.807 104.965 122.697 1.00 88.31  ? 3206 ARG A CG    1 
ATOM   14810 C CD    . ARG A 1 3206 ? 134.180 106.331 122.519 1.00 88.31  ? 3206 ARG A CD    1 
ATOM   14811 N NE    . ARG A 1 3206 ? 135.142 107.296 122.000 1.00 88.31  ? 3206 ARG A NE    1 
ATOM   14812 C CZ    . ARG A 1 3206 ? 134.927 108.085 120.956 1.00 88.31  ? 3206 ARG A CZ    1 
ATOM   14813 N NH1   . ARG A 1 3206 ? 133.783 108.057 120.291 1.00 88.31  ? 3206 ARG A NH1   1 
ATOM   14814 N NH2   . ARG A 1 3206 ? 135.882 108.926 120.571 1.00 88.31  ? 3206 ARG A NH2   1 
ATOM   14815 N N     . LYS A 1 3207 ? 138.788 103.931 120.635 1.00 88.88  ? 3207 LYS A N     1 
ATOM   14816 C CA    . LYS A 1 3207 ? 139.664 103.692 119.495 1.00 88.88  ? 3207 LYS A CA    1 
ATOM   14817 C C     . LYS A 1 3207 ? 140.266 102.299 119.550 1.00 88.88  ? 3207 LYS A C     1 
ATOM   14818 O O     . LYS A 1 3207 ? 140.345 101.602 118.529 1.00 88.88  ? 3207 LYS A O     1 
ATOM   14819 C CB    . LYS A 1 3207 ? 140.775 104.737 119.460 1.00 88.88  ? 3207 LYS A CB    1 
ATOM   14820 C CG    . LYS A 1 3207 ? 141.592 104.728 118.181 1.00 88.88  ? 3207 LYS A CG    1 
ATOM   14821 C CD    . LYS A 1 3207 ? 142.844 103.863 118.290 1.00 88.88  ? 3207 LYS A CD    1 
ATOM   14822 C CE    . LYS A 1 3207 ? 143.846 104.485 119.238 1.00 88.88  ? 3207 LYS A CE    1 
ATOM   14823 N NZ    . LYS A 1 3207 ? 145.087 103.679 119.351 1.00 88.88  ? 3207 LYS A NZ    1 
ATOM   14824 N N     . ILE A 1 3208 ? 140.719 101.873 120.727 1.00 94.15  ? 3208 ILE A N     1 
ATOM   14825 C CA    . ILE A 1 3208 ? 141.345 100.559 120.763 1.00 94.15  ? 3208 ILE A CA    1 
ATOM   14826 C C     . ILE A 1 3208 ? 140.315 99.435  120.792 1.00 94.15  ? 3208 ILE A C     1 
ATOM   14827 O O     . ILE A 1 3208 ? 140.617 98.321  120.363 1.00 94.15  ? 3208 ILE A O     1 
ATOM   14828 C CB    . ILE A 1 3208 ? 142.366 100.466 121.907 1.00 94.15  ? 3208 ILE A CB    1 
ATOM   14829 C CG1   . ILE A 1 3208 ? 143.507 101.423 121.613 1.00 94.15  ? 3208 ILE A CG1   1 
ATOM   14830 C CG2   . ILE A 1 3208 ? 142.985 99.093  122.000 1.00 94.15  ? 3208 ILE A CG2   1 
ATOM   14831 C CD1   . ILE A 1 3208 ? 144.400 101.658 122.774 1.00 94.15  ? 3208 ILE A CD1   1 
ATOM   14832 N N     . LYS A 1 3209 ? 139.089 99.685  121.262 1.00 96.54  ? 3209 LYS A N     1 
ATOM   14833 C CA    . LYS A 1 3209 ? 138.018 98.722  120.998 1.00 96.54  ? 3209 LYS A CA    1 
ATOM   14834 C C     . LYS A 1 3209 ? 137.797 98.547  119.496 1.00 96.54  ? 3209 LYS A C     1 
ATOM   14835 O O     . LYS A 1 3209 ? 137.610 97.421  119.012 1.00 96.54  ? 3209 LYS A O     1 
ATOM   14836 C CB    . LYS A 1 3209 ? 136.716 99.153  121.677 1.00 96.54  ? 3209 LYS A CB    1 
ATOM   14837 C CG    . LYS A 1 3209 ? 136.600 98.758  123.137 1.00 96.54  ? 3209 LYS A CG    1 
ATOM   14838 C CD    . LYS A 1 3209 ? 136.772 97.261  123.328 1.00 96.54  ? 3209 LYS A CD    1 
ATOM   14839 C CE    . LYS A 1 3209 ? 135.632 96.476  122.709 1.00 96.54  ? 3209 LYS A CE    1 
ATOM   14840 N NZ    . LYS A 1 3209 ? 134.430 96.339  123.579 1.00 96.54  ? 3209 LYS A NZ    1 
ATOM   14841 N N     . GLU A 1 3210 ? 137.826 99.651  118.741 1.00 98.10  ? 3210 GLU A N     1 
ATOM   14842 C CA    . GLU A 1 3210 ? 137.762 99.547  117.283 1.00 98.10  ? 3210 GLU A CA    1 
ATOM   14843 C C     . GLU A 1 3210 ? 138.933 98.734  116.734 1.00 98.10  ? 3210 GLU A C     1 
ATOM   14844 O O     . GLU A 1 3210 ? 138.763 97.917  115.819 1.00 98.10  ? 3210 GLU A O     1 
ATOM   14845 C CB    . GLU A 1 3210 ? 137.741 100.940 116.655 1.00 98.10  ? 3210 GLU A CB    1 
ATOM   14846 C CG    . GLU A 1 3210 ? 136.521 101.769 117.011 1.00 98.10  ? 3210 GLU A CG    1 
ATOM   14847 C CD    . GLU A 1 3210 ? 135.284 100.923 117.195 1.00 98.10  ? 3210 GLU A CD    1 
ATOM   14848 O OE1   . GLU A 1 3210 ? 134.738 100.441 116.181 1.00 98.10  ? 3210 GLU A OE1   1 
ATOM   14849 O OE2   . GLU A 1 3210 ? 134.850 100.754 118.353 1.00 98.10  ? 3210 GLU A OE2   1 
ATOM   14850 N N     . THR A 1 3211 ? 140.135 98.953  117.272 1.00 99.59  ? 3211 THR A N     1 
ATOM   14851 C CA    . THR A 1 3211 ? 141.291 98.191  116.798 1.00 99.59  ? 3211 THR A CA    1 
ATOM   14852 C C     . THR A 1 3211 ? 141.186 96.714  117.167 1.00 99.59  ? 3211 THR A C     1 
ATOM   14853 O O     . THR A 1 3211 ? 141.674 95.857  116.427 1.00 99.59  ? 3211 THR A O     1 
ATOM   14854 C CB    . THR A 1 3211 ? 142.595 98.768  117.349 1.00 99.59  ? 3211 THR A CB    1 
ATOM   14855 O OG1   . THR A 1 3211 ? 142.616 98.638  118.774 1.00 99.59  ? 3211 THR A OG1   1 
ATOM   14856 C CG2   . THR A 1 3211 ? 142.742 100.236 116.966 1.00 99.59  ? 3211 THR A CG2   1 
ATOM   14857 N N     . VAL A 1 3212 ? 140.579 96.403  118.315 1.00 100.64 ? 3212 VAL A N     1 
ATOM   14858 C CA    . VAL A 1 3212 ? 140.332 95.015  118.701 1.00 100.64 ? 3212 VAL A CA    1 
ATOM   14859 C C     . VAL A 1 3212 ? 139.387 94.358  117.710 1.00 100.64 ? 3212 VAL A C     1 
ATOM   14860 O O     . VAL A 1 3212 ? 139.590 93.209  117.300 1.00 100.64 ? 3212 VAL A O     1 
ATOM   14861 C CB    . VAL A 1 3212 ? 139.773 94.947  120.135 1.00 100.64 ? 3212 VAL A CB    1 
ATOM   14862 C CG1   . VAL A 1 3212 ? 139.091 93.603  120.390 1.00 100.64 ? 3212 VAL A CG1   1 
ATOM   14863 C CG2   . VAL A 1 3212 ? 140.875 95.183  121.145 1.00 100.64 ? 3212 VAL A CG2   1 
ATOM   14864 N N     . ASP A 1 3213 ? 138.329 95.074  117.321 1.00 104.59 ? 3213 ASP A N     1 
ATOM   14865 C CA    . ASP A 1 3213 ? 137.433 94.559  116.290 1.00 104.59 ? 3213 ASP A CA    1 
ATOM   14866 C C     . ASP A 1 3213 ? 138.176 94.345  114.975 1.00 104.59 ? 3213 ASP A C     1 
ATOM   14867 O O     . ASP A 1 3213 ? 137.975 93.331  114.293 1.00 104.59 ? 3213 ASP A O     1 
ATOM   14868 C CB    . ASP A 1 3213 ? 136.254 95.513  116.096 1.00 104.59 ? 3213 ASP A CB    1 
ATOM   14869 C CG    . ASP A 1 3213 ? 135.422 95.681  117.355 1.00 104.59 ? 3213 ASP A CG    1 
ATOM   14870 O OD1   . ASP A 1 3213 ? 135.335 94.721  118.149 1.00 104.59 ? 3213 ASP A OD1   1 
ATOM   14871 O OD2   . ASP A 1 3213 ? 134.845 96.773  117.546 1.00 104.59 ? 3213 ASP A OD2   1 
ATOM   14872 N N     . GLN A 1 3214 ? 139.048 95.288  114.608 1.00 107.33 ? 3214 GLN A N     1 
ATOM   14873 C CA    . GLN A 1 3214 ? 139.823 95.150  113.378 1.00 107.33 ? 3214 GLN A CA    1 
ATOM   14874 C C     . GLN A 1 3214 ? 140.749 93.938  113.436 1.00 107.33 ? 3214 GLN A C     1 
ATOM   14875 O O     . GLN A 1 3214 ? 140.890 93.204  112.451 1.00 107.33 ? 3214 GLN A O     1 
ATOM   14876 C CB    . GLN A 1 3214 ? 140.619 96.431  113.122 1.00 107.33 ? 3214 GLN A CB    1 
ATOM   14877 C CG    . GLN A 1 3214 ? 140.898 96.720  111.655 1.00 107.33 ? 3214 GLN A CG    1 
ATOM   14878 C CD    . GLN A 1 3214 ? 142.281 96.275  111.225 1.00 107.33 ? 3214 GLN A CD    1 
ATOM   14879 O OE1   . GLN A 1 3214 ? 143.109 95.895  112.053 1.00 107.33 ? 3214 GLN A OE1   1 
ATOM   14880 N NE2   . GLN A 1 3214 ? 142.541 96.324  109.924 1.00 107.33 ? 3214 GLN A NE2   1 
ATOM   14881 N N     . VAL A 1 3215 ? 141.385 93.711  114.587 1.00 105.57 ? 3215 VAL A N     1 
ATOM   14882 C CA    . VAL A 1 3215 ? 142.272 92.563  114.749 1.00 105.57 ? 3215 VAL A CA    1 
ATOM   14883 C C     . VAL A 1 3215 ? 141.479 91.262  114.698 1.00 105.57 ? 3215 VAL A C     1 
ATOM   14884 O O     . VAL A 1 3215 ? 141.927 90.268  114.114 1.00 105.57 ? 3215 VAL A O     1 
ATOM   14885 C CB    . VAL A 1 3215 ? 143.073 92.694  116.058 1.00 105.57 ? 3215 VAL A CB    1 
ATOM   14886 C CG1   . VAL A 1 3215 ? 143.752 91.379  116.413 1.00 105.57 ? 3215 VAL A CG1   1 
ATOM   14887 C CG2   . VAL A 1 3215 ? 144.097 93.811  115.935 1.00 105.57 ? 3215 VAL A CG2   1 
ATOM   14888 N N     . GLU A 1 3216 ? 140.290 91.246  115.307 1.00 109.86 ? 3216 GLU A N     1 
ATOM   14889 C CA    . GLU A 1 3216 ? 139.428 90.072  115.218 1.00 109.86 ? 3216 GLU A CA    1 
ATOM   14890 C C     . GLU A 1 3216 ? 139.057 89.780  113.771 1.00 109.86 ? 3216 GLU A C     1 
ATOM   14891 O O     . GLU A 1 3216 ? 139.027 88.617  113.351 1.00 109.86 ? 3216 GLU A O     1 
ATOM   14892 C CB    . GLU A 1 3216 ? 138.168 90.275  116.060 1.00 109.86 ? 3216 GLU A CB    1 
ATOM   14893 C CG    . GLU A 1 3216 ? 138.408 90.331  117.561 1.00 109.86 ? 3216 GLU A CG    1 
ATOM   14894 C CD    . GLU A 1 3216 ? 138.414 88.960  118.204 1.00 109.86 ? 3216 GLU A CD    1 
ATOM   14895 O OE1   . GLU A 1 3216 ? 137.747 88.049  117.671 1.00 109.86 ? 3216 GLU A OE1   1 
ATOM   14896 O OE2   . GLU A 1 3216 ? 139.087 88.793  119.243 1.00 109.86 ? 3216 GLU A OE2   1 
ATOM   14897 N N     . GLU A 1 3217 ? 138.764 90.826  112.995 1.00 111.75 ? 3217 GLU A N     1 
ATOM   14898 C CA    . GLU A 1 3217 ? 138.470 90.633  111.578 1.00 111.75 ? 3217 GLU A CA    1 
ATOM   14899 C C     . GLU A 1 3217 ? 139.683 90.093  110.828 1.00 111.75 ? 3217 GLU A C     1 
ATOM   14900 O O     . GLU A 1 3217 ? 139.553 89.195  109.987 1.00 111.75 ? 3217 GLU A O     1 
ATOM   14901 C CB    . GLU A 1 3217 ? 137.997 91.946  110.955 1.00 111.75 ? 3217 GLU A CB    1 
ATOM   14902 C CG    . GLU A 1 3217 ? 136.628 92.403  111.430 1.00 111.75 ? 3217 GLU A CG    1 
ATOM   14903 C CD    . GLU A 1 3217 ? 136.549 93.906  111.614 1.00 111.75 ? 3217 GLU A CD    1 
ATOM   14904 O OE1   . GLU A 1 3217 ? 137.342 94.627  110.973 1.00 111.75 ? 3217 GLU A OE1   1 
ATOM   14905 O OE2   . GLU A 1 3217 ? 135.694 94.366  112.399 1.00 111.75 ? 3217 GLU A OE2   1 
ATOM   14906 N N     . LEU A 1 3218 ? 140.872 90.626  111.118 1.00 111.43 ? 3218 LEU A N     1 
ATOM   14907 C CA    . LEU A 1 3218 ? 142.075 90.229  110.393 1.00 111.43 ? 3218 LEU A CA    1 
ATOM   14908 C C     . LEU A 1 3218 ? 142.597 88.854  110.788 1.00 111.43 ? 3218 LEU A C     1 
ATOM   14909 O O     . LEU A 1 3218 ? 143.354 88.254  110.016 1.00 111.43 ? 3218 LEU A O     1 
ATOM   14910 C CB    . LEU A 1 3218 ? 143.189 91.258  110.597 1.00 111.43 ? 3218 LEU A CB    1 
ATOM   14911 C CG    . LEU A 1 3218 ? 143.043 92.619  109.916 1.00 111.43 ? 3218 LEU A CG    1 
ATOM   14912 C CD1   . LEU A 1 3218 ? 144.255 93.484  110.221 1.00 111.43 ? 3218 LEU A CD1   1 
ATOM   14913 C CD2   . LEU A 1 3218 ? 142.861 92.455  108.417 1.00 111.43 ? 3218 LEU A CD2   1 
ATOM   14914 N N     . ARG A 1 3219 ? 142.227 88.346  111.967 1.00 114.74 ? 3219 ARG A N     1 
ATOM   14915 C CA    . ARG A 1 3219 ? 142.769 87.067  112.420 1.00 114.74 ? 3219 ARG A CA    1 
ATOM   14916 C C     . ARG A 1 3219 ? 142.360 85.927  111.495 1.00 114.74 ? 3219 ARG A C     1 
ATOM   14917 O O     . ARG A 1 3219 ? 143.175 85.052  111.178 1.00 114.74 ? 3219 ARG A O     1 
ATOM   14918 C CB    . ARG A 1 3219 ? 142.319 86.781  113.852 1.00 114.74 ? 3219 ARG A CB    1 
ATOM   14919 C CG    . ARG A 1 3219 ? 142.980 85.560  114.475 1.00 114.74 ? 3219 ARG A CG    1 
ATOM   14920 C CD    . ARG A 1 3219 ? 142.679 85.465  115.962 1.00 114.74 ? 3219 ARG A CD    1 
ATOM   14921 N NE    . ARG A 1 3219 ? 142.523 86.782  116.566 1.00 114.74 ? 3219 ARG A NE    1 
ATOM   14922 C CZ    . ARG A 1 3219 ? 141.428 87.197  117.189 1.00 114.74 ? 3219 ARG A CZ    1 
ATOM   14923 N NH1   . ARG A 1 3219 ? 140.370 86.414  117.322 1.00 114.74 ? 3219 ARG A NH1   1 
ATOM   14924 N NH2   . ARG A 1 3219 ? 141.394 88.429  117.688 1.00 114.74 ? 3219 ARG A NH2   1 
ATOM   14925 N N     . ARG A 1 3220 ? 141.108 85.918  111.053 1.00 114.45 ? 3220 ARG A N     1 
ATOM   14926 C CA    . ARG A 1 3220 ? 140.617 84.868  110.169 1.00 114.45 ? 3220 ARG A CA    1 
ATOM   14927 C C     . ARG A 1 3220 ? 140.305 85.419  108.781 1.00 114.45 ? 3220 ARG A C     1 
ATOM   14928 O O     . ARG A 1 3220 ? 140.128 84.664  107.826 0.00 114.45 ? 3220 ARG A O     1 
ATOM   14929 C CB    . ARG A 1 3220 ? 139.374 84.206  110.766 1.00 114.45 ? 3220 ARG A CB    1 
ATOM   14930 C CG    . ARG A 1 3220 ? 138.201 85.153  110.948 1.00 114.45 ? 3220 ARG A CG    1 
ATOM   14931 C CD    . ARG A 1 3220 ? 136.997 84.439  111.536 1.00 114.45 ? 3220 ARG A CD    1 
ATOM   14932 N NE    . ARG A 1 3220 ? 135.905 85.363  111.815 1.00 114.45 ? 3220 ARG A NE    1 
ATOM   14933 C CZ    . ARG A 1 3220 ? 134.998 85.741  110.925 1.00 114.45 ? 3220 ARG A CZ    1 
ATOM   14934 N NH1   . ARG A 1 3220 ? 135.022 85.294  109.680 1.00 114.45 ? 3220 ARG A NH1   1 
ATOM   14935 N NH2   . ARG A 1 3220 ? 134.043 86.591  111.293 1.00 114.45 ? 3220 ARG A NH2   1 
ATOM   14936 N N     . LYS A 1 3471 ? 149.878 85.600  111.749 1.00 86.68  ? 3471 LYS A N     1 
ATOM   14937 C CA    . LYS A 1 3471 ? 150.377 84.517  112.588 1.00 86.68  ? 3471 LYS A CA    1 
ATOM   14938 C C     . LYS A 1 3471 ? 149.519 84.360  113.840 1.00 86.68  ? 3471 LYS A C     1 
ATOM   14939 O O     . LYS A 1 3471 ? 149.066 85.347  114.420 1.00 86.68  ? 3471 LYS A O     1 
ATOM   14940 C CB    . LYS A 1 3471 ? 151.837 84.765  112.968 1.00 86.68  ? 3471 LYS A CB    1 
ATOM   14941 C CG    . LYS A 1 3471 ? 152.676 83.502  113.062 1.00 86.68  ? 3471 LYS A CG    1 
ATOM   14942 C CD    . LYS A 1 3471 ? 154.161 83.822  113.044 1.00 86.68  ? 3471 LYS A CD    1 
ATOM   14943 C CE    . LYS A 1 3471 ? 154.614 84.252  111.658 1.00 86.68  ? 3471 LYS A CE    1 
ATOM   14944 N NZ    . LYS A 1 3471 ? 156.000 84.796  111.665 1.00 86.68  ? 3471 LYS A NZ    1 
ATOM   14945 N N     . VAL A 1 3472 ? 149.295 83.108  114.247 1.00 92.14  ? 3472 VAL A N     1 
ATOM   14946 C CA    . VAL A 1 3472 ? 148.440 82.841  115.400 1.00 92.14  ? 3472 VAL A CA    1 
ATOM   14947 C C     . VAL A 1 3472 ? 149.105 83.312  116.690 1.00 92.14  ? 3472 VAL A C     1 
ATOM   14948 O O     . VAL A 1 3472 ? 148.437 83.832  117.592 1.00 92.14  ? 3472 VAL A O     1 
ATOM   14949 C CB    . VAL A 1 3472 ? 148.069 81.346  115.451 1.00 92.14  ? 3472 VAL A CB    1 
ATOM   14950 C CG1   . VAL A 1 3472 ? 149.319 80.474  115.436 1.00 92.14  ? 3472 VAL A CG1   1 
ATOM   14951 C CG2   . VAL A 1 3472 ? 147.212 81.046  116.673 1.00 92.14  ? 3472 VAL A CG2   1 
ATOM   14952 N N     . ASN A 1 3473 ? 150.426 83.142  116.798 1.00 94.55  ? 3473 ASN A N     1 
ATOM   14953 C CA    . ASN A 1 3473 ? 151.135 83.594  117.992 1.00 94.55  ? 3473 ASN A CA    1 
ATOM   14954 C C     . ASN A 1 3473 ? 151.031 85.104  118.150 1.00 94.55  ? 3473 ASN A C     1 
ATOM   14955 O O     . ASN A 1 3473 ? 150.859 85.612  119.267 1.00 94.55  ? 3473 ASN A O     1 
ATOM   14956 C CB    . ASN A 1 3473 ? 152.600 83.161  117.928 1.00 94.55  ? 3473 ASN A CB    1 
ATOM   14957 C CG    . ASN A 1 3473 ? 152.772 81.662  118.072 1.00 94.55  ? 3473 ASN A CG    1 
ATOM   14958 O OD1   . ASN A 1 3473 ? 152.122 81.028  118.903 1.00 94.55  ? 3473 ASN A OD1   1 
ATOM   14959 N ND2   . ASN A 1 3473 ? 153.652 81.087  117.261 1.00 94.55  ? 3473 ASN A ND2   1 
ATOM   14960 N N     . ARG A 1 3474 ? 151.139 85.838  117.040 1.00 90.59  ? 3474 ARG A N     1 
ATOM   14961 C CA    . ARG A 1 3474 ? 150.969 87.286  117.083 1.00 90.59  ? 3474 ARG A CA    1 
ATOM   14962 C C     . ARG A 1 3474 ? 149.592 87.658  117.616 1.00 90.59  ? 3474 ARG A C     1 
ATOM   14963 O O     . ARG A 1 3474 ? 149.468 88.543  118.471 1.00 90.59  ? 3474 ARG A O     1 
ATOM   14964 C CB    . ARG A 1 3474 ? 151.179 87.880  115.689 1.00 90.59  ? 3474 ARG A CB    1 
ATOM   14965 C CG    . ARG A 1 3474 ? 152.616 88.266  115.357 1.00 90.59  ? 3474 ARG A CG    1 
ATOM   14966 C CD    . ARG A 1 3474 ? 153.552 87.071  115.316 1.00 90.59  ? 3474 ARG A CD    1 
ATOM   14967 N NE    . ARG A 1 3474 ? 154.874 87.446  114.829 1.00 90.59  ? 3474 ARG A NE    1 
ATOM   14968 C CZ    . ARG A 1 3474 ? 155.949 86.674  114.904 1.00 90.59  ? 3474 ARG A CZ    1 
ATOM   14969 N NH1   . ARG A 1 3474 ? 155.897 85.469  115.448 1.00 90.59  ? 3474 ARG A NH1   1 
ATOM   14970 N NH2   . ARG A 1 3474 ? 157.105 87.122  114.423 1.00 90.59  ? 3474 ARG A NH2   1 
ATOM   14971 N N     . SER A 1 3475 ? 148.548 86.979  117.136 1.00 92.46  ? 3475 SER A N     1 
ATOM   14972 C CA    . SER A 1 3475 ? 147.195 87.275  117.594 1.00 92.46  ? 3475 SER A CA    1 
ATOM   14973 C C     . SER A 1 3475 ? 147.026 86.961  119.076 1.00 92.46  ? 3475 SER A C     1 
ATOM   14974 O O     . SER A 1 3475 ? 146.419 87.742  119.816 1.00 92.46  ? 3475 SER A O     1 
ATOM   14975 C CB    . SER A 1 3475 ? 146.177 86.498  116.760 1.00 92.46  ? 3475 SER A CB    1 
ATOM   14976 O OG    . SER A 1 3475 ? 146.263 85.107  117.015 1.00 92.46  ? 3475 SER A OG    1 
ATOM   14977 N N     . THR A 1 3476 ? 147.553 85.821  119.531 1.00 92.66  ? 3476 THR A N     1 
ATOM   14978 C CA    . THR A 1 3476 ? 147.416 85.467  120.941 1.00 92.66  ? 3476 THR A CA    1 
ATOM   14979 C C     . THR A 1 3476 ? 148.135 86.470  121.838 1.00 92.66  ? 3476 THR A C     1 
ATOM   14980 O O     . THR A 1 3476 ? 147.584 86.916  122.855 1.00 92.66  ? 3476 THR A O     1 
ATOM   14981 C CB    . THR A 1 3476 ? 147.945 84.053  121.186 1.00 92.66  ? 3476 THR A CB    1 
ATOM   14982 O OG1   . THR A 1 3476 ? 149.321 83.977  120.790 1.00 92.66  ? 3476 THR A OG1   1 
ATOM   14983 C CG2   . THR A 1 3476 ? 147.132 83.034  120.399 1.00 92.66  ? 3476 THR A CG2   1 
ATOM   14984 N N     . ALA A 1 3477 ? 149.364 86.847  121.470 1.00 92.29  ? 3477 ALA A N     1 
ATOM   14985 C CA    . ALA A 1 3477 ? 150.095 87.837  122.253 1.00 92.29  ? 3477 ALA A CA    1 
ATOM   14986 C C     . ALA A 1 3477 ? 149.374 89.178  122.248 1.00 92.29  ? 3477 ALA A C     1 
ATOM   14987 O O     . ALA A 1 3477 ? 149.326 89.871  123.273 1.00 92.29  ? 3477 ALA A O     1 
ATOM   14988 C CB    . ALA A 1 3477 ? 151.517 87.989  121.716 1.00 92.29  ? 3477 ALA A CB    1 
ATOM   14989 N N     . LEU A 1 3478 ? 148.806 89.560  121.102 1.00 93.70  ? 3478 LEU A N     1 
ATOM   14990 C CA    . LEU A 1 3478 ? 148.079 90.820  121.024 1.00 93.70  ? 3478 LEU A CA    1 
ATOM   14991 C C     . LEU A 1 3478 ? 146.854 90.805  121.929 1.00 93.70  ? 3478 LEU A C     1 
ATOM   14992 O O     . LEU A 1 3478 ? 146.587 91.783  122.630 1.00 93.70  ? 3478 LEU A O     1 
ATOM   14993 C CB    . LEU A 1 3478 ? 147.685 91.105  119.575 1.00 93.70  ? 3478 LEU A CB    1 
ATOM   14994 C CG    . LEU A 1 3478 ? 147.247 92.534  119.256 1.00 93.70  ? 3478 LEU A CG    1 
ATOM   14995 C CD1   . LEU A 1 3478 ? 148.314 93.518  119.695 1.00 93.70  ? 3478 LEU A CD1   1 
ATOM   14996 C CD2   . LEU A 1 3478 ? 146.978 92.677  117.771 1.00 93.70  ? 3478 LEU A CD2   1 
ATOM   14997 N N     . LEU A 1 3479 ? 146.103 89.702  121.939 1.00 91.70  ? 3479 LEU A N     1 
ATOM   14998 C CA    . LEU A 1 3479 ? 144.943 89.617  122.824 1.00 91.70  ? 3479 LEU A CA    1 
ATOM   14999 C C     . LEU A 1 3479 ? 145.352 89.666  124.294 1.00 91.70  ? 3479 LEU A C     1 
ATOM   15000 O O     . LEU A 1 3479 ? 144.686 90.319  125.108 1.00 91.70  ? 3479 LEU A O     1 
ATOM   15001 C CB    . LEU A 1 3479 ? 144.129 88.357  122.523 1.00 91.70  ? 3479 LEU A CB    1 
ATOM   15002 C CG    . LEU A 1 3479 ? 143.059 88.435  121.425 1.00 91.70  ? 3479 LEU A CG    1 
ATOM   15003 C CD1   . LEU A 1 3479 ? 141.968 89.405  121.845 1.00 91.70  ? 3479 LEU A CD1   1 
ATOM   15004 C CD2   . LEU A 1 3479 ? 143.615 88.846  120.076 1.00 91.70  ? 3479 LEU A CD2   1 
ATOM   15005 N N     . LYS A 1 3480 ? 146.445 88.987  124.656 1.00 93.28  ? 3480 LYS A N     1 
ATOM   15006 C CA    . LYS A 1 3480 ? 146.912 89.043  126.041 1.00 93.28  ? 3480 LYS A CA    1 
ATOM   15007 C C     . LYS A 1 3480 ? 147.286 90.469  126.437 1.00 93.28  ? 3480 LYS A C     1 
ATOM   15008 O O     . LYS A 1 3480 ? 146.893 90.960  127.510 1.00 93.28  ? 3480 LYS A O     1 
ATOM   15009 C CB    . LYS A 1 3480 ? 148.102 88.102  126.230 1.00 93.28  ? 3480 LYS A CB    1 
ATOM   15010 C CG    . LYS A 1 3480 ? 147.769 86.634  126.032 1.00 93.28  ? 3480 LYS A CG    1 
ATOM   15011 C CD    . LYS A 1 3480 ? 149.000 85.757  126.191 1.00 93.28  ? 3480 LYS A CD    1 
ATOM   15012 C CE    . LYS A 1 3480 ? 148.648 84.281  126.074 1.00 93.28  ? 3480 LYS A CE    1 
ATOM   15013 N NZ    . LYS A 1 3480 ? 148.192 83.919  124.701 1.00 93.28  ? 3480 LYS A NZ    1 
ATOM   15014 N N     . SER A 1 3481 ? 148.045 91.153  125.575 1.00 95.18  ? 3481 SER A N     1 
ATOM   15015 C CA    . SER A 1 3481 ? 148.434 92.527  125.867 1.00 95.18  ? 3481 SER A CA    1 
ATOM   15016 C C     . SER A 1 3481 ? 147.222 93.439  125.934 1.00 95.18  ? 3481 SER A C     1 
ATOM   15017 O O     . SER A 1 3481 ? 147.174 94.340  126.773 1.00 95.18  ? 3481 SER A O     1 
ATOM   15018 C CB    . SER A 1 3481 ? 149.415 93.041  124.815 1.00 95.18  ? 3481 SER A CB    1 
ATOM   15019 O OG    . SER A 1 3481 ? 148.874 92.909  123.512 1.00 95.18  ? 3481 SER A OG    1 
ATOM   15020 N N     . LEU A 1 3482 ? 146.233 93.216  125.069 1.00 95.25  ? 3482 LEU A N     1 
ATOM   15021 C CA    . LEU A 1 3482 ? 145.017 94.019  125.101 1.00 95.25  ? 3482 LEU A CA    1 
ATOM   15022 C C     . LEU A 1 3482 ? 144.243 93.814  126.395 1.00 95.25  ? 3482 LEU A C     1 
ATOM   15023 O O     . LEU A 1 3482 ? 143.669 94.764  126.932 1.00 95.25  ? 3482 LEU A O     1 
ATOM   15024 C CB    . LEU A 1 3482 ? 144.146 93.699  123.885 1.00 95.25  ? 3482 LEU A CB    1 
ATOM   15025 C CG    . LEU A 1 3482 ? 144.334 94.581  122.649 1.00 95.25  ? 3482 LEU A CG    1 
ATOM   15026 C CD1   . LEU A 1 3482 ? 143.878 95.961  123.012 1.00 95.25  ? 3482 LEU A CD1   1 
ATOM   15027 C CD2   . LEU A 1 3482 ? 145.772 94.650  122.178 1.00 95.25  ? 3482 LEU A CD2   1 
ATOM   15028 N N     . SER A 1 3483 ? 144.199 92.582  126.905 1.00 92.22  ? 3483 SER A N     1 
ATOM   15029 C CA    . SER A 1 3483 ? 143.502 92.340  128.167 1.00 92.22  ? 3483 SER A CA    1 
ATOM   15030 C C     . SER A 1 3483 ? 144.211 93.024  129.331 1.00 92.22  ? 3483 SER A C     1 
ATOM   15031 O O     . SER A 1 3483 ? 143.569 93.653  130.189 1.00 92.22  ? 3483 SER A O     1 
ATOM   15032 C CB    . SER A 1 3483 ? 143.387 90.837  128.417 1.00 92.22  ? 3483 SER A CB    1 
ATOM   15033 O OG    . SER A 1 3483 ? 142.594 90.210  127.420 1.00 92.22  ? 3483 SER A OG    1 
ATOM   15034 N N     . ALA A 1 3484 ? 145.538 92.891  129.389 1.00 92.48  ? 3484 ALA A N     1 
ATOM   15035 C CA    . ALA A 1 3484 ? 146.295 93.616  130.402 1.00 92.48  ? 3484 ALA A CA    1 
ATOM   15036 C C     . ALA A 1 3484 ? 146.072 95.119  130.264 1.00 92.48  ? 3484 ALA A C     1 
ATOM   15037 O O     . ALA A 1 3484 ? 145.908 95.829  131.261 1.00 92.48  ? 3484 ALA A O     1 
ATOM   15038 C CB    . ALA A 1 3484 ? 147.775 93.256  130.297 1.00 92.48  ? 3484 ALA A CB    1 
ATOM   15039 N N     . GLU A 1 3485 ? 146.001 95.605  129.028 1.00 94.62  ? 3485 GLU A N     1 
ATOM   15040 C CA    . GLU A 1 3485 ? 145.741 97.015  128.765 1.00 94.62  ? 3485 GLU A CA    1 
ATOM   15041 C C     . GLU A 1 3485 ? 144.364 97.438  129.282 1.00 94.62  ? 3485 GLU A C     1 
ATOM   15042 O O     . GLU A 1 3485 ? 144.215 98.521  129.865 1.00 94.62  ? 3485 GLU A O     1 
ATOM   15043 C CB    . GLU A 1 3485 ? 145.887 97.245  127.258 1.00 94.62  ? 3485 GLU A CB    1 
ATOM   15044 C CG    . GLU A 1 3485 ? 145.730 98.644  126.767 1.00 94.62  ? 3485 GLU A CG    1 
ATOM   15045 C CD    . GLU A 1 3485 ? 144.352 98.818  126.230 1.00 94.62  ? 3485 GLU A CD    1 
ATOM   15046 O OE1   . GLU A 1 3485 ? 143.851 97.858  125.618 1.00 94.62  ? 3485 GLU A OE1   1 
ATOM   15047 O OE2   . GLU A 1 3485 ? 143.764 99.887  126.395 1.00 94.62  ? 3485 GLU A OE2   1 
ATOM   15048 N N     . ARG A 1 3486 ? 143.357 96.582  129.088 1.00 92.58  ? 3486 ARG A N     1 
ATOM   15049 C CA    . ARG A 1 3486 ? 141.998 96.853  129.552 1.00 92.58  ? 3486 ARG A CA    1 
ATOM   15050 C C     . ARG A 1 3486 ? 141.925 96.932  131.075 1.00 92.58  ? 3486 ARG A C     1 
ATOM   15051 O O     . ARG A 1 3486 ? 141.290 97.837  131.634 1.00 92.58  ? 3486 ARG A O     1 
ATOM   15052 C CB    . ARG A 1 3486 ? 141.055 95.767  129.027 1.00 92.58  ? 3486 ARG A CB    1 
ATOM   15053 C CG    . ARG A 1 3486 ? 140.476 96.012  127.627 1.00 92.58  ? 3486 ARG A CG    1 
ATOM   15054 C CD    . ARG A 1 3486 ? 139.708 97.326  127.513 1.00 92.58  ? 3486 ARG A CD    1 
ATOM   15055 N NE    . ARG A 1 3486 ? 139.375 97.658  126.131 1.00 92.58  ? 3486 ARG A NE    1 
ATOM   15056 C CZ    . ARG A 1 3486 ? 140.179 98.300  125.293 1.00 92.58  ? 3486 ARG A CZ    1 
ATOM   15057 N NH1   . ARG A 1 3486 ? 141.389 98.691  125.657 1.00 92.58  ? 3486 ARG A NH1   1 
ATOM   15058 N NH2   . ARG A 1 3486 ? 139.754 98.565  124.062 1.00 92.58  ? 3486 ARG A NH2   1 
ATOM   15059 N N     . GLU A 1 3487 ? 142.560 95.981  131.769 1.00 93.88  ? 3487 GLU A N     1 
ATOM   15060 C CA    . GLU A 1 3487 ? 142.524 96.018  133.232 1.00 93.88  ? 3487 GLU A CA    1 
ATOM   15061 C C     . GLU A 1 3487 ? 143.313 97.209  133.771 1.00 93.88  ? 3487 GLU A C     1 
ATOM   15062 O O     . GLU A 1 3487 ? 142.892 97.860  134.743 1.00 93.88  ? 3487 GLU A O     1 
ATOM   15063 C CB    . GLU A 1 3487 ? 143.038 94.700  133.820 1.00 93.88  ? 3487 GLU A CB    1 
ATOM   15064 C CG    . GLU A 1 3487 ? 144.520 94.440  133.634 1.00 93.88  ? 3487 GLU A CG    1 
ATOM   15065 C CD    . GLU A 1 3487 ? 144.950 93.092  134.173 1.00 93.88  ? 3487 GLU A CD    1 
ATOM   15066 O OE1   . GLU A 1 3487 ? 144.083 92.338  134.664 1.00 93.88  ? 3487 GLU A OE1   1 
ATOM   15067 O OE2   . GLU A 1 3487 ? 146.154 92.777  134.079 1.00 93.88  ? 3487 GLU A OE2   1 
ATOM   15068 N N     . ARG A 1 3488 ? 144.437 97.538  133.125 1.00 93.95  ? 3488 ARG A N     1 
ATOM   15069 C CA    . ARG A 1 3488 ? 145.187 98.720  133.521 1.00 93.95  ? 3488 ARG A CA    1 
ATOM   15070 C C     . ARG A 1 3488 ? 144.335 99.971  133.391 1.00 93.95  ? 3488 ARG A C     1 
ATOM   15071 O O     . ARG A 1 3488 ? 144.355 100.831 134.277 1.00 93.95  ? 3488 ARG A O     1 
ATOM   15072 C CB    . ARG A 1 3488 ? 146.450 98.863  132.667 1.00 93.95  ? 3488 ARG A CB    1 
ATOM   15073 C CG    . ARG A 1 3488 ? 147.640 98.030  133.104 1.00 93.95  ? 3488 ARG A CG    1 
ATOM   15074 C CD    . ARG A 1 3488 ? 148.958 98.769  132.871 1.00 93.95  ? 3488 ARG A CD    1 
ATOM   15075 N NE    . ARG A 1 3488 ? 149.146 99.200  131.491 1.00 93.95  ? 3488 ARG A NE    1 
ATOM   15076 C CZ    . ARG A 1 3488 ? 149.069 100.461 131.086 1.00 93.95  ? 3488 ARG A CZ    1 
ATOM   15077 N NH1   . ARG A 1 3488 ? 148.798 101.444 131.931 1.00 93.95  ? 3488 ARG A NH1   1 
ATOM   15078 N NH2   . ARG A 1 3488 ? 149.269 100.744 129.802 1.00 93.95  ? 3488 ARG A NH2   1 
ATOM   15079 N N     . TRP A 1 3489 ? 143.584 100.103 132.290 1.00 88.86  ? 3489 TRP A N     1 
ATOM   15080 C CA    . TRP A 1 3489 ? 142.826 101.340 132.140 1.00 88.86  ? 3489 TRP A CA    1 
ATOM   15081 C C     . TRP A 1 3489 ? 141.599 101.362 133.034 1.00 88.86  ? 3489 TRP A C     1 
ATOM   15082 O O     . TRP A 1 3489 ? 141.141 102.445 133.409 1.00 88.86  ? 3489 TRP A O     1 
ATOM   15083 C CB    . TRP A 1 3489 ? 142.395 101.606 130.700 1.00 88.86  ? 3489 TRP A CB    1 
ATOM   15084 C CG    . TRP A 1 3489 ? 143.523 101.906 129.802 1.00 88.86  ? 3489 TRP A CG    1 
ATOM   15085 C CD1   . TRP A 1 3489 ? 144.831 102.080 130.150 1.00 88.86  ? 3489 TRP A CD1   1 
ATOM   15086 C CD2   . TRP A 1 3489 ? 143.423 102.259 128.433 1.00 88.86  ? 3489 TRP A CD2   1 
ATOM   15087 N NE1   . TRP A 1 3489 ? 145.573 102.403 129.043 1.00 88.86  ? 3489 TRP A NE1   1 
ATOM   15088 C CE2   . TRP A 1 3489 ? 144.720 102.538 127.978 1.00 88.86  ? 3489 TRP A CE2   1 
ATOM   15089 C CE3   . TRP A 1 3489 ? 142.359 102.330 127.528 1.00 88.86  ? 3489 TRP A CE3   1 
ATOM   15090 C CZ2   . TRP A 1 3489 ? 144.983 102.862 126.659 1.00 88.86  ? 3489 TRP A CZ2   1 
ATOM   15091 C CZ3   . TRP A 1 3489 ? 142.628 102.668 126.229 1.00 88.86  ? 3489 TRP A CZ3   1 
ATOM   15092 C CH2   . TRP A 1 3489 ? 143.921 102.940 125.800 1.00 88.86  ? 3489 TRP A CH2   1 
ATOM   15093 N N     . GLU A 1 3490 ? 141.044 100.200 133.386 1.00 91.29  ? 3490 GLU A N     1 
ATOM   15094 C CA    . GLU A 1 3490 ? 139.988 100.203 134.394 1.00 91.29  ? 3490 GLU A CA    1 
ATOM   15095 C C     . GLU A 1 3490 ? 140.526 100.726 135.719 1.00 91.29  ? 3490 GLU A C     1 
ATOM   15096 O O     . GLU A 1 3490 ? 139.882 101.547 136.389 1.00 91.29  ? 3490 GLU A O     1 
ATOM   15097 C CB    . GLU A 1 3490 ? 139.402 98.799  134.552 1.00 91.29  ? 3490 GLU A CB    1 
ATOM   15098 C CG    . GLU A 1 3490 ? 138.250 98.708  135.548 1.00 91.29  ? 3490 GLU A CG    1 
ATOM   15099 C CD    . GLU A 1 3490 ? 136.976 99.345  135.019 1.00 91.29  ? 3490 GLU A CD    1 
ATOM   15100 O OE1   . GLU A 1 3490 ? 136.779 99.339  133.787 1.00 91.29  ? 3490 GLU A OE1   1 
ATOM   15101 O OE2   . GLU A 1 3490 ? 136.171 99.844  135.835 1.00 91.29  ? 3490 GLU A OE2   1 
ATOM   15102 N N     . LYS A 1 3491 ? 141.736 100.293 136.087 1.00 91.91  ? 3491 LYS A N     1 
ATOM   15103 C CA    . LYS A 1 3491 ? 142.381 100.819 137.288 1.00 91.91  ? 3491 LYS A CA    1 
ATOM   15104 C C     . LYS A 1 3491 ? 142.642 102.320 137.172 1.00 91.91  ? 3491 LYS A C     1 
ATOM   15105 O O     . LYS A 1 3491 ? 142.483 103.066 138.147 1.00 91.91  ? 3491 LYS A O     1 
ATOM   15106 C CB    . LYS A 1 3491 ? 143.686 100.067 137.541 1.00 91.91  ? 3491 LYS A CB    1 
ATOM   15107 C CG    . LYS A 1 3491 ? 143.490 98.588  137.829 1.00 91.91  ? 3491 LYS A CG    1 
ATOM   15108 C CD    . LYS A 1 3491 ? 144.809 97.867  138.039 1.00 91.91  ? 3491 LYS A CD    1 
ATOM   15109 C CE    . LYS A 1 3491 ? 144.569 96.405  138.382 1.00 91.91  ? 3491 LYS A CE    1 
ATOM   15110 N NZ    . LYS A 1 3491 ? 144.024 95.648  137.221 1.00 91.91  ? 3491 LYS A NZ    1 
ATOM   15111 N N     . THR A 1 3492 ? 143.066 102.776 135.990 1.00 87.97  ? 3492 THR A N     1 
ATOM   15112 C CA    . THR A 1 3492 ? 143.345 104.197 135.794 1.00 87.97  ? 3492 THR A CA    1 
ATOM   15113 C C     . THR A 1 3492 ? 142.074 105.034 135.903 1.00 87.97  ? 3492 THR A C     1 
ATOM   15114 O O     . THR A 1 3492 ? 142.086 106.127 136.481 1.00 87.97  ? 3492 THR A O     1 
ATOM   15115 C CB    . THR A 1 3492 ? 144.020 104.417 134.440 1.00 87.97  ? 3492 THR A CB    1 
ATOM   15116 O OG1   . THR A 1 3492 ? 145.250 103.685 134.397 1.00 87.97  ? 3492 THR A OG1   1 
ATOM   15117 C CG2   . THR A 1 3492 ? 144.317 105.893 134.223 1.00 87.97  ? 3492 THR A CG2   1 
ATOM   15118 N N     . SER A 1 3493 ? 140.967 104.543 135.348 1.00 84.48  ? 3493 SER A N     1 
ATOM   15119 C CA    . SER A 1 3493 ? 139.698 105.246 135.501 1.00 84.48  ? 3493 SER A CA    1 
ATOM   15120 C C     . SER A 1 3493 ? 139.268 105.279 136.962 1.00 84.48  ? 3493 SER A C     1 
ATOM   15121 O O     . SER A 1 3493 ? 138.741 106.292 137.440 1.00 84.48  ? 3493 SER A O     1 
ATOM   15122 C CB    . SER A 1 3493 ? 138.624 104.593 134.632 1.00 84.48  ? 3493 SER A CB    1 
ATOM   15123 O OG    . SER A 1 3493 ? 138.339 103.278 135.072 1.00 84.48  ? 3493 SER A OG    1 
ATOM   15124 N N     . GLU A 1 3494 ? 139.494 104.183 137.693 1.00 84.84  ? 3494 GLU A N     1 
ATOM   15125 C CA    . GLU A 1 3494 ? 139.164 104.176 139.115 1.00 84.84  ? 3494 GLU A CA    1 
ATOM   15126 C C     . GLU A 1 3494 ? 139.987 105.205 139.885 1.00 84.84  ? 3494 GLU A C     1 
ATOM   15127 O O     . GLU A 1 3494 ? 139.458 105.922 140.745 1.00 84.84  ? 3494 GLU A O     1 
ATOM   15128 C CB    . GLU A 1 3494 ? 139.372 102.777 139.694 1.00 84.84  ? 3494 GLU A CB    1 
ATOM   15129 C CG    . GLU A 1 3494 ? 138.762 102.585 141.070 1.00 84.84  ? 3494 GLU A CG    1 
ATOM   15130 C CD    . GLU A 1 3494 ? 137.247 102.570 141.034 1.00 84.84  ? 3494 GLU A CD    1 
ATOM   15131 O OE1   . GLU A 1 3494 ? 136.637 103.652 141.167 1.00 84.84  ? 3494 GLU A OE1   1 
ATOM   15132 O OE2   . GLU A 1 3494 ? 136.664 101.477 140.873 1.00 84.84  ? 3494 GLU A OE2   1 
ATOM   15133 N N     . THR A 1 3495 ? 141.285 105.304 139.587 1.00 81.96  ? 3495 THR A N     1 
ATOM   15134 C CA    . THR A 1 3495 ? 142.107 106.268 140.313 1.00 81.96  ? 3495 THR A CA    1 
ATOM   15135 C C     . THR A 1 3495 ? 141.797 107.701 139.889 1.00 81.96  ? 3495 THR A C     1 
ATOM   15136 O O     . THR A 1 3495 ? 141.928 108.624 140.699 1.00 81.96  ? 3495 THR A O     1 
ATOM   15137 C CB    . THR A 1 3495 ? 143.600 105.955 140.149 1.00 81.96  ? 3495 THR A CB    1 
ATOM   15138 O OG1   . THR A 1 3495 ? 144.355 106.732 141.088 1.00 81.96  ? 3495 THR A OG1   1 
ATOM   15139 C CG2   . THR A 1 3495 ? 144.092 106.276 138.753 1.00 81.96  ? 3495 THR A CG2   1 
ATOM   15140 N N     . PHE A 1 3496 ? 141.361 107.910 138.643 1.00 77.23  ? 3496 PHE A N     1 
ATOM   15141 C CA    . PHE A 1 3496 ? 140.879 109.231 138.249 1.00 77.23  ? 3496 PHE A CA    1 
ATOM   15142 C C     . PHE A 1 3496 ? 139.601 109.593 138.994 1.00 77.23  ? 3496 PHE A C     1 
ATOM   15143 O O     . PHE A 1 3496 ? 139.411 110.749 139.391 1.00 77.23  ? 3496 PHE A O     1 
ATOM   15144 C CB    . PHE A 1 3496 ? 140.658 109.290 136.737 1.00 77.23  ? 3496 PHE A CB    1 
ATOM   15145 C CG    . PHE A 1 3496 ? 141.878 109.703 135.964 1.00 77.23  ? 3496 PHE A CG    1 
ATOM   15146 C CD1   . PHE A 1 3496 ? 143.142 109.315 136.375 1.00 77.23  ? 3496 PHE A CD1   1 
ATOM   15147 C CD2   . PHE A 1 3496 ? 141.760 110.487 134.829 1.00 77.23  ? 3496 PHE A CD2   1 
ATOM   15148 C CE1   . PHE A 1 3496 ? 144.264 109.697 135.666 1.00 77.23  ? 3496 PHE A CE1   1 
ATOM   15149 C CE2   . PHE A 1 3496 ? 142.878 110.872 134.117 1.00 77.23  ? 3496 PHE A CE2   1 
ATOM   15150 C CZ    . PHE A 1 3496 ? 144.131 110.477 134.536 1.00 77.23  ? 3496 PHE A CZ    1 
ATOM   15151 N N     . LYS A 1 3497 ? 138.710 108.619 139.191 1.00 78.19  ? 3497 LYS A N     1 
ATOM   15152 C CA    . LYS A 1 3497 ? 137.522 108.862 140.003 1.00 78.19  ? 3497 LYS A CA    1 
ATOM   15153 C C     . LYS A 1 3497 ? 137.904 109.216 141.436 1.00 78.19  ? 3497 LYS A C     1 
ATOM   15154 O O     . LYS A 1 3497 ? 137.296 110.101 142.050 1.00 78.19  ? 3497 LYS A O     1 
ATOM   15155 C CB    . LYS A 1 3497 ? 136.604 107.641 139.974 1.00 78.19  ? 3497 LYS A CB    1 
ATOM   15156 C CG    . LYS A 1 3497 ? 135.632 107.621 138.804 1.00 78.19  ? 3497 LYS A CG    1 
ATOM   15157 C CD    . LYS A 1 3497 ? 134.868 106.307 138.736 1.00 78.19  ? 3497 LYS A CD    1 
ATOM   15158 C CE    . LYS A 1 3497 ? 135.704 105.213 138.091 1.00 78.19  ? 3497 LYS A CE    1 
ATOM   15159 N NZ    . LYS A 1 3497 ? 134.972 103.918 138.025 1.00 78.19  ? 3497 LYS A NZ    1 
ATOM   15160 N N     . ASN A 1 3498 ? 138.910 108.534 141.986 1.00 74.30  ? 3498 ASN A N     1 
ATOM   15161 C CA    . ASN A 1 3498 ? 139.381 108.865 143.331 1.00 74.30  ? 3498 ASN A CA    1 
ATOM   15162 C C     . ASN A 1 3498 ? 139.950 110.282 143.384 1.00 74.30  ? 3498 ASN A C     1 
ATOM   15163 O O     . ASN A 1 3498 ? 139.669 111.046 144.319 1.00 74.30  ? 3498 ASN A O     1 
ATOM   15164 C CB    . ASN A 1 3498 ? 140.425 107.844 143.785 1.00 74.30  ? 3498 ASN A CB    1 
ATOM   15165 C CG    . ASN A 1 3498 ? 140.734 107.945 145.267 1.00 74.30  ? 3498 ASN A CG    1 
ATOM   15166 O OD1   . ASN A 1 3498 ? 140.108 108.716 145.995 1.00 74.30  ? 3498 ASN A OD1   1 
ATOM   15167 N ND2   . ASN A 1 3498 ? 141.703 107.159 145.723 1.00 74.30  ? 3498 ASN A ND2   1 
ATOM   15168 N N     . GLN A 1 3499 ? 140.753 110.652 142.382 1.00 71.02  ? 3499 GLN A N     1 
ATOM   15169 C CA    . GLN A 1 3499 ? 141.298 112.006 142.328 1.00 71.02  ? 3499 GLN A CA    1 
ATOM   15170 C C     . GLN A 1 3499 ? 140.185 113.039 142.239 1.00 71.02  ? 3499 GLN A C     1 
ATOM   15171 O O     . GLN A 1 3499 ? 140.271 114.111 142.850 1.00 71.02  ? 3499 GLN A O     1 
ATOM   15172 C CB    . GLN A 1 3499 ? 142.251 112.158 141.143 1.00 71.02  ? 3499 GLN A CB    1 
ATOM   15173 C CG    . GLN A 1 3499 ? 143.528 111.345 141.236 1.00 71.02  ? 3499 GLN A CG    1 
ATOM   15174 C CD    . GLN A 1 3499 ? 144.417 111.528 140.022 1.00 71.02  ? 3499 GLN A CD    1 
ATOM   15175 O OE1   . GLN A 1 3499 ? 144.052 112.217 139.069 1.00 71.02  ? 3499 GLN A OE1   1 
ATOM   15176 N NE2   . GLN A 1 3499 ? 145.593 110.911 140.051 1.00 71.02  ? 3499 GLN A NE2   1 
ATOM   15177 N N     . MET A 1 3500 ? 139.134 112.739 141.473 1.00 66.02  ? 3500 MET A N     1 
ATOM   15178 C CA    . MET A 1 3500 ? 137.979 113.628 141.427 1.00 66.02  ? 3500 MET A CA    1 
ATOM   15179 C C     . MET A 1 3500 ? 137.312 113.717 142.792 1.00 66.02  ? 3500 MET A C     1 
ATOM   15180 O O     . MET A 1 3500 ? 136.826 114.782 143.189 1.00 66.02  ? 3500 MET A O     1 
ATOM   15181 C CB    . MET A 1 3500 ? 136.978 113.144 140.380 1.00 66.02  ? 3500 MET A CB    1 
ATOM   15182 C CG    . MET A 1 3500 ? 136.212 114.276 139.741 1.00 66.02  ? 3500 MET A CG    1 
ATOM   15183 S SD    . MET A 1 3500 ? 137.394 115.381 138.956 1.00 66.02  ? 3500 MET A SD    1 
ATOM   15184 C CE    . MET A 1 3500 ? 136.910 116.964 139.613 1.00 66.02  ? 3500 MET A CE    1 
ATOM   15185 N N     . SER A 1 3501 ? 137.269 112.598 143.516 1.00 65.92  ? 3501 SER A N     1 
ATOM   15186 C CA    . SER A 1 3501 ? 136.702 112.606 144.859 1.00 65.92  ? 3501 SER A CA    1 
ATOM   15187 C C     . SER A 1 3501 ? 137.502 113.494 145.799 1.00 65.92  ? 3501 SER A C     1 
ATOM   15188 O O     . SER A 1 3501 ? 136.931 114.105 146.709 1.00 65.92  ? 3501 SER A O     1 
ATOM   15189 C CB    . SER A 1 3501 ? 136.630 111.182 145.411 1.00 65.92  ? 3501 SER A CB    1 
ATOM   15190 O OG    . SER A 1 3501 ? 137.900 110.744 145.860 1.00 65.92  ? 3501 SER A OG    1 
ATOM   15191 N N     . THR A 1 3502 ? 138.817 113.580 145.605 1.00 56.19  ? 3502 THR A N     1 
ATOM   15192 C CA    . THR A 1 3502 ? 139.670 114.419 146.450 1.00 56.19  ? 3502 THR A CA    1 
ATOM   15193 C C     . THR A 1 3502 ? 140.358 115.493 145.598 1.00 56.19  ? 3502 THR A C     1 
ATOM   15194 O O     . THR A 1 3502 ? 141.525 115.383 145.220 1.00 56.19  ? 3502 THR A O     1 
ATOM   15195 C CB    . THR A 1 3502 ? 140.696 113.511 147.263 1.00 56.19  ? 3502 THR A CB    1 
ATOM   15196 O OG1   . THR A 1 3502 ? 141.425 114.309 148.206 1.00 56.19  ? 3502 THR A OG1   1 
ATOM   15197 C CG2   . THR A 1 3502 ? 141.637 112.706 146.358 1.00 56.19  ? 3502 THR A CG2   1 
ATOM   15198 N N     . ILE A 1 3503 ? 139.614 116.561 145.311 1.00 42.34  ? 3503 ILE A N     1 
ATOM   15199 C CA    . ILE A 1 3503 ? 140.152 117.708 144.585 1.00 42.34  ? 3503 ILE A CA    1 
ATOM   15200 C C     . ILE A 1 3503 ? 139.939 118.991 145.383 1.00 42.34  ? 3503 ILE A C     1 
ATOM   15201 O O     . ILE A 1 3503 ? 140.848 119.822 145.492 1.00 42.34  ? 3503 ILE A O     1 
ATOM   15202 C CB    . ILE A 1 3503 ? 139.541 117.819 143.174 1.00 42.34  ? 3503 ILE A CB    1 
ATOM   15203 C CG1   . ILE A 1 3503 ? 140.053 119.077 142.467 1.00 42.34  ? 3503 ILE A CG1   1 
ATOM   15204 C CG2   . ILE A 1 3503 ? 138.019 117.792 143.222 1.00 42.34  ? 3503 ILE A CG2   1 
ATOM   15205 C CD1   . ILE A 1 3503 ? 139.823 119.073 140.973 1.00 42.34  ? 3503 ILE A CD1   1 
ATOM   15206 N N     . ALA A 1 3504 ? 138.735 119.161 145.938 1.00 34.80  ? 3504 ALA A N     1 
ATOM   15207 C CA    . ALA A 1 3504 ? 138.342 120.445 146.513 1.00 34.80  ? 3504 ALA A CA    1 
ATOM   15208 C C     . ALA A 1 3504 ? 139.242 120.842 147.677 1.00 34.80  ? 3504 ALA A C     1 
ATOM   15209 O O     . ALA A 1 3504 ? 139.666 121.999 147.779 1.00 34.80  ? 3504 ALA A O     1 
ATOM   15210 C CB    . ALA A 1 3504 ? 136.881 120.390 146.959 1.00 34.80  ? 3504 ALA A CB    1 
ATOM   15211 N N     . GLY A 1 3505 ? 139.540 119.898 148.570 1.00 35.77  ? 3505 GLY A N     1 
ATOM   15212 C CA    . GLY A 1 3505 ? 140.384 120.219 149.710 1.00 35.77  ? 3505 GLY A CA    1 
ATOM   15213 C C     . GLY A 1 3505 ? 141.794 120.604 149.306 1.00 35.77  ? 3505 GLY A C     1 
ATOM   15214 O O     . GLY A 1 3505 ? 142.375 121.543 149.857 1.00 35.77  ? 3505 GLY A O     1 
ATOM   15215 N N     . ASP A 1 3506 ? 142.364 119.882 148.340 1.00 37.23  ? 3506 ASP A N     1 
ATOM   15216 C CA    . ASP A 1 3506 ? 143.706 120.203 147.868 1.00 37.23  ? 3506 ASP A CA    1 
ATOM   15217 C C     . ASP A 1 3506 ? 143.748 121.583 147.224 1.00 37.23  ? 3506 ASP A C     1 
ATOM   15218 O O     . ASP A 1 3506 ? 144.686 122.356 147.456 1.00 37.23  ? 3506 ASP A O     1 
ATOM   15219 C CB    . ASP A 1 3506 ? 144.178 119.132 146.886 1.00 37.23  ? 3506 ASP A CB    1 
ATOM   15220 C CG    . ASP A 1 3506 ? 145.676 119.152 146.677 1.00 37.23  ? 3506 ASP A CG    1 
ATOM   15221 O OD1   . ASP A 1 3506 ? 146.360 119.975 147.321 1.00 37.23  ? 3506 ASP A OD1   1 
ATOM   15222 O OD2   . ASP A 1 3506 ? 146.173 118.339 145.871 1.00 37.23  ? 3506 ASP A OD2   1 
ATOM   15223 N N     . CYS A 1 3507 ? 142.739 121.909 146.412 1.00 32.56  ? 3507 CYS A N     1 
ATOM   15224 C CA    . CYS A 1 3507 ? 142.675 123.234 145.805 1.00 32.56  ? 3507 CYS A CA    1 
ATOM   15225 C C     . CYS A 1 3507 ? 142.527 124.316 146.865 1.00 32.56  ? 3507 CYS A C     1 
ATOM   15226 O O     . CYS A 1 3507 ? 143.159 125.374 146.769 1.00 32.56  ? 3507 CYS A O     1 
ATOM   15227 C CB    . CYS A 1 3507 ? 141.522 123.299 144.805 1.00 32.56  ? 3507 CYS A CB    1 
ATOM   15228 S SG    . CYS A 1 3507 ? 141.774 122.309 143.317 1.00 32.56  ? 3507 CYS A SG    1 
ATOM   15229 N N     . LEU A 1 3508 ? 141.698 124.068 147.882 1.00 28.70  ? 3508 LEU A N     1 
ATOM   15230 C CA    . LEU A 1 3508 ? 141.551 125.024 148.975 1.00 28.70  ? 3508 LEU A CA    1 
ATOM   15231 C C     . LEU A 1 3508 ? 142.885 125.267 149.665 1.00 28.70  ? 3508 LEU A C     1 
ATOM   15232 O O     . LEU A 1 3508 ? 143.268 126.416 149.917 1.00 28.70  ? 3508 LEU A O     1 
ATOM   15233 C CB    . LEU A 1 3508 ? 140.510 124.511 149.974 1.00 28.70  ? 3508 LEU A CB    1 
ATOM   15234 C CG    . LEU A 1 3508 ? 139.797 125.481 150.921 1.00 28.70  ? 3508 LEU A CG    1 
ATOM   15235 C CD1   . LEU A 1 3508 ? 138.557 124.820 151.489 1.00 28.70  ? 3508 LEU A CD1   1 
ATOM   15236 C CD2   . LEU A 1 3508 ? 140.702 125.936 152.053 1.00 28.70  ? 3508 LEU A CD2   1 
ATOM   15237 N N     . LEU A 1 3509 ? 143.609 124.190 149.975 1.00 28.41  ? 3509 LEU A N     1 
ATOM   15238 C CA    . LEU A 1 3509 ? 144.889 124.334 150.660 1.00 28.41  ? 3509 LEU A CA    1 
ATOM   15239 C C     . LEU A 1 3509 ? 145.891 125.099 149.808 1.00 28.41  ? 3509 LEU A C     1 
ATOM   15240 O O     . LEU A 1 3509 ? 146.574 126.004 150.302 1.00 28.41  ? 3509 LEU A O     1 
ATOM   15241 C CB    . LEU A 1 3509 ? 145.442 122.959 151.029 1.00 28.41  ? 3509 LEU A CB    1 
ATOM   15242 C CG    . LEU A 1 3509 ? 144.692 122.237 152.144 1.00 28.41  ? 3509 LEU A CG    1 
ATOM   15243 C CD1   . LEU A 1 3509 ? 145.482 121.038 152.628 1.00 28.41  ? 3509 LEU A CD1   1 
ATOM   15244 C CD2   . LEU A 1 3509 ? 144.412 123.194 153.282 1.00 28.41  ? 3509 LEU A CD2   1 
ATOM   15245 N N     . SER A 1 3510 ? 145.988 124.758 148.522 1.00 27.98  ? 3510 SER A N     1 
ATOM   15246 C CA    . SER A 1 3510 ? 146.954 125.429 147.659 1.00 27.98  ? 3510 SER A CA    1 
ATOM   15247 C C     . SER A 1 3510 ? 146.614 126.905 147.485 1.00 27.98  ? 3510 SER A C     1 
ATOM   15248 O O     . SER A 1 3510 ? 147.508 127.760 147.493 1.00 27.98  ? 3510 SER A O     1 
ATOM   15249 C CB    . SER A 1 3510 ? 147.024 124.727 146.306 1.00 27.98  ? 3510 SER A CB    1 
ATOM   15250 O OG    . SER A 1 3510 ? 147.418 123.375 146.456 1.00 27.98  ? 3510 SER A OG    1 
ATOM   15251 N N     . ALA A 1 3511 ? 145.327 127.224 147.320 1.00 23.99  ? 3511 ALA A N     1 
ATOM   15252 C CA    . ALA A 1 3511 ? 144.927 128.619 147.178 1.00 23.99  ? 3511 ALA A CA    1 
ATOM   15253 C C     . ALA A 1 3511 ? 145.194 129.406 148.452 1.00 23.99  ? 3511 ALA A C     1 
ATOM   15254 O O     . ALA A 1 3511 ? 145.672 130.545 148.394 1.00 23.99  ? 3511 ALA A O     1 
ATOM   15255 C CB    . ALA A 1 3511 ? 143.452 128.706 146.797 1.00 23.99  ? 3511 ALA A CB    1 
ATOM   15256 N N     . ALA A 1 3512 ? 144.891 128.821 149.613 1.00 22.84  ? 3512 ALA A N     1 
ATOM   15257 C CA    . ALA A 1 3512 ? 145.179 129.499 150.871 1.00 22.84  ? 3512 ALA A CA    1 
ATOM   15258 C C     . ALA A 1 3512 ? 146.675 129.710 151.046 1.00 22.84  ? 3512 ALA A C     1 
ATOM   15259 O O     . ALA A 1 3512 ? 147.106 130.727 151.601 1.00 22.84  ? 3512 ALA A O     1 
ATOM   15260 C CB    . ALA A 1 3512 ? 144.604 128.703 152.041 1.00 22.84  ? 3512 ALA A CB    1 
ATOM   15261 N N     . PHE A 1 3513 ? 147.484 128.758 150.581 1.00 26.46  ? 3513 PHE A N     1 
ATOM   15262 C CA    . PHE A 1 3513 ? 148.931 128.911 150.672 1.00 26.46  ? 3513 PHE A CA    1 
ATOM   15263 C C     . PHE A 1 3513 ? 149.425 130.044 149.781 1.00 26.46  ? 3513 PHE A C     1 
ATOM   15264 O O     . PHE A 1 3513 ? 150.194 130.904 150.224 1.00 26.46  ? 3513 PHE A O     1 
ATOM   15265 C CB    . PHE A 1 3513 ? 149.620 127.599 150.300 1.00 26.46  ? 3513 PHE A CB    1 
ATOM   15266 C CG    . PHE A 1 3513 ? 151.097 127.735 150.079 1.00 26.46  ? 3513 PHE A CG    1 
ATOM   15267 C CD1   . PHE A 1 3513 ? 151.955 127.925 151.147 1.00 26.46  ? 3513 PHE A CD1   1 
ATOM   15268 C CD2   . PHE A 1 3513 ? 151.627 127.682 148.801 1.00 26.46  ? 3513 PHE A CD2   1 
ATOM   15269 C CE1   . PHE A 1 3513 ? 153.313 128.053 150.947 1.00 26.46  ? 3513 PHE A CE1   1 
ATOM   15270 C CE2   . PHE A 1 3513 ? 152.984 127.810 148.594 1.00 26.46  ? 3513 PHE A CE2   1 
ATOM   15271 C CZ    . PHE A 1 3513 ? 153.828 127.995 149.669 1.00 26.46  ? 3513 PHE A CZ    1 
ATOM   15272 N N     . ILE A 1 3514 ? 148.990 130.065 148.518 1.00 22.52  ? 3514 ILE A N     1 
ATOM   15273 C CA    . ILE A 1 3514 ? 149.520 131.047 147.571 1.00 22.52  ? 3514 ILE A CA    1 
ATOM   15274 C C     . ILE A 1 3514 ? 148.876 132.415 147.702 1.00 22.52  ? 3514 ILE A C     1 
ATOM   15275 O O     . ILE A 1 3514 ? 149.371 133.378 147.103 1.00 22.52  ? 3514 ILE A O     1 
ATOM   15276 C CB    . ILE A 1 3514 ? 149.372 130.568 146.115 1.00 22.52  ? 3514 ILE A CB    1 
ATOM   15277 C CG1   . ILE A 1 3514 ? 147.899 130.416 145.742 1.00 22.52  ? 3514 ILE A CG1   1 
ATOM   15278 C CG2   . ILE A 1 3514 ? 150.111 129.261 145.908 1.00 22.52  ? 3514 ILE A CG2   1 
ATOM   15279 C CD1   . ILE A 1 3514 ? 147.683 130.076 144.288 1.00 22.52  ? 3514 ILE A CD1   1 
ATOM   15280 N N     . ALA A 1 3515 ? 147.790 132.538 148.462 1.00 21.52  ? 3515 ALA A N     1 
ATOM   15281 C CA    . ALA A 1 3515 ? 147.135 133.820 148.680 1.00 21.52  ? 3515 ALA A CA    1 
ATOM   15282 C C     . ALA A 1 3515 ? 147.431 134.408 150.050 1.00 21.52  ? 3515 ALA A C     1 
ATOM   15283 O O     . ALA A 1 3515 ? 147.672 135.612 150.169 1.00 21.52  ? 3515 ALA A O     1 
ATOM   15284 C CB    . ALA A 1 3515 ? 145.619 133.675 148.495 1.00 21.52  ? 3515 ALA A CB    1 
ATOM   15285 N N     . TYR A 1 3516 ? 147.418 133.583 151.095 1.00 23.35  ? 3516 TYR A N     1 
ATOM   15286 C CA    . TYR A 1 3516 ? 147.664 134.056 152.451 1.00 23.35  ? 3516 TYR A CA    1 
ATOM   15287 C C     . TYR A 1 3516 ? 149.105 133.829 152.892 1.00 23.35  ? 3516 TYR A C     1 
ATOM   15288 O O     . TYR A 1 3516 ? 149.762 134.756 153.376 1.00 23.35  ? 3516 TYR A O     1 
ATOM   15289 C CB    . TYR A 1 3516 ? 146.722 133.360 153.435 1.00 23.35  ? 3516 TYR A CB    1 
ATOM   15290 C CG    . TYR A 1 3516 ? 145.354 133.980 153.540 1.00 23.35  ? 3516 TYR A CG    1 
ATOM   15291 C CD1   . TYR A 1 3516 ? 145.180 135.228 154.118 1.00 23.35  ? 3516 TYR A CD1   1 
ATOM   15292 C CD2   . TYR A 1 3516 ? 144.231 133.302 153.096 1.00 23.35  ? 3516 TYR A CD2   1 
ATOM   15293 C CE1   . TYR A 1 3516 ? 143.933 135.790 154.230 1.00 23.35  ? 3516 TYR A CE1   1 
ATOM   15294 C CE2   . TYR A 1 3516 ? 142.980 133.857 153.205 1.00 23.35  ? 3516 TYR A CE2   1 
ATOM   15295 C CZ    . TYR A 1 3516 ? 142.836 135.101 153.771 1.00 23.35  ? 3516 TYR A CZ    1 
ATOM   15296 O OH    . TYR A 1 3516 ? 141.588 135.657 153.882 1.00 23.35  ? 3516 TYR A OH    1 
ATOM   15297 N N     . ALA A 1 3517 ? 149.609 132.605 152.730 1.00 23.76  ? 3517 ALA A N     1 
ATOM   15298 C CA    . ALA A 1 3517 ? 150.889 132.208 153.315 1.00 23.76  ? 3517 ALA A CA    1 
ATOM   15299 C C     . ALA A 1 3517 ? 152.059 132.777 152.511 1.00 23.76  ? 3517 ALA A C     1 
ATOM   15300 O O     . ALA A 1 3517 ? 152.926 132.064 152.009 1.00 23.76  ? 3517 ALA A O     1 
ATOM   15301 C CB    . ALA A 1 3517 ? 150.972 130.691 153.416 1.00 23.76  ? 3517 ALA A CB    1 
ATOM   15302 N N     . GLY A 1 3518 ? 152.068 134.101 152.405 1.00 25.04  ? 3518 GLY A N     1 
ATOM   15303 C CA    . GLY A 1 3518 ? 153.207 134.825 151.886 1.00 25.04  ? 3518 GLY A CA    1 
ATOM   15304 C C     . GLY A 1 3518 ? 153.807 135.653 152.999 1.00 25.04  ? 3518 GLY A C     1 
ATOM   15305 O O     . GLY A 1 3518 ? 153.156 135.855 154.028 1.00 25.04  ? 3518 GLY A O     1 
ATOM   15306 N N     . TYR A 1 3519 ? 155.057 136.090 152.831 1.00 31.49  ? 3519 TYR A N     1 
ATOM   15307 C CA    . TYR A 1 3519 ? 155.749 136.944 153.793 1.00 31.49  ? 3519 TYR A CA    1 
ATOM   15308 C C     . TYR A 1 3519 ? 156.118 136.169 155.054 1.00 31.49  ? 3519 TYR A C     1 
ATOM   15309 O O     . TYR A 1 3519 ? 156.860 136.670 155.905 1.00 31.49  ? 3519 TYR A O     1 
ATOM   15310 C CB    . TYR A 1 3519 ? 154.896 138.173 154.135 1.00 31.49  ? 3519 TYR A CB    1 
ATOM   15311 C CG    . TYR A 1 3519 ? 155.426 139.019 155.265 1.00 31.49  ? 3519 TYR A CG    1 
ATOM   15312 C CD1   . TYR A 1 3519 ? 156.512 139.859 155.076 1.00 31.49  ? 3519 TYR A CD1   1 
ATOM   15313 C CD2   . TYR A 1 3519 ? 154.844 138.971 156.523 1.00 31.49  ? 3519 TYR A CD2   1 
ATOM   15314 C CE1   . TYR A 1 3519 ? 157.001 140.631 156.105 1.00 31.49  ? 3519 TYR A CE1   1 
ATOM   15315 C CE2   . TYR A 1 3519 ? 155.328 139.738 157.560 1.00 31.49  ? 3519 TYR A CE2   1 
ATOM   15316 C CZ    . TYR A 1 3519 ? 156.405 140.567 157.345 1.00 31.49  ? 3519 TYR A CZ    1 
ATOM   15317 O OH    . TYR A 1 3519 ? 156.890 141.336 158.375 1.00 31.49  ? 3519 TYR A OH    1 
ATOM   15318 N N     . PHE A 1 3520 ? 155.646 134.934 155.168 1.00 26.16  ? 3520 PHE A N     1 
ATOM   15319 C CA    . PHE A 1 3520 ? 155.942 134.107 156.326 1.00 26.16  ? 3520 PHE A CA    1 
ATOM   15320 C C     . PHE A 1 3520 ? 157.132 133.203 156.043 1.00 26.16  ? 3520 PHE A C     1 
ATOM   15321 O O     . PHE A 1 3520 ? 157.321 132.721 154.923 1.00 26.16  ? 3520 PHE A O     1 
ATOM   15322 C CB    . PHE A 1 3520 ? 154.728 133.263 156.716 1.00 26.16  ? 3520 PHE A CB    1 
ATOM   15323 C CG    . PHE A 1 3520 ? 153.585 134.062 157.271 1.00 26.16  ? 3520 PHE A CG    1 
ATOM   15324 C CD1   . PHE A 1 3520 ? 153.697 134.695 158.496 1.00 26.16  ? 3520 PHE A CD1   1 
ATOM   15325 C CD2   . PHE A 1 3520 ? 152.398 134.177 156.570 1.00 26.16  ? 3520 PHE A CD2   1 
ATOM   15326 C CE1   . PHE A 1 3520 ? 152.647 135.429 159.010 1.00 26.16  ? 3520 PHE A CE1   1 
ATOM   15327 C CE2   . PHE A 1 3520 ? 151.345 134.910 157.079 1.00 26.16  ? 3520 PHE A CE2   1 
ATOM   15328 C CZ    . PHE A 1 3520 ? 151.470 135.537 158.300 1.00 26.16  ? 3520 PHE A CZ    1 
ATOM   15329 N N     . ASP A 1 3521 ? 157.940 132.977 157.075 1.00 30.71  ? 3521 ASP A N     1 
ATOM   15330 C CA    . ASP A 1 3521 ? 159.086 132.091 156.955 1.00 30.71  ? 3521 ASP A CA    1 
ATOM   15331 C C     . ASP A 1 3521 ? 158.614 130.643 156.828 1.00 30.71  ? 3521 ASP A C     1 
ATOM   15332 O O     . ASP A 1 3521 ? 157.426 130.331 156.951 1.00 30.71  ? 3521 ASP A O     1 
ATOM   15333 C CB    . ASP A 1 3521 ? 160.024 132.279 158.143 1.00 30.71  ? 3521 ASP A CB    1 
ATOM   15334 C CG    . ASP A 1 3521 ? 159.288 132.316 159.464 1.00 30.71  ? 3521 ASP A CG    1 
ATOM   15335 O OD1   . ASP A 1 3521 ? 158.295 133.066 159.570 1.00 30.71  ? 3521 ASP A OD1   1 
ATOM   15336 O OD2   . ASP A 1 3521 ? 159.710 131.609 160.400 1.00 30.71  ? 3521 ASP A OD2   1 
ATOM   15337 N N     . GLN A 1 3522 ? 159.569 129.744 156.576 1.00 32.90  ? 3522 GLN A N     1 
ATOM   15338 C CA    . GLN A 1 3522 ? 159.220 128.371 156.220 1.00 32.90  ? 3522 GLN A CA    1 
ATOM   15339 C C     . GLN A 1 3522 ? 158.452 127.674 157.336 1.00 32.90  ? 3522 GLN A C     1 
ATOM   15340 O O     . GLN A 1 3522 ? 157.460 126.982 157.075 1.00 32.90  ? 3522 GLN A O     1 
ATOM   15341 C CB    . GLN A 1 3522 ? 160.481 127.586 155.864 1.00 32.90  ? 3522 GLN A CB    1 
ATOM   15342 C CG    . GLN A 1 3522 ? 160.221 126.129 155.530 1.00 32.90  ? 3522 GLN A CG    1 
ATOM   15343 C CD    . GLN A 1 3522 ? 161.064 125.639 154.373 1.00 32.90  ? 3522 GLN A CD    1 
ATOM   15344 O OE1   . GLN A 1 3522 ? 161.441 126.413 153.494 1.00 32.90  ? 3522 GLN A OE1   1 
ATOM   15345 N NE2   . GLN A 1 3522 ? 161.363 124.346 154.365 1.00 32.90  ? 3522 GLN A NE2   1 
ATOM   15346 N N     . GLN A 1 3523 ? 158.887 127.843 158.586 1.00 32.47  ? 3523 GLN A N     1 
ATOM   15347 C CA    . GLN A 1 3523 ? 158.196 127.178 159.685 1.00 32.47  ? 3523 GLN A CA    1 
ATOM   15348 C C     . GLN A 1 3523 ? 156.790 127.733 159.869 1.00 32.47  ? 3523 GLN A C     1 
ATOM   15349 O O     . GLN A 1 3523 ? 155.860 126.985 160.183 1.00 32.47  ? 3523 GLN A O     1 
ATOM   15350 C CB    . GLN A 1 3523 ? 159.001 127.296 160.981 1.00 32.47  ? 3523 GLN A CB    1 
ATOM   15351 C CG    . GLN A 1 3523 ? 159.159 128.707 161.515 1.00 32.47  ? 3523 GLN A CG    1 
ATOM   15352 C CD    . GLN A 1 3523 ? 160.014 128.764 162.764 1.00 32.47  ? 3523 GLN A CD    1 
ATOM   15353 O OE1   . GLN A 1 3523 ? 160.457 127.736 163.275 1.00 32.47  ? 3523 GLN A OE1   1 
ATOM   15354 N NE2   . GLN A 1 3523 ? 160.248 129.971 163.266 1.00 32.47  ? 3523 GLN A NE2   1 
ATOM   15355 N N     . MET A 1 3524 ? 156.611 129.042 159.672 1.00 30.09  ? 3524 MET A N     1 
ATOM   15356 C CA    . MET A 1 3524 ? 155.278 129.624 159.797 1.00 30.09  ? 3524 MET A CA    1 
ATOM   15357 C C     . MET A 1 3524 ? 154.349 129.121 158.699 1.00 30.09  ? 3524 MET A C     1 
ATOM   15358 O O     . MET A 1 3524 ? 153.183 128.802 158.963 1.00 30.09  ? 3524 MET A O     1 
ATOM   15359 C CB    . MET A 1 3524 ? 155.362 131.148 159.774 1.00 30.09  ? 3524 MET A CB    1 
ATOM   15360 C CG    . MET A 1 3524 ? 154.251 131.833 160.547 1.00 30.09  ? 3524 MET A CG    1 
ATOM   15361 S SD    . MET A 1 3524 ? 154.301 131.456 162.307 1.00 30.09  ? 3524 MET A SD    1 
ATOM   15362 C CE    . MET A 1 3524 ? 152.555 131.282 162.663 1.00 30.09  ? 3524 MET A CE    1 
ATOM   15363 N N     . ARG A 1 3525 ? 154.846 129.044 157.462 1.00 27.28  ? 3525 ARG A N     1 
ATOM   15364 C CA    . ARG A 1 3525 ? 154.041 128.496 156.376 1.00 27.28  ? 3525 ARG A CA    1 
ATOM   15365 C C     . ARG A 1 3525 ? 153.673 127.045 156.650 1.00 27.28  ? 3525 ARG A C     1 
ATOM   15366 O O     . ARG A 1 3525 ? 152.527 126.633 156.429 1.00 27.28  ? 3525 ARG A O     1 
ATOM   15367 C CB    . ARG A 1 3525 ? 154.794 128.606 155.052 1.00 27.28  ? 3525 ARG A CB    1 
ATOM   15368 C CG    . ARG A 1 3525 ? 154.996 130.022 154.552 1.00 27.28  ? 3525 ARG A CG    1 
ATOM   15369 C CD    . ARG A 1 3525 ? 155.752 130.018 153.235 1.00 27.28  ? 3525 ARG A CD    1 
ATOM   15370 N NE    . ARG A 1 3525 ? 156.383 131.301 152.957 1.00 27.28  ? 3525 ARG A NE    1 
ATOM   15371 C CZ    . ARG A 1 3525 ? 156.962 131.614 151.807 1.00 27.28  ? 3525 ARG A CZ    1 
ATOM   15372 N NH1   . ARG A 1 3525 ? 157.007 130.758 150.801 1.00 27.28  ? 3525 ARG A NH1   1 
ATOM   15373 N NH2   . ARG A 1 3525 ? 157.511 132.817 151.663 1.00 27.28  ? 3525 ARG A NH2   1 
ATOM   15374 N N     . GLN A 1 3526 ? 154.635 126.255 157.132 1.00 29.76  ? 3526 GLN A N     1 
ATOM   15375 C CA    . GLN A 1 3526 ? 154.359 124.857 157.442 1.00 29.76  ? 3526 GLN A CA    1 
ATOM   15376 C C     . GLN A 1 3526 ? 153.334 124.731 158.561 1.00 29.76  ? 3526 GLN A C     1 
ATOM   15377 O O     . GLN A 1 3526 ? 152.445 123.876 158.502 1.00 29.76  ? 3526 GLN A O     1 
ATOM   15378 C CB    . GLN A 1 3526 ? 155.653 124.136 157.814 1.00 29.76  ? 3526 GLN A CB    1 
ATOM   15379 C CG    . GLN A 1 3526 ? 155.493 122.637 157.983 1.00 29.76  ? 3526 GLN A CG    1 
ATOM   15380 C CD    . GLN A 1 3526 ? 154.715 122.006 156.846 1.00 29.76  ? 3526 GLN A CD    1 
ATOM   15381 O OE1   . GLN A 1 3526 ? 155.075 122.151 155.678 1.00 29.76  ? 3526 GLN A OE1   1 
ATOM   15382 N NE2   . GLN A 1 3526 ? 153.641 121.302 157.183 1.00 29.76  ? 3526 GLN A NE2   1 
ATOM   15383 N N     . ASN A 1 3527 ? 153.441 125.574 159.590 1.00 28.53  ? 3527 ASN A N     1 
ATOM   15384 C CA    . ASN A 1 3527 ? 152.484 125.534 160.690 1.00 28.53  ? 3527 ASN A CA    1 
ATOM   15385 C C     . ASN A 1 3527 ? 151.085 125.903 160.213 1.00 28.53  ? 3527 ASN A C     1 
ATOM   15386 O O     . ASN A 1 3527 ? 150.101 125.257 160.592 1.00 28.53  ? 3527 ASN A O     1 
ATOM   15387 C CB    . ASN A 1 3527 ? 152.941 126.475 161.806 1.00 28.53  ? 3527 ASN A CB    1 
ATOM   15388 C CG    . ASN A 1 3527 ? 152.123 126.324 163.079 1.00 28.53  ? 3527 ASN A CG    1 
ATOM   15389 O OD1   . ASN A 1 3527 ? 151.187 125.529 163.145 1.00 28.53  ? 3527 ASN A OD1   1 
ATOM   15390 N ND2   . ASN A 1 3527 ? 152.477 127.097 164.099 1.00 28.53  ? 3527 ASN A ND2   1 
ATOM   15391 N N     . LEU A 1 3528 ? 150.976 126.938 159.376 1.00 26.91  ? 3528 LEU A N     1 
ATOM   15392 C CA    . LEU A 1 3528 ? 149.669 127.323 158.854 1.00 26.91  ? 3528 LEU A CA    1 
ATOM   15393 C C     . LEU A 1 3528 ? 149.072 126.218 157.992 1.00 26.91  ? 3528 LEU A C     1 
ATOM   15394 O O     . LEU A 1 3528 ? 147.875 125.917 158.095 1.00 26.91  ? 3528 LEU A O     1 
ATOM   15395 C CB    . LEU A 1 3528 ? 149.782 128.620 158.057 1.00 26.91  ? 3528 LEU A CB    1 
ATOM   15396 C CG    . LEU A 1 3528 ? 150.055 129.885 158.868 1.00 26.91  ? 3528 LEU A CG    1 
ATOM   15397 C CD1   . LEU A 1 3528 ? 150.134 131.093 157.952 1.00 26.91  ? 3528 LEU A CD1   1 
ATOM   15398 C CD2   . LEU A 1 3528 ? 148.988 130.079 159.928 1.00 26.91  ? 3528 LEU A CD2   1 
ATOM   15399 N N     . PHE A 1 3529 ? 149.888 125.601 157.135 1.00 29.03  ? 3529 PHE A N     1 
ATOM   15400 C CA    . PHE A 1 3529 ? 149.382 124.525 156.290 1.00 29.03  ? 3529 PHE A CA    1 
ATOM   15401 C C     . PHE A 1 3529 ? 148.955 123.331 157.134 1.00 29.03  ? 3529 PHE A C     1 
ATOM   15402 O O     . PHE A 1 3529 ? 147.934 122.693 156.850 1.00 29.03  ? 3529 PHE A O     1 
ATOM   15403 C CB    . PHE A 1 3529 ? 150.443 124.128 155.262 1.00 29.03  ? 3529 PHE A CB    1 
ATOM   15404 C CG    . PHE A 1 3529 ? 149.922 123.268 154.141 1.00 29.03  ? 3529 PHE A CG    1 
ATOM   15405 C CD1   . PHE A 1 3529 ? 149.821 123.781 152.859 1.00 29.03  ? 3529 PHE A CD1   1 
ATOM   15406 C CD2   . PHE A 1 3529 ? 149.567 121.947 154.355 1.00 29.03  ? 3529 PHE A CD2   1 
ATOM   15407 C CE1   . PHE A 1 3529 ? 149.351 123.004 151.821 1.00 29.03  ? 3529 PHE A CE1   1 
ATOM   15408 C CE2   . PHE A 1 3529 ? 149.097 121.165 153.320 1.00 29.03  ? 3529 PHE A CE2   1 
ATOM   15409 C CZ    . PHE A 1 3529 ? 148.990 121.694 152.051 1.00 29.03  ? 3529 PHE A CZ    1 
ATOM   15410 N N     . THR A 1 3530 ? 149.722 123.017 158.180 1.00 27.87  ? 3530 THR A N     1 
ATOM   15411 C CA    . THR A 1 3530 ? 149.348 121.929 159.075 1.00 27.87  ? 3530 THR A CA    1 
ATOM   15412 C C     . THR A 1 3530 ? 148.030 122.225 159.776 1.00 27.87  ? 3530 THR A C     1 
ATOM   15413 O O     . THR A 1 3530 ? 147.180 121.340 159.910 1.00 27.87  ? 3530 THR A O     1 
ATOM   15414 C CB    . THR A 1 3530 ? 150.458 121.685 160.098 1.00 27.87  ? 3530 THR A CB    1 
ATOM   15415 O OG1   . THR A 1 3530 ? 151.665 121.323 159.416 1.00 27.87  ? 3530 THR A OG1   1 
ATOM   15416 C CG2   . THR A 1 3530 ? 150.070 120.570 161.056 1.00 27.87  ? 3530 THR A CG2   1 
ATOM   15417 N N     . THR A 1 3531 ? 147.839 123.468 160.226 1.00 27.72  ? 3531 THR A N     1 
ATOM   15418 C CA    . THR A 1 3531 ? 146.581 123.833 160.869 1.00 27.72  ? 3531 THR A CA    1 
ATOM   15419 C C     . THR A 1 3531 ? 145.408 123.707 159.903 1.00 27.72  ? 3531 THR A C     1 
ATOM   15420 O O     . THR A 1 3531 ? 144.347 123.184 160.266 1.00 27.72  ? 3531 THR A O     1 
ATOM   15421 C CB    . THR A 1 3531 ? 146.665 125.255 161.423 1.00 27.72  ? 3531 THR A CB    1 
ATOM   15422 O OG1   . THR A 1 3531 ? 147.878 125.409 162.168 1.00 27.72  ? 3531 THR A OG1   1 
ATOM   15423 C CG2   . THR A 1 3531 ? 145.481 125.541 162.332 1.00 27.72  ? 3531 THR A CG2   1 
ATOM   15424 N N     . TRP A 1 3532 ? 145.584 124.176 158.664 1.00 26.44  ? 3532 TRP A N     1 
ATOM   15425 C CA    . TRP A 1 3532 ? 144.508 124.075 157.681 1.00 26.44  ? 3532 TRP A CA    1 
ATOM   15426 C C     . TRP A 1 3532 ? 144.174 122.619 157.374 1.00 26.44  ? 3532 TRP A C     1 
ATOM   15427 O O     . TRP A 1 3532 ? 142.997 122.247 157.291 1.00 26.44  ? 3532 TRP A O     1 
ATOM   15428 C CB    . TRP A 1 3532 ? 144.891 124.808 156.397 1.00 26.44  ? 3532 TRP A CB    1 
ATOM   15429 C CG    . TRP A 1 3532 ? 145.281 126.236 156.582 1.00 26.44  ? 3532 TRP A CG    1 
ATOM   15430 C CD1   . TRP A 1 3532 ? 144.936 127.056 157.614 1.00 26.44  ? 3532 TRP A CD1   1 
ATOM   15431 C CD2   . TRP A 1 3532 ? 146.096 127.016 155.703 1.00 26.44  ? 3532 TRP A CD2   1 
ATOM   15432 N NE1   . TRP A 1 3532 ? 145.487 128.301 157.431 1.00 26.44  ? 3532 TRP A NE1   1 
ATOM   15433 C CE2   . TRP A 1 3532 ? 146.204 128.301 156.264 1.00 26.44  ? 3532 TRP A CE2   1 
ATOM   15434 C CE3   . TRP A 1 3532 ? 146.745 126.752 154.494 1.00 26.44  ? 3532 TRP A CE3   1 
ATOM   15435 C CZ2   . TRP A 1 3532 ? 146.936 129.319 155.659 1.00 26.44  ? 3532 TRP A CZ2   1 
ATOM   15436 C CZ3   . TRP A 1 3532 ? 147.470 127.762 153.896 1.00 26.44  ? 3532 TRP A CZ3   1 
ATOM   15437 C CH2   . TRP A 1 3532 ? 147.559 129.030 154.478 1.00 26.44  ? 3532 TRP A CH2   1 
ATOM   15438 N N     . SER A 1 3533 ? 145.198 121.781 157.194 1.00 30.35  ? 3533 SER A N     1 
ATOM   15439 C CA    . SER A 1 3533 ? 144.957 120.372 156.904 1.00 30.35  ? 3533 SER A CA    1 
ATOM   15440 C C     . SER A 1 3533 ? 144.298 119.671 158.084 1.00 30.35  ? 3533 SER A C     1 
ATOM   15441 O O     . SER A 1 3533 ? 143.421 118.820 157.897 1.00 30.35  ? 3533 SER A O     1 
ATOM   15442 C CB    . SER A 1 3533 ? 146.266 119.682 156.528 1.00 30.35  ? 3533 SER A CB    1 
ATOM   15443 O OG    . SER A 1 3533 ? 147.309 120.061 157.406 1.00 30.35  ? 3533 SER A OG    1 
ATOM   15444 N N     . HIS A 1 3534 ? 144.709 120.012 159.307 1.00 35.53  ? 3534 HIS A N     1 
ATOM   15445 C CA    . HIS A 1 3534 ? 144.077 119.437 160.488 1.00 35.53  ? 3534 HIS A CA    1 
ATOM   15446 C C     . HIS A 1 3534 ? 142.610 119.834 160.568 1.00 35.53  ? 3534 HIS A C     1 
ATOM   15447 O O     . HIS A 1 3534 ? 141.757 119.013 160.919 1.00 35.53  ? 3534 HIS A O     1 
ATOM   15448 C CB    . HIS A 1 3534 ? 144.830 119.871 161.746 1.00 35.53  ? 3534 HIS A CB    1 
ATOM   15449 C CG    . HIS A 1 3534 ? 144.116 119.553 163.022 1.00 35.53  ? 3534 HIS A CG    1 
ATOM   15450 N ND1   . HIS A 1 3534 ? 143.141 120.369 163.554 1.00 35.53  ? 3534 HIS A ND1   1 
ATOM   15451 C CD2   . HIS A 1 3534 ? 144.238 118.508 163.875 1.00 35.53  ? 3534 HIS A CD2   1 
ATOM   15452 C CE1   . HIS A 1 3534 ? 142.693 119.840 164.679 1.00 35.53  ? 3534 HIS A CE1   1 
ATOM   15453 N NE2   . HIS A 1 3534 ? 143.341 118.710 164.895 1.00 35.53  ? 3534 HIS A NE2   1 
ATOM   15454 N N     . HIS A 1 3535 ? 142.296 121.092 160.247 1.00 34.95  ? 3535 HIS A N     1 
ATOM   15455 C CA    . HIS A 1 3535 ? 140.898 121.513 160.242 1.00 34.95  ? 3535 HIS A CA    1 
ATOM   15456 C C     . HIS A 1 3535 ? 140.100 120.776 159.176 1.00 34.95  ? 3535 HIS A C     1 
ATOM   15457 O O     . HIS A 1 3535 ? 138.955 120.374 159.416 1.00 34.95  ? 3535 HIS A O     1 
ATOM   15458 C CB    . HIS A 1 3535 ? 140.791 123.018 160.028 1.00 34.95  ? 3535 HIS A CB    1 
ATOM   15459 C CG    . HIS A 1 3535 ? 139.390 123.536 160.120 1.00 34.95  ? 3535 HIS A CG    1 
ATOM   15460 N ND1   . HIS A 1 3535 ? 138.839 123.988 161.300 1.00 34.95  ? 3535 HIS A ND1   1 
ATOM   15461 C CD2   . HIS A 1 3535 ? 138.423 123.663 159.181 1.00 34.95  ? 3535 HIS A CD2   1 
ATOM   15462 C CE1   . HIS A 1 3535 ? 137.595 124.376 161.083 1.00 34.95  ? 3535 HIS A CE1   1 
ATOM   15463 N NE2   . HIS A 1 3535 ? 137.318 124.189 159.805 1.00 34.95  ? 3535 HIS A NE2   1 
ATOM   15464 N N     . LEU A 1 3536 ? 140.679 120.599 157.987 1.00 37.14  ? 3536 LEU A N     1 
ATOM   15465 C CA    . LEU A 1 3536 ? 139.982 119.856 156.941 1.00 37.14  ? 3536 LEU A CA    1 
ATOM   15466 C C     . LEU A 1 3536 ? 139.739 118.413 157.365 1.00 37.14  ? 3536 LEU A C     1 
ATOM   15467 O O     . LEU A 1 3536 ? 138.686 117.838 157.064 1.00 37.14  ? 3536 LEU A O     1 
ATOM   15468 C CB    . LEU A 1 3536 ? 140.768 119.907 155.633 1.00 37.14  ? 3536 LEU A CB    1 
ATOM   15469 C CG    . LEU A 1 3536 ? 140.765 121.249 154.903 1.00 37.14  ? 3536 LEU A CG    1 
ATOM   15470 C CD1   . LEU A 1 3536 ? 141.455 121.118 153.559 1.00 37.14  ? 3536 LEU A CD1   1 
ATOM   15471 C CD2   . LEU A 1 3536 ? 139.347 121.759 154.731 1.00 37.14  ? 3536 LEU A CD2   1 
ATOM   15472 N N     . GLN A 1 3537 ? 140.707 117.808 158.056 1.00 40.16  ? 3537 GLN A N     1 
ATOM   15473 C CA    . GLN A 1 3537 ? 140.502 116.470 158.600 1.00 40.16  ? 3537 GLN A CA    1 
ATOM   15474 C C     . GLN A 1 3537 ? 139.383 116.463 159.635 1.00 40.16  ? 3537 GLN A C     1 
ATOM   15475 O O     . GLN A 1 3537 ? 138.559 115.542 159.664 1.00 40.16  ? 3537 GLN A O     1 
ATOM   15476 C CB    . GLN A 1 3537 ? 141.804 115.946 159.208 1.00 40.16  ? 3537 GLN A CB    1 
ATOM   15477 C CG    . GLN A 1 3537 ? 141.658 114.712 160.095 1.00 40.16  ? 3537 GLN A CG    1 
ATOM   15478 C CD    . GLN A 1 3537 ? 141.248 113.462 159.332 1.00 40.16  ? 3537 GLN A CD    1 
ATOM   15479 O OE1   . GLN A 1 3537 ? 140.166 113.394 158.748 1.00 40.16  ? 3537 GLN A OE1   1 
ATOM   15480 N NE2   . GLN A 1 3537 ? 142.119 112.460 159.338 1.00 40.16  ? 3537 GLN A NE2   1 
ATOM   15481 N N     . GLN A 1 3538 ? 139.337 117.485 160.495 1.00 45.80  ? 3538 GLN A N     1 
ATOM   15482 C CA    . GLN A 1 3538 ? 138.245 117.596 161.457 1.00 45.80  ? 3538 GLN A CA    1 
ATOM   15483 C C     . GLN A 1 3538 ? 136.902 117.776 160.764 1.00 45.80  ? 3538 GLN A C     1 
ATOM   15484 O O     . GLN A 1 3538 ? 135.873 117.331 161.285 1.00 45.80  ? 3538 GLN A O     1 
ATOM   15485 C CB    . GLN A 1 3538 ? 138.497 118.759 162.418 1.00 45.80  ? 3538 GLN A CB    1 
ATOM   15486 C CG    . GLN A 1 3538 ? 139.725 118.597 163.297 1.00 45.80  ? 3538 GLN A CG    1 
ATOM   15487 C CD    . GLN A 1 3538 ? 139.594 117.453 164.281 1.00 45.80  ? 3538 GLN A CD    1 
ATOM   15488 O OE1   . GLN A 1 3538 ? 138.523 117.222 164.842 1.00 45.80  ? 3538 GLN A OE1   1 
ATOM   15489 N NE2   . GLN A 1 3538 ? 140.687 116.731 164.500 1.00 45.80  ? 3538 GLN A NE2   1 
ATOM   15490 N N     . ALA A 1 3539 ? 136.889 118.420 159.600 1.00 48.66  ? 3539 ALA A N     1 
ATOM   15491 C CA    . ALA A 1 3539 ? 135.661 118.628 158.844 1.00 48.66  ? 3539 ALA A CA    1 
ATOM   15492 C C     . ALA A 1 3539 ? 135.372 117.500 157.864 1.00 48.66  ? 3539 ALA A C     1 
ATOM   15493 O O     . ALA A 1 3539 ? 134.397 117.595 157.111 1.00 48.66  ? 3539 ALA A O     1 
ATOM   15494 C CB    . ALA A 1 3539 ? 135.726 119.958 158.091 1.00 48.66  ? 3539 ALA A CB    1 
ATOM   15495 N N     . ASN A 1 3540 ? 136.192 116.447 157.857 1.00 51.11  ? 3540 ASN A N     1 
ATOM   15496 C CA    . ASN A 1 3540 ? 136.031 115.316 156.941 1.00 51.11  ? 3540 ASN A CA    1 
ATOM   15497 C C     . ASN A 1 3540 ? 135.998 115.776 155.486 1.00 51.11  ? 3540 ASN A C     1 
ATOM   15498 O O     . ASN A 1 3540 ? 135.214 115.279 154.675 1.00 51.11  ? 3540 ASN A O     1 
ATOM   15499 C CB    . ASN A 1 3540 ? 134.786 114.494 157.281 1.00 51.11  ? 3540 ASN A CB    1 
ATOM   15500 C CG    . ASN A 1 3540 ? 135.009 113.556 158.450 1.00 51.11  ? 3540 ASN A CG    1 
ATOM   15501 O OD1   . ASN A 1 3540 ? 136.096 113.001 158.614 1.00 51.11  ? 3540 ASN A OD1   1 
ATOM   15502 N ND2   . ASN A 1 3540 ? 133.978 113.366 159.263 1.00 51.11  ? 3540 ASN A ND2   1 
ATOM   15503 N N     . ILE A 1 3541 ? 136.854 116.737 155.154 1.00 46.69  ? 3541 ILE A N     1 
ATOM   15504 C CA    . ILE A 1 3541 ? 137.023 117.207 153.786 1.00 46.69  ? 3541 ILE A CA    1 
ATOM   15505 C C     . ILE A 1 3541 ? 138.120 116.380 153.136 1.00 46.69  ? 3541 ILE A C     1 
ATOM   15506 O O     . ILE A 1 3541 ? 139.249 116.325 153.640 1.00 46.69  ? 3541 ILE A O     1 
ATOM   15507 C CB    . ILE A 1 3541 ? 137.363 118.706 153.744 1.00 46.69  ? 3541 ILE A CB    1 
ATOM   15508 C CG1   . ILE A 1 3541 ? 136.254 119.520 154.412 1.00 46.69  ? 3541 ILE A CG1   1 
ATOM   15509 C CG2   . ILE A 1 3541 ? 137.571 119.161 152.311 1.00 46.69  ? 3541 ILE A CG2   1 
ATOM   15510 C CD1   . ILE A 1 3541 ? 134.911 119.378 153.739 1.00 46.69  ? 3541 ILE A CD1   1 
ATOM   15511 N N     . GLN A 1 3542 ? 137.793 115.735 152.021 1.00 46.78  ? 3542 GLN A N     1 
ATOM   15512 C CA    . GLN A 1 3542 ? 138.707 114.792 151.383 1.00 46.78  ? 3542 GLN A CA    1 
ATOM   15513 C C     . GLN A 1 3542 ? 139.761 115.566 150.604 1.00 46.78  ? 3542 GLN A C     1 
ATOM   15514 O O     . GLN A 1 3542 ? 139.560 115.920 149.440 1.00 46.78  ? 3542 GLN A O     1 
ATOM   15515 C CB    . GLN A 1 3542 ? 137.942 113.831 150.481 1.00 46.78  ? 3542 GLN A CB    1 
ATOM   15516 C CG    . GLN A 1 3542 ? 137.284 112.682 151.226 1.00 46.78  ? 3542 GLN A CG    1 
ATOM   15517 C CD    . GLN A 1 3542 ? 138.211 112.045 152.243 1.00 46.78  ? 3542 GLN A CD    1 
ATOM   15518 O OE1   . GLN A 1 3542 ? 138.107 112.302 153.443 1.00 46.78  ? 3542 GLN A OE1   1 
ATOM   15519 N NE2   . GLN A 1 3542 ? 139.127 111.210 151.767 1.00 46.78  ? 3542 GLN A NE2   1 
ATOM   15520 N N     . PHE A 1 3543 ? 140.893 115.826 151.249 1.00 44.27  ? 3543 PHE A N     1 
ATOM   15521 C CA    . PHE A 1 3543 ? 142.063 116.393 150.599 1.00 44.27  ? 3543 PHE A CA    1 
ATOM   15522 C C     . PHE A 1 3543 ? 143.171 115.351 150.576 1.00 44.27  ? 3543 PHE A C     1 
ATOM   15523 O O     . PHE A 1 3543 ? 143.297 114.537 151.496 1.00 44.27  ? 3543 PHE A O     1 
ATOM   15524 C CB    . PHE A 1 3543 ? 142.543 117.660 151.313 1.00 44.27  ? 3543 PHE A CB    1 
ATOM   15525 C CG    . PHE A 1 3543 ? 143.236 117.398 152.618 1.00 44.27  ? 3543 PHE A CG    1 
ATOM   15526 C CD1   . PHE A 1 3543 ? 142.512 117.062 153.748 1.00 44.27  ? 3543 PHE A CD1   1 
ATOM   15527 C CD2   . PHE A 1 3543 ? 144.613 117.496 152.717 1.00 44.27  ? 3543 PHE A CD2   1 
ATOM   15528 C CE1   . PHE A 1 3543 ? 143.147 116.823 154.950 1.00 44.27  ? 3543 PHE A CE1   1 
ATOM   15529 C CE2   . PHE A 1 3543 ? 145.254 117.259 153.917 1.00 44.27  ? 3543 PHE A CE2   1 
ATOM   15530 C CZ    . PHE A 1 3543 ? 144.520 116.922 155.034 1.00 44.27  ? 3543 PHE A CZ    1 
ATOM   15531 N N     . ARG A 1 3544 ? 143.965 115.371 149.509 1.00 50.34  ? 3544 ARG A N     1 
ATOM   15532 C CA    . ARG A 1 3544 ? 145.012 114.373 149.341 1.00 50.34  ? 3544 ARG A CA    1 
ATOM   15533 C C     . ARG A 1 3544 ? 146.023 114.476 150.475 1.00 50.34  ? 3544 ARG A C     1 
ATOM   15534 O O     . ARG A 1 3544 ? 146.606 115.540 150.706 1.00 50.34  ? 3544 ARG A O     1 
ATOM   15535 C CB    . ARG A 1 3544 ? 145.698 114.552 147.989 1.00 50.34  ? 3544 ARG A CB    1 
ATOM   15536 C CG    . ARG A 1 3544 ? 146.991 113.773 147.839 1.00 50.34  ? 3544 ARG A CG    1 
ATOM   15537 C CD    . ARG A 1 3544 ? 147.232 113.351 146.392 1.00 50.34  ? 3544 ARG A CD    1 
ATOM   15538 N NE    . ARG A 1 3544 ? 146.943 114.413 145.434 1.00 50.34  ? 3544 ARG A NE    1 
ATOM   15539 C CZ    . ARG A 1 3544 ? 145.863 114.462 144.664 1.00 50.34  ? 3544 ARG A CZ    1 
ATOM   15540 N NH1   . ARG A 1 3544 ? 144.933 113.523 144.717 1.00 50.34  ? 3544 ARG A NH1   1 
ATOM   15541 N NH2   . ARG A 1 3544 ? 145.713 115.480 143.823 1.00 50.34  ? 3544 ARG A NH2   1 
ATOM   15542 N N     . THR A 1 3545 ? 146.221 113.367 151.182 1.00 54.09  ? 3545 THR A N     1 
ATOM   15543 C CA    . THR A 1 3545 ? 147.094 113.354 152.348 1.00 54.09  ? 3545 THR A CA    1 
ATOM   15544 C C     . THR A 1 3545 ? 148.537 113.632 151.936 1.00 54.09  ? 3545 THR A C     1 
ATOM   15545 O O     . THR A 1 3545 ? 148.975 113.257 150.846 1.00 54.09  ? 3545 THR A O     1 
ATOM   15546 C CB    . THR A 1 3545 ? 146.986 112.004 153.065 1.00 54.09  ? 3545 THR A CB    1 
ATOM   15547 O OG1   . THR A 1 3545 ? 145.623 111.778 153.445 1.00 54.09  ? 3545 THR A OG1   1 
ATOM   15548 C CG2   . THR A 1 3545 ? 147.852 111.973 154.316 1.00 54.09  ? 3545 THR A CG2   1 
ATOM   15549 N N     . ASP A 1 3546 ? 149.259 114.320 152.823 1.00 59.72  ? 3546 ASP A N     1 
ATOM   15550 C CA    . ASP A 1 3546 ? 150.667 114.700 152.654 1.00 59.72  ? 3546 ASP A CA    1 
ATOM   15551 C C     . ASP A 1 3546 ? 150.956 115.219 151.246 1.00 59.72  ? 3546 ASP A C     1 
ATOM   15552 O O     . ASP A 1 3546 ? 151.926 114.833 150.590 1.00 59.72  ? 3546 ASP A O     1 
ATOM   15553 C CB    . ASP A 1 3546 ? 151.610 113.551 153.045 1.00 59.72  ? 3546 ASP A CB    1 
ATOM   15554 C CG    . ASP A 1 3546 ? 151.341 112.256 152.292 1.00 59.72  ? 3546 ASP A CG    1 
ATOM   15555 O OD1   . ASP A 1 3546 ? 151.393 112.244 151.044 1.00 59.72  ? 3546 ASP A OD1   1 
ATOM   15556 O OD2   . ASP A 1 3546 ? 151.067 111.239 152.962 1.00 59.72  ? 3546 ASP A OD2   1 
ATOM   15557 N N     . ILE A 1 3547 ? 150.103 116.130 150.792 1.00 49.45  ? 3547 ILE A N     1 
ATOM   15558 C CA    . ILE A 1 3547 ? 150.305 116.789 149.507 1.00 49.45  ? 3547 ILE A CA    1 
ATOM   15559 C C     . ILE A 1 3547 ? 151.504 117.723 149.601 1.00 49.45  ? 3547 ILE A C     1 
ATOM   15560 O O     . ILE A 1 3547 ? 151.751 118.343 150.644 1.00 49.45  ? 3547 ILE A O     1 
ATOM   15561 C CB    . ILE A 1 3547 ? 149.035 117.542 149.073 1.00 49.45  ? 3547 ILE A CB    1 
ATOM   15562 C CG1   . ILE A 1 3547 ? 149.089 117.856 147.578 1.00 49.45  ? 3547 ILE A CG1   1 
ATOM   15563 C CG2   . ILE A 1 3547 ? 148.841 118.814 149.880 1.00 49.45  ? 3547 ILE A CG2   1 
ATOM   15564 C CD1   . ILE A 1 3547 ? 148.854 116.672 146.694 1.00 49.45  ? 3547 ILE A CD1   1 
ATOM   15565 N N     . ALA A 1 3548 ? 152.278 117.793 148.522 1.00 45.86  ? 3548 ALA A N     1 
ATOM   15566 C CA    . ALA A 1 3548 ? 153.374 118.744 148.410 1.00 45.86  ? 3548 ALA A CA    1 
ATOM   15567 C C     . ALA A 1 3548 ? 152.993 119.803 147.383 1.00 45.86  ? 3548 ALA A C     1 
ATOM   15568 O O     . ALA A 1 3548 ? 152.639 119.474 146.246 1.00 45.86  ? 3548 ALA A O     1 
ATOM   15569 C CB    . ALA A 1 3548 ? 154.672 118.042 148.016 1.00 45.86  ? 3548 ALA A CB    1 
ATOM   15570 N N     . ARG A 1 3549 ? 153.065 121.071 147.787 1.00 39.86  ? 3549 ARG A N     1 
ATOM   15571 C CA    . ARG A 1 3549 ? 152.595 122.168 146.952 1.00 39.86  ? 3549 ARG A CA    1 
ATOM   15572 C C     . ARG A 1 3549 ? 153.577 122.548 145.853 1.00 39.86  ? 3549 ARG A C     1 
ATOM   15573 O O     . ARG A 1 3549 ? 153.198 123.294 144.944 1.00 39.86  ? 3549 ARG A O     1 
ATOM   15574 C CB    . ARG A 1 3549 ? 152.305 123.386 147.827 1.00 39.86  ? 3549 ARG A CB    1 
ATOM   15575 C CG    . ARG A 1 3549 ? 153.246 123.509 149.012 1.00 39.86  ? 3549 ARG A CG    1 
ATOM   15576 C CD    . ARG A 1 3549 ? 152.774 124.557 150.002 1.00 39.86  ? 3549 ARG A CD    1 
ATOM   15577 N NE    . ARG A 1 3549 ? 153.682 124.689 151.135 1.00 39.86  ? 3549 ARG A NE    1 
ATOM   15578 C CZ    . ARG A 1 3549 ? 153.852 123.772 152.078 1.00 39.86  ? 3549 ARG A CZ    1 
ATOM   15579 N NH1   . ARG A 1 3549 ? 153.176 122.634 152.069 1.00 39.86  ? 3549 ARG A NH1   1 
ATOM   15580 N NH2   . ARG A 1 3549 ? 154.718 124.004 153.060 1.00 39.86  ? 3549 ARG A NH2   1 
ATOM   15581 N N     . THR A 1 3550 ? 154.820 122.067 145.914 1.00 45.08  ? 3550 THR A N     1 
ATOM   15582 C CA    . THR A 1 3550 ? 155.817 122.455 144.920 1.00 45.08  ? 3550 THR A CA    1 
ATOM   15583 C C     . THR A 1 3550 ? 155.425 121.984 143.524 1.00 45.08  ? 3550 THR A C     1 
ATOM   15584 O O     . THR A 1 3550 ? 155.551 122.732 142.548 1.00 45.08  ? 3550 THR A O     1 
ATOM   15585 C CB    . THR A 1 3550 ? 157.187 121.900 145.307 1.00 45.08  ? 3550 THR A CB    1 
ATOM   15586 O OG1   . THR A 1 3550 ? 157.131 120.468 145.342 1.00 45.08  ? 3550 THR A OG1   1 
ATOM   15587 C CG2   . THR A 1 3550 ? 157.597 122.414 146.672 1.00 45.08  ? 3550 THR A CG2   1 
ATOM   15588 N N     . GLU A 1 3551 ? 154.949 120.745 143.407 1.00 50.86  ? 3551 GLU A N     1 
ATOM   15589 C CA    . GLU A 1 3551 ? 154.624 120.179 142.105 1.00 50.86  ? 3551 GLU A CA    1 
ATOM   15590 C C     . GLU A 1 3551 ? 153.128 120.096 141.832 1.00 50.86  ? 3551 GLU A C     1 
ATOM   15591 O O     . GLU A 1 3551 ? 152.740 119.786 140.700 1.00 50.86  ? 3551 GLU A O     1 
ATOM   15592 C CB    . GLU A 1 3551 ? 155.256 118.786 141.952 1.00 50.86  ? 3551 GLU A CB    1 
ATOM   15593 C CG    . GLU A 1 3551 ? 154.656 117.650 142.784 1.00 50.86  ? 3551 GLU A CG    1 
ATOM   15594 C CD    . GLU A 1 3551 ? 154.603 117.920 144.281 1.00 50.86  ? 3551 GLU A CD    1 
ATOM   15595 O OE1   . GLU A 1 3551 ? 155.202 118.908 144.757 1.00 50.86  ? 3551 GLU A OE1   1 
ATOM   15596 O OE2   . GLU A 1 3551 ? 153.963 117.123 144.993 1.00 50.86  ? 3551 GLU A OE2   1 
ATOM   15597 N N     . TYR A 1 3552 ? 152.281 120.356 142.829 1.00 41.99  ? 3552 TYR A N     1 
ATOM   15598 C CA    . TYR A 1 3552 ? 150.849 120.430 142.561 1.00 41.99  ? 3552 TYR A CA    1 
ATOM   15599 C C     . TYR A 1 3552 ? 150.511 121.630 141.686 1.00 41.99  ? 3552 TYR A C     1 
ATOM   15600 O O     . TYR A 1 3552 ? 149.659 121.538 140.795 1.00 41.99  ? 3552 TYR A O     1 
ATOM   15601 C CB    . TYR A 1 3552 ? 150.061 120.483 143.870 1.00 41.99  ? 3552 TYR A CB    1 
ATOM   15602 C CG    . TYR A 1 3552 ? 148.573 120.303 143.672 1.00 41.99  ? 3552 TYR A CG    1 
ATOM   15603 C CD1   . TYR A 1 3552 ? 147.677 121.285 144.069 1.00 41.99  ? 3552 TYR A CD1   1 
ATOM   15604 C CD2   . TYR A 1 3552 ? 148.067 119.162 143.065 1.00 41.99  ? 3552 TYR A CD2   1 
ATOM   15605 C CE1   . TYR A 1 3552 ? 146.317 121.129 143.881 1.00 41.99  ? 3552 TYR A CE1   1 
ATOM   15606 C CE2   . TYR A 1 3552 ? 146.708 118.999 142.870 1.00 41.99  ? 3552 TYR A CE2   1 
ATOM   15607 C CZ    . TYR A 1 3552 ? 145.838 119.986 143.281 1.00 41.99  ? 3552 TYR A CZ    1 
ATOM   15608 O OH    . TYR A 1 3552 ? 144.485 119.832 143.093 1.00 41.99  ? 3552 TYR A OH    1 
ATOM   15609 N N     . LEU A 1 3553 ? 151.167 122.762 141.923 1.00 38.95  ? 3553 LEU A N     1 
ATOM   15610 C CA    . LEU A 1 3553 ? 150.880 123.994 141.202 1.00 38.95  ? 3553 LEU A CA    1 
ATOM   15611 C C     . LEU A 1 3553 ? 151.810 124.236 140.020 1.00 38.95  ? 3553 LEU A C     1 
ATOM   15612 O O     . LEU A 1 3553 ? 151.594 125.193 139.270 1.00 38.95  ? 3553 LEU A O     1 
ATOM   15613 C CB    . LEU A 1 3553 ? 150.948 125.182 142.164 1.00 38.95  ? 3553 LEU A CB    1 
ATOM   15614 C CG    . LEU A 1 3553 ? 150.101 125.006 143.423 1.00 38.95  ? 3553 LEU A CG    1 
ATOM   15615 C CD1   . LEU A 1 3553 ? 150.602 125.893 144.545 1.00 38.95  ? 3553 LEU A CD1   1 
ATOM   15616 C CD2   . LEU A 1 3553 ? 148.647 125.306 143.112 1.00 38.95  ? 3553 LEU A CD2   1 
ATOM   15617 N N     . SER A 1 3554 ? 152.830 123.402 139.832 1.00 47.38  ? 3554 SER A N     1 
ATOM   15618 C CA    . SER A 1 3554 ? 153.752 123.569 138.711 1.00 47.38  ? 3554 SER A CA    1 
ATOM   15619 C C     . SER A 1 3554 ? 154.493 122.261 138.498 1.00 47.38  ? 3554 SER A C     1 
ATOM   15620 O O     . SER A 1 3554 ? 155.207 121.806 139.397 1.00 47.38  ? 3554 SER A O     1 
ATOM   15621 C CB    . SER A 1 3554 ? 154.733 124.710 138.977 1.00 47.38  ? 3554 SER A CB    1 
ATOM   15622 O OG    . SER A 1 3554 ? 155.695 124.336 139.946 1.00 47.38  ? 3554 SER A OG    1 
ATOM   15623 N N     . ASN A 1 3555 ? 154.339 121.664 137.319 1.00 57.08  ? 3555 ASN A N     1 
ATOM   15624 C CA    . ASN A 1 3555 ? 155.018 120.411 137.030 1.00 57.08  ? 3555 ASN A CA    1 
ATOM   15625 C C     . ASN A 1 3555 ? 156.473 120.674 136.639 1.00 57.08  ? 3555 ASN A C     1 
ATOM   15626 O O     . ASN A 1 3555 ? 157.010 121.769 136.825 1.00 57.08  ? 3555 ASN A O     1 
ATOM   15627 C CB    . ASN A 1 3555 ? 154.261 119.624 135.959 1.00 57.08  ? 3555 ASN A CB    1 
ATOM   15628 C CG    . ASN A 1 3555 ? 154.136 120.374 134.652 1.00 57.08  ? 3555 ASN A CG    1 
ATOM   15629 O OD1   . ASN A 1 3555 ? 154.457 121.554 134.569 1.00 57.08  ? 3555 ASN A OD1   1 
ATOM   15630 N ND2   . ASN A 1 3555 ? 153.661 119.687 133.620 1.00 57.08  ? 3555 ASN A ND2   1 
ATOM   15631 N N     . ALA A 1 3556 ? 157.121 119.641 136.092 1.00 58.82  ? 3556 ALA A N     1 
ATOM   15632 C CA    . ALA A 1 3556 ? 158.579 119.628 135.995 1.00 58.82  ? 3556 ALA A CA    1 
ATOM   15633 C C     . ALA A 1 3556 ? 159.115 120.743 135.103 1.00 58.82  ? 3556 ALA A C     1 
ATOM   15634 O O     . ALA A 1 3556 ? 160.140 121.356 135.427 1.00 58.82  ? 3556 ALA A O     1 
ATOM   15635 C CB    . ALA A 1 3556 ? 159.054 118.268 135.485 1.00 58.82  ? 3556 ALA A CB    1 
ATOM   15636 N N     . ASP A 1 3557 ? 158.455 121.011 133.973 1.00 62.24  ? 3557 ASP A N     1 
ATOM   15637 C CA    . ASP A 1 3557 ? 159.045 121.899 132.974 1.00 62.24  ? 3557 ASP A CA    1 
ATOM   15638 C C     . ASP A 1 3557 ? 159.246 123.312 133.513 1.00 62.24  ? 3557 ASP A C     1 
ATOM   15639 O O     . ASP A 1 3557 ? 160.296 123.923 133.276 1.00 62.24  ? 3557 ASP A O     1 
ATOM   15640 C CB    . ASP A 1 3557 ? 158.194 121.906 131.702 1.00 62.24  ? 3557 ASP A CB    1 
ATOM   15641 C CG    . ASP A 1 3557 ? 156.782 122.396 131.939 1.00 62.24  ? 3557 ASP A CG    1 
ATOM   15642 O OD1   . ASP A 1 3557 ? 156.441 122.701 133.098 1.00 62.24  ? 3557 ASP A OD1   1 
ATOM   15643 O OD2   . ASP A 1 3557 ? 156.010 122.476 130.961 1.00 62.24  ? 3557 ASP A OD2   1 
ATOM   15644 N N     . GLU A 1 3558 ? 158.265 123.851 134.245 1.00 60.21  ? 3558 GLU A N     1 
ATOM   15645 C CA    . GLU A 1 3558 ? 158.446 125.183 134.817 1.00 60.21  ? 3558 GLU A CA    1 
ATOM   15646 C C     . GLU A 1 3558 ? 159.566 125.194 135.848 1.00 60.21  ? 3558 GLU A C     1 
ATOM   15647 O O     . GLU A 1 3558 ? 160.316 126.170 135.943 1.00 60.21  ? 3558 GLU A O     1 
ATOM   15648 C CB    . GLU A 1 3558 ? 157.150 125.703 135.444 1.00 60.21  ? 3558 GLU A CB    1 
ATOM   15649 C CG    . GLU A 1 3558 ? 156.062 126.081 134.452 1.00 60.21  ? 3558 GLU A CG    1 
ATOM   15650 C CD    . GLU A 1 3558 ? 154.999 125.017 134.326 1.00 60.21  ? 3558 GLU A CD    1 
ATOM   15651 O OE1   . GLU A 1 3558 ? 155.024 124.070 135.135 1.00 60.21  ? 3558 GLU A OE1   1 
ATOM   15652 O OE2   . GLU A 1 3558 ? 154.143 125.126 133.424 1.00 60.21  ? 3558 GLU A OE2   1 
ATOM   15653 N N     . ARG A 1 3559 ? 159.689 124.126 136.640 1.00 56.43  ? 3559 ARG A N     1 
ATOM   15654 C CA    . ARG A 1 3559 ? 160.762 124.072 137.628 1.00 56.43  ? 3559 ARG A CA    1 
ATOM   15655 C C     . ARG A 1 3559 ? 162.130 124.069 136.958 1.00 56.43  ? 3559 ARG A C     1 
ATOM   15656 O O     . ARG A 1 3559 ? 163.041 124.787 137.386 1.00 56.43  ? 3559 ARG A O     1 
ATOM   15657 C CB    . ARG A 1 3559 ? 160.599 122.842 138.519 1.00 56.43  ? 3559 ARG A CB    1 
ATOM   15658 C CG    . ARG A 1 3559 ? 159.459 122.947 139.512 1.00 56.43  ? 3559 ARG A CG    1 
ATOM   15659 C CD    . ARG A 1 3559 ? 159.280 121.647 140.270 1.00 56.43  ? 3559 ARG A CD    1 
ATOM   15660 N NE    . ARG A 1 3559 ? 158.181 120.858 139.729 1.00 56.43  ? 3559 ARG A NE    1 
ATOM   15661 C CZ    . ARG A 1 3559 ? 158.061 119.546 139.872 1.00 56.43  ? 3559 ARG A CZ    1 
ATOM   15662 N NH1   . ARG A 1 3559 ? 158.937 118.843 140.570 1.00 56.43  ? 3559 ARG A NH1   1 
ATOM   15663 N NH2   . ARG A 1 3559 ? 157.037 118.923 139.296 1.00 56.43  ? 3559 ARG A NH2   1 
ATOM   15664 N N     . LEU A 1 3560 ? 162.292 123.269 135.901 1.00 58.12  ? 3560 LEU A N     1 
ATOM   15665 C CA    . LEU A 1 3560 ? 163.559 123.262 135.173 1.00 58.12  ? 3560 LEU A CA    1 
ATOM   15666 C C     . LEU A 1 3560 ? 163.830 124.612 134.520 1.00 58.12  ? 3560 LEU A C     1 
ATOM   15667 O O     . LEU A 1 3560 ? 164.975 125.081 134.501 1.00 58.12  ? 3560 LEU A O     1 
ATOM   15668 C CB    . LEU A 1 3560 ? 163.573 122.145 134.127 1.00 58.12  ? 3560 LEU A CB    1 
ATOM   15669 C CG    . LEU A 1 3560 ? 163.948 120.723 134.565 1.00 58.12  ? 3560 LEU A CG    1 
ATOM   15670 C CD1   . LEU A 1 3560 ? 165.388 120.690 135.055 1.00 58.12  ? 3560 LEU A CD1   1 
ATOM   15671 C CD2   . LEU A 1 3560 ? 163.015 120.160 135.625 1.00 58.12  ? 3560 LEU A CD2   1 
ATOM   15672 N N     . ARG A 1 3561 ? 162.792 125.252 133.976 1.00 58.64  ? 3561 ARG A N     1 
ATOM   15673 C CA    . ARG A 1 3561 ? 162.975 126.566 133.369 1.00 58.64  ? 3561 ARG A CA    1 
ATOM   15674 C C     . ARG A 1 3561 ? 163.401 127.598 134.407 1.00 58.64  ? 3561 ARG A C     1 
ATOM   15675 O O     . ARG A 1 3561 ? 164.261 128.445 134.136 1.00 58.64  ? 3561 ARG A O     1 
ATOM   15676 C CB    . ARG A 1 3561 ? 161.686 126.997 132.669 1.00 58.64  ? 3561 ARG A CB    1 
ATOM   15677 C CG    . ARG A 1 3561 ? 161.895 127.939 131.496 1.00 58.64  ? 3561 ARG A CG    1 
ATOM   15678 C CD    . ARG A 1 3561 ? 161.766 129.393 131.919 1.00 58.64  ? 3561 ARG A CD    1 
ATOM   15679 N NE    . ARG A 1 3561 ? 160.412 129.724 132.350 1.00 58.64  ? 3561 ARG A NE    1 
ATOM   15680 C CZ    . ARG A 1 3561 ? 159.360 129.803 131.546 1.00 58.64  ? 3561 ARG A CZ    1 
ATOM   15681 N NH1   . ARG A 1 3561 ? 159.466 129.595 130.244 1.00 58.64  ? 3561 ARG A NH1   1 
ATOM   15682 N NH2   . ARG A 1 3561 ? 158.172 130.104 132.062 1.00 58.64  ? 3561 ARG A NH2   1 
ATOM   15683 N N     . TRP A 1 3562 ? 162.806 127.545 135.601 1.00 53.09  ? 3562 TRP A N     1 
ATOM   15684 C CA    . TRP A 1 3562 ? 163.205 128.446 136.677 1.00 53.09  ? 3562 TRP A CA    1 
ATOM   15685 C C     . TRP A 1 3562 ? 164.640 128.183 137.112 1.00 53.09  ? 3562 TRP A C     1 
ATOM   15686 O O     . TRP A 1 3562 ? 165.401 129.123 137.370 1.00 53.09  ? 3562 TRP A O     1 
ATOM   15687 C CB    . TRP A 1 3562 ? 162.255 128.301 137.865 1.00 53.09  ? 3562 TRP A CB    1 
ATOM   15688 C CG    . TRP A 1 3562 ? 160.840 128.684 137.566 1.00 53.09  ? 3562 TRP A CG    1 
ATOM   15689 C CD1   . TRP A 1 3562 ? 160.408 129.529 136.588 1.00 53.09  ? 3562 TRP A CD1   1 
ATOM   15690 C CD2   . TRP A 1 3562 ? 159.668 128.228 138.251 1.00 53.09  ? 3562 TRP A CD2   1 
ATOM   15691 N NE1   . TRP A 1 3562 ? 159.038 129.631 136.624 1.00 53.09  ? 3562 TRP A NE1   1 
ATOM   15692 C CE2   . TRP A 1 3562 ? 158.560 128.841 137.635 1.00 53.09  ? 3562 TRP A CE2   1 
ATOM   15693 C CE3   . TRP A 1 3562 ? 159.449 127.361 139.325 1.00 53.09  ? 3562 TRP A CE3   1 
ATOM   15694 C CZ2   . TRP A 1 3562 ? 157.253 128.615 138.058 1.00 53.09  ? 3562 TRP A CZ2   1 
ATOM   15695 C CZ3   . TRP A 1 3562 ? 158.151 127.138 139.743 1.00 53.09  ? 3562 TRP A CZ3   1 
ATOM   15696 C CH2   . TRP A 1 3562 ? 157.070 127.762 139.111 1.00 53.09  ? 3562 TRP A CH2   1 
ATOM   15697 N N     . GLN A 1 3563 ? 165.026 126.908 137.210 1.00 55.24  ? 3563 GLN A N     1 
ATOM   15698 C CA    . GLN A 1 3563 ? 166.405 126.581 137.559 1.00 55.24  ? 3563 GLN A CA    1 
ATOM   15699 C C     . GLN A 1 3563 ? 167.373 127.126 136.518 1.00 55.24  ? 3563 GLN A C     1 
ATOM   15700 O O     . GLN A 1 3563 ? 168.437 127.654 136.863 1.00 55.24  ? 3563 GLN A O     1 
ATOM   15701 C CB    . GLN A 1 3563 ? 166.570 125.068 137.708 1.00 55.24  ? 3563 GLN A CB    1 
ATOM   15702 C CG    . GLN A 1 3563 ? 165.807 124.468 138.876 1.00 55.24  ? 3563 GLN A CG    1 
ATOM   15703 C CD    . GLN A 1 3563 ? 166.498 124.699 140.205 1.00 55.24  ? 3563 GLN A CD    1 
ATOM   15704 O OE1   . GLN A 1 3563 ? 167.633 125.173 140.255 1.00 55.24  ? 3563 GLN A OE1   1 
ATOM   15705 N NE2   . GLN A 1 3563 ? 165.814 124.364 141.293 1.00 55.24  ? 3563 GLN A NE2   1 
ATOM   15706 N N     . ALA A 1 3564 ? 167.020 127.010 135.237 1.00 54.24  ? 3564 ALA A N     1 
ATOM   15707 C CA    . ALA A 1 3564 ? 167.810 127.626 134.179 1.00 54.24  ? 3564 ALA A CA    1 
ATOM   15708 C C     . ALA A 1 3564 ? 167.712 129.146 134.185 1.00 54.24  ? 3564 ALA A C     1 
ATOM   15709 O O     . ALA A 1 3564 ? 168.498 129.802 133.494 1.00 54.24  ? 3564 ALA A O     1 
ATOM   15710 C CB    . ALA A 1 3564 ? 167.377 127.086 132.816 1.00 54.24  ? 3564 ALA A CB    1 
ATOM   15711 N N     . SER A 1 3565 ? 166.770 129.716 134.941 1.00 53.21  ? 3565 SER A N     1 
ATOM   15712 C CA    . SER A 1 3565 ? 166.600 131.160 135.042 1.00 53.21  ? 3565 SER A CA    1 
ATOM   15713 C C     . SER A 1 3565 ? 167.282 131.747 136.272 1.00 53.21  ? 3565 SER A C     1 
ATOM   15714 O O     . SER A 1 3565 ? 166.865 132.806 136.760 1.00 53.21  ? 3565 SER A O     1 
ATOM   15715 C CB    . SER A 1 3565 ? 165.112 131.513 135.040 1.00 53.21  ? 3565 SER A CB    1 
ATOM   15716 O OG    . SER A 1 3565 ? 164.909 132.870 134.691 1.00 53.21  ? 3565 SER A OG    1 
ATOM   15717 N N     . SER A 1 3566 ? 168.318 131.080 136.785 1.00 51.36  ? 3566 SER A N     1 
ATOM   15718 C CA    . SER A 1 3566 ? 169.085 131.543 137.943 1.00 51.36  ? 3566 SER A CA    1 
ATOM   15719 C C     . SER A 1 3566 ? 168.188 131.714 139.171 1.00 51.36  ? 3566 SER A C     1 
ATOM   15720 O O     . SER A 1 3566 ? 168.023 132.809 139.712 1.00 51.36  ? 3566 SER A O     1 
ATOM   15721 C CB    . SER A 1 3566 ? 169.838 132.839 137.620 1.00 51.36  ? 3566 SER A CB    1 
ATOM   15722 O OG    . SER A 1 3566 ? 168.961 133.951 137.620 1.00 51.36  ? 3566 SER A OG    1 
ATOM   15723 N N     . LEU A 1 3567 ? 167.606 130.598 139.603 1.00 45.04  ? 3567 LEU A N     1 
ATOM   15724 C CA    . LEU A 1 3567 ? 166.778 130.555 140.794 1.00 45.04  ? 3567 LEU A CA    1 
ATOM   15725 C C     . LEU A 1 3567 ? 167.326 129.511 141.759 1.00 45.04  ? 3567 LEU A C     1 
ATOM   15726 O O     . LEU A 1 3567 ? 167.684 128.406 141.328 1.00 45.04  ? 3567 LEU A O     1 
ATOM   15727 C CB    . LEU A 1 3567 ? 165.318 130.227 140.441 1.00 45.04  ? 3567 LEU A CB    1 
ATOM   15728 C CG    . LEU A 1 3567 ? 164.339 130.130 141.613 1.00 45.04  ? 3567 LEU A CG    1 
ATOM   15729 C CD1   . LEU A 1 3567 ? 163.894 131.514 142.058 1.00 45.04  ? 3567 LEU A CD1   1 
ATOM   15730 C CD2   . LEU A 1 3567 ? 163.141 129.271 141.248 1.00 45.04  ? 3567 LEU A CD2   1 
ATOM   15731 N N     . PRO A 1 3568 ? 167.416 129.816 143.053 1.00 41.75  ? 3568 PRO A N     1 
ATOM   15732 C CA    . PRO A 1 3568 ? 167.944 128.832 144.004 1.00 41.75  ? 3568 PRO A CA    1 
ATOM   15733 C C     . PRO A 1 3568 ? 167.055 127.601 144.092 1.00 41.75  ? 3568 PRO A C     1 
ATOM   15734 O O     . PRO A 1 3568 ? 165.850 127.655 143.840 1.00 41.75  ? 3568 PRO A O     1 
ATOM   15735 C CB    . PRO A 1 3568 ? 167.969 129.599 145.332 1.00 41.75  ? 3568 PRO A CB    1 
ATOM   15736 C CG    . PRO A 1 3568 ? 167.995 131.039 144.940 1.00 41.75  ? 3568 PRO A CG    1 
ATOM   15737 C CD    . PRO A 1 3568 ? 167.187 131.127 143.682 1.00 41.75  ? 3568 PRO A CD    1 
ATOM   15738 N N     . ALA A 1 3569 ? 167.674 126.477 144.451 1.00 44.83  ? 3569 ALA A N     1 
ATOM   15739 C CA    . ALA A 1 3569 ? 166.969 125.209 144.583 1.00 44.83  ? 3569 ALA A CA    1 
ATOM   15740 C C     . ALA A 1 3569 ? 166.272 125.053 145.928 1.00 44.83  ? 3569 ALA A C     1 
ATOM   15741 O O     . ALA A 1 3569 ? 165.749 123.969 146.211 1.00 44.83  ? 3569 ALA A O     1 
ATOM   15742 C CB    . ALA A 1 3569 ? 167.938 124.044 144.368 1.00 44.83  ? 3569 ALA A CB    1 
ATOM   15743 N N     . ASP A 1 3570 ? 166.262 126.093 146.760 1.00 40.94  ? 3570 ASP A N     1 
ATOM   15744 C CA    . ASP A 1 3570 ? 165.591 126.025 148.051 1.00 40.94  ? 3570 ASP A CA    1 
ATOM   15745 C C     . ASP A 1 3570 ? 164.098 125.784 147.870 1.00 40.94  ? 3570 ASP A C     1 
ATOM   15746 O O     . ASP A 1 3570 ? 163.481 126.291 146.931 1.00 40.94  ? 3570 ASP A O     1 
ATOM   15747 C CB    . ASP A 1 3570 ? 165.820 127.321 148.831 1.00 40.94  ? 3570 ASP A CB    1 
ATOM   15748 C CG    . ASP A 1 3570 ? 165.494 127.185 150.306 1.00 40.94  ? 3570 ASP A CG    1 
ATOM   15749 O OD1   . ASP A 1 3570 ? 164.841 126.192 150.692 1.00 40.94  ? 3570 ASP A OD1   1 
ATOM   15750 O OD2   . ASP A 1 3570 ? 165.884 128.082 151.083 1.00 40.94  ? 3570 ASP A OD2   1 
ATOM   15751 N N     . ASP A 1 3571 ? 163.522 125.002 148.786 1.00 39.56  ? 3571 ASP A N     1 
ATOM   15752 C CA    . ASP A 1 3571 ? 162.082 124.764 148.761 1.00 39.56  ? 3571 ASP A CA    1 
ATOM   15753 C C     . ASP A 1 3571 ? 161.310 126.067 148.929 1.00 39.56  ? 3571 ASP A C     1 
ATOM   15754 O O     . ASP A 1 3571 ? 160.296 126.292 148.254 1.00 39.56  ? 3571 ASP A O     1 
ATOM   15755 C CB    . ASP A 1 3571 ? 161.703 123.764 149.854 1.00 39.56  ? 3571 ASP A CB    1 
ATOM   15756 C CG    . ASP A 1 3571 ? 160.220 123.453 149.875 1.00 39.56  ? 3571 ASP A CG    1 
ATOM   15757 O OD1   . ASP A 1 3571 ? 159.716 123.028 150.936 1.00 39.56  ? 3571 ASP A OD1   1 
ATOM   15758 O OD2   . ASP A 1 3571 ? 159.558 123.626 148.832 1.00 39.56  ? 3571 ASP A OD2   1 
ATOM   15759 N N     . LEU A 1 3572 ? 161.778 126.939 149.824 1.00 36.31  ? 3572 LEU A N     1 
ATOM   15760 C CA    . LEU A 1 3572 ? 161.157 128.248 149.981 1.00 36.31  ? 3572 LEU A CA    1 
ATOM   15761 C C     . LEU A 1 3572 ? 161.234 129.047 148.686 1.00 36.31  ? 3572 LEU A C     1 
ATOM   15762 O O     . LEU A 1 3572 ? 160.273 129.727 148.308 1.00 36.31  ? 3572 LEU A O     1 
ATOM   15763 C CB    . LEU A 1 3572 ? 161.827 129.010 151.123 1.00 36.31  ? 3572 LEU A CB    1 
ATOM   15764 C CG    . LEU A 1 3572 ? 161.185 130.332 151.540 1.00 36.31  ? 3572 LEU A CG    1 
ATOM   15765 C CD1   . LEU A 1 3572 ? 160.106 130.088 152.581 1.00 36.31  ? 3572 LEU A CD1   1 
ATOM   15766 C CD2   . LEU A 1 3572 ? 162.233 131.299 152.065 1.00 36.31  ? 3572 LEU A CD2   1 
ATOM   15767 N N     . CYS A 1 3573 ? 162.372 128.974 147.993 1.00 38.47  ? 3573 CYS A N     1 
ATOM   15768 C CA    . CYS A 1 3573 ? 162.512 129.686 146.727 1.00 38.47  ? 3573 CYS A CA    1 
ATOM   15769 C C     . CYS A 1 3573 ? 161.564 129.133 145.670 1.00 38.47  ? 3573 CYS A C     1 
ATOM   15770 O O     . CYS A 1 3573 ? 160.995 129.896 144.883 1.00 38.47  ? 3573 CYS A O     1 
ATOM   15771 C CB    . CYS A 1 3573 ? 163.960 129.621 146.246 1.00 38.47  ? 3573 CYS A CB    1 
ATOM   15772 S SG    . CYS A 1 3573 ? 165.114 130.561 147.271 1.00 38.47  ? 3573 CYS A SG    1 
ATOM   15773 N N     . THR A 1 3574 ? 161.383 127.810 145.628 1.00 36.50  ? 3574 THR A N     1 
ATOM   15774 C CA    . THR A 1 3574 ? 160.431 127.234 144.681 1.00 36.50  ? 3574 THR A CA    1 
ATOM   15775 C C     . THR A 1 3574 ? 159.003 127.661 145.000 1.00 36.50  ? 3574 THR A C     1 
ATOM   15776 O O     . THR A 1 3574 ? 158.220 127.960 144.091 1.00 36.50  ? 3574 THR A O     1 
ATOM   15777 C CB    . THR A 1 3574 ? 160.541 125.709 144.668 1.00 36.50  ? 3574 THR A CB    1 
ATOM   15778 O OG1   . THR A 1 3574 ? 160.134 125.183 145.937 1.00 36.50  ? 3574 THR A OG1   1 
ATOM   15779 C CG2   . THR A 1 3574 ? 161.964 125.273 144.358 1.00 36.50  ? 3574 THR A CG2   1 
ATOM   15780 N N     . GLU A 1 3575 ? 158.643 127.694 146.285 1.00 32.62  ? 3575 GLU A N     1 
ATOM   15781 C CA    . GLU A 1 3575 ? 157.311 128.158 146.664 1.00 32.62  ? 3575 GLU A CA    1 
ATOM   15782 C C     . GLU A 1 3575 ? 157.111 129.618 146.273 1.00 32.62  ? 3575 GLU A C     1 
ATOM   15783 O O     . GLU A 1 3575 ? 156.041 130.008 145.788 1.00 32.62  ? 3575 GLU A O     1 
ATOM   15784 C CB    . GLU A 1 3575 ? 157.096 127.965 148.164 1.00 32.62  ? 3575 GLU A CB    1 
ATOM   15785 C CG    . GLU A 1 3575 ? 156.981 126.513 148.592 1.00 32.62  ? 3575 GLU A CG    1 
ATOM   15786 C CD    . GLU A 1 3575 ? 156.845 126.359 150.093 1.00 32.62  ? 3575 GLU A CD    1 
ATOM   15787 O OE1   . GLU A 1 3575 ? 156.907 127.382 150.806 1.00 32.62  ? 3575 GLU A OE1   1 
ATOM   15788 O OE2   . GLU A 1 3575 ? 156.674 125.214 150.562 1.00 32.62  ? 3575 GLU A OE2   1 
ATOM   15789 N N     . ASN A 1 3576 ? 158.138 130.443 146.478 1.00 30.55  ? 3576 ASN A N     1 
ATOM   15790 C CA    . ASN A 1 3576 ? 158.053 131.847 146.092 1.00 30.55  ? 3576 ASN A CA    1 
ATOM   15791 C C     . ASN A 1 3576 ? 157.935 131.995 144.580 1.00 30.55  ? 3576 ASN A C     1 
ATOM   15792 O O     . ASN A 1 3576 ? 157.216 132.869 144.084 1.00 30.55  ? 3576 ASN A O     1 
ATOM   15793 C CB    . ASN A 1 3576 ? 159.267 132.605 146.624 1.00 30.55  ? 3576 ASN A CB    1 
ATOM   15794 C CG    . ASN A 1 3576 ? 159.297 132.664 148.136 1.00 30.55  ? 3576 ASN A CG    1 
ATOM   15795 O OD1   . ASN A 1 3576 ? 158.403 132.150 148.807 1.00 30.55  ? 3576 ASN A OD1   1 
ATOM   15796 N ND2   . ASN A 1 3576 ? 160.329 133.293 148.682 1.00 30.55  ? 3576 ASN A ND2   1 
ATOM   15797 N N     . ALA A 1 3577 ? 158.640 131.149 143.829 1.00 33.12  ? 3577 ALA A N     1 
ATOM   15798 C CA    . ALA A 1 3577 ? 158.520 131.171 142.375 1.00 33.12  ? 3577 ALA A CA    1 
ATOM   15799 C C     . ALA A 1 3577 ? 157.114 130.780 141.939 1.00 33.12  ? 3577 ALA A C     1 
ATOM   15800 O O     . ALA A 1 3577 ? 156.570 131.338 140.980 1.00 33.12  ? 3577 ALA A O     1 
ATOM   15801 C CB    . ALA A 1 3577 ? 159.559 130.240 141.749 1.00 33.12  ? 3577 ALA A CB    1 
ATOM   15802 N N     . ILE A 1 3578 ? 156.516 129.809 142.631 1.00 31.02  ? 3578 ILE A N     1 
ATOM   15803 C CA    . ILE A 1 3578 ? 155.134 129.429 142.343 1.00 31.02  ? 3578 ILE A CA    1 
ATOM   15804 C C     . ILE A 1 3578 ? 154.198 130.598 142.612 1.00 31.02  ? 3578 ILE A C     1 
ATOM   15805 O O     . ILE A 1 3578 ? 153.278 130.872 141.831 1.00 31.02  ? 3578 ILE A O     1 
ATOM   15806 C CB    . ILE A 1 3578 ? 154.739 128.189 143.164 1.00 31.02  ? 3578 ILE A CB    1 
ATOM   15807 C CG1   . ILE A 1 3578 ? 155.476 126.956 142.648 1.00 31.02  ? 3578 ILE A CG1   1 
ATOM   15808 C CG2   . ILE A 1 3578 ? 153.240 127.969 143.109 1.00 31.02  ? 3578 ILE A CG2   1 
ATOM   15809 C CD1   . ILE A 1 3578 ? 155.354 125.767 143.557 1.00 31.02  ? 3578 ILE A CD1   1 
ATOM   15810 N N     . MET A 1 3579 ? 154.417 131.305 143.723 1.00 29.98  ? 3579 MET A N     1 
ATOM   15811 C CA    . MET A 1 3579 ? 153.614 132.491 144.011 1.00 29.98  ? 3579 MET A CA    1 
ATOM   15812 C C     . MET A 1 3579 ? 153.777 133.542 142.920 1.00 29.98  ? 3579 MET A C     1 
ATOM   15813 O O     . MET A 1 3579 ? 152.802 134.182 142.511 1.00 29.98  ? 3579 MET A O     1 
ATOM   15814 C CB    . MET A 1 3579 ? 153.999 133.076 145.369 1.00 29.98  ? 3579 MET A CB    1 
ATOM   15815 C CG    . MET A 1 3579 ? 153.206 132.525 146.535 1.00 29.98  ? 3579 MET A CG    1 
ATOM   15816 S SD    . MET A 1 3579 ? 153.922 133.001 148.116 1.00 29.98  ? 3579 MET A SD    1 
ATOM   15817 C CE    . MET A 1 3579 ? 153.962 131.419 148.946 1.00 29.98  ? 3579 MET A CE    1 
ATOM   15818 N N     . LEU A 1 3580 ? 155.008 133.736 142.443 1.00 30.96  ? 3580 LEU A N     1 
ATOM   15819 C CA    . LEU A 1 3580 ? 155.255 134.690 141.367 1.00 30.96  ? 3580 LEU A CA    1 
ATOM   15820 C C     . LEU A 1 3580 ? 154.569 134.271 140.074 1.00 30.96  ? 3580 LEU A C     1 
ATOM   15821 O O     . LEU A 1 3580 ? 154.124 135.130 139.305 1.00 30.96  ? 3580 LEU A O     1 
ATOM   15822 C CB    . LEU A 1 3580 ? 156.758 134.843 141.136 1.00 30.96  ? 3580 LEU A CB    1 
ATOM   15823 C CG    . LEU A 1 3580 ? 157.570 135.531 142.234 1.00 30.96  ? 3580 LEU A CG    1 
ATOM   15824 C CD1   . LEU A 1 3580 ? 159.032 135.628 141.836 1.00 30.96  ? 3580 LEU A CD1   1 
ATOM   15825 C CD2   . LEU A 1 3580 ? 157.006 136.907 142.529 1.00 30.96  ? 3580 LEU A CD2   1 
ATOM   15826 N N     . LYS A 1 3581 ? 154.488 132.967 139.808 1.00 31.76  ? 3581 LYS A N     1 
ATOM   15827 C CA    . LYS A 1 3581 ? 153.850 132.502 138.581 1.00 31.76  ? 3581 LYS A CA    1 
ATOM   15828 C C     . LYS A 1 3581 ? 152.338 132.676 138.637 1.00 31.76  ? 3581 LYS A C     1 
ATOM   15829 O O     . LYS A 1 3581 ? 151.727 133.153 137.674 1.00 31.76  ? 3581 LYS A O     1 
ATOM   15830 C CB    . LYS A 1 3581 ? 154.211 131.039 138.325 1.00 31.76  ? 3581 LYS A CB    1 
ATOM   15831 C CG    . LYS A 1 3581 ? 153.461 130.411 137.164 1.00 31.76  ? 3581 LYS A CG    1 
ATOM   15832 C CD    . LYS A 1 3581 ? 153.553 128.896 137.203 1.00 31.76  ? 3581 LYS A CD    1 
ATOM   15833 C CE    . LYS A 1 3581 ? 152.934 128.277 135.962 1.00 31.76  ? 3581 LYS A CE    1 
ATOM   15834 N NZ    . LYS A 1 3581 ? 151.544 128.758 135.740 1.00 31.76  ? 3581 LYS A NZ    1 
ATOM   15835 N N     . ARG A 1 3582 ? 151.718 132.303 139.753 1.00 32.12  ? 3582 ARG A N     1 
ATOM   15836 C CA    . ARG A 1 3582 ? 150.266 132.360 139.917 1.00 32.12  ? 3582 ARG A CA    1 
ATOM   15837 C C     . ARG A 1 3582 ? 149.946 133.420 140.966 1.00 32.12  ? 3582 ARG A C     1 
ATOM   15838 O O     . ARG A 1 3582 ? 149.929 133.143 142.166 1.00 32.12  ? 3582 ARG A O     1 
ATOM   15839 C CB    . ARG A 1 3582 ? 149.706 130.999 140.314 1.00 32.12  ? 3582 ARG A CB    1 
ATOM   15840 C CG    . ARG A 1 3582 ? 150.567 129.825 139.892 1.00 32.12  ? 3582 ARG A CG    1 
ATOM   15841 C CD    . ARG A 1 3582 ? 150.073 128.535 140.518 1.00 32.12  ? 3582 ARG A CD    1 
ATOM   15842 N NE    . ARG A 1 3582 ? 148.910 128.005 139.819 1.00 32.12  ? 3582 ARG A NE    1 
ATOM   15843 C CZ    . ARG A 1 3582 ? 148.969 127.152 138.806 1.00 32.12  ? 3582 ARG A CZ    1 
ATOM   15844 N NH1   . ARG A 1 3582 ? 150.126 126.712 138.340 1.00 32.12  ? 3582 ARG A NH1   1 
ATOM   15845 N NH2   . ARG A 1 3582 ? 147.839 126.732 138.244 1.00 32.12  ? 3582 ARG A NH2   1 
ATOM   15846 N N     . PHE A 1 3583 ? 149.688 134.641 140.505 1.00 33.58  ? 3583 PHE A N     1 
ATOM   15847 C CA    . PHE A 1 3583 ? 149.336 135.741 141.387 1.00 33.58  ? 3583 PHE A CA    1 
ATOM   15848 C C     . PHE A 1 3583 ? 148.165 136.509 140.796 1.00 33.58  ? 3583 PHE A C     1 
ATOM   15849 O O     . PHE A 1 3583 ? 148.024 136.614 139.575 1.00 33.58  ? 3583 PHE A O     1 
ATOM   15850 C CB    . PHE A 1 3583 ? 150.519 136.693 141.612 1.00 33.58  ? 3583 PHE A CB    1 
ATOM   15851 C CG    . PHE A 1 3583 ? 150.893 137.495 140.397 1.00 33.58  ? 3583 PHE A CG    1 
ATOM   15852 C CD1   . PHE A 1 3583 ? 151.670 136.940 139.397 1.00 33.58  ? 3583 PHE A CD1   1 
ATOM   15853 C CD2   . PHE A 1 3583 ? 150.465 138.803 140.254 1.00 33.58  ? 3583 PHE A CD2   1 
ATOM   15854 C CE1   . PHE A 1 3583 ? 152.016 137.673 138.280 1.00 33.58  ? 3583 PHE A CE1   1 
ATOM   15855 C CE2   . PHE A 1 3583 ? 150.807 139.541 139.139 1.00 33.58  ? 3583 PHE A CE2   1 
ATOM   15856 C CZ    . PHE A 1 3583 ? 151.583 138.975 138.151 1.00 33.58  ? 3583 PHE A CZ    1 
ATOM   15857 N N     . ASN A 1 3584 ? 147.324 137.045 141.677 1.00 32.05  ? 3584 ASN A N     1 
ATOM   15858 C CA    . ASN A 1 3584 ? 146.259 137.955 141.279 1.00 32.05  ? 3584 ASN A CA    1 
ATOM   15859 C C     . ASN A 1 3584 ? 146.592 139.406 141.588 1.00 32.05  ? 3584 ASN A C     1 
ATOM   15860 O O     . ASN A 1 3584 ? 146.412 140.274 140.729 1.00 32.05  ? 3584 ASN A O     1 
ATOM   15861 C CB    . ASN A 1 3584 ? 144.945 137.572 141.965 1.00 32.05  ? 3584 ASN A CB    1 
ATOM   15862 C CG    . ASN A 1 3584 ? 144.114 136.614 141.138 1.00 32.05  ? 3584 ASN A CG    1 
ATOM   15863 O OD1   . ASN A 1 3584 ? 144.573 136.095 140.121 1.00 32.05  ? 3584 ASN A OD1   1 
ATOM   15864 N ND2   . ASN A 1 3584 ? 142.881 136.376 141.569 1.00 32.05  ? 3584 ASN A ND2   1 
ATOM   15865 N N     . ARG A 1 3585 ? 147.075 139.690 142.793 1.00 32.63  ? 3585 ARG A N     1 
ATOM   15866 C CA    . ARG A 1 3585 ? 147.622 140.995 143.127 1.00 32.63  ? 3585 ARG A CA    1 
ATOM   15867 C C     . ARG A 1 3585 ? 149.115 140.997 142.833 1.00 32.63  ? 3585 ARG A C     1 
ATOM   15868 O O     . ARG A 1 3585 ? 149.798 139.990 143.040 1.00 32.63  ? 3585 ARG A O     1 
ATOM   15869 C CB    . ARG A 1 3585 ? 147.370 141.350 144.593 1.00 32.63  ? 3585 ARG A CB    1 
ATOM   15870 C CG    . ARG A 1 3585 ? 145.905 141.557 144.937 1.00 32.63  ? 3585 ARG A CG    1 
ATOM   15871 C CD    . ARG A 1 3585 ? 145.658 141.431 146.431 1.00 32.63  ? 3585 ARG A CD    1 
ATOM   15872 N NE    . ARG A 1 3585 ? 146.028 140.120 146.949 1.00 32.63  ? 3585 ARG A NE    1 
ATOM   15873 C CZ    . ARG A 1 3585 ? 146.467 139.902 148.180 1.00 32.63  ? 3585 ARG A CZ    1 
ATOM   15874 N NH1   . ARG A 1 3585 ? 146.615 140.890 149.046 1.00 32.63  ? 3585 ARG A NH1   1 
ATOM   15875 N NH2   . ARG A 1 3585 ? 146.766 138.660 148.552 1.00 32.63  ? 3585 ARG A NH2   1 
ATOM   15876 N N     . TYR A 1 3586 ? 149.611 142.128 142.348 1.00 38.93  ? 3586 TYR A N     1 
ATOM   15877 C CA    . TYR A 1 3586 ? 150.984 142.201 141.870 1.00 38.93  ? 3586 TYR A CA    1 
ATOM   15878 C C     . TYR A 1 3586 ? 151.961 141.929 143.010 1.00 38.93  ? 3586 TYR A C     1 
ATOM   15879 O O     . TYR A 1 3586 ? 151.825 142.516 144.092 1.00 38.93  ? 3586 TYR A O     1 
ATOM   15880 C CB    . TYR A 1 3586 ? 151.246 143.571 141.251 1.00 38.93  ? 3586 TYR A CB    1 
ATOM   15881 C CG    . TYR A 1 3586 ? 150.402 143.836 140.025 1.00 38.93  ? 3586 TYR A CG    1 
ATOM   15882 C CD1   . TYR A 1 3586 ? 150.526 143.046 138.891 1.00 38.93  ? 3586 TYR A CD1   1 
ATOM   15883 C CD2   . TYR A 1 3586 ? 149.473 144.866 140.007 1.00 38.93  ? 3586 TYR A CD2   1 
ATOM   15884 C CE1   . TYR A 1 3586 ? 149.756 143.281 137.770 1.00 38.93  ? 3586 TYR A CE1   1 
ATOM   15885 C CE2   . TYR A 1 3586 ? 148.697 145.108 138.890 1.00 38.93  ? 3586 TYR A CE2   1 
ATOM   15886 C CZ    . TYR A 1 3586 ? 148.844 144.313 137.775 1.00 38.93  ? 3586 TYR A CZ    1 
ATOM   15887 O OH    . TYR A 1 3586 ? 148.073 144.549 136.660 1.00 38.93  ? 3586 TYR A OH    1 
ATOM   15888 N N     . PRO A 1 3587 ? 152.945 141.054 142.815 1.00 34.64  ? 3587 PRO A N     1 
ATOM   15889 C CA    . PRO A 1 3587 ? 153.806 140.646 143.928 1.00 34.64  ? 3587 PRO A CA    1 
ATOM   15890 C C     . PRO A 1 3587 ? 154.721 141.765 144.394 1.00 34.64  ? 3587 PRO A C     1 
ATOM   15891 O O     . PRO A 1 3587 ? 155.039 142.696 143.650 1.00 34.64  ? 3587 PRO A O     1 
ATOM   15892 C CB    . PRO A 1 3587 ? 154.618 139.483 143.342 1.00 34.64  ? 3587 PRO A CB    1 
ATOM   15893 C CG    . PRO A 1 3587 ? 153.900 139.090 142.082 1.00 34.64  ? 3587 PRO A CG    1 
ATOM   15894 C CD    . PRO A 1 3587 ? 153.289 140.349 141.573 1.00 34.64  ? 3587 PRO A CD    1 
ATOM   15895 N N     . LEU A 1 3588 ? 155.143 141.660 145.652 1.00 35.45  ? 3588 LEU A N     1 
ATOM   15896 C CA    . LEU A 1 3588 ? 156.116 142.568 146.249 1.00 35.45  ? 3588 LEU A CA    1 
ATOM   15897 C C     . LEU A 1 3588 ? 157.276 141.723 146.758 1.00 35.45  ? 3588 LEU A C     1 
ATOM   15898 O O     . LEU A 1 3588 ? 157.201 141.151 147.850 1.00 35.45  ? 3588 LEU A O     1 
ATOM   15899 C CB    . LEU A 1 3588 ? 155.482 143.391 147.372 1.00 35.45  ? 3588 LEU A CB    1 
ATOM   15900 C CG    . LEU A 1 3588 ? 156.241 144.605 147.918 1.00 35.45  ? 3588 LEU A CG    1 
ATOM   15901 C CD1   . LEU A 1 3588 ? 155.264 145.598 148.519 1.00 35.45  ? 3588 LEU A CD1   1 
ATOM   15902 C CD2   . LEU A 1 3588 ? 157.275 144.207 148.955 1.00 35.45  ? 3588 LEU A CD2   1 
ATOM   15903 N N     . ILE A 1 3589 ? 158.342 141.644 145.970 1.00 36.48  ? 3589 ILE A N     1 
ATOM   15904 C CA    . ILE A 1 3589 ? 159.480 140.792 146.298 1.00 36.48  ? 3589 ILE A CA    1 
ATOM   15905 C C     . ILE A 1 3589 ? 160.284 141.424 147.426 1.00 36.48  ? 3589 ILE A C     1 
ATOM   15906 O O     . ILE A 1 3589 ? 160.621 142.613 147.377 1.00 36.48  ? 3589 ILE A O     1 
ATOM   15907 C CB    . ILE A 1 3589 ? 160.359 140.548 145.060 1.00 36.48  ? 3589 ILE A CB    1 
ATOM   15908 C CG1   . ILE A 1 3589 ? 159.590 139.795 143.968 1.00 36.48  ? 3589 ILE A CG1   1 
ATOM   15909 C CG2   . ILE A 1 3589 ? 161.620 139.800 145.443 1.00 36.48  ? 3589 ILE A CG2   1 
ATOM   15910 C CD1   . ILE A 1 3589 ? 158.834 140.675 142.999 1.00 36.48  ? 3589 ILE A CD1   1 
ATOM   15911 N N     . ILE A 1 3590 ? 160.592 140.627 148.447 1.00 35.78  ? 3590 ILE A N     1 
ATOM   15912 C CA    . ILE A 1 3590 ? 161.444 141.037 149.559 1.00 35.78  ? 3590 ILE A CA    1 
ATOM   15913 C C     . ILE A 1 3590 ? 162.598 140.045 149.613 1.00 35.78  ? 3590 ILE A C     1 
ATOM   15914 O O     . ILE A 1 3590 ? 162.425 138.902 150.053 1.00 35.78  ? 3590 ILE A O     1 
ATOM   15915 C CB    . ILE A 1 3590 ? 160.687 141.079 150.891 1.00 35.78  ? 3590 ILE A CB    1 
ATOM   15916 C CG1   . ILE A 1 3590 ? 159.374 141.846 150.740 1.00 35.78  ? 3590 ILE A CG1   1 
ATOM   15917 C CG2   . ILE A 1 3590 ? 161.552 141.698 151.976 1.00 35.78  ? 3590 ILE A CG2   1 
ATOM   15918 C CD1   . ILE A 1 3590 ? 158.481 141.764 151.956 1.00 35.78  ? 3590 ILE A CD1   1 
ATOM   15919 N N     . ASP A 1 3591 ? 163.779 140.471 149.168 1.00 45.77  ? 3591 ASP A N     1 
ATOM   15920 C CA    . ASP A 1 3591 ? 164.947 139.598 149.106 1.00 45.77  ? 3591 ASP A CA    1 
ATOM   15921 C C     . ASP A 1 3591 ? 166.174 140.354 149.594 1.00 45.77  ? 3591 ASP A C     1 
ATOM   15922 O O     . ASP A 1 3591 ? 166.590 141.338 148.949 1.00 45.77  ? 3591 ASP A O     1 
ATOM   15923 C CB    . ASP A 1 3591 ? 165.163 139.078 147.683 1.00 45.77  ? 3591 ASP A CB    1 
ATOM   15924 C CG    . ASP A 1 3591 ? 165.012 140.163 146.638 1.00 45.77  ? 3591 ASP A CG    1 
ATOM   15925 O OD1   . ASP A 1 3591 ? 164.424 141.217 146.956 1.00 45.77  ? 3591 ASP A OD1   1 
ATOM   15926 O OD2   . ASP A 1 3591 ? 165.487 139.967 145.501 1.00 45.77  ? 3591 ASP A OD2   1 
ATOM   15927 N N     . PRO A 1 3592 ? 166.778 139.955 150.716 1.00 47.58  ? 3592 PRO A N     1 
ATOM   15928 C CA    . PRO A 1 3592 ? 168.063 140.558 151.104 1.00 47.58  ? 3592 PRO A CA    1 
ATOM   15929 C C     . PRO A 1 3592 ? 169.151 140.351 150.067 1.00 47.58  ? 3592 PRO A C     1 
ATOM   15930 O O     . PRO A 1 3592 ? 170.005 141.230 149.892 1.00 47.58  ? 3592 PRO A O     1 
ATOM   15931 C CB    . PRO A 1 3592 ? 168.398 139.856 152.429 1.00 47.58  ? 3592 PRO A CB    1 
ATOM   15932 C CG    . PRO A 1 3592 ? 167.103 139.293 152.915 1.00 47.58  ? 3592 PRO A CG    1 
ATOM   15933 C CD    . PRO A 1 3592 ? 166.308 138.962 151.694 1.00 47.58  ? 3592 PRO A CD    1 
ATOM   15934 N N     . SER A 1 3593 ? 169.150 139.215 149.376 1.00 50.85  ? 3593 SER A N     1 
ATOM   15935 C CA    . SER A 1 3593 ? 170.058 138.966 148.270 1.00 50.85  ? 3593 SER A CA    1 
ATOM   15936 C C     . SER A 1 3593 ? 169.396 139.390 146.961 1.00 50.85  ? 3593 SER A C     1 
ATOM   15937 O O     . SER A 1 3593 ? 168.225 139.774 146.921 1.00 50.85  ? 3593 SER A O     1 
ATOM   15938 C CB    . SER A 1 3593 ? 170.471 137.494 148.236 1.00 50.85  ? 3593 SER A CB    1 
ATOM   15939 O OG    . SER A 1 3593 ? 169.343 136.645 148.348 1.00 50.85  ? 3593 SER A OG    1 
ATOM   15940 N N     . GLY A 1 3594 ? 170.160 139.325 145.875 1.00 48.15  ? 3594 GLY A N     1 
ATOM   15941 C CA    . GLY A 1 3594 ? 169.647 139.732 144.583 1.00 48.15  ? 3594 GLY A CA    1 
ATOM   15942 C C     . GLY A 1 3594 ? 169.185 138.571 143.729 1.00 48.15  ? 3594 GLY A C     1 
ATOM   15943 O O     . GLY A 1 3594 ? 168.962 138.728 142.526 1.00 48.15  ? 3594 GLY A O     1 
ATOM   15944 N N     . GLN A 1 3595 ? 169.040 137.396 144.346 1.00 47.28  ? 3595 GLN A N     1 
ATOM   15945 C CA    . GLN A 1 3595 ? 168.675 136.199 143.593 1.00 47.28  ? 3595 GLN A CA    1 
ATOM   15946 C C     . GLN A 1 3595 ? 167.293 136.335 142.967 1.00 47.28  ? 3595 GLN A C     1 
ATOM   15947 O O     . GLN A 1 3595 ? 167.086 135.967 141.805 1.00 47.28  ? 3595 GLN A O     1 
ATOM   15948 C CB    . GLN A 1 3595 ? 168.733 134.974 144.505 1.00 47.28  ? 3595 GLN A CB    1 
ATOM   15949 C CG    . GLN A 1 3595 ? 169.892 134.986 145.485 1.00 47.28  ? 3595 GLN A CG    1 
ATOM   15950 C CD    . GLN A 1 3595 ? 171.168 134.435 144.884 1.00 47.28  ? 3595 GLN A CD    1 
ATOM   15951 O OE1   . GLN A 1 3595 ? 171.224 134.122 143.694 1.00 47.28  ? 3595 GLN A OE1   1 
ATOM   15952 N NE2   . GLN A 1 3595 ? 172.203 134.313 145.705 1.00 47.28  ? 3595 GLN A NE2   1 
ATOM   15953 N N     . ALA A 1 3596 ? 166.329 136.858 143.728 1.00 46.87  ? 3596 ALA A N     1 
ATOM   15954 C CA    . ALA A 1 3596 ? 164.962 136.951 143.225 1.00 46.87  ? 3596 ALA A CA    1 
ATOM   15955 C C     . ALA A 1 3596 ? 164.855 137.942 142.073 1.00 46.87  ? 3596 ALA A C     1 
ATOM   15956 O O     . ALA A 1 3596 ? 164.150 137.683 141.090 1.00 46.87  ? 3596 ALA A O     1 
ATOM   15957 C CB    . ALA A 1 3596 ? 164.015 137.340 144.356 1.00 46.87  ? 3596 ALA A CB    1 
ATOM   15958 N N     . THR A 1 3597 ? 165.535 139.085 142.181 1.00 52.75  ? 3597 THR A N     1 
ATOM   15959 C CA    . THR A 1 3597 ? 165.502 140.069 141.103 1.00 52.75  ? 3597 THR A CA    1 
ATOM   15960 C C     . THR A 1 3597 ? 166.117 139.503 139.829 1.00 52.75  ? 3597 THR A C     1 
ATOM   15961 O O     . THR A 1 3597 ? 165.559 139.651 138.737 1.00 52.75  ? 3597 THR A O     1 
ATOM   15962 C CB    . THR A 1 3597 ? 166.226 141.345 141.533 1.00 52.75  ? 3597 THR A CB    1 
ATOM   15963 O OG1   . THR A 1 3597 ? 165.580 141.898 142.686 1.00 52.75  ? 3597 THR A OG1   1 
ATOM   15964 C CG2   . THR A 1 3597 ? 166.209 142.371 140.410 1.00 52.75  ? 3597 THR A CG2   1 
ATOM   15965 N N     . GLU A 1 3598 ? 167.262 138.829 139.954 1.00 55.78  ? 3598 GLU A N     1 
ATOM   15966 C CA    . GLU A 1 3598 ? 167.897 138.237 138.781 1.00 55.78  ? 3598 GLU A CA    1 
ATOM   15967 C C     . GLU A 1 3598 ? 167.030 137.137 138.180 1.00 55.78  ? 3598 GLU A C     1 
ATOM   15968 O O     . GLU A 1 3598 ? 166.962 136.992 136.954 1.00 55.78  ? 3598 GLU A O     1 
ATOM   15969 C CB    . GLU A 1 3598 ? 169.280 137.702 139.147 1.00 55.78  ? 3598 GLU A CB    1 
ATOM   15970 C CG    . GLU A 1 3598 ? 170.266 138.786 139.551 1.00 55.78  ? 3598 GLU A CG    1 
ATOM   15971 C CD    . GLU A 1 3598 ? 171.556 138.225 140.111 1.00 55.78  ? 3598 GLU A CD    1 
ATOM   15972 O OE1   . GLU A 1 3598 ? 172.030 137.191 139.596 1.00 55.78  ? 3598 GLU A OE1   1 
ATOM   15973 O OE2   . GLU A 1 3598 ? 172.100 138.821 141.064 1.00 55.78  ? 3598 GLU A OE2   1 
ATOM   15974 N N     . PHE A 1 3599 ? 166.358 136.354 139.028 1.00 51.12  ? 3599 PHE A N     1 
ATOM   15975 C CA    . PHE A 1 3599 ? 165.468 135.314 138.523 1.00 51.12  ? 3599 PHE A CA    1 
ATOM   15976 C C     . PHE A 1 3599 ? 164.299 135.912 137.752 1.00 51.12  ? 3599 PHE A C     1 
ATOM   15977 O O     . PHE A 1 3599 ? 164.002 135.484 136.630 1.00 51.12  ? 3599 PHE A O     1 
ATOM   15978 C CB    . PHE A 1 3599 ? 164.954 134.454 139.676 1.00 51.12  ? 3599 PHE A CB    1 
ATOM   15979 C CG    . PHE A 1 3599 ? 163.653 133.763 139.378 1.00 51.12  ? 3599 PHE A CG    1 
ATOM   15980 C CD1   . PHE A 1 3599 ? 163.597 132.724 138.466 1.00 51.12  ? 3599 PHE A CD1   1 
ATOM   15981 C CD2   . PHE A 1 3599 ? 162.485 134.161 140.005 1.00 51.12  ? 3599 PHE A CD2   1 
ATOM   15982 C CE1   . PHE A 1 3599 ? 162.402 132.091 138.189 1.00 51.12  ? 3599 PHE A CE1   1 
ATOM   15983 C CE2   . PHE A 1 3599 ? 161.287 133.531 139.732 1.00 51.12  ? 3599 PHE A CE2   1 
ATOM   15984 C CZ    . PHE A 1 3599 ? 161.245 132.496 138.823 1.00 51.12  ? 3599 PHE A CZ    1 
ATOM   15985 N N     . ILE A 1 3600 ? 163.626 136.907 138.334 1.00 54.35  ? 3600 ILE A N     1 
ATOM   15986 C CA    . ILE A 1 3600 ? 162.471 137.497 137.668 1.00 54.35  ? 3600 ILE A CA    1 
ATOM   15987 C C     . ILE A 1 3600 ? 162.913 138.292 136.446 1.00 54.35  ? 3600 ILE A C     1 
ATOM   15988 O O     . ILE A 1 3600 ? 162.109 138.564 135.546 1.00 54.35  ? 3600 ILE A O     1 
ATOM   15989 C CB    . ILE A 1 3600 ? 161.666 138.361 138.660 1.00 54.35  ? 3600 ILE A CB    1 
ATOM   15990 C CG1   . ILE A 1 3600 ? 160.296 138.728 138.085 1.00 54.35  ? 3600 ILE A CG1   1 
ATOM   15991 C CG2   . ILE A 1 3600 ? 162.430 139.616 139.024 1.00 54.35  ? 3600 ILE A CG2   1 
ATOM   15992 C CD1   . ILE A 1 3600 ? 159.377 137.543 137.893 1.00 54.35  ? 3600 ILE A CD1   1 
ATOM   15993 N N     . MET A 1 3601 ? 164.193 138.663 136.380 1.00 58.98  ? 3601 MET A N     1 
ATOM   15994 C CA    . MET A 1 3601 ? 164.694 139.385 135.218 1.00 58.98  ? 3601 MET A CA    1 
ATOM   15995 C C     . MET A 1 3601 ? 164.989 138.427 134.071 1.00 58.98  ? 3601 MET A C     1 
ATOM   15996 O O     . MET A 1 3601 ? 164.581 138.660 132.928 1.00 58.98  ? 3601 MET A O     1 
ATOM   15997 C CB    . MET A 1 3601 ? 165.942 140.180 135.605 1.00 58.98  ? 3601 MET A CB    1 
ATOM   15998 C CG    . MET A 1 3601 ? 165.596 141.555 136.122 1.00 58.98  ? 3601 MET A CG    1 
ATOM   15999 S SD    . MET A 1 3601 ? 164.583 142.456 134.948 1.00 58.98  ? 3601 MET A SD    1 
ATOM   16000 C CE    . MET A 1 3601 ? 164.534 144.063 135.716 1.00 58.98  ? 3601 MET A CE    1 
ATOM   16001 N N     . ASN A 1 3602 ? 165.702 137.335 134.361 1.00 59.65  ? 3602 ASN A N     1 
ATOM   16002 C CA    . ASN A 1 3602 ? 165.956 136.320 133.345 1.00 59.65  ? 3602 ASN A CA    1 
ATOM   16003 C C     . ASN A 1 3602 ? 164.675 135.641 132.883 1.00 59.65  ? 3602 ASN A C     1 
ATOM   16004 O O     . ASN A 1 3602 ? 164.611 135.174 131.740 1.00 59.65  ? 3602 ASN A O     1 
ATOM   16005 C CB    . ASN A 1 3602 ? 166.933 135.269 133.874 1.00 59.65  ? 3602 ASN A CB    1 
ATOM   16006 C CG    . ASN A 1 3602 ? 168.252 135.867 134.320 1.00 59.65  ? 3602 ASN A CG    1 
ATOM   16007 O OD1   . ASN A 1 3602 ? 168.913 135.345 135.216 1.00 59.65  ? 3602 ASN A OD1   1 
ATOM   16008 N ND2   . ASN A 1 3602 ? 168.634 136.980 133.703 1.00 59.65  ? 3602 ASN A ND2   1 
ATOM   16009 N N     . GLU A 1 3603 ? 163.657 135.574 133.742 1.00 59.48  ? 3603 GLU A N     1 
ATOM   16010 C CA    . GLU A 1 3603 ? 162.404 134.927 133.374 1.00 59.48  ? 3603 GLU A CA    1 
ATOM   16011 C C     . GLU A 1 3603 ? 161.624 135.726 132.337 1.00 59.48  ? 3603 GLU A C     1 
ATOM   16012 O O     . GLU A 1 3603 ? 160.947 135.135 131.489 1.00 59.48  ? 3603 GLU A O     1 
ATOM   16013 C CB    . GLU A 1 3603 ? 161.547 134.705 134.624 1.00 59.48  ? 3603 GLU A CB    1 
ATOM   16014 C CG    . GLU A 1 3603 ? 160.183 134.056 134.384 1.00 59.48  ? 3603 GLU A CG    1 
ATOM   16015 C CD    . GLU A 1 3603 ? 160.257 132.617 133.891 1.00 59.48  ? 3603 GLU A CD    1 
ATOM   16016 O OE1   . GLU A 1 3603 ? 159.186 131.987 133.763 1.00 59.48  ? 3603 GLU A OE1   1 
ATOM   16017 O OE2   . GLU A 1 3603 ? 161.370 132.101 133.656 1.00 59.48  ? 3603 GLU A OE2   1 
ATOM   16018 N N     . TYR A 1 3604 ? 161.710 137.057 132.379 1.00 62.84  ? 3604 TYR A N     1 
ATOM   16019 C CA    . TYR A 1 3604 ? 160.897 137.916 131.525 1.00 62.84  ? 3604 TYR A CA    1 
ATOM   16020 C C     . TYR A 1 3604 ? 161.725 138.653 130.477 1.00 62.84  ? 3604 TYR A C     1 
ATOM   16021 O O     . TYR A 1 3604 ? 161.299 139.704 129.988 1.00 62.84  ? 3604 TYR A O     1 
ATOM   16022 C CB    . TYR A 1 3604 ? 160.111 138.918 132.374 1.00 62.84  ? 3604 TYR A CB    1 
ATOM   16023 C CG    . TYR A 1 3604 ? 158.897 138.333 133.060 1.00 62.84  ? 3604 TYR A CG    1 
ATOM   16024 C CD1   . TYR A 1 3604 ? 159.033 137.399 134.078 1.00 62.84  ? 3604 TYR A CD1   1 
ATOM   16025 C CD2   . TYR A 1 3604 ? 157.615 138.719 132.694 1.00 62.84  ? 3604 TYR A CD2   1 
ATOM   16026 C CE1   . TYR A 1 3604 ? 157.927 136.863 134.709 1.00 62.84  ? 3604 TYR A CE1   1 
ATOM   16027 C CE2   . TYR A 1 3604 ? 156.503 138.189 133.320 1.00 62.84  ? 3604 TYR A CE2   1 
ATOM   16028 C CZ    . TYR A 1 3604 ? 156.666 137.262 134.327 1.00 62.84  ? 3604 TYR A CZ    1 
ATOM   16029 O OH    . TYR A 1 3604 ? 155.562 136.730 134.953 1.00 62.84  ? 3604 TYR A OH    1 
ATOM   16030 N N     . LYS A 1 3605 ? 162.901 138.129 130.120 1.00 67.05  ? 3605 LYS A N     1 
ATOM   16031 C CA    . LYS A 1 3605 ? 163.701 138.766 129.078 1.00 67.05  ? 3605 LYS A CA    1 
ATOM   16032 C C     . LYS A 1 3605 ? 162.972 138.758 127.740 1.00 67.05  ? 3605 LYS A C     1 
ATOM   16033 O O     . LYS A 1 3605 ? 163.060 139.725 126.974 1.00 67.05  ? 3605 LYS A O     1 
ATOM   16034 C CB    . LYS A 1 3605 ? 165.060 138.077 128.949 1.00 67.05  ? 3605 LYS A CB    1 
ATOM   16035 C CG    . LYS A 1 3605 ? 165.985 138.300 130.130 1.00 67.05  ? 3605 LYS A CG    1 
ATOM   16036 C CD    . LYS A 1 3605 ? 167.257 137.478 130.004 1.00 67.05  ? 3605 LYS A CD    1 
ATOM   16037 C CE    . LYS A 1 3605 ? 168.150 138.014 128.898 1.00 67.05  ? 3605 LYS A CE    1 
ATOM   16038 N NZ    . LYS A 1 3605 ? 169.449 137.290 128.840 1.00 67.05  ? 3605 LYS A NZ    1 
ATOM   16039 N N     . ASP A 1 3606 ? 162.255 137.673 127.440 1.00 74.77  ? 3606 ASP A N     1 
ATOM   16040 C CA    . ASP A 1 3606 ? 161.499 137.604 126.194 1.00 74.77  ? 3606 ASP A CA    1 
ATOM   16041 C C     . ASP A 1 3606 ? 160.434 138.690 126.120 1.00 74.77  ? 3606 ASP A C     1 
ATOM   16042 O O     . ASP A 1 3606 ? 160.105 139.163 125.027 1.00 74.77  ? 3606 ASP A O     1 
ATOM   16043 C CB    . ASP A 1 3606 ? 160.861 136.222 126.047 1.00 74.77  ? 3606 ASP A CB    1 
ATOM   16044 C CG    . ASP A 1 3606 ? 160.177 136.036 124.708 1.00 74.77  ? 3606 ASP A CG    1 
ATOM   16045 O OD1   . ASP A 1 3606 ? 160.887 135.867 123.695 1.00 74.77  ? 3606 ASP A OD1   1 
ATOM   16046 O OD2   . ASP A 1 3606 ? 158.929 136.058 124.669 1.00 74.77  ? 3606 ASP A OD2   1 
ATOM   16047 N N     . ARG A 1 3607 ? 159.889 139.097 127.263 1.00 72.37  ? 3607 ARG A N     1 
ATOM   16048 C CA    . ARG A 1 3607 ? 158.864 140.130 127.315 1.00 72.37  ? 3607 ARG A CA    1 
ATOM   16049 C C     . ARG A 1 3607 ? 159.437 141.531 127.486 1.00 72.37  ? 3607 ARG A C     1 
ATOM   16050 O O     . ARG A 1 3607 ? 158.663 142.488 127.592 1.00 72.37  ? 3607 ARG A O     1 
ATOM   16051 C CB    . ARG A 1 3607 ? 157.882 139.833 128.452 1.00 72.37  ? 3607 ARG A CB    1 
ATOM   16052 C CG    . ARG A 1 3607 ? 157.414 138.389 128.510 1.00 72.37  ? 3607 ARG A CG    1 
ATOM   16053 C CD    . ARG A 1 3607 ? 156.171 138.176 127.656 1.00 72.37  ? 3607 ARG A CD    1 
ATOM   16054 N NE    . ARG A 1 3607 ? 155.044 139.008 128.068 1.00 72.37  ? 3607 ARG A NE    1 
ATOM   16055 C CZ    . ARG A 1 3607 ? 154.473 138.987 129.266 1.00 72.37  ? 3607 ARG A CZ    1 
ATOM   16056 N NH1   . ARG A 1 3607 ? 154.855 138.136 130.205 1.00 72.37  ? 3607 ARG A NH1   1 
ATOM   16057 N NH2   . ARG A 1 3607 ? 153.478 139.832 129.524 1.00 72.37  ? 3607 ARG A NH2   1 
ATOM   16058 N N     . LYS A 1 3608 ? 160.764 141.672 127.516 1.00 73.73  ? 3608 LYS A N     1 
ATOM   16059 C CA    . LYS A 1 3608 ? 161.439 142.962 127.672 1.00 73.73  ? 3608 LYS A CA    1 
ATOM   16060 C C     . LYS A 1 3608 ? 161.065 143.631 128.998 1.00 73.73  ? 3608 LYS A C     1 
ATOM   16061 O O     . LYS A 1 3608 ? 160.506 144.728 129.044 1.00 73.73  ? 3608 LYS A O     1 
ATOM   16062 C CB    . LYS A 1 3608 ? 161.148 143.887 126.484 1.00 73.73  ? 3608 LYS A CB    1 
ATOM   16063 C CG    . LYS A 1 3608 ? 161.806 143.453 125.184 1.00 73.73  ? 3608 LYS A CG    1 
ATOM   16064 C CD    . LYS A 1 3608 ? 161.181 144.148 123.985 1.00 73.73  ? 3608 LYS A CD    1 
ATOM   16065 C CE    . LYS A 1 3608 ? 159.665 144.044 124.010 1.00 73.73  ? 3608 LYS A CE    1 
ATOM   16066 N NZ    . LYS A 1 3608 ? 159.020 145.154 123.257 1.00 73.73  ? 3608 LYS A NZ    1 
ATOM   16067 N N     . ILE A 1 3609 ? 161.388 142.934 130.090 1.00 70.09  ? 3609 ILE A N     1 
ATOM   16068 C CA    . ILE A 1 3609 ? 161.233 143.509 131.420 1.00 70.09  ? 3609 ILE A CA    1 
ATOM   16069 C C     . ILE A 1 3609 ? 162.262 144.614 131.613 1.00 70.09  ? 3609 ILE A C     1 
ATOM   16070 O O     . ILE A 1 3609 ? 163.436 144.465 131.249 1.00 70.09  ? 3609 ILE A O     1 
ATOM   16071 C CB    . ILE A 1 3609 ? 161.356 142.409 132.485 1.00 70.09  ? 3609 ILE A CB    1 
ATOM   16072 C CG1   . ILE A 1 3609 ? 161.329 143.003 133.897 1.00 70.09  ? 3609 ILE A CG1   1 
ATOM   16073 C CG2   . ILE A 1 3609 ? 162.605 141.573 132.247 1.00 70.09  ? 3609 ILE A CG2   1 
ATOM   16074 C CD1   . ILE A 1 3609 ? 160.017 143.633 134.280 1.00 70.09  ? 3609 ILE A CD1   1 
ATOM   16075 N N     . THR A 1 3610 ? 161.825 145.737 132.177 1.00 67.19  ? 3610 THR A N     1 
ATOM   16076 C CA    . THR A 1 3610 ? 162.645 146.935 132.297 1.00 67.19  ? 3610 THR A CA    1 
ATOM   16077 C C     . THR A 1 3610 ? 162.920 147.244 133.762 1.00 67.19  ? 3610 THR A C     1 
ATOM   16078 O O     . THR A 1 3610 ? 162.032 147.101 134.608 1.00 67.19  ? 3610 THR A O     1 
ATOM   16079 C CB    . THR A 1 3610 ? 161.958 148.130 131.634 1.00 67.19  ? 3610 THR A CB    1 
ATOM   16080 O OG1   . THR A 1 3610 ? 160.669 148.328 132.228 1.00 67.19  ? 3610 THR A OG1   1 
ATOM   16081 C CG2   . THR A 1 3610 ? 161.789 147.884 130.144 1.00 67.19  ? 3610 THR A CG2   1 
ATOM   16082 N N     . ARG A 1 3611 ? 164.146 147.672 134.056 1.00 67.52  ? 3611 ARG A N     1 
ATOM   16083 C CA    . ARG A 1 3611 ? 164.527 148.061 135.407 1.00 67.52  ? 3611 ARG A CA    1 
ATOM   16084 C C     . ARG A 1 3611 ? 164.102 149.500 135.662 1.00 67.52  ? 3611 ARG A C     1 
ATOM   16085 O O     . ARG A 1 3611 ? 164.344 150.381 134.831 1.00 67.52  ? 3611 ARG A O     1 
ATOM   16086 C CB    . ARG A 1 3611 ? 166.037 147.928 135.619 1.00 67.52  ? 3611 ARG A CB    1 
ATOM   16087 C CG    . ARG A 1 3611 ? 166.647 146.643 135.099 1.00 67.52  ? 3611 ARG A CG    1 
ATOM   16088 C CD    . ARG A 1 3611 ? 168.084 146.491 135.563 1.00 67.52  ? 3611 ARG A CD    1 
ATOM   16089 N NE    . ARG A 1 3611 ? 168.257 146.965 136.931 1.00 67.52  ? 3611 ARG A NE    1 
ATOM   16090 C CZ    . ARG A 1 3611 ? 167.957 146.262 138.015 1.00 67.52  ? 3611 ARG A CZ    1 
ATOM   16091 N NH1   . ARG A 1 3611 ? 167.462 145.038 137.930 1.00 67.52  ? 3611 ARG A NH1   1 
ATOM   16092 N NH2   . ARG A 1 3611 ? 168.157 146.801 139.214 1.00 67.52  ? 3611 ARG A NH2   1 
ATOM   16093 N N     . THR A 1 3612 ? 163.467 149.736 136.809 1.00 67.41  ? 3612 THR A N     1 
ATOM   16094 C CA    . THR A 1 3612 ? 163.083 151.079 137.221 1.00 67.41  ? 3612 THR A CA    1 
ATOM   16095 C C     . THR A 1 3612 ? 162.986 151.088 138.744 1.00 67.41  ? 3612 THR A C     1 
ATOM   16096 O O     . THR A 1 3612 ? 162.904 150.036 139.385 1.00 67.41  ? 3612 THR A O     1 
ATOM   16097 C CB    . THR A 1 3612 ? 161.765 151.502 136.553 1.00 67.41  ? 3612 THR A CB    1 
ATOM   16098 O OG1   . THR A 1 3612 ? 161.849 151.280 135.141 1.00 67.41  ? 3612 THR A OG1   1 
ATOM   16099 C CG2   . THR A 1 3612 ? 161.507 152.983 136.760 1.00 67.41  ? 3612 THR A CG2   1 
ATOM   16100 N N     . SER A 1 3613 ? 162.995 152.283 139.332 1.00 73.56  ? 3613 SER A N     1 
ATOM   16101 C CA    . SER A 1 3613 ? 162.894 152.425 140.777 1.00 73.56  ? 3613 SER A CA    1 
ATOM   16102 C C     . SER A 1 3613 ? 162.053 153.650 141.096 1.00 73.56  ? 3613 SER A C     1 
ATOM   16103 O O     . SER A 1 3613 ? 161.897 154.548 140.264 1.00 73.56  ? 3613 SER A O     1 
ATOM   16104 C CB    . SER A 1 3613 ? 164.274 152.548 141.434 1.00 73.56  ? 3613 SER A CB    1 
ATOM   16105 O OG    . SER A 1 3613 ? 164.759 153.877 141.358 1.00 73.56  ? 3613 SER A OG    1 
ATOM   16106 N N     . PHE A 1 3614 ? 161.508 153.675 142.314 1.00 76.34  ? 3614 PHE A N     1 
ATOM   16107 C CA    . PHE A 1 3614 ? 160.687 154.800 142.743 1.00 76.34  ? 3614 PHE A CA    1 
ATOM   16108 C C     . PHE A 1 3614 ? 161.484 156.092 142.853 1.00 76.34  ? 3614 PHE A C     1 
ATOM   16109 O O     . PHE A 1 3614 ? 160.923 157.171 142.633 1.00 76.34  ? 3614 PHE A O     1 
ATOM   16110 C CB    . PHE A 1 3614 ? 160.031 154.491 144.088 1.00 76.34  ? 3614 PHE A CB    1 
ATOM   16111 C CG    . PHE A 1 3614 ? 158.813 153.622 143.984 1.00 76.34  ? 3614 PHE A CG    1 
ATOM   16112 C CD1   . PHE A 1 3614 ? 157.774 153.961 143.138 1.00 76.34  ? 3614 PHE A CD1   1 
ATOM   16113 C CD2   . PHE A 1 3614 ? 158.707 152.468 144.736 1.00 76.34  ? 3614 PHE A CD2   1 
ATOM   16114 C CE1   . PHE A 1 3614 ? 156.655 153.161 143.045 1.00 76.34  ? 3614 PHE A CE1   1 
ATOM   16115 C CE2   . PHE A 1 3614 ? 157.590 151.666 144.647 1.00 76.34  ? 3614 PHE A CE2   1 
ATOM   16116 C CZ    . PHE A 1 3614 ? 156.564 152.013 143.802 1.00 76.34  ? 3614 PHE A CZ    1 
ATOM   16117 N N     . LEU A 1 3615 ? 162.772 156.009 143.189 1.00 82.61  ? 3615 LEU A N     1 
ATOM   16118 C CA    . LEU A 1 3615 ? 163.592 157.205 143.325 1.00 82.61  ? 3615 LEU A CA    1 
ATOM   16119 C C     . LEU A 1 3615 ? 163.901 157.861 141.987 1.00 82.61  ? 3615 LEU A C     1 
ATOM   16120 O O     . LEU A 1 3615 ? 164.260 159.043 141.961 1.00 82.61  ? 3615 LEU A O     1 
ATOM   16121 C CB    . LEU A 1 3615 ? 164.899 156.863 144.045 1.00 82.61  ? 3615 LEU A CB    1 
ATOM   16122 C CG    . LEU A 1 3615 ? 164.761 156.326 145.471 1.00 82.61  ? 3615 LEU A CG    1 
ATOM   16123 C CD1   . LEU A 1 3615 ? 166.109 156.313 146.174 1.00 82.61  ? 3615 LEU A CD1   1 
ATOM   16124 C CD2   . LEU A 1 3615 ? 163.748 157.142 146.260 1.00 82.61  ? 3615 LEU A CD2   1 
ATOM   16125 N N     . ASP A 1 3616 ? 163.771 157.128 140.885 1.00 81.63  ? 3616 ASP A N     1 
ATOM   16126 C CA    . ASP A 1 3616 ? 164.034 157.695 139.571 1.00 81.63  ? 3616 ASP A CA    1 
ATOM   16127 C C     . ASP A 1 3616 ? 162.965 158.716 139.203 1.00 81.63  ? 3616 ASP A C     1 
ATOM   16128 O O     . ASP A 1 3616 ? 161.773 158.510 139.449 1.00 81.63  ? 3616 ASP A O     1 
ATOM   16129 C CB    . ASP A 1 3616 ? 164.087 156.589 138.518 1.00 81.63  ? 3616 ASP A CB    1 
ATOM   16130 C CG    . ASP A 1 3616 ? 165.269 155.662 138.708 1.00 81.63  ? 3616 ASP A CG    1 
ATOM   16131 O OD1   . ASP A 1 3616 ? 165.600 154.915 137.763 1.00 81.63  ? 3616 ASP A OD1   1 
ATOM   16132 O OD2   . ASP A 1 3616 ? 165.868 155.680 139.804 1.00 81.63  ? 3616 ASP A OD2   1 
ATOM   16133 N N     . ASP A 1 3617 ? 163.400 159.829 138.609 1.00 83.54  ? 3617 ASP A N     1 
ATOM   16134 C CA    . ASP A 1 3617 ? 162.457 160.846 138.160 1.00 83.54  ? 3617 ASP A CA    1 
ATOM   16135 C C     . ASP A 1 3617 ? 161.713 160.415 136.904 1.00 83.54  ? 3617 ASP A C     1 
ATOM   16136 O O     . ASP A 1 3617 ? 160.574 160.844 136.685 1.00 83.54  ? 3617 ASP A O     1 
ATOM   16137 C CB    . ASP A 1 3617 ? 163.185 162.168 137.918 1.00 83.54  ? 3617 ASP A CB    1 
ATOM   16138 C CG    . ASP A 1 3617 ? 163.693 162.795 139.201 1.00 83.54  ? 3617 ASP A CG    1 
ATOM   16139 O OD1   . ASP A 1 3617 ? 162.860 163.258 140.009 1.00 83.54  ? 3617 ASP A OD1   1 
ATOM   16140 O OD2   . ASP A 1 3617 ? 164.925 162.821 139.405 1.00 83.54  ? 3617 ASP A OD2   1 
ATOM   16141 N N     . ALA A 1 3618 ? 162.331 159.575 136.077 1.00 80.65  ? 3618 ALA A N     1 
ATOM   16142 C CA    . ALA A 1 3618 ? 161.678 159.025 134.897 1.00 80.65  ? 3618 ALA A CA    1 
ATOM   16143 C C     . ALA A 1 3618 ? 160.886 157.761 135.201 1.00 80.65  ? 3618 ALA A C     1 
ATOM   16144 O O     . ALA A 1 3618 ? 160.506 157.047 134.263 1.00 80.65  ? 3618 ALA A O     1 
ATOM   16145 C CB    . ALA A 1 3618 ? 162.713 158.738 133.806 1.00 80.65  ? 3618 ALA A CB    1 
ATOM   16146 N N     . PHE A 1 3619 ? 160.652 157.461 136.482 1.00 78.89  ? 3619 PHE A N     1 
ATOM   16147 C CA    . PHE A 1 3619 ? 159.876 156.282 136.847 1.00 78.89  ? 3619 PHE A CA    1 
ATOM   16148 C C     . PHE A 1 3619 ? 158.486 156.324 136.233 1.00 78.89  ? 3619 PHE A C     1 
ATOM   16149 O O     . PHE A 1 3619 ? 158.005 155.324 135.691 1.00 78.89  ? 3619 PHE A O     1 
ATOM   16150 C CB    . PHE A 1 3619 ? 159.772 156.161 138.367 1.00 78.89  ? 3619 PHE A CB    1 
ATOM   16151 C CG    . PHE A 1 3619 ? 158.693 155.217 138.819 1.00 78.89  ? 3619 PHE A CG    1 
ATOM   16152 C CD1   . PHE A 1 3619 ? 158.812 153.855 138.611 1.00 78.89  ? 3619 PHE A CD1   1 
ATOM   16153 C CD2   . PHE A 1 3619 ? 157.552 155.696 139.438 1.00 78.89  ? 3619 PHE A CD2   1 
ATOM   16154 C CE1   . PHE A 1 3619 ? 157.819 152.988 139.016 1.00 78.89  ? 3619 PHE A CE1   1 
ATOM   16155 C CE2   . PHE A 1 3619 ? 156.555 154.832 139.847 1.00 78.89  ? 3619 PHE A CE2   1 
ATOM   16156 C CZ    . PHE A 1 3619 ? 156.690 153.476 139.635 1.00 78.89  ? 3619 PHE A CZ    1 
ATOM   16157 N N     . ARG A 1 3620 ? 157.823 157.477 136.312 1.00 78.92  ? 3620 ARG A N     1 
ATOM   16158 C CA    . ARG A 1 3620 ? 156.478 157.592 135.762 1.00 78.92  ? 3620 ARG A CA    1 
ATOM   16159 C C     . ARG A 1 3620 ? 156.488 157.375 134.254 1.00 78.92  ? 3620 ARG A C     1 
ATOM   16160 O O     . ARG A 1 3620 ? 155.617 156.687 133.705 1.00 78.92  ? 3620 ARG A O     1 
ATOM   16161 C CB    . ARG A 1 3620 ? 155.888 158.958 136.118 1.00 78.92  ? 3620 ARG A CB    1 
ATOM   16162 C CG    . ARG A 1 3620 ? 154.436 159.144 135.715 1.00 78.92  ? 3620 ARG A CG    1 
ATOM   16163 C CD    . ARG A 1 3620 ? 153.753 160.145 136.633 1.00 78.92  ? 3620 ARG A CD    1 
ATOM   16164 N NE    . ARG A 1 3620 ? 152.694 160.890 135.963 1.00 78.92  ? 3620 ARG A NE    1 
ATOM   16165 C CZ    . ARG A 1 3620 ? 151.737 161.556 136.593 1.00 78.92  ? 3620 ARG A CZ    1 
ATOM   16166 N NH1   . ARG A 1 3620 ? 151.674 161.592 137.913 1.00 78.92  ? 3620 ARG A NH1   1 
ATOM   16167 N NH2   . ARG A 1 3620 ? 150.820 162.204 135.880 1.00 78.92  ? 3620 ARG A NH2   1 
ATOM   16168 N N     . LYS A 1 3621 ? 157.477 157.955 133.568 1.00 81.44  ? 3621 LYS A N     1 
ATOM   16169 C CA    . LYS A 1 3621 ? 157.563 157.802 132.120 1.00 81.44  ? 3621 LYS A CA    1 
ATOM   16170 C C     . LYS A 1 3621 ? 157.773 156.346 131.731 1.00 81.44  ? 3621 LYS A C     1 
ATOM   16171 O O     . LYS A 1 3621 ? 157.111 155.832 130.821 1.00 81.44  ? 3621 LYS A O     1 
ATOM   16172 C CB    . LYS A 1 3621 ? 158.673 158.691 131.557 1.00 81.44  ? 3621 LYS A CB    1 
ATOM   16173 C CG    . LYS A 1 3621 ? 158.712 160.082 132.167 1.00 81.44  ? 3621 LYS A CG    1 
ATOM   16174 C CD    . LYS A 1 3621 ? 159.381 161.076 131.231 1.00 81.44  ? 3621 LYS A CD    1 
ATOM   16175 C CE    . LYS A 1 3621 ? 160.884 161.110 131.430 1.00 81.44  ? 3621 LYS A CE    1 
ATOM   16176 N NZ    . LYS A 1 3621 ? 161.511 162.220 130.660 1.00 81.44  ? 3621 LYS A NZ    1 
ATOM   16177 N N     . ASN A 1 3622 ? 158.680 155.655 132.427 1.00 79.35  ? 3622 ASN A N     1 
ATOM   16178 C CA    . ASN A 1 3622 ? 158.845 154.224 132.189 1.00 79.35  ? 3622 ASN A CA    1 
ATOM   16179 C C     . ASN A 1 3622 ? 157.559 153.470 132.506 1.00 79.35  ? 3622 ASN A C     1 
ATOM   16180 O O     . ASN A 1 3622 ? 157.236 152.469 131.858 1.00 79.35  ? 3622 ASN A O     1 
ATOM   16181 C CB    . ASN A 1 3622 ? 160.013 153.674 133.009 1.00 79.35  ? 3622 ASN A CB    1 
ATOM   16182 C CG    . ASN A 1 3622 ? 161.344 154.275 132.607 1.00 79.35  ? 3622 ASN A CG    1 
ATOM   16183 O OD1   . ASN A 1 3622 ? 161.982 154.981 133.386 1.00 79.35  ? 3622 ASN A OD1   1 
ATOM   16184 N ND2   . ASN A 1 3622 ? 161.772 153.995 131.381 1.00 79.35  ? 3622 ASN A ND2   1 
ATOM   16185 N N     . LEU A 1 3623 ? 156.800 153.955 133.491 1.00 79.47  ? 3623 LEU A N     1 
ATOM   16186 C CA    . LEU A 1 3623 ? 155.552 153.301 133.864 1.00 79.47  ? 3623 LEU A CA    1 
ATOM   16187 C C     . LEU A 1 3623 ? 154.550 153.336 132.717 1.00 79.47  ? 3623 LEU A C     1 
ATOM   16188 O O     . LEU A 1 3623 ? 154.020 152.292 132.318 1.00 79.47  ? 3623 LEU A O     1 
ATOM   16189 C CB    . LEU A 1 3623 ? 154.974 153.975 135.111 1.00 79.47  ? 3623 LEU A CB    1 
ATOM   16190 C CG    . LEU A 1 3623 ? 153.832 153.398 135.954 1.00 79.47  ? 3623 LEU A CG    1 
ATOM   16191 C CD1   . LEU A 1 3623 ? 153.679 154.265 137.189 1.00 79.47  ? 3623 LEU A CD1   1 
ATOM   16192 C CD2   . LEU A 1 3623 ? 152.503 153.313 135.216 1.00 79.47  ? 3623 LEU A CD2   1 
ATOM   16193 N N     . GLU A 1 3624 ? 154.283 154.521 132.165 1.00 84.86  ? 3624 GLU A N     1 
ATOM   16194 C CA    . GLU A 1 3624 ? 153.314 154.576 131.070 1.00 84.86  ? 3624 GLU A CA    1 
ATOM   16195 C C     . GLU A 1 3624 ? 153.875 153.941 129.802 1.00 84.86  ? 3624 GLU A C     1 
ATOM   16196 O O     . GLU A 1 3624 ? 153.117 153.436 128.965 1.00 84.86  ? 3624 GLU A O     1 
ATOM   16197 C CB    . GLU A 1 3624 ? 152.825 155.997 130.771 1.00 84.86  ? 3624 GLU A CB    1 
ATOM   16198 C CG    . GLU A 1 3624 ? 153.842 156.930 130.167 1.00 84.86  ? 3624 GLU A CG    1 
ATOM   16199 C CD    . GLU A 1 3624 ? 154.335 157.961 131.149 1.00 84.86  ? 3624 GLU A CD    1 
ATOM   16200 O OE1   . GLU A 1 3624 ? 153.968 157.871 132.334 1.00 84.86  ? 3624 GLU A OE1   1 
ATOM   16201 O OE2   . GLU A 1 3624 ? 155.084 158.869 130.735 1.00 84.86  ? 3624 GLU A OE2   1 
ATOM   16202 N N     . SER A 1 3625 ? 155.201 153.964 129.630 1.00 83.68  ? 3625 SER A N     1 
ATOM   16203 C CA    . SER A 1 3625 ? 155.792 153.279 128.485 1.00 83.68  ? 3625 SER A CA    1 
ATOM   16204 C C     . SER A 1 3625 ? 155.552 151.776 128.565 1.00 83.68  ? 3625 SER A C     1 
ATOM   16205 O O     . SER A 1 3625 ? 155.219 151.137 127.561 1.00 83.68  ? 3625 SER A O     1 
ATOM   16206 C CB    . SER A 1 3625 ? 157.288 153.583 128.405 1.00 83.68  ? 3625 SER A CB    1 
ATOM   16207 O OG    . SER A 1 3625 ? 157.519 154.969 128.220 1.00 83.68  ? 3625 SER A OG    1 
ATOM   16208 N N     . ALA A 1 3626 ? 155.718 151.197 129.756 1.00 79.43  ? 3626 ALA A N     1 
ATOM   16209 C CA    . ALA A 1 3626 ? 155.435 149.780 129.941 1.00 79.43  ? 3626 ALA A CA    1 
ATOM   16210 C C     . ALA A 1 3626 ? 153.943 149.490 129.856 1.00 79.43  ? 3626 ALA A C     1 
ATOM   16211 O O     . ALA A 1 3626 ? 153.544 148.411 129.404 1.00 79.43  ? 3626 ALA A O     1 
ATOM   16212 C CB    . ALA A 1 3626 ? 155.993 149.310 131.284 1.00 79.43  ? 3626 ALA A CB    1 
ATOM   16213 N N     . LEU A 1 3627 ? 153.108 150.434 130.281 1.00 84.16  ? 3627 LEU A N     1 
ATOM   16214 C CA    . LEU A 1 3627 ? 151.666 150.241 130.310 1.00 84.16  ? 3627 LEU A CA    1 
ATOM   16215 C C     . LEU A 1 3627 ? 151.038 150.321 128.920 1.00 84.16  ? 3627 LEU A C     1 
ATOM   16216 O O     . LEU A 1 3627 ? 149.890 149.899 128.748 1.00 84.16  ? 3627 LEU A O     1 
ATOM   16217 C CB    . LEU A 1 3627 ? 151.042 151.275 131.266 1.00 84.16  ? 3627 LEU A CB    1 
ATOM   16218 C CG    . LEU A 1 3627 ? 149.670 151.122 131.940 1.00 84.16  ? 3627 LEU A CG    1 
ATOM   16219 C CD1   . LEU A 1 3627 ? 149.581 152.094 133.108 1.00 84.16  ? 3627 LEU A CD1   1 
ATOM   16220 C CD2   . LEU A 1 3627 ? 148.503 151.357 131.008 1.00 84.16  ? 3627 LEU A CD2   1 
ATOM   16221 N N     . ARG A 1 3628 ? 151.774 150.808 127.918 1.00 90.51  ? 3628 ARG A N     1 
ATOM   16222 C CA    . ARG A 1 3628 ? 151.255 150.972 126.561 1.00 90.51  ? 3628 ARG A CA    1 
ATOM   16223 C C     . ARG A 1 3628 ? 151.444 149.724 125.705 1.00 90.51  ? 3628 ARG A C     1 
ATOM   16224 O O     . ARG A 1 3628 ? 150.498 149.261 125.061 1.00 90.51  ? 3628 ARG A O     1 
ATOM   16225 C CB    . ARG A 1 3628 ? 151.931 152.168 125.878 1.00 90.51  ? 3628 ARG A CB    1 
ATOM   16226 C CG    . ARG A 1 3628 ? 151.119 152.788 124.748 1.00 90.51  ? 3628 ARG A CG    1 
ATOM   16227 C CD    . ARG A 1 3628 ? 151.594 154.200 124.455 1.00 90.51  ? 3628 ARG A CD    1 
ATOM   16228 N NE    . ARG A 1 3628 ? 152.028 154.871 125.673 1.00 90.51  ? 3628 ARG A NE    1 
ATOM   16229 C CZ    . ARG A 1 3628 ? 151.205 155.346 126.597 1.00 90.51  ? 3628 ARG A CZ    1 
ATOM   16230 N NH1   . ARG A 1 3628 ? 149.893 155.302 126.441 1.00 90.51  ? 3628 ARG A NH1   1 
ATOM   16231 N NH2   . ARG A 1 3628 ? 151.712 155.873 127.707 1.00 90.51  ? 3628 ARG A NH2   1 
ATOM   16232 N N     . PHE A 1 3629 ? 152.657 149.182 125.670 1.00 92.32  ? 3629 PHE A N     1 
ATOM   16233 C CA    . PHE A 1 3629 ? 152.984 148.057 124.806 1.00 92.32  ? 3629 PHE A CA    1 
ATOM   16234 C C     . PHE A 1 3629 ? 152.871 146.713 125.514 1.00 92.32  ? 3629 PHE A C     1 
ATOM   16235 O O     . PHE A 1 3629 ? 153.322 145.701 124.968 1.00 92.32  ? 3629 PHE A O     1 
ATOM   16236 C CB    . PHE A 1 3629 ? 154.395 148.224 124.236 1.00 92.32  ? 3629 PHE A CB    1 
ATOM   16237 C CG    . PHE A 1 3629 ? 154.543 149.400 123.315 1.00 92.32  ? 3629 PHE A CG    1 
ATOM   16238 C CD1   . PHE A 1 3629 ? 154.146 149.316 121.990 1.00 92.32  ? 3629 PHE A CD1   1 
ATOM   16239 C CD2   . PHE A 1 3629 ? 155.076 150.593 123.774 1.00 92.32  ? 3629 PHE A CD2   1 
ATOM   16240 C CE1   . PHE A 1 3629 ? 154.281 150.398 121.140 1.00 92.32  ? 3629 PHE A CE1   1 
ATOM   16241 C CE2   . PHE A 1 3629 ? 155.214 151.678 122.930 1.00 92.32  ? 3629 PHE A CE2   1 
ATOM   16242 C CZ    . PHE A 1 3629 ? 154.816 151.581 121.612 1.00 92.32  ? 3629 PHE A CZ    1 
ATOM   16243 N N     . GLY A 1 3630 ? 152.283 146.679 126.705 1.00 83.22  ? 3630 GLY A N     1 
ATOM   16244 C CA    . GLY A 1 3630 ? 152.224 145.440 127.464 1.00 83.22  ? 3630 GLY A CA    1 
ATOM   16245 C C     . GLY A 1 3630 ? 153.584 144.959 127.916 1.00 83.22  ? 3630 GLY A C     1 
ATOM   16246 O O     . GLY A 1 3630 ? 153.840 143.748 127.936 1.00 83.22  ? 3630 GLY A O     1 
ATOM   16247 N N     . ASN A 1 3631 ? 154.468 145.885 128.278 1.00 75.72  ? 3631 ASN A N     1 
ATOM   16248 C CA    . ASN A 1 3631 ? 155.811 145.566 128.738 1.00 75.72  ? 3631 ASN A CA    1 
ATOM   16249 C C     . ASN A 1 3631 ? 155.813 145.368 130.243 1.00 75.72  ? 3631 ASN A C     1 
ATOM   16250 O O     . ASN A 1 3631 ? 155.332 146.245 130.974 1.00 75.72  ? 3631 ASN A O     1 
ATOM   16251 C CB    . ASN A 1 3631 ? 156.784 146.680 128.364 1.00 75.72  ? 3631 ASN A CB    1 
ATOM   16252 C CG    . ASN A 1 3631 ? 157.539 146.389 127.084 1.00 75.72  ? 3631 ASN A CG    1 
ATOM   16253 O OD1   . ASN A 1 3631 ? 157.050 145.672 126.211 1.00 75.72  ? 3631 ASN A OD1   1 
ATOM   16254 N ND2   . ASN A 1 3631 ? 158.740 146.943 126.967 1.00 75.72  ? 3631 ASN A ND2   1 
ATOM   16255 N N     . PRO A 1 3632 ? 156.311 144.239 130.743 1.00 70.15  ? 3632 PRO A N     1 
ATOM   16256 C CA    . PRO A 1 3632 ? 156.445 144.078 132.195 1.00 70.15  ? 3632 PRO A CA    1 
ATOM   16257 C C     . PRO A 1 3632 ? 157.370 145.135 132.779 1.00 70.15  ? 3632 PRO A C     1 
ATOM   16258 O O     . PRO A 1 3632 ? 158.351 145.543 132.155 1.00 70.15  ? 3632 PRO A O     1 
ATOM   16259 C CB    . PRO A 1 3632 ? 157.030 142.668 132.346 1.00 70.15  ? 3632 PRO A CB    1 
ATOM   16260 C CG    . PRO A 1 3632 ? 157.575 142.321 130.998 1.00 70.15  ? 3632 PRO A CG    1 
ATOM   16261 C CD    . PRO A 1 3632 ? 156.699 143.022 130.015 1.00 70.15  ? 3632 PRO A CD    1 
ATOM   16262 N N     . LEU A 1 3633 ? 157.045 145.578 133.991 1.00 64.00  ? 3633 LEU A N     1 
ATOM   16263 C CA    . LEU A 1 3633 ? 157.789 146.633 134.666 1.00 64.00  ? 3633 LEU A CA    1 
ATOM   16264 C C     . LEU A 1 3633 ? 158.194 146.155 136.051 1.00 64.00  ? 3633 LEU A C     1 
ATOM   16265 O O     . LEU A 1 3633 ? 157.397 145.524 136.750 1.00 64.00  ? 3633 LEU A O     1 
ATOM   16266 C CB    . LEU A 1 3633 ? 156.952 147.913 134.769 1.00 64.00  ? 3633 LEU A CB    1 
ATOM   16267 C CG    . LEU A 1 3633 ? 157.608 149.123 135.434 1.00 64.00  ? 3633 LEU A CG    1 
ATOM   16268 C CD1   . LEU A 1 3633 ? 158.742 149.659 134.574 1.00 64.00  ? 3633 LEU A CD1   1 
ATOM   16269 C CD2   . LEU A 1 3633 ? 156.577 150.205 135.708 1.00 64.00  ? 3633 LEU A CD2   1 
ATOM   16270 N N     . LEU A 1 3634 ? 159.429 146.452 136.443 1.00 58.82  ? 3634 LEU A N     1 
ATOM   16271 C CA    . LEU A 1 3634 ? 159.935 146.130 137.770 1.00 58.82  ? 3634 LEU A CA    1 
ATOM   16272 C C     . LEU A 1 3634 ? 160.301 147.420 138.489 1.00 58.82  ? 3634 LEU A C     1 
ATOM   16273 O O     . LEU A 1 3634 ? 160.946 148.298 137.907 1.00 58.82  ? 3634 LEU A O     1 
ATOM   16274 C CB    . LEU A 1 3634 ? 161.147 145.199 137.687 1.00 58.82  ? 3634 LEU A CB    1 
ATOM   16275 C CG    . LEU A 1 3634 ? 161.696 144.665 139.013 1.00 58.82  ? 3634 LEU A CG    1 
ATOM   16276 C CD1   . LEU A 1 3634 ? 162.115 143.217 138.858 1.00 58.82  ? 3634 LEU A CD1   1 
ATOM   16277 C CD2   . LEU A 1 3634 ? 162.868 145.501 139.503 1.00 58.82  ? 3634 LEU A CD2   1 
ATOM   16278 N N     . VAL A 1 3635 ? 159.892 147.530 139.750 1.00 59.74  ? 3635 VAL A N     1 
ATOM   16279 C CA    . VAL A 1 3635 ? 160.126 148.720 140.559 1.00 59.74  ? 3635 VAL A CA    1 
ATOM   16280 C C     . VAL A 1 3635 ? 160.899 148.315 141.804 1.00 59.74  ? 3635 VAL A C     1 
ATOM   16281 O O     . VAL A 1 3635 ? 160.519 147.362 142.494 1.00 59.74  ? 3635 VAL A O     1 
ATOM   16282 C CB    . VAL A 1 3635 ? 158.808 149.417 140.941 1.00 59.74  ? 3635 VAL A CB    1 
ATOM   16283 C CG1   . VAL A 1 3635 ? 159.088 150.799 141.504 1.00 59.74  ? 3635 VAL A CG1   1 
ATOM   16284 C CG2   . VAL A 1 3635 ? 157.882 149.501 139.740 1.00 59.74  ? 3635 VAL A CG2   1 
ATOM   16285 N N     . GLN A 1 3636 ? 161.977 149.035 142.089 1.00 68.73  ? 3636 GLN A N     1 
ATOM   16286 C CA    . GLN A 1 3636 ? 162.770 148.822 143.289 1.00 68.73  ? 3636 GLN A CA    1 
ATOM   16287 C C     . GLN A 1 3636 ? 162.547 149.958 144.281 1.00 68.73  ? 3636 GLN A C     1 
ATOM   16288 O O     . GLN A 1 3636 ? 161.921 150.975 143.972 1.00 68.73  ? 3636 GLN A O     1 
ATOM   16289 C CB    . GLN A 1 3636 ? 164.256 148.698 142.941 1.00 68.73  ? 3636 GLN A CB    1 
ATOM   16290 C CG    . GLN A 1 3636 ? 164.570 147.590 141.954 1.00 68.73  ? 3636 GLN A CG    1 
ATOM   16291 C CD    . GLN A 1 3636 ? 165.962 147.709 141.369 1.00 68.73  ? 3636 GLN A CD    1 
ATOM   16292 O OE1   . GLN A 1 3636 ? 166.130 147.832 140.155 1.00 68.73  ? 3636 GLN A OE1   1 
ATOM   16293 N NE2   . GLN A 1 3636 ? 166.971 147.675 142.231 1.00 68.73  ? 3636 GLN A NE2   1 
ATOM   16294 N N     . ASP A 1 3637 ? 163.077 149.769 145.490 1.00 72.74  ? 3637 ASP A N     1 
ATOM   16295 C CA    . ASP A 1 3637 ? 162.950 150.736 146.580 1.00 72.74  ? 3637 ASP A CA    1 
ATOM   16296 C C     . ASP A 1 3637 ? 161.480 151.075 146.838 1.00 72.74  ? 3637 ASP A C     1 
ATOM   16297 O O     . ASP A 1 3637 ? 161.050 152.227 146.759 1.00 72.74  ? 3637 ASP A O     1 
ATOM   16298 C CB    . ASP A 1 3637 ? 163.769 151.999 146.293 1.00 72.74  ? 3637 ASP A CB    1 
ATOM   16299 C CG    . ASP A 1 3637 ? 165.262 151.757 146.385 1.00 72.74  ? 3637 ASP A CG    1 
ATOM   16300 O OD1   . ASP A 1 3637 ? 165.675 150.578 146.384 1.00 72.74  ? 3637 ASP A OD1   1 
ATOM   16301 O OD2   . ASP A 1 3637 ? 166.023 152.744 146.460 1.00 72.74  ? 3637 ASP A OD2   1 
ATOM   16302 N N     . VAL A 1 3638 ? 160.713 150.036 147.163 1.00 66.21  ? 3638 VAL A N     1 
ATOM   16303 C CA    . VAL A 1 3638 ? 159.271 150.163 147.343 1.00 66.21  ? 3638 VAL A CA    1 
ATOM   16304 C C     . VAL A 1 3638 ? 158.985 150.768 148.713 1.00 66.21  ? 3638 VAL A C     1 
ATOM   16305 O O     . VAL A 1 3638 ? 157.825 150.994 149.077 1.00 66.21  ? 3638 VAL A O     1 
ATOM   16306 C CB    . VAL A 1 3638 ? 158.574 148.800 147.157 1.00 66.21  ? 3638 VAL A CB    1 
ATOM   16307 C CG1   . VAL A 1 3638 ? 158.887 147.877 148.313 1.00 66.21  ? 3638 VAL A CG1   1 
ATOM   16308 C CG2   . VAL A 1 3638 ? 157.067 148.965 146.960 1.00 66.21  ? 3638 VAL A CG2   1 
ATOM   16309 N N     . GLU A 1 3639 ? 160.042 151.044 149.482 1.00 70.83  ? 3639 GLU A N     1 
ATOM   16310 C CA    . GLU A 1 3639 ? 159.864 151.770 150.736 1.00 70.83  ? 3639 GLU A CA    1 
ATOM   16311 C C     . GLU A 1 3639 ? 159.270 153.149 150.483 1.00 70.83  ? 3639 GLU A C     1 
ATOM   16312 O O     . GLU A 1 3639 ? 158.346 153.576 151.185 1.00 70.83  ? 3639 GLU A O     1 
ATOM   16313 C CB    . GLU A 1 3639 ? 161.199 151.897 151.471 1.00 70.83  ? 3639 GLU A CB    1 
ATOM   16314 C CG    . GLU A 1 3639 ? 161.767 150.587 151.977 1.00 70.83  ? 3639 GLU A CG    1 
ATOM   16315 C CD    . GLU A 1 3639 ? 162.521 149.826 150.907 1.00 70.83  ? 3639 GLU A CD    1 
ATOM   16316 O OE1   . GLU A 1 3639 ? 162.653 150.352 149.783 1.00 70.83  ? 3639 GLU A OE1   1 
ATOM   16317 O OE2   . GLU A 1 3639 ? 162.982 148.701 151.189 1.00 70.83  ? 3639 GLU A OE2   1 
ATOM   16318 N N     . SER A 1 3640 ? 159.789 153.858 149.484 1.00 76.65  ? 3640 SER A N     1 
ATOM   16319 C CA    . SER A 1 3640 ? 159.222 155.134 149.057 1.00 76.65  ? 3640 SER A CA    1 
ATOM   16320 C C     . SER A 1 3640 ? 158.193 154.878 147.957 1.00 76.65  ? 3640 SER A C     1 
ATOM   16321 O O     . SER A 1 3640 ? 158.375 155.219 146.788 1.00 76.65  ? 3640 SER A O     1 
ATOM   16322 C CB    . SER A 1 3640 ? 160.328 156.077 148.594 1.00 76.65  ? 3640 SER A CB    1 
ATOM   16323 O OG    . SER A 1 3640 ? 161.211 155.423 147.700 1.00 76.65  ? 3640 SER A OG    1 
ATOM   16324 N N     . TYR A 1 3641 ? 157.096 154.246 148.365 1.00 70.54  ? 3641 TYR A N     1 
ATOM   16325 C CA    . TYR A 1 3641 ? 156.048 153.876 147.424 1.00 70.54  ? 3641 TYR A CA    1 
ATOM   16326 C C     . TYR A 1 3641 ? 155.400 155.116 146.821 1.00 70.54  ? 3641 TYR A C     1 
ATOM   16327 O O     . TYR A 1 3641 ? 155.111 156.091 147.520 1.00 70.54  ? 3641 TYR A O     1 
ATOM   16328 C CB    . TYR A 1 3641 ? 154.994 153.018 148.124 1.00 70.54  ? 3641 TYR A CB    1 
ATOM   16329 C CG    . TYR A 1 3641 ? 153.765 152.748 147.288 1.00 70.54  ? 3641 TYR A CG    1 
ATOM   16330 C CD1   . TYR A 1 3641 ? 153.868 152.150 146.040 1.00 70.54  ? 3641 TYR A CD1   1 
ATOM   16331 C CD2   . TYR A 1 3641 ? 152.502 153.088 147.750 1.00 70.54  ? 3641 TYR A CD2   1 
ATOM   16332 C CE1   . TYR A 1 3641 ? 152.746 151.901 145.274 1.00 70.54  ? 3641 TYR A CE1   1 
ATOM   16333 C CE2   . TYR A 1 3641 ? 151.374 152.844 146.992 1.00 70.54  ? 3641 TYR A CE2   1 
ATOM   16334 C CZ    . TYR A 1 3641 ? 151.502 152.250 145.755 1.00 70.54  ? 3641 TYR A CZ    1 
ATOM   16335 O OH    . TYR A 1 3641 ? 150.379 152.006 144.998 1.00 70.54  ? 3641 TYR A OH    1 
ATOM   16336 N N     . ASP A 1 3642 ? 155.173 155.071 145.510 1.00 76.36  ? 3642 ASP A N     1 
ATOM   16337 C CA    . ASP A 1 3642 ? 154.538 156.176 144.808 1.00 76.36  ? 3642 ASP A CA    1 
ATOM   16338 C C     . ASP A 1 3642 ? 153.029 155.979 144.813 1.00 76.36  ? 3642 ASP A C     1 
ATOM   16339 O O     . ASP A 1 3642 ? 152.549 154.958 144.301 1.00 76.36  ? 3642 ASP A O     1 
ATOM   16340 C CB    . ASP A 1 3642 ? 155.043 156.268 143.379 1.00 76.36  ? 3642 ASP A CB    1 
ATOM   16341 C CG    . ASP A 1 3642 ? 155.016 157.683 142.842 1.00 76.36  ? 3642 ASP A CG    1 
ATOM   16342 O OD1   . ASP A 1 3642 ? 153.992 158.373 143.032 1.00 76.36  ? 3642 ASP A OD1   1 
ATOM   16343 O OD2   . ASP A 1 3642 ? 156.016 158.104 142.224 1.00 76.36  ? 3642 ASP A OD2   1 
ATOM   16344 N N     . PRO A 1 3643 ? 152.252 156.908 145.372 1.00 71.12  ? 3643 PRO A N     1 
ATOM   16345 C CA    . PRO A 1 3643 ? 150.790 156.731 145.391 1.00 71.12  ? 3643 PRO A CA    1 
ATOM   16346 C C     . PRO A 1 3643 ? 150.161 156.679 144.010 1.00 71.12  ? 3643 PRO A C     1 
ATOM   16347 O O     . PRO A 1 3643 ? 148.997 156.277 143.894 1.00 71.12  ? 3643 PRO A O     1 
ATOM   16348 C CB    . PRO A 1 3643 ? 150.302 157.951 146.183 1.00 71.12  ? 3643 PRO A CB    1 
ATOM   16349 C CG    . PRO A 1 3643 ? 151.471 158.341 147.026 1.00 71.12  ? 3643 PRO A CG    1 
ATOM   16350 C CD    . PRO A 1 3643 ? 152.678 158.063 146.178 1.00 71.12  ? 3643 PRO A CD    1 
ATOM   16351 N N     . VAL A 1 3644 ? 150.886 157.078 142.962 1.00 72.03  ? 3644 VAL A N     1 
ATOM   16352 C CA    . VAL A 1 3644 ? 150.339 157.057 141.611 1.00 72.03  ? 3644 VAL A CA    1 
ATOM   16353 C C     . VAL A 1 3644 ? 150.052 155.633 141.146 1.00 72.03  ? 3644 VAL A C     1 
ATOM   16354 O O     . VAL A 1 3644 ? 149.318 155.435 140.172 1.00 72.03  ? 3644 VAL A O     1 
ATOM   16355 C CB    . VAL A 1 3644 ? 151.304 157.779 140.644 1.00 72.03  ? 3644 VAL A CB    1 
ATOM   16356 C CG1   . VAL A 1 3644 ? 152.578 156.968 140.450 1.00 72.03  ? 3644 VAL A CG1   1 
ATOM   16357 C CG2   . VAL A 1 3644 ? 150.627 158.090 139.316 1.00 72.03  ? 3644 VAL A CG2   1 
ATOM   16358 N N     . LEU A 1 3645 ? 150.603 154.630 141.829 1.00 65.78  ? 3645 LEU A N     1 
ATOM   16359 C CA    . LEU A 1 3645 ? 150.359 153.234 141.485 1.00 65.78  ? 3645 LEU A CA    1 
ATOM   16360 C C     . LEU A 1 3645 ? 149.056 152.694 142.057 1.00 65.78  ? 3645 LEU A C     1 
ATOM   16361 O O     . LEU A 1 3645 ? 148.740 151.524 141.823 1.00 65.78  ? 3645 LEU A O     1 
ATOM   16362 C CB    . LEU A 1 3645 ? 151.516 152.355 141.965 1.00 65.78  ? 3645 LEU A CB    1 
ATOM   16363 C CG    . LEU A 1 3645 ? 152.827 152.407 141.188 1.00 65.78  ? 3645 LEU A CG    1 
ATOM   16364 C CD1   . LEU A 1 3645 ? 153.816 151.429 141.783 1.00 65.78  ? 3645 LEU A CD1   1 
ATOM   16365 C CD2   . LEU A 1 3645 ? 152.579 152.081 139.733 1.00 65.78  ? 3645 LEU A CD2   1 
ATOM   16366 N N     . ASN A 1 3646 ? 148.308 153.497 142.810 1.00 61.22  ? 3646 ASN A N     1 
ATOM   16367 C CA    . ASN A 1 3646 ? 147.044 153.016 143.365 1.00 61.22  ? 3646 ASN A CA    1 
ATOM   16368 C C     . ASN A 1 3646 ? 146.055 152.570 142.294 1.00 61.22  ? 3646 ASN A C     1 
ATOM   16369 O O     . ASN A 1 3646 ? 145.462 151.487 142.451 1.00 61.22  ? 3646 ASN A O     1 
ATOM   16370 C CB    . ASN A 1 3646 ? 146.444 154.092 144.277 1.00 61.22  ? 3646 ASN A CB    1 
ATOM   16371 C CG    . ASN A 1 3646 ? 147.070 154.101 145.655 1.00 61.22  ? 3646 ASN A CG    1 
ATOM   16372 O OD1   . ASN A 1 3646 ? 147.219 153.057 146.289 1.00 61.22  ? 3646 ASN A OD1   1 
ATOM   16373 N ND2   . ASN A 1 3646 ? 147.445 155.284 146.127 1.00 61.22  ? 3646 ASN A ND2   1 
ATOM   16374 N N     . PRO A 1 3647 ? 145.812 153.324 141.212 1.00 60.30  ? 3647 PRO A N     1 
ATOM   16375 C CA    . PRO A 1 3647 ? 144.865 152.834 140.195 1.00 60.30  ? 3647 PRO A CA    1 
ATOM   16376 C C     . PRO A 1 3647 ? 145.274 151.523 139.545 1.00 60.30  ? 3647 PRO A C     1 
ATOM   16377 O O     . PRO A 1 3647 ? 144.398 150.714 139.213 1.00 60.30  ? 3647 PRO A O     1 
ATOM   16378 C CB    . PRO A 1 3647 ? 144.829 153.980 139.174 1.00 60.30  ? 3647 PRO A CB    1 
ATOM   16379 C CG    . PRO A 1 3647 ? 145.222 155.180 139.947 1.00 60.30  ? 3647 PRO A CG    1 
ATOM   16380 C CD    . PRO A 1 3647 ? 146.264 154.692 140.901 1.00 60.30  ? 3647 PRO A CD    1 
ATOM   16381 N N     . VAL A 1 3648 ? 146.571 151.282 139.345 1.00 54.74  ? 3648 VAL A N     1 
ATOM   16382 C CA    . VAL A 1 3648 ? 146.985 150.055 138.671 1.00 54.74  ? 3648 VAL A CA    1 
ATOM   16383 C C     . VAL A 1 3648 ? 147.023 148.888 139.653 1.00 54.74  ? 3648 VAL A C     1 
ATOM   16384 O O     . VAL A 1 3648 ? 146.733 147.743 139.286 1.00 54.74  ? 3648 VAL A O     1 
ATOM   16385 C CB    . VAL A 1 3648 ? 148.334 150.256 137.954 1.00 54.74  ? 3648 VAL A CB    1 
ATOM   16386 C CG1   . VAL A 1 3648 ? 149.451 150.514 138.945 1.00 54.74  ? 3648 VAL A CG1   1 
ATOM   16387 C CG2   . VAL A 1 3648 ? 148.659 149.052 137.083 1.00 54.74  ? 3648 VAL A CG2   1 
ATOM   16388 N N     . LEU A 1 3649 ? 147.379 149.153 140.913 1.00 52.25  ? 3649 LEU A N     1 
ATOM   16389 C CA    . LEU A 1 3649 ? 147.338 148.098 141.921 1.00 52.25  ? 3649 LEU A CA    1 
ATOM   16390 C C     . LEU A 1 3649 ? 145.905 147.672 142.210 1.00 52.25  ? 3649 LEU A C     1 
ATOM   16391 O O     . LEU A 1 3649 ? 145.631 146.483 142.411 1.00 52.25  ? 3649 LEU A O     1 
ATOM   16392 C CB    . LEU A 1 3649 ? 148.034 148.558 143.202 1.00 52.25  ? 3649 LEU A CB    1 
ATOM   16393 C CG    . LEU A 1 3649 ? 149.558 148.667 143.140 1.00 52.25  ? 3649 LEU A CG    1 
ATOM   16394 C CD1   . LEU A 1 3649 ? 150.143 148.787 144.536 1.00 52.25  ? 3649 LEU A CD1   1 
ATOM   16395 C CD2   . LEU A 1 3649 ? 150.153 147.474 142.410 1.00 52.25  ? 3649 LEU A CD2   1 
ATOM   16396 N N     . ASN A 1 3650 ? 144.974 148.628 142.236 1.00 53.49  ? 3650 ASN A N     1 
ATOM   16397 C CA    . ASN A 1 3650 ? 143.567 148.299 142.419 1.00 53.49  ? 3650 ASN A CA    1 
ATOM   16398 C C     . ASN A 1 3650 ? 142.958 147.624 141.199 1.00 53.49  ? 3650 ASN A C     1 
ATOM   16399 O O     . ASN A 1 3650 ? 141.837 147.111 141.295 1.00 53.49  ? 3650 ASN A O     1 
ATOM   16400 C CB    . ASN A 1 3650 ? 142.773 149.562 142.757 1.00 53.49  ? 3650 ASN A CB    1 
ATOM   16401 C CG    . ASN A 1 3650 ? 142.987 150.020 144.184 1.00 53.49  ? 3650 ASN A CG    1 
ATOM   16402 O OD1   . ASN A 1 3650 ? 143.680 149.364 144.961 1.00 53.49  ? 3650 ASN A OD1   1 
ATOM   16403 N ND2   . ASN A 1 3650 ? 142.391 151.152 144.537 1.00 53.49  ? 3650 ASN A ND2   1 
ATOM   16404 N N     . ARG A 1 3651 ? 143.662 147.614 140.065 1.00 55.54  ? 3651 ARG A N     1 
ATOM   16405 C CA    . ARG A 1 3651 ? 143.176 147.015 138.822 1.00 55.54  ? 3651 ARG A CA    1 
ATOM   16406 C C     . ARG A 1 3651 ? 141.840 147.611 138.390 1.00 55.54  ? 3651 ARG A C     1 
ATOM   16407 O O     . ARG A 1 3651 ? 140.969 146.903 137.877 1.00 55.54  ? 3651 ARG A O     1 
ATOM   16408 C CB    . ARG A 1 3651 ? 143.069 145.492 138.938 1.00 55.54  ? 3651 ARG A CB    1 
ATOM   16409 C CG    . ARG A 1 3651 ? 144.327 144.818 139.457 1.00 55.54  ? 3651 ARG A CG    1 
ATOM   16410 C CD    . ARG A 1 3651 ? 144.045 143.387 139.889 1.00 55.54  ? 3651 ARG A CD    1 
ATOM   16411 N NE    . ARG A 1 3651 ? 144.258 142.436 138.804 1.00 55.54  ? 3651 ARG A NE    1 
ATOM   16412 C CZ    . ARG A 1 3651 ? 145.449 142.048 138.368 1.00 55.54  ? 3651 ARG A CZ    1 
ATOM   16413 N NH1   . ARG A 1 3651 ? 146.566 142.497 138.915 1.00 55.54  ? 3651 ARG A NH1   1 
ATOM   16414 N NH2   . ARG A 1 3651 ? 145.520 141.183 137.360 1.00 55.54  ? 3651 ARG A NH2   1 
ATOM   16415 N N     . GLU A 1 3652 ? 141.666 148.913 138.595 1.00 71.13  ? 3652 GLU A N     1 
ATOM   16416 C CA    . GLU A 1 3652 ? 140.445 149.578 138.164 1.00 71.13  ? 3652 GLU A CA    1 
ATOM   16417 C C     . GLU A 1 3652 ? 140.415 149.690 136.645 1.00 71.13  ? 3652 GLU A C     1 
ATOM   16418 O O     . GLU A 1 3652 ? 141.395 150.098 136.015 1.00 71.13  ? 3652 GLU A O     1 
ATOM   16419 C CB    . GLU A 1 3652 ? 140.340 150.963 138.798 1.00 71.13  ? 3652 GLU A CB    1 
ATOM   16420 C CG    . GLU A 1 3652 ? 139.755 150.957 140.200 1.00 71.13  ? 3652 GLU A CG    1 
ATOM   16421 C CD    . GLU A 1 3652 ? 139.076 152.265 140.553 1.00 71.13  ? 3652 GLU A CD    1 
ATOM   16422 O OE1   . GLU A 1 3652 ? 139.375 153.286 139.900 1.00 71.13  ? 3652 GLU A OE1   1 
ATOM   16423 O OE2   . GLU A 1 3652 ? 138.242 152.272 141.483 1.00 71.13  ? 3652 GLU A OE2   1 
ATOM   16424 N N     . VAL A 1 3653 ? 139.280 149.324 136.056 1.00 84.91  ? 3653 VAL A N     1 
ATOM   16425 C CA    . VAL A 1 3653 ? 139.109 149.317 134.609 1.00 84.91  ? 3653 VAL A CA    1 
ATOM   16426 C C     . VAL A 1 3653 ? 137.900 150.173 134.263 1.00 84.91  ? 3653 VAL A C     1 
ATOM   16427 O O     . VAL A 1 3653 ? 136.776 149.863 134.675 1.00 84.91  ? 3653 VAL A O     1 
ATOM   16428 C CB    . VAL A 1 3653 ? 138.936 147.892 134.057 1.00 84.91  ? 3653 VAL A CB    1 
ATOM   16429 C CG1   . VAL A 1 3653 ? 138.539 147.937 132.593 1.00 84.91  ? 3653 VAL A CG1   1 
ATOM   16430 C CG2   . VAL A 1 3653 ? 140.218 147.093 134.241 1.00 84.91  ? 3653 VAL A CG2   1 
ATOM   16431 N N     . ARG A 1 3654 ? 138.129 151.246 133.512 1.00 88.44  ? 3654 ARG A N     1 
ATOM   16432 C CA    . ARG A 1 3654 ? 137.049 152.086 132.996 1.00 88.44  ? 3654 ARG A CA    1 
ATOM   16433 C C     . ARG A 1 3654 ? 136.697 151.677 131.566 1.00 88.44  ? 3654 ARG A C     1 
ATOM   16434 O O     . ARG A 1 3654 ? 136.761 152.471 130.629 1.00 88.44  ? 3654 ARG A O     1 
ATOM   16435 C CB    . ARG A 1 3654 ? 137.444 153.559 133.066 1.00 88.44  ? 3654 ARG A CB    1 
ATOM   16436 C CG    . ARG A 1 3654 ? 137.794 154.053 134.458 1.00 88.44  ? 3654 ARG A CG    1 
ATOM   16437 C CD    . ARG A 1 3654 ? 136.579 154.645 135.154 1.00 88.44  ? 3654 ARG A CD    1 
ATOM   16438 N NE    . ARG A 1 3654 ? 135.806 153.633 135.864 1.00 88.44  ? 3654 ARG A NE    1 
ATOM   16439 C CZ    . ARG A 1 3654 ? 136.108 153.171 137.069 1.00 88.44  ? 3654 ARG A CZ    1 
ATOM   16440 N NH1   . ARG A 1 3654 ? 137.163 153.613 137.735 1.00 88.44  ? 3654 ARG A NH1   1 
ATOM   16441 N NH2   . ARG A 1 3654 ? 135.332 152.243 137.621 1.00 88.44  ? 3654 ARG A NH2   1 
ATOM   16442 N N     . ARG A 1 3655 ? 136.321 150.409 131.410 1.00 94.89  ? 3655 ARG A N     1 
ATOM   16443 C CA    . ARG A 1 3655 ? 136.027 149.876 130.086 1.00 94.89  ? 3655 ARG A CA    1 
ATOM   16444 C C     . ARG A 1 3655 ? 134.829 150.594 129.474 1.00 94.89  ? 3655 ARG A C     1 
ATOM   16445 O O     . ARG A 1 3655 ? 133.758 150.679 130.084 1.00 94.89  ? 3655 ARG A O     1 
ATOM   16446 C CB    . ARG A 1 3655 ? 135.783 148.368 130.170 1.00 94.89  ? 3655 ARG A CB    1 
ATOM   16447 C CG    . ARG A 1 3655 ? 134.651 147.944 131.093 1.00 94.89  ? 3655 ARG A CG    1 
ATOM   16448 C CD    . ARG A 1 3655 ? 134.531 146.430 131.154 1.00 94.89  ? 3655 ARG A CD    1 
ATOM   16449 N NE    . ARG A 1 3655 ? 135.677 145.819 131.818 1.00 94.89  ? 3655 ARG A NE    1 
ATOM   16450 C CZ    . ARG A 1 3655 ? 136.611 145.110 131.200 1.00 94.89  ? 3655 ARG A CZ    1 
ATOM   16451 N NH1   . ARG A 1 3655 ? 136.569 144.898 129.895 1.00 94.89  ? 3655 ARG A NH1   1 
ATOM   16452 N NH2   . ARG A 1 3655 ? 137.614 144.601 131.910 1.00 94.89  ? 3655 ARG A NH2   1 
ATOM   16453 N N     . THR A 1 3656 ? 135.024 151.134 128.272 1.00 98.51  ? 3656 THR A N     1 
ATOM   16454 C CA    . THR A 1 3656 ? 133.994 151.902 127.587 1.00 98.51  ? 3656 THR A CA    1 
ATOM   16455 C C     . THR A 1 3656 ? 134.297 151.906 126.096 1.00 98.51  ? 3656 THR A C     1 
ATOM   16456 O O     . THR A 1 3656 ? 135.451 152.073 125.692 1.00 98.51  ? 3656 THR A O     1 
ATOM   16457 C CB    . THR A 1 3656 ? 133.917 153.342 128.115 1.00 98.51  ? 3656 THR A CB    1 
ATOM   16458 O OG1   . THR A 1 3656 ? 133.683 153.329 129.529 1.00 98.51  ? 3656 THR A OG1   1 
ATOM   16459 C CG2   . THR A 1 3656 ? 132.791 154.108 127.433 1.00 98.51  ? 3656 THR A CG2   1 
ATOM   16460 N N     . GLY A 1 3657 ? 133.258 151.725 125.288 1.00 99.62  ? 3657 GLY A N     1 
ATOM   16461 C CA    . GLY A 1 3657 ? 133.415 151.730 123.843 1.00 99.62  ? 3657 GLY A CA    1 
ATOM   16462 C C     . GLY A 1 3657 ? 134.217 150.570 123.296 1.00 99.62  ? 3657 GLY A C     1 
ATOM   16463 O O     . GLY A 1 3657 ? 135.003 150.754 122.357 1.00 99.62  ? 3657 GLY A O     1 
ATOM   16464 N N     . GLY A 1 3658 ? 134.040 149.378 123.860 1.00 97.51  ? 3658 GLY A N     1 
ATOM   16465 C CA    . GLY A 1 3658 ? 134.730 148.206 123.361 1.00 97.51  ? 3658 GLY A CA    1 
ATOM   16466 C C     . GLY A 1 3658 ? 136.225 148.199 123.578 1.00 97.51  ? 3658 GLY A C     1 
ATOM   16467 O O     . GLY A 1 3658 ? 136.930 147.420 122.932 1.00 97.51  ? 3658 GLY A O     1 
ATOM   16468 N N     . ARG A 1 3659 ? 136.733 149.047 124.469 1.00 100.88 ? 3659 ARG A N     1 
ATOM   16469 C CA    . ARG A 1 3659 ? 138.156 149.105 124.763 1.00 100.88 ? 3659 ARG A CA    1 
ATOM   16470 C C     . ARG A 1 3659 ? 138.365 149.349 126.251 1.00 100.88 ? 3659 ARG A C     1 
ATOM   16471 O O     . ARG A 1 3659 ? 137.494 149.890 126.939 1.00 100.88 ? 3659 ARG A O     1 
ATOM   16472 C CB    . ARG A 1 3659 ? 138.857 150.191 123.935 1.00 100.88 ? 3659 ARG A CB    1 
ATOM   16473 C CG    . ARG A 1 3659 ? 138.366 151.604 124.187 1.00 100.88 ? 3659 ARG A CG    1 
ATOM   16474 C CD    . ARG A 1 3659 ? 139.134 152.585 123.321 1.00 100.88 ? 3659 ARG A CD    1 
ATOM   16475 N NE    . ARG A 1 3659 ? 140.547 152.600 123.679 1.00 100.88 ? 3659 ARG A NE    1 
ATOM   16476 C CZ    . ARG A 1 3659 ? 141.065 153.338 124.650 1.00 100.88 ? 3659 ARG A CZ    1 
ATOM   16477 N NH1   . ARG A 1 3659 ? 140.326 154.189 125.343 1.00 100.88 ? 3659 ARG A NH1   1 
ATOM   16478 N NH2   . ARG A 1 3659 ? 142.358 153.220 124.933 1.00 100.88 ? 3659 ARG A NH2   1 
ATOM   16479 N N     . VAL A 1 3660 ? 139.530 148.940 126.738 1.00 96.64  ? 3660 VAL A N     1 
ATOM   16480 C CA    . VAL A 1 3660 ? 139.854 148.971 128.159 1.00 96.64  ? 3660 VAL A CA    1 
ATOM   16481 C C     . VAL A 1 3660 ? 140.599 150.260 128.483 1.00 96.64  ? 3660 VAL A C     1 
ATOM   16482 O O     . VAL A 1 3660 ? 141.475 150.699 127.727 1.00 96.64  ? 3660 VAL A O     1 
ATOM   16483 C CB    . VAL A 1 3660 ? 140.671 147.724 128.551 1.00 96.64  ? 3660 VAL A CB    1 
ATOM   16484 C CG1   . VAL A 1 3660 ? 141.906 147.598 127.674 1.00 96.64  ? 3660 VAL A CG1   1 
ATOM   16485 C CG2   . VAL A 1 3660 ? 141.054 147.768 130.019 1.00 96.64  ? 3660 VAL A CG2   1 
ATOM   16486 N N     . LEU A 1 3661 ? 140.240 150.878 129.607 1.00 92.89  ? 3661 LEU A N     1 
ATOM   16487 C CA    . LEU A 1 3661 ? 140.790 152.165 130.005 1.00 92.89  ? 3661 LEU A CA    1 
ATOM   16488 C C     . LEU A 1 3661 ? 141.309 152.095 131.435 1.00 92.89  ? 3661 LEU A C     1 
ATOM   16489 O O     . LEU A 1 3661 ? 140.877 151.264 132.238 1.00 92.89  ? 3661 LEU A O     1 
ATOM   16490 C CB    . LEU A 1 3661 ? 139.744 153.285 129.905 1.00 92.89  ? 3661 LEU A CB    1 
ATOM   16491 C CG    . LEU A 1 3661 ? 139.385 153.863 128.536 1.00 92.89  ? 3661 LEU A CG    1 
ATOM   16492 C CD1   . LEU A 1 3661 ? 138.465 152.927 127.767 1.00 92.89  ? 3661 LEU A CD1   1 
ATOM   16493 C CD2   . LEU A 1 3661 ? 138.741 155.228 128.703 1.00 92.89  ? 3661 LEU A CD2   1 
ATOM   16494 N N     . ILE A 1 3662 ? 142.247 152.991 131.743 1.00 89.22  ? 3662 ILE A N     1 
ATOM   16495 C CA    . ILE A 1 3662 ? 142.737 153.178 133.103 1.00 89.22  ? 3662 ILE A CA    1 
ATOM   16496 C C     . ILE A 1 3662 ? 143.211 154.618 133.237 1.00 89.22  ? 3662 ILE A C     1 
ATOM   16497 O O     . ILE A 1 3662 ? 143.851 155.167 132.335 1.00 89.22  ? 3662 ILE A O     1 
ATOM   16498 C CB    . ILE A 1 3662 ? 143.859 152.171 133.461 1.00 89.22  ? 3662 ILE A CB    1 
ATOM   16499 C CG1   . ILE A 1 3662 ? 144.353 152.400 134.891 1.00 89.22  ? 3662 ILE A CG1   1 
ATOM   16500 C CG2   . ILE A 1 3662 ? 145.009 152.257 132.472 1.00 89.22  ? 3662 ILE A CG2   1 
ATOM   16501 C CD1   . ILE A 1 3662 ? 145.359 151.373 135.358 1.00 89.22  ? 3662 ILE A CD1   1 
ATOM   16502 N N     . THR A 1 3663 ? 142.886 155.234 134.369 1.00 90.37  ? 3663 THR A N     1 
ATOM   16503 C CA    . THR A 1 3663 ? 143.182 156.641 134.611 1.00 90.37  ? 3663 THR A CA    1 
ATOM   16504 C C     . THR A 1 3663 ? 144.426 156.751 135.483 1.00 90.37  ? 3663 THR A C     1 
ATOM   16505 O O     . THR A 1 3663 ? 144.476 156.178 136.577 1.00 90.37  ? 3663 THR A O     1 
ATOM   16506 C CB    . THR A 1 3663 ? 142.000 157.343 135.278 1.00 90.37  ? 3663 THR A CB    1 
ATOM   16507 O OG1   . THR A 1 3663 ? 141.768 156.769 136.571 1.00 90.37  ? 3663 THR A OG1   1 
ATOM   16508 C CG2   . THR A 1 3663 ? 140.745 157.193 134.430 1.00 90.37  ? 3663 THR A CG2   1 
ATOM   16509 N N     . LEU A 1 3664 ? 145.420 157.492 135.001 1.00 90.00  ? 3664 LEU A N     1 
ATOM   16510 C CA    . LEU A 1 3664 ? 146.674 157.715 135.716 1.00 90.00  ? 3664 LEU A CA    1 
ATOM   16511 C C     . LEU A 1 3664 ? 146.790 159.214 135.971 1.00 90.00  ? 3664 LEU A C     1 
ATOM   16512 O O     . LEU A 1 3664 ? 147.244 159.965 135.101 1.00 90.00  ? 3664 LEU A O     1 
ATOM   16513 C CB    . LEU A 1 3664 ? 147.861 157.187 134.917 1.00 90.00  ? 3664 LEU A CB    1 
ATOM   16514 C CG    . LEU A 1 3664 ? 149.194 157.083 135.658 1.00 90.00  ? 3664 LEU A CG    1 
ATOM   16515 C CD1   . LEU A 1 3664 ? 149.107 156.029 136.750 1.00 90.00  ? 3664 LEU A CD1   1 
ATOM   16516 C CD2   . LEU A 1 3664 ? 150.323 156.768 134.691 1.00 90.00  ? 3664 LEU A CD2   1 
ATOM   16517 N N     . GLY A 1 3665 ? 146.390 159.647 137.162 1.00 92.64  ? 3665 GLY A N     1 
ATOM   16518 C CA    . GLY A 1 3665 ? 146.342 161.073 137.435 1.00 92.64  ? 3665 GLY A CA    1 
ATOM   16519 C C     . GLY A 1 3665 ? 145.297 161.737 136.561 1.00 92.64  ? 3665 GLY A C     1 
ATOM   16520 O O     . GLY A 1 3665 ? 144.202 161.205 136.348 1.00 92.64  ? 3665 GLY A O     1 
ATOM   16521 N N     . ASP A 1 3666 ? 145.629 162.920 136.044 1.00 100.03 ? 3666 ASP A N     1 
ATOM   16522 C CA    . ASP A 1 3666 ? 144.759 163.579 135.080 1.00 100.03 ? 3666 ASP A CA    1 
ATOM   16523 C C     . ASP A 1 3666 ? 144.832 162.938 133.701 1.00 100.03 ? 3666 ASP A C     1 
ATOM   16524 O O     . ASP A 1 3666 ? 143.991 163.239 132.846 1.00 100.03 ? 3666 ASP A O     1 
ATOM   16525 C CB    . ASP A 1 3666 ? 145.112 165.065 134.978 1.00 100.03 ? 3666 ASP A CB    1 
ATOM   16526 C CG    . ASP A 1 3666 ? 144.726 165.843 136.222 1.00 100.03 ? 3666 ASP A CG    1 
ATOM   16527 O OD1   . ASP A 1 3666 ? 144.134 165.240 137.142 1.00 100.03 ? 3666 ASP A OD1   1 
ATOM   16528 O OD2   . ASP A 1 3666 ? 145.013 167.057 136.278 1.00 100.03 ? 3666 ASP A OD2   1 
ATOM   16529 N N     . GLN A 1 3667 ? 145.811 162.069 133.468 1.00 95.37  ? 3667 GLN A N     1 
ATOM   16530 C CA    . GLN A 1 3667 ? 145.977 161.424 132.176 1.00 95.37  ? 3667 GLN A CA    1 
ATOM   16531 C C     . GLN A 1 3667 ? 145.244 160.089 132.130 1.00 95.37  ? 3667 GLN A C     1 
ATOM   16532 O O     . GLN A 1 3667 ? 145.134 159.377 133.132 1.00 95.37  ? 3667 GLN A O     1 
ATOM   16533 C CB    . GLN A 1 3667 ? 147.462 161.212 131.876 1.00 95.37  ? 3667 GLN A CB    1 
ATOM   16534 C CG    . GLN A 1 3667 ? 147.768 160.922 130.417 1.00 95.37  ? 3667 GLN A CG    1 
ATOM   16535 C CD    . GLN A 1 3667 ? 147.130 161.925 129.479 1.00 95.37  ? 3667 GLN A CD    1 
ATOM   16536 O OE1   . GLN A 1 3667 ? 146.333 161.563 128.615 1.00 95.37  ? 3667 GLN A OE1   1 
ATOM   16537 N NE2   . GLN A 1 3667 ? 147.479 163.196 129.643 1.00 95.37  ? 3667 GLN A NE2   1 
ATOM   16538 N N     . ASP A 1 3668 ? 144.738 159.755 130.945 1.00 95.57  ? 3668 ASP A N     1 
ATOM   16539 C CA    . ASP A 1 3668 ? 144.105 158.471 130.683 1.00 95.57  ? 3668 ASP A CA    1 
ATOM   16540 C C     . ASP A 1 3668 ? 144.994 157.679 129.736 1.00 95.57  ? 3668 ASP A C     1 
ATOM   16541 O O     . ASP A 1 3668 ? 145.518 158.234 128.765 1.00 95.57  ? 3668 ASP A O     1 
ATOM   16542 C CB    . ASP A 1 3668 ? 142.707 158.654 130.086 1.00 95.57  ? 3668 ASP A CB    1 
ATOM   16543 C CG    . ASP A 1 3668 ? 142.096 157.348 129.615 1.00 95.57  ? 3668 ASP A CG    1 
ATOM   16544 O OD1   . ASP A 1 3668 ? 142.228 156.334 130.330 1.00 95.57  ? 3668 ASP A OD1   1 
ATOM   16545 O OD2   . ASP A 1 3668 ? 141.473 157.339 128.532 1.00 95.57  ? 3668 ASP A OD2   1 
ATOM   16546 N N     . ILE A 1 3669 ? 145.177 156.394 130.029 1.00 93.14  ? 3669 ILE A N     1 
ATOM   16547 C CA    . ILE A 1 3669 ? 146.071 155.529 129.268 1.00 93.14  ? 3669 ILE A CA    1 
ATOM   16548 C C     . ILE A 1 3669 ? 145.331 154.236 128.951 1.00 93.14  ? 3669 ILE A C     1 
ATOM   16549 O O     . ILE A 1 3669 ? 144.485 153.787 129.732 1.00 93.14  ? 3669 ILE A O     1 
ATOM   16550 C CB    . ILE A 1 3669 ? 147.375 155.241 130.044 1.00 93.14  ? 3669 ILE A CB    1 
ATOM   16551 C CG1   . ILE A 1 3669 ? 148.059 156.545 130.450 1.00 93.14  ? 3669 ILE A CG1   1 
ATOM   16552 C CG2   . ILE A 1 3669 ? 148.342 154.436 129.195 1.00 93.14  ? 3669 ILE A CG2   1 
ATOM   16553 C CD1   . ILE A 1 3669 ? 148.574 157.349 129.283 1.00 93.14  ? 3669 ILE A CD1   1 
ATOM   16554 N N     . ASP A 1 3670 ? 145.634 153.645 127.797 1.00 96.73  ? 3670 ASP A N     1 
ATOM   16555 C CA    . ASP A 1 3670 ? 145.054 152.357 127.443 1.00 96.73  ? 3670 ASP A CA    1 
ATOM   16556 C C     . ASP A 1 3670 ? 145.725 151.245 128.240 1.00 96.73  ? 3670 ASP A C     1 
ATOM   16557 O O     . ASP A 1 3670 ? 146.956 151.153 128.279 1.00 96.73  ? 3670 ASP A O     1 
ATOM   16558 C CB    . ASP A 1 3670 ? 145.211 152.099 125.946 1.00 96.73  ? 3670 ASP A CB    1 
ATOM   16559 C CG    . ASP A 1 3670 ? 144.657 150.752 125.525 1.00 96.73  ? 3670 ASP A CG    1 
ATOM   16560 O OD1   . ASP A 1 3670 ? 145.387 149.744 125.626 1.00 96.73  ? 3670 ASP A OD1   1 
ATOM   16561 O OD2   . ASP A 1 3670 ? 143.490 150.703 125.081 1.00 96.73  ? 3670 ASP A OD2   1 
ATOM   16562 N N     . LEU A 1 3671 ? 144.917 150.381 128.853 1.00 90.69  ? 3671 LEU A N     1 
ATOM   16563 C CA    . LEU A 1 3671 ? 145.428 149.292 129.687 1.00 90.69  ? 3671 LEU A CA    1 
ATOM   16564 C C     . LEU A 1 3671 ? 145.777 148.120 128.779 1.00 90.69  ? 3671 LEU A C     1 
ATOM   16565 O O     . LEU A 1 3671 ? 144.948 147.255 128.495 1.00 90.69  ? 3671 LEU A O     1 
ATOM   16566 C CB    . LEU A 1 3671 ? 144.406 148.900 130.746 1.00 90.69  ? 3671 LEU A CB    1 
ATOM   16567 C CG    . LEU A 1 3671 ? 144.821 147.834 131.763 1.00 90.69  ? 3671 LEU A CG    1 
ATOM   16568 C CD1   . LEU A 1 3671 ? 146.113 148.226 132.467 1.00 90.69  ? 3671 LEU A CD1   1 
ATOM   16569 C CD2   . LEU A 1 3671 ? 143.706 147.588 132.766 1.00 90.69  ? 3671 LEU A CD2   1 
ATOM   16570 N N     . SER A 1 3672 ? 147.023 148.091 128.320 1.00 86.78  ? 3672 SER A N     1 
ATOM   16571 C CA    . SER A 1 3672 ? 147.449 147.046 127.403 1.00 86.78  ? 3672 SER A CA    1 
ATOM   16572 C C     . SER A 1 3672 ? 147.418 145.687 128.098 1.00 86.78  ? 3672 SER A C     1 
ATOM   16573 O O     . SER A 1 3672 ? 147.735 145.590 129.289 1.00 86.78  ? 3672 SER A O     1 
ATOM   16574 C CB    . SER A 1 3672 ? 148.857 147.331 126.881 1.00 86.78  ? 3672 SER A CB    1 
ATOM   16575 O OG    . SER A 1 3672 ? 149.349 146.240 126.123 1.00 86.78  ? 3672 SER A OG    1 
ATOM   16576 N N     . PRO A 1 3673 ? 147.039 144.625 127.393 1.00 82.16  ? 3673 PRO A N     1 
ATOM   16577 C CA    . PRO A 1 3673 ? 147.070 143.287 127.995 1.00 82.16  ? 3673 PRO A CA    1 
ATOM   16578 C C     . PRO A 1 3673 ? 148.500 142.794 128.157 1.00 82.16  ? 3673 PRO A C     1 
ATOM   16579 O O     . PRO A 1 3673 ? 149.461 143.390 127.666 1.00 82.16  ? 3673 PRO A O     1 
ATOM   16580 C CB    . PRO A 1 3673 ? 146.291 142.425 126.999 1.00 82.16  ? 3673 PRO A CB    1 
ATOM   16581 C CG    . PRO A 1 3673 ? 146.403 143.149 125.700 1.00 82.16  ? 3673 PRO A CG    1 
ATOM   16582 C CD    . PRO A 1 3673 ? 146.504 144.612 126.021 1.00 82.16  ? 3673 PRO A CD    1 
ATOM   16583 N N     . SER A 1 3674 ? 148.625 141.672 128.869 1.00 75.58  ? 3674 SER A N     1 
ATOM   16584 C CA    . SER A 1 3674 ? 149.919 141.042 129.142 1.00 75.58  ? 3674 SER A CA    1 
ATOM   16585 C C     . SER A 1 3674 ? 150.875 142.014 129.828 1.00 75.58  ? 3674 SER A C     1 
ATOM   16586 O O     . SER A 1 3674 ? 152.073 142.046 129.538 1.00 75.58  ? 3674 SER A O     1 
ATOM   16587 C CB    . SER A 1 3674 ? 150.544 140.474 127.865 1.00 75.58  ? 3674 SER A CB    1 
ATOM   16588 O OG    . SER A 1 3674 ? 150.950 141.510 126.986 1.00 75.58  ? 3674 SER A OG    1 
ATOM   16589 N N     . PHE A 1 3675 ? 150.341 142.816 130.745 1.00 64.40  ? 3675 PHE A N     1 
ATOM   16590 C CA    . PHE A 1 3675 ? 151.121 143.780 131.510 1.00 64.40  ? 3675 PHE A CA    1 
ATOM   16591 C C     . PHE A 1 3675 ? 151.176 143.326 132.962 1.00 64.40  ? 3675 PHE A C     1 
ATOM   16592 O O     . PHE A 1 3675 ? 150.133 143.139 133.597 1.00 64.40  ? 3675 PHE A O     1 
ATOM   16593 C CB    . PHE A 1 3675 ? 150.515 145.180 131.409 1.00 64.40  ? 3675 PHE A CB    1 
ATOM   16594 C CG    . PHE A 1 3675 ? 150.948 146.106 132.507 1.00 64.40  ? 3675 PHE A CG    1 
ATOM   16595 C CD1   . PHE A 1 3675 ? 152.252 146.565 132.573 1.00 64.40  ? 3675 PHE A CD1   1 
ATOM   16596 C CD2   . PHE A 1 3675 ? 150.050 146.518 133.476 1.00 64.40  ? 3675 PHE A CD2   1 
ATOM   16597 C CE1   . PHE A 1 3675 ? 152.651 147.418 133.585 1.00 64.40  ? 3675 PHE A CE1   1 
ATOM   16598 C CE2   . PHE A 1 3675 ? 150.443 147.369 134.490 1.00 64.40  ? 3675 PHE A CE2   1 
ATOM   16599 C CZ    . PHE A 1 3675 ? 151.745 147.820 134.544 1.00 64.40  ? 3675 PHE A CZ    1 
ATOM   16600 N N     . VAL A 1 3676 ? 152.388 143.149 133.480 1.00 55.38  ? 3676 VAL A N     1 
ATOM   16601 C CA    . VAL A 1 3676 ? 152.610 142.749 134.863 1.00 55.38  ? 3676 VAL A CA    1 
ATOM   16602 C C     . VAL A 1 3676 ? 153.657 143.669 135.474 1.00 55.38  ? 3676 VAL A C     1 
ATOM   16603 O O     . VAL A 1 3676 ? 154.599 144.091 134.795 1.00 55.38  ? 3676 VAL A O     1 
ATOM   16604 C CB    . VAL A 1 3676 ? 153.043 141.270 134.974 1.00 55.38  ? 3676 VAL A CB    1 
ATOM   16605 C CG1   . VAL A 1 3676 ? 151.954 140.354 134.441 1.00 55.38  ? 3676 VAL A CG1   1 
ATOM   16606 C CG2   . VAL A 1 3676 ? 154.339 141.035 134.221 1.00 55.38  ? 3676 VAL A CG2   1 
ATOM   16607 N N     . ILE A 1 3677 ? 153.479 143.998 136.750 1.00 49.82  ? 3677 ILE A N     1 
ATOM   16608 C CA    . ILE A 1 3677 ? 154.418 144.836 137.485 1.00 49.82  ? 3677 ILE A CA    1 
ATOM   16609 C C     . ILE A 1 3677 ? 154.851 144.086 138.737 1.00 49.82  ? 3677 ILE A C     1 
ATOM   16610 O O     . ILE A 1 3677 ? 154.022 143.477 139.422 1.00 49.82  ? 3677 ILE A O     1 
ATOM   16611 C CB    . ILE A 1 3677 ? 153.813 146.212 137.836 1.00 49.82  ? 3677 ILE A CB    1 
ATOM   16612 C CG1   . ILE A 1 3677 ? 154.850 147.098 138.529 1.00 49.82  ? 3677 ILE A CG1   1 
ATOM   16613 C CG2   . ILE A 1 3677 ? 152.560 146.071 138.682 1.00 49.82  ? 3677 ILE A CG2   1 
ATOM   16614 C CD1   . ILE A 1 3677 ? 154.431 148.547 138.639 1.00 49.82  ? 3677 ILE A CD1   1 
ATOM   16615 N N     . PHE A 1 3678 ? 156.151 144.103 139.016 1.00 46.45  ? 3678 PHE A N     1 
ATOM   16616 C CA    . PHE A 1 3678 ? 156.735 143.361 140.130 1.00 46.45  ? 3678 PHE A CA    1 
ATOM   16617 C C     . PHE A 1 3678 ? 157.449 144.345 141.050 1.00 46.45  ? 3678 PHE A C     1 
ATOM   16618 O O     . PHE A 1 3678 ? 158.607 144.699 140.812 1.00 46.45  ? 3678 PHE A O     1 
ATOM   16619 C CB    . PHE A 1 3678 ? 157.695 142.290 139.622 1.00 46.45  ? 3678 PHE A CB    1 
ATOM   16620 C CG    . PHE A 1 3678 ? 157.038 141.233 138.787 1.00 46.45  ? 3678 PHE A CG    1 
ATOM   16621 C CD1   . PHE A 1 3678 ? 156.118 140.364 139.343 1.00 46.45  ? 3678 PHE A CD1   1 
ATOM   16622 C CD2   . PHE A 1 3678 ? 157.344 141.107 137.444 1.00 46.45  ? 3678 PHE A CD2   1 
ATOM   16623 C CE1   . PHE A 1 3678 ? 155.513 139.390 138.575 1.00 46.45  ? 3678 PHE A CE1   1 
ATOM   16624 C CE2   . PHE A 1 3678 ? 156.743 140.135 136.672 1.00 46.45  ? 3678 PHE A CE2   1 
ATOM   16625 C CZ    . PHE A 1 3678 ? 155.826 139.276 137.238 1.00 46.45  ? 3678 PHE A CZ    1 
ATOM   16626 N N     . LEU A 1 3679 ? 156.759 144.784 142.097 1.00 42.46  ? 3679 LEU A N     1 
ATOM   16627 C CA    . LEU A 1 3679 ? 157.397 145.611 143.110 1.00 42.46  ? 3679 LEU A CA    1 
ATOM   16628 C C     . LEU A 1 3679 ? 158.464 144.806 143.839 1.00 42.46  ? 3679 LEU A C     1 
ATOM   16629 O O     . LEU A 1 3679 ? 158.282 143.619 144.124 1.00 42.46  ? 3679 LEU A O     1 
ATOM   16630 C CB    . LEU A 1 3679 ? 156.361 146.137 144.100 1.00 42.46  ? 3679 LEU A CB    1 
ATOM   16631 C CG    . LEU A 1 3679 ? 155.203 146.941 143.508 1.00 42.46  ? 3679 LEU A CG    1 
ATOM   16632 C CD1   . LEU A 1 3679 ? 154.362 147.563 144.610 1.00 42.46  ? 3679 LEU A CD1   1 
ATOM   16633 C CD2   . LEU A 1 3679 ? 155.720 148.009 142.559 1.00 42.46  ? 3679 LEU A CD2   1 
ATOM   16634 N N     . SER A 1 3680 ? 159.586 145.453 144.140 1.00 46.87  ? 3680 SER A N     1 
ATOM   16635 C CA    . SER A 1 3680 ? 160.708 144.779 144.774 1.00 46.87  ? 3680 SER A CA    1 
ATOM   16636 C C     . SER A 1 3680 ? 161.297 145.681 145.848 1.00 46.87  ? 3680 SER A C     1 
ATOM   16637 O O     . SER A 1 3680 ? 161.051 146.889 145.879 1.00 46.87  ? 3680 SER A O     1 
ATOM   16638 C CB    . SER A 1 3680 ? 161.785 144.392 143.753 1.00 46.87  ? 3680 SER A CB    1 
ATOM   16639 O OG    . SER A 1 3680 ? 162.972 143.964 144.399 1.00 46.87  ? 3680 SER A OG    1 
ATOM   16640 N N     . THR A 1 3681 ? 162.082 145.075 146.736 1.00 49.95  ? 3681 THR A N     1 
ATOM   16641 C CA    . THR A 1 3681 ? 162.713 145.813 147.820 1.00 49.95  ? 3681 THR A CA    1 
ATOM   16642 C C     . THR A 1 3681 ? 164.007 145.118 148.217 1.00 49.95  ? 3681 THR A C     1 
ATOM   16643 O O     . THR A 1 3681 ? 164.251 143.962 147.864 1.00 49.95  ? 3681 THR A O     1 
ATOM   16644 C CB    . THR A 1 3681 ? 161.790 145.942 149.035 1.00 49.95  ? 3681 THR A CB    1 
ATOM   16645 O OG1   . THR A 1 3681 ? 162.274 146.981 149.892 1.00 49.95  ? 3681 THR A OG1   1 
ATOM   16646 C CG2   . THR A 1 3681 ? 161.749 144.642 149.812 1.00 49.95  ? 3681 THR A CG2   1 
ATOM   16647 N N     . ARG A 1 3682 ? 164.835 145.849 148.961 1.00 53.26  ? 3682 ARG A N     1 
ATOM   16648 C CA    . ARG A 1 3682 ? 166.126 145.355 149.416 1.00 53.26  ? 3682 ARG A CA    1 
ATOM   16649 C C     . ARG A 1 3682 ? 166.169 145.091 150.913 1.00 53.26  ? 3682 ARG A C     1 
ATOM   16650 O O     . ARG A 1 3682 ? 166.927 144.219 151.352 1.00 53.26  ? 3682 ARG A O     1 
ATOM   16651 C CB    . ARG A 1 3682 ? 167.230 146.360 149.060 1.00 53.26  ? 3682 ARG A CB    1 
ATOM   16652 C CG    . ARG A 1 3682 ? 168.565 145.732 148.710 1.00 53.26  ? 3682 ARG A CG    1 
ATOM   16653 C CD    . ARG A 1 3682 ? 168.488 145.034 147.366 1.00 53.26  ? 3682 ARG A CD    1 
ATOM   16654 N NE    . ARG A 1 3682 ? 169.663 144.213 147.109 1.00 53.26  ? 3682 ARG A NE    1 
ATOM   16655 C CZ    . ARG A 1 3682 ? 169.690 142.897 147.262 1.00 53.26  ? 3682 ARG A CZ    1 
ATOM   16656 N NH1   . ARG A 1 3682 ? 168.622 142.228 147.670 1.00 53.26  ? 3682 ARG A NH1   1 
ATOM   16657 N NH2   . ARG A 1 3682 ? 170.813 142.235 147.005 1.00 53.26  ? 3682 ARG A NH2   1 
ATOM   16658 N N     . ASP A 1 3683 ? 165.376 145.814 151.703 1.00 57.12  ? 3683 ASP A N     1 
ATOM   16659 C CA    . ASP A 1 3683 ? 165.459 145.765 153.157 1.00 57.12  ? 3683 ASP A CA    1 
ATOM   16660 C C     . ASP A 1 3683 ? 164.449 144.758 153.683 1.00 57.12  ? 3683 ASP A C     1 
ATOM   16661 O O     . ASP A 1 3683 ? 163.243 144.943 153.480 1.00 57.12  ? 3683 ASP A O     1 
ATOM   16662 C CB    . ASP A 1 3683 ? 165.180 147.149 153.732 1.00 57.12  ? 3683 ASP A CB    1 
ATOM   16663 C CG    . ASP A 1 3683 ? 165.446 147.241 155.228 1.00 57.12  ? 3683 ASP A CG    1 
ATOM   16664 O OD1   . ASP A 1 3683 ? 165.826 146.225 155.847 1.00 57.12  ? 3683 ASP A OD1   1 
ATOM   16665 O OD2   . ASP A 1 3683 ? 165.269 148.342 155.789 1.00 57.12  ? 3683 ASP A OD2   1 
ATOM   16666 N N     . PRO A 1 3684 ? 164.885 143.684 154.346 1.00 54.65  ? 3684 PRO A N     1 
ATOM   16667 C CA    . PRO A 1 3684 ? 163.910 142.710 154.875 1.00 54.65  ? 3684 PRO A CA    1 
ATOM   16668 C C     . PRO A 1 3684 ? 163.000 143.267 155.955 1.00 54.65  ? 3684 PRO A C     1 
ATOM   16669 O O     . PRO A 1 3684 ? 161.879 142.769 156.127 1.00 54.65  ? 3684 PRO A O     1 
ATOM   16670 C CB    . PRO A 1 3684 ? 164.803 141.583 155.399 1.00 54.65  ? 3684 PRO A CB    1 
ATOM   16671 C CG    . PRO A 1 3684 ? 166.084 142.252 155.746 1.00 54.65  ? 3684 PRO A CG    1 
ATOM   16672 C CD    . PRO A 1 3684 ? 166.270 143.370 154.764 1.00 54.65  ? 3684 PRO A CD    1 
ATOM   16673 N N     . THR A 1 3685 ? 163.441 144.282 156.695 1.00 55.92  ? 3685 THR A N     1 
ATOM   16674 C CA    . THR A 1 3685 ? 162.651 144.855 157.788 1.00 55.92  ? 3685 THR A CA    1 
ATOM   16675 C C     . THR A 1 3685 ? 162.128 146.227 157.361 1.00 55.92  ? 3685 THR A C     1 
ATOM   16676 O O     . THR A 1 3685 ? 162.765 147.262 157.572 1.00 55.92  ? 3685 THR A O     1 
ATOM   16677 C CB    . THR A 1 3685 ? 163.462 144.913 159.081 1.00 55.92  ? 3685 THR A CB    1 
ATOM   16678 O OG1   . THR A 1 3685 ? 162.731 145.595 160.095 1.00 55.92  ? 3685 THR A OG1   1 
ATOM   16679 C CG2   . THR A 1 3685 ? 164.834 145.566 158.866 1.00 55.92  ? 3685 THR A CG2   1 
ATOM   16680 N N     . VAL A 1 3686 ? 160.943 146.233 156.753 1.00 55.41  ? 3686 VAL A N     1 
ATOM   16681 C CA    . VAL A 1 3686 ? 160.266 147.452 156.327 1.00 55.41  ? 3686 VAL A CA    1 
ATOM   16682 C C     . VAL A 1 3686 ? 158.786 147.328 156.658 1.00 55.41  ? 3686 VAL A C     1 
ATOM   16683 O O     . VAL A 1 3686 ? 158.197 146.252 156.505 1.00 55.41  ? 3686 VAL A O     1 
ATOM   16684 C CB    . VAL A 1 3686 ? 160.473 147.723 154.826 1.00 55.41  ? 3686 VAL A CB    1 
ATOM   16685 C CG1   . VAL A 1 3686 ? 161.894 148.164 154.567 1.00 55.41  ? 3686 VAL A CG1   1 
ATOM   16686 C CG2   . VAL A 1 3686 ? 160.176 146.472 154.026 1.00 55.41  ? 3686 VAL A CG2   1 
ATOM   16687 N N     . GLU A 1 3687 ? 158.190 148.425 157.117 1.00 53.89  ? 3687 GLU A N     1 
ATOM   16688 C CA    . GLU A 1 3687 ? 156.795 148.450 157.551 1.00 53.89  ? 3687 GLU A CA    1 
ATOM   16689 C C     . GLU A 1 3687 ? 155.972 149.184 156.499 1.00 53.89  ? 3687 GLU A C     1 
ATOM   16690 O O     . GLU A 1 3687 ? 155.918 150.416 156.485 1.00 53.89  ? 3687 GLU A O     1 
ATOM   16691 C CB    . GLU A 1 3687 ? 156.671 149.116 158.919 1.00 53.89  ? 3687 GLU A CB    1 
ATOM   16692 C CG    . GLU A 1 3687 ? 155.286 149.026 159.543 1.00 53.89  ? 3687 GLU A CG    1 
ATOM   16693 C CD    . GLU A 1 3687 ? 154.622 147.683 159.314 1.00 53.89  ? 3687 GLU A CD    1 
ATOM   16694 O OE1   . GLU A 1 3687 ? 154.997 146.710 160.000 1.00 53.89  ? 3687 GLU A OE1   1 
ATOM   16695 O OE2   . GLU A 1 3687 ? 153.721 147.601 158.453 1.00 53.89  ? 3687 GLU A OE2   1 
ATOM   16696 N N     . PHE A 1 3688 ? 155.331 148.424 155.615 1.00 49.63  ? 3688 PHE A N     1 
ATOM   16697 C CA    . PHE A 1 3688 ? 154.463 149.029 154.620 1.00 49.63  ? 3688 PHE A CA    1 
ATOM   16698 C C     . PHE A 1 3688 ? 153.126 149.430 155.240 1.00 49.63  ? 3688 PHE A C     1 
ATOM   16699 O O     . PHE A 1 3688 ? 152.649 148.785 156.177 1.00 49.63  ? 3688 PHE A O     1 
ATOM   16700 C CB    . PHE A 1 3688 ? 154.216 148.065 153.467 1.00 49.63  ? 3688 PHE A CB    1 
ATOM   16701 C CG    . PHE A 1 3688 ? 155.466 147.567 152.814 1.00 49.63  ? 3688 PHE A CG    1 
ATOM   16702 C CD1   . PHE A 1 3688 ? 156.194 148.390 151.976 1.00 49.63  ? 3688 PHE A CD1   1 
ATOM   16703 C CD2   . PHE A 1 3688 ? 155.907 146.274 153.026 1.00 49.63  ? 3688 PHE A CD2   1 
ATOM   16704 C CE1   . PHE A 1 3688 ? 157.342 147.937 151.370 1.00 49.63  ? 3688 PHE A CE1   1 
ATOM   16705 C CE2   . PHE A 1 3688 ? 157.055 145.813 152.418 1.00 49.63  ? 3688 PHE A CE2   1 
ATOM   16706 C CZ    . PHE A 1 3688 ? 157.772 146.647 151.587 1.00 49.63  ? 3688 PHE A CZ    1 
ATOM   16707 N N     . PRO A 1 3689 ? 152.501 150.493 154.731 1.00 51.60  ? 3689 PRO A N     1 
ATOM   16708 C CA    . PRO A 1 3689 ? 151.166 150.842 155.204 1.00 51.60  ? 3689 PRO A CA    1 
ATOM   16709 C C     . PRO A 1 3689 ? 150.162 149.779 154.793 1.00 51.60  ? 3689 PRO A C     1 
ATOM   16710 O O     . PRO A 1 3689 ? 150.361 149.077 153.787 1.00 51.60  ? 3689 PRO A O     1 
ATOM   16711 C CB    . PRO A 1 3689 ? 150.881 152.184 154.506 1.00 51.60  ? 3689 PRO A CB    1 
ATOM   16712 C CG    . PRO A 1 3689 ? 151.744 152.162 153.295 1.00 51.60  ? 3689 PRO A CG    1 
ATOM   16713 C CD    . PRO A 1 3689 ? 152.985 151.421 153.695 1.00 51.60  ? 3689 PRO A CD    1 
ATOM   16714 N N     . PRO A 1 3690 ? 149.074 149.616 155.548 1.00 51.52  ? 3690 PRO A N     1 
ATOM   16715 C CA    . PRO A 1 3690 ? 148.068 148.610 155.167 1.00 51.52  ? 3690 PRO A CA    1 
ATOM   16716 C C     . PRO A 1 3690 ? 147.480 148.841 153.787 1.00 51.52  ? 3690 PRO A C     1 
ATOM   16717 O O     . PRO A 1 3690 ? 147.078 147.874 153.125 1.00 51.52  ? 3690 PRO A O     1 
ATOM   16718 C CB    . PRO A 1 3690 ? 147.004 148.745 156.265 1.00 51.52  ? 3690 PRO A CB    1 
ATOM   16719 C CG    . PRO A 1 3690 ? 147.725 149.357 157.422 1.00 51.52  ? 3690 PRO A CG    1 
ATOM   16720 C CD    . PRO A 1 3690 ? 148.749 150.273 156.824 1.00 51.52  ? 3690 PRO A CD    1 
ATOM   16721 N N     . ASP A 1 3691 ? 147.425 150.095 153.330 1.00 51.15  ? 3691 ASP A N     1 
ATOM   16722 C CA    . ASP A 1 3691 ? 146.928 150.372 151.987 1.00 51.15  ? 3691 ASP A CA    1 
ATOM   16723 C C     . ASP A 1 3691 ? 147.784 149.686 150.932 1.00 51.15  ? 3691 ASP A C     1 
ATOM   16724 O O     . ASP A 1 3691 ? 147.257 149.094 149.983 1.00 51.15  ? 3691 ASP A O     1 
ATOM   16725 C CB    . ASP A 1 3691 ? 146.888 151.881 151.745 1.00 51.15  ? 3691 ASP A CB    1 
ATOM   16726 C CG    . ASP A 1 3691 ? 145.861 152.584 152.610 1.00 51.15  ? 3691 ASP A CG    1 
ATOM   16727 O OD1   . ASP A 1 3691 ? 144.856 151.943 152.982 1.00 51.15  ? 3691 ASP A OD1   1 
ATOM   16728 O OD2   . ASP A 1 3691 ? 146.060 153.778 152.918 1.00 51.15  ? 3691 ASP A OD2   1 
ATOM   16729 N N     . LEU A 1 3692 ? 149.108 149.750 151.081 1.00 47.28  ? 3692 LEU A N     1 
ATOM   16730 C CA    . LEU A 1 3692 ? 149.984 149.039 150.157 1.00 47.28  ? 3692 LEU A CA    1 
ATOM   16731 C C     . LEU A 1 3692 ? 149.998 147.543 150.438 1.00 47.28  ? 3692 LEU A C     1 
ATOM   16732 O O     . LEU A 1 3692 ? 150.118 146.741 149.506 1.00 47.28  ? 3692 LEU A O     1 
ATOM   16733 C CB    . LEU A 1 3692 ? 151.402 149.606 150.229 1.00 47.28  ? 3692 LEU A CB    1 
ATOM   16734 C CG    . LEU A 1 3692 ? 152.448 148.933 149.338 1.00 47.28  ? 3692 LEU A CG    1 
ATOM   16735 C CD1   . LEU A 1 3692 ? 152.014 148.973 147.883 1.00 47.28  ? 3692 LEU A CD1   1 
ATOM   16736 C CD2   . LEU A 1 3692 ? 153.806 149.589 149.512 1.00 47.28  ? 3692 LEU A CD2   1 
ATOM   16737 N N     . CYS A 1 3693 ? 149.870 147.151 151.708 1.00 43.85  ? 3693 CYS A N     1 
ATOM   16738 C CA    . CYS A 1 3693 ? 149.902 145.734 152.056 1.00 43.85  ? 3693 CYS A CA    1 
ATOM   16739 C C     . CYS A 1 3693 ? 148.746 144.972 151.424 1.00 43.85  ? 3693 CYS A C     1 
ATOM   16740 O O     . CYS A 1 3693 ? 148.931 143.842 150.958 1.00 43.85  ? 3693 CYS A O     1 
ATOM   16741 C CB    . CYS A 1 3693 ? 149.876 145.564 153.575 1.00 43.85  ? 3693 CYS A CB    1 
ATOM   16742 S SG    . CYS A 1 3693 ? 151.417 145.997 154.409 1.00 43.85  ? 3693 CYS A SG    1 
ATOM   16743 N N     . SER A 1 3694 ? 147.552 145.565 151.400 1.00 39.67  ? 3694 SER A N     1 
ATOM   16744 C CA    . SER A 1 3694 ? 146.392 144.868 150.859 1.00 39.67  ? 3694 SER A CA    1 
ATOM   16745 C C     . SER A 1 3694 ? 146.458 144.701 149.347 1.00 39.67  ? 3694 SER A C     1 
ATOM   16746 O O     . SER A 1 3694 ? 145.848 143.770 148.814 1.00 39.67  ? 3694 SER A O     1 
ATOM   16747 C CB    . SER A 1 3694 ? 145.110 145.609 151.237 1.00 39.67  ? 3694 SER A CB    1 
ATOM   16748 O OG    . SER A 1 3694 ? 145.055 146.878 150.612 1.00 39.67  ? 3694 SER A OG    1 
ATOM   16749 N N     . ARG A 1 3695 ? 147.187 145.567 148.646 1.00 42.72  ? 3695 ARG A N     1 
ATOM   16750 C CA    . ARG A 1 3695 ? 147.183 145.584 147.190 1.00 42.72  ? 3695 ARG A CA    1 
ATOM   16751 C C     . ARG A 1 3695 ? 148.268 144.716 146.564 1.00 42.72  ? 3695 ARG A C     1 
ATOM   16752 O O     . ARG A 1 3695 ? 148.342 144.640 145.335 1.00 42.72  ? 3695 ARG A O     1 
ATOM   16753 C CB    . ARG A 1 3695 ? 147.328 147.021 146.679 1.00 42.72  ? 3695 ARG A CB    1 
ATOM   16754 C CG    . ARG A 1 3695 ? 146.122 147.903 146.945 1.00 42.72  ? 3695 ARG A CG    1 
ATOM   16755 C CD    . ARG A 1 3695 ? 146.490 149.374 146.854 1.00 42.72  ? 3695 ARG A CD    1 
ATOM   16756 N NE    . ARG A 1 3695 ? 145.314 150.234 146.864 1.00 42.72  ? 3695 ARG A NE    1 
ATOM   16757 C CZ    . ARG A 1 3695 ? 144.673 150.616 147.960 1.00 42.72  ? 3695 ARG A CZ    1 
ATOM   16758 N NH1   . ARG A 1 3695 ? 145.068 150.228 149.161 1.00 42.72  ? 3695 ARG A NH1   1 
ATOM   16759 N NH2   . ARG A 1 3695 ? 143.610 151.406 147.848 1.00 42.72  ? 3695 ARG A NH2   1 
ATOM   16760 N N     . VAL A 1 3696 ? 149.111 144.062 147.365 1.00 36.92  ? 3696 VAL A N     1 
ATOM   16761 C CA    . VAL A 1 3696 ? 150.200 143.248 146.841 1.00 36.92  ? 3696 VAL A CA    1 
ATOM   16762 C C     . VAL A 1 3696 ? 150.217 141.900 147.546 1.00 36.92  ? 3696 VAL A C     1 
ATOM   16763 O O     . VAL A 1 3696 ? 149.729 141.750 148.668 1.00 36.92  ? 3696 VAL A O     1 
ATOM   16764 C CB    . VAL A 1 3696 ? 151.574 143.936 146.997 1.00 36.92  ? 3696 VAL A CB    1 
ATOM   16765 C CG1   . VAL A 1 3696 ? 151.650 145.184 146.133 1.00 36.92  ? 3696 VAL A CG1   1 
ATOM   16766 C CG2   . VAL A 1 3696 ? 151.836 144.265 148.454 1.00 36.92  ? 3696 VAL A CG2   1 
ATOM   16767 N N     . THR A 1 3697 ? 150.793 140.912 146.867 1.00 32.02  ? 3697 THR A N     1 
ATOM   16768 C CA    . THR A 1 3697 ? 151.049 139.600 147.446 1.00 32.02  ? 3697 THR A CA    1 
ATOM   16769 C C     . THR A 1 3697 ? 152.506 139.552 147.882 1.00 32.02  ? 3697 THR A C     1 
ATOM   16770 O O     . THR A 1 3697 ? 153.408 139.513 147.039 1.00 32.02  ? 3697 THR A O     1 
ATOM   16771 C CB    . THR A 1 3697 ? 150.755 138.480 146.449 1.00 32.02  ? 3697 THR A CB    1 
ATOM   16772 O OG1   . THR A 1 3697 ? 151.332 138.806 145.179 1.00 32.02  ? 3697 THR A OG1   1 
ATOM   16773 C CG2   . THR A 1 3697 ? 149.258 138.289 146.284 1.00 32.02  ? 3697 THR A CG2   1 
ATOM   16774 N N     . PHE A 1 3698 ? 152.733 139.554 149.192 1.00 33.02  ? 3698 PHE A N     1 
ATOM   16775 C CA    . PHE A 1 3698 ? 154.085 139.607 149.728 1.00 33.02  ? 3698 PHE A CA    1 
ATOM   16776 C C     . PHE A 1 3698 ? 154.803 138.296 149.441 1.00 33.02  ? 3698 PHE A C     1 
ATOM   16777 O O     . PHE A 1 3698 ? 154.325 137.222 149.821 1.00 33.02  ? 3698 PHE A O     1 
ATOM   16778 C CB    . PHE A 1 3698 ? 154.054 139.884 151.227 1.00 33.02  ? 3698 PHE A CB    1 
ATOM   16779 C CG    . PHE A 1 3698 ? 153.812 141.321 151.573 1.00 33.02  ? 3698 PHE A CG    1 
ATOM   16780 C CD1   . PHE A 1 3698 ? 152.738 141.684 152.364 1.00 33.02  ? 3698 PHE A CD1   1 
ATOM   16781 C CD2   . PHE A 1 3698 ? 154.660 142.308 151.107 1.00 33.02  ? 3698 PHE A CD2   1 
ATOM   16782 C CE1   . PHE A 1 3698 ? 152.514 143.006 152.686 1.00 33.02  ? 3698 PHE A CE1   1 
ATOM   16783 C CE2   . PHE A 1 3698 ? 154.441 143.631 151.424 1.00 33.02  ? 3698 PHE A CE2   1 
ATOM   16784 C CZ    . PHE A 1 3698 ? 153.367 143.981 152.215 1.00 33.02  ? 3698 PHE A CZ    1 
ATOM   16785 N N     . VAL A 1 3699 ? 155.950 138.386 148.773 1.00 29.19  ? 3699 VAL A N     1 
ATOM   16786 C CA    . VAL A 1 3699 ? 156.764 137.218 148.467 1.00 29.19  ? 3699 VAL A CA    1 
ATOM   16787 C C     . VAL A 1 3699 ? 158.111 137.381 149.157 1.00 29.19  ? 3699 VAL A C     1 
ATOM   16788 O O     . VAL A 1 3699 ? 158.985 138.106 148.670 1.00 29.19  ? 3699 VAL A O     1 
ATOM   16789 C CB    . VAL A 1 3699 ? 156.929 137.036 146.949 1.00 29.19  ? 3699 VAL A CB    1 
ATOM   16790 C CG1   . VAL A 1 3699 ? 157.706 135.776 146.652 1.00 29.19  ? 3699 VAL A CG1   1 
ATOM   16791 C CG2   . VAL A 1 3699 ? 155.571 136.998 146.270 1.00 29.19  ? 3699 VAL A CG2   1 
ATOM   16792 N N     . ASN A 1 3700 ? 158.287 136.712 150.293 1.00 28.87  ? 3700 ASN A N     1 
ATOM   16793 C CA    . ASN A 1 3700 ? 159.463 136.905 151.130 1.00 28.87  ? 3700 ASN A CA    1 
ATOM   16794 C C     . ASN A 1 3700 ? 160.547 135.897 150.773 1.00 28.87  ? 3700 ASN A C     1 
ATOM   16795 O O     . ASN A 1 3700 ? 160.297 134.688 150.746 1.00 28.87  ? 3700 ASN A O     1 
ATOM   16796 C CB    . ASN A 1 3700 ? 159.093 136.775 152.607 1.00 28.87  ? 3700 ASN A CB    1 
ATOM   16797 C CG    . ASN A 1 3700 ? 159.962 137.631 153.501 1.00 28.87  ? 3700 ASN A CG    1 
ATOM   16798 O OD1   . ASN A 1 3700 ? 160.548 138.616 153.057 1.00 28.87  ? 3700 ASN A OD1   1 
ATOM   16799 N ND2   . ASN A 1 3700 ? 160.047 137.261 154.773 1.00 28.87  ? 3700 ASN A ND2   1 
ATOM   16800 N N     . PHE A 1 3701 ? 161.750 136.401 150.502 1.00 28.77  ? 3701 PHE A N     1 
ATOM   16801 C CA    . PHE A 1 3701 ? 162.916 135.570 150.242 1.00 28.77  ? 3701 PHE A CA    1 
ATOM   16802 C C     . PHE A 1 3701 ? 163.933 135.608 151.373 1.00 28.77  ? 3701 PHE A C     1 
ATOM   16803 O O     . PHE A 1 3701 ? 165.017 135.033 151.230 1.00 28.77  ? 3701 PHE A O     1 
ATOM   16804 C CB    . PHE A 1 3701 ? 163.594 136.001 148.937 1.00 28.77  ? 3701 PHE A CB    1 
ATOM   16805 C CG    . PHE A 1 3701 ? 162.789 135.708 147.708 1.00 28.77  ? 3701 PHE A CG    1 
ATOM   16806 C CD1   . PHE A 1 3701 ? 161.872 136.627 147.230 1.00 28.77  ? 3701 PHE A CD1   1 
ATOM   16807 C CD2   . PHE A 1 3701 ? 162.965 134.524 147.016 1.00 28.77  ? 3701 PHE A CD2   1 
ATOM   16808 C CE1   . PHE A 1 3701 ? 161.135 136.362 146.095 1.00 28.77  ? 3701 PHE A CE1   1 
ATOM   16809 C CE2   . PHE A 1 3701 ? 162.233 134.255 145.879 1.00 28.77  ? 3701 PHE A CE2   1 
ATOM   16810 C CZ    . PHE A 1 3701 ? 161.316 135.176 145.418 1.00 28.77  ? 3701 PHE A CZ    1 
ATOM   16811 N N     . THR A 1 3702 ? 163.619 136.271 152.484 1.00 28.83  ? 3702 THR A N     1 
ATOM   16812 C CA    . THR A 1 3702 ? 164.575 136.423 153.573 1.00 28.83  ? 3702 THR A CA    1 
ATOM   16813 C C     . THR A 1 3702 ? 164.932 135.072 154.177 1.00 28.83  ? 3702 THR A C     1 
ATOM   16814 O O     . THR A 1 3702 ? 164.055 134.260 154.484 1.00 28.83  ? 3702 THR A O     1 
ATOM   16815 C CB    . THR A 1 3702 ? 163.999 137.347 154.648 1.00 28.83  ? 3702 THR A CB    1 
ATOM   16816 O OG1   . THR A 1 3702 ? 163.710 138.626 154.073 1.00 28.83  ? 3702 THR A OG1   1 
ATOM   16817 C CG2   . THR A 1 3702 ? 164.989 137.525 155.787 1.00 28.83  ? 3702 THR A CG2   1 
ATOM   16818 N N     . VAL A 1 3703 ? 166.234 134.838 154.348 1.00 24.57  ? 3703 VAL A N     1 
ATOM   16819 C CA    . VAL A 1 3703 ? 166.702 133.589 154.931 1.00 24.57  ? 3703 VAL A CA    1 
ATOM   16820 C C     . VAL A 1 3703 ? 166.510 133.625 156.440 1.00 24.57  ? 3703 VAL A C     1 
ATOM   16821 O O     . VAL A 1 3703 ? 166.970 134.549 157.124 1.00 24.57  ? 3703 VAL A O     1 
ATOM   16822 C CB    . VAL A 1 3703 ? 168.175 133.346 154.565 1.00 24.57  ? 3703 VAL A CB    1 
ATOM   16823 C CG1   . VAL A 1 3703 ? 168.721 132.157 155.333 1.00 24.57  ? 3703 VAL A CG1   1 
ATOM   16824 C CG2   . VAL A 1 3703 ? 168.319 133.130 153.069 1.00 24.57  ? 3703 VAL A CG2   1 
ATOM   16825 N N     . THR A 1 3704 ? 165.828 132.613 156.967 1.00 25.85  ? 3704 THR A N     1 
ATOM   16826 C CA    . THR A 1 3704 ? 165.579 132.491 158.394 1.00 25.85  ? 3704 THR A CA    1 
ATOM   16827 C C     . THR A 1 3704 ? 166.205 131.200 158.900 1.00 25.85  ? 3704 THR A C     1 
ATOM   16828 O O     . THR A 1 3704 ? 166.903 130.494 158.169 1.00 25.85  ? 3704 THR A O     1 
ATOM   16829 C CB    . THR A 1 3704 ? 164.078 132.512 158.710 1.00 25.85  ? 3704 THR A CB    1 
ATOM   16830 O OG1   . THR A 1 3704 ? 163.439 131.401 158.071 1.00 25.85  ? 3704 THR A OG1   1 
ATOM   16831 C CG2   . THR A 1 3704 ? 163.450 133.804 158.217 1.00 25.85  ? 3704 THR A CG2   1 
ATOM   16832 N N     . ARG A 1 3705 ? 165.952 130.901 160.175 1.00 26.59  ? 3705 ARG A N     1 
ATOM   16833 C CA    . ARG A 1 3705 ? 166.491 129.683 160.771 1.00 26.59  ? 3705 ARG A CA    1 
ATOM   16834 C C     . ARG A 1 3705 ? 165.956 128.444 160.067 1.00 26.59  ? 3705 ARG A C     1 
ATOM   16835 O O     . ARG A 1 3705 ? 166.714 127.530 159.726 1.00 26.59  ? 3705 ARG A O     1 
ATOM   16836 C CB    . ARG A 1 3705 ? 166.159 129.641 162.263 1.00 26.59  ? 3705 ARG A CB    1 
ATOM   16837 C CG    . ARG A 1 3705 ? 167.178 130.341 163.144 1.00 26.59  ? 3705 ARG A CG    1 
ATOM   16838 C CD    . ARG A 1 3705 ? 166.956 130.023 164.616 1.00 26.59  ? 3705 ARG A CD    1 
ATOM   16839 N NE    . ARG A 1 3705 ? 168.149 130.246 165.427 1.00 26.59  ? 3705 ARG A NE    1 
ATOM   16840 C CZ    . ARG A 1 3705 ? 168.728 131.423 165.620 1.00 26.59  ? 3705 ARG A CZ    1 
ATOM   16841 N NH1   . ARG A 1 3705 ? 168.230 132.535 165.104 1.00 26.59  ? 3705 ARG A NH1   1 
ATOM   16842 N NH2   . ARG A 1 3705 ? 169.831 131.489 166.361 1.00 26.59  ? 3705 ARG A NH2   1 
ATOM   16843 N N     . SER A 1 3706 ? 164.645 128.407 159.824 1.00 29.04  ? 3706 SER A N     1 
ATOM   16844 C CA    . SER A 1 3706 ? 164.040 127.222 159.226 1.00 29.04  ? 3706 SER A CA    1 
ATOM   16845 C C     . SER A 1 3706 ? 164.436 127.070 157.763 1.00 29.04  ? 3706 SER A C     1 
ATOM   16846 O O     . SER A 1 3706 ? 164.693 125.955 157.298 1.00 29.04  ? 3706 SER A O     1 
ATOM   16847 C CB    . SER A 1 3706 ? 162.522 127.285 159.372 1.00 29.04  ? 3706 SER A CB    1 
ATOM   16848 O OG    . SER A 1 3706 ? 162.159 127.401 160.737 1.00 29.04  ? 3706 SER A OG    1 
ATOM   16849 N N     . SER A 1 3707 ? 164.493 128.178 157.021 1.00 29.74  ? 3707 SER A N     1 
ATOM   16850 C CA    . SER A 1 3707 ? 164.876 128.104 155.614 1.00 29.74  ? 3707 SER A CA    1 
ATOM   16851 C C     . SER A 1 3707 ? 166.307 127.605 155.459 1.00 29.74  ? 3707 SER A C     1 
ATOM   16852 O O     . SER A 1 3707 ? 166.586 126.718 154.643 1.00 29.74  ? 3707 SER A O     1 
ATOM   16853 C CB    . SER A 1 3707 ? 164.708 129.472 154.954 1.00 29.74  ? 3707 SER A CB    1 
ATOM   16854 O OG    . SER A 1 3707 ? 165.183 129.453 153.620 1.00 29.74  ? 3707 SER A OG    1 
ATOM   16855 N N     . LEU A 1 3708 ? 167.230 128.160 156.246 1.00 24.20  ? 3708 LEU A N     1 
ATOM   16856 C CA    . LEU A 1 3708 ? 168.619 127.720 156.172 1.00 24.20  ? 3708 LEU A CA    1 
ATOM   16857 C C     . LEU A 1 3708 ? 168.769 126.288 156.667 1.00 24.20  ? 3708 LEU A C     1 
ATOM   16858 O O     . LEU A 1 3708 ? 169.575 125.521 156.127 1.00 24.20  ? 3708 LEU A O     1 
ATOM   16859 C CB    . LEU A 1 3708 ? 169.514 128.661 156.973 1.00 24.20  ? 3708 LEU A CB    1 
ATOM   16860 C CG    . LEU A 1 3708 ? 170.991 128.277 156.966 1.00 24.20  ? 3708 LEU A CG    1 
ATOM   16861 C CD1   . LEU A 1 3708 ? 171.621 128.594 155.621 1.00 24.20  ? 3708 LEU A CD1   1 
ATOM   16862 C CD2   . LEU A 1 3708 ? 171.722 128.980 158.082 1.00 24.20  ? 3708 LEU A CD2   1 
ATOM   16863 N N     . GLN A 1 3709 ? 168.008 125.910 157.695 1.00 25.49  ? 3709 GLN A N     1 
ATOM   16864 C CA    . GLN A 1 3709 ? 168.041 124.535 158.175 1.00 25.49  ? 3709 GLN A CA    1 
ATOM   16865 C C     . GLN A 1 3709 ? 167.588 123.570 157.086 1.00 25.49  ? 3709 GLN A C     1 
ATOM   16866 O O     . GLN A 1 3709 ? 168.190 122.510 156.885 1.00 25.49  ? 3709 GLN A O     1 
ATOM   16867 C CB    . GLN A 1 3709 ? 167.173 124.402 159.428 1.00 25.49  ? 3709 GLN A CB    1 
ATOM   16868 C CG    . GLN A 1 3709 ? 167.274 123.054 160.116 1.00 25.49  ? 3709 GLN A CG    1 
ATOM   16869 C CD    . GLN A 1 3709 ? 166.324 122.031 159.530 1.00 25.49  ? 3709 GLN A CD    1 
ATOM   16870 O OE1   . GLN A 1 3709 ? 165.255 122.377 159.029 1.00 25.49  ? 3709 GLN A OE1   1 
ATOM   16871 N NE2   . GLN A 1 3709 ? 166.720 120.767 159.568 1.00 25.49  ? 3709 GLN A NE2   1 
ATOM   16872 N N     . SER A 1 3710 ? 166.521 123.927 156.366 1.00 28.08  ? 3710 SER A N     1 
ATOM   16873 C CA    . SER A 1 3710 ? 166.049 123.087 155.272 1.00 28.08  ? 3710 SER A CA    1 
ATOM   16874 C C     . SER A 1 3710 ? 167.076 123.010 154.151 1.00 28.08  ? 3710 SER A C     1 
ATOM   16875 O O     . SER A 1 3710 ? 167.293 121.940 153.570 1.00 28.08  ? 3710 SER A O     1 
ATOM   16876 C CB    . SER A 1 3710 ? 164.717 123.615 154.739 1.00 28.08  ? 3710 SER A CB    1 
ATOM   16877 O OG    . SER A 1 3710 ? 164.895 124.842 154.054 1.00 28.08  ? 3710 SER A OG    1 
ATOM   16878 N N     . GLN A 1 3711 ? 167.716 124.137 153.830 1.00 29.23  ? 3711 GLN A N     1 
ATOM   16879 C CA    . GLN A 1 3711 ? 168.754 124.130 152.802 1.00 29.23  ? 3711 GLN A CA    1 
ATOM   16880 C C     . GLN A 1 3711 ? 169.898 123.202 153.188 1.00 29.23  ? 3711 GLN A C     1 
ATOM   16881 O O     . GLN A 1 3711 ? 170.366 122.397 152.373 1.00 29.23  ? 3711 GLN A O     1 
ATOM   16882 C CB    . GLN A 1 3711 ? 169.278 125.546 152.570 1.00 29.23  ? 3711 GLN A CB    1 
ATOM   16883 C CG    . GLN A 1 3711 ? 168.571 126.307 151.470 1.00 29.23  ? 3711 GLN A CG    1 
ATOM   16884 C CD    . GLN A 1 3711 ? 169.206 127.656 151.203 1.00 29.23  ? 3711 GLN A CD    1 
ATOM   16885 O OE1   . GLN A 1 3711 ? 170.427 127.771 151.104 1.00 29.23  ? 3711 GLN A OE1   1 
ATOM   16886 N NE2   . GLN A 1 3711 ? 168.378 128.688 151.085 1.00 29.23  ? 3711 GLN A NE2   1 
ATOM   16887 N N     . CYS A 1 3712 ? 170.360 123.300 154.436 1.00 27.66  ? 3712 CYS A N     1 
ATOM   16888 C CA    . CYS A 1 3712 ? 171.457 122.455 154.893 1.00 27.66  ? 3712 CYS A CA    1 
ATOM   16889 C C     . CYS A 1 3712 ? 171.056 120.986 154.912 1.00 27.66  ? 3712 CYS A C     1 
ATOM   16890 O O     . CYS A 1 3712 ? 171.854 120.117 154.544 1.00 27.66  ? 3712 CYS A O     1 
ATOM   16891 C CB    . CYS A 1 3712 ? 171.925 122.906 156.275 1.00 27.66  ? 3712 CYS A CB    1 
ATOM   16892 S SG    . CYS A 1 3712 ? 172.604 124.578 156.307 1.00 27.66  ? 3712 CYS A SG    1 
ATOM   16893 N N     . LEU A 1 3713 ? 169.826 120.689 155.337 1.00 29.94  ? 3713 LEU A N     1 
ATOM   16894 C CA    . LEU A 1 3713 ? 169.365 119.305 155.348 1.00 29.94  ? 3713 LEU A CA    1 
ATOM   16895 C C     . LEU A 1 3713 ? 169.307 118.736 153.938 1.00 29.94  ? 3713 LEU A C     1 
ATOM   16896 O O     . LEU A 1 3713 ? 169.748 117.609 153.693 1.00 29.94  ? 3713 LEU A O     1 
ATOM   16897 C CB    . LEU A 1 3713 ? 167.999 119.212 156.027 1.00 29.94  ? 3713 LEU A CB    1 
ATOM   16898 C CG    . LEU A 1 3713 ? 167.456 117.800 156.253 1.00 29.94  ? 3713 LEU A CG    1 
ATOM   16899 C CD1   . LEU A 1 3713 ? 168.518 116.912 156.879 1.00 29.94  ? 3713 LEU A CD1   1 
ATOM   16900 C CD2   . LEU A 1 3713 ? 166.210 117.840 157.121 1.00 29.94  ? 3713 LEU A CD2   1 
ATOM   16901 N N     . ASN A 1 3714 ? 168.770 119.508 152.990 1.00 31.77  ? 3714 ASN A N     1 
ATOM   16902 C CA    . ASN A 1 3714 ? 168.714 119.040 151.610 1.00 31.77  ? 3714 ASN A CA    1 
ATOM   16903 C C     . ASN A 1 3714 ? 170.112 118.829 151.046 1.00 31.77  ? 3714 ASN A C     1 
ATOM   16904 O O     . ASN A 1 3714 ? 170.371 117.829 150.367 1.00 31.77  ? 3714 ASN A O     1 
ATOM   16905 C CB    . ASN A 1 3714 ? 167.930 120.030 150.749 1.00 31.77  ? 3714 ASN A CB    1 
ATOM   16906 C CG    . ASN A 1 3714 ? 166.450 120.036 151.071 1.00 31.77  ? 3714 ASN A CG    1 
ATOM   16907 O OD1   . ASN A 1 3714 ? 165.952 119.152 151.767 1.00 31.77  ? 3714 ASN A OD1   1 
ATOM   16908 N ND2   . ASN A 1 3714 ? 165.739 121.036 150.564 1.00 31.77  ? 3714 ASN A ND2   1 
ATOM   16909 N N     . GLU A 1 3715 ? 171.030 119.757 151.326 1.00 31.28  ? 3715 GLU A N     1 
ATOM   16910 C CA    . GLU A 1 3715 ? 172.392 119.630 150.820 1.00 31.28  ? 3715 GLU A CA    1 
ATOM   16911 C C     . GLU A 1 3715 ? 173.078 118.393 151.388 1.00 31.28  ? 3715 GLU A C     1 
ATOM   16912 O O     . GLU A 1 3715 ? 173.739 117.644 150.658 1.00 31.28  ? 3715 GLU A O     1 
ATOM   16913 C CB    . GLU A 1 3715 ? 173.189 120.891 151.153 1.00 31.28  ? 3715 GLU A CB    1 
ATOM   16914 C CG    . GLU A 1 3715 ? 174.576 120.932 150.540 1.00 31.28  ? 3715 GLU A CG    1 
ATOM   16915 C CD    . GLU A 1 3715 ? 174.542 121.098 149.033 1.00 31.28  ? 3715 GLU A CD    1 
ATOM   16916 O OE1   . GLU A 1 3715 ? 173.555 121.664 148.517 1.00 31.28  ? 3715 GLU A OE1   1 
ATOM   16917 O OE2   . GLU A 1 3715 ? 175.503 120.664 148.364 1.00 31.28  ? 3715 GLU A OE2   1 
ATOM   16918 N N     . VAL A 1 3716 ? 172.925 118.156 152.694 1.00 31.22  ? 3716 VAL A N     1 
ATOM   16919 C CA    . VAL A 1 3716 ? 173.600 117.018 153.307 1.00 31.22  ? 3716 VAL A CA    1 
ATOM   16920 C C     . VAL A 1 3716 ? 172.964 115.703 152.871 1.00 31.22  ? 3716 VAL A C     1 
ATOM   16921 O O     . VAL A 1 3716 ? 173.660 114.691 152.743 1.00 31.22  ? 3716 VAL A O     1 
ATOM   16922 C CB    . VAL A 1 3716 ? 173.636 117.162 154.841 1.00 31.22  ? 3716 VAL A CB    1 
ATOM   16923 C CG1   . VAL A 1 3716 ? 172.269 116.925 155.454 1.00 31.22  ? 3716 VAL A CG1   1 
ATOM   16924 C CG2   . VAL A 1 3716 ? 174.659 116.208 155.431 1.00 31.22  ? 3716 VAL A CG2   1 
ATOM   16925 N N     . LEU A 1 3717 ? 171.650 115.680 152.630 1.00 34.69  ? 3717 LEU A N     1 
ATOM   16926 C CA    . LEU A 1 3717 ? 171.039 114.471 152.085 1.00 34.69  ? 3717 LEU A CA    1 
ATOM   16927 C C     . LEU A 1 3717 ? 171.517 114.206 150.664 1.00 34.69  ? 3717 LEU A C     1 
ATOM   16928 O O     . LEU A 1 3717 ? 171.779 113.055 150.297 1.00 34.69  ? 3717 LEU A O     1 
ATOM   16929 C CB    . LEU A 1 3717 ? 169.515 114.570 152.126 1.00 34.69  ? 3717 LEU A CB    1 
ATOM   16930 C CG    . LEU A 1 3717 ? 168.864 114.609 153.506 1.00 34.69  ? 3717 LEU A CG    1 
ATOM   16931 C CD1   . LEU A 1 3717 ? 167.368 114.847 153.383 1.00 34.69  ? 3717 LEU A CD1   1 
ATOM   16932 C CD2   . LEU A 1 3717 ? 169.147 113.324 154.255 1.00 34.69  ? 3717 LEU A CD2   1 
ATOM   16933 N N     . LYS A 1 3718 ? 171.636 115.256 149.850 1.00 39.04  ? 3718 LYS A N     1 
ATOM   16934 C CA    . LYS A 1 3718 ? 172.111 115.077 148.483 1.00 39.04  ? 3718 LYS A CA    1 
ATOM   16935 C C     . LYS A 1 3718 ? 173.556 114.592 148.458 1.00 39.04  ? 3718 LYS A C     1 
ATOM   16936 O O     . LYS A 1 3718 ? 173.920 113.755 147.625 1.00 39.04  ? 3718 LYS A O     1 
ATOM   16937 C CB    . LYS A 1 3718 ? 171.965 116.384 147.705 1.00 39.04  ? 3718 LYS A CB    1 
ATOM   16938 C CG    . LYS A 1 3718 ? 172.559 116.352 146.307 1.00 39.04  ? 3718 LYS A CG    1 
ATOM   16939 C CD    . LYS A 1 3718 ? 172.381 117.688 145.605 1.00 39.04  ? 3718 LYS A CD    1 
ATOM   16940 C CE    . LYS A 1 3718 ? 172.742 117.591 144.132 1.00 39.04  ? 3718 LYS A CE    1 
ATOM   16941 N NZ    . LYS A 1 3718 ? 171.870 116.625 143.409 1.00 39.04  ? 3718 LYS A NZ    1 
ATOM   16942 N N     . ALA A 1 3719 ? 174.391 115.102 149.364 1.00 37.78  ? 3719 ALA A N     1 
ATOM   16943 C CA    . ALA A 1 3719 ? 175.808 114.751 149.346 1.00 37.78  ? 3719 ALA A CA    1 
ATOM   16944 C C     . ALA A 1 3719 ? 176.069 113.401 150.007 1.00 37.78  ? 3719 ALA A C     1 
ATOM   16945 O O     . ALA A 1 3719 ? 176.633 112.493 149.387 1.00 37.78  ? 3719 ALA A O     1 
ATOM   16946 C CB    . ALA A 1 3719 ? 176.625 115.850 150.030 1.00 37.78  ? 3719 ALA A CB    1 
ATOM   16947 N N     . GLU A 1 3720 ? 175.671 113.255 151.273 1.00 39.22  ? 3720 GLU A N     1 
ATOM   16948 C CA    . GLU A 1 3720 ? 176.037 112.068 152.042 1.00 39.22  ? 3720 GLU A CA    1 
ATOM   16949 C C     . GLU A 1 3720 ? 175.332 110.817 151.531 1.00 39.22  ? 3720 GLU A C     1 
ATOM   16950 O O     . GLU A 1 3720 ? 175.973 109.779 151.328 1.00 39.22  ? 3720 GLU A O     1 
ATOM   16951 C CB    . GLU A 1 3720 ? 175.720 112.290 153.519 1.00 39.22  ? 3720 GLU A CB    1 
ATOM   16952 C CG    . GLU A 1 3720 ? 176.878 112.852 154.313 1.00 39.22  ? 3720 GLU A CG    1 
ATOM   16953 C CD    . GLU A 1 3720 ? 178.194 112.204 153.943 1.00 39.22  ? 3720 GLU A CD    1 
ATOM   16954 O OE1   . GLU A 1 3720 ? 178.367 111.003 154.235 1.00 39.22  ? 3720 GLU A OE1   1 
ATOM   16955 O OE2   . GLU A 1 3720 ? 179.055 112.894 153.357 1.00 39.22  ? 3720 GLU A OE2   1 
ATOM   16956 N N     . ARG A 1 3721 ? 174.021 110.891 151.317 1.00 45.89  ? 3721 ARG A N     1 
ATOM   16957 C CA    . ARG A 1 3721 ? 173.206 109.728 150.966 1.00 45.89  ? 3721 ARG A CA    1 
ATOM   16958 C C     . ARG A 1 3721 ? 172.427 110.034 149.696 1.00 45.89  ? 3721 ARG A C     1 
ATOM   16959 O O     . ARG A 1 3721 ? 171.240 110.383 149.748 1.00 45.89  ? 3721 ARG A O     1 
ATOM   16960 C CB    . ARG A 1 3721 ? 172.267 109.349 152.112 1.00 45.89  ? 3721 ARG A CB    1 
ATOM   16961 C CG    . ARG A 1 3721 ? 172.971 108.772 153.328 1.00 45.89  ? 3721 ARG A CG    1 
ATOM   16962 C CD    . ARG A 1 3721 ? 172.024 108.678 154.512 1.00 45.89  ? 3721 ARG A CD    1 
ATOM   16963 N NE    . ARG A 1 3721 ? 170.930 107.746 154.269 1.00 45.89  ? 3721 ARG A NE    1 
ATOM   16964 C CZ    . ARG A 1 3721 ? 170.899 106.493 154.701 1.00 45.89  ? 3721 ARG A CZ    1 
ATOM   16965 N NH1   . ARG A 1 3721 ? 171.884 105.988 155.425 1.00 45.89  ? 3721 ARG A NH1   1 
ATOM   16966 N NH2   . ARG A 1 3721 ? 169.852 105.729 154.406 1.00 45.89  ? 3721 ARG A NH2   1 
ATOM   16967 N N     . PRO A 1 3722 ? 173.067 109.912 148.531 1.00 52.50  ? 3722 PRO A N     1 
ATOM   16968 C CA    . PRO A 1 3722 ? 172.353 110.191 147.274 1.00 52.50  ? 3722 PRO A CA    1 
ATOM   16969 C C     . PRO A 1 3722 ? 171.168 109.274 147.034 1.00 52.50  ? 3722 PRO A C     1 
ATOM   16970 O O     . PRO A 1 3722 ? 170.230 109.667 146.331 1.00 52.50  ? 3722 PRO A O     1 
ATOM   16971 C CB    . PRO A 1 3722 ? 173.440 110.003 146.206 1.00 52.50  ? 3722 PRO A CB    1 
ATOM   16972 C CG    . PRO A 1 3722 ? 174.444 109.101 146.840 1.00 52.50  ? 3722 PRO A CG    1 
ATOM   16973 C CD    . PRO A 1 3722 ? 174.445 109.450 148.299 1.00 52.50  ? 3722 PRO A CD    1 
ATOM   16974 N N     . ASP A 1 3723 ? 171.183 108.059 147.587 1.00 55.58  ? 3723 ASP A N     1 
ATOM   16975 C CA    . ASP A 1 3723 ? 170.056 107.150 147.401 1.00 55.58  ? 3723 ASP A CA    1 
ATOM   16976 C C     . ASP A 1 3723 ? 168.790 107.689 148.061 1.00 55.58  ? 3723 ASP A C     1 
ATOM   16977 O O     . ASP A 1 3723 ? 167.702 107.622 147.476 1.00 55.58  ? 3723 ASP A O     1 
ATOM   16978 C CB    . ASP A 1 3723 ? 170.409 105.761 147.936 1.00 55.58  ? 3723 ASP A CB    1 
ATOM   16979 C CG    . ASP A 1 3723 ? 170.570 105.733 149.444 1.00 55.58  ? 3723 ASP A CG    1 
ATOM   16980 O OD1   . ASP A 1 3723 ? 169.566 105.494 150.146 1.00 55.58  ? 3723 ASP A OD1   1 
ATOM   16981 O OD2   . ASP A 1 3723 ? 171.701 105.948 149.926 1.00 55.58  ? 3723 ASP A OD2   1 
ATOM   16982 N N     . VAL A 1 3724 ? 168.910 108.242 149.270 1.00 54.51  ? 3724 VAL A N     1 
ATOM   16983 C CA    . VAL A 1 3724 ? 167.741 108.791 149.950 1.00 54.51  ? 3724 VAL A CA    1 
ATOM   16984 C C     . VAL A 1 3724 ? 167.235 110.031 149.224 1.00 54.51  ? 3724 VAL A C     1 
ATOM   16985 O O     . VAL A 1 3724 ? 166.024 110.252 149.117 1.00 54.51  ? 3724 VAL A O     1 
ATOM   16986 C CB    . VAL A 1 3724 ? 168.069 109.087 151.424 1.00 54.51  ? 3724 VAL A CB    1 
ATOM   16987 C CG1   . VAL A 1 3724 ? 166.889 109.757 152.108 1.00 54.51  ? 3724 VAL A CG1   1 
ATOM   16988 C CG2   . VAL A 1 3724 ? 168.438 107.805 152.142 1.00 54.51  ? 3724 VAL A CG2   1 
ATOM   16989 N N     . ASP A 1 3725 ? 168.150 110.860 148.717 1.00 59.83  ? 3725 ASP A N     1 
ATOM   16990 C CA    . ASP A 1 3725 ? 167.739 112.019 147.932 1.00 59.83  ? 3725 ASP A CA    1 
ATOM   16991 C C     . ASP A 1 3725 ? 167.007 111.593 146.665 1.00 59.83  ? 3725 ASP A C     1 
ATOM   16992 O O     . ASP A 1 3725 ? 165.999 112.201 146.285 1.00 59.83  ? 3725 ASP A O     1 
ATOM   16993 C CB    . ASP A 1 3725 ? 168.956 112.876 147.587 1.00 59.83  ? 3725 ASP A CB    1 
ATOM   16994 C CG    . ASP A 1 3725 ? 168.633 113.975 146.595 1.00 59.83  ? 3725 ASP A CG    1 
ATOM   16995 O OD1   . ASP A 1 3725 ? 168.092 115.019 147.017 1.00 59.83  ? 3725 ASP A OD1   1 
ATOM   16996 O OD2   . ASP A 1 3725 ? 168.922 113.796 145.393 1.00 59.83  ? 3725 ASP A OD2   1 
ATOM   16997 N N     . GLU A 1 3726 ? 167.501 110.547 145.999 1.00 65.45  ? 3726 GLU A N     1 
ATOM   16998 C CA    . GLU A 1 3726 ? 166.826 110.044 144.808 1.00 65.45  ? 3726 GLU A CA    1 
ATOM   16999 C C     . GLU A 1 3726 ? 165.444 109.503 145.147 1.00 65.45  ? 3726 GLU A C     1 
ATOM   17000 O O     . GLU A 1 3726 ? 164.485 109.720 144.399 1.00 65.45  ? 3726 GLU A O     1 
ATOM   17001 C CB    . GLU A 1 3726 ? 167.678 108.968 144.135 1.00 65.45  ? 3726 GLU A CB    1 
ATOM   17002 C CG    . GLU A 1 3726 ? 167.054 108.375 142.883 1.00 65.45  ? 3726 GLU A CG    1 
ATOM   17003 C CD    . GLU A 1 3726 ? 168.072 107.688 141.995 1.00 65.45  ? 3726 GLU A CD    1 
ATOM   17004 O OE1   . GLU A 1 3726 ? 169.010 108.369 141.528 1.00 65.45  ? 3726 GLU A OE1   1 
ATOM   17005 O OE2   . GLU A 1 3726 ? 167.936 106.469 141.763 1.00 65.45  ? 3726 GLU A OE2   1 
ATOM   17006 N N     . LYS A 1 3727 ? 165.320 108.797 146.273 1.00 65.44  ? 3727 LYS A N     1 
ATOM   17007 C CA    . LYS A 1 3727 ? 164.014 108.285 146.680 1.00 65.44  ? 3727 LYS A CA    1 
ATOM   17008 C C     . LYS A 1 3727 ? 163.049 109.420 147.007 1.00 65.44  ? 3727 LYS A C     1 
ATOM   17009 O O     . LYS A 1 3727 ? 161.861 109.349 146.671 1.00 65.44  ? 3727 LYS A O     1 
ATOM   17010 C CB    . LYS A 1 3727 ? 164.172 107.342 147.872 1.00 65.44  ? 3727 LYS A CB    1 
ATOM   17011 C CG    . LYS A 1 3727 ? 164.921 106.061 147.535 1.00 65.44  ? 3727 LYS A CG    1 
ATOM   17012 C CD    . LYS A 1 3727 ? 165.174 105.210 148.768 1.00 65.44  ? 3727 LYS A CD    1 
ATOM   17013 C CE    . LYS A 1 3727 ? 163.917 104.481 149.203 1.00 65.44  ? 3727 LYS A CE    1 
ATOM   17014 N NZ    . LYS A 1 3727 ? 164.187 103.520 150.306 1.00 65.44  ? 3727 LYS A NZ    1 
ATOM   17015 N N     . ARG A 1 3728 ? 163.538 110.474 147.664 1.00 62.41  ? 3728 ARG A N     1 
ATOM   17016 C CA    . ARG A 1 3728 ? 162.693 111.630 147.953 1.00 62.41  ? 3728 ARG A CA    1 
ATOM   17017 C C     . ARG A 1 3728 ? 162.244 112.323 146.671 1.00 62.41  ? 3728 ARG A C     1 
ATOM   17018 O O     . ARG A 1 3728 ? 161.081 112.731 146.548 1.00 62.41  ? 3728 ARG A O     1 
ATOM   17019 C CB    . ARG A 1 3728 ? 163.438 112.610 148.857 1.00 62.41  ? 3728 ARG A CB    1 
ATOM   17020 C CG    . ARG A 1 3728 ? 162.568 113.713 149.430 1.00 62.41  ? 3728 ARG A CG    1 
ATOM   17021 C CD    . ARG A 1 3728 ? 163.423 114.815 150.028 1.00 62.41  ? 3728 ARG A CD    1 
ATOM   17022 N NE    . ARG A 1 3728 ? 164.105 115.587 148.996 1.00 62.41  ? 3728 ARG A NE    1 
ATOM   17023 C CZ    . ARG A 1 3728 ? 165.412 115.548 148.773 1.00 62.41  ? 3728 ARG A CZ    1 
ATOM   17024 N NH1   . ARG A 1 3728 ? 166.213 114.779 149.492 1.00 62.41  ? 3728 ARG A NH1   1 
ATOM   17025 N NH2   . ARG A 1 3728 ? 165.927 116.298 147.803 1.00 62.41  ? 3728 ARG A NH2   1 
ATOM   17026 N N     . SER A 1 3729 ? 163.158 112.482 145.711 1.00 65.55  ? 3729 SER A N     1 
ATOM   17027 C CA    . SER A 1 3729 ? 162.783 113.071 144.431 1.00 65.55  ? 3729 SER A CA    1 
ATOM   17028 C C     . SER A 1 3729 ? 161.771 112.195 143.706 1.00 65.55  ? 3729 SER A C     1 
ATOM   17029 O O     . SER A 1 3729 ? 160.856 112.703 143.049 1.00 65.55  ? 3729 SER A O     1 
ATOM   17030 C CB    . SER A 1 3729 ? 164.023 113.294 143.566 1.00 65.55  ? 3729 SER A CB    1 
ATOM   17031 O OG    . SER A 1 3729 ? 164.779 112.103 143.443 1.00 65.55  ? 3729 SER A OG    1 
ATOM   17032 N N     . ASP A 1 3730 ? 161.920 110.873 143.815 1.00 68.10  ? 3730 ASP A N     1 
ATOM   17033 C CA    . ASP A 1 3730 ? 160.937 109.963 143.236 1.00 68.10  ? 3730 ASP A CA    1 
ATOM   17034 C C     . ASP A 1 3730 ? 159.572 110.146 143.885 1.00 68.10  ? 3730 ASP A C     1 
ATOM   17035 O O     . ASP A 1 3730 ? 158.547 110.155 143.197 1.00 68.10  ? 3730 ASP A O     1 
ATOM   17036 C CB    . ASP A 1 3730 ? 161.410 108.517 143.385 1.00 68.10  ? 3730 ASP A CB    1 
ATOM   17037 C CG    . ASP A 1 3730 ? 162.298 108.073 142.240 1.00 68.10  ? 3730 ASP A CG    1 
ATOM   17038 O OD1   . ASP A 1 3730 ? 162.364 108.794 141.222 1.00 68.10  ? 3730 ASP A OD1   1 
ATOM   17039 O OD2   . ASP A 1 3730 ? 162.930 107.002 142.359 1.00 68.10  ? 3730 ASP A OD2   1 
ATOM   17040 N N     . LEU A 1 3731 ? 159.542 110.294 145.212 1.00 63.98  ? 3731 LEU A N     1 
ATOM   17041 C CA    . LEU A 1 3731 ? 158.277 110.534 145.900 1.00 63.98  ? 3731 LEU A CA    1 
ATOM   17042 C C     . LEU A 1 3731 ? 157.633 111.831 145.431 1.00 63.98  ? 3731 LEU A C     1 
ATOM   17043 O O     . LEU A 1 3731 ? 156.418 111.888 145.213 1.00 63.98  ? 3731 LEU A O     1 
ATOM   17044 C CB    . LEU A 1 3731 ? 158.489 110.574 147.413 1.00 63.98  ? 3731 LEU A CB    1 
ATOM   17045 C CG    . LEU A 1 3731 ? 158.928 109.292 148.116 1.00 63.98  ? 3731 LEU A CG    1 
ATOM   17046 C CD1   . LEU A 1 3731 ? 159.216 109.580 149.579 1.00 63.98  ? 3731 LEU A CD1   1 
ATOM   17047 C CD2   . LEU A 1 3731 ? 157.861 108.222 147.978 1.00 63.98  ? 3731 LEU A CD2   1 
ATOM   17048 N N     . LEU A 1 3732 ? 158.433 112.889 145.283 1.00 62.54  ? 3732 LEU A N     1 
ATOM   17049 C CA    . LEU A 1 3732 ? 157.888 114.160 144.814 1.00 62.54  ? 3732 LEU A CA    1 
ATOM   17050 C C     . LEU A 1 3732 ? 157.367 114.048 143.386 1.00 62.54  ? 3732 LEU A C     1 
ATOM   17051 O O     . LEU A 1 3732 ? 156.314 114.608 143.058 1.00 62.54  ? 3732 LEU A O     1 
ATOM   17052 C CB    . LEU A 1 3732 ? 158.944 115.259 144.917 1.00 62.54  ? 3732 LEU A CB    1 
ATOM   17053 C CG    . LEU A 1 3732 ? 158.839 116.156 146.152 1.00 62.54  ? 3732 LEU A CG    1 
ATOM   17054 C CD1   . LEU A 1 3732 ? 159.049 115.353 147.427 1.00 62.54  ? 3732 LEU A CD1   1 
ATOM   17055 C CD2   . LEU A 1 3732 ? 159.829 117.306 146.066 1.00 62.54  ? 3732 LEU A CD2   1 
ATOM   17056 N N     . LYS A 1 3733 ? 158.088 113.330 142.524 1.00 64.54  ? 3733 LYS A N     1 
ATOM   17057 C CA    . LYS A 1 3733 ? 157.648 113.167 141.143 1.00 64.54  ? 3733 LYS A CA    1 
ATOM   17058 C C     . LYS A 1 3733 ? 156.410 112.286 141.045 1.00 64.54  ? 3733 LYS A C     1 
ATOM   17059 O O     . LYS A 1 3733 ? 155.611 112.451 140.118 1.00 64.54  ? 3733 LYS A O     1 
ATOM   17060 C CB    . LYS A 1 3733 ? 158.781 112.588 140.295 1.00 64.54  ? 3733 LYS A CB    1 
ATOM   17061 C CG    . LYS A 1 3733 ? 159.950 113.538 140.087 1.00 64.54  ? 3733 LYS A CG    1 
ATOM   17062 C CD    . LYS A 1 3733 ? 160.905 113.021 139.024 1.00 64.54  ? 3733 LYS A CD    1 
ATOM   17063 C CE    . LYS A 1 3733 ? 161.655 111.788 139.504 1.00 64.54  ? 3733 LYS A CE    1 
ATOM   17064 N NZ    . LYS A 1 3733 ? 162.606 112.107 140.605 1.00 64.54  ? 3733 LYS A NZ    1 
ATOM   17065 N N     . LEU A 1 3734 ? 156.227 111.368 141.997 1.00 63.34  ? 3734 LEU A N     1 
ATOM   17066 C CA    . LEU A 1 3734 ? 155.165 110.373 141.903 1.00 63.34  ? 3734 LEU A CA    1 
ATOM   17067 C C     . LEU A 1 3734 ? 153.775 110.988 141.821 1.00 63.34  ? 3734 LEU A C     1 
ATOM   17068 O O     . LEU A 1 3734 ? 152.850 110.330 141.332 1.00 63.34  ? 3734 LEU A O     1 
ATOM   17069 C CB    . LEU A 1 3734 ? 155.245 109.425 143.101 1.00 63.34  ? 3734 LEU A CB    1 
ATOM   17070 C CG    . LEU A 1 3734 ? 154.395 108.158 143.042 1.00 63.34  ? 3734 LEU A CG    1 
ATOM   17071 C CD1   . LEU A 1 3734 ? 155.073 107.116 142.175 1.00 63.34  ? 3734 LEU A CD1   1 
ATOM   17072 C CD2   . LEU A 1 3734 ? 154.148 107.618 144.439 1.00 63.34  ? 3734 LEU A CD2   1 
ATOM   17073 N N     . GLN A 1 3735 ? 153.597 112.226 142.277 1.00 60.07  ? 3735 GLN A N     1 
ATOM   17074 C CA    . GLN A 1 3735 ? 152.270 112.827 142.231 1.00 60.07  ? 3735 GLN A CA    1 
ATOM   17075 C C     . GLN A 1 3735 ? 151.899 113.238 140.810 1.00 60.07  ? 3735 GLN A C     1 
ATOM   17076 O O     . GLN A 1 3735 ? 150.853 112.836 140.289 1.00 60.07  ? 3735 GLN A O     1 
ATOM   17077 C CB    . GLN A 1 3735 ? 152.188 114.014 143.192 1.00 60.07  ? 3735 GLN A CB    1 
ATOM   17078 C CG    . GLN A 1 3735 ? 152.648 113.684 144.602 1.00 60.07  ? 3735 GLN A CG    1 
ATOM   17079 C CD    . GLN A 1 3735 ? 151.881 114.452 145.658 1.00 60.07  ? 3735 GLN A CD    1 
ATOM   17080 O OE1   . GLN A 1 3735 ? 151.765 115.674 145.595 1.00 60.07  ? 3735 GLN A OE1   1 
ATOM   17081 N NE2   . GLN A 1 3735 ? 151.350 113.732 146.638 1.00 60.07  ? 3735 GLN A NE2   1 
ATOM   17082 N N     . GLY A 1 3736 ? 152.741 114.042 140.163 1.00 68.17  ? 3736 GLY A N     1 
ATOM   17083 C CA    . GLY A 1 3736 ? 152.394 114.515 138.836 1.00 68.17  ? 3736 GLY A CA    1 
ATOM   17084 C C     . GLY A 1 3736 ? 153.310 114.133 137.690 1.00 68.17  ? 3736 GLY A C     1 
ATOM   17085 O O     . GLY A 1 3736 ? 152.832 113.890 136.578 1.00 68.17  ? 3736 GLY A O     1 
ATOM   17086 N N     . GLU A 1 3737 ? 154.620 114.048 137.936 1.00 68.05  ? 3737 GLU A N     1 
ATOM   17087 C CA    . GLU A 1 3737 ? 155.561 113.906 136.828 1.00 68.05  ? 3737 GLU A CA    1 
ATOM   17088 C C     . GLU A 1 3737 ? 155.535 112.501 136.243 1.00 68.05  ? 3737 GLU A C     1 
ATOM   17089 O O     . GLU A 1 3737 ? 155.565 112.334 135.018 1.00 68.05  ? 3737 GLU A O     1 
ATOM   17090 C CB    . GLU A 1 3737 ? 156.973 114.272 137.285 1.00 68.05  ? 3737 GLU A CB    1 
ATOM   17091 C CG    . GLU A 1 3737 ? 157.084 115.630 137.963 1.00 68.05  ? 3737 GLU A CG    1 
ATOM   17092 C CD    . GLU A 1 3737 ? 156.116 116.655 137.397 1.00 68.05  ? 3737 GLU A CD    1 
ATOM   17093 O OE1   . GLU A 1 3737 ? 156.174 116.926 136.179 1.00 68.05  ? 3737 GLU A OE1   1 
ATOM   17094 O OE2   . GLU A 1 3737 ? 155.296 117.188 138.173 1.00 68.05  ? 3737 GLU A OE2   1 
ATOM   17095 N N     . PHE A 1 3738 ? 155.490 111.476 137.096 1.00 69.10  ? 3738 PHE A N     1 
ATOM   17096 C CA    . PHE A 1 3738 ? 155.411 110.111 136.589 1.00 69.10  ? 3738 PHE A CA    1 
ATOM   17097 C C     . PHE A 1 3738 ? 154.106 109.882 135.839 1.00 69.10  ? 3738 PHE A C     1 
ATOM   17098 O O     . PHE A 1 3738 ? 154.090 109.224 134.793 1.00 69.10  ? 3738 PHE A O     1 
ATOM   17099 C CB    . PHE A 1 3738 ? 155.563 109.110 137.733 1.00 69.10  ? 3738 PHE A CB    1 
ATOM   17100 C CG    . PHE A 1 3738 ? 156.977 108.948 138.210 1.00 69.10  ? 3738 PHE A CG    1 
ATOM   17101 C CD1   . PHE A 1 3738 ? 157.257 108.820 139.559 1.00 69.10  ? 3738 PHE A CD1   1 
ATOM   17102 C CD2   . PHE A 1 3738 ? 158.027 108.929 137.309 1.00 69.10  ? 3738 PHE A CD2   1 
ATOM   17103 C CE1   . PHE A 1 3738 ? 158.556 108.673 140.001 1.00 69.10  ? 3738 PHE A CE1   1 
ATOM   17104 C CE2   . PHE A 1 3738 ? 159.330 108.783 137.744 1.00 69.10  ? 3738 PHE A CE2   1 
ATOM   17105 C CZ    . PHE A 1 3738 ? 159.594 108.654 139.092 1.00 69.10  ? 3738 PHE A CZ    1 
ATOM   17106 N N     . GLN A 1 3739 ? 153.001 110.421 136.355 1.00 70.70  ? 3739 GLN A N     1 
ATOM   17107 C CA    . GLN A 1 3739 ? 151.726 110.296 135.656 1.00 70.70  ? 3739 GLN A CA    1 
ATOM   17108 C C     . GLN A 1 3739 ? 151.756 111.025 134.319 1.00 70.70  ? 3739 GLN A C     1 
ATOM   17109 O O     . GLN A 1 3739 ? 151.211 110.532 133.326 1.00 70.70  ? 3739 GLN A O     1 
ATOM   17110 C CB    . GLN A 1 3739 ? 150.585 110.814 136.534 1.00 70.70  ? 3739 GLN A CB    1 
ATOM   17111 C CG    . GLN A 1 3739 ? 150.118 109.850 137.631 1.00 70.70  ? 3739 GLN A CG    1 
ATOM   17112 C CD    . GLN A 1 3739 ? 151.231 109.367 138.548 1.00 70.70  ? 3739 GLN A CD    1 
ATOM   17113 O OE1   . GLN A 1 3739 ? 152.290 109.987 138.646 1.00 70.70  ? 3739 GLN A OE1   1 
ATOM   17114 N NE2   . GLN A 1 3739 ? 150.993 108.250 139.225 1.00 70.70  ? 3739 GLN A NE2   1 
ATOM   17115 N N     . LEU A 1 3740 ? 152.390 112.200 134.270 1.00 71.10  ? 3740 LEU A N     1 
ATOM   17116 C CA    . LEU A 1 3740 ? 152.523 112.912 133.003 1.00 71.10  ? 3740 LEU A CA    1 
ATOM   17117 C C     . LEU A 1 3740 ? 153.350 112.111 132.004 1.00 71.10  ? 3740 LEU A C     1 
ATOM   17118 O O     . LEU A 1 3740 ? 153.007 112.037 130.818 1.00 71.10  ? 3740 LEU A O     1 
ATOM   17119 C CB    . LEU A 1 3740 ? 153.147 114.287 133.238 1.00 71.10  ? 3740 LEU A CB    1 
ATOM   17120 C CG    . LEU A 1 3740 ? 153.419 115.150 132.003 1.00 71.10  ? 3740 LEU A CG    1 
ATOM   17121 C CD1   . LEU A 1 3740 ? 152.174 115.271 131.136 1.00 71.10  ? 3740 LEU A CD1   1 
ATOM   17122 C CD2   . LEU A 1 3740 ? 153.934 116.523 132.405 1.00 71.10  ? 3740 LEU A CD2   1 
ATOM   17123 N N     . ARG A 1 3741 ? 154.447 111.505 132.467 1.00 70.89  ? 3741 ARG A N     1 
ATOM   17124 C CA    . ARG A 1 3741 ? 155.274 110.696 131.576 1.00 70.89  ? 3741 ARG A CA    1 
ATOM   17125 C C     . ARG A 1 3741 ? 154.511 109.479 131.067 1.00 70.89  ? 3741 ARG A C     1 
ATOM   17126 O O     . ARG A 1 3741 ? 154.615 109.121 129.888 1.00 70.89  ? 3741 ARG A O     1 
ATOM   17127 C CB    . ARG A 1 3741 ? 156.556 110.267 132.288 1.00 70.89  ? 3741 ARG A CB    1 
ATOM   17128 C CG    . ARG A 1 3741 ? 157.745 111.167 132.002 1.00 70.89  ? 3741 ARG A CG    1 
ATOM   17129 C CD    . ARG A 1 3741 ? 158.728 111.189 133.166 1.00 70.89  ? 3741 ARG A CD    1 
ATOM   17130 N NE    . ARG A 1 3741 ? 159.978 111.867 132.836 1.00 70.89  ? 3741 ARG A NE    1 
ATOM   17131 C CZ    . ARG A 1 3741 ? 160.084 113.139 132.471 1.00 70.89  ? 3741 ARG A CZ    1 
ATOM   17132 N NH1   . ARG A 1 3741 ? 159.035 113.946 132.448 1.00 70.89  ? 3741 ARG A NH1   1 
ATOM   17133 N NH2   . ARG A 1 3741 ? 161.278 113.619 132.136 1.00 70.89  ? 3741 ARG A NH2   1 
ATOM   17134 N N     . LEU A 1 3742 ? 153.742 108.828 131.943 1.00 73.02  ? 3742 LEU A N     1 
ATOM   17135 C CA    . LEU A 1 3742 ? 152.934 107.691 131.515 1.00 73.02  ? 3742 LEU A CA    1 
ATOM   17136 C C     . LEU A 1 3742 ? 151.864 108.114 130.517 1.00 73.02  ? 3742 LEU A C     1 
ATOM   17137 O O     . LEU A 1 3742 ? 151.597 107.398 129.546 1.00 73.02  ? 3742 LEU A O     1 
ATOM   17138 C CB    . LEU A 1 3742 ? 152.304 107.001 132.726 1.00 73.02  ? 3742 LEU A CB    1 
ATOM   17139 C CG    . LEU A 1 3742 ? 153.070 105.813 133.316 1.00 73.02  ? 3742 LEU A CG    1 
ATOM   17140 C CD1   . LEU A 1 3742 ? 154.405 106.237 133.906 1.00 73.02  ? 3742 LEU A CD1   1 
ATOM   17141 C CD2   . LEU A 1 3742 ? 152.223 105.104 134.363 1.00 73.02  ? 3742 LEU A CD2   1 
ATOM   17142 N N     . ARG A 1 3743 ? 151.237 109.272 130.738 1.00 78.00  ? 3743 ARG A N     1 
ATOM   17143 C CA    . ARG A 1 3743 ? 150.240 109.761 129.792 1.00 78.00  ? 3743 ARG A CA    1 
ATOM   17144 C C     . ARG A 1 3743 ? 150.868 110.060 128.435 1.00 78.00  ? 3743 ARG A C     1 
ATOM   17145 O O     . ARG A 1 3743 ? 150.280 109.760 127.390 1.00 78.00  ? 3743 ARG A O     1 
ATOM   17146 C CB    . ARG A 1 3743 ? 149.548 111.005 130.351 1.00 78.00  ? 3743 ARG A CB    1 
ATOM   17147 C CG    . ARG A 1 3743 ? 148.588 110.733 131.506 1.00 78.00  ? 3743 ARG A CG    1 
ATOM   17148 C CD    . ARG A 1 3743 ? 147.802 109.444 131.316 1.00 78.00  ? 3743 ARG A CD    1 
ATOM   17149 N NE    . ARG A 1 3743 ? 146.679 109.611 130.402 1.00 78.00  ? 3743 ARG A NE    1 
ATOM   17150 C CZ    . ARG A 1 3743 ? 145.788 108.666 130.130 1.00 78.00  ? 3743 ARG A CZ    1 
ATOM   17151 N NH1   . ARG A 1 3743 ? 145.854 107.471 130.694 1.00 78.00  ? 3743 ARG A NH1   1 
ATOM   17152 N NH2   . ARG A 1 3743 ? 144.806 108.927 129.272 1.00 78.00  ? 3743 ARG A NH2   1 
ATOM   17153 N N     . GLN A 1 3744 ? 152.064 110.655 128.429 1.00 76.37  ? 3744 GLN A N     1 
ATOM   17154 C CA    . GLN A 1 3744 ? 152.742 110.932 127.164 1.00 76.37  ? 3744 GLN A CA    1 
ATOM   17155 C C     . GLN A 1 3744 ? 153.142 109.644 126.450 1.00 76.37  ? 3744 GLN A C     1 
ATOM   17156 O O     . GLN A 1 3744 ? 153.016 109.541 125.224 1.00 76.37  ? 3744 GLN A O     1 
ATOM   17157 C CB    . GLN A 1 3744 ? 153.962 111.821 127.405 1.00 76.37  ? 3744 GLN A CB    1 
ATOM   17158 C CG    . GLN A 1 3744 ? 153.624 113.221 127.902 1.00 76.37  ? 3744 GLN A CG    1 
ATOM   17159 C CD    . GLN A 1 3744 ? 152.762 114.004 126.928 1.00 76.37  ? 3744 GLN A CD    1 
ATOM   17160 O OE1   . GLN A 1 3744 ? 152.834 113.804 125.715 1.00 76.37  ? 3744 GLN A OE1   1 
ATOM   17161 N NE2   . GLN A 1 3744 ? 151.940 114.903 127.457 1.00 76.37  ? 3744 GLN A NE2   1 
ATOM   17162 N N     . LEU A 1 3745 ? 153.630 108.652 127.199 1.00 79.62  ? 3745 LEU A N     1 
ATOM   17163 C CA    . LEU A 1 3745 ? 153.982 107.371 126.593 1.00 79.62  ? 3745 LEU A CA    1 
ATOM   17164 C C     . LEU A 1 3745 ? 152.745 106.668 126.040 1.00 79.62  ? 3745 LEU A C     1 
ATOM   17165 O O     . LEU A 1 3745 ? 152.796 106.042 124.974 1.00 79.62  ? 3745 LEU A O     1 
ATOM   17166 C CB    . LEU A 1 3745 ? 154.706 106.497 127.618 1.00 79.62  ? 3745 LEU A CB    1 
ATOM   17167 C CG    . LEU A 1 3745 ? 156.241 106.494 127.604 1.00 79.62  ? 3745 LEU A CG    1 
ATOM   17168 C CD1   . LEU A 1 3745 ? 156.775 105.807 126.355 1.00 79.62  ? 3745 LEU A CD1   1 
ATOM   17169 C CD2   . LEU A 1 3745 ? 156.811 107.902 127.727 1.00 79.62  ? 3745 LEU A CD2   1 
ATOM   17170 N N     . GLU A 1 3746 ? 151.617 106.776 126.745 1.00 82.35  ? 3746 GLU A N     1 
ATOM   17171 C CA    . GLU A 1 3746 ? 150.348 106.290 126.209 1.00 82.35  ? 3746 GLU A CA    1 
ATOM   17172 C C     . GLU A 1 3746 ? 149.942 107.013 124.934 1.00 82.35  ? 3746 GLU A C     1 
ATOM   17173 O O     . GLU A 1 3746 ? 149.423 106.386 124.005 1.00 82.35  ? 3746 GLU A O     1 
ATOM   17174 C CB    . GLU A 1 3746 ? 149.243 106.422 127.254 1.00 82.35  ? 3746 GLU A CB    1 
ATOM   17175 C CG    . GLU A 1 3746 ? 148.186 105.369 127.095 1.00 82.35  ? 3746 GLU A CG    1 
ATOM   17176 C CD    . GLU A 1 3746 ? 147.165 105.819 126.063 1.00 82.35  ? 3746 GLU A CD    1 
ATOM   17177 O OE1   . GLU A 1 3746 ? 146.326 105.021 125.638 1.00 82.35  ? 3746 GLU A OE1   1 
ATOM   17178 O OE2   . GLU A 1 3746 ? 147.179 107.014 125.702 1.00 82.35  ? 3746 GLU A OE2   1 
ATOM   17179 N N     . LYS A 1 3747 ? 150.112 108.332 124.887 1.00 82.97  ? 3747 LYS A N     1 
ATOM   17180 C CA    . LYS A 1 3747 ? 149.749 109.062 123.678 1.00 82.97  ? 3747 LYS A CA    1 
ATOM   17181 C C     . LYS A 1 3747 ? 150.634 108.633 122.514 1.00 82.97  ? 3747 LYS A C     1 
ATOM   17182 O O     . LYS A 1 3747 ? 150.177 108.547 121.366 1.00 82.97  ? 3747 LYS A O     1 
ATOM   17183 C CB    . LYS A 1 3747 ? 149.849 110.566 123.931 1.00 82.97  ? 3747 LYS A CB    1 
ATOM   17184 C CG    . LYS A 1 3747 ? 148.500 111.251 124.087 1.00 82.97  ? 3747 LYS A CG    1 
ATOM   17185 C CD    . LYS A 1 3747 ? 147.776 110.742 125.330 1.00 82.97  ? 3747 LYS A CD    1 
ATOM   17186 C CE    . LYS A 1 3747 ? 146.526 111.555 125.626 1.00 82.97  ? 3747 LYS A CE    1 
ATOM   17187 N NZ    . LYS A 1 3747 ? 145.614 110.854 126.575 1.00 82.97  ? 3747 LYS A NZ    1 
ATOM   17188 N N     . SER A 1 3748 ? 151.906 108.346 122.802 1.00 85.98  ? 3748 SER A N     1 
ATOM   17189 C CA    . SER A 1 3748 ? 152.792 107.773 121.793 1.00 85.98  ? 3748 SER A CA    1 
ATOM   17190 C C     . SER A 1 3748 ? 152.294 106.409 121.326 1.00 85.98  ? 3748 SER A C     1 
ATOM   17191 O O     . SER A 1 3748 ? 152.333 106.104 120.128 1.00 85.98  ? 3748 SER A O     1 
ATOM   17192 C CB    . SER A 1 3748 ? 154.215 107.666 122.343 1.00 85.98  ? 3748 SER A CB    1 
ATOM   17193 O OG    . SER A 1 3748 ? 154.756 108.949 122.609 1.00 85.98  ? 3748 SER A OG    1 
ATOM   17194 N N     . LEU A 1 3749 ? 151.831 105.573 122.258 1.00 84.08  ? 3749 LEU A N     1 
ATOM   17195 C CA    . LEU A 1 3749 ? 151.261 104.281 121.878 1.00 84.08  ? 3749 LEU A CA    1 
ATOM   17196 C C     . LEU A 1 3749 ? 150.052 104.465 120.969 1.00 84.08  ? 3749 LEU A C     1 
ATOM   17197 O O     . LEU A 1 3749 ? 149.900 103.761 119.964 1.00 84.08  ? 3749 LEU A O     1 
ATOM   17198 C CB    . LEU A 1 3749 ? 150.869 103.489 123.125 1.00 84.08  ? 3749 LEU A CB    1 
ATOM   17199 C CG    . LEU A 1 3749 ? 149.961 102.281 122.873 1.00 84.08  ? 3749 LEU A CG    1 
ATOM   17200 C CD1   . LEU A 1 3749 ? 150.706 101.187 122.125 1.00 84.08  ? 3749 LEU A CD1   1 
ATOM   17201 C CD2   . LEU A 1 3749 ? 149.371 101.747 124.169 1.00 84.08  ? 3749 LEU A CD2   1 
ATOM   17202 N N     . LEU A 1 3750 ? 149.178 105.411 121.318 1.00 85.32  ? 3750 LEU A N     1 
ATOM   17203 C CA    . LEU A 1 3750 ? 147.978 105.669 120.526 1.00 85.32  ? 3750 LEU A CA    1 
ATOM   17204 C C     . LEU A 1 3750 ? 148.329 106.121 119.114 1.00 85.32  ? 3750 LEU A C     1 
ATOM   17205 O O     . LEU A 1 3750 ? 147.760 105.623 118.131 1.00 85.32  ? 3750 LEU A O     1 
ATOM   17206 C CB    . LEU A 1 3750 ? 147.114 106.726 121.216 1.00 85.32  ? 3750 LEU A CB    1 
ATOM   17207 C CG    . LEU A 1 3750 ? 146.510 106.397 122.581 1.00 85.32  ? 3750 LEU A CG    1 
ATOM   17208 C CD1   . LEU A 1 3750 ? 145.507 107.467 123.001 1.00 85.32  ? 3750 LEU A CD1   1 
ATOM   17209 C CD2   . LEU A 1 3750 ? 145.854 105.030 122.540 1.00 85.32  ? 3750 LEU A CD2   1 
ATOM   17210 N N     . GLN A 1 3751 ? 149.260 107.072 118.992 1.00 86.26  ? 3751 GLN A N     1 
ATOM   17211 C CA    . GLN A 1 3751 ? 149.647 107.548 117.669 1.00 86.26  ? 3751 GLN A CA    1 
ATOM   17212 C C     . GLN A 1 3751 ? 150.363 106.474 116.858 1.00 86.26  ? 3751 GLN A C     1 
ATOM   17213 O O     . GLN A 1 3751 ? 150.120 106.367 115.653 1.00 86.26  ? 3751 GLN A O     1 
ATOM   17214 C CB    . GLN A 1 3751 ? 150.499 108.818 117.781 1.00 86.26  ? 3751 GLN A CB    1 
ATOM   17215 C CG    . GLN A 1 3751 ? 151.877 108.643 118.390 1.00 86.26  ? 3751 GLN A CG    1 
ATOM   17216 C CD    . GLN A 1 3751 ? 152.340 109.882 119.134 1.00 86.26  ? 3751 GLN A CD    1 
ATOM   17217 O OE1   . GLN A 1 3751 ? 151.539 110.756 119.466 1.00 86.26  ? 3751 GLN A OE1   1 
ATOM   17218 N NE2   . GLN A 1 3751 ? 153.638 109.962 119.405 1.00 86.26  ? 3751 GLN A NE2   1 
ATOM   17219 N N     . ALA A 1 3752 ? 151.213 105.659 117.487 1.00 87.73  ? 3752 ALA A N     1 
ATOM   17220 C CA    . ALA A 1 3752 ? 151.836 104.555 116.766 1.00 87.73  ? 3752 ALA A CA    1 
ATOM   17221 C C     . ALA A 1 3752 ? 150.797 103.550 116.282 1.00 87.73  ? 3752 ALA A C     1 
ATOM   17222 O O     . ALA A 1 3752 ? 150.871 103.082 115.139 1.00 87.73  ? 3752 ALA A O     1 
ATOM   17223 C CB    . ALA A 1 3752 ? 152.874 103.867 117.653 1.00 87.73  ? 3752 ALA A CB    1 
ATOM   17224 N N     . LEU A 1 3753 ? 149.821 103.218 117.131 1.00 88.93  ? 3753 LEU A N     1 
ATOM   17225 C CA    . LEU A 1 3753 ? 148.787 102.267 116.737 1.00 88.93  ? 3753 LEU A CA    1 
ATOM   17226 C C     . LEU A 1 3753 ? 147.961 102.793 115.572 1.00 88.93  ? 3753 LEU A C     1 
ATOM   17227 O O     . LEU A 1 3753 ? 147.698 102.057 114.613 1.00 88.93  ? 3753 LEU A O     1 
ATOM   17228 C CB    . LEU A 1 3753 ? 147.883 101.943 117.925 1.00 88.93  ? 3753 LEU A CB    1 
ATOM   17229 C CG    . LEU A 1 3753 ? 148.446 100.999 118.987 1.00 88.93  ? 3753 LEU A CG    1 
ATOM   17230 C CD1   . LEU A 1 3753 ? 147.540 100.971 120.206 1.00 88.93  ? 3753 LEU A CD1   1 
ATOM   17231 C CD2   . LEU A 1 3753 ? 148.621 99.603  118.415 1.00 88.93  ? 3753 LEU A CD2   1 
ATOM   17232 N N     . ASN A 1 3754 ? 147.542 104.060 115.627 1.00 87.54  ? 3754 ASN A N     1 
ATOM   17233 C CA    . ASN A 1 3754 ? 146.728 104.576 114.531 1.00 87.54  ? 3754 ASN A CA    1 
ATOM   17234 C C     . ASN A 1 3754 ? 147.554 104.869 113.284 1.00 87.54  ? 3754 ASN A C     1 
ATOM   17235 O O     . ASN A 1 3754 ? 146.984 104.974 112.193 1.00 87.54  ? 3754 ASN A O     1 
ATOM   17236 C CB    . ASN A 1 3754 ? 145.946 105.819 114.968 1.00 87.54  ? 3754 ASN A CB    1 
ATOM   17237 C CG    . ASN A 1 3754 ? 146.835 106.929 115.486 1.00 87.54  ? 3754 ASN A CG    1 
ATOM   17238 O OD1   . ASN A 1 3754 ? 147.734 107.402 114.792 1.00 87.54  ? 3754 ASN A OD1   1 
ATOM   17239 N ND2   . ASN A 1 3754 ? 146.573 107.365 116.713 1.00 87.54  ? 3754 ASN A ND2   1 
ATOM   17240 N N     . GLU A 1 3755 ? 148.877 105.004 113.414 1.00 86.85  ? 3755 GLU A N     1 
ATOM   17241 C CA    . GLU A 1 3755 ? 149.720 105.122 112.231 1.00 86.85  ? 3755 GLU A CA    1 
ATOM   17242 C C     . GLU A 1 3755 ? 149.934 103.770 111.558 1.00 86.85  ? 3755 GLU A C     1 
ATOM   17243 O O     . GLU A 1 3755 ? 149.958 103.686 110.325 1.00 86.85  ? 3755 GLU A O     1 
ATOM   17244 C CB    . GLU A 1 3755 ? 151.062 105.755 112.604 1.00 86.85  ? 3755 GLU A CB    1 
ATOM   17245 C CG    . GLU A 1 3755 ? 151.887 106.232 111.416 0.00 86.85  ? 3755 GLU A CG    1 
ATOM   17246 C CD    . GLU A 1 3755 ? 152.781 105.148 110.846 0.00 86.85  ? 3755 GLU A CD    1 
ATOM   17247 O OE1   . GLU A 1 3755 ? 153.190 104.248 111.610 0.00 86.85  ? 3755 GLU A OE1   1 
ATOM   17248 O OE2   . GLU A 1 3755 ? 153.078 105.196 109.633 0.00 86.85  ? 3755 GLU A OE2   1 
ATOM   17249 N N     . VAL A 1 3756 ? 150.092 102.701 112.348 1.00 88.10  ? 3756 VAL A N     1 
ATOM   17250 C CA    . VAL A 1 3756 ? 150.322 101.373 111.779 1.00 88.10  ? 3756 VAL A CA    1 
ATOM   17251 C C     . VAL A 1 3756 ? 149.037 100.591 111.551 1.00 88.10  ? 3756 VAL A C     1 
ATOM   17252 O O     . VAL A 1 3756 ? 149.087 99.503  110.956 1.00 88.10  ? 3756 VAL A O     1 
ATOM   17253 C CB    . VAL A 1 3756 ? 151.258 100.531 112.669 1.00 88.10  ? 3756 VAL A CB    1 
ATOM   17254 C CG1   . VAL A 1 3756 ? 152.538 101.296 112.972 1.00 88.10  ? 3756 VAL A CG1   1 
ATOM   17255 C CG2   . VAL A 1 3756 ? 150.549 100.119 113.951 1.00 88.10  ? 3756 VAL A CG2   1 
ATOM   17256 N N     . LYS A 1 3757 ? 147.893 101.100 112.013 1.00 85.57  ? 3757 LYS A N     1 
ATOM   17257 C CA    . LYS A 1 3757 ? 146.585 100.470 111.836 1.00 85.57  ? 3757 LYS A CA    1 
ATOM   17258 C C     . LYS A 1 3757 ? 146.511 99.084  112.472 1.00 85.57  ? 3757 LYS A C     1 
ATOM   17259 O O     . LYS A 1 3757 ? 145.655 98.274  112.101 1.00 85.57  ? 3757 LYS A O     1 
ATOM   17260 C CB    . LYS A 1 3757 ? 146.200 100.387 110.354 1.00 85.57  ? 3757 LYS A CB    1 
ATOM   17261 C CG    . LYS A 1 3757 ? 146.350 101.695 109.596 0.00 85.57  ? 3757 LYS A CG    1 
ATOM   17262 C CD    . LYS A 1 3757 ? 146.501 101.449 108.104 0.00 85.57  ? 3757 LYS A CD    1 
ATOM   17263 C CE    . LYS A 1 3757 ? 147.674 100.525 107.810 0.00 85.57  ? 3757 LYS A CE    1 
ATOM   17264 N NZ    . LYS A 1 3757 ? 148.962 101.076 108.313 0.00 85.57  ? 3757 LYS A NZ    1 
ATOM   17265 N N     . GLY A 1 3758 ? 147.388 98.797  113.429 1.00 84.88  ? 3758 GLY A N     1 
ATOM   17266 C CA    . GLY A 1 3758 ? 147.377 97.501  114.092 1.00 84.88  ? 3758 GLY A CA    1 
ATOM   17267 C C     . GLY A 1 3758 ? 147.667 96.335  113.172 1.00 84.88  ? 3758 GLY A C     1 
ATOM   17268 O O     . GLY A 1 3758 ? 147.020 95.286  113.280 1.00 84.88  ? 3758 GLY A O     1 
ATOM   17269 N N     . ARG A 1 3759 ? 148.626 96.495  112.265 1.00 83.79  ? 3759 ARG A N     1 
ATOM   17270 C CA    . ARG A 1 3759 ? 148.970 95.423  111.341 1.00 83.79  ? 3759 ARG A CA    1 
ATOM   17271 C C     . ARG A 1 3759 ? 149.636 94.269  112.080 1.00 83.79  ? 3759 ARG A C     1 
ATOM   17272 O O     . ARG A 1 3759 ? 150.419 94.475  113.012 1.00 83.79  ? 3759 ARG A O     1 
ATOM   17273 C CB    . ARG A 1 3759 ? 149.894 95.943  110.241 1.00 83.79  ? 3759 ARG A CB    1 
ATOM   17274 C CG    . ARG A 1 3759 ? 149.176 96.681  109.124 0.00 83.79  ? 3759 ARG A CG    1 
ATOM   17275 C CD    . ARG A 1 3759 ? 150.168 97.300  108.156 0.00 83.79  ? 3759 ARG A CD    1 
ATOM   17276 N NE    . ARG A 1 3759 ? 151.078 96.303  107.605 0.00 83.79  ? 3759 ARG A NE    1 
ATOM   17277 C CZ    . ARG A 1 3759 ? 151.212 96.043  106.312 0.00 83.79  ? 3759 ARG A CZ    1 
ATOM   17278 N NH1   . ARG A 1 3759 ? 150.507 96.692  105.400 0.00 83.79  ? 3759 ARG A NH1   1 
ATOM   17279 N NH2   . ARG A 1 3759 ? 152.075 95.108  105.924 0.00 83.79  ? 3759 ARG A NH2   1 
ATOM   17280 N N     . ILE A 1 3760 ? 149.315 93.044  111.658 1.00 83.49  ? 3760 ILE A N     1 
ATOM   17281 C CA    . ILE A 1 3760 ? 149.907 91.865  112.277 1.00 83.49  ? 3760 ILE A CA    1 
ATOM   17282 C C     . ILE A 1 3760 ? 151.393 91.751  111.959 1.00 83.49  ? 3760 ILE A C     1 
ATOM   17283 O O     . ILE A 1 3760 ? 152.125 91.059  112.676 1.00 83.49  ? 3760 ILE A O     1 
ATOM   17284 C CB    . ILE A 1 3760 ? 149.145 90.596  111.848 1.00 83.49  ? 3760 ILE A CB    1 
ATOM   17285 C CG1   . ILE A 1 3760 ? 149.281 89.505  112.912 0.00 83.49  ? 3760 ILE A CG1   1 
ATOM   17286 C CG2   . ILE A 1 3760 ? 149.634 90.097  110.496 0.00 83.49  ? 3760 ILE A CG2   1 
ATOM   17287 C CD1   . ILE A 1 3760 ? 148.293 88.371  112.750 0.00 83.49  ? 3760 ILE A CD1   1 
ATOM   17288 N N     . LEU A 1 3761 ? 151.862 92.408  110.895 1.00 85.29  ? 3761 LEU A N     1 
ATOM   17289 C CA    . LEU A 1 3761 ? 153.295 92.440  110.622 1.00 85.29  ? 3761 LEU A CA    1 
ATOM   17290 C C     . LEU A 1 3761 ? 154.015 93.413  111.546 1.00 85.29  ? 3761 LEU A C     1 
ATOM   17291 O O     . LEU A 1 3761 ? 155.167 93.171  111.926 1.00 85.29  ? 3761 LEU A O     1 
ATOM   17292 C CB    . LEU A 1 3761 ? 153.542 92.805  109.158 1.00 85.29  ? 3761 LEU A CB    1 
ATOM   17293 C CG    . LEU A 1 3761 ? 154.999 92.831  108.691 0.00 85.29  ? 3761 LEU A CG    1 
ATOM   17294 C CD1   . LEU A 1 3761 ? 155.513 91.418  108.462 0.00 85.29  ? 3761 LEU A CD1   1 
ATOM   17295 C CD2   . LEU A 1 3761 ? 155.141 93.668  107.430 0.00 85.29  ? 3761 LEU A CD2   1 
ATOM   17296 N N     . ASP A 1 3762 ? 153.356 94.509  111.920 1.00 88.95  ? 3762 ASP A N     1 
ATOM   17297 C CA    . ASP A 1 3762 ? 153.892 95.478  112.868 1.00 88.95  ? 3762 ASP A CA    1 
ATOM   17298 C C     . ASP A 1 3762 ? 153.752 95.011  114.313 1.00 88.95  ? 3762 ASP A C     1 
ATOM   17299 O O     . ASP A 1 3762 ? 153.987 95.802  115.238 1.00 88.95  ? 3762 ASP A O     1 
ATOM   17300 C CB    . ASP A 1 3762 ? 153.186 96.825  112.668 1.00 88.95  ? 3762 ASP A CB    1 
ATOM   17301 C CG    . ASP A 1 3762 ? 153.956 97.989  113.260 0.00 88.95  ? 3762 ASP A CG    1 
ATOM   17302 O OD1   . ASP A 1 3762 ? 154.902 98.473  112.603 0.00 88.95  ? 3762 ASP A OD1   1 
ATOM   17303 O OD2   . ASP A 1 3762 ? 153.610 98.430  114.376 0.00 88.95  ? 3762 ASP A OD2   1 
ATOM   17304 N N     . ASP A 1 3763 ? 153.384 93.744  114.520 1.00 91.10  ? 3763 ASP A N     1 
ATOM   17305 C CA    . ASP A 1 3763 ? 153.075 93.237  115.849 1.00 91.10  ? 3763 ASP A CA    1 
ATOM   17306 C C     . ASP A 1 3763 ? 154.289 93.243  116.767 1.00 91.10  ? 3763 ASP A C     1 
ATOM   17307 O O     . ASP A 1 3763 ? 154.160 93.489  117.965 1.00 91.10  ? 3763 ASP A O     1 
ATOM   17308 C CB    . ASP A 1 3763 ? 152.495 91.824  115.756 1.00 91.10  ? 3763 ASP A CB    1 
ATOM   17309 C CG    . ASP A 1 3763 ? 152.053 91.292  117.106 0.00 91.10  ? 3763 ASP A CG    1 
ATOM   17310 O OD1   . ASP A 1 3763 ? 151.033 91.783  117.632 0.00 91.10  ? 3763 ASP A OD1   1 
ATOM   17311 O OD2   . ASP A 1 3763 ? 152.734 90.398  117.650 0.00 91.10  ? 3763 ASP A OD2   1 
ATOM   17312 N N     . ASP A 1 3764 ? 155.474 92.942  116.234 1.00 91.75  ? 3764 ASP A N     1 
ATOM   17313 C CA    . ASP A 1 3764 ? 156.669 92.944  117.075 1.00 91.75  ? 3764 ASP A CA    1 
ATOM   17314 C C     . ASP A 1 3764 ? 156.939 94.336  117.635 1.00 91.75  ? 3764 ASP A C     1 
ATOM   17315 O O     . ASP A 1 3764 ? 157.202 94.500  118.835 1.00 91.75  ? 3764 ASP A O     1 
ATOM   17316 C CB    . ASP A 1 3764 ? 157.874 92.437  116.282 1.00 91.75  ? 3764 ASP A CB    1 
ATOM   17317 C CG    . ASP A 1 3764 ? 159.171 92.552  117.059 0.00 91.75  ? 3764 ASP A CG    1 
ATOM   17318 O OD1   . ASP A 1 3764 ? 159.272 91.943  118.145 0.00 91.75  ? 3764 ASP A OD1   1 
ATOM   17319 O OD2   . ASP A 1 3764 ? 160.091 93.252  116.585 0.00 91.75  ? 3764 ASP A OD2   1 
ATOM   17320 N N     . THR A 1 3765 ? 156.861 95.357  116.778 1.00 91.96  ? 3765 THR A N     1 
ATOM   17321 C CA    . THR A 1 3765 ? 157.072 96.727  117.234 1.00 91.96  ? 3765 THR A CA    1 
ATOM   17322 C C     . THR A 1 3765 ? 155.978 97.157  118.202 1.00 91.96  ? 3765 THR A C     1 
ATOM   17323 O O     . THR A 1 3765 ? 156.245 97.880  119.169 1.00 91.96  ? 3765 THR A O     1 
ATOM   17324 C CB    . THR A 1 3765 ? 157.132 97.680  116.041 1.00 91.96  ? 3765 THR A CB    1 
ATOM   17325 O OG1   . THR A 1 3765 ? 155.803 97.967  115.592 1.00 91.96  ? 3765 THR A OG1   1 
ATOM   17326 C CG2   . THR A 1 3765 ? 157.923 97.055  114.900 1.00 91.96  ? 3765 THR A CG2   1 
ATOM   17327 N N     . ILE A 1 3766 ? 154.737 96.733  117.954 1.00 92.20  ? 3766 ILE A N     1 
ATOM   17328 C CA    . ILE A 1 3766 ? 153.648 97.073  118.868 1.00 92.20  ? 3766 ILE A CA    1 
ATOM   17329 C C     . ILE A 1 3766 ? 153.866 96.416  120.228 1.00 92.20  ? 3766 ILE A C     1 
ATOM   17330 O O     . ILE A 1 3766 ? 153.682 97.045  121.277 1.00 92.20  ? 3766 ILE A O     1 
ATOM   17331 C CB    . ILE A 1 3766 ? 152.290 96.678  118.260 1.00 92.20  ? 3766 ILE A CB    1 
ATOM   17332 C CG1   . ILE A 1 3766 ? 151.986 97.541  117.034 1.00 92.20  ? 3766 ILE A CG1   1 
ATOM   17333 C CG2   . ILE A 1 3766 ? 151.181 96.809  119.291 1.00 92.20  ? 3766 ILE A CG2   1 
ATOM   17334 C CD1   . ILE A 1 3766 ? 152.104 99.029  117.289 1.00 92.20  ? 3766 ILE A CD1   1 
ATOM   17335 N N     . ILE A 1 3767 ? 154.270 95.144  120.229 1.00 93.97  ? 3767 ILE A N     1 
ATOM   17336 C CA    . ILE A 1 3767 ? 154.408 94.387  121.470 1.00 93.97  ? 3767 ILE A CA    1 
ATOM   17337 C C     . ILE A 1 3767 ? 155.585 94.905  122.286 1.00 93.97  ? 3767 ILE A C     1 
ATOM   17338 O O     . ILE A 1 3767 ? 155.534 94.937  123.519 1.00 93.97  ? 3767 ILE A O     1 
ATOM   17339 C CB    . ILE A 1 3767 ? 154.538 92.882  121.169 1.00 93.97  ? 3767 ILE A CB    1 
ATOM   17340 C CG1   . ILE A 1 3767 ? 153.203 92.321  120.676 1.00 93.97  ? 3767 ILE A CG1   1 
ATOM   17341 C CG2   . ILE A 1 3767 ? 155.001 92.114  122.399 1.00 93.97  ? 3767 ILE A CG2   1 
ATOM   17342 C CD1   . ILE A 1 3767 ? 152.076 92.459  121.675 1.00 93.97  ? 3767 ILE A CD1   1 
ATOM   17343 N N     . THR A 1 3768 ? 156.670 95.305  121.617 1.00 92.61  ? 3768 THR A N     1 
ATOM   17344 C CA    . THR A 1 3768 ? 157.801 95.867  122.351 1.00 92.61  ? 3768 THR A CA    1 
ATOM   17345 C C     . THR A 1 3768 ? 157.391 97.134  123.097 1.00 92.61  ? 3768 THR A C     1 
ATOM   17346 O O     . THR A 1 3768 ? 157.695 97.302  124.286 1.00 92.61  ? 3768 THR A O     1 
ATOM   17347 C CB    . THR A 1 3768 ? 158.961 96.155  121.396 1.00 92.61  ? 3768 THR A CB    1 
ATOM   17348 O OG1   . THR A 1 3768 ? 159.165 95.026  120.537 1.00 92.61  ? 3768 THR A OG1   1 
ATOM   17349 C CG2   . THR A 1 3768 ? 160.237 96.427  122.178 1.00 92.61  ? 3768 THR A CG2   1 
ATOM   17350 N N     . THR A 1 3769 ? 156.667 98.025  122.417 1.00 91.06  ? 3769 THR A N     1 
ATOM   17351 C CA    . THR A 1 3769 ? 156.176 99.236  123.064 1.00 91.06  ? 3769 THR A CA    1 
ATOM   17352 C C     . THR A 1 3769 ? 155.203 98.899  124.187 1.00 91.06  ? 3769 THR A C     1 
ATOM   17353 O O     . THR A 1 3769 ? 155.237 99.510  125.260 1.00 91.06  ? 3769 THR A O     1 
ATOM   17354 C CB    . THR A 1 3769 ? 155.511 100.149 122.032 1.00 91.06  ? 3769 THR A CB    1 
ATOM   17355 O OG1   . THR A 1 3769 ? 156.346 100.253 120.872 1.00 91.06  ? 3769 THR A OG1   1 
ATOM   17356 C CG2   . THR A 1 3769 ? 155.285 101.537 122.613 1.00 91.06  ? 3769 THR A CG2   1 
ATOM   17357 N N     . LEU A 1 3770 ? 154.328 97.918  123.954 1.00 91.92  ? 3770 LEU A N     1 
ATOM   17358 C CA    . LEU A 1 3770 ? 153.331 97.549  124.953 1.00 91.92  ? 3770 LEU A CA    1 
ATOM   17359 C C     . LEU A 1 3770 ? 153.986 96.988  126.211 1.00 91.92  ? 3770 LEU A C     1 
ATOM   17360 O O     . LEU A 1 3770 ? 153.584 97.313  127.332 1.00 91.92  ? 3770 LEU A O     1 
ATOM   17361 C CB    . LEU A 1 3770 ? 152.350 96.539  124.355 1.00 91.92  ? 3770 LEU A CB    1 
ATOM   17362 C CG    . LEU A 1 3770 ? 151.147 97.143  123.629 1.00 91.92  ? 3770 LEU A CG    1 
ATOM   17363 C CD1   . LEU A 1 3770 ? 150.311 96.057  122.974 1.00 91.92  ? 3770 LEU A CD1   1 
ATOM   17364 C CD2   . LEU A 1 3770 ? 150.304 97.968  124.588 1.00 91.92  ? 3770 LEU A CD2   1 
ATOM   17365 N N     . GLU A 1 3771 ? 155.005 96.142  126.043 1.00 93.75  ? 3771 GLU A N     1 
ATOM   17366 C CA    . GLU A 1 3771 ? 155.680 95.573  127.204 1.00 93.75  ? 3771 GLU A CA    1 
ATOM   17367 C C     . GLU A 1 3771 ? 156.524 96.623  127.916 1.00 93.75  ? 3771 GLU A C     1 
ATOM   17368 O O     . GLU A 1 3771 ? 156.654 96.590  129.144 1.00 93.75  ? 3771 GLU A O     1 
ATOM   17369 C CB    . GLU A 1 3771 ? 156.530 94.364  126.798 1.00 93.75  ? 3771 GLU A CB    1 
ATOM   17370 C CG    . GLU A 1 3771 ? 157.690 94.658  125.864 1.00 93.75  ? 3771 GLU A CG    1 
ATOM   17371 C CD    . GLU A 1 3771 ? 158.967 95.008  126.605 1.00 93.75  ? 3771 GLU A CD    1 
ATOM   17372 O OE1   . GLU A 1 3771 ? 159.073 94.666  127.802 1.00 93.75  ? 3771 GLU A OE1   1 
ATOM   17373 O OE2   . GLU A 1 3771 ? 159.863 95.626  125.992 1.00 93.75  ? 3771 GLU A OE2   1 
ATOM   17374 N N     . ASN A 1 3772 ? 157.093 97.576  127.170 1.00 91.28  ? 3772 ASN A N     1 
ATOM   17375 C CA    . ASN A 1 3772 ? 157.782 98.685  127.823 1.00 91.28  ? 3772 ASN A CA    1 
ATOM   17376 C C     . ASN A 1 3772 ? 156.813 99.516  128.657 1.00 91.28  ? 3772 ASN A C     1 
ATOM   17377 O O     . ASN A 1 3772 ? 157.134 99.921  129.783 1.00 91.28  ? 3772 ASN A O     1 
ATOM   17378 C CB    . ASN A 1 3772 ? 158.484 99.558  126.783 1.00 91.28  ? 3772 ASN A CB    1 
ATOM   17379 C CG    . ASN A 1 3772 ? 159.659 100.320 127.362 1.00 91.28  ? 3772 ASN A CG    1 
ATOM   17380 O OD1   . ASN A 1 3772 ? 159.484 101.244 128.156 1.00 91.28  ? 3772 ASN A OD1   1 
ATOM   17381 N ND2   . ASN A 1 3772 ? 160.867 99.934  126.968 1.00 91.28  ? 3772 ASN A ND2   1 
ATOM   17382 N N     . LEU A 1 3773 ? 155.617 99.773  128.124 1.00 89.27  ? 3773 LEU A N     1 
ATOM   17383 C CA    . LEU A 1 3773 ? 154.609 100.512 128.879 1.00 89.27  ? 3773 LEU A CA    1 
ATOM   17384 C C     . LEU A 1 3773 ? 154.160 99.728  130.105 1.00 89.27  ? 3773 LEU A C     1 
ATOM   17385 O O     . LEU A 1 3773 ? 153.929 100.303 131.174 1.00 89.27  ? 3773 LEU A O     1 
ATOM   17386 C CB    . LEU A 1 3773 ? 153.414 100.841 127.987 1.00 89.27  ? 3773 LEU A CB    1 
ATOM   17387 C CG    . LEU A 1 3773 ? 153.704 101.770 126.811 1.00 89.27  ? 3773 LEU A CG    1 
ATOM   17388 C CD1   . LEU A 1 3773 ? 152.424 102.108 126.073 1.00 89.27  ? 3773 LEU A CD1   1 
ATOM   17389 C CD2   . LEU A 1 3773 ? 154.407 103.023 127.286 1.00 89.27  ? 3773 LEU A CD2   1 
ATOM   17390 N N     . LYS A 1 3774 ? 154.013 98.410  129.962 1.00 86.78  ? 3774 LYS A N     1 
ATOM   17391 C CA    . LYS A 1 3774 ? 153.644 97.579  131.102 1.00 86.78  ? 3774 LYS A CA    1 
ATOM   17392 C C     . LYS A 1 3774 ? 154.728 97.614  132.171 1.00 86.78  ? 3774 LYS A C     1 
ATOM   17393 O O     . LYS A 1 3774 ? 154.434 97.646  133.369 1.00 86.78  ? 3774 LYS A O     1 
ATOM   17394 C CB    . LYS A 1 3774 ? 153.377 96.142  130.648 1.00 86.78  ? 3774 LYS A CB    1 
ATOM   17395 C CG    . LYS A 1 3774 ? 152.826 95.249  131.751 1.00 86.78  ? 3774 LYS A CG    1 
ATOM   17396 C CD    . LYS A 1 3774 ? 152.438 93.874  131.230 1.00 86.78  ? 3774 LYS A CD    1 
ATOM   17397 C CE    . LYS A 1 3774 ? 153.493 93.311  130.292 1.00 86.78  ? 3774 LYS A CE    1 
ATOM   17398 N NZ    . LYS A 1 3774 ? 153.498 91.822  130.300 1.00 86.78  ? 3774 LYS A NZ    1 
ATOM   17399 N N     . ARG A 1 3775 ? 155.995 97.608  131.751 1.00 86.55  ? 3775 ARG A N     1 
ATOM   17400 C CA    . ARG A 1 3775 ? 157.100 97.717  132.698 1.00 86.55  ? 3775 ARG A CA    1 
ATOM   17401 C C     . ARG A 1 3775 ? 157.074 99.057  133.423 1.00 86.55  ? 3775 ARG A C     1 
ATOM   17402 O O     . ARG A 1 3775 ? 157.292 99.125  134.638 1.00 86.55  ? 3775 ARG A O     1 
ATOM   17403 C CB    . ARG A 1 3775 ? 158.430 97.524  131.967 1.00 86.55  ? 3775 ARG A CB    1 
ATOM   17404 C CG    . ARG A 1 3775 ? 159.639 97.447  132.881 0.00 86.55  ? 3775 ARG A CG    1 
ATOM   17405 C CD    . ARG A 1 3775 ? 160.858 96.932  132.134 0.00 86.55  ? 3775 ARG A CD    1 
ATOM   17406 N NE    . ARG A 1 3775 ? 160.537 95.792  131.283 0.00 86.55  ? 3775 ARG A NE    1 
ATOM   17407 C CZ    . ARG A 1 3775 ? 160.363 94.553  131.722 0.00 86.55  ? 3775 ARG A CZ    1 
ATOM   17408 N NH1   . ARG A 1 3775 ? 160.478 94.250  133.005 0.00 86.55  ? 3775 ARG A NH1   1 
ATOM   17409 N NH2   . ARG A 1 3775 ? 160.067 93.592  130.851 0.00 86.55  ? 3775 ARG A NH2   1 
ATOM   17410 N N     . GLU A 1 3776 ? 156.813 100.140 132.687 1.00 84.44  ? 3776 GLU A N     1 
ATOM   17411 C CA    . GLU A 1 3776 ? 156.726 101.459 133.309 1.00 84.44  ? 3776 GLU A CA    1 
ATOM   17412 C C     . GLU A 1 3776 ? 155.581 101.515 134.316 1.00 84.44  ? 3776 GLU A C     1 
ATOM   17413 O O     . GLU A 1 3776 ? 155.732 102.040 135.428 1.00 84.44  ? 3776 GLU A O     1 
ATOM   17414 C CB    . GLU A 1 3776 ? 156.549 102.533 132.233 1.00 84.44  ? 3776 GLU A CB    1 
ATOM   17415 C CG    . GLU A 1 3776 ? 157.771 102.748 131.354 1.00 84.44  ? 3776 GLU A CG    1 
ATOM   17416 C CD    . GLU A 1 3776 ? 158.985 103.200 132.138 1.00 84.44  ? 3776 GLU A CD    1 
ATOM   17417 O OE1   . GLU A 1 3776 ? 158.899 104.242 132.821 1.00 84.44  ? 3776 GLU A OE1   1 
ATOM   17418 O OE2   . GLU A 1 3776 ? 160.026 102.514 132.070 1.00 84.44  ? 3776 GLU A OE2   1 
ATOM   17419 N N     . ALA A 1 3777 ? 154.424 100.968 133.937 1.00 81.30  ? 3777 ALA A N     1 
ATOM   17420 C CA    . ALA A 1 3777 ? 153.277 100.950 134.836 1.00 81.30  ? 3777 ALA A CA    1 
ATOM   17421 C C     . ALA A 1 3777 ? 153.554 100.093 136.064 1.00 81.30  ? 3777 ALA A C     1 
ATOM   17422 O O     . ALA A 1 3777 ? 153.131 100.433 137.173 1.00 81.30  ? 3777 ALA A O     1 
ATOM   17423 C CB    . ALA A 1 3777 ? 152.037 100.449 134.097 1.00 81.30  ? 3777 ALA A CB    1 
ATOM   17424 N N     . ALA A 1 3778 ? 154.262 98.976  135.885 1.00 83.25  ? 3778 ALA A N     1 
ATOM   17425 C CA    . ALA A 1 3778 ? 154.622 98.129  137.016 1.00 83.25  ? 3778 ALA A CA    1 
ATOM   17426 C C     . ALA A 1 3778 ? 155.584 98.846  137.953 1.00 83.25  ? 3778 ALA A C     1 
ATOM   17427 O O     . ALA A 1 3778 ? 155.491 98.715  139.176 1.00 83.25  ? 3778 ALA A O     1 
ATOM   17428 C CB    . ALA A 1 3778 ? 155.230 96.818  136.515 1.00 83.25  ? 3778 ALA A CB    1 
ATOM   17429 N N     . GLU A 1 3779 ? 156.525 99.607  137.391 1.00 81.70  ? 3779 GLU A N     1 
ATOM   17430 C CA    . GLU A 1 3779 ? 157.437 100.390 138.220 1.00 81.70  ? 3779 GLU A CA    1 
ATOM   17431 C C     . GLU A 1 3779 ? 156.677 101.440 139.022 1.00 81.70  ? 3779 GLU A C     1 
ATOM   17432 O O     . GLU A 1 3779 ? 156.932 101.634 140.218 1.00 81.70  ? 3779 GLU A O     1 
ATOM   17433 C CB    . GLU A 1 3779 ? 158.506 101.046 137.345 1.00 81.70  ? 3779 GLU A CB    1 
ATOM   17434 C CG    . GLU A 1 3779 ? 159.544 101.842 138.119 1.00 81.70  ? 3779 GLU A CG    1 
ATOM   17435 C CD    . GLU A 1 3779 ? 160.425 100.966 138.989 1.00 81.70  ? 3779 GLU A CD    1 
ATOM   17436 O OE1   . GLU A 1 3779 ? 160.621 99.783  138.640 1.00 81.70  ? 3779 GLU A OE1   1 
ATOM   17437 O OE2   . GLU A 1 3779 ? 160.922 101.460 140.022 1.00 81.70  ? 3779 GLU A OE2   1 
ATOM   17438 N N     . VAL A 1 3780 ? 155.729 102.124 138.378 1.00 76.79  ? 3780 VAL A N     1 
ATOM   17439 C CA    . VAL A 1 3780 ? 154.926 103.123 139.083 1.00 76.79  ? 3780 VAL A CA    1 
ATOM   17440 C C     . VAL A 1 3780 ? 154.085 102.462 140.170 1.00 76.79  ? 3780 VAL A C     1 
ATOM   17441 O O     . VAL A 1 3780 ? 153.937 102.994 141.277 1.00 76.79  ? 3780 VAL A O     1 
ATOM   17442 C CB    . VAL A 1 3780 ? 154.053 103.911 138.089 1.00 76.79  ? 3780 VAL A CB    1 
ATOM   17443 C CG1   . VAL A 1 3780 ? 153.112 104.846 138.830 1.00 76.79  ? 3780 VAL A CG1   1 
ATOM   17444 C CG2   . VAL A 1 3780 ? 154.932 104.696 137.135 1.00 76.79  ? 3780 VAL A CG2   1 
ATOM   17445 N N     . THR A 1 3781 ? 153.518 101.293 139.868 1.00 78.77  ? 3781 THR A N     1 
ATOM   17446 C CA    . THR A 1 3781 ? 152.706 100.577 140.846 1.00 78.77  ? 3781 THR A CA    1 
ATOM   17447 C C     . THR A 1 3781 ? 153.550 100.126 142.033 1.00 78.77  ? 3781 THR A C     1 
ATOM   17448 O O     . THR A 1 3781 ? 153.097 100.164 143.181 1.00 78.77  ? 3781 THR A O     1 
ATOM   17449 C CB    . THR A 1 3781 ? 152.022 99.381  140.180 1.00 78.77  ? 3781 THR A CB    1 
ATOM   17450 O OG1   . THR A 1 3781 ? 151.255 99.834  139.057 1.00 78.77  ? 3781 THR A OG1   1 
ATOM   17451 C CG2   . THR A 1 3781 ? 151.095 98.681  141.161 1.00 78.77  ? 3781 THR A CG2   1 
ATOM   17452 N N     . ARG A 1 3782 ? 154.781 99.683  141.769 1.00 79.73  ? 3782 ARG A N     1 
ATOM   17453 C CA    . ARG A 1 3782 ? 155.694 99.332  142.852 1.00 79.73  ? 3782 ARG A CA    1 
ATOM   17454 C C     . ARG A 1 3782 ? 156.026 100.550 143.704 1.00 79.73  ? 3782 ARG A C     1 
ATOM   17455 O O     . ARG A 1 3782 ? 156.076 100.461 144.936 1.00 79.73  ? 3782 ARG A O     1 
ATOM   17456 C CB    . ARG A 1 3782 ? 156.971 98.713  142.282 1.00 79.73  ? 3782 ARG A CB    1 
ATOM   17457 C CG    . ARG A 1 3782 ? 158.168 98.787  143.216 1.00 79.73  ? 3782 ARG A CG    1 
ATOM   17458 C CD    . ARG A 1 3782 ? 159.436 98.295  142.539 1.00 79.73  ? 3782 ARG A CD    1 
ATOM   17459 N NE    . ARG A 1 3782 ? 160.620 98.555  143.349 1.00 79.73  ? 3782 ARG A NE    1 
ATOM   17460 C CZ    . ARG A 1 3782 ? 161.474 99.546  143.131 1.00 79.73  ? 3782 ARG A CZ    1 
ATOM   17461 N NH1   . ARG A 1 3782 ? 161.308 100.394 142.129 1.00 79.73  ? 3782 ARG A NH1   1 
ATOM   17462 N NH2   . ARG A 1 3782 ? 162.521 99.691  143.938 1.00 79.73  ? 3782 ARG A NH2   1 
ATOM   17463 N N     . LYS A 1 3783 ? 156.255 101.699 143.062 1.00 74.84  ? 3783 LYS A N     1 
ATOM   17464 C CA    . LYS A 1 3783 ? 156.521 102.921 143.813 1.00 74.84  ? 3783 LYS A CA    1 
ATOM   17465 C C     . LYS A 1 3783 ? 155.343 103.301 144.700 1.00 74.84  ? 3783 LYS A C     1 
ATOM   17466 O O     . LYS A 1 3783 ? 155.535 103.670 145.864 1.00 74.84  ? 3783 LYS A O     1 
ATOM   17467 C CB    . LYS A 1 3783 ? 156.852 104.066 142.856 1.00 74.84  ? 3783 LYS A CB    1 
ATOM   17468 C CG    . LYS A 1 3783 ? 158.238 103.994 142.240 1.00 74.84  ? 3783 LYS A CG    1 
ATOM   17469 C CD    . LYS A 1 3783 ? 158.562 105.269 141.477 1.00 74.84  ? 3783 LYS A CD    1 
ATOM   17470 C CE    . LYS A 1 3783 ? 159.987 105.251 140.952 1.00 74.84  ? 3783 LYS A CE    1 
ATOM   17471 N NZ    . LYS A 1 3783 ? 160.903 104.517 141.867 1.00 74.84  ? 3783 LYS A NZ    1 
ATOM   17472 N N     . VAL A 1 3784 ? 154.117 103.213 144.172 1.00 76.28  ? 3784 VAL A N     1 
ATOM   17473 C CA    . VAL A 1 3784 ? 152.922 103.518 144.956 1.00 76.28  ? 3784 VAL A CA    1 
ATOM   17474 C C     . VAL A 1 3784 ? 152.690 102.514 146.077 1.00 76.28  ? 3784 VAL A C     1 
ATOM   17475 O O     . VAL A 1 3784 ? 152.280 102.909 147.177 1.00 76.28  ? 3784 VAL A O     1 
ATOM   17476 C CB    . VAL A 1 3784 ? 151.675 103.599 144.050 1.00 76.28  ? 3784 VAL A CB    1 
ATOM   17477 C CG1   . VAL A 1 3784 ? 150.435 103.915 144.871 1.00 76.28  ? 3784 VAL A CG1   1 
ATOM   17478 C CG2   . VAL A 1 3784 ? 151.870 104.657 142.980 1.00 76.28  ? 3784 VAL A CG2   1 
ATOM   17479 N N     . GLU A 1 3785 ? 152.951 101.230 145.841 1.00 79.78  ? 3785 GLU A N     1 
ATOM   17480 C CA    . GLU A 1 3785 ? 152.783 100.199 146.854 1.00 79.78  ? 3785 GLU A CA    1 
ATOM   17481 C C     . GLU A 1 3785 ? 153.851 100.251 147.938 1.00 79.78  ? 3785 GLU A C     1 
ATOM   17482 O O     . GLU A 1 3785 ? 153.709 99.567  148.957 1.00 79.78  ? 3785 GLU A O     1 
ATOM   17483 C CB    . GLU A 1 3785 ? 152.793 98.811  146.200 1.00 79.78  ? 3785 GLU A CB    1 
ATOM   17484 C CG    . GLU A 1 3785 ? 151.479 98.423  145.540 1.00 79.78  ? 3785 GLU A CG    1 
ATOM   17485 C CD    . GLU A 1 3785 ? 151.672 97.472  144.373 1.00 79.78  ? 3785 GLU A CD    1 
ATOM   17486 O OE1   . GLU A 1 3785 ? 152.819 97.334  143.898 1.00 79.78  ? 3785 GLU A OE1   1 
ATOM   17487 O OE2   . GLU A 1 3785 ? 150.675 96.863  143.930 1.00 79.78  ? 3785 GLU A OE2   1 
ATOM   17488 N N     . GLU A 1 3786 ? 154.910 101.039 147.744 1.00 80.53  ? 3786 GLU A N     1 
ATOM   17489 C CA    . GLU A 1 3786 ? 155.991 101.155 148.715 1.00 80.53  ? 3786 GLU A CA    1 
ATOM   17490 C C     . GLU A 1 3786 ? 156.147 102.581 149.233 1.00 80.53  ? 3786 GLU A C     1 
ATOM   17491 O O     . GLU A 1 3786 ? 157.223 102.945 149.715 1.00 80.53  ? 3786 GLU A O     1 
ATOM   17492 C CB    . GLU A 1 3786 ? 157.308 100.669 148.106 1.00 80.53  ? 3786 GLU A CB    1 
ATOM   17493 C CG    . GLU A 1 3786 ? 157.405 99.160  147.951 1.00 80.53  ? 3786 GLU A CG    1 
ATOM   17494 C CD    . GLU A 1 3786 ? 158.816 98.694  147.649 1.00 80.53  ? 3786 GLU A CD    1 
ATOM   17495 O OE1   . GLU A 1 3786 ? 159.757 99.167  148.321 1.00 80.53  ? 3786 GLU A OE1   1 
ATOM   17496 O OE2   . GLU A 1 3786 ? 158.986 97.854  146.741 1.00 80.53  ? 3786 GLU A OE2   1 
ATOM   17497 N N     . THR A 1 3787 ? 155.094 103.398 149.141 1.00 78.56  ? 3787 THR A N     1 
ATOM   17498 C CA    . THR A 1 3787 ? 155.191 104.786 149.586 1.00 78.56  ? 3787 THR A CA    1 
ATOM   17499 C C     . THR A 1 3787 ? 155.458 104.872 151.083 1.00 78.56  ? 3787 THR A C     1 
ATOM   17500 O O     . THR A 1 3787 ? 156.266 105.691 151.532 1.00 78.56  ? 3787 THR A O     1 
ATOM   17501 C CB    . THR A 1 3787 ? 153.916 105.552 149.230 1.00 78.56  ? 3787 THR A CB    1 
ATOM   17502 O OG1   . THR A 1 3787 ? 152.774 104.853 149.742 1.00 78.56  ? 3787 THR A OG1   1 
ATOM   17503 C CG2   . THR A 1 3787 ? 153.788 105.714 147.725 1.00 78.56  ? 3787 THR A CG2   1 
ATOM   17504 N N     . ASP A 1 3788 ? 154.778 104.039 151.874 1.00 80.91  ? 3788 ASP A N     1 
ATOM   17505 C CA    . ASP A 1 3788 ? 154.936 104.109 153.324 1.00 80.91  ? 3788 ASP A CA    1 
ATOM   17506 C C     . ASP A 1 3788 ? 156.359 103.763 153.751 1.00 80.91  ? 3788 ASP A C     1 
ATOM   17507 O O     . ASP A 1 3788 ? 156.943 104.449 154.598 1.00 80.91  ? 3788 ASP A O     1 
ATOM   17508 C CB    . ASP A 1 3788 ? 153.923 103.190 154.009 1.00 80.91  ? 3788 ASP A CB    1 
ATOM   17509 C CG    . ASP A 1 3788 ? 154.040 101.745 153.559 1.00 80.91  ? 3788 ASP A CG    1 
ATOM   17510 O OD1   . ASP A 1 3788 ? 154.848 101.462 152.649 1.00 80.91  ? 3788 ASP A OD1   1 
ATOM   17511 O OD2   . ASP A 1 3788 ? 153.323 100.889 154.119 1.00 80.91  ? 3788 ASP A OD2   1 
ATOM   17512 N N     . ILE A 1 3789 ? 156.936 102.708 153.170 1.00 78.20  ? 3789 ILE A N     1 
ATOM   17513 C CA    . ILE A 1 3789 ? 158.280 102.287 153.557 1.00 78.20  ? 3789 ILE A CA    1 
ATOM   17514 C C     . ILE A 1 3789 ? 159.303 103.355 153.190 1.00 78.20  ? 3789 ILE A C     1 
ATOM   17515 O O     . ILE A 1 3789 ? 160.182 103.698 153.993 1.00 78.20  ? 3789 ILE A O     1 
ATOM   17516 C CB    . ILE A 1 3789 ? 158.621 100.932 152.910 1.00 78.20  ? 3789 ILE A CB    1 
ATOM   17517 C CG1   . ILE A 1 3789 ? 157.637 99.856  153.376 1.00 78.20  ? 3789 ILE A CG1   1 
ATOM   17518 C CG2   . ILE A 1 3789 ? 160.054 100.530 153.230 1.00 78.20  ? 3789 ILE A CG2   1 
ATOM   17519 C CD1   . ILE A 1 3789 ? 157.879 99.376  154.790 1.00 78.20  ? 3789 ILE A CD1   1 
ATOM   17520 N N     . VAL A 1 3790 ? 159.204 103.898 151.976 1.00 73.98  ? 3790 VAL A N     1 
ATOM   17521 C CA    . VAL A 1 3790 ? 160.142 104.927 151.541 1.00 73.98  ? 3790 VAL A CA    1 
ATOM   17522 C C     . VAL A 1 3790 ? 159.992 106.182 152.391 1.00 73.98  ? 3790 VAL A C     1 
ATOM   17523 O O     . VAL A 1 3790 ? 160.986 106.812 152.773 1.00 73.98  ? 3790 VAL A O     1 
ATOM   17524 C CB    . VAL A 1 3790 ? 159.950 105.225 150.043 1.00 73.98  ? 3790 VAL A CB    1 
ATOM   17525 C CG1   . VAL A 1 3790 ? 160.858 106.360 149.606 1.00 73.98  ? 3790 VAL A CG1   1 
ATOM   17526 C CG2   . VAL A 1 3790 ? 160.226 103.978 149.220 1.00 73.98  ? 3790 VAL A CG2   1 
ATOM   17527 N N     . MET A 1 3791 ? 158.751 106.568 152.700 1.00 72.12  ? 3791 MET A N     1 
ATOM   17528 C CA    . MET A 1 3791 ? 158.531 107.748 153.528 1.00 72.12  ? 3791 MET A CA    1 
ATOM   17529 C C     . MET A 1 3791 ? 159.105 107.560 154.926 1.00 72.12  ? 3791 MET A C     1 
ATOM   17530 O O     . MET A 1 3791 ? 159.733 108.474 155.470 1.00 72.12  ? 3791 MET A O     1 
ATOM   17531 C CB    . MET A 1 3791 ? 157.039 108.074 153.597 1.00 72.12  ? 3791 MET A CB    1 
ATOM   17532 C CG    . MET A 1 3791 ? 156.546 108.934 152.445 1.00 72.12  ? 3791 MET A CG    1 
ATOM   17533 S SD    . MET A 1 3791 ? 154.970 109.738 152.790 1.00 72.12  ? 3791 MET A SD    1 
ATOM   17534 C CE    . MET A 1 3791 ? 154.218 109.716 151.165 1.00 72.12  ? 3791 MET A CE    1 
ATOM   17535 N N     . GLN A 1 3792 ? 158.909 106.382 155.524 1.00 72.36  ? 3792 GLN A N     1 
ATOM   17536 C CA    . GLN A 1 3792 ? 159.476 106.134 156.846 1.00 72.36  ? 3792 GLN A CA    1 
ATOM   17537 C C     . GLN A 1 3792 ? 160.999 106.112 156.815 1.00 72.36  ? 3792 GLN A C     1 
ATOM   17538 O O     . GLN A 1 3792 ? 161.641 106.620 157.741 1.00 72.36  ? 3792 GLN A O     1 
ATOM   17539 C CB    . GLN A 1 3792 ? 158.935 104.827 157.424 1.00 72.36  ? 3792 GLN A CB    1 
ATOM   17540 C CG    . GLN A 1 3792 ? 157.449 104.863 157.738 1.00 72.36  ? 3792 GLN A CG    1 
ATOM   17541 C CD    . GLN A 1 3792 ? 156.937 103.549 158.293 1.00 72.36  ? 3792 GLN A CD    1 
ATOM   17542 O OE1   . GLN A 1 3792 ? 157.678 102.571 158.389 1.00 72.36  ? 3792 GLN A OE1   1 
ATOM   17543 N NE2   . GLN A 1 3792 ? 155.663 103.521 158.666 1.00 72.36  ? 3792 GLN A NE2   1 
ATOM   17544 N N     . GLU A 1 3793 ? 161.596 105.533 155.770 1.00 68.79  ? 3793 GLU A N     1 
ATOM   17545 C CA    . GLU A 1 3793 ? 163.052 105.549 155.657 1.00 68.79  ? 3793 GLU A CA    1 
ATOM   17546 C C     . GLU A 1 3793 ? 163.577 106.974 155.524 1.00 68.79  ? 3793 GLU A C     1 
ATOM   17547 O O     . GLU A 1 3793 ? 164.576 107.342 156.158 1.00 68.79  ? 3793 GLU A O     1 
ATOM   17548 C CB    . GLU A 1 3793 ? 163.494 104.697 154.467 1.00 68.79  ? 3793 GLU A CB    1 
ATOM   17549 C CG    . GLU A 1 3793 ? 165.000 104.592 154.303 1.00 68.79  ? 3793 GLU A CG    1 
ATOM   17550 C CD    . GLU A 1 3793 ? 165.399 103.613 153.217 1.00 68.79  ? 3793 GLU A CD    1 
ATOM   17551 O OE1   . GLU A 1 3793 ? 164.498 102.996 152.612 1.00 68.79  ? 3793 GLU A OE1   1 
ATOM   17552 O OE2   . GLU A 1 3793 ? 166.613 103.460 152.967 1.00 68.79  ? 3793 GLU A OE2   1 
ATOM   17553 N N     . VAL A 1 3794 ? 162.908 107.794 154.710 1.00 62.56  ? 3794 VAL A N     1 
ATOM   17554 C CA    . VAL A 1 3794 ? 163.312 109.189 154.558 1.00 62.56  ? 3794 VAL A CA    1 
ATOM   17555 C C     . VAL A 1 3794 ? 163.166 109.930 155.880 1.00 62.56  ? 3794 VAL A C     1 
ATOM   17556 O O     . VAL A 1 3794 ? 164.013 110.755 156.241 1.00 62.56  ? 3794 VAL A O     1 
ATOM   17557 C CB    . VAL A 1 3794 ? 162.501 109.859 153.432 1.00 62.56  ? 3794 VAL A CB    1 
ATOM   17558 C CG1   . VAL A 1 3794 ? 162.657 111.371 153.483 1.00 62.56  ? 3794 VAL A CG1   1 
ATOM   17559 C CG2   . VAL A 1 3794 ? 162.938 109.325 152.078 1.00 62.56  ? 3794 VAL A CG2   1 
ATOM   17560 N N     . GLU A 1 3795 ? 162.093 109.648 156.624 1.00 61.09  ? 3795 GLU A N     1 
ATOM   17561 C CA    . GLU A 1 3795 ? 161.910 110.279 157.927 1.00 61.09  ? 3795 GLU A CA    1 
ATOM   17562 C C     . GLU A 1 3795 ? 163.021 109.891 158.892 1.00 61.09  ? 3795 GLU A C     1 
ATOM   17563 O O     . GLU A 1 3795 ? 163.528 110.738 159.635 1.00 61.09  ? 3795 GLU A O     1 
ATOM   17564 C CB    . GLU A 1 3795 ? 160.544 109.909 158.509 1.00 61.09  ? 3795 GLU A CB    1 
ATOM   17565 C CG    . GLU A 1 3795 ? 159.352 110.543 157.801 1.00 61.09  ? 3795 GLU A CG    1 
ATOM   17566 C CD    . GLU A 1 3795 ? 159.454 112.054 157.689 1.00 61.09  ? 3795 GLU A CD    1 
ATOM   17567 O OE1   . GLU A 1 3795 ? 160.048 112.688 158.587 1.00 61.09  ? 3795 GLU A OE1   1 
ATOM   17568 O OE2   . GLU A 1 3795 ? 158.936 112.609 156.697 1.00 61.09  ? 3795 GLU A OE2   1 
ATOM   17569 N N     . THR A 1 3796 ? 163.410 108.613 158.904 1.00 55.31  ? 3796 THR A N     1 
ATOM   17570 C CA    . THR A 1 3796 ? 164.495 108.185 159.782 1.00 55.31  ? 3796 THR A CA    1 
ATOM   17571 C C     . THR A 1 3796 ? 165.808 108.864 159.411 1.00 55.31  ? 3796 THR A C     1 
ATOM   17572 O O     . THR A 1 3796 ? 166.551 109.320 160.289 1.00 55.31  ? 3796 THR A O     1 
ATOM   17573 C CB    . THR A 1 3796 ? 164.651 106.665 159.738 1.00 55.31  ? 3796 THR A CB    1 
ATOM   17574 O OG1   . THR A 1 3796 ? 164.836 106.239 158.383 1.00 55.31  ? 3796 THR A OG1   1 
ATOM   17575 C CG2   . THR A 1 3796 ? 163.425 105.984 160.325 1.00 55.31  ? 3796 THR A CG2   1 
ATOM   17576 N N     . VAL A 1 3797 ? 166.108 108.949 158.112 1.00 49.93  ? 3797 VAL A N     1 
ATOM   17577 C CA    . VAL A 1 3797 ? 167.346 109.602 157.689 1.00 49.93  ? 3797 VAL A CA    1 
ATOM   17578 C C     . VAL A 1 3797 ? 167.322 111.085 158.045 1.00 49.93  ? 3797 VAL A C     1 
ATOM   17579 O O     . VAL A 1 3797 ? 168.330 111.649 158.495 1.00 49.93  ? 3797 VAL A O     1 
ATOM   17580 C CB    . VAL A 1 3797 ? 167.582 109.379 156.184 1.00 49.93  ? 3797 VAL A CB    1 
ATOM   17581 C CG1   . VAL A 1 3797 ? 168.852 110.075 155.744 1.00 49.93  ? 3797 VAL A CG1   1 
ATOM   17582 C CG2   . VAL A 1 3797 ? 167.669 107.895 155.879 1.00 49.93  ? 3797 VAL A CG2   1 
ATOM   17583 N N     . SER A 1 3798 ? 166.177 111.742 157.850 1.00 48.67  ? 3798 SER A N     1 
ATOM   17584 C CA    . SER A 1 3798 ? 166.062 113.154 158.195 1.00 48.67  ? 3798 SER A CA    1 
ATOM   17585 C C     . SER A 1 3798 ? 166.208 113.372 159.695 1.00 48.67  ? 3798 SER A C     1 
ATOM   17586 O O     . SER A 1 3798 ? 166.823 114.351 160.125 1.00 48.67  ? 3798 SER A O     1 
ATOM   17587 C CB    . SER A 1 3798 ? 164.729 113.710 157.696 1.00 48.67  ? 3798 SER A CB    1 
ATOM   17588 O OG    . SER A 1 3798 ? 164.608 113.561 156.293 1.00 48.67  ? 3798 SER A OG    1 
ATOM   17589 N N     . GLN A 1 3799 ? 165.642 112.479 160.509 1.00 46.62  ? 3799 GLN A N     1 
ATOM   17590 C CA    . GLN A 1 3799 ? 165.823 112.588 161.953 1.00 46.62  ? 3799 GLN A CA    1 
ATOM   17591 C C     . GLN A 1 3799 ? 167.283 112.390 162.335 1.00 46.62  ? 3799 GLN A C     1 
ATOM   17592 O O     . GLN A 1 3799 ? 167.786 113.042 163.257 1.00 46.62  ? 3799 GLN A O     1 
ATOM   17593 C CB    . GLN A 1 3799 ? 164.935 111.576 162.677 1.00 46.62  ? 3799 GLN A CB    1 
ATOM   17594 C CG    . GLN A 1 3799 ? 163.445 111.882 162.608 1.00 46.62  ? 3799 GLN A CG    1 
ATOM   17595 C CD    . GLN A 1 3799 ? 163.148 113.369 162.590 1.00 46.62  ? 3799 GLN A CD    1 
ATOM   17596 O OE1   . GLN A 1 3799 ? 162.992 113.971 161.527 1.00 46.62  ? 3799 GLN A OE1   1 
ATOM   17597 N NE2   . GLN A 1 3799 ? 163.071 113.971 163.771 1.00 46.62  ? 3799 GLN A NE2   1 
ATOM   17598 N N     . GLN A 1 3800 ? 167.976 111.484 161.642 1.00 41.69  ? 3800 GLN A N     1 
ATOM   17599 C CA    . GLN A 1 3800 ? 169.398 111.287 161.903 1.00 41.69  ? 3800 GLN A CA    1 
ATOM   17600 C C     . GLN A 1 3800 ? 170.202 112.540 161.575 1.00 41.69  ? 3800 GLN A C     1 
ATOM   17601 O O     . GLN A 1 3800 ? 171.098 112.928 162.334 1.00 41.69  ? 3800 GLN A O     1 
ATOM   17602 C CB    . GLN A 1 3800 ? 169.916 110.092 161.103 1.00 41.69  ? 3800 GLN A CB    1 
ATOM   17603 C CG    . GLN A 1 3800 ? 171.428 109.951 161.108 1.00 41.69  ? 3800 GLN A CG    1 
ATOM   17604 C CD    . GLN A 1 3800 ? 171.891 108.613 160.569 1.00 41.69  ? 3800 GLN A CD    1 
ATOM   17605 O OE1   . GLN A 1 3800 ? 171.452 108.172 159.507 1.00 41.69  ? 3800 GLN A OE1   1 
ATOM   17606 N NE2   . GLN A 1 3800 ? 172.786 107.958 161.300 1.00 41.69  ? 3800 GLN A NE2   1 
ATOM   17607 N N     . TYR A 1 3801 ? 169.896 113.189 160.454 1.00 37.03  ? 3801 TYR A N     1 
ATOM   17608 C CA    . TYR A 1 3801 ? 170.686 114.326 159.990 1.00 37.03  ? 3801 TYR A CA    1 
ATOM   17609 C C     . TYR A 1 3801 ? 170.170 115.674 160.485 1.00 37.03  ? 3801 TYR A C     1 
ATOM   17610 O O     . TYR A 1 3801 ? 170.765 116.705 160.157 1.00 37.03  ? 3801 TYR A O     1 
ATOM   17611 C CB    . TYR A 1 3801 ? 170.749 114.332 158.460 1.00 37.03  ? 3801 TYR A CB    1 
ATOM   17612 C CG    . TYR A 1 3801 ? 171.724 113.328 157.891 1.00 37.03  ? 3801 TYR A CG    1 
ATOM   17613 C CD1   . TYR A 1 3801 ? 171.461 111.967 157.949 1.00 37.03  ? 3801 TYR A CD1   1 
ATOM   17614 C CD2   . TYR A 1 3801 ? 172.911 113.740 157.305 1.00 37.03  ? 3801 TYR A CD2   1 
ATOM   17615 C CE1   . TYR A 1 3801 ? 172.349 111.045 157.434 1.00 37.03  ? 3801 TYR A CE1   1 
ATOM   17616 C CE2   . TYR A 1 3801 ? 173.807 112.825 156.788 1.00 37.03  ? 3801 TYR A CE2   1 
ATOM   17617 C CZ    . TYR A 1 3801 ? 173.520 111.479 156.855 1.00 37.03  ? 3801 TYR A CZ    1 
ATOM   17618 O OH    . TYR A 1 3801 ? 174.408 110.563 156.342 1.00 37.03  ? 3801 TYR A OH    1 
ATOM   17619 N N     . LEU A 1 3802 ? 169.078 115.693 161.249 1.00 32.38  ? 3802 LEU A N     1 
ATOM   17620 C CA    . LEU A 1 3802 ? 168.545 116.951 161.771 1.00 32.38  ? 3802 LEU A CA    1 
ATOM   17621 C C     . LEU A 1 3802 ? 169.517 117.706 162.671 1.00 32.38  ? 3802 LEU A C     1 
ATOM   17622 O O     . LEU A 1 3802 ? 169.633 118.936 162.516 1.00 32.38  ? 3802 LEU A O     1 
ATOM   17623 C CB    . LEU A 1 3802 ? 167.224 116.669 162.495 1.00 32.38  ? 3802 LEU A CB    1 
ATOM   17624 C CG    . LEU A 1 3802 ? 166.405 117.853 163.010 1.00 32.38  ? 3802 LEU A CG    1 
ATOM   17625 C CD1   . LEU A 1 3802 ? 165.891 118.687 161.855 1.00 32.38  ? 3802 LEU A CD1   1 
ATOM   17626 C CD2   . LEU A 1 3802 ? 165.254 117.368 163.877 1.00 32.38  ? 3802 LEU A CD2   1 
ATOM   17627 N N     . PRO A 1 3803 ? 170.208 117.074 163.634 1.00 29.13  ? 3803 PRO A N     1 
ATOM   17628 C CA    . PRO A 1 3803 ? 171.105 117.858 164.501 1.00 29.13  ? 3803 PRO A CA    1 
ATOM   17629 C C     . PRO A 1 3803 ? 172.184 118.609 163.742 1.00 29.13  ? 3803 PRO A C     1 
ATOM   17630 O O     . PRO A 1 3803 ? 172.534 119.731 164.128 1.00 29.13  ? 3803 PRO A O     1 
ATOM   17631 C CB    . PRO A 1 3803 ? 171.701 116.796 165.434 1.00 29.13  ? 3803 PRO A CB    1 
ATOM   17632 C CG    . PRO A 1 3803 ? 170.686 115.722 165.466 1.00 29.13  ? 3803 PRO A CG    1 
ATOM   17633 C CD    . PRO A 1 3803 ? 170.128 115.671 164.080 1.00 29.13  ? 3803 PRO A CD    1 
ATOM   17634 N N     . LEU A 1 3804 ? 172.721 118.027 162.669 1.00 25.14  ? 3804 LEU A N     1 
ATOM   17635 C CA    . LEU A 1 3804 ? 173.726 118.731 161.880 1.00 25.14  ? 3804 LEU A CA    1 
ATOM   17636 C C     . LEU A 1 3804 ? 173.147 119.988 161.244 1.00 25.14  ? 3804 LEU A C     1 
ATOM   17637 O O     . LEU A 1 3804 ? 173.798 121.038 161.221 1.00 25.14  ? 3804 LEU A O     1 
ATOM   17638 C CB    . LEU A 1 3804 ? 174.304 117.804 160.813 1.00 25.14  ? 3804 LEU A CB    1 
ATOM   17639 C CG    . LEU A 1 3804 ? 175.240 118.467 159.802 1.00 25.14  ? 3804 LEU A CG    1 
ATOM   17640 C CD1   . LEU A 1 3804 ? 176.491 118.977 160.491 1.00 25.14  ? 3804 LEU A CD1   1 
ATOM   17641 C CD2   . LEU A 1 3804 ? 175.601 117.495 158.697 1.00 25.14  ? 3804 LEU A CD2   1 
ATOM   17642 N N     . SER A 1 3805 ? 171.922 119.904 160.723 1.00 25.83  ? 3805 SER A N     1 
ATOM   17643 C CA    . SER A 1 3805 ? 171.295 121.077 160.122 1.00 25.83  ? 3805 SER A CA    1 
ATOM   17644 C C     . SER A 1 3805 ? 171.007 122.150 161.165 1.00 25.83  ? 3805 SER A C     1 
ATOM   17645 O O     . SER A 1 3805 ? 171.198 123.346 160.905 1.00 25.83  ? 3805 SER A O     1 
ATOM   17646 C CB    . SER A 1 3805 ? 170.013 120.668 159.402 1.00 25.83  ? 3805 SER A CB    1 
ATOM   17647 O OG    . SER A 1 3805 ? 170.304 119.805 158.320 1.00 25.83  ? 3805 SER A OG    1 
ATOM   17648 N N     . THR A 1 3806 ? 170.539 121.744 162.348 1.00 22.73  ? 3806 THR A N     1 
ATOM   17649 C CA    . THR A 1 3806 ? 170.317 122.718 163.413 1.00 22.73  ? 3806 THR A CA    1 
ATOM   17650 C C     . THR A 1 3806 ? 171.624 123.385 163.820 1.00 22.73  ? 3806 THR A C     1 
ATOM   17651 O O     . THR A 1 3806 ? 171.666 124.599 164.060 1.00 22.73  ? 3806 THR A O     1 
ATOM   17652 C CB    . THR A 1 3806 ? 169.658 122.049 164.618 1.00 22.73  ? 3806 THR A CB    1 
ATOM   17653 O OG1   . THR A 1 3806 ? 170.537 121.053 165.155 1.00 22.73  ? 3806 THR A OG1   1 
ATOM   17654 C CG2   . THR A 1 3806 ? 168.345 121.397 164.214 1.00 22.73  ? 3806 THR A CG2   1 
ATOM   17655 N N     . ALA A 1 3807 ? 172.705 122.605 163.896 1.00 21.43  ? 3807 ALA A N     1 
ATOM   17656 C CA    . ALA A 1 3807 ? 174.012 123.173 164.202 1.00 21.43  ? 3807 ALA A CA    1 
ATOM   17657 C C     . ALA A 1 3807 ? 174.448 124.155 163.125 1.00 21.43  ? 3807 ALA A C     1 
ATOM   17658 O O     . ALA A 1 3807 ? 175.006 125.211 163.434 1.00 21.43  ? 3807 ALA A O     1 
ATOM   17659 C CB    . ALA A 1 3807 ? 175.045 122.059 164.363 1.00 21.43  ? 3807 ALA A CB    1 
ATOM   17660 N N     . CYS A 1 3808 ? 174.204 123.825 161.855 1.00 22.69  ? 3808 CYS A N     1 
ATOM   17661 C CA    . CYS A 1 3808 ? 174.557 124.735 160.769 1.00 22.69  ? 3808 CYS A CA    1 
ATOM   17662 C C     . CYS A 1 3808 ? 173.807 126.054 160.893 1.00 22.69  ? 3808 CYS A C     1 
ATOM   17663 O O     . CYS A 1 3808 ? 174.396 127.135 160.761 1.00 22.69  ? 3808 CYS A O     1 
ATOM   17664 C CB    . CYS A 1 3808 ? 174.261 124.084 159.417 1.00 22.69  ? 3808 CYS A CB    1 
ATOM   17665 S SG    . CYS A 1 3808 ? 175.310 122.684 158.991 1.00 22.69  ? 3808 CYS A SG    1 
ATOM   17666 N N     . SER A 1 3809 ? 172.498 125.984 161.145 1.00 21.03  ? 3809 SER A N     1 
ATOM   17667 C CA    . SER A 1 3809 ? 171.708 127.206 161.269 1.00 21.03  ? 3809 SER A CA    1 
ATOM   17668 C C     . SER A 1 3809 ? 172.174 128.048 162.451 1.00 21.03  ? 3809 SER A C     1 
ATOM   17669 O O     . SER A 1 3809 ? 172.353 129.269 162.326 1.00 21.03  ? 3809 SER A O     1 
ATOM   17670 C CB    . SER A 1 3809 ? 170.227 126.863 161.408 1.00 21.03  ? 3809 SER A CB    1 
ATOM   17671 O OG    . SER A 1 3809 ? 169.432 128.036 161.403 1.00 21.03  ? 3809 SER A OG    1 
ATOM   17672 N N     . SER A 1 3810 ? 172.387 127.410 163.606 1.00 20.11  ? 3810 SER A N     1 
ATOM   17673 C CA    . SER A 1 3810 ? 172.840 128.145 164.781 1.00 20.11  ? 3810 SER A CA    1 
ATOM   17674 C C     . SER A 1 3810 ? 174.209 128.767 164.543 1.00 20.11  ? 3810 SER A C     1 
ATOM   17675 O O     . SER A 1 3810 ? 174.453 129.917 164.930 1.00 20.11  ? 3810 SER A O     1 
ATOM   17676 C CB    . SER A 1 3810 ? 172.872 127.222 165.997 1.00 20.11  ? 3810 SER A CB    1 
ATOM   17677 O OG    . SER A 1 3810 ? 171.622 126.582 166.184 1.00 20.11  ? 3810 SER A OG    1 
ATOM   17678 N N     . ILE A 1 3811 ? 175.111 128.026 163.896 1.00 18.19  ? 3811 ILE A N     1 
ATOM   17679 C CA    . ILE A 1 3811 ? 176.446 128.541 163.619 1.00 18.19  ? 3811 ILE A CA    1 
ATOM   17680 C C     . ILE A 1 3811 ? 176.363 129.760 162.716 1.00 18.19  ? 3811 ILE A C     1 
ATOM   17681 O O     . ILE A 1 3811 ? 176.987 130.791 162.984 1.00 18.19  ? 3811 ILE A O     1 
ATOM   17682 C CB    . ILE A 1 3811 ? 177.328 127.442 163.000 1.00 18.19  ? 3811 ILE A CB    1 
ATOM   17683 C CG1   . ILE A 1 3811 ? 177.883 126.523 164.086 1.00 18.19  ? 3811 ILE A CG1   1 
ATOM   17684 C CG2   . ILE A 1 3811 ? 178.466 128.055 162.202 1.00 18.19  ? 3811 ILE A CG2   1 
ATOM   17685 C CD1   . ILE A 1 3811 ? 178.708 125.386 163.541 1.00 18.19  ? 3811 ILE A CD1   1 
ATOM   17686 N N     . TYR A 1 3812 ? 175.577 129.670 161.639 1.00 19.52  ? 3812 TYR A N     1 
ATOM   17687 C CA    . TYR A 1 3812 ? 175.496 130.794 160.713 1.00 19.52  ? 3812 TYR A CA    1 
ATOM   17688 C C     . TYR A 1 3812 ? 174.891 132.020 161.376 1.00 19.52  ? 3812 TYR A C     1 
ATOM   17689 O O     . TYR A 1 3812 ? 175.331 133.148 161.129 1.00 19.52  ? 3812 TYR A O     1 
ATOM   17690 C CB    . TYR A 1 3812 ? 174.684 130.436 159.474 1.00 19.52  ? 3812 TYR A CB    1 
ATOM   17691 C CG    . TYR A 1 3812 ? 174.285 131.672 158.698 1.00 19.52  ? 3812 TYR A CG    1 
ATOM   17692 C CD1   . TYR A 1 3812 ? 175.233 132.418 158.014 1.00 19.52  ? 3812 TYR A CD1   1 
ATOM   17693 C CD2   . TYR A 1 3812 ? 172.970 132.114 158.680 1.00 19.52  ? 3812 TYR A CD2   1 
ATOM   17694 C CE1   . TYR A 1 3812 ? 174.881 133.554 157.317 1.00 19.52  ? 3812 TYR A CE1   1 
ATOM   17695 C CE2   . TYR A 1 3812 ? 172.607 133.249 157.984 1.00 19.52  ? 3812 TYR A CE2   1 
ATOM   17696 C CZ    . TYR A 1 3812 ? 173.567 133.965 157.305 1.00 19.52  ? 3812 TYR A CZ    1 
ATOM   17697 O OH    . TYR A 1 3812 ? 173.210 135.097 156.611 1.00 19.52  ? 3812 TYR A OH    1 
ATOM   17698 N N     . PHE A 1 3813 ? 173.866 131.831 162.206 1.00 21.06  ? 3813 PHE A N     1 
ATOM   17699 C CA    . PHE A 1 3813 ? 173.248 133.009 162.802 1.00 21.06  ? 3813 PHE A CA    1 
ATOM   17700 C C     . PHE A 1 3813 ? 174.103 133.610 163.909 1.00 21.06  ? 3813 PHE A C     1 
ATOM   17701 O O     . PHE A 1 3813 ? 174.086 134.831 164.097 1.00 21.06  ? 3813 PHE A O     1 
ATOM   17702 C CB    . PHE A 1 3813 ? 171.842 132.671 163.283 1.00 21.06  ? 3813 PHE A CB    1 
ATOM   17703 C CG    . PHE A 1 3813 ? 170.827 132.719 162.184 1.00 21.06  ? 3813 PHE A CG    1 
ATOM   17704 C CD1   . PHE A 1 3813 ? 170.515 133.922 161.575 1.00 21.06  ? 3813 PHE A CD1   1 
ATOM   17705 C CD2   . PHE A 1 3813 ? 170.233 131.565 161.716 1.00 21.06  ? 3813 PHE A CD2   1 
ATOM   17706 C CE1   . PHE A 1 3813 ? 169.601 133.977 160.547 1.00 21.06  ? 3813 PHE A CE1   1 
ATOM   17707 C CE2   . PHE A 1 3813 ? 169.321 131.614 160.685 1.00 21.06  ? 3813 PHE A CE2   1 
ATOM   17708 C CZ    . PHE A 1 3813 ? 169.002 132.822 160.102 1.00 21.06  ? 3813 PHE A CZ    1 
ATOM   17709 N N     . THR A 1 3814 ? 174.883 132.793 164.621 1.00 19.25  ? 3814 THR A N     1 
ATOM   17710 C CA    . THR A 1 3814 ? 175.897 133.353 165.509 1.00 19.25  ? 3814 THR A CA    1 
ATOM   17711 C C     . THR A 1 3814 ? 176.944 134.130 164.717 1.00 19.25  ? 3814 THR A C     1 
ATOM   17712 O O     . THR A 1 3814 ? 177.361 135.221 165.124 1.00 19.25  ? 3814 THR A O     1 
ATOM   17713 C CB    . THR A 1 3814 ? 176.545 132.239 166.330 1.00 19.25  ? 3814 THR A CB    1 
ATOM   17714 O OG1   . THR A 1 3814 ? 175.619 131.779 167.322 1.00 19.25  ? 3814 THR A OG1   1 
ATOM   17715 C CG2   . THR A 1 3814 ? 177.805 132.734 167.015 1.00 19.25  ? 3814 THR A CG2   1 
ATOM   17716 N N     . MET A 1 3815 ? 177.359 133.594 163.565 1.00 19.21  ? 3815 MET A N     1 
ATOM   17717 C CA    . MET A 1 3815 ? 178.283 134.308 162.688 1.00 19.21  ? 3815 MET A CA    1 
ATOM   17718 C C     . MET A 1 3815 ? 177.721 135.660 162.273 1.00 19.21  ? 3815 MET A C     1 
ATOM   17719 O O     . MET A 1 3815 ? 178.441 136.664 162.257 1.00 19.21  ? 3815 MET A O     1 
ATOM   17720 C CB    . MET A 1 3815 ? 178.573 133.466 161.446 1.00 19.21  ? 3815 MET A CB    1 
ATOM   17721 C CG    . MET A 1 3815 ? 179.344 132.187 161.689 1.00 19.21  ? 3815 MET A CG    1 
ATOM   17722 S SD    . MET A 1 3815 ? 179.523 131.256 160.158 1.00 19.21  ? 3815 MET A SD    1 
ATOM   17723 C CE    . MET A 1 3815 ? 180.666 132.293 159.268 1.00 19.21  ? 3815 MET A CE    1 
ATOM   17724 N N     . GLU A 1 3816 ? 176.439 135.699 161.918 1.00 19.65  ? 3816 GLU A N     1 
ATOM   17725 C CA    . GLU A 1 3816 ? 175.842 136.949 161.462 1.00 19.65  ? 3816 GLU A CA    1 
ATOM   17726 C C     . GLU A 1 3816 ? 175.695 137.942 162.608 1.00 19.65  ? 3816 GLU A C     1 
ATOM   17727 O O     . GLU A 1 3816 ? 175.988 139.132 162.445 1.00 19.65  ? 3816 GLU A O     1 
ATOM   17728 C CB    . GLU A 1 3816 ? 174.491 136.677 160.804 1.00 19.65  ? 3816 GLU A CB    1 
ATOM   17729 C CG    . GLU A 1 3816 ? 173.693 137.926 160.479 1.00 19.65  ? 3816 GLU A CG    1 
ATOM   17730 C CD    . GLU A 1 3816 ? 172.714 137.699 159.347 1.00 19.65  ? 3816 GLU A CD    1 
ATOM   17731 O OE1   . GLU A 1 3816 ? 171.641 138.337 159.345 1.00 19.65  ? 3816 GLU A OE1   1 
ATOM   17732 O OE2   . GLU A 1 3816 ? 173.022 136.879 158.457 1.00 19.65  ? 3816 GLU A OE2   1 
ATOM   17733 N N     . SER A 1 3817 ? 175.254 137.474 163.778 1.00 20.28  ? 3817 SER A N     1 
ATOM   17734 C CA    . SER A 1 3817 ? 175.117 138.360 164.928 1.00 20.28  ? 3817 SER A CA    1 
ATOM   17735 C C     . SER A 1 3817 ? 176.462 138.743 165.532 1.00 20.28  ? 3817 SER A C     1 
ATOM   17736 O O     . SER A 1 3817 ? 176.502 139.592 166.427 1.00 20.28  ? 3817 SER A O     1 
ATOM   17737 C CB    . SER A 1 3817 ? 174.232 137.713 165.992 1.00 20.28  ? 3817 SER A CB    1 
ATOM   17738 O OG    . SER A 1 3817 ? 174.854 136.568 166.545 1.00 20.28  ? 3817 SER A OG    1 
ATOM   17739 N N     . LEU A 1 3818 ? 177.557 138.124 165.082 1.00 19.39  ? 3818 LEU A N     1 
ATOM   17740 C CA    . LEU A 1 3818 ? 178.886 138.524 165.537 1.00 19.39  ? 3818 LEU A CA    1 
ATOM   17741 C C     . LEU A 1 3818 ? 179.184 139.995 165.280 1.00 19.39  ? 3818 LEU A C     1 
ATOM   17742 O O     . LEU A 1 3818 ? 180.139 140.531 165.853 1.00 19.39  ? 3818 LEU A O     1 
ATOM   17743 C CB    . LEU A 1 3818 ? 179.953 137.663 164.857 1.00 19.39  ? 3818 LEU A CB    1 
ATOM   17744 C CG    . LEU A 1 3818 ? 180.482 136.453 165.627 1.00 19.39  ? 3818 LEU A CG    1 
ATOM   17745 C CD1   . LEU A 1 3818 ? 181.398 135.630 164.745 1.00 19.39  ? 3818 LEU A CD1   1 
ATOM   17746 C CD2   . LEU A 1 3818 ? 181.212 136.892 166.877 1.00 19.39  ? 3818 LEU A CD2   1 
ATOM   17747 N N     . LYS A 1 3819 ? 178.400 140.662 164.430 1.00 20.74  ? 3819 LYS A N     1 
ATOM   17748 C CA    . LYS A 1 3819 ? 178.624 142.079 164.164 1.00 20.74  ? 3819 LYS A CA    1 
ATOM   17749 C C     . LYS A 1 3819 ? 178.379 142.949 165.390 1.00 20.74  ? 3819 LYS A C     1 
ATOM   17750 O O     . LYS A 1 3819 ? 178.802 144.110 165.401 1.00 20.74  ? 3819 LYS A O     1 
ATOM   17751 C CB    . LYS A 1 3819 ? 177.729 142.551 163.018 1.00 20.74  ? 3819 LYS A CB    1 
ATOM   17752 C CG    . LYS A 1 3819 ? 176.243 142.493 163.330 1.00 20.74  ? 3819 LYS A CG    1 
ATOM   17753 C CD    . LYS A 1 3819 ? 175.398 142.868 162.122 1.00 20.74  ? 3819 LYS A CD    1 
ATOM   17754 C CE    . LYS A 1 3819 ? 175.690 141.969 160.934 1.00 20.74  ? 3819 LYS A CE    1 
ATOM   17755 N NZ    . LYS A 1 3819 ? 174.794 142.264 159.783 1.00 20.74  ? 3819 LYS A NZ    1 
ATOM   17756 N N     . GLN A 1 3820 ? 177.703 142.424 166.416 1.00 21.91  ? 3820 GLN A N     1 
ATOM   17757 C CA    . GLN A 1 3820 ? 177.405 143.233 167.594 1.00 21.91  ? 3820 GLN A CA    1 
ATOM   17758 C C     . GLN A 1 3820 ? 178.659 143.529 168.407 1.00 21.91  ? 3820 GLN A C     1 
ATOM   17759 O O     . GLN A 1 3820 ? 178.795 144.624 168.964 1.00 21.91  ? 3820 GLN A O     1 
ATOM   17760 C CB    . GLN A 1 3820 ? 176.354 142.538 168.459 1.00 21.91  ? 3820 GLN A CB    1 
ATOM   17761 C CG    . GLN A 1 3820 ? 175.117 142.115 167.695 1.00 21.91  ? 3820 GLN A CG    1 
ATOM   17762 C CD    . GLN A 1 3820 ? 174.309 143.298 167.208 1.00 21.91  ? 3820 GLN A CD    1 
ATOM   17763 O OE1   . GLN A 1 3820 ? 174.310 144.362 167.827 1.00 21.91  ? 3820 GLN A OE1   1 
ATOM   17764 N NE2   . GLN A 1 3820 ? 173.620 143.123 166.087 1.00 21.91  ? 3820 GLN A NE2   1 
ATOM   17765 N N     . ILE A 1 3821 ? 179.580 142.568 168.500 1.00 21.77  ? 3821 ILE A N     1 
ATOM   17766 C CA    . ILE A 1 3821 ? 180.815 142.803 169.243 1.00 21.77  ? 3821 ILE A CA    1 
ATOM   17767 C C     . ILE A 1 3821 ? 181.643 143.890 168.574 1.00 21.77  ? 3821 ILE A C     1 
ATOM   17768 O O     . ILE A 1 3821 ? 182.135 144.816 169.230 1.00 21.77  ? 3821 ILE A O     1 
ATOM   17769 C CB    . ILE A 1 3821 ? 181.629 141.505 169.382 1.00 21.77  ? 3821 ILE A CB    1 
ATOM   17770 C CG1   . ILE A 1 3821 ? 180.740 140.325 169.765 1.00 21.77  ? 3821 ILE A CG1   1 
ATOM   17771 C CG2   . ILE A 1 3821 ? 182.756 141.695 170.376 1.00 21.77  ? 3821 ILE A CG2   1 
ATOM   17772 C CD1   . ILE A 1 3821 ? 181.493 139.014 169.792 1.00 21.77  ? 3821 ILE A CD1   1 
ATOM   17773 N N     . HIS A 1 3822 ? 181.814 143.791 167.260 1.00 23.16  ? 3822 HIS A N     1 
ATOM   17774 C CA    . HIS A 1 3822 ? 182.754 144.648 166.560 1.00 23.16  ? 3822 HIS A CA    1 
ATOM   17775 C C     . HIS A 1 3822 ? 182.236 144.887 165.151 1.00 23.16  ? 3822 HIS A C     1 
ATOM   17776 O O     . HIS A 1 3822 ? 181.610 144.011 164.549 1.00 23.16  ? 3822 HIS A O     1 
ATOM   17777 C CB    . HIS A 1 3822 ? 184.147 144.008 166.538 1.00 23.16  ? 3822 HIS A CB    1 
ATOM   17778 C CG    . HIS A 1 3822 ? 185.259 144.971 166.271 1.00 23.16  ? 3822 HIS A CG    1 
ATOM   17779 N ND1   . HIS A 1 3822 ? 185.686 145.286 165.000 1.00 23.16  ? 3822 HIS A ND1   1 
ATOM   17780 C CD2   . HIS A 1 3822 ? 186.047 145.677 167.117 1.00 23.16  ? 3822 HIS A CD2   1 
ATOM   17781 C CE1   . HIS A 1 3822 ? 186.682 146.150 165.073 1.00 23.16  ? 3822 HIS A CE1   1 
ATOM   17782 N NE2   . HIS A 1 3822 ? 186.920 146.404 166.346 1.00 23.16  ? 3822 HIS A NE2   1 
ATOM   17783 N N     . PHE A 1 3823 ? 182.499 146.086 164.632 1.00 24.91  ? 3823 PHE A N     1 
ATOM   17784 C CA    . PHE A 1 3823 ? 182.030 146.445 163.299 1.00 24.91  ? 3823 PHE A CA    1 
ATOM   17785 C C     . PHE A 1 3823 ? 182.727 145.655 162.201 1.00 24.91  ? 3823 PHE A C     1 
ATOM   17786 O O     . PHE A 1 3823 ? 182.251 145.650 161.061 1.00 24.91  ? 3823 PHE A O     1 
ATOM   17787 C CB    . PHE A 1 3823 ? 182.226 147.943 163.065 1.00 24.91  ? 3823 PHE A CB    1 
ATOM   17788 C CG    . PHE A 1 3823 ? 183.658 148.389 163.157 1.00 24.91  ? 3823 PHE A CG    1 
ATOM   17789 C CD1   . PHE A 1 3823 ? 184.478 148.378 162.043 1.00 24.91  ? 3823 PHE A CD1   1 
ATOM   17790 C CD2   . PHE A 1 3823 ? 184.183 148.823 164.362 1.00 24.91  ? 3823 PHE A CD2   1 
ATOM   17791 C CE1   . PHE A 1 3823 ? 185.793 148.785 162.131 1.00 24.91  ? 3823 PHE A CE1   1 
ATOM   17792 C CE2   . PHE A 1 3823 ? 185.496 149.234 164.454 1.00 24.91  ? 3823 PHE A CE2   1 
ATOM   17793 C CZ    . PHE A 1 3823 ? 186.302 149.215 163.337 1.00 24.91  ? 3823 PHE A CZ    1 
ATOM   17794 N N     . LEU A 1 3824 ? 183.835 144.992 162.514 1.00 23.00  ? 3824 LEU A N     1 
ATOM   17795 C CA    . LEU A 1 3824 ? 184.651 144.302 161.526 1.00 23.00  ? 3824 LEU A CA    1 
ATOM   17796 C C     . LEU A 1 3824 ? 184.239 142.846 161.334 1.00 23.00  ? 3824 LEU A C     1 
ATOM   17797 O O     . LEU A 1 3824 ? 184.822 142.154 160.494 1.00 23.00  ? 3824 LEU A O     1 
ATOM   17798 C CB    . LEU A 1 3824 ? 186.125 144.394 161.940 1.00 23.00  ? 3824 LEU A CB    1 
ATOM   17799 C CG    . LEU A 1 3824 ? 187.258 143.846 161.076 1.00 23.00  ? 3824 LEU A CG    1 
ATOM   17800 C CD1   . LEU A 1 3824 ? 187.302 144.581 159.755 1.00 23.00  ? 3824 LEU A CD1   1 
ATOM   17801 C CD2   . LEU A 1 3824 ? 188.576 143.985 161.808 1.00 23.00  ? 3824 LEU A CD2   1 
ATOM   17802 N N     . TYR A 1 3825 ? 183.230 142.374 162.062 1.00 22.05  ? 3825 TYR A N     1 
ATOM   17803 C CA    . TYR A 1 3825 ? 182.818 140.972 162.026 1.00 22.05  ? 3825 TYR A CA    1 
ATOM   17804 C C     . TYR A 1 3825 ? 181.635 140.749 161.094 1.00 22.05  ? 3825 TYR A C     1 
ATOM   17805 O O     . TYR A 1 3825 ? 180.756 139.930 161.375 1.00 22.05  ? 3825 TYR A O     1 
ATOM   17806 C CB    . TYR A 1 3825 ? 182.491 140.481 163.433 1.00 22.05  ? 3825 TYR A CB    1 
ATOM   17807 C CG    . TYR A 1 3825 ? 183.663 140.516 164.389 1.00 22.05  ? 3825 TYR A CG    1 
ATOM   17808 C CD1   . TYR A 1 3825 ? 184.966 140.609 163.921 1.00 22.05  ? 3825 TYR A CD1   1 
ATOM   17809 C CD2   . TYR A 1 3825 ? 183.465 140.458 165.760 1.00 22.05  ? 3825 TYR A CD2   1 
ATOM   17810 C CE1   . TYR A 1 3825 ? 186.034 140.643 164.790 1.00 22.05  ? 3825 TYR A CE1   1 
ATOM   17811 C CE2   . TYR A 1 3825 ? 184.528 140.490 166.635 1.00 22.05  ? 3825 TYR A CE2   1 
ATOM   17812 C CZ    . TYR A 1 3825 ? 185.810 140.584 166.145 1.00 22.05  ? 3825 TYR A CZ    1 
ATOM   17813 O OH    . TYR A 1 3825 ? 186.873 140.616 167.016 1.00 22.05  ? 3825 TYR A OH    1 
ATOM   17814 N N     . GLN A 1 3826 ? 181.587 141.471 159.979 1.00 22.47  ? 3826 GLN A N     1 
ATOM   17815 C CA    . GLN A 1 3826 ? 180.506 141.319 159.014 1.00 22.47  ? 3826 GLN A CA    1 
ATOM   17816 C C     . GLN A 1 3826 ? 180.724 140.048 158.200 1.00 22.47  ? 3826 GLN A C     1 
ATOM   17817 O O     . GLN A 1 3826 ? 181.718 139.932 157.476 1.00 22.47  ? 3826 GLN A O     1 
ATOM   17818 C CB    . GLN A 1 3826 ? 180.440 142.539 158.100 1.00 22.47  ? 3826 GLN A CB    1 
ATOM   17819 C CG    . GLN A 1 3826 ? 180.232 143.853 158.830 1.00 22.47  ? 3826 GLN A CG    1 
ATOM   17820 C CD    . GLN A 1 3826 ? 178.843 143.980 159.420 1.00 22.47  ? 3826 GLN A CD    1 
ATOM   17821 O OE1   . GLN A 1 3826 ? 177.863 143.525 158.831 1.00 22.47  ? 3826 GLN A OE1   1 
ATOM   17822 N NE2   . GLN A 1 3826 ? 178.751 144.607 160.586 1.00 22.47  ? 3826 GLN A NE2   1 
ATOM   17823 N N     . TYR A 1 3827 ? 179.798 139.099 158.317 1.00 21.29  ? 3827 TYR A N     1 
ATOM   17824 C CA    . TYR A 1 3827 ? 179.869 137.840 157.590 1.00 21.29  ? 3827 TYR A CA    1 
ATOM   17825 C C     . TYR A 1 3827 ? 178.571 137.619 156.830 1.00 21.29  ? 3827 TYR A C     1 
ATOM   17826 O O     . TYR A 1 3827 ? 177.481 137.820 157.372 1.00 21.29  ? 3827 TYR A O     1 
ATOM   17827 C CB    . TYR A 1 3827 ? 180.133 136.664 158.536 1.00 21.29  ? 3827 TYR A CB    1 
ATOM   17828 C CG    . TYR A 1 3827 ? 181.462 136.751 159.249 1.00 21.29  ? 3827 TYR A CG    1 
ATOM   17829 C CD1   . TYR A 1 3827 ? 182.654 136.647 158.549 1.00 21.29  ? 3827 TYR A CD1   1 
ATOM   17830 C CD2   . TYR A 1 3827 ? 181.523 136.941 160.622 1.00 21.29  ? 3827 TYR A CD2   1 
ATOM   17831 C CE1   . TYR A 1 3827 ? 183.871 136.729 159.196 1.00 21.29  ? 3827 TYR A CE1   1 
ATOM   17832 C CE2   . TYR A 1 3827 ? 182.735 137.023 161.277 1.00 21.29  ? 3827 TYR A CE2   1 
ATOM   17833 C CZ    . TYR A 1 3827 ? 183.905 136.916 160.559 1.00 21.29  ? 3827 TYR A CZ    1 
ATOM   17834 O OH    . TYR A 1 3827 ? 185.115 136.998 161.206 1.00 21.29  ? 3827 TYR A OH    1 
ATOM   17835 N N     . SER A 1 3828 ? 178.694 137.203 155.574 1.00 21.30  ? 3828 SER A N     1 
ATOM   17836 C CA    . SER A 1 3828 ? 177.555 137.013 154.691 1.00 21.30  ? 3828 SER A CA    1 
ATOM   17837 C C     . SER A 1 3828 ? 177.134 135.548 154.656 1.00 21.30  ? 3828 SER A C     1 
ATOM   17838 O O     . SER A 1 3828 ? 177.807 134.664 155.190 1.00 21.30  ? 3828 SER A O     1 
ATOM   17839 C CB    . SER A 1 3828 ? 177.886 137.508 153.280 1.00 21.30  ? 3828 SER A CB    1 
ATOM   17840 O OG    . SER A 1 3828 ? 179.091 136.928 152.811 1.00 21.30  ? 3828 SER A OG    1 
ATOM   17841 N N     . LEU A 1 3829 ? 175.989 135.299 154.015 1.00 19.69  ? 3829 LEU A N     1 
ATOM   17842 C CA    . LEU A 1 3829 ? 175.507 133.930 153.867 1.00 19.69  ? 3829 LEU A CA    1 
ATOM   17843 C C     . LEU A 1 3829 ? 176.420 133.116 152.961 1.00 19.69  ? 3829 LEU A C     1 
ATOM   17844 O O     . LEU A 1 3829 ? 176.602 131.911 153.175 1.00 19.69  ? 3829 LEU A O     1 
ATOM   17845 C CB    . LEU A 1 3829 ? 174.078 133.926 153.327 1.00 19.69  ? 3829 LEU A CB    1 
ATOM   17846 C CG    . LEU A 1 3829 ? 173.423 132.550 153.182 1.00 19.69  ? 3829 LEU A CG    1 
ATOM   17847 C CD1   . LEU A 1 3829 ? 173.292 131.868 154.531 1.00 19.69  ? 3829 LEU A CD1   1 
ATOM   17848 C CD2   . LEU A 1 3829 ? 172.068 132.666 152.505 1.00 19.69  ? 3829 LEU A CD2   1 
ATOM   17849 N N     . GLN A 1 3830 ? 176.995 133.753 151.938 1.00 20.92  ? 3830 GLN A N     1 
ATOM   17850 C CA    . GLN A 1 3830 ? 177.875 133.034 151.025 1.00 20.92  ? 3830 GLN A CA    1 
ATOM   17851 C C     . GLN A 1 3830 ? 179.111 132.505 151.738 1.00 20.92  ? 3830 GLN A C     1 
ATOM   17852 O O     . GLN A 1 3830 ? 179.624 131.441 151.379 1.00 20.92  ? 3830 GLN A O     1 
ATOM   17853 C CB    . GLN A 1 3830 ? 178.281 133.933 149.860 1.00 20.92  ? 3830 GLN A CB    1 
ATOM   17854 C CG    . GLN A 1 3830 ? 178.768 133.170 148.642 1.00 20.92  ? 3830 GLN A CG    1 
ATOM   17855 C CD    . GLN A 1 3830 ? 177.888 131.981 148.311 1.00 20.92  ? 3830 GLN A CD    1 
ATOM   17856 O OE1   . GLN A 1 3830 ? 176.676 132.118 148.148 1.00 20.92  ? 3830 GLN A OE1   1 
ATOM   17857 N NE2   . GLN A 1 3830 ? 178.493 130.803 148.218 1.00 20.92  ? 3830 GLN A NE2   1 
ATOM   17858 N N     . PHE A 1 3831 ? 179.601 133.225 152.748 1.00 19.67  ? 3831 PHE A N     1 
ATOM   17859 C CA    . PHE A 1 3831 ? 180.753 132.750 153.508 1.00 19.67  ? 3831 PHE A CA    1 
ATOM   17860 C C     . PHE A 1 3831 ? 180.438 131.439 154.221 1.00 19.67  ? 3831 PHE A C     1 
ATOM   17861 O O     . PHE A 1 3831 ? 181.201 130.466 154.134 1.00 19.67  ? 3831 PHE A O     1 
ATOM   17862 C CB    . PHE A 1 3831 ? 181.189 133.829 154.500 1.00 19.67  ? 3831 PHE A CB    1 
ATOM   17863 C CG    . PHE A 1 3831 ? 182.414 133.477 155.288 1.00 19.67  ? 3831 PHE A CG    1 
ATOM   17864 C CD1   . PHE A 1 3831 ? 183.567 133.053 154.654 1.00 19.67  ? 3831 PHE A CD1   1 
ATOM   17865 C CD2   . PHE A 1 3831 ? 182.422 133.600 156.664 1.00 19.67  ? 3831 PHE A CD2   1 
ATOM   17866 C CE1   . PHE A 1 3831 ? 184.695 132.736 155.383 1.00 19.67  ? 3831 PHE A CE1   1 
ATOM   17867 C CE2   . PHE A 1 3831 ? 183.545 133.285 157.397 1.00 19.67  ? 3831 PHE A CE2   1 
ATOM   17868 C CZ    . PHE A 1 3831 ? 184.684 132.854 156.757 1.00 19.67  ? 3831 PHE A CZ    1 
ATOM   17869 N N     . PHE A 1 3832 ? 179.297 131.382 154.913 1.00 17.19  ? 3832 PHE A N     1 
ATOM   17870 C CA    . PHE A 1 3832 ? 178.930 130.149 155.598 1.00 17.19  ? 3832 PHE A CA    1 
ATOM   17871 C C     . PHE A 1 3832 ? 178.592 129.039 154.614 1.00 17.19  ? 3832 PHE A C     1 
ATOM   17872 O O     . PHE A 1 3832 ? 178.857 127.866 154.895 1.00 17.19  ? 3832 PHE A O     1 
ATOM   17873 C CB    . PHE A 1 3832 ? 177.754 130.383 156.542 1.00 17.19  ? 3832 PHE A CB    1 
ATOM   17874 C CG    . PHE A 1 3832 ? 177.214 129.121 157.143 1.00 17.19  ? 3832 PHE A CG    1 
ATOM   17875 C CD1   . PHE A 1 3832 ? 177.937 128.434 158.100 1.00 17.19  ? 3832 PHE A CD1   1 
ATOM   17876 C CD2   . PHE A 1 3832 ? 175.995 128.611 156.738 1.00 17.19  ? 3832 PHE A CD2   1 
ATOM   17877 C CE1   . PHE A 1 3832 ? 177.451 127.270 158.651 1.00 17.19  ? 3832 PHE A CE1   1 
ATOM   17878 C CE2   . PHE A 1 3832 ? 175.503 127.446 157.286 1.00 17.19  ? 3832 PHE A CE2   1 
ATOM   17879 C CZ    . PHE A 1 3832 ? 176.233 126.774 158.243 1.00 17.19  ? 3832 PHE A CZ    1 
ATOM   17880 N N     . LEU A 1 3833 ? 178.005 129.379 153.465 1.00 20.30  ? 3833 LEU A N     1 
ATOM   17881 C CA    . LEU A 1 3833 ? 177.748 128.361 152.452 1.00 20.30  ? 3833 LEU A CA    1 
ATOM   17882 C C     . LEU A 1 3833 ? 179.052 127.782 151.920 1.00 20.30  ? 3833 LEU A C     1 
ATOM   17883 O O     . LEU A 1 3833 ? 179.151 126.574 151.678 1.00 20.30  ? 3833 LEU A O     1 
ATOM   17884 C CB    . LEU A 1 3833 ? 176.910 128.944 151.316 1.00 20.30  ? 3833 LEU A CB    1 
ATOM   17885 C CG    . LEU A 1 3833 ? 175.406 129.016 151.578 1.00 20.30  ? 3833 LEU A CG    1 
ATOM   17886 C CD1   . LEU A 1 3833 ? 174.650 129.273 150.285 1.00 20.30  ? 3833 LEU A CD1   1 
ATOM   17887 C CD2   . LEU A 1 3833 ? 174.916 127.741 152.244 1.00 20.30  ? 3833 LEU A CD2   1 
ATOM   17888 N N     . ASP A 1 3834 ? 180.064 128.631 151.731 1.00 21.96  ? 3834 ASP A N     1 
ATOM   17889 C CA    . ASP A 1 3834 ? 181.377 128.143 151.326 1.00 21.96  ? 3834 ASP A CA    1 
ATOM   17890 C C     . ASP A 1 3834 ? 181.973 127.236 152.393 1.00 21.96  ? 3834 ASP A C     1 
ATOM   17891 O O     . ASP A 1 3834 ? 182.571 126.204 152.073 1.00 21.96  ? 3834 ASP A O     1 
ATOM   17892 C CB    . ASP A 1 3834 ? 182.309 129.319 151.038 1.00 21.96  ? 3834 ASP A CB    1 
ATOM   17893 C CG    . ASP A 1 3834 ? 182.218 129.796 149.603 1.00 21.96  ? 3834 ASP A CG    1 
ATOM   17894 O OD1   . ASP A 1 3834 ? 183.061 130.623 149.195 1.00 21.96  ? 3834 ASP A OD1   1 
ATOM   17895 O OD2   . ASP A 1 3834 ? 181.304 129.345 148.882 1.00 21.96  ? 3834 ASP A OD2   1 
ATOM   17896 N N     . ILE A 1 3835 ? 181.815 127.603 153.667 1.00 19.92  ? 3835 ILE A N     1 
ATOM   17897 C CA    . ILE A 1 3835 ? 182.306 126.753 154.752 1.00 19.92  ? 3835 ILE A CA    1 
ATOM   17898 C C     . ILE A 1 3835 ? 181.621 125.390 154.711 1.00 19.92  ? 3835 ILE A C     1 
ATOM   17899 O O     . ILE A 1 3835 ? 182.265 124.340 154.839 1.00 19.92  ? 3835 ILE A O     1 
ATOM   17900 C CB    . ILE A 1 3835 ? 182.092 127.440 156.113 1.00 19.92  ? 3835 ILE A CB    1 
ATOM   17901 C CG1   . ILE A 1 3835 ? 182.940 128.706 156.218 1.00 19.92  ? 3835 ILE A CG1   1 
ATOM   17902 C CG2   . ILE A 1 3835 ? 182.414 126.486 157.248 1.00 19.92  ? 3835 ILE A CG2   1 
ATOM   17903 C CD1   . ILE A 1 3835 ? 182.767 129.443 157.525 1.00 19.92  ? 3835 ILE A CD1   1 
ATOM   17904 N N     . TYR A 1 3836 ? 180.299 125.394 154.534 1.00 23.72  ? 3836 TYR A N     1 
ATOM   17905 C CA    . TYR A 1 3836 ? 179.536 124.150 154.519 1.00 23.72  ? 3836 TYR A CA    1 
ATOM   17906 C C     . TYR A 1 3836 ? 179.925 123.274 153.335 1.00 23.72  ? 3836 TYR A C     1 
ATOM   17907 O O     . TYR A 1 3836 ? 180.071 122.054 153.475 1.00 23.72  ? 3836 TYR A O     1 
ATOM   17908 C CB    . TYR A 1 3836 ? 178.041 124.467 154.488 1.00 23.72  ? 3836 TYR A CB    1 
ATOM   17909 C CG    . TYR A 1 3836 ? 177.149 123.301 154.835 1.00 23.72  ? 3836 TYR A CG    1 
ATOM   17910 C CD1   . TYR A 1 3836 ? 177.535 122.364 155.781 1.00 23.72  ? 3836 TYR A CD1   1 
ATOM   17911 C CD2   . TYR A 1 3836 ? 175.914 123.146 154.224 1.00 23.72  ? 3836 TYR A CD2   1 
ATOM   17912 C CE1   . TYR A 1 3836 ? 176.718 121.300 156.103 1.00 23.72  ? 3836 TYR A CE1   1 
ATOM   17913 C CE2   . TYR A 1 3836 ? 175.091 122.086 154.540 1.00 23.72  ? 3836 TYR A CE2   1 
ATOM   17914 C CZ    . TYR A 1 3836 ? 175.497 121.167 155.480 1.00 23.72  ? 3836 TYR A CZ    1 
ATOM   17915 O OH    . TYR A 1 3836 ? 174.678 120.110 155.796 1.00 23.72  ? 3836 TYR A OH    1 
ATOM   17916 N N     . HIS A 1 3837 ? 180.098 123.876 152.158 1.00 24.37  ? 3837 HIS A N     1 
ATOM   17917 C CA    . HIS A 1 3837 ? 180.489 123.094 150.991 1.00 24.37  ? 3837 HIS A CA    1 
ATOM   17918 C C     . HIS A 1 3837 ? 181.914 122.573 151.129 1.00 24.37  ? 3837 HIS A C     1 
ATOM   17919 O O     . HIS A 1 3837 ? 182.223 121.470 150.665 1.00 24.37  ? 3837 HIS A O     1 
ATOM   17920 C CB    . HIS A 1 3837 ? 180.333 123.929 149.722 1.00 24.37  ? 3837 HIS A CB    1 
ATOM   17921 C CG    . HIS A 1 3837 ? 178.911 124.254 149.389 1.00 24.37  ? 3837 HIS A CG    1 
ATOM   17922 N ND1   . HIS A 1 3837 ? 178.556 125.330 148.605 1.00 24.37  ? 3837 HIS A ND1   1 
ATOM   17923 C CD2   . HIS A 1 3837 ? 177.753 123.647 149.740 1.00 24.37  ? 3837 HIS A CD2   1 
ATOM   17924 C CE1   . HIS A 1 3837 ? 177.242 125.370 148.484 1.00 24.37  ? 3837 HIS A CE1   1 
ATOM   17925 N NE2   . HIS A 1 3837 ? 176.730 124.359 149.164 1.00 24.37  ? 3837 HIS A NE2   1 
ATOM   17926 N N     . ASN A 1 3838 ? 182.796 123.351 151.760 1.00 26.21  ? 3838 ASN A N     1 
ATOM   17927 C CA    . ASN A 1 3838 ? 184.159 122.886 151.989 1.00 26.21  ? 3838 ASN A CA    1 
ATOM   17928 C C     . ASN A 1 3838 ? 184.183 121.694 152.934 1.00 26.21  ? 3838 ASN A C     1 
ATOM   17929 O O     . ASN A 1 3838 ? 184.911 120.723 152.699 1.00 26.21  ? 3838 ASN A O     1 
ATOM   17930 C CB    . ASN A 1 3838 ? 185.016 124.022 152.542 1.00 26.21  ? 3838 ASN A CB    1 
ATOM   17931 C CG    . ASN A 1 3838 ? 186.420 123.575 152.889 1.00 26.21  ? 3838 ASN A CG    1 
ATOM   17932 O OD1   . ASN A 1 3838 ? 186.701 123.196 154.026 1.00 26.21  ? 3838 ASN A OD1   1 
ATOM   17933 N ND2   . ASN A 1 3838 ? 187.313 123.617 151.908 1.00 26.21  ? 3838 ASN A ND2   1 
ATOM   17934 N N     . VAL A 1 3839 ? 183.400 121.748 154.013 1.00 25.15  ? 3839 VAL A N     1 
ATOM   17935 C CA    . VAL A 1 3839 ? 183.412 120.634 154.955 1.00 25.15  ? 3839 VAL A CA    1 
ATOM   17936 C C     . VAL A 1 3839 ? 182.705 119.415 154.370 1.00 25.15  ? 3839 VAL A C     1 
ATOM   17937 O O     . VAL A 1 3839 ? 183.080 118.275 154.665 1.00 25.15  ? 3839 VAL A O     1 
ATOM   17938 C CB    . VAL A 1 3839 ? 182.813 121.052 156.313 1.00 25.15  ? 3839 VAL A CB    1 
ATOM   17939 C CG1   . VAL A 1 3839 ? 181.331 121.341 156.201 1.00 25.15  ? 3839 VAL A CG1   1 
ATOM   17940 C CG2   . VAL A 1 3839 ? 183.064 119.974 157.350 1.00 25.15  ? 3839 VAL A CG2   1 
ATOM   17941 N N     . LEU A 1 3840 ? 181.683 119.621 153.535 1.00 24.86  ? 3840 LEU A N     1 
ATOM   17942 C CA    . LEU A 1 3840 ? 180.959 118.484 152.974 1.00 24.86  ? 3840 LEU A CA    1 
ATOM   17943 C C     . LEU A 1 3840 ? 181.752 117.772 151.884 1.00 24.86  ? 3840 LEU A C     1 
ATOM   17944 O O     . LEU A 1 3840 ? 181.782 116.537 151.846 1.00 24.86  ? 3840 LEU A O     1 
ATOM   17945 C CB    . LEU A 1 3840 ? 179.605 118.935 152.426 1.00 24.86  ? 3840 LEU A CB    1 
ATOM   17946 C CG    . LEU A 1 3840 ? 178.498 119.157 153.454 1.00 24.86  ? 3840 LEU A CG    1 
ATOM   17947 C CD1   . LEU A 1 3840 ? 177.283 119.775 152.791 1.00 24.86  ? 3840 LEU A CD1   1 
ATOM   17948 C CD2   . LEU A 1 3840 ? 178.133 117.847 154.127 1.00 24.86  ? 3840 LEU A CD2   1 
ATOM   17949 N N     . TYR A 1 3841 ? 182.398 118.521 150.990 1.00 29.90  ? 3841 TYR A N     1 
ATOM   17950 C CA    . TYR A 1 3841 ? 183.049 117.941 149.822 1.00 29.90  ? 3841 TYR A CA    1 
ATOM   17951 C C     . TYR A 1 3841 ? 184.564 117.881 149.964 1.00 29.90  ? 3841 TYR A C     1 
ATOM   17952 O O     . TYR A 1 3841 ? 185.153 116.804 149.841 1.00 29.90  ? 3841 TYR A O     1 
ATOM   17953 C CB    . TYR A 1 3841 ? 182.665 118.731 148.563 1.00 29.90  ? 3841 TYR A CB    1 
ATOM   17954 C CG    . TYR A 1 3841 ? 181.175 118.851 148.347 1.00 29.90  ? 3841 TYR A CG    1 
ATOM   17955 C CD1   . TYR A 1 3841 ? 180.349 117.743 148.454 1.00 29.90  ? 3841 TYR A CD1   1 
ATOM   17956 C CD2   . TYR A 1 3841 ? 180.596 120.072 148.032 1.00 29.90  ? 3841 TYR A CD2   1 
ATOM   17957 C CE1   . TYR A 1 3841 ? 178.987 117.846 148.256 1.00 29.90  ? 3841 TYR A CE1   1 
ATOM   17958 C CE2   . TYR A 1 3841 ? 179.235 120.185 147.833 1.00 29.90  ? 3841 TYR A CE2   1 
ATOM   17959 C CZ    . TYR A 1 3841 ? 178.436 119.069 147.947 1.00 29.90  ? 3841 TYR A CZ    1 
ATOM   17960 O OH    . TYR A 1 3841 ? 177.079 119.176 147.749 1.00 29.90  ? 3841 TYR A OH    1 
ATOM   17961 N N     . GLU A 1 3842 ? 185.216 119.013 150.220 1.00 34.37  ? 3842 GLU A N     1 
ATOM   17962 C CA    . GLU A 1 3842 ? 186.675 119.057 150.319 1.00 34.37  ? 3842 GLU A CA    1 
ATOM   17963 C C     . GLU A 1 3842 ? 187.123 118.774 151.754 1.00 34.37  ? 3842 GLU A C     1 
ATOM   17964 O O     . GLU A 1 3842 ? 187.753 119.592 152.423 1.00 34.37  ? 3842 GLU A O     1 
ATOM   17965 C CB    . GLU A 1 3842 ? 187.196 120.402 149.828 1.00 34.37  ? 3842 GLU A CB    1 
ATOM   17966 C CG    . GLU A 1 3842 ? 186.436 120.960 148.636 1.00 34.37  ? 3842 GLU A CG    1 
ATOM   17967 C CD    . GLU A 1 3842 ? 187.034 122.253 148.118 1.00 34.37  ? 3842 GLU A CD    1 
ATOM   17968 O OE1   . GLU A 1 3842 ? 188.045 122.192 147.388 1.00 34.37  ? 3842 GLU A OE1   1 
ATOM   17969 O OE2   . GLU A 1 3842 ? 186.492 123.332 148.440 1.00 34.37  ? 3842 GLU A OE2   1 
ATOM   17970 N N     . ASN A 1 3843 ? 186.780 117.578 152.220 1.00 37.14  ? 3843 ASN A N     1 
ATOM   17971 C CA    . ASN A 1 3843 ? 187.103 117.154 153.577 1.00 37.14  ? 3843 ASN A CA    1 
ATOM   17972 C C     . ASN A 1 3843 ? 188.214 116.116 153.545 1.00 37.14  ? 3843 ASN A C     1 
ATOM   17973 O O     . ASN A 1 3843 ? 187.967 114.966 153.148 1.00 37.14  ? 3843 ASN A O     1 
ATOM   17974 C CB    . ASN A 1 3843 ? 185.862 116.586 154.267 1.00 37.14  ? 3843 ASN A CB    1 
ATOM   17975 C CG    . ASN A 1 3843 ? 185.931 116.700 155.773 1.00 37.14  ? 3843 ASN A CG    1 
ATOM   17976 O OD1   . ASN A 1 3843 ? 186.970 116.438 156.376 1.00 37.14  ? 3843 ASN A OD1   1 
ATOM   17977 N ND2   . ASN A 1 3843 ? 184.824 117.095 156.390 1.00 37.14  ? 3843 ASN A ND2   1 
ATOM   17978 N N     . PRO A 1 3844 ? 189.440 116.462 153.941 1.00 40.52  ? 3844 PRO A N     1 
ATOM   17979 C CA    . PRO A 1 3844 ? 190.512 115.454 153.970 1.00 40.52  ? 3844 PRO A CA    1 
ATOM   17980 C C     . PRO A 1 3844 ? 190.251 114.318 154.942 1.00 40.52  ? 3844 PRO A C     1 
ATOM   17981 O O     . PRO A 1 3844 ? 190.811 113.230 154.761 1.00 40.52  ? 3844 PRO A O     1 
ATOM   17982 C CB    . PRO A 1 3844 ? 191.750 116.266 154.376 1.00 40.52  ? 3844 PRO A CB    1 
ATOM   17983 C CG    . PRO A 1 3844 ? 191.208 117.482 155.054 1.00 40.52  ? 3844 PRO A CG    1 
ATOM   17984 C CD    . PRO A 1 3844 ? 189.911 117.789 154.370 1.00 40.52  ? 3844 PRO A CD    1 
ATOM   17985 N N     . ASN A 1 3845 ? 189.421 114.530 155.963 1.00 40.96  ? 3845 ASN A N     1 
ATOM   17986 C CA    . ASN A 1 3845 ? 189.095 113.475 156.913 1.00 40.96  ? 3845 ASN A CA    1 
ATOM   17987 C C     . ASN A 1 3845 ? 188.054 112.500 156.381 1.00 40.96  ? 3845 ASN A C     1 
ATOM   17988 O O     . ASN A 1 3845 ? 187.779 111.492 157.041 1.00 40.96  ? 3845 ASN A O     1 
ATOM   17989 C CB    . ASN A 1 3845 ? 188.596 114.083 158.226 1.00 40.96  ? 3845 ASN A CB    1 
ATOM   17990 C CG    . ASN A 1 3845 ? 189.673 114.858 158.955 1.00 40.96  ? 3845 ASN A CG    1 
ATOM   17991 O OD1   . ASN A 1 3845 ? 190.695 114.299 159.350 1.00 40.96  ? 3845 ASN A OD1   1 
ATOM   17992 N ND2   . ASN A 1 3845 ? 189.447 116.153 159.141 1.00 40.96  ? 3845 ASN A ND2   1 
ATOM   17993 N N     . LEU A 1 3846 ? 187.471 112.773 155.214 1.00 45.93  ? 3846 LEU A N     1 
ATOM   17994 C CA    . LEU A 1 3846 ? 186.443 111.927 154.623 1.00 45.93  ? 3846 LEU A CA    1 
ATOM   17995 C C     . LEU A 1 3846 ? 186.944 111.211 153.372 1.00 45.93  ? 3846 LEU A C     1 
ATOM   17996 O O     . LEU A 1 3846 ? 186.154 110.864 152.491 1.00 45.93  ? 3846 LEU A O     1 
ATOM   17997 C CB    . LEU A 1 3846 ? 185.201 112.752 154.296 1.00 45.93  ? 3846 LEU A CB    1 
ATOM   17998 C CG    . LEU A 1 3846 ? 184.256 113.077 155.452 1.00 45.93  ? 3846 LEU A CG    1 
ATOM   17999 C CD1   . LEU A 1 3846 ? 182.974 113.678 154.915 1.00 45.93  ? 3846 LEU A CD1   1 
ATOM   18000 C CD2   . LEU A 1 3846 ? 183.964 111.835 156.276 1.00 45.93  ? 3846 LEU A CD2   1 
ATOM   18001 N N     . LYS A 1 3847 ? 188.256 110.987 153.281 1.00 59.25  ? 3847 LYS A N     1 
ATOM   18002 C CA    . LYS A 1 3847 ? 188.816 110.376 152.081 1.00 59.25  ? 3847 LYS A CA    1 
ATOM   18003 C C     . LYS A 1 3847 ? 188.430 108.908 151.952 1.00 59.25  ? 3847 LYS A C     1 
ATOM   18004 O O     . LYS A 1 3847 ? 188.206 108.425 150.836 1.00 59.25  ? 3847 LYS A O     1 
ATOM   18005 C CB    . LYS A 1 3847 ? 190.337 110.523 152.078 1.00 59.25  ? 3847 LYS A CB    1 
ATOM   18006 C CG    . LYS A 1 3847 ? 190.957 110.484 150.691 1.00 59.25  ? 3847 LYS A CG    1 
ATOM   18007 C CD    . LYS A 1 3847 ? 192.474 110.540 150.761 1.00 59.25  ? 3847 LYS A CD    1 
ATOM   18008 C CE    . LYS A 1 3847 ? 193.025 109.475 151.695 1.00 59.25  ? 3847 LYS A CE    1 
ATOM   18009 N NZ    . LYS A 1 3847 ? 192.530 108.115 151.343 1.00 59.25  ? 3847 LYS A NZ    1 
ATOM   18010 N N     . GLY A 1 3848 ? 188.345 108.185 153.066 1.00 60.31  ? 3848 GLY A N     1 
ATOM   18011 C CA    . GLY A 1 3848 ? 188.055 106.766 153.009 1.00 60.31  ? 3848 GLY A CA    1 
ATOM   18012 C C     . GLY A 1 3848 ? 186.973 106.310 153.966 1.00 60.31  ? 3848 GLY A C     1 
ATOM   18013 O O     . GLY A 1 3848 ? 186.683 105.113 154.057 1.00 60.31  ? 3848 GLY A O     1 
ATOM   18014 N N     . VAL A 1 3849 ? 186.368 107.252 154.687 1.00 57.03  ? 3849 VAL A N     1 
ATOM   18015 C CA    . VAL A 1 3849 ? 185.313 106.909 155.633 1.00 57.03  ? 3849 VAL A CA    1 
ATOM   18016 C C     . VAL A 1 3849 ? 184.061 106.506 154.867 1.00 57.03  ? 3849 VAL A C     1 
ATOM   18017 O O     . VAL A 1 3849 ? 183.644 107.188 153.922 1.00 57.03  ? 3849 VAL A O     1 
ATOM   18018 C CB    . VAL A 1 3849 ? 185.039 108.084 156.581 1.00 57.03  ? 3849 VAL A CB    1 
ATOM   18019 C CG1   . VAL A 1 3849 ? 183.977 107.708 157.598 1.00 57.03  ? 3849 VAL A CG1   1 
ATOM   18020 C CG2   . VAL A 1 3849 ? 186.320 108.512 157.277 1.00 57.03  ? 3849 VAL A CG2   1 
ATOM   18021 N N     . THR A 1 3850 ? 183.456 105.391 155.270 1.00 54.90  ? 3850 THR A N     1 
ATOM   18022 C CA    . THR A 1 3850 ? 182.284 104.850 154.590 1.00 54.90  ? 3850 THR A CA    1 
ATOM   18023 C C     . THR A 1 3850 ? 181.057 104.743 155.481 1.00 54.90  ? 3850 THR A C     1 
ATOM   18024 O O     . THR A 1 3850 ? 179.937 104.909 154.993 1.00 54.90  ? 3850 THR A O     1 
ATOM   18025 C CB    . THR A 1 3850 ? 182.601 103.466 154.005 1.00 54.90  ? 3850 THR A CB    1 
ATOM   18026 O OG1   . THR A 1 3850 ? 183.035 102.590 155.053 1.00 54.90  ? 3850 THR A OG1   1 
ATOM   18027 C CG2   . THR A 1 3850 ? 183.693 103.570 152.951 1.00 54.90  ? 3850 THR A CG2   1 
ATOM   18028 N N     . ASP A 1 3851 ? 181.232 104.460 156.771 1.00 53.39  ? 3851 ASP A N     1 
ATOM   18029 C CA    . ASP A 1 3851 ? 180.090 104.340 157.668 1.00 53.39  ? 3851 ASP A CA    1 
ATOM   18030 C C     . ASP A 1 3851 ? 179.358 105.671 157.769 1.00 53.39  ? 3851 ASP A C     1 
ATOM   18031 O O     . ASP A 1 3851 ? 179.958 106.699 158.095 1.00 53.39  ? 3851 ASP A O     1 
ATOM   18032 C CB    . ASP A 1 3851 ? 180.550 103.880 159.051 1.00 53.39  ? 3851 ASP A CB    1 
ATOM   18033 C CG    . ASP A 1 3851 ? 179.402 103.394 159.917 1.00 53.39  ? 3851 ASP A CG    1 
ATOM   18034 O OD1   . ASP A 1 3851 ? 178.239 103.468 159.469 1.00 53.39  ? 3851 ASP A OD1   1 
ATOM   18035 O OD2   . ASP A 1 3851 ? 179.664 102.939 161.051 1.00 53.39  ? 3851 ASP A OD2   1 
ATOM   18036 N N     . HIS A 1 3852 ? 178.049 105.640 157.510 1.00 52.86  ? 3852 HIS A N     1 
ATOM   18037 C CA    . HIS A 1 3852 ? 177.278 106.876 157.404 1.00 52.86  ? 3852 HIS A CA    1 
ATOM   18038 C C     . HIS A 1 3852 ? 177.288 107.661 158.710 1.00 52.86  ? 3852 HIS A C     1 
ATOM   18039 O O     . HIS A 1 3852 ? 177.427 108.890 158.700 1.00 52.86  ? 3852 HIS A O     1 
ATOM   18040 C CB    . HIS A 1 3852 ? 175.848 106.560 156.970 1.00 52.86  ? 3852 HIS A CB    1 
ATOM   18041 C CG    . HIS A 1 3852 ? 175.757 105.948 155.608 1.00 52.86  ? 3852 HIS A CG    1 
ATOM   18042 N ND1   . HIS A 1 3852 ? 174.663 105.221 155.189 1.00 52.86  ? 3852 HIS A ND1   1 
ATOM   18043 C CD2   . HIS A 1 3852 ? 176.622 105.959 154.566 1.00 52.86  ? 3852 HIS A CD2   1 
ATOM   18044 C CE1   . HIS A 1 3852 ? 174.859 104.809 153.950 1.00 52.86  ? 3852 HIS A CE1   1 
ATOM   18045 N NE2   . HIS A 1 3852 ? 176.040 105.243 153.548 1.00 52.86  ? 3852 HIS A NE2   1 
ATOM   18046 N N     . THR A 1 3853 ? 177.137 106.975 159.845 1.00 48.28  ? 3853 THR A N     1 
ATOM   18047 C CA    . THR A 1 3853 ? 177.204 107.669 161.127 1.00 48.28  ? 3853 THR A CA    1 
ATOM   18048 C C     . THR A 1 3853 ? 178.597 108.240 161.375 1.00 48.28  ? 3853 THR A C     1 
ATOM   18049 O O     . THR A 1 3853 ? 178.735 109.341 161.922 1.00 48.28  ? 3853 THR A O     1 
ATOM   18050 C CB    . THR A 1 3853 ? 176.781 106.730 162.261 1.00 48.28  ? 3853 THR A CB    1 
ATOM   18051 O OG1   . THR A 1 3853 ? 176.892 107.410 163.518 1.00 48.28  ? 3853 THR A OG1   1 
ATOM   18052 C CG2   . THR A 1 3853 ? 177.632 105.466 162.282 1.00 48.28  ? 3853 THR A CG2   1 
ATOM   18053 N N     . GLN A 1 3854 ? 179.640 107.512 160.969 1.00 45.00  ? 3854 GLN A N     1 
ATOM   18054 C CA    . GLN A 1 3854 ? 180.999 108.019 161.125 1.00 45.00  ? 3854 GLN A CA    1 
ATOM   18055 C C     . GLN A 1 3854 ? 181.234 109.239 160.243 1.00 45.00  ? 3854 GLN A C     1 
ATOM   18056 O O     . GLN A 1 3854 ? 181.858 110.215 160.678 1.00 45.00  ? 3854 GLN A O     1 
ATOM   18057 C CB    . GLN A 1 3854 ? 182.007 106.914 160.812 1.00 45.00  ? 3854 GLN A CB    1 
ATOM   18058 C CG    . GLN A 1 3854 ? 183.302 107.014 161.600 1.00 45.00  ? 3854 GLN A CG    1 
ATOM   18059 C CD    . GLN A 1 3854 ? 184.313 105.959 161.198 1.00 45.00  ? 3854 GLN A CD    1 
ATOM   18060 O OE1   . GLN A 1 3854 ? 184.910 106.029 160.126 1.00 45.00  ? 3854 GLN A OE1   1 
ATOM   18061 N NE2   . GLN A 1 3854 ? 184.507 104.969 162.061 1.00 45.00  ? 3854 GLN A NE2   1 
ATOM   18062 N N     . ARG A 1 3855 ? 180.733 109.207 159.005 1.00 41.94  ? 3855 ARG A N     1 
ATOM   18063 C CA    . ARG A 1 3855 ? 180.827 110.382 158.144 1.00 41.94  ? 3855 ARG A CA    1 
ATOM   18064 C C     . ARG A 1 3855 ? 180.067 111.559 158.737 1.00 41.94  ? 3855 ARG A C     1 
ATOM   18065 O O     . ARG A 1 3855 ? 180.528 112.700 158.661 1.00 41.94  ? 3855 ARG A O     1 
ATOM   18066 C CB    . ARG A 1 3855 ? 180.308 110.066 156.740 1.00 41.94  ? 3855 ARG A CB    1 
ATOM   18067 C CG    . ARG A 1 3855 ? 180.913 108.832 156.102 1.00 41.94  ? 3855 ARG A CG    1 
ATOM   18068 C CD    . ARG A 1 3855 ? 180.796 108.867 154.587 1.00 41.94  ? 3855 ARG A CD    1 
ATOM   18069 N NE    . ARG A 1 3855 ? 181.969 109.451 153.949 1.00 41.94  ? 3855 ARG A NE    1 
ATOM   18070 C CZ    . ARG A 1 3855 ? 181.923 110.404 153.028 1.00 41.94  ? 3855 ARG A CZ    1 
ATOM   18071 N NH1   . ARG A 1 3855 ? 180.774 110.908 152.612 1.00 41.94  ? 3855 ARG A NH1   1 
ATOM   18072 N NH2   . ARG A 1 3855 ? 183.059 110.858 152.507 1.00 41.94  ? 3855 ARG A NH2   1 
ATOM   18073 N N     . LEU A 1 3856 ? 178.898 111.304 159.331 1.00 36.32  ? 3856 LEU A N     1 
ATOM   18074 C CA    . LEU A 1 3856 ? 178.137 112.384 159.955 1.00 36.32  ? 3856 LEU A CA    1 
ATOM   18075 C C     . LEU A 1 3856 ? 178.903 113.004 161.117 1.00 36.32  ? 3856 LEU A C     1 
ATOM   18076 O O     . LEU A 1 3856 ? 178.960 114.233 161.250 1.00 36.32  ? 3856 LEU A O     1 
ATOM   18077 C CB    . LEU A 1 3856 ? 176.781 111.864 160.428 1.00 36.32  ? 3856 LEU A CB    1 
ATOM   18078 C CG    . LEU A 1 3856 ? 175.861 112.899 161.074 1.00 36.32  ? 3856 LEU A CG    1 
ATOM   18079 C CD1   . LEU A 1 3856 ? 175.490 113.980 160.075 1.00 36.32  ? 3856 LEU A CD1   1 
ATOM   18080 C CD2   . LEU A 1 3856 ? 174.615 112.234 161.638 1.00 36.32  ? 3856 LEU A CD2   1 
ATOM   18081 N N     . SER A 1 3857 ? 179.496 112.167 161.973 1.00 33.15  ? 3857 SER A N     1 
ATOM   18082 C CA    . SER A 1 3857 ? 180.257 112.689 163.105 1.00 33.15  ? 3857 SER A CA    1 
ATOM   18083 C C     . SER A 1 3857 ? 181.470 113.483 162.635 1.00 33.15  ? 3857 SER A C     1 
ATOM   18084 O O     . SER A 1 3857 ? 181.758 114.568 163.162 1.00 33.15  ? 3857 SER A O     1 
ATOM   18085 C CB    . SER A 1 3857 ? 180.688 111.544 164.019 1.00 33.15  ? 3857 SER A CB    1 
ATOM   18086 O OG    . SER A 1 3857 ? 181.522 110.630 163.328 1.00 33.15  ? 3857 SER A OG    1 
ATOM   18087 N N     . ILE A 1 3858 ? 182.191 112.960 161.640 1.00 32.11  ? 3858 ILE A N     1 
ATOM   18088 C CA    . ILE A 1 3858 ? 183.347 113.671 161.104 1.00 32.11  ? 3858 ILE A CA    1 
ATOM   18089 C C     . ILE A 1 3858 ? 182.917 114.994 160.488 1.00 32.11  ? 3858 ILE A C     1 
ATOM   18090 O O     . ILE A 1 3858 ? 183.587 116.020 160.656 1.00 32.11  ? 3858 ILE A O     1 
ATOM   18091 C CB    . ILE A 1 3858 ? 184.096 112.787 160.090 1.00 32.11  ? 3858 ILE A CB    1 
ATOM   18092 C CG1   . ILE A 1 3858 ? 184.755 111.601 160.798 1.00 32.11  ? 3858 ILE A CG1   1 
ATOM   18093 C CG2   . ILE A 1 3858 ? 185.129 113.600 159.329 1.00 32.11  ? 3858 ILE A CG2   1 
ATOM   18094 C CD1   . ILE A 1 3858 ? 186.074 111.934 161.455 1.00 32.11  ? 3858 ILE A CD1   1 
ATOM   18095 N N     . ILE A 1 3859 ? 181.791 114.995 159.770 1.00 28.93  ? 3859 ILE A N     1 
ATOM   18096 C CA    . ILE A 1 3859 ? 181.299 116.217 159.147 1.00 28.93  ? 3859 ILE A CA    1 
ATOM   18097 C C     . ILE A 1 3859 ? 180.963 117.256 160.204 1.00 28.93  ? 3859 ILE A C     1 
ATOM   18098 O O     . ILE A 1 3859 ? 181.315 118.429 160.066 1.00 28.93  ? 3859 ILE A O     1 
ATOM   18099 C CB    . ILE A 1 3859 ? 180.086 115.912 158.248 1.00 28.93  ? 3859 ILE A CB    1 
ATOM   18100 C CG1   . ILE A 1 3859 ? 180.549 115.417 156.881 1.00 28.93  ? 3859 ILE A CG1   1 
ATOM   18101 C CG2   . ILE A 1 3859 ? 179.217 117.145 158.080 1.00 28.93  ? 3859 ILE A CG2   1 
ATOM   18102 C CD1   . ILE A 1 3859 ? 179.472 114.718 156.095 1.00 28.93  ? 3859 ILE A CD1   1 
ATOM   18103 N N     . THR A 1 3860 ? 180.289 116.845 161.280 1.00 25.36  ? 3860 THR A N     1 
ATOM   18104 C CA    . THR A 1 3860 ? 179.942 117.794 162.336 1.00 25.36  ? 3860 THR A CA    1 
ATOM   18105 C C     . THR A 1 3860 ? 181.193 118.374 162.991 1.00 25.36  ? 3860 THR A C     1 
ATOM   18106 O O     . THR A 1 3860 ? 181.316 119.598 163.163 1.00 25.36  ? 3860 THR A O     1 
ATOM   18107 C CB    . THR A 1 3860 ? 179.057 117.114 163.380 1.00 25.36  ? 3860 THR A CB    1 
ATOM   18108 O OG1   . THR A 1 3860 ? 177.944 116.489 162.731 1.00 25.36  ? 3860 THR A OG1   1 
ATOM   18109 C CG2   . THR A 1 3860 ? 178.545 118.130 164.386 1.00 25.36  ? 3860 THR A CG2   1 
ATOM   18110 N N     . LYS A 1 3861 ? 182.138 117.505 163.359 1.00 22.59  ? 3861 LYS A N     1 
ATOM   18111 C CA    . LYS A 1 3861 ? 183.344 117.970 164.037 1.00 22.59  ? 3861 LYS A CA    1 
ATOM   18112 C C     . LYS A 1 3861 ? 184.151 118.906 163.144 1.00 22.59  ? 3861 LYS A C     1 
ATOM   18113 O O     . LYS A 1 3861 ? 184.579 119.985 163.578 1.00 22.59  ? 3861 LYS A O     1 
ATOM   18114 C CB    . LYS A 1 3861 ? 184.188 116.774 164.474 1.00 22.59  ? 3861 LYS A CB    1 
ATOM   18115 C CG    . LYS A 1 3861 ? 185.419 117.142 165.281 1.00 22.59  ? 3861 LYS A CG    1 
ATOM   18116 C CD    . LYS A 1 3861 ? 186.134 115.899 165.781 1.00 22.59  ? 3861 LYS A CD    1 
ATOM   18117 C CE    . LYS A 1 3861 ? 186.867 115.196 164.651 1.00 22.59  ? 3861 LYS A CE    1 
ATOM   18118 N NZ    . LYS A 1 3861 ? 187.663 114.040 165.144 1.00 22.59  ? 3861 LYS A NZ    1 
ATOM   18119 N N     . ASP A 1 3862 ? 184.355 118.518 161.883 1.00 21.82  ? 3862 ASP A N     1 
ATOM   18120 C CA    . ASP A 1 3862 ? 185.120 119.360 160.976 1.00 21.82  ? 3862 ASP A CA    1 
ATOM   18121 C C     . ASP A 1 3862 ? 184.365 120.630 160.616 1.00 21.82  ? 3862 ASP A C     1 
ATOM   18122 O O     . ASP A 1 3862 ? 184.992 121.655 160.351 1.00 21.82  ? 3862 ASP A O     1 
ATOM   18123 C CB    . ASP A 1 3862 ? 185.493 118.589 159.713 1.00 21.82  ? 3862 ASP A CB    1 
ATOM   18124 C CG    . ASP A 1 3862 ? 186.802 119.062 159.114 1.00 21.82  ? 3862 ASP A CG    1 
ATOM   18125 O OD1   . ASP A 1 3862 ? 187.480 119.892 159.754 1.00 21.82  ? 3862 ASP A OD1   1 
ATOM   18126 O OD2   . ASP A 1 3862 ? 187.152 118.613 158.004 1.00 21.82  ? 3862 ASP A OD2   1 
ATOM   18127 N N     . LEU A 1 3863 ? 183.032 120.593 160.610 1.00 20.45  ? 3863 LEU A N     1 
ATOM   18128 C CA    . LEU A 1 3863 ? 182.262 121.813 160.411 1.00 20.45  ? 3863 LEU A CA    1 
ATOM   18129 C C     . LEU A 1 3863 ? 182.544 122.810 161.518 1.00 20.45  ? 3863 LEU A C     1 
ATOM   18130 O O     . LEU A 1 3863 ? 182.845 123.980 161.255 1.00 20.45  ? 3863 LEU A O     1 
ATOM   18131 C CB    . LEU A 1 3863 ? 180.770 121.487 160.356 1.00 20.45  ? 3863 LEU A CB    1 
ATOM   18132 C CG    . LEU A 1 3863 ? 179.833 122.692 160.420 1.00 20.45  ? 3863 LEU A CG    1 
ATOM   18133 C CD1   . LEU A 1 3863 ? 179.976 123.565 159.184 1.00 20.45  ? 3863 LEU A CD1   1 
ATOM   18134 C CD2   . LEU A 1 3863 ? 178.399 122.237 160.606 1.00 20.45  ? 3863 LEU A CD2   1 
ATOM   18135 N N     . PHE A 1 3864 ? 182.469 122.356 162.770 1.00 18.85  ? 3864 PHE A N     1 
ATOM   18136 C CA    . PHE A 1 3864 ? 182.769 123.252 163.883 1.00 18.85  ? 3864 PHE A CA    1 
ATOM   18137 C C     . PHE A 1 3864 ? 184.195 123.782 163.785 1.00 18.85  ? 3864 PHE A C     1 
ATOM   18138 O O     . PHE A 1 3864 ? 184.433 124.992 163.912 1.00 18.85  ? 3864 PHE A O     1 
ATOM   18139 C CB    . PHE A 1 3864 ? 182.545 122.533 165.213 1.00 18.85  ? 3864 PHE A CB    1 
ATOM   18140 C CG    . PHE A 1 3864 ? 181.114 122.527 165.661 1.00 18.85  ? 3864 PHE A CG    1 
ATOM   18141 C CD1   . PHE A 1 3864 ? 180.528 123.675 166.159 1.00 18.85  ? 3864 PHE A CD1   1 
ATOM   18142 C CD2   . PHE A 1 3864 ? 180.355 121.375 165.581 1.00 18.85  ? 3864 PHE A CD2   1 
ATOM   18143 C CE1   . PHE A 1 3864 ? 179.212 123.673 166.570 1.00 18.85  ? 3864 PHE A CE1   1 
ATOM   18144 C CE2   . PHE A 1 3864 ? 179.040 121.368 165.990 1.00 18.85  ? 3864 PHE A CE2   1 
ATOM   18145 C CZ    . PHE A 1 3864 ? 178.468 122.518 166.485 1.00 18.85  ? 3864 PHE A CZ    1 
ATOM   18146 N N     . GLN A 1 3865 ? 185.154 122.892 163.519 1.00 19.78  ? 3865 GLN A N     1 
ATOM   18147 C CA    . GLN A 1 3865 ? 186.557 123.298 163.477 1.00 19.78  ? 3865 GLN A CA    1 
ATOM   18148 C C     . GLN A 1 3865 ? 186.816 124.306 162.361 1.00 19.78  ? 3865 GLN A C     1 
ATOM   18149 O O     . GLN A 1 3865 ? 187.459 125.339 162.580 1.00 19.78  ? 3865 GLN A O     1 
ATOM   18150 C CB    . GLN A 1 3865 ? 187.448 122.069 163.308 1.00 19.78  ? 3865 GLN A CB    1 
ATOM   18151 C CG    . GLN A 1 3865 ? 188.928 122.384 163.223 1.00 19.78  ? 3865 GLN A CG    1 
ATOM   18152 C CD    . GLN A 1 3865 ? 189.486 122.905 164.528 1.00 19.78  ? 3865 GLN A CD    1 
ATOM   18153 O OE1   . GLN A 1 3865 ? 189.852 124.075 164.638 1.00 19.78  ? 3865 GLN A OE1   1 
ATOM   18154 N NE2   . GLN A 1 3865 ? 189.553 122.037 165.530 1.00 19.78  ? 3865 GLN A NE2   1 
ATOM   18155 N N     . VAL A 1 3866 ? 186.319 124.023 161.155 1.00 17.53  ? 3866 VAL A N     1 
ATOM   18156 C CA    . VAL A 1 3866 ? 186.584 124.881 160.007 1.00 17.53  ? 3866 VAL A CA    1 
ATOM   18157 C C     . VAL A 1 3866 ? 185.870 126.215 160.157 1.00 17.53  ? 3866 VAL A C     1 
ATOM   18158 O O     . VAL A 1 3866 ? 186.422 127.269 159.815 1.00 17.53  ? 3866 VAL A O     1 
ATOM   18159 C CB    . VAL A 1 3866 ? 186.185 124.160 158.707 1.00 17.53  ? 3866 VAL A CB    1 
ATOM   18160 C CG1   . VAL A 1 3866 ? 186.189 125.121 157.538 1.00 17.53  ? 3866 VAL A CG1   1 
ATOM   18161 C CG2   . VAL A 1 3866 ? 187.131 123.004 158.436 1.00 17.53  ? 3866 VAL A CG2   1 
ATOM   18162 N N     . ALA A 1 3867 ? 184.636 126.202 160.670 1.00 18.50  ? 3867 ALA A N     1 
ATOM   18163 C CA    . ALA A 1 3867 ? 183.935 127.456 160.910 1.00 18.50  ? 3867 ALA A CA    1 
ATOM   18164 C C     . ALA A 1 3867 ? 184.698 128.316 161.905 1.00 18.50  ? 3867 ALA A C     1 
ATOM   18165 O O     . ALA A 1 3867 ? 184.897 129.516 161.678 1.00 18.50  ? 3867 ALA A O     1 
ATOM   18166 C CB    . ALA A 1 3867 ? 182.517 127.180 161.407 1.00 18.50  ? 3867 ALA A CB    1 
ATOM   18167 N N     . PHE A 1 3868 ? 185.166 127.712 163.002 1.00 19.16  ? 3868 PHE A N     1 
ATOM   18168 C CA    . PHE A 1 3868 ? 185.930 128.480 163.978 1.00 19.16  ? 3868 PHE A CA    1 
ATOM   18169 C C     . PHE A 1 3868 ? 187.202 129.041 163.362 1.00 19.16  ? 3868 PHE A C     1 
ATOM   18170 O O     . PHE A 1 3868 ? 187.535 130.212 163.563 1.00 19.16  ? 3868 PHE A O     1 
ATOM   18171 C CB    . PHE A 1 3868 ? 186.274 127.625 165.194 1.00 19.16  ? 3868 PHE A CB    1 
ATOM   18172 C CG    . PHE A 1 3868 ? 187.330 128.234 166.067 1.00 19.16  ? 3868 PHE A CG    1 
ATOM   18173 C CD1   . PHE A 1 3868 ? 187.059 129.369 166.811 1.00 19.16  ? 3868 PHE A CD1   1 
ATOM   18174 C CD2   . PHE A 1 3868 ? 188.600 127.690 166.125 1.00 19.16  ? 3868 PHE A CD2   1 
ATOM   18175 C CE1   . PHE A 1 3868 ? 188.029 129.939 167.606 1.00 19.16  ? 3868 PHE A CE1   1 
ATOM   18176 C CE2   . PHE A 1 3868 ? 189.574 128.258 166.919 1.00 19.16  ? 3868 PHE A CE2   1 
ATOM   18177 C CZ    . PHE A 1 3868 ? 189.288 129.383 167.659 1.00 19.16  ? 3868 PHE A CZ    1 
ATOM   18178 N N     . ASN A 1 3869 ? 187.932 128.216 162.609 1.00 20.35  ? 3869 ASN A N     1 
ATOM   18179 C CA    . ASN A 1 3869 ? 189.194 128.669 162.033 1.00 20.35  ? 3869 ASN A CA    1 
ATOM   18180 C C     . ASN A 1 3869 ? 188.974 129.831 161.075 1.00 20.35  ? 3869 ASN A C     1 
ATOM   18181 O O     . ASN A 1 3869 ? 189.649 130.864 161.165 1.00 20.35  ? 3869 ASN A O     1 
ATOM   18182 C CB    . ASN A 1 3869 ? 189.894 127.512 161.324 1.00 20.35  ? 3869 ASN A CB    1 
ATOM   18183 C CG    . ASN A 1 3869 ? 190.387 126.454 162.285 1.00 20.35  ? 3869 ASN A CG    1 
ATOM   18184 O OD1   . ASN A 1 3869 ? 190.471 126.686 163.491 1.00 20.35  ? 3869 ASN A OD1   1 
ATOM   18185 N ND2   . ASN A 1 3869 ? 190.713 125.281 161.757 1.00 20.35  ? 3869 ASN A ND2   1 
ATOM   18186 N N     . ARG A 1 3870 ? 188.014 129.689 160.160 1.00 22.19  ? 3870 ARG A N     1 
ATOM   18187 C CA    . ARG A 1 3870 ? 187.803 130.721 159.153 1.00 22.19  ? 3870 ARG A CA    1 
ATOM   18188 C C     . ARG A 1 3870 ? 187.255 132.001 159.772 1.00 22.19  ? 3870 ARG A C     1 
ATOM   18189 O O     . ARG A 1 3870 ? 187.607 133.102 159.335 1.00 22.19  ? 3870 ARG A O     1 
ATOM   18190 C CB    . ARG A 1 3870 ? 186.872 130.202 158.060 1.00 22.19  ? 3870 ARG A CB    1 
ATOM   18191 C CG    . ARG A 1 3870 ? 187.517 129.158 157.162 1.00 22.19  ? 3870 ARG A CG    1 
ATOM   18192 C CD    . ARG A 1 3870 ? 186.490 128.467 156.287 1.00 22.19  ? 3870 ARG A CD    1 
ATOM   18193 N NE    . ARG A 1 3870 ? 186.418 129.038 154.948 1.00 22.19  ? 3870 ARG A NE    1 
ATOM   18194 C CZ    . ARG A 1 3870 ? 186.637 128.353 153.834 1.00 22.19  ? 3870 ARG A CZ    1 
ATOM   18195 N NH1   . ARG A 1 3870 ? 186.946 127.067 153.863 1.00 22.19  ? 3870 ARG A NH1   1 
ATOM   18196 N NH2   . ARG A 1 3870 ? 186.538 128.973 152.662 1.00 22.19  ? 3870 ARG A NH2   1 
ATOM   18197 N N     . VAL A 1 3871 ? 186.391 131.886 160.785 1.00 19.34  ? 3871 VAL A N     1 
ATOM   18198 C CA    . VAL A 1 3871 ? 185.866 133.090 161.420 1.00 19.34  ? 3871 VAL A CA    1 
ATOM   18199 C C     . VAL A 1 3871 ? 186.948 133.786 162.238 1.00 19.34  ? 3871 VAL A C     1 
ATOM   18200 O O     . VAL A 1 3871 ? 187.111 135.009 162.157 1.00 19.34  ? 3871 VAL A O     1 
ATOM   18201 C CB    . VAL A 1 3871 ? 184.635 132.750 162.279 1.00 19.34  ? 3871 VAL A CB    1 
ATOM   18202 C CG1   . VAL A 1 3871 ? 184.224 133.949 163.107 1.00 19.34  ? 3871 VAL A CG1   1 
ATOM   18203 C CG2   . VAL A 1 3871 ? 183.488 132.298 161.401 1.00 19.34  ? 3871 VAL A CG2   1 
ATOM   18204 N N     . ALA A 1 3872 ? 187.715 133.027 163.023 1.00 21.51  ? 3872 ALA A N     1 
ATOM   18205 C CA    . ALA A 1 3872 ? 188.713 133.601 163.913 1.00 21.51  ? 3872 ALA A CA    1 
ATOM   18206 C C     . ALA A 1 3872 ? 189.958 134.090 163.190 1.00 21.51  ? 3872 ALA A C     1 
ATOM   18207 O O     . ALA A 1 3872 ? 190.699 134.897 163.759 1.00 21.51  ? 3872 ALA A O     1 
ATOM   18208 C CB    . ALA A 1 3872 ? 189.115 132.580 164.979 1.00 21.51  ? 3872 ALA A CB    1 
ATOM   18209 N N     . ARG A 1 3873 ? 190.218 133.624 161.965 1.00 25.53  ? 3873 ARG A N     1 
ATOM   18210 C CA    . ARG A 1 3873 ? 191.351 134.160 161.219 1.00 25.53  ? 3873 ARG A CA    1 
ATOM   18211 C C     . ARG A 1 3873 ? 191.198 135.654 160.979 1.00 25.53  ? 3873 ARG A C     1 
ATOM   18212 O O     . ARG A 1 3873 ? 192.198 136.365 160.833 1.00 25.53  ? 3873 ARG A O     1 
ATOM   18213 C CB    . ARG A 1 3873 ? 191.505 133.428 159.887 1.00 25.53  ? 3873 ARG A CB    1 
ATOM   18214 C CG    . ARG A 1 3873 ? 192.341 132.164 159.964 1.00 25.53  ? 3873 ARG A CG    1 
ATOM   18215 C CD    . ARG A 1 3873 ? 193.653 132.419 160.687 1.00 25.53  ? 3873 ARG A CD    1 
ATOM   18216 N NE    . ARG A 1 3873 ? 194.540 131.262 160.649 1.00 25.53  ? 3873 ARG A NE    1 
ATOM   18217 C CZ    . ARG A 1 3873 ? 195.654 131.144 161.359 1.00 25.53  ? 3873 ARG A CZ    1 
ATOM   18218 N NH1   . ARG A 1 3873 ? 196.035 132.082 162.211 1.00 25.53  ? 3873 ARG A NH1   1 
ATOM   18219 N NH2   . ARG A 1 3873 ? 196.403 130.055 161.213 1.00 25.53  ? 3873 ARG A NH2   1 
ATOM   18220 N N     . GLY A 1 3874 ? 189.962 136.143 160.933 1.00 20.72  ? 3874 GLY A N     1 
ATOM   18221 C CA    . GLY A 1 3874 ? 189.701 137.558 160.780 1.00 20.72  ? 3874 GLY A CA    1 
ATOM   18222 C C     . GLY A 1 3874 ? 188.954 138.148 161.957 1.00 20.72  ? 3874 GLY A C     1 
ATOM   18223 O O     . GLY A 1 3874 ? 188.040 138.958 161.779 1.00 20.72  ? 3874 GLY A O     1 
ATOM   18224 N N     . MET A 1 3875 ? 189.331 137.750 163.169 1.00 20.36  ? 3875 MET A N     1 
ATOM   18225 C CA    . MET A 1 3875 ? 188.682 138.238 164.375 1.00 20.36  ? 3875 MET A CA    1 
ATOM   18226 C C     . MET A 1 3875 ? 189.754 138.585 165.397 1.00 20.36  ? 3875 MET A C     1 
ATOM   18227 O O     . MET A 1 3875 ? 190.813 137.951 165.433 1.00 20.36  ? 3875 MET A O     1 
ATOM   18228 C CB    . MET A 1 3875 ? 187.697 137.196 164.935 1.00 20.36  ? 3875 MET A CB    1 
ATOM   18229 C CG    . MET A 1 3875 ? 187.305 137.402 166.388 1.00 20.36  ? 3875 MET A CG    1 
ATOM   18230 S SD    . MET A 1 3875 ? 185.709 136.683 166.818 1.00 20.36  ? 3875 MET A SD    1 
ATOM   18231 C CE    . MET A 1 3875 ? 185.879 135.055 166.105 1.00 20.36  ? 3875 MET A CE    1 
ATOM   18232 N N     . LEU A 1 3876 ? 189.485 139.606 166.209 1.00 20.39  ? 3876 LEU A N     1 
ATOM   18233 C CA    . LEU A 1 3876 ? 190.453 140.058 167.200 1.00 20.39  ? 3876 LEU A CA    1 
ATOM   18234 C C     . LEU A 1 3876 ? 190.787 138.932 168.172 1.00 20.39  ? 3876 LEU A C     1 
ATOM   18235 O O     . LEU A 1 3876 ? 189.939 138.101 168.508 1.00 20.39  ? 3876 LEU A O     1 
ATOM   18236 C CB    . LEU A 1 3876 ? 189.903 141.262 167.964 1.00 20.39  ? 3876 LEU A CB    1 
ATOM   18237 C CG    . LEU A 1 3876 ? 189.868 142.603 167.230 1.00 20.39  ? 3876 LEU A CG    1 
ATOM   18238 C CD1   . LEU A 1 3876 ? 189.309 143.678 168.141 1.00 20.39  ? 3876 LEU A CD1   1 
ATOM   18239 C CD2   . LEU A 1 3876 ? 191.241 142.994 166.723 1.00 20.39  ? 3876 LEU A CD2   1 
ATOM   18240 N N     . HIS A 1 3877 ? 192.045 138.906 168.621 1.00 19.71  ? 3877 HIS A N     1 
ATOM   18241 C CA    . HIS A 1 3877 ? 192.508 137.800 169.455 1.00 19.71  ? 3877 HIS A CA    1 
ATOM   18242 C C     . HIS A 1 3877 ? 191.753 137.725 170.775 1.00 19.71  ? 3877 HIS A C     1 
ATOM   18243 O O     . HIS A 1 3877 ? 191.624 136.640 171.353 1.00 19.71  ? 3877 HIS A O     1 
ATOM   18244 C CB    . HIS A 1 3877 ? 194.007 137.921 169.722 1.00 19.71  ? 3877 HIS A CB    1 
ATOM   18245 C CG    . HIS A 1 3877 ? 194.603 136.706 170.362 1.00 19.71  ? 3877 HIS A CG    1 
ATOM   18246 N ND1   . HIS A 1 3877 ? 194.682 136.547 171.729 1.00 19.71  ? 3877 HIS A ND1   1 
ATOM   18247 C CD2   . HIS A 1 3877 ? 195.144 135.588 169.823 1.00 19.71  ? 3877 HIS A CD2   1 
ATOM   18248 C CE1   . HIS A 1 3877 ? 195.248 135.386 172.004 1.00 19.71  ? 3877 HIS A CE1   1 
ATOM   18249 N NE2   . HIS A 1 3877 ? 195.538 134.784 170.864 1.00 19.71  ? 3877 HIS A NE2   1 
ATOM   18250 N N     . GLN A 1 3878 ? 191.251 138.856 171.270 1.00 18.89  ? 3878 GLN A N     1 
ATOM   18251 C CA    . GLN A 1 3878 ? 190.495 138.842 172.515 1.00 18.89  ? 3878 GLN A CA    1 
ATOM   18252 C C     . GLN A 1 3878 ? 189.097 138.263 172.348 1.00 18.89  ? 3878 GLN A C     1 
ATOM   18253 O O     . GLN A 1 3878 ? 188.429 138.009 173.356 1.00 18.89  ? 3878 GLN A O     1 
ATOM   18254 C CB    . GLN A 1 3878 ? 190.406 140.256 173.090 1.00 18.89  ? 3878 GLN A CB    1 
ATOM   18255 C CG    . GLN A 1 3878 ? 189.700 141.252 172.188 1.00 18.89  ? 3878 GLN A CG    1 
ATOM   18256 C CD    . GLN A 1 3878 ? 189.717 142.657 172.752 1.00 18.89  ? 3878 GLN A CD    1 
ATOM   18257 O OE1   . GLN A 1 3878 ? 190.406 142.936 173.733 1.00 18.89  ? 3878 GLN A OE1   1 
ATOM   18258 N NE2   . GLN A 1 3878 ? 188.956 143.553 172.135 1.00 18.89  ? 3878 GLN A NE2   1 
ATOM   18259 N N     . ASP A 1 3879 ? 188.641 138.051 171.114 1.00 20.10  ? 3879 ASP A N     1 
ATOM   18260 C CA    . ASP A 1 3879 ? 187.312 137.518 170.853 1.00 20.10  ? 3879 ASP A CA    1 
ATOM   18261 C C     . ASP A 1 3879 ? 187.323 136.061 170.410 1.00 20.10  ? 3879 ASP A C     1 
ATOM   18262 O O     . ASP A 1 3879 ? 186.253 135.508 170.138 1.00 20.10  ? 3879 ASP A O     1 
ATOM   18263 C CB    . ASP A 1 3879 ? 186.602 138.369 169.795 1.00 20.10  ? 3879 ASP A CB    1 
ATOM   18264 C CG    . ASP A 1 3879 ? 186.463 139.817 170.209 1.00 20.10  ? 3879 ASP A CG    1 
ATOM   18265 O OD1   . ASP A 1 3879 ? 186.459 140.090 171.427 1.00 20.10  ? 3879 ASP A OD1   1 
ATOM   18266 O OD2   . ASP A 1 3879 ? 186.360 140.684 169.318 1.00 20.10  ? 3879 ASP A OD2   1 
ATOM   18267 N N     . HIS A 1 3880 ? 188.495 135.428 170.322 1.00 17.93  ? 3880 HIS A N     1 
ATOM   18268 C CA    . HIS A 1 3880 ? 188.540 134.013 169.965 1.00 17.93  ? 3880 HIS A CA    1 
ATOM   18269 C C     . HIS A 1 3880 ? 187.836 133.159 171.009 1.00 17.93  ? 3880 HIS A C     1 
ATOM   18270 O O     . HIS A 1 3880 ? 187.090 132.232 170.667 1.00 17.93  ? 3880 HIS A O     1 
ATOM   18271 C CB    . HIS A 1 3880 ? 189.988 133.552 169.801 1.00 17.93  ? 3880 HIS A CB    1 
ATOM   18272 C CG    . HIS A 1 3880 ? 190.693 134.159 168.629 1.00 17.93  ? 3880 HIS A CG    1 
ATOM   18273 N ND1   . HIS A 1 3880 ? 191.958 133.773 168.243 1.00 17.93  ? 3880 HIS A ND1   1 
ATOM   18274 C CD2   . HIS A 1 3880 ? 190.309 135.119 167.756 1.00 17.93  ? 3880 HIS A CD2   1 
ATOM   18275 C CE1   . HIS A 1 3880 ? 192.325 134.472 167.185 1.00 17.93  ? 3880 HIS A CE1   1 
ATOM   18276 N NE2   . HIS A 1 3880 ? 191.343 135.296 166.869 1.00 17.93  ? 3880 HIS A NE2   1 
ATOM   18277 N N     . ILE A 1 3881 ? 188.061 133.456 172.290 1.00 19.23  ? 3881 ILE A N     1 
ATOM   18278 C CA    . ILE A 1 3881 ? 187.471 132.653 173.353 1.00 19.23  ? 3881 ILE A CA    1 
ATOM   18279 C C     . ILE A 1 3881 ? 185.954 132.802 173.357 1.00 19.23  ? 3881 ILE A C     1 
ATOM   18280 O O     . ILE A 1 3881 ? 185.228 131.847 173.651 1.00 19.23  ? 3881 ILE A O     1 
ATOM   18281 C CB    . ILE A 1 3881 ? 188.092 133.022 174.713 1.00 19.23  ? 3881 ILE A CB    1 
ATOM   18282 C CG1   . ILE A 1 3881 ? 187.460 132.194 175.830 1.00 19.23  ? 3881 ILE A CG1   1 
ATOM   18283 C CG2   . ILE A 1 3881 ? 187.951 134.510 174.988 1.00 19.23  ? 3881 ILE A CG2   1 
ATOM   18284 C CD1   . ILE A 1 3881 ? 187.660 130.707 175.661 1.00 19.23  ? 3881 ILE A CD1   1 
ATOM   18285 N N     . THR A 1 3882 ? 185.449 133.991 173.024 1.00 18.27  ? 3882 THR A N     1 
ATOM   18286 C CA    . THR A 1 3882 ? 184.004 134.191 172.962 1.00 18.27  ? 3882 THR A CA    1 
ATOM   18287 C C     . THR A 1 3882 ? 183.373 133.310 171.888 1.00 18.27  ? 3882 THR A C     1 
ATOM   18288 O O     . THR A 1 3882 ? 182.356 132.647 172.128 1.00 18.27  ? 3882 THR A O     1 
ATOM   18289 C CB    . THR A 1 3882 ? 183.693 135.665 172.701 1.00 18.27  ? 3882 THR A CB    1 
ATOM   18290 O OG1   . THR A 1 3882 ? 183.910 136.418 173.900 1.00 18.27  ? 3882 THR A OG1   1 
ATOM   18291 C CG2   . THR A 1 3882 ? 182.252 135.840 172.255 1.00 18.27  ? 3882 THR A CG2   1 
ATOM   18292 N N     . PHE A 1 3883 ? 183.970 133.285 170.696 1.00 15.04  ? 3883 PHE A N     1 
ATOM   18293 C CA    . PHE A 1 3883 ? 183.429 132.456 169.624 1.00 15.04  ? 3883 PHE A CA    1 
ATOM   18294 C C     . PHE A 1 3883 ? 183.563 130.975 169.950 1.00 15.04  ? 3883 PHE A C     1 
ATOM   18295 O O     . PHE A 1 3883 ? 182.669 130.181 169.633 1.00 15.04  ? 3883 PHE A O     1 
ATOM   18296 C CB    . PHE A 1 3883 ? 184.124 132.779 168.304 1.00 15.04  ? 3883 PHE A CB    1 
ATOM   18297 C CG    . PHE A 1 3883 ? 183.386 132.280 167.100 1.00 15.04  ? 3883 PHE A CG    1 
ATOM   18298 C CD1   . PHE A 1 3883 ? 182.064 132.631 166.892 1.00 15.04  ? 3883 PHE A CD1   1 
ATOM   18299 C CD2   . PHE A 1 3883 ? 184.008 131.457 166.180 1.00 15.04  ? 3883 PHE A CD2   1 
ATOM   18300 C CE1   . PHE A 1 3883 ? 181.377 132.173 165.788 1.00 15.04  ? 3883 PHE A CE1   1 
ATOM   18301 C CE2   . PHE A 1 3883 ? 183.325 130.996 165.074 1.00 15.04  ? 3883 PHE A CE2   1 
ATOM   18302 C CZ    . PHE A 1 3883 ? 182.009 131.355 164.877 1.00 15.04  ? 3883 PHE A CZ    1 
ATOM   18303 N N     . ALA A 1 3884 ? 184.673 130.582 170.578 1.00 17.69  ? 3884 ALA A N     1 
ATOM   18304 C CA    . ALA A 1 3884 ? 184.818 129.193 170.996 1.00 17.69  ? 3884 ALA A CA    1 
ATOM   18305 C C     . ALA A 1 3884 ? 183.754 128.814 172.018 1.00 17.69  ? 3884 ALA A C     1 
ATOM   18306 O O     . ALA A 1 3884 ? 183.203 127.711 171.967 1.00 17.69  ? 3884 ALA A O     1 
ATOM   18307 C CB    . ALA A 1 3884 ? 186.215 128.953 171.561 1.00 17.69  ? 3884 ALA A CB    1 
ATOM   18308 N N     . MET A 1 3885 ? 183.452 129.718 172.952 1.00 20.37  ? 3885 MET A N     1 
ATOM   18309 C CA    . MET A 1 3885 ? 182.404 129.460 173.933 1.00 20.37  ? 3885 MET A CA    1 
ATOM   18310 C C     . MET A 1 3885 ? 181.045 129.327 173.260 1.00 20.37  ? 3885 MET A C     1 
ATOM   18311 O O     . MET A 1 3885 ? 180.245 128.455 173.622 1.00 20.37  ? 3885 MET A O     1 
ATOM   18312 C CB    . MET A 1 3885 ? 182.379 130.581 174.970 1.00 20.37  ? 3885 MET A CB    1 
ATOM   18313 C CG    . MET A 1 3885 ? 183.462 130.476 176.027 1.00 20.37  ? 3885 MET A CG    1 
ATOM   18314 S SD    . MET A 1 3885 ? 183.142 129.198 177.248 1.00 20.37  ? 3885 MET A SD    1 
ATOM   18315 C CE    . MET A 1 3885 ? 181.807 129.946 178.174 1.00 20.37  ? 3885 MET A CE    1 
ATOM   18316 N N     . LEU A 1 3886 ? 180.763 130.191 172.283 1.00 18.69  ? 3886 LEU A N     1 
ATOM   18317 C CA    . LEU A 1 3886 ? 179.493 130.104 171.567 1.00 18.69  ? 3886 LEU A CA    1 
ATOM   18318 C C     . LEU A 1 3886 ? 179.371 128.787 170.809 1.00 18.69  ? 3886 LEU A C     1 
ATOM   18319 O O     . LEU A 1 3886 ? 178.312 128.147 170.828 1.00 18.69  ? 3886 LEU A O     1 
ATOM   18320 C CB    . LEU A 1 3886 ? 179.343 131.291 170.616 1.00 18.69  ? 3886 LEU A CB    1 
ATOM   18321 C CG    . LEU A 1 3886 ? 179.136 132.656 171.274 1.00 18.69  ? 3886 LEU A CG    1 
ATOM   18322 C CD1   . LEU A 1 3886 ? 179.430 133.782 170.297 1.00 18.69  ? 3886 LEU A CD1   1 
ATOM   18323 C CD2   . LEU A 1 3886 ? 177.725 132.775 171.818 1.00 18.69  ? 3886 LEU A CD2   1 
ATOM   18324 N N     . LEU A 1 3887 ? 180.445 128.361 170.141 1.00 17.01  ? 3887 LEU A N     1 
ATOM   18325 C CA    . LEU A 1 3887 ? 180.404 127.088 169.428 1.00 17.01  ? 3887 LEU A CA    1 
ATOM   18326 C C     . LEU A 1 3887 ? 180.289 125.915 170.395 1.00 17.01  ? 3887 LEU A C     1 
ATOM   18327 O O     . LEU A 1 3887 ? 179.630 124.915 170.089 1.00 17.01  ? 3887 LEU A O     1 
ATOM   18328 C CB    . LEU A 1 3887 ? 181.634 126.938 168.539 1.00 17.01  ? 3887 LEU A CB    1 
ATOM   18329 C CG    . LEU A 1 3887 ? 181.709 127.921 167.371 1.00 17.01  ? 3887 LEU A CG    1 
ATOM   18330 C CD1   . LEU A 1 3887 ? 182.964 127.683 166.561 1.00 17.01  ? 3887 LEU A CD1   1 
ATOM   18331 C CD2   . LEU A 1 3887 ? 180.476 127.804 166.497 1.00 17.01  ? 3887 LEU A CD2   1 
ATOM   18332 N N     . ALA A 1 3888 ? 180.923 126.015 171.565 1.00 19.09  ? 3888 ALA A N     1 
ATOM   18333 C CA    . ALA A 1 3888 ? 180.773 124.979 172.579 1.00 19.09  ? 3888 ALA A CA    1 
ATOM   18334 C C     . ALA A 1 3888 ? 179.331 124.885 173.057 1.00 19.09  ? 3888 ALA A C     1 
ATOM   18335 O O     . ALA A 1 3888 ? 178.800 123.785 173.244 1.00 19.09  ? 3888 ALA A O     1 
ATOM   18336 C CB    . ALA A 1 3888 ? 181.713 125.254 173.751 1.00 19.09  ? 3888 ALA A CB    1 
ATOM   18337 N N     . ARG A 1 3889 ? 178.682 126.033 173.264 1.00 22.89  ? 3889 ARG A N     1 
ATOM   18338 C CA    . ARG A 1 3889 ? 177.274 126.028 173.647 1.00 22.89  ? 3889 ARG A CA    1 
ATOM   18339 C C     . ARG A 1 3889 ? 176.407 125.421 172.551 1.00 22.89  ? 3889 ARG A C     1 
ATOM   18340 O O     . ARG A 1 3889 ? 175.463 124.674 172.836 1.00 22.89  ? 3889 ARG A O     1 
ATOM   18341 C CB    . ARG A 1 3889 ? 176.813 127.449 173.970 1.00 22.89  ? 3889 ARG A CB    1 
ATOM   18342 C CG    . ARG A 1 3889 ? 177.313 127.977 175.301 1.00 22.89  ? 3889 ARG A CG    1 
ATOM   18343 C CD    . ARG A 1 3889 ? 176.754 129.360 175.580 1.00 22.89  ? 3889 ARG A CD    1 
ATOM   18344 N NE    . ARG A 1 3889 ? 175.321 129.423 175.325 1.00 22.89  ? 3889 ARG A NE    1 
ATOM   18345 C CZ    . ARG A 1 3889 ? 174.404 129.658 176.253 1.00 22.89  ? 3889 ARG A CZ    1 
ATOM   18346 N NH1   . ARG A 1 3889 ? 174.738 129.866 177.516 1.00 22.89  ? 3889 ARG A NH1   1 
ATOM   18347 N NH2   . ARG A 1 3889 ? 173.121 129.684 175.906 1.00 22.89  ? 3889 ARG A NH2   1 
ATOM   18348 N N     . ILE A 1 3890 ? 176.708 125.738 171.290 1.00 22.02  ? 3890 ILE A N     1 
ATOM   18349 C CA    . ILE A 1 3890 ? 175.951 125.168 170.176 1.00 22.02  ? 3890 ILE A CA    1 
ATOM   18350 C C     . ILE A 1 3890 ? 176.107 123.652 170.149 1.00 22.02  ? 3890 ILE A C     1 
ATOM   18351 O O     . ILE A 1 3890 ? 175.133 122.909 169.969 1.00 22.02  ? 3890 ILE A O     1 
ATOM   18352 C CB    . ILE A 1 3890 ? 176.394 125.806 168.847 1.00 22.02  ? 3890 ILE A CB    1 
ATOM   18353 C CG1   . ILE A 1 3890 ? 175.897 127.249 168.759 1.00 22.02  ? 3890 ILE A CG1   1 
ATOM   18354 C CG2   . ILE A 1 3890 ? 175.888 124.994 167.669 1.00 22.02  ? 3890 ILE A CG2   1 
ATOM   18355 C CD1   . ILE A 1 3890 ? 176.252 127.937 167.463 1.00 22.02  ? 3890 ILE A CD1   1 
ATOM   18356 N N     . LYS A 1 3891 ? 177.338 123.172 170.334 1.00 23.31  ? 3891 LYS A N     1 
ATOM   18357 C CA    . LYS A 1 3891 ? 177.586 121.734 170.361 1.00 23.31  ? 3891 LYS A CA    1 
ATOM   18358 C C     . LYS A 1 3891 ? 176.860 121.070 171.523 1.00 23.31  ? 3891 LYS A C     1 
ATOM   18359 O O     . LYS A 1 3891 ? 176.304 119.976 171.375 1.00 23.31  ? 3891 LYS A O     1 
ATOM   18360 C CB    . LYS A 1 3891 ? 179.087 121.472 170.450 1.00 23.31  ? 3891 LYS A CB    1 
ATOM   18361 C CG    . LYS A 1 3891 ? 179.485 120.009 170.405 1.00 23.31  ? 3891 LYS A CG    1 
ATOM   18362 C CD    . LYS A 1 3891 ? 179.253 119.415 169.030 1.00 23.31  ? 3891 LYS A CD    1 
ATOM   18363 C CE    . LYS A 1 3891 ? 179.721 117.972 168.974 1.00 23.31  ? 3891 LYS A CE    1 
ATOM   18364 N NZ    . LYS A 1 3891 ? 181.197 117.868 169.139 1.00 23.31  ? 3891 LYS A NZ    1 
ATOM   18365 N N     . LEU A 1 3892 ? 176.864 121.714 172.693 1.00 27.93  ? 3892 LEU A N     1 
ATOM   18366 C CA    . LEU A 1 3892 ? 176.170 121.158 173.850 1.00 27.93  ? 3892 LEU A CA    1 
ATOM   18367 C C     . LEU A 1 3892 ? 174.669 121.078 173.611 1.00 27.93  ? 3892 LEU A C     1 
ATOM   18368 O O     . LEU A 1 3892 ? 174.023 120.099 174.000 1.00 27.93  ? 3892 LEU A O     1 
ATOM   18369 C CB    . LEU A 1 3892 ? 176.472 121.993 175.093 1.00 27.93  ? 3892 LEU A CB    1 
ATOM   18370 C CG    . LEU A 1 3892 ? 176.359 121.236 176.413 1.00 27.93  ? 3892 LEU A CG    1 
ATOM   18371 C CD1   . LEU A 1 3892 ? 177.247 120.009 176.388 1.00 27.93  ? 3892 LEU A CD1   1 
ATOM   18372 C CD2   . LEU A 1 3892 ? 176.723 122.141 177.577 1.00 27.93  ? 3892 LEU A CD2   1 
ATOM   18373 N N     . LYS A 1 3893 ? 174.092 122.106 172.986 1.00 25.60  ? 3893 LYS A N     1 
ATOM   18374 C CA    . LYS A 1 3893 ? 172.679 122.040 172.633 1.00 25.60  ? 3893 LYS A CA    1 
ATOM   18375 C C     . LYS A 1 3893 ? 172.410 120.927 171.630 1.00 25.60  ? 3893 LYS A C     1 
ATOM   18376 O O     . LYS A 1 3893 ? 171.390 120.236 171.728 1.00 25.60  ? 3893 LYS A O     1 
ATOM   18377 C CB    . LYS A 1 3893 ? 172.205 123.382 172.077 1.00 25.60  ? 3893 LYS A CB    1 
ATOM   18378 C CG    . LYS A 1 3893 ? 172.181 124.507 173.099 1.00 25.60  ? 3893 LYS A CG    1 
ATOM   18379 C CD    . LYS A 1 3893 ? 172.065 125.878 172.439 1.00 25.60  ? 3893 LYS A CD    1 
ATOM   18380 C CE    . LYS A 1 3893 ? 171.435 125.795 171.054 1.00 25.60  ? 3893 LYS A CE    1 
ATOM   18381 N NZ    . LYS A 1 3893 ? 171.391 127.122 170.382 1.00 25.60  ? 3893 LYS A NZ    1 
ATOM   18382 N N     . GLY A 1 3894 ? 173.310 120.736 170.663 1.00 29.32  ? 3894 GLY A N     1 
ATOM   18383 C CA    . GLY A 1 3894 ? 173.103 119.705 169.662 1.00 29.32  ? 3894 GLY A CA    1 
ATOM   18384 C C     . GLY A 1 3894 ? 173.377 118.297 170.144 1.00 29.32  ? 3894 GLY A C     1 
ATOM   18385 O O     . GLY A 1 3894 ? 172.776 117.344 169.640 1.00 29.32  ? 3894 GLY A O     1 
ATOM   18386 N N     . THR A 1 3895 ? 174.274 118.137 171.113 1.00 34.29  ? 3895 THR A N     1 
ATOM   18387 C CA    . THR A 1 3895 ? 174.634 116.805 171.575 1.00 34.29  ? 3895 THR A CA    1 
ATOM   18388 C C     . THR A 1 3895 ? 173.501 116.195 172.398 1.00 34.29  ? 3895 THR A C     1 
ATOM   18389 O O     . THR A 1 3895 ? 172.637 116.891 172.938 1.00 34.29  ? 3895 THR A O     1 
ATOM   18390 C CB    . THR A 1 3895 ? 175.924 116.843 172.397 1.00 34.29  ? 3895 THR A CB    1 
ATOM   18391 O OG1   . THR A 1 3895 ? 176.477 115.524 172.480 1.00 34.29  ? 3895 THR A OG1   1 
ATOM   18392 C CG2   . THR A 1 3895 ? 175.654 117.354 173.802 1.00 34.29  ? 3895 THR A CG2   1 
ATOM   18393 N N     . VAL A 1 3896 ? 173.511 114.867 172.478 1.00 44.96  ? 3896 VAL A N     1 
ATOM   18394 C CA    . VAL A 1 3896 ? 172.486 114.119 173.190 1.00 44.96  ? 3896 VAL A CA    1 
ATOM   18395 C C     . VAL A 1 3896 ? 173.110 113.458 174.411 1.00 44.96  ? 3896 VAL A C     1 
ATOM   18396 O O     . VAL A 1 3896 ? 174.329 113.286 174.509 1.00 44.96  ? 3896 VAL A O     1 
ATOM   18397 C CB    . VAL A 1 3896 ? 171.805 113.069 172.289 1.00 44.96  ? 3896 VAL A CB    1 
ATOM   18398 C CG1   . VAL A 1 3896 ? 170.969 113.749 171.217 1.00 44.96  ? 3896 VAL A CG1   1 
ATOM   18399 C CG2   . VAL A 1 3896 ? 172.846 112.155 171.663 1.00 44.96  ? 3896 VAL A CG2   1 
ATOM   18400 N N     . GLY A 1 3897 ? 172.251 113.081 175.354 1.00 58.10  ? 3897 GLY A N     1 
ATOM   18401 C CA    . GLY A 1 3897 ? 172.702 112.460 176.580 1.00 58.10  ? 3897 GLY A CA    1 
ATOM   18402 C C     . GLY A 1 3897 ? 173.280 113.407 177.605 1.00 58.10  ? 3897 GLY A C     1 
ATOM   18403 O O     . GLY A 1 3897 ? 173.894 112.945 178.573 1.00 58.10  ? 3897 GLY A O     1 
ATOM   18404 N N     . GLU A 1 3898 ? 173.103 114.712 177.429 1.00 57.74  ? 3898 GLU A N     1 
ATOM   18405 C CA    . GLU A 1 3898 ? 173.629 115.707 178.347 1.00 57.74  ? 3898 GLU A CA    1 
ATOM   18406 C C     . GLU A 1 3898 ? 172.524 116.662 178.768 1.00 57.74  ? 3898 GLU A C     1 
ATOM   18407 O O     . GLU A 1 3898 ? 171.642 116.991 177.969 1.00 57.74  ? 3898 GLU A O     1 
ATOM   18408 C CB    . GLU A 1 3898 ? 174.772 116.506 177.704 1.00 57.74  ? 3898 GLU A CB    1 
ATOM   18409 C CG    . GLU A 1 3898 ? 175.938 115.657 177.231 1.00 57.74  ? 3898 GLU A CG    1 
ATOM   18410 C CD    . GLU A 1 3898 ? 177.043 115.567 178.262 1.00 57.74  ? 3898 GLU A CD    1 
ATOM   18411 O OE1   . GLU A 1 3898 ? 176.956 116.274 179.287 1.00 57.74  ? 3898 GLU A OE1   1 
ATOM   18412 O OE2   . GLU A 1 3898 ? 177.997 114.790 178.048 1.00 57.74  ? 3898 GLU A OE2   1 
ATOM   18413 N N     . PRO A 1 3899 ? 172.546 117.120 180.017 1.00 58.13  ? 3899 PRO A N     1 
ATOM   18414 C CA    . PRO A 1 3899 ? 171.566 118.120 180.448 1.00 58.13  ? 3899 PRO A CA    1 
ATOM   18415 C C     . PRO A 1 3899 ? 171.778 119.441 179.729 1.00 58.13  ? 3899 PRO A C     1 
ATOM   18416 O O     . PRO A 1 3899 ? 172.886 119.774 179.303 1.00 58.13  ? 3899 PRO A O     1 
ATOM   18417 C CB    . PRO A 1 3899 ? 171.830 118.257 181.954 1.00 58.13  ? 3899 PRO A CB    1 
ATOM   18418 C CG    . PRO A 1 3899 ? 172.612 117.037 182.330 1.00 58.13  ? 3899 PRO A CG    1 
ATOM   18419 C CD    . PRO A 1 3899 ? 173.415 116.683 181.120 1.00 58.13  ? 3899 PRO A CD    1 
ATOM   18420 N N     . THR A 1 3900 ? 170.687 120.197 179.591 1.00 57.84  ? 3900 THR A N     1 
ATOM   18421 C CA    . THR A 1 3900 ? 170.762 121.493 178.928 1.00 57.84  ? 3900 THR A CA    1 
ATOM   18422 C C     . THR A 1 3900 ? 171.614 122.493 179.700 1.00 57.84  ? 3900 THR A C     1 
ATOM   18423 O O     . THR A 1 3900 ? 172.164 123.416 179.089 1.00 57.84  ? 3900 THR A O     1 
ATOM   18424 C CB    . THR A 1 3900 ? 169.359 122.065 178.724 1.00 57.84  ? 3900 THR A CB    1 
ATOM   18425 O OG1   . THR A 1 3900 ? 168.712 122.214 179.994 1.00 57.84  ? 3900 THR A OG1   1 
ATOM   18426 C CG2   . THR A 1 3900 ? 168.532 121.139 177.845 1.00 57.84  ? 3900 THR A CG2   1 
ATOM   18427 N N     . TYR A 1 3901 ? 171.734 122.328 181.019 1.00 53.31  ? 3901 TYR A N     1 
ATOM   18428 C CA    . TYR A 1 3901 ? 172.491 123.245 181.873 1.00 53.31  ? 3901 TYR A CA    1 
ATOM   18429 C C     . TYR A 1 3901 ? 171.991 124.680 181.723 1.00 53.31  ? 3901 TYR A C     1 
ATOM   18430 O O     . TYR A 1 3901 ? 172.766 125.636 181.788 1.00 53.31  ? 3901 TYR A O     1 
ATOM   18431 C CB    . TYR A 1 3901 ? 173.993 123.164 181.585 1.00 53.31  ? 3901 TYR A CB    1 
ATOM   18432 C CG    . TYR A 1 3901 ? 174.586 121.786 181.761 1.00 53.31  ? 3901 TYR A CG    1 
ATOM   18433 C CD1   . TYR A 1 3901 ? 174.409 121.077 182.941 1.00 53.31  ? 3901 TYR A CD1   1 
ATOM   18434 C CD2   . TYR A 1 3901 ? 175.330 121.196 180.749 1.00 53.31  ? 3901 TYR A CD2   1 
ATOM   18435 C CE1   . TYR A 1 3901 ? 174.951 119.817 183.105 1.00 53.31  ? 3901 TYR A CE1   1 
ATOM   18436 C CE2   . TYR A 1 3901 ? 175.877 119.939 180.904 1.00 53.31  ? 3901 TYR A CE2   1 
ATOM   18437 C CZ    . TYR A 1 3901 ? 175.685 119.254 182.084 1.00 53.31  ? 3901 TYR A CZ    1 
ATOM   18438 O OH    . TYR A 1 3901 ? 176.228 118.000 182.242 1.00 53.31  ? 3901 TYR A OH    1 
ATOM   18439 N N     . ASP A 1 3902 ? 170.680 124.831 181.520 1.00 57.54  ? 3902 ASP A N     1 
ATOM   18440 C CA    . ASP A 1 3902 ? 170.113 126.159 181.309 1.00 57.54  ? 3902 ASP A CA    1 
ATOM   18441 C C     . ASP A 1 3902 ? 170.304 127.045 182.534 1.00 57.54  ? 3902 ASP A C     1 
ATOM   18442 O O     . ASP A 1 3902 ? 170.691 128.213 182.406 1.00 57.54  ? 3902 ASP A O     1 
ATOM   18443 C CB    . ASP A 1 3902 ? 168.631 126.044 180.954 1.00 57.54  ? 3902 ASP A CB    1 
ATOM   18444 C CG    . ASP A 1 3902 ? 168.094 127.288 180.272 1.00 57.54  ? 3902 ASP A CG    1 
ATOM   18445 O OD1   . ASP A 1 3902 ? 168.817 128.306 180.227 1.00 57.54  ? 3902 ASP A OD1   1 
ATOM   18446 O OD2   . ASP A 1 3902 ? 166.946 127.249 179.782 1.00 57.54  ? 3902 ASP A OD2   1 
ATOM   18447 N N     . ALA A 1 3903 ? 170.044 126.508 183.727 1.00 51.44  ? 3903 ALA A N     1 
ATOM   18448 C CA    . ALA A 1 3903 ? 170.214 127.293 184.945 1.00 51.44  ? 3903 ALA A CA    1 
ATOM   18449 C C     . ALA A 1 3903 ? 171.674 127.671 185.156 1.00 51.44  ? 3903 ALA A C     1 
ATOM   18450 O O     . ALA A 1 3903 ? 171.985 128.810 185.522 1.00 51.44  ? 3903 ALA A O     1 
ATOM   18451 C CB    . ALA A 1 3903 ? 169.676 126.519 186.147 1.00 51.44  ? 3903 ALA A CB    1 
ATOM   18452 N N     . GLU A 1 3904 ? 172.587 126.724 184.924 1.00 47.93  ? 3904 GLU A N     1 
ATOM   18453 C CA    . GLU A 1 3904 ? 174.006 126.999 185.127 1.00 47.93  ? 3904 GLU A CA    1 
ATOM   18454 C C     . GLU A 1 3904 ? 174.506 128.076 184.172 1.00 47.93  ? 3904 GLU A C     1 
ATOM   18455 O O     . GLU A 1 3904 ? 175.193 129.014 184.590 1.00 47.93  ? 3904 GLU A O     1 
ATOM   18456 C CB    . GLU A 1 3904 ? 174.817 125.715 184.961 1.00 47.93  ? 3904 GLU A CB    1 
ATOM   18457 C CG    . GLU A 1 3904 ? 175.073 124.967 186.259 1.00 47.93  ? 3904 GLU A CG    1 
ATOM   18458 C CD    . GLU A 1 3904 ? 173.950 124.015 186.620 1.00 47.93  ? 3904 GLU A CD    1 
ATOM   18459 O OE1   . GLU A 1 3904 ? 172.903 124.040 185.940 1.00 47.93  ? 3904 GLU A OE1   1 
ATOM   18460 O OE2   . GLU A 1 3904 ? 174.115 123.240 187.586 1.00 47.93  ? 3904 GLU A OE2   1 
ATOM   18461 N N     . PHE A 1 3905 ? 174.164 127.964 182.886 1.00 43.52  ? 3905 PHE A N     1 
ATOM   18462 C CA    . PHE A 1 3905 ? 174.582 128.979 181.924 1.00 43.52  ? 3905 PHE A CA    1 
ATOM   18463 C C     . PHE A 1 3905 ? 173.937 130.327 182.218 1.00 43.52  ? 3905 PHE A C     1 
ATOM   18464 O O     . PHE A 1 3905 ? 174.583 131.371 182.073 1.00 43.52  ? 3905 PHE A O     1 
ATOM   18465 C CB    . PHE A 1 3905 ? 174.258 128.534 180.499 1.00 43.52  ? 3905 PHE A CB    1 
ATOM   18466 C CG    . PHE A 1 3905 ? 175.260 127.578 179.918 1.00 43.52  ? 3905 PHE A CG    1 
ATOM   18467 C CD1   . PHE A 1 3905 ? 176.531 128.011 179.585 1.00 43.52  ? 3905 PHE A CD1   1 
ATOM   18468 C CD2   . PHE A 1 3905 ? 174.927 126.256 179.686 1.00 43.52  ? 3905 PHE A CD2   1 
ATOM   18469 C CE1   . PHE A 1 3905 ? 177.455 127.139 179.046 1.00 43.52  ? 3905 PHE A CE1   1 
ATOM   18470 C CE2   . PHE A 1 3905 ? 175.848 125.379 179.146 1.00 43.52  ? 3905 PHE A CE2   1 
ATOM   18471 C CZ    . PHE A 1 3905 ? 177.112 125.822 178.825 1.00 43.52  ? 3905 PHE A CZ    1 
ATOM   18472 N N     . GLN A 1 3906 ? 172.664 130.331 182.618 1.00 47.45  ? 3906 GLN A N     1 
ATOM   18473 C CA    . GLN A 1 3906 ? 171.998 131.593 182.922 1.00 47.45  ? 3906 GLN A CA    1 
ATOM   18474 C C     . GLN A 1 3906 ? 172.639 132.278 184.121 1.00 47.45  ? 3906 GLN A C     1 
ATOM   18475 O O     . GLN A 1 3906 ? 172.786 133.506 184.138 1.00 47.45  ? 3906 GLN A O     1 
ATOM   18476 C CB    . GLN A 1 3906 ? 170.508 131.360 183.166 1.00 47.45  ? 3906 GLN A CB    1 
ATOM   18477 C CG    . GLN A 1 3906 ? 169.679 132.632 183.134 1.00 47.45  ? 3906 GLN A CG    1 
ATOM   18478 C CD    . GLN A 1 3906 ? 168.203 132.360 182.931 1.00 47.45  ? 3906 GLN A CD    1 
ATOM   18479 O OE1   . GLN A 1 3906 ? 167.822 131.494 182.145 1.00 47.45  ? 3906 GLN A OE1   1 
ATOM   18480 N NE2   . GLN A 1 3906 ? 167.363 133.104 183.640 1.00 47.45  ? 3906 GLN A NE2   1 
ATOM   18481 N N     . HIS A 1 3907 ? 173.022 131.504 185.139 1.00 48.32  ? 3907 HIS A N     1 
ATOM   18482 C CA    . HIS A 1 3907 ? 173.742 132.084 186.268 1.00 48.32  ? 3907 HIS A CA    1 
ATOM   18483 C C     . HIS A 1 3907 ? 175.123 132.570 185.850 1.00 48.32  ? 3907 HIS A C     1 
ATOM   18484 O O     . HIS A 1 3907 ? 175.589 133.614 186.322 1.00 48.32  ? 3907 HIS A O     1 
ATOM   18485 C CB    . HIS A 1 3907 ? 173.855 131.070 187.403 1.00 48.32  ? 3907 HIS A CB    1 
ATOM   18486 C CG    . HIS A 1 3907 ? 174.584 131.591 188.602 1.00 48.32  ? 3907 HIS A CG    1 
ATOM   18487 N ND1   . HIS A 1 3907 ? 174.132 132.664 189.339 1.00 48.32  ? 3907 HIS A ND1   1 
ATOM   18488 C CD2   . HIS A 1 3907 ? 175.736 131.190 189.189 1.00 48.32  ? 3907 HIS A CD2   1 
ATOM   18489 C CE1   . HIS A 1 3907 ? 174.972 132.900 190.330 1.00 48.32  ? 3907 HIS A CE1   1 
ATOM   18490 N NE2   . HIS A 1 3907 ? 175.955 132.020 190.262 1.00 48.32  ? 3907 HIS A NE2   1 
ATOM   18491 N N     . PHE A 1 3908 ? 175.795 131.820 184.974 1.00 36.59  ? 3908 PHE A N     1 
ATOM   18492 C CA    . PHE A 1 3908 ? 177.126 132.211 184.522 1.00 36.59  ? 3908 PHE A CA    1 
ATOM   18493 C C     . PHE A 1 3908 ? 177.089 133.528 183.759 1.00 36.59  ? 3908 PHE A C     1 
ATOM   18494 O O     . PHE A 1 3908 ? 177.951 134.392 183.956 1.00 36.59  ? 3908 PHE A O     1 
ATOM   18495 C CB    . PHE A 1 3908 ? 177.718 131.104 183.651 1.00 36.59  ? 3908 PHE A CB    1 
ATOM   18496 C CG    . PHE A 1 3908 ? 179.119 131.375 183.190 1.00 36.59  ? 3908 PHE A CG    1 
ATOM   18497 C CD1   . PHE A 1 3908 ? 180.139 131.561 184.105 1.00 36.59  ? 3908 PHE A CD1   1 
ATOM   18498 C CD2   . PHE A 1 3908 ? 179.418 131.433 181.840 1.00 36.59  ? 3908 PHE A CD2   1 
ATOM   18499 C CE1   . PHE A 1 3908 ? 181.429 131.807 183.682 1.00 36.59  ? 3908 PHE A CE1   1 
ATOM   18500 C CE2   . PHE A 1 3908 ? 180.705 131.677 181.412 1.00 36.59  ? 3908 PHE A CE2   1 
ATOM   18501 C CZ    . PHE A 1 3908 ? 181.713 131.864 182.334 1.00 36.59  ? 3908 PHE A CZ    1 
ATOM   18502 N N     . LEU A 1 3909 ? 176.095 133.704 182.890 1.00 35.35  ? 3909 LEU A N     1 
ATOM   18503 C CA    . LEU A 1 3909 ? 176.060 134.883 182.033 1.00 35.35  ? 3909 LEU A CA    1 
ATOM   18504 C C     . LEU A 1 3909 ? 175.404 136.070 182.729 1.00 35.35  ? 3909 LEU A C     1 
ATOM   18505 O O     . LEU A 1 3909 ? 176.035 137.117 182.910 1.00 35.35  ? 3909 LEU A O     1 
ATOM   18506 C CB    . LEU A 1 3909 ? 175.331 134.559 180.728 1.00 35.35  ? 3909 LEU A CB    1 
ATOM   18507 C CG    . LEU A 1 3909 ? 176.170 134.028 179.564 1.00 35.35  ? 3909 LEU A CG    1 
ATOM   18508 C CD1   . LEU A 1 3909 ? 176.693 132.632 179.852 1.00 35.35  ? 3909 LEU A CD1   1 
ATOM   18509 C CD2   . LEU A 1 3909 ? 175.358 134.041 178.280 1.00 35.35  ? 3909 LEU A CD2   1 
ATOM   18510 N N     . ARG A 1 3910 ? 174.146 135.928 183.130 1.00 46.84  ? 3910 ARG A N     1 
ATOM   18511 C CA    . ARG A 1 3910 ? 173.380 137.042 183.677 1.00 46.84  ? 3910 ARG A CA    1 
ATOM   18512 C C     . ARG A 1 3910 ? 172.956 136.842 185.121 1.00 46.84  ? 3910 ARG A C     1 
ATOM   18513 O O     . ARG A 1 3910 ? 172.629 137.818 185.800 1.00 46.84  ? 3910 ARG A O     1 
ATOM   18514 C CB    . ARG A 1 3910 ? 172.135 137.296 182.816 1.00 46.84  ? 3910 ARG A CB    1 
ATOM   18515 C CG    . ARG A 1 3910 ? 170.952 136.408 183.151 1.00 46.84  ? 3910 ARG A CG    1 
ATOM   18516 C CD    . ARG A 1 3910 ? 169.654 136.984 182.612 1.00 46.84  ? 3910 ARG A CD    1 
ATOM   18517 N NE    . ARG A 1 3910 ? 169.743 137.312 181.194 1.00 46.84  ? 3910 ARG A NE    1 
ATOM   18518 C CZ    . ARG A 1 3910 ? 169.746 138.546 180.709 1.00 46.84  ? 3910 ARG A CZ    1 
ATOM   18519 N NH1   . ARG A 1 3910 ? 169.668 139.601 181.503 1.00 46.84  ? 3910 ARG A NH1   1 
ATOM   18520 N NH2   . ARG A 1 3910 ? 169.828 138.726 179.394 1.00 46.84  ? 3910 ARG A NH2   1 
ATOM   18521 N N     . GLY A 1 3911 ? 172.950 135.605 185.614 1.00 54.62  ? 3911 GLY A N     1 
ATOM   18522 C CA    . GLY A 1 3911 ? 172.498 135.356 186.970 1.00 54.62  ? 3911 GLY A CA    1 
ATOM   18523 C C     . GLY A 1 3911 ? 173.460 135.801 188.049 1.00 54.62  ? 3911 GLY A C     1 
ATOM   18524 O O     . GLY A 1 3911 ? 173.058 135.881 189.214 1.00 54.62  ? 3911 GLY A O     1 
ATOM   18525 N N     . ASN A 1 3912 ? 174.714 136.089 187.694 1.00 61.44  ? 3912 ASN A N     1 
ATOM   18526 C CA    . ASN A 1 3912 ? 175.676 136.550 188.686 1.00 61.44  ? 3912 ASN A CA    1 
ATOM   18527 C C     . ASN A 1 3912 ? 175.307 137.915 189.249 1.00 61.44  ? 3912 ASN A C     1 
ATOM   18528 O O     . ASN A 1 3912 ? 175.734 138.253 190.357 1.00 61.44  ? 3912 ASN A O     1 
ATOM   18529 C CB    . ASN A 1 3912 ? 177.079 136.591 188.075 1.00 61.44  ? 3912 ASN A CB    1 
ATOM   18530 C CG    . ASN A 1 3912 ? 178.129 137.083 189.053 1.00 61.44  ? 3912 ASN A CG    1 
ATOM   18531 O OD1   . ASN A 1 3912 ? 178.358 136.469 190.095 1.00 61.44  ? 3912 ASN A OD1   1 
ATOM   18532 N ND2   . ASN A 1 3912 ? 178.774 138.195 188.721 1.00 61.44  ? 3912 ASN A ND2   1 
ATOM   18533 N N     . GLU A 1 3913 ? 174.524 138.706 188.514 1.00 63.38  ? 3913 GLU A N     1 
ATOM   18534 C CA    . GLU A 1 3913 ? 174.095 140.025 188.974 1.00 63.38  ? 3913 GLU A CA    1 
ATOM   18535 C C     . GLU A 1 3913 ? 172.642 139.936 189.434 1.00 63.38  ? 3913 GLU A C     1 
ATOM   18536 O O     . GLU A 1 3913 ? 171.703 140.256 188.706 1.00 63.38  ? 3913 GLU A O     1 
ATOM   18537 C CB    . GLU A 1 3913 ? 174.286 141.064 187.874 1.00 63.38  ? 3913 GLU A CB    1 
ATOM   18538 C CG    . GLU A 1 3913 ? 175.743 141.358 187.549 1.00 63.38  ? 3913 GLU A CG    1 
ATOM   18539 C CD    . GLU A 1 3913 ? 176.351 140.345 186.598 1.00 63.38  ? 3913 GLU A CD    1 
ATOM   18540 O OE1   . GLU A 1 3913 ? 175.615 139.459 186.118 1.00 63.38  ? 3913 GLU A OE1   1 
ATOM   18541 O OE2   . GLU A 1 3913 ? 177.568 140.434 186.334 1.00 63.38  ? 3913 GLU A OE2   1 
ATOM   18542 N N     . ILE A 1 3914 ? 172.467 139.490 190.679 1.00 66.64  ? 3914 ILE A N     1 
ATOM   18543 C CA    . ILE A 1 3914 ? 171.166 139.429 191.329 1.00 66.64  ? 3914 ILE A CA    1 
ATOM   18544 C C     . ILE A 1 3914 ? 171.336 139.955 192.749 1.00 66.64  ? 3914 ILE A C     1 
ATOM   18545 O O     . ILE A 1 3914 ? 172.406 139.850 193.350 1.00 66.64  ? 3914 ILE A O     1 
ATOM   18546 C CB    . ILE A 1 3914 ? 170.577 137.997 191.324 1.00 66.64  ? 3914 ILE A CB    1 
ATOM   18547 C CG1   . ILE A 1 3914 ? 169.170 137.972 191.927 1.00 66.64  ? 3914 ILE A CG1   1 
ATOM   18548 C CG2   . ILE A 1 3914 ? 171.489 137.034 192.063 1.00 66.64  ? 3914 ILE A CG2   1 
ATOM   18549 C CD1   . ILE A 1 3914 ? 168.151 138.755 191.130 1.00 66.64  ? 3914 ILE A CD1   1 
ATOM   18550 N N     . VAL A 1 3915 ? 170.265 140.542 193.280 1.00 72.16  ? 3915 VAL A N     1 
ATOM   18551 C CA    . VAL A 1 3915 ? 170.317 141.202 194.585 1.00 72.16  ? 3915 VAL A CA    1 
ATOM   18552 C C     . VAL A 1 3915 ? 170.415 140.128 195.671 1.00 72.16  ? 3915 VAL A C     1 
ATOM   18553 O O     . VAL A 1 3915 ? 169.448 139.434 195.991 1.00 72.16  ? 3915 VAL A O     1 
ATOM   18554 C CB    . VAL A 1 3915 ? 169.133 142.154 194.794 1.00 72.16  ? 3915 VAL A CB    1 
ATOM   18555 C CG1   . VAL A 1 3915 ? 167.783 141.431 194.771 1.00 72.16  ? 3915 VAL A CG1   1 
ATOM   18556 C CG2   . VAL A 1 3915 ? 169.301 142.923 196.097 1.00 72.16  ? 3915 VAL A CG2   1 
ATOM   18557 N N     . LEU A 1 3916 ? 171.625 139.957 196.211 1.00 72.78  ? 3916 LEU A N     1 
ATOM   18558 C CA    . LEU A 1 3916 ? 171.861 139.071 197.345 1.00 72.78  ? 3916 LEU A CA    1 
ATOM   18559 C C     . LEU A 1 3916 ? 172.883 139.665 198.306 1.00 72.78  ? 3916 LEU A C     1 
ATOM   18560 O O     . LEU A 1 3916 ? 173.626 138.927 198.962 1.00 72.78  ? 3916 LEU A O     1 
ATOM   18561 C CB    . LEU A 1 3916 ? 172.321 137.686 196.882 1.00 72.78  ? 3916 LEU A CB    1 
ATOM   18562 C CG    . LEU A 1 3916 ? 171.223 136.673 196.553 1.00 72.78  ? 3916 LEU A CG    1 
ATOM   18563 C CD1   . LEU A 1 3916 ? 171.822 135.303 196.275 1.00 72.78  ? 3916 LEU A CD1   1 
ATOM   18564 C CD2   . LEU A 1 3916 ? 170.208 136.597 197.681 1.00 72.78  ? 3916 LEU A CD2   1 
ATOM   18565 N N     . SER A 1 3917 ? 172.940 140.996 198.397 1.00 77.85  ? 3917 SER A N     1 
ATOM   18566 C CA    . SER A 1 3917 ? 173.951 141.638 199.232 1.00 77.85  ? 3917 SER A CA    1 
ATOM   18567 C C     . SER A 1 3917 ? 173.656 141.467 200.716 1.00 77.85  ? 3917 SER A C     1 
ATOM   18568 O O     . SER A 1 3917 ? 174.581 141.501 201.536 1.00 77.85  ? 3917 SER A O     1 
ATOM   18569 C CB    . SER A 1 3917 ? 174.055 143.122 198.881 1.00 77.85  ? 3917 SER A CB    1 
ATOM   18570 O OG    . SER A 1 3917 ? 172.835 143.795 199.139 1.00 77.85  ? 3917 SER A OG    1 
ATOM   18571 N N     . ALA A 1 3918 ? 172.389 141.290 201.080 1.00 73.72  ? 3918 ALA A N     1 
ATOM   18572 C CA    . ALA A 1 3918 ? 172.024 141.150 202.483 1.00 73.72  ? 3918 ALA A CA    1 
ATOM   18573 C C     . ALA A 1 3918 ? 172.581 139.854 203.061 1.00 73.72  ? 3918 ALA A C     1 
ATOM   18574 O O     . ALA A 1 3918 ? 172.561 138.804 202.413 1.00 73.72  ? 3918 ALA A O     1 
ATOM   18575 C CB    . ALA A 1 3918 ? 170.505 141.186 202.642 1.00 73.72  ? 3918 ALA A CB    1 
ATOM   18576 N N     . GLY A 1 3919 ? 173.078 139.935 204.291 1.00 71.10  ? 3919 GLY A N     1 
ATOM   18577 C CA    . GLY A 1 3919 ? 173.625 138.770 204.963 1.00 71.10  ? 3919 GLY A CA    1 
ATOM   18578 C C     . GLY A 1 3919 ? 174.883 138.212 204.333 1.00 71.10  ? 3919 GLY A C     1 
ATOM   18579 O O     . GLY A 1 3919 ? 175.019 136.988 204.210 1.00 71.10  ? 3919 GLY A O     1 
ATOM   18580 N N     . SER A 1 3920 ? 175.809 139.079 203.928 1.00 71.81  ? 3920 SER A N     1 
ATOM   18581 C CA    . SER A 1 3920 ? 177.072 138.648 203.330 1.00 71.81  ? 3920 SER A CA    1 
ATOM   18582 C C     . SER A 1 3920 ? 178.094 138.486 204.448 1.00 71.81  ? 3920 SER A C     1 
ATOM   18583 O O     . SER A 1 3920 ? 178.832 139.412 204.786 1.00 71.81  ? 3920 SER A O     1 
ATOM   18584 C CB    . SER A 1 3920 ? 177.539 139.644 202.276 1.00 71.81  ? 3920 SER A CB    1 
ATOM   18585 O OG    . SER A 1 3920 ? 177.683 140.940 202.830 1.00 71.81  ? 3920 SER A OG    1 
ATOM   18586 N N     . THR A 1 3921 ? 178.134 137.291 205.030 1.00 76.61  ? 3921 THR A N     1 
ATOM   18587 C CA    . THR A 1 3921 ? 179.057 137.023 206.118 1.00 76.61  ? 3921 THR A CA    1 
ATOM   18588 C C     . THR A 1 3921 ? 180.496 136.998 205.602 1.00 76.61  ? 3921 THR A C     1 
ATOM   18589 O O     . THR A 1 3921 ? 180.741 136.680 204.436 1.00 76.61  ? 3921 THR A O     1 
ATOM   18590 C CB    . THR A 1 3921 ? 178.725 135.692 206.789 1.00 76.61  ? 3921 THR A CB    1 
ATOM   18591 O OG1   . THR A 1 3921 ? 178.854 134.630 205.837 1.00 76.61  ? 3921 THR A OG1   1 
ATOM   18592 C CG2   . THR A 1 3921 ? 177.303 135.711 207.329 1.00 76.61  ? 3921 THR A CG2   1 
ATOM   18593 N N     . PRO A 1 3922 ? 181.468 137.340 206.452 1.00 76.68  ? 3922 PRO A N     1 
ATOM   18594 C CA    . PRO A 1 3922 ? 182.873 137.307 206.010 1.00 76.68  ? 3922 PRO A CA    1 
ATOM   18595 C C     . PRO A 1 3922 ? 183.372 135.916 205.660 1.00 76.68  ? 3922 PRO A C     1 
ATOM   18596 O O     . PRO A 1 3922 ? 184.419 135.801 205.009 1.00 76.68  ? 3922 PRO A O     1 
ATOM   18597 C CB    . PRO A 1 3922 ? 183.634 137.891 207.209 1.00 76.68  ? 3922 PRO A CB    1 
ATOM   18598 C CG    . PRO A 1 3922 ? 182.722 137.692 208.376 1.00 76.68  ? 3922 PRO A CG    1 
ATOM   18599 C CD    . PRO A 1 3922 ? 181.336 137.842 207.831 1.00 76.68  ? 3922 PRO A CD    1 
ATOM   18600 N N     . ARG A 1 3923 ? 182.668 134.862 206.079 1.00 78.59  ? 3923 ARG A N     1 
ATOM   18601 C CA    . ARG A 1 3923 ? 183.047 133.469 205.816 1.00 78.59  ? 3923 ARG A CA    1 
ATOM   18602 C C     . ARG A 1 3923 ? 184.398 133.224 206.477 1.00 78.59  ? 3923 ARG A C     1 
ATOM   18603 O O     . ARG A 1 3923 ? 184.504 133.404 207.702 1.00 78.59  ? 3923 ARG A O     1 
ATOM   18604 C CB    . ARG A 1 3923 ? 182.983 133.200 204.310 1.00 78.59  ? 3923 ARG A CB    1 
ATOM   18605 C CG    . ARG A 1 3923 ? 181.676 133.611 203.654 1.00 78.59  ? 3923 ARG A CG    1 
ATOM   18606 C CD    . ARG A 1 3923 ? 180.596 132.562 203.867 1.00 78.59  ? 3923 ARG A CD    1 
ATOM   18607 N NE    . ARG A 1 3923 ? 179.271 133.156 204.007 1.00 78.59  ? 3923 ARG A NE    1 
ATOM   18608 C CZ    . ARG A 1 3923 ? 178.557 133.646 203.003 1.00 78.59  ? 3923 ARG A CZ    1 
ATOM   18609 N NH1   . ARG A 1 3923 ? 179.006 133.625 201.759 1.00 78.59  ? 3923 ARG A NH1   1 
ATOM   18610 N NH2   . ARG A 1 3923 ? 177.359 134.168 203.253 1.00 78.59  ? 3923 ARG A NH2   1 
ATOM   18611 N N     . ILE A 1 3924 ? 185.430 132.825 205.746 1.00 80.28  ? 3924 ILE A N     1 
ATOM   18612 C CA    . ILE A 1 3924 ? 186.736 132.586 206.320 1.00 80.28  ? 3924 ILE A CA    1 
ATOM   18613 C C     . ILE A 1 3924 ? 187.648 133.752 205.956 1.00 80.28  ? 3924 ILE A C     1 
ATOM   18614 O O     . ILE A 1 3924 ? 187.315 134.595 205.126 1.00 80.28  ? 3924 ILE A O     1 
ATOM   18615 C CB    . ILE A 1 3924 ? 187.325 131.228 205.858 1.00 80.28  ? 3924 ILE A CB    1 
ATOM   18616 C CG1   . ILE A 1 3924 ? 188.305 130.677 206.896 1.00 80.28  ? 3924 ILE A CG1   1 
ATOM   18617 C CG2   . ILE A 1 3924 ? 188.002 131.366 204.506 1.00 80.28  ? 3924 ILE A CG2   1 
ATOM   18618 C CD1   . ILE A 1 3924 ? 188.667 129.223 206.679 1.00 80.28  ? 3924 ILE A CD1   1 
ATOM   18619 N N     . GLN A 1 3925 ? 188.820 133.810 206.597 1.00 83.57  ? 3925 GLN A N     1 
ATOM   18620 C CA    . GLN A 1 3925 ? 189.749 134.909 206.354 1.00 83.57  ? 3925 GLN A CA    1 
ATOM   18621 C C     . GLN A 1 3925 ? 190.212 134.953 204.903 1.00 83.57  ? 3925 GLN A C     1 
ATOM   18622 O O     . GLN A 1 3925 ? 190.575 136.024 204.402 1.00 83.57  ? 3925 GLN A O     1 
ATOM   18623 C CB    . GLN A 1 3925 ? 190.953 134.796 207.292 1.00 83.57  ? 3925 GLN A CB    1 
ATOM   18624 C CG    . GLN A 1 3925 ? 191.784 133.537 207.098 1.00 83.57  ? 3925 GLN A CG    1 
ATOM   18625 C CD    . GLN A 1 3925 ? 191.275 132.368 207.919 1.00 83.57  ? 3925 GLN A CD    1 
ATOM   18626 O OE1   . GLN A 1 3925 ? 190.365 132.516 208.735 1.00 83.57  ? 3925 GLN A OE1   1 
ATOM   18627 N NE2   . GLN A 1 3925 ? 191.862 131.196 207.707 1.00 83.57  ? 3925 GLN A NE2   1 
ATOM   18628 N N     . GLY A 1 3926 ? 190.213 133.809 204.216 1.00 74.19  ? 3926 GLY A N     1 
ATOM   18629 C CA    . GLY A 1 3926 ? 190.581 133.805 202.810 1.00 74.19  ? 3926 GLY A CA    1 
ATOM   18630 C C     . GLY A 1 3926 ? 189.579 134.538 201.939 1.00 74.19  ? 3926 GLY A C     1 
ATOM   18631 O O     . GLY A 1 3926 ? 189.959 135.241 200.998 1.00 74.19  ? 3926 GLY A O     1 
ATOM   18632 N N     . LEU A 1 3927 ? 188.291 134.386 202.235 1.00 68.73  ? 3927 LEU A N     1 
ATOM   18633 C CA    . LEU A 1 3927 ? 187.257 135.038 201.445 1.00 68.73  ? 3927 LEU A CA    1 
ATOM   18634 C C     . LEU A 1 3927 ? 187.247 136.541 201.697 1.00 68.73  ? 3927 LEU A C     1 
ATOM   18635 O O     . LEU A 1 3927 ? 187.269 136.996 202.843 1.00 68.73  ? 3927 LEU A O     1 
ATOM   18636 C CB    . LEU A 1 3927 ? 185.881 134.453 201.770 1.00 68.73  ? 3927 LEU A CB    1 
ATOM   18637 C CG    . LEU A 1 3927 ? 185.420 133.158 201.091 1.00 68.73  ? 3927 LEU A CG    1 
ATOM   18638 C CD1   . LEU A 1 3927 ? 185.284 133.354 199.591 1.00 68.73  ? 3927 LEU A CD1   1 
ATOM   18639 C CD2   . LEU A 1 3927 ? 186.342 131.993 201.397 1.00 68.73  ? 3927 LEU A CD2   1 
ATOM   18640 N N     . THR A 1 3928 ? 187.216 137.311 200.614 1.00 66.24  ? 3928 THR A N     1 
ATOM   18641 C CA    . THR A 1 3928 ? 187.042 138.751 200.680 1.00 66.24  ? 3928 THR A CA    1 
ATOM   18642 C C     . THR A 1 3928 ? 185.559 139.088 200.543 1.00 66.24  ? 3928 THR A C     1 
ATOM   18643 O O     . THR A 1 3928 ? 184.706 138.207 200.410 1.00 66.24  ? 3928 THR A O     1 
ATOM   18644 C CB    . THR A 1 3928 ? 187.872 139.448 199.601 1.00 66.24  ? 3928 THR A CB    1 
ATOM   18645 O OG1   . THR A 1 3928 ? 187.427 139.024 198.308 1.00 66.24  ? 3928 THR A OG1   1 
ATOM   18646 C CG2   . THR A 1 3928 ? 189.346 139.109 199.762 1.00 66.24  ? 3928 THR A CG2   1 
ATOM   18647 N N     . VAL A 1 3929 ? 185.247 140.385 200.575 1.00 64.70  ? 3929 VAL A N     1 
ATOM   18648 C CA    . VAL A 1 3929 ? 183.848 140.801 200.540 1.00 64.70  ? 3929 VAL A CA    1 
ATOM   18649 C C     . VAL A 1 3929 ? 183.230 140.523 199.172 1.00 64.70  ? 3929 VAL A C     1 
ATOM   18650 O O     . VAL A 1 3929 ? 182.103 140.020 199.079 1.00 64.70  ? 3929 VAL A O     1 
ATOM   18651 C CB    . VAL A 1 3929 ? 183.714 142.280 200.958 1.00 64.70  ? 3929 VAL A CB    1 
ATOM   18652 C CG1   . VAL A 1 3929 ? 184.415 143.211 199.973 1.00 64.70  ? 3929 VAL A CG1   1 
ATOM   18653 C CG2   . VAL A 1 3929 ? 182.247 142.656 201.109 1.00 64.70  ? 3929 VAL A CG2   1 
ATOM   18654 N N     . GLU A 1 3930 ? 183.950 140.832 198.089 1.00 65.55  ? 3930 GLU A N     1 
ATOM   18655 C CA    . GLU A 1 3930 ? 183.438 140.514 196.760 1.00 65.55  ? 3930 GLU A CA    1 
ATOM   18656 C C     . GLU A 1 3930 ? 183.367 139.006 196.546 1.00 65.55  ? 3930 GLU A C     1 
ATOM   18657 O O     . GLU A 1 3930 ? 182.408 138.503 195.949 1.00 65.55  ? 3930 GLU A O     1 
ATOM   18658 C CB    . GLU A 1 3930 ? 184.287 141.196 195.682 1.00 65.55  ? 3930 GLU A CB    1 
ATOM   18659 C CG    . GLU A 1 3930 ? 185.705 140.666 195.518 1.00 65.55  ? 3930 GLU A CG    1 
ATOM   18660 C CD    . GLU A 1 3930 ? 186.686 141.302 196.487 1.00 65.55  ? 3930 GLU A CD    1 
ATOM   18661 O OE1   . GLU A 1 3930 ? 186.240 141.924 197.474 1.00 65.55  ? 3930 GLU A OE1   1 
ATOM   18662 O OE2   . GLU A 1 3930 ? 187.909 141.177 196.262 1.00 65.55  ? 3930 GLU A OE2   1 
ATOM   18663 N N     . GLN A 1 3931 ? 184.361 138.266 197.044 1.00 62.64  ? 3931 GLN A N     1 
ATOM   18664 C CA    . GLN A 1 3931 ? 184.293 136.810 196.979 1.00 62.64  ? 3931 GLN A CA    1 
ATOM   18665 C C     . GLN A 1 3931 ? 183.132 136.277 197.809 1.00 62.64  ? 3931 GLN A C     1 
ATOM   18666 O O     . GLN A 1 3931 ? 182.469 135.314 197.411 1.00 62.64  ? 3931 GLN A O     1 
ATOM   18667 C CB    . GLN A 1 3931 ? 185.614 136.196 197.440 1.00 62.64  ? 3931 GLN A CB    1 
ATOM   18668 C CG    . GLN A 1 3931 ? 186.782 136.453 196.503 1.00 62.64  ? 3931 GLN A CG    1 
ATOM   18669 C CD    . GLN A 1 3931 ? 188.076 135.837 197.000 1.00 62.64  ? 3931 GLN A CD    1 
ATOM   18670 O OE1   . GLN A 1 3931 ? 188.122 135.250 198.080 1.00 62.64  ? 3931 GLN A OE1   1 
ATOM   18671 N NE2   . GLN A 1 3931 ? 189.134 135.965 196.209 1.00 62.64  ? 3931 GLN A NE2   1 
ATOM   18672 N N     . ALA A 1 3932 ? 182.870 136.888 198.967 1.00 63.25  ? 3932 ALA A N     1 
ATOM   18673 C CA    . ALA A 1 3932 ? 181.737 136.461 199.783 1.00 63.25  ? 3932 ALA A CA    1 
ATOM   18674 C C     . ALA A 1 3932 ? 180.418 136.692 199.057 1.00 63.25  ? 3932 ALA A C     1 
ATOM   18675 O O     . ALA A 1 3932 ? 179.530 135.829 199.073 1.00 63.25  ? 3932 ALA A O     1 
ATOM   18676 C CB    . ALA A 1 3932 ? 181.747 137.192 201.125 1.00 63.25  ? 3932 ALA A CB    1 
ATOM   18677 N N     . GLU A 1 3933 ? 180.270 137.852 198.412 1.00 65.18  ? 3933 GLU A N     1 
ATOM   18678 C CA    . GLU A 1 3933 ? 179.059 138.108 197.639 1.00 65.18  ? 3933 GLU A CA    1 
ATOM   18679 C C     . GLU A 1 3933 ? 178.929 137.125 196.483 1.00 65.18  ? 3933 GLU A C     1 
ATOM   18680 O O     . GLU A 1 3933 ? 177.828 136.645 196.189 1.00 65.18  ? 3933 GLU A O     1 
ATOM   18681 C CB    . GLU A 1 3933 ? 179.050 139.547 197.126 1.00 65.18  ? 3933 GLU A CB    1 
ATOM   18682 C CG    . GLU A 1 3933 ? 178.924 140.594 198.219 1.00 65.18  ? 3933 GLU A CG    1 
ATOM   18683 C CD    . GLU A 1 3933 ? 178.936 142.009 197.673 1.00 65.18  ? 3933 GLU A CD    1 
ATOM   18684 O OE1   . GLU A 1 3933 ? 179.167 142.175 196.457 1.00 65.18  ? 3933 GLU A OE1   1 
ATOM   18685 O OE2   . GLU A 1 3933 ? 178.712 142.954 198.458 1.00 65.18  ? 3933 GLU A OE2   1 
ATOM   18686 N N     . ALA A 1 3934 ? 180.044 136.810 195.818 1.00 60.47  ? 3934 ALA A N     1 
ATOM   18687 C CA    . ALA A 1 3934 ? 180.004 135.830 194.737 1.00 60.47  ? 3934 ALA A CA    1 
ATOM   18688 C C     . ALA A 1 3934 ? 179.579 134.461 195.251 1.00 60.47  ? 3934 ALA A C     1 
ATOM   18689 O O     . ALA A 1 3934 ? 178.823 133.747 194.583 1.00 60.47  ? 3934 ALA A O     1 
ATOM   18690 C CB    . ALA A 1 3934 ? 181.367 135.749 194.051 1.00 60.47  ? 3934 ALA A CB    1 
ATOM   18691 N N     . VAL A 1 3935 ? 180.060 134.077 196.436 1.00 59.66  ? 3935 VAL A N     1 
ATOM   18692 C CA    . VAL A 1 3935 ? 179.654 132.809 197.037 1.00 59.66  ? 3935 VAL A CA    1 
ATOM   18693 C C     . VAL A 1 3935 ? 178.162 132.814 197.335 1.00 59.66  ? 3935 VAL A C     1 
ATOM   18694 O O     . VAL A 1 3935 ? 177.463 131.821 197.097 1.00 59.66  ? 3935 VAL A O     1 
ATOM   18695 C CB    . VAL A 1 3935 ? 180.479 132.530 198.306 1.00 59.66  ? 3935 VAL A CB    1 
ATOM   18696 C CG1   . VAL A 1 3935 ? 179.911 131.341 199.056 1.00 59.66  ? 3935 VAL A CG1   1 
ATOM   18697 C CG2   . VAL A 1 3935 ? 181.919 132.276 197.945 1.00 59.66  ? 3935 VAL A CG2   1 
ATOM   18698 N N     . VAL A 1 3936 ? 177.652 133.925 197.870 1.00 62.26  ? 3936 VAL A N     1 
ATOM   18699 C CA    . VAL A 1 3936 ? 176.221 134.019 198.152 1.00 62.26  ? 3936 VAL A CA    1 
ATOM   18700 C C     . VAL A 1 3936 ? 175.413 133.874 196.869 1.00 62.26  ? 3936 VAL A C     1 
ATOM   18701 O O     . VAL A 1 3936 ? 174.405 133.157 196.830 1.00 62.26  ? 3936 VAL A O     1 
ATOM   18702 C CB    . VAL A 1 3936 ? 175.900 135.340 198.875 1.00 62.26  ? 3936 VAL A CB    1 
ATOM   18703 C CG1   . VAL A 1 3936 ? 174.400 135.483 199.069 1.00 62.26  ? 3936 VAL A CG1   1 
ATOM   18704 C CG2   . VAL A 1 3936 ? 176.607 135.394 200.216 1.00 62.26  ? 3936 VAL A CG2   1 
ATOM   18705 N N     . ARG A 1 3937 ? 175.839 134.551 195.799 1.00 62.48  ? 3937 ARG A N     1 
ATOM   18706 C CA    . ARG A 1 3937 ? 175.125 134.452 194.529 1.00 62.48  ? 3937 ARG A CA    1 
ATOM   18707 C C     . ARG A 1 3937 ? 175.170 133.034 193.972 1.00 62.48  ? 3937 ARG A C     1 
ATOM   18708 O O     . ARG A 1 3937 ? 174.159 132.520 193.479 1.00 62.48  ? 3937 ARG A O     1 
ATOM   18709 C CB    . ARG A 1 3937 ? 175.707 135.435 193.514 1.00 62.48  ? 3937 ARG A CB    1 
ATOM   18710 C CG    . ARG A 1 3937 ? 175.773 136.867 193.997 1.00 62.48  ? 3937 ARG A CG    1 
ATOM   18711 C CD    . ARG A 1 3937 ? 174.737 137.732 193.316 1.00 62.48  ? 3937 ARG A CD    1 
ATOM   18712 N NE    . ARG A 1 3937 ? 174.709 139.084 193.859 1.00 62.48  ? 3937 ARG A NE    1 
ATOM   18713 C CZ    . ARG A 1 3937 ? 175.645 140.000 193.648 1.00 62.48  ? 3937 ARG A CZ    1 
ATOM   18714 N NH1   . ARG A 1 3937 ? 176.698 139.750 192.887 1.00 62.48  ? 3937 ARG A NH1   1 
ATOM   18715 N NH2   . ARG A 1 3937 ? 175.519 141.198 194.211 1.00 62.48  ? 3937 ARG A NH2   1 
ATOM   18716 N N     . LEU A 1 3938 ? 176.336 132.388 194.036 1.00 59.97  ? 3938 LEU A N     1 
ATOM   18717 C CA    . LEU A 1 3938 ? 176.479 131.056 193.460 1.00 59.97  ? 3938 LEU A CA    1 
ATOM   18718 C C     . LEU A 1 3938 ? 175.689 130.029 194.262 1.00 59.97  ? 3938 LEU A C     1 
ATOM   18719 O O     . LEU A 1 3938 ? 175.138 129.078 193.695 1.00 59.97  ? 3938 LEU A O     1 
ATOM   18720 C CB    . LEU A 1 3938 ? 177.962 130.683 193.392 1.00 59.97  ? 3938 LEU A CB    1 
ATOM   18721 C CG    . LEU A 1 3938 ? 178.412 129.230 193.229 1.00 59.97  ? 3938 LEU A CG    1 
ATOM   18722 C CD1   . LEU A 1 3938 ? 177.743 128.579 192.027 1.00 59.97  ? 3938 LEU A CD1   1 
ATOM   18723 C CD2   . LEU A 1 3938 ? 179.925 129.149 193.109 1.00 59.97  ? 3938 LEU A CD2   1 
ATOM   18724 N N     . SER A 1 3939 ? 175.606 130.214 195.581 1.00 63.27  ? 3939 SER A N     1 
ATOM   18725 C CA    . SER A 1 3939 ? 174.867 129.293 196.436 1.00 63.27  ? 3939 SER A CA    1 
ATOM   18726 C C     . SER A 1 3939 ? 173.371 129.303 196.161 1.00 63.27  ? 3939 SER A C     1 
ATOM   18727 O O     . SER A 1 3939 ? 172.667 128.407 196.640 1.00 63.27  ? 3939 SER A O     1 
ATOM   18728 C CB    . SER A 1 3939 ? 175.123 129.622 197.908 1.00 63.27  ? 3939 SER A CB    1 
ATOM   18729 O OG    . SER A 1 3939 ? 174.585 130.887 198.249 1.00 63.27  ? 3939 SER A OG    1 
ATOM   18730 N N     . CYS A 1 3940 ? 172.868 130.292 195.417 1.00 64.87  ? 3940 CYS A N     1 
ATOM   18731 C CA    . CYS A 1 3940 ? 171.459 130.290 195.042 1.00 64.87  ? 3940 CYS A CA    1 
ATOM   18732 C C     . CYS A 1 3940 ? 171.114 129.083 194.179 1.00 64.87  ? 3940 CYS A C     1 
ATOM   18733 O O     . CYS A 1 3940 ? 169.968 128.619 194.190 1.00 64.87  ? 3940 CYS A O     1 
ATOM   18734 C CB    . CYS A 1 3940 ? 171.110 131.587 194.311 1.00 64.87  ? 3940 CYS A CB    1 
ATOM   18735 S SG    . CYS A 1 3940 ? 169.364 131.764 193.885 1.00 64.87  ? 3940 CYS A SG    1 
ATOM   18736 N N     . LEU A 1 3941 ? 172.083 128.566 193.429 1.00 59.69  ? 3941 LEU A N     1 
ATOM   18737 C CA    . LEU A 1 3941 ? 171.849 127.386 192.617 1.00 59.69  ? 3941 LEU A CA    1 
ATOM   18738 C C     . LEU A 1 3941 ? 171.636 126.161 193.507 1.00 59.69  ? 3941 LEU A C     1 
ATOM   18739 O O     . LEU A 1 3941 ? 172.275 126.025 194.554 1.00 59.69  ? 3941 LEU A O     1 
ATOM   18740 C CB    . LEU A 1 3941 ? 173.024 127.146 191.674 1.00 59.69  ? 3941 LEU A CB    1 
ATOM   18741 C CG    . LEU A 1 3941 ? 172.816 127.574 190.221 1.00 59.69  ? 3941 LEU A CG    1 
ATOM   18742 C CD1   . LEU A 1 3941 ? 172.544 129.065 190.139 1.00 59.69  ? 3941 LEU A CD1   1 
ATOM   18743 C CD2   . LEU A 1 3941 ? 174.025 127.203 189.382 1.00 59.69  ? 3941 LEU A CD2   1 
ATOM   18744 N N     . PRO A 1 3942 ? 170.732 125.259 193.115 1.00 58.21  ? 3942 PRO A N     1 
ATOM   18745 C CA    . PRO A 1 3942 ? 170.478 124.069 193.945 1.00 58.21  ? 3942 PRO A CA    1 
ATOM   18746 C C     . PRO A 1 3942 ? 171.696 123.183 194.133 1.00 58.21  ? 3942 PRO A C     1 
ATOM   18747 O O     . PRO A 1 3942 ? 171.843 122.570 195.198 1.00 58.21  ? 3942 PRO A O     1 
ATOM   18748 C CB    . PRO A 1 3942 ? 169.363 123.343 193.179 1.00 58.21  ? 3942 PRO A CB    1 
ATOM   18749 C CG    . PRO A 1 3942 ? 169.469 123.849 191.776 1.00 58.21  ? 3942 PRO A CG    1 
ATOM   18750 C CD    . PRO A 1 3942 ? 169.903 125.275 191.899 1.00 58.21  ? 3942 PRO A CD    1 
ATOM   18751 N N     . ALA A 1 3943 ? 172.575 123.093 193.135 1.00 58.59  ? 3943 ALA A N     1 
ATOM   18752 C CA    . ALA A 1 3943 ? 173.756 122.247 193.249 1.00 58.59  ? 3943 ALA A CA    1 
ATOM   18753 C C     . ALA A 1 3943 ? 174.827 122.843 194.152 1.00 58.59  ? 3943 ALA A C     1 
ATOM   18754 O O     . ALA A 1 3943 ? 175.782 122.139 194.496 1.00 58.59  ? 3943 ALA A O     1 
ATOM   18755 C CB    . ALA A 1 3943 ? 174.343 121.975 191.863 1.00 58.59  ? 3943 ALA A CB    1 
ATOM   18756 N N     . PHE A 1 3944 ? 174.694 124.112 194.541 1.00 59.63  ? 3944 PHE A N     1 
ATOM   18757 C CA    . PHE A 1 3944 ? 175.670 124.779 195.397 1.00 59.63  ? 3944 PHE A CA    1 
ATOM   18758 C C     . PHE A 1 3944 ? 175.043 125.288 196.690 1.00 59.63  ? 3944 PHE A C     1 
ATOM   18759 O O     . PHE A 1 3944 ? 175.570 126.220 197.305 1.00 59.63  ? 3944 PHE A O     1 
ATOM   18760 C CB    . PHE A 1 3944 ? 176.338 125.931 194.645 1.00 59.63  ? 3944 PHE A CB    1 
ATOM   18761 C CG    . PHE A 1 3944 ? 177.190 125.491 193.489 1.00 59.63  ? 3944 PHE A CG    1 
ATOM   18762 C CD1   . PHE A 1 3944 ? 176.632 125.285 192.238 1.00 59.63  ? 3944 PHE A CD1   1 
ATOM   18763 C CD2   . PHE A 1 3944 ? 178.551 125.293 193.650 1.00 59.63  ? 3944 PHE A CD2   1 
ATOM   18764 C CE1   . PHE A 1 3944 ? 177.414 124.886 191.173 1.00 59.63  ? 3944 PHE A CE1   1 
ATOM   18765 C CE2   . PHE A 1 3944 ? 179.337 124.893 192.587 1.00 59.63  ? 3944 PHE A CE2   1 
ATOM   18766 C CZ    . PHE A 1 3944 ? 178.768 124.689 191.348 1.00 59.63  ? 3944 PHE A CZ    1 
ATOM   18767 N N     . LYS A 1 3945 ? 173.926 124.693 197.116 1.00 63.97  ? 3945 LYS A N     1 
ATOM   18768 C CA    . LYS A 1 3945 ? 173.235 125.164 198.311 1.00 63.97  ? 3945 LYS A CA    1 
ATOM   18769 C C     . LYS A 1 3945 ? 174.057 124.969 199.580 1.00 63.97  ? 3945 LYS A C     1 
ATOM   18770 O O     . LYS A 1 3945 ? 173.846 125.696 200.557 1.00 63.97  ? 3945 LYS A O     1 
ATOM   18771 C CB    . LYS A 1 3945 ? 171.886 124.455 198.445 1.00 63.97  ? 3945 LYS A CB    1 
ATOM   18772 C CG    . LYS A 1 3945 ? 171.989 122.972 198.762 1.00 63.97  ? 3945 LYS A CG    1 
ATOM   18773 C CD    . LYS A 1 3945 ? 170.797 122.493 199.572 1.00 63.97  ? 3945 LYS A CD    1 
ATOM   18774 C CE    . LYS A 1 3945 ? 170.866 120.995 199.814 1.00 63.97  ? 3945 LYS A CE    1 
ATOM   18775 N NZ    . LYS A 1 3945 ? 170.331 120.221 198.660 1.00 63.97  ? 3945 LYS A NZ    1 
ATOM   18776 N N     . ASP A 1 3946 ? 174.984 124.011 199.591 1.00 67.88  ? 3946 ASP A N     1 
ATOM   18777 C CA    . ASP A 1 3946 ? 175.835 123.750 200.746 1.00 67.88  ? 3946 ASP A CA    1 
ATOM   18778 C C     . ASP A 1 3946 ? 177.236 124.327 200.573 1.00 67.88  ? 3946 ASP A C     1 
ATOM   18779 O O     . ASP A 1 3946 ? 178.209 123.763 201.085 1.00 67.88  ? 3946 ASP A O     1 
ATOM   18780 C CB    . ASP A 1 3946 ? 175.910 122.248 201.018 1.00 67.88  ? 3946 ASP A CB    1 
ATOM   18781 C CG    . ASP A 1 3946 ? 174.594 121.678 201.506 1.00 67.88  ? 3946 ASP A CG    1 
ATOM   18782 O OD1   . ASP A 1 3946 ? 173.823 122.423 202.147 1.00 67.88  ? 3946 ASP A OD1   1 
ATOM   18783 O OD2   . ASP A 1 3946 ? 174.331 120.485 201.250 1.00 67.88  ? 3946 ASP A OD2   1 
ATOM   18784 N N     . LEU A 1 3947 ? 177.355 125.447 199.856 1.00 65.77  ? 3947 LEU A N     1 
ATOM   18785 C CA    . LEU A 1 3947 ? 178.672 125.992 199.545 1.00 65.77  ? 3947 LEU A CA    1 
ATOM   18786 C C     . LEU A 1 3947 ? 179.376 126.514 200.791 1.00 65.77  ? 3947 LEU A C     1 
ATOM   18787 O O     . LEU A 1 3947 ? 180.600 126.387 200.917 1.00 65.77  ? 3947 LEU A O     1 
ATOM   18788 C CB    . LEU A 1 3947 ? 178.545 127.099 198.499 1.00 65.77  ? 3947 LEU A CB    1 
ATOM   18789 C CG    . LEU A 1 3947 ? 179.840 127.490 197.785 1.00 65.77  ? 3947 LEU A CG    1 
ATOM   18790 C CD1   . LEU A 1 3947 ? 180.510 126.266 197.183 1.00 65.77  ? 3947 LEU A CD1   1 
ATOM   18791 C CD2   . LEU A 1 3947 ? 179.563 128.530 196.716 1.00 65.77  ? 3947 LEU A CD2   1 
ATOM   18792 N N     . ILE A 1 3948 ? 178.626 127.113 201.719 1.00 69.61  ? 3948 ILE A N     1 
ATOM   18793 C CA    . ILE A 1 3948 ? 179.239 127.732 202.894 1.00 69.61  ? 3948 ILE A CA    1 
ATOM   18794 C C     . ILE A 1 3948 ? 179.949 126.681 203.740 1.00 69.61  ? 3948 ILE A C     1 
ATOM   18795 O O     . ILE A 1 3948 ? 181.123 126.829 204.099 1.00 69.61  ? 3948 ILE A O     1 
ATOM   18796 C CB    . ILE A 1 3948 ? 178.184 128.488 203.720 1.00 69.61  ? 3948 ILE A CB    1 
ATOM   18797 C CG1   . ILE A 1 3948 ? 177.303 129.349 202.813 1.00 69.61  ? 3948 ILE A CG1   1 
ATOM   18798 C CG2   . ILE A 1 3948 ? 178.855 129.340 204.786 1.00 69.61  ? 3948 ILE A CG2   1 
ATOM   18799 C CD1   . ILE A 1 3948 ? 178.067 130.371 202.013 1.00 69.61  ? 3948 ILE A CD1   1 
ATOM   18800 N N     . ALA A 1 3949 ? 179.243 125.595 204.061 1.00 69.68  ? 3949 ALA A N     1 
ATOM   18801 C CA    . ALA A 1 3949 ? 179.848 124.533 204.856 1.00 69.68  ? 3949 ALA A CA    1 
ATOM   18802 C C     . ALA A 1 3949 ? 180.983 123.861 204.097 1.00 69.68  ? 3949 ALA A C     1 
ATOM   18803 O O     . ALA A 1 3949 ? 181.998 123.479 204.692 1.00 69.68  ? 3949 ALA A O     1 
ATOM   18804 C CB    . ALA A 1 3949 ? 178.788 123.509 205.261 1.00 69.68  ? 3949 ALA A CB    1 
ATOM   18805 N N     . LYS A 1 3950 ? 180.828 123.707 202.780 1.00 68.20  ? 3950 LYS A N     1 
ATOM   18806 C CA    . LYS A 1 3950 ? 181.870 123.073 201.980 1.00 68.20  ? 3950 LYS A CA    1 
ATOM   18807 C C     . LYS A 1 3950 ? 183.164 123.876 202.012 1.00 68.20  ? 3950 LYS A C     1 
ATOM   18808 O O     . LYS A 1 3950 ? 184.250 123.309 202.182 1.00 68.20  ? 3950 LYS A O     1 
ATOM   18809 C CB    . LYS A 1 3950 ? 181.387 122.895 200.541 1.00 68.20  ? 3950 LYS A CB    1 
ATOM   18810 C CG    . LYS A 1 3950 ? 180.622 121.606 200.297 1.00 68.20  ? 3950 LYS A CG    1 
ATOM   18811 C CD    . LYS A 1 3950 ? 181.538 120.519 199.762 1.00 68.20  ? 3950 LYS A CD    1 
ATOM   18812 C CE    . LYS A 1 3950 ? 180.745 119.316 199.281 1.00 68.20  ? 3950 LYS A CE    1 
ATOM   18813 N NZ    . LYS A 1 3950 ? 181.636 118.200 198.859 1.00 68.20  ? 3950 LYS A NZ    1 
ATOM   18814 N N     . VAL A 1 3951 ? 183.073 125.198 201.850 1.00 67.70  ? 3951 VAL A N     1 
ATOM   18815 C CA    . VAL A 1 3951 ? 184.283 126.015 201.852 1.00 67.70  ? 3951 VAL A CA    1 
ATOM   18816 C C     . VAL A 1 3951 ? 184.844 126.144 203.263 1.00 67.70  ? 3951 VAL A C     1 
ATOM   18817 O O     . VAL A 1 3951 ? 186.063 126.227 203.452 1.00 67.70  ? 3951 VAL A O     1 
ATOM   18818 C CB    . VAL A 1 3951 ? 184.019 127.391 201.209 1.00 67.70  ? 3951 VAL A CB    1 
ATOM   18819 C CG1   . VAL A 1 3951 ? 183.601 127.227 199.755 1.00 67.70  ? 3951 VAL A CG1   1 
ATOM   18820 C CG2   . VAL A 1 3951 ? 182.982 128.181 201.989 1.00 67.70  ? 3951 VAL A CG2   1 
ATOM   18821 N N     . GLN A 1 3952 ? 183.974 126.164 204.278 1.00 71.58  ? 3952 GLN A N     1 
ATOM   18822 C CA    . GLN A 1 3952 ? 184.458 126.306 205.647 1.00 71.58  ? 3952 GLN A CA    1 
ATOM   18823 C C     . GLN A 1 3952 ? 185.185 125.051 206.114 1.00 71.58  ? 3952 GLN A C     1 
ATOM   18824 O O     . GLN A 1 3952 ? 186.223 125.138 206.780 1.00 71.58  ? 3952 GLN A O     1 
ATOM   18825 C CB    . GLN A 1 3952 ? 183.295 126.637 206.582 1.00 71.58  ? 3952 GLN A CB    1 
ATOM   18826 C CG    . GLN A 1 3952 ? 182.975 128.121 206.664 1.00 71.58  ? 3952 GLN A CG    1 
ATOM   18827 C CD    . GLN A 1 3952 ? 183.847 128.852 207.666 1.00 71.58  ? 3952 GLN A CD    1 
ATOM   18828 O OE1   . GLN A 1 3952 ? 184.690 128.249 208.329 1.00 71.58  ? 3952 GLN A OE1   1 
ATOM   18829 N NE2   . GLN A 1 3952 ? 183.648 130.160 207.779 1.00 71.58  ? 3952 GLN A NE2   1 
ATOM   18830 N N     . ALA A 1 3953 ? 184.655 123.873 205.778 1.00 74.06  ? 3953 ALA A N     1 
ATOM   18831 C CA    . ALA A 1 3953 ? 185.257 122.629 206.247 1.00 74.06  ? 3953 ALA A CA    1 
ATOM   18832 C C     . ALA A 1 3953 ? 186.605 122.372 205.585 1.00 74.06  ? 3953 ALA A C     1 
ATOM   18833 O O     . ALA A 1 3953 ? 187.533 121.870 206.230 1.00 74.06  ? 3953 ALA A O     1 
ATOM   18834 C CB    . ALA A 1 3953 ? 184.305 121.459 205.997 1.00 74.06  ? 3953 ALA A CB    1 
ATOM   18835 N N     . ASP A 1 3954 ? 186.730 122.700 204.302 1.00 72.61  ? 3954 ASP A N     1 
ATOM   18836 C CA    . ASP A 1 3954 ? 187.969 122.451 203.580 1.00 72.61  ? 3954 ASP A CA    1 
ATOM   18837 C C     . ASP A 1 3954 ? 189.095 123.320 204.127 1.00 72.61  ? 3954 ASP A C     1 
ATOM   18838 O O     . ASP A 1 3954 ? 188.890 124.486 204.474 1.00 72.61  ? 3954 ASP A O     1 
ATOM   18839 C CB    . ASP A 1 3954 ? 187.775 122.723 202.088 1.00 72.61  ? 3954 ASP A CB    1 
ATOM   18840 C CG    . ASP A 1 3954 ? 188.904 122.168 201.243 1.00 72.61  ? 3954 ASP A CG    1 
ATOM   18841 O OD1   . ASP A 1 3954 ? 189.742 121.417 201.783 1.00 72.61  ? 3954 ASP A OD1   1 
ATOM   18842 O OD2   . ASP A 1 3954 ? 188.953 122.486 200.036 1.00 72.61  ? 3954 ASP A OD2   1 
ATOM   18843 N N     . GLU A 1 3955 ? 190.292 122.741 204.208 1.00 74.73  ? 3955 GLU A N     1 
ATOM   18844 C CA    . GLU A 1 3955 ? 191.460 123.466 204.693 1.00 74.73  ? 3955 GLU A CA    1 
ATOM   18845 C C     . GLU A 1 3955 ? 192.542 123.654 203.636 1.00 74.73  ? 3955 GLU A C     1 
ATOM   18846 O O     . GLU A 1 3955 ? 193.436 124.484 203.830 1.00 74.73  ? 3955 GLU A O     1 
ATOM   18847 C CB    . GLU A 1 3955 ? 192.046 122.773 205.933 1.00 74.73  ? 3955 GLU A CB    1 
ATOM   18848 C CG    . GLU A 1 3955 ? 192.532 121.347 205.736 1.00 74.73  ? 3955 GLU A CG    1 
ATOM   18849 C CD    . GLU A 1 3955 ? 191.403 120.334 205.671 1.00 74.73  ? 3955 GLU A CD    1 
ATOM   18850 O OE1   . GLU A 1 3955 ? 190.235 120.723 205.884 1.00 74.73  ? 3955 GLU A OE1   1 
ATOM   18851 O OE2   . GLU A 1 3955 ? 191.684 119.146 205.407 1.00 74.73  ? 3955 GLU A OE2   1 
ATOM   18852 N N     . GLN A 1 3956 ? 192.492 122.917 202.525 1.00 69.43  ? 3956 GLN A N     1 
ATOM   18853 C CA    . GLN A 1 3956 ? 193.298 123.251 201.355 1.00 69.43  ? 3956 GLN A CA    1 
ATOM   18854 C C     . GLN A 1 3956 ? 192.646 124.313 200.481 1.00 69.43  ? 3956 GLN A C     1 
ATOM   18855 O O     . GLN A 1 3956 ? 193.229 124.707 199.466 1.00 69.43  ? 3956 GLN A O     1 
ATOM   18856 C CB    . GLN A 1 3956 ? 193.586 122.010 200.491 1.00 69.43  ? 3956 GLN A CB    1 
ATOM   18857 C CG    . GLN A 1 3956 ? 194.672 121.055 200.997 1.00 69.43  ? 3956 GLN A CG    1 
ATOM   18858 C CD    . GLN A 1 3956 ? 194.458 120.566 202.412 1.00 69.43  ? 3956 GLN A CD    1 
ATOM   18859 O OE1   . GLN A 1 3956 ? 193.348 120.612 202.935 1.00 69.43  ? 3956 GLN A OE1   1 
ATOM   18860 N NE2   . GLN A 1 3956 ? 195.527 120.095 203.043 1.00 69.43  ? 3956 GLN A NE2   1 
ATOM   18861 N N     . PHE A 1 3957 ? 191.447 124.772 200.840 1.00 55.17  ? 3957 PHE A N     1 
ATOM   18862 C CA    . PHE A 1 3957 ? 190.772 125.786 200.039 1.00 55.17  ? 3957 PHE A CA    1 
ATOM   18863 C C     . PHE A 1 3957 ? 191.536 127.105 200.068 1.00 55.17  ? 3957 PHE A C     1 
ATOM   18864 O O     . PHE A 1 3957 ? 191.629 127.806 199.051 1.00 55.17  ? 3957 PHE A O     1 
ATOM   18865 C CB    . PHE A 1 3957 ? 189.338 125.957 200.543 1.00 55.17  ? 3957 PHE A CB    1 
ATOM   18866 C CG    . PHE A 1 3957 ? 188.581 127.062 199.874 1.00 55.17  ? 3957 PHE A CG    1 
ATOM   18867 C CD1   . PHE A 1 3957 ? 188.571 128.339 200.406 1.00 55.17  ? 3957 PHE A CD1   1 
ATOM   18868 C CD2   . PHE A 1 3957 ? 187.871 126.820 198.711 1.00 55.17  ? 3957 PHE A CD2   1 
ATOM   18869 C CE1   . PHE A 1 3957 ? 187.870 129.349 199.790 1.00 55.17  ? 3957 PHE A CE1   1 
ATOM   18870 C CE2   . PHE A 1 3957 ? 187.170 127.830 198.091 1.00 55.17  ? 3957 PHE A CE2   1 
ATOM   18871 C CZ    . PHE A 1 3957 ? 187.171 129.096 198.631 1.00 55.17  ? 3957 PHE A CZ    1 
ATOM   18872 N N     . GLY A 1 3958 ? 192.102 127.455 201.225 1.00 51.18  ? 3958 GLY A N     1 
ATOM   18873 C CA    . GLY A 1 3958 ? 192.878 128.680 201.317 1.00 51.18  ? 3958 GLY A CA    1 
ATOM   18874 C C     . GLY A 1 3958 ? 194.112 128.663 200.436 1.00 51.18  ? 3958 GLY A C     1 
ATOM   18875 O O     . GLY A 1 3958 ? 194.405 129.642 199.744 1.00 51.18  ? 3958 GLY A O     1 
ATOM   18876 N N     . ILE A 1 3959 ? 194.855 127.554 200.447 1.00 52.22  ? 3959 ILE A N     1 
ATOM   18877 C CA    . ILE A 1 3959 ? 196.043 127.463 199.604 1.00 52.22  ? 3959 ILE A CA    1 
ATOM   18878 C C     . ILE A 1 3959 ? 195.646 127.356 198.136 1.00 52.22  ? 3959 ILE A C     1 
ATOM   18879 O O     . ILE A 1 3959 ? 196.390 127.787 197.247 1.00 52.22  ? 3959 ILE A O     1 
ATOM   18880 C CB    . ILE A 1 3959 ? 196.942 126.292 200.049 1.00 52.22  ? 3959 ILE A CB    1 
ATOM   18881 C CG1   . ILE A 1 3959 ? 198.296 126.356 199.341 1.00 52.22  ? 3959 ILE A CG1   1 
ATOM   18882 C CG2   . ILE A 1 3959 ? 196.283 124.954 199.779 1.00 52.22  ? 3959 ILE A CG2   1 
ATOM   18883 C CD1   . ILE A 1 3959 ? 199.345 125.449 199.946 1.00 52.22  ? 3959 ILE A CD1   1 
ATOM   18884 N N     . TRP A 1 3960 ? 194.472 126.784 197.855 1.00 46.97  ? 3960 TRP A N     1 
ATOM   18885 C CA    . TRP A 1 3960 ? 193.980 126.760 196.482 1.00 46.97  ? 3960 TRP A CA    1 
ATOM   18886 C C     . TRP A 1 3960 ? 193.696 128.166 195.974 1.00 46.97  ? 3960 TRP A C     1 
ATOM   18887 O O     . TRP A 1 3960 ? 193.982 128.485 194.813 1.00 46.97  ? 3960 TRP A O     1 
ATOM   18888 C CB    . TRP A 1 3960 ? 192.722 125.901 196.376 1.00 46.97  ? 3960 TRP A CB    1 
ATOM   18889 C CG    . TRP A 1 3960 ? 192.105 125.963 195.015 1.00 46.97  ? 3960 TRP A CG    1 
ATOM   18890 C CD1   . TRP A 1 3960 ? 192.621 125.460 193.859 1.00 46.97  ? 3960 TRP A CD1   1 
ATOM   18891 C CD2   . TRP A 1 3960 ? 190.867 126.592 194.662 1.00 46.97  ? 3960 TRP A CD2   1 
ATOM   18892 N NE1   . TRP A 1 3960 ? 191.776 125.721 192.809 1.00 46.97  ? 3960 TRP A NE1   1 
ATOM   18893 C CE2   . TRP A 1 3960 ? 190.692 126.418 193.275 1.00 46.97  ? 3960 TRP A CE2   1 
ATOM   18894 C CE3   . TRP A 1 3960 ? 189.888 127.279 195.383 1.00 46.97  ? 3960 TRP A CE3   1 
ATOM   18895 C CZ2   . TRP A 1 3960 ? 189.578 126.904 192.597 1.00 46.97  ? 3960 TRP A CZ2   1 
ATOM   18896 C CZ3   . TRP A 1 3960 ? 188.783 127.762 194.708 1.00 46.97  ? 3960 TRP A CZ3   1 
ATOM   18897 C CH2   . TRP A 1 3960 ? 188.637 127.572 193.329 1.00 46.97  ? 3960 TRP A CH2   1 
ATOM   18898 N N     . LEU A 1 3961 ? 193.117 129.018 196.826 1.00 45.86  ? 3961 LEU A N     1 
ATOM   18899 C CA    . LEU A 1 3961 ? 192.815 130.387 196.415 1.00 45.86  ? 3961 LEU A CA    1 
ATOM   18900 C C     . LEU A 1 3961 ? 194.059 131.131 195.950 1.00 45.86  ? 3961 LEU A C     1 
ATOM   18901 O O     . LEU A 1 3961 ? 193.981 131.955 195.031 1.00 45.86  ? 3961 LEU A O     1 
ATOM   18902 C CB    . LEU A 1 3961 ? 192.158 131.157 197.560 1.00 45.86  ? 3961 LEU A CB    1 
ATOM   18903 C CG    . LEU A 1 3961 ? 190.684 130.898 197.858 1.00 45.86  ? 3961 LEU A CG    1 
ATOM   18904 C CD1   . LEU A 1 3961 ? 190.248 131.746 199.039 1.00 45.86  ? 3961 LEU A CD1   1 
ATOM   18905 C CD2   . LEU A 1 3961 ? 189.836 131.201 196.638 1.00 45.86  ? 3961 LEU A CD2   1 
ATOM   18906 N N     . ASP A 1 3962 ? 195.208 130.863 196.565 1.00 47.66  ? 3962 ASP A N     1 
ATOM   18907 C CA    . ASP A 1 3962 ? 196.443 131.572 196.264 1.00 47.66  ? 3962 ASP A CA    1 
ATOM   18908 C C     . ASP A 1 3962 ? 197.307 130.851 195.237 1.00 47.66  ? 3962 ASP A C     1 
ATOM   18909 O O     . ASP A 1 3962 ? 198.422 131.301 194.957 1.00 47.66  ? 3962 ASP A O     1 
ATOM   18910 C CB    . ASP A 1 3962 ? 197.241 131.800 197.549 1.00 47.66  ? 3962 ASP A CB    1 
ATOM   18911 C CG    . ASP A 1 3962 ? 196.444 132.541 198.604 1.00 47.66  ? 3962 ASP A CG    1 
ATOM   18912 O OD1   . ASP A 1 3962 ? 195.579 133.359 198.230 1.00 47.66  ? 3962 ASP A OD1   1 
ATOM   18913 O OD2   . ASP A 1 3962 ? 196.682 132.303 199.807 1.00 47.66  ? 3962 ASP A OD2   1 
ATOM   18914 N N     . SER A 1 3963 ? 196.824 129.748 194.672 1.00 41.61  ? 3963 SER A N     1 
ATOM   18915 C CA    . SER A 1 3963 ? 197.607 129.008 193.696 1.00 41.61  ? 3963 SER A CA    1 
ATOM   18916 C C     . SER A 1 3963 ? 197.761 129.810 192.407 1.00 41.61  ? 3963 SER A C     1 
ATOM   18917 O O     . SER A 1 3963 ? 196.936 130.662 192.067 1.00 41.61  ? 3963 SER A O     1 
ATOM   18918 C CB    . SER A 1 3963 ? 196.959 127.656 193.399 1.00 41.61  ? 3963 SER A CB    1 
ATOM   18919 O OG    . SER A 1 3963 ? 196.573 127.004 194.595 1.00 41.61  ? 3963 SER A OG    1 
ATOM   18920 N N     . SER A 1 3964 ? 198.850 129.527 191.688 1.00 39.39  ? 3964 SER A N     1 
ATOM   18921 C CA    . SER A 1 3964 ? 199.116 130.231 190.437 1.00 39.39  ? 3964 SER A CA    1 
ATOM   18922 C C     . SER A 1 3964 ? 198.038 129.947 189.399 1.00 39.39  ? 3964 SER A C     1 
ATOM   18923 O O     . SER A 1 3964 ? 197.583 130.863 188.704 1.00 39.39  ? 3964 SER A O     1 
ATOM   18924 C CB    . SER A 1 3964 ? 200.493 129.842 189.900 1.00 39.39  ? 3964 SER A CB    1 
ATOM   18925 O OG    . SER A 1 3964 ? 200.451 128.580 189.259 1.00 39.39  ? 3964 SER A OG    1 
ATOM   18926 N N     . SER A 1 3965 ? 197.617 128.690 189.278 1.00 36.41  ? 3965 SER A N     1 
ATOM   18927 C CA    . SER A 1 3965 ? 196.595 128.280 188.315 1.00 36.41  ? 3965 SER A CA    1 
ATOM   18928 C C     . SER A 1 3965 ? 195.530 127.473 189.043 1.00 36.41  ? 3965 SER A C     1 
ATOM   18929 O O     . SER A 1 3965 ? 195.542 126.235 189.012 1.00 36.41  ? 3965 SER A O     1 
ATOM   18930 C CB    . SER A 1 3965 ? 197.207 127.479 187.165 1.00 36.41  ? 3965 SER A CB    1 
ATOM   18931 O OG    . SER A 1 3965 ? 197.892 126.338 187.647 1.00 36.41  ? 3965 SER A OG    1 
ATOM   18932 N N     . PRO A 1 3966 ? 194.595 128.144 189.721 1.00 37.97  ? 3966 PRO A N     1 
ATOM   18933 C CA    . PRO A 1 3966 ? 193.507 127.408 190.386 1.00 37.97  ? 3966 PRO A CA    1 
ATOM   18934 C C     . PRO A 1 3966 ? 192.659 126.599 189.425 1.00 37.97  ? 3966 PRO A C     1 
ATOM   18935 O O     . PRO A 1 3966 ? 192.117 125.557 189.813 1.00 37.97  ? 3966 PRO A O     1 
ATOM   18936 C CB    . PRO A 1 3966 ? 192.687 128.521 191.054 1.00 37.97  ? 3966 PRO A CB    1 
ATOM   18937 C CG    . PRO A 1 3966 ? 193.604 129.691 191.135 1.00 37.97  ? 3966 PRO A CG    1 
ATOM   18938 C CD    . PRO A 1 3966 ? 194.508 129.594 189.949 1.00 37.97  ? 3966 PRO A CD    1 
ATOM   18939 N N     . GLU A 1 3967 ? 192.527 127.055 188.179 1.00 35.72  ? 3967 GLU A N     1 
ATOM   18940 C CA    . GLU A 1 3967 ? 191.703 126.369 187.192 1.00 35.72  ? 3967 GLU A CA    1 
ATOM   18941 C C     . GLU A 1 3967 ? 192.208 124.966 186.873 1.00 35.72  ? 3967 GLU A C     1 
ATOM   18942 O O     . GLU A 1 3967 ? 191.419 124.129 186.422 1.00 35.72  ? 3967 GLU A O     1 
ATOM   18943 C CB    . GLU A 1 3967 ? 191.631 127.213 185.919 1.00 35.72  ? 3967 GLU A CB    1 
ATOM   18944 C CG    . GLU A 1 3967 ? 192.710 126.892 184.904 1.00 35.72  ? 3967 GLU A CG    1 
ATOM   18945 C CD    . GLU A 1 3967 ? 193.921 127.792 185.031 1.00 35.72  ? 3967 GLU A CD    1 
ATOM   18946 O OE1   . GLU A 1 3967 ? 194.696 127.890 184.058 1.00 35.72  ? 3967 GLU A OE1   1 
ATOM   18947 O OE2   . GLU A 1 3967 ? 194.096 128.406 186.104 1.00 35.72  ? 3967 GLU A OE2   1 
ATOM   18948 N N     . GLN A 1 3968 ? 193.495 124.690 187.091 1.00 38.16  ? 3968 GLN A N     1 
ATOM   18949 C CA    . GLN A 1 3968 ? 194.022 123.357 186.819 1.00 38.16  ? 3968 GLN A CA    1 
ATOM   18950 C C     . GLN A 1 3968 ? 193.454 122.330 187.791 1.00 38.16  ? 3968 GLN A C     1 
ATOM   18951 O O     . GLN A 1 3968 ? 193.056 121.232 187.388 1.00 38.16  ? 3968 GLN A O     1 
ATOM   18952 C CB    . GLN A 1 3968 ? 195.549 123.372 186.884 1.00 38.16  ? 3968 GLN A CB    1 
ATOM   18953 C CG    . GLN A 1 3968 ? 196.219 123.938 185.644 1.00 38.16  ? 3968 GLN A CG    1 
ATOM   18954 C CD    . GLN A 1 3968 ? 195.616 123.401 184.361 1.00 38.16  ? 3968 GLN A CD    1 
ATOM   18955 O OE1   . GLN A 1 3968 ? 194.991 124.139 183.599 1.00 38.16  ? 3968 GLN A OE1   1 
ATOM   18956 N NE2   . GLN A 1 3968 ? 195.802 122.110 184.114 1.00 38.16  ? 3968 GLN A NE2   1 
ATOM   18957 N N     . THR A 1 3969 ? 193.408 122.671 189.077 1.00 42.70  ? 3969 THR A N     1 
ATOM   18958 C CA    . THR A 1 3969 ? 192.932 121.775 190.129 1.00 42.70  ? 3969 THR A CA    1 
ATOM   18959 C C     . THR A 1 3969 ? 191.821 122.490 190.893 1.00 42.70  ? 3969 THR A C     1 
ATOM   18960 O O     . THR A 1 3969 ? 192.078 123.174 191.886 1.00 42.70  ? 3969 THR A O     1 
ATOM   18961 C CB    . THR A 1 3969 ? 194.071 121.360 191.063 1.00 42.70  ? 3969 THR A CB    1 
ATOM   18962 O OG1   . THR A 1 3969 ? 194.614 122.522 191.703 1.00 42.70  ? 3969 THR A OG1   1 
ATOM   18963 C CG2   . THR A 1 3969 ? 195.172 120.655 190.286 1.00 42.70  ? 3969 THR A CG2   1 
ATOM   18964 N N     . VAL A 1 3970 ? 190.589 122.330 190.427 1.00 42.16  ? 3970 VAL A N     1 
ATOM   18965 C CA    . VAL A 1 3970 ? 189.421 122.916 191.076 1.00 42.16  ? 3970 VAL A CA    1 
ATOM   18966 C C     . VAL A 1 3970 ? 188.854 121.881 192.044 1.00 42.16  ? 3970 VAL A C     1 
ATOM   18967 O O     . VAL A 1 3970 ? 188.514 120.769 191.609 1.00 42.16  ? 3970 VAL A O     1 
ATOM   18968 C CB    . VAL A 1 3970 ? 188.363 123.345 190.053 1.00 42.16  ? 3970 VAL A CB    1 
ATOM   18969 C CG1   . VAL A 1 3970 ? 187.095 123.787 190.761 1.00 42.16  ? 3970 VAL A CG1   1 
ATOM   18970 C CG2   . VAL A 1 3970 ? 188.902 124.459 189.172 1.00 42.16  ? 3970 VAL A CG2   1 
ATOM   18971 N N     . PRO A 1 3971 ? 188.748 122.188 193.336 1.00 50.85  ? 3971 PRO A N     1 
ATOM   18972 C CA    . PRO A 1 3971 ? 188.230 121.198 194.286 1.00 50.85  ? 3971 PRO A CA    1 
ATOM   18973 C C     . PRO A 1 3971 ? 186.773 120.859 194.009 1.00 50.85  ? 3971 PRO A C     1 
ATOM   18974 O O     . PRO A 1 3971 ? 185.997 121.686 193.526 1.00 50.85  ? 3971 PRO A O     1 
ATOM   18975 C CB    . PRO A 1 3971 ? 188.396 121.889 195.644 1.00 50.85  ? 3971 PRO A CB    1 
ATOM   18976 C CG    . PRO A 1 3971 ? 188.392 123.344 195.325 1.00 50.85  ? 3971 PRO A CG    1 
ATOM   18977 C CD    . PRO A 1 3971 ? 189.059 123.471 193.986 1.00 50.85  ? 3971 PRO A CD    1 
ATOM   18978 N N     . TYR A 1 3972 ? 186.410 119.619 194.323 1.00 62.52  ? 3972 TYR A N     1 
ATOM   18979 C CA    . TYR A 1 3972 ? 185.045 119.130 194.142 1.00 62.52  ? 3972 TYR A CA    1 
ATOM   18980 C C     . TYR A 1 3972 ? 184.170 119.709 195.246 1.00 62.52  ? 3972 TYR A C     1 
ATOM   18981 O O     . TYR A 1 3972 ? 184.147 119.201 196.368 1.00 62.52  ? 3972 TYR A O     1 
ATOM   18982 C CB    . TYR A 1 3972 ? 185.031 117.607 194.161 1.00 62.52  ? 3972 TYR A CB    1 
ATOM   18983 C CG    . TYR A 1 3972 ? 183.671 116.987 193.940 1.00 62.52  ? 3972 TYR A CG    1 
ATOM   18984 C CD1   . TYR A 1 3972 ? 183.104 116.944 192.674 1.00 62.52  ? 3972 TYR A CD1   1 
ATOM   18985 C CD2   . TYR A 1 3972 ? 182.959 116.437 194.996 1.00 62.52  ? 3972 TYR A CD2   1 
ATOM   18986 C CE1   . TYR A 1 3972 ? 181.864 116.374 192.467 1.00 62.52  ? 3972 TYR A CE1   1 
ATOM   18987 C CE2   . TYR A 1 3972 ? 181.718 115.865 194.799 1.00 62.52  ? 3972 TYR A CE2   1 
ATOM   18988 C CZ    . TYR A 1 3972 ? 181.175 115.837 193.533 1.00 62.52  ? 3972 TYR A CZ    1 
ATOM   18989 O OH    . TYR A 1 3972 ? 179.939 115.268 193.333 1.00 62.52  ? 3972 TYR A OH    1 
ATOM   18990 N N     . LEU A 1 3973 ? 183.443 120.780 194.931 1.00 56.33  ? 3973 LEU A N     1 
ATOM   18991 C CA    . LEU A 1 3973 ? 182.648 121.495 195.922 1.00 56.33  ? 3973 LEU A CA    1 
ATOM   18992 C C     . LEU A 1 3973 ? 181.148 121.380 195.714 1.00 56.33  ? 3973 LEU A C     1 
ATOM   18993 O O     . LEU A 1 3973 ? 180.401 121.416 196.694 1.00 56.33  ? 3973 LEU A O     1 
ATOM   18994 C CB    . LEU A 1 3973 ? 183.028 122.981 195.938 1.00 56.33  ? 3973 LEU A CB    1 
ATOM   18995 C CG    . LEU A 1 3973 ? 184.461 123.315 196.352 1.00 56.33  ? 3973 LEU A CG    1 
ATOM   18996 C CD1   . LEU A 1 3973 ? 184.603 124.802 196.631 1.00 56.33  ? 3973 LEU A CD1   1 
ATOM   18997 C CD2   . LEU A 1 3973 ? 184.877 122.498 197.564 1.00 56.33  ? 3973 LEU A CD2   1 
ATOM   18998 N N     . TRP A 1 3974 ? 180.686 121.251 194.474 1.00 57.54  ? 3974 TRP A N     1 
ATOM   18999 C CA    . TRP A 1 3974 ? 179.256 121.159 194.221 1.00 57.54  ? 3974 TRP A CA    1 
ATOM   19000 C C     . TRP A 1 3974 ? 178.704 119.829 194.721 1.00 57.54  ? 3974 TRP A C     1 
ATOM   19001 O O     . TRP A 1 3974 ? 179.368 118.790 194.661 1.00 57.54  ? 3974 TRP A O     1 
ATOM   19002 C CB    . TRP A 1 3974 ? 178.963 121.319 192.730 1.00 57.54  ? 3974 TRP A CB    1 
ATOM   19003 C CG    . TRP A 1 3974 ? 179.636 120.299 191.870 1.00 57.54  ? 3974 TRP A CG    1 
ATOM   19004 C CD1   . TRP A 1 3974 ? 179.103 119.128 191.419 1.00 57.54  ? 3974 TRP A CD1   1 
ATOM   19005 C CD2   . TRP A 1 3974 ? 180.967 120.362 191.344 1.00 57.54  ? 3974 TRP A CD2   1 
ATOM   19006 N NE1   . TRP A 1 3974 ? 180.020 118.455 190.650 1.00 57.54  ? 3974 TRP A NE1   1 
ATOM   19007 C CE2   . TRP A 1 3974 ? 181.173 119.192 190.588 1.00 57.54  ? 3974 TRP A CE2   1 
ATOM   19008 C CE3   . TRP A 1 3974 ? 182.004 121.293 191.440 1.00 57.54  ? 3974 TRP A CE3   1 
ATOM   19009 C CZ2   . TRP A 1 3974 ? 182.373 118.928 189.934 1.00 57.54  ? 3974 TRP A CZ2   1 
ATOM   19010 C CZ3   . TRP A 1 3974 ? 183.195 121.029 190.790 1.00 57.54  ? 3974 TRP A CZ3   1 
ATOM   19011 C CH2   . TRP A 1 3974 ? 183.369 119.857 190.047 1.00 57.54  ? 3974 TRP A CH2   1 
ATOM   19012 N N     . SER A 1 3975 ? 177.472 119.871 195.221 1.00 69.94  ? 3975 SER A N     1 
ATOM   19013 C CA    . SER A 1 3975 ? 176.789 118.697 195.754 1.00 69.94  ? 3975 SER A CA    1 
ATOM   19014 C C     . SER A 1 3975 ? 175.793 118.208 194.711 1.00 69.94  ? 3975 SER A C     1 
ATOM   19015 O O     . SER A 1 3975 ? 174.830 118.910 194.386 1.00 69.94  ? 3975 SER A O     1 
ATOM   19016 C CB    . SER A 1 3975 ? 176.089 119.024 197.071 1.00 69.94  ? 3975 SER A CB    1 
ATOM   19017 O OG    . SER A 1 3975 ? 175.028 119.941 196.866 1.00 69.94  ? 3975 SER A OG    1 
ATOM   19018 N N     . GLU A 1 3976 ? 176.025 117.005 194.192 1.00 74.01  ? 3976 GLU A N     1 
ATOM   19019 C CA    . GLU A 1 3976 ? 175.172 116.409 193.176 1.00 74.01  ? 3976 GLU A CA    1 
ATOM   19020 C C     . GLU A 1 3976 ? 174.795 114.995 193.594 1.00 74.01  ? 3976 GLU A C     1 
ATOM   19021 O O     . GLU A 1 3976 ? 175.623 114.253 194.131 1.00 74.01  ? 3976 GLU A O     1 
ATOM   19022 C CB    . GLU A 1 3976 ? 175.868 116.400 191.807 1.00 74.01  ? 3976 GLU A CB    1 
ATOM   19023 C CG    . GLU A 1 3976 ? 177.155 115.595 191.762 1.00 74.01  ? 3976 GLU A CG    1 
ATOM   19024 C CD    . GLU A 1 3976 ? 177.874 115.719 190.434 1.00 74.01  ? 3976 GLU A CD    1 
ATOM   19025 O OE1   . GLU A 1 3976 ? 177.384 116.464 189.561 1.00 74.01  ? 3976 GLU A OE1   1 
ATOM   19026 O OE2   . GLU A 1 3976 ? 178.928 115.071 190.264 1.00 74.01  ? 3976 GLU A OE2   1 
ATOM   19027 N N     . GLU A 1 3977 ? 173.531 114.633 193.359 1.00 82.49  ? 3977 GLU A N     1 
ATOM   19028 C CA    . GLU A 1 3977 ? 173.058 113.309 193.751 1.00 82.49  ? 3977 GLU A CA    1 
ATOM   19029 C C     . GLU A 1 3977 ? 173.648 112.220 192.862 1.00 82.49  ? 3977 GLU A C     1 
ATOM   19030 O O     . GLU A 1 3977 ? 173.903 111.103 193.328 1.00 82.49  ? 3977 GLU A O     1 
ATOM   19031 C CB    . GLU A 1 3977 ? 171.529 113.268 193.722 1.00 82.49  ? 3977 GLU A CB    1 
ATOM   19032 C CG    . GLU A 1 3977 ? 170.915 113.434 192.341 1.00 82.49  ? 3977 GLU A CG    1 
ATOM   19033 C CD    . GLU A 1 3977 ? 169.400 113.450 192.375 1.00 82.49  ? 3977 GLU A CD    1 
ATOM   19034 O OE1   . GLU A 1 3977 ? 168.828 113.354 193.480 1.00 82.49  ? 3977 GLU A OE1   1 
ATOM   19035 O OE2   . GLU A 1 3977 ? 168.782 113.559 191.295 1.00 82.49  ? 3977 GLU A OE2   1 
ATOM   19036 N N     . THR A 1 3978 ? 173.872 112.520 191.585 1.00 79.97  ? 3978 THR A N     1 
ATOM   19037 C CA    . THR A 1 3978 ? 174.398 111.548 190.643 1.00 79.97  ? 3978 THR A CA    1 
ATOM   19038 C C     . THR A 1 3978 ? 175.669 112.078 189.991 1.00 79.97  ? 3978 THR A C     1 
ATOM   19039 O O     . THR A 1 3978 ? 175.820 113.291 189.816 1.00 79.97  ? 3978 THR A O     1 
ATOM   19040 C CB    . THR A 1 3978 ? 173.374 111.219 189.550 1.00 79.97  ? 3978 THR A CB    1 
ATOM   19041 O OG1   . THR A 1 3978 ? 173.065 112.406 188.809 1.00 79.97  ? 3978 THR A OG1   1 
ATOM   19042 C CG2   . THR A 1 3978 ? 172.098 110.662 190.162 1.00 79.97  ? 3978 THR A CG2   1 
ATOM   19043 N N     . PRO A 1 3979 ? 176.602 111.197 189.631 1.00 73.91  ? 3979 PRO A N     1 
ATOM   19044 C CA    . PRO A 1 3979 ? 177.799 111.650 188.914 1.00 73.91  ? 3979 PRO A CA    1 
ATOM   19045 C C     . PRO A 1 3979 ? 177.425 112.310 187.596 1.00 73.91  ? 3979 PRO A C     1 
ATOM   19046 O O     . PRO A 1 3979 ? 176.502 111.879 186.902 1.00 73.91  ? 3979 PRO A O     1 
ATOM   19047 C CB    . PRO A 1 3979 ? 178.591 110.357 188.693 1.00 73.91  ? 3979 PRO A CB    1 
ATOM   19048 C CG    . PRO A 1 3979 ? 178.118 109.436 189.765 1.00 73.91  ? 3979 PRO A CG    1 
ATOM   19049 C CD    . PRO A 1 3979 ? 176.671 109.768 189.980 1.00 73.91  ? 3979 PRO A CD    1 
ATOM   19050 N N     . ALA A 1 3980 ? 178.156 113.365 187.254 1.00 61.91  ? 3980 ALA A N     1 
ATOM   19051 C CA    . ALA A 1 3980 ? 177.872 114.159 186.070 1.00 61.91  ? 3980 ALA A CA    1 
ATOM   19052 C C     . ALA A 1 3980 ? 178.901 113.883 184.983 1.00 61.91  ? 3980 ALA A C     1 
ATOM   19053 O O     . ALA A 1 3980 ? 179.982 113.343 185.234 1.00 61.91  ? 3980 ALA A O     1 
ATOM   19054 C CB    . ALA A 1 3980 ? 177.851 115.654 186.404 1.00 61.91  ? 3980 ALA A CB    1 
ATOM   19055 N N     . THR A 1 3981 ? 178.542 114.264 183.761 1.00 57.86  ? 3981 THR A N     1 
ATOM   19056 C CA    . THR A 1 3981 ? 179.440 114.128 182.632 1.00 57.86  ? 3981 THR A CA    1 
ATOM   19057 C C     . THR A 1 3981 ? 180.610 115.097 182.779 1.00 57.86  ? 3981 THR A C     1 
ATOM   19058 O O     . THR A 1 3981 ? 180.527 116.073 183.528 1.00 57.86  ? 3981 THR A O     1 
ATOM   19059 C CB    . THR A 1 3981 ? 178.693 114.394 181.328 1.00 57.86  ? 3981 THR A CB    1 
ATOM   19060 O OG1   . THR A 1 3981 ? 178.015 115.654 181.413 1.00 57.86  ? 3981 THR A OG1   1 
ATOM   19061 C CG2   . THR A 1 3981 ? 177.676 113.295 181.065 1.00 57.86  ? 3981 THR A CG2   1 
ATOM   19062 N N     . PRO A 1 3982 ? 181.723 114.838 182.086 1.00 53.44  ? 3982 PRO A N     1 
ATOM   19063 C CA    . PRO A 1 3982 ? 182.854 115.777 182.158 1.00 53.44  ? 3982 PRO A CA    1 
ATOM   19064 C C     . PRO A 1 3982 ? 182.487 117.194 181.757 1.00 53.44  ? 3982 PRO A C     1 
ATOM   19065 O O     . PRO A 1 3982 ? 183.083 118.146 182.273 1.00 53.44  ? 3982 PRO A O     1 
ATOM   19066 C CB    . PRO A 1 3982 ? 183.877 115.163 181.194 1.00 53.44  ? 3982 PRO A CB    1 
ATOM   19067 C CG    . PRO A 1 3982 ? 183.572 113.710 181.210 1.00 53.44  ? 3982 PRO A CG    1 
ATOM   19068 C CD    . PRO A 1 3982 ? 182.082 113.597 181.375 1.00 53.44  ? 3982 PRO A CD    1 
ATOM   19069 N N     . ILE A 1 3983 ? 181.518 117.367 180.856 1.00 46.62  ? 3983 ILE A N     1 
ATOM   19070 C CA    . ILE A 1 3983 ? 181.088 118.712 180.488 1.00 46.62  ? 3983 ILE A CA    1 
ATOM   19071 C C     . ILE A 1 3983 ? 180.378 119.388 181.655 1.00 46.62  ? 3983 ILE A C     1 
ATOM   19072 O O     . ILE A 1 3983 ? 180.564 120.585 181.902 1.00 46.62  ? 3983 ILE A O     1 
ATOM   19073 C CB    . ILE A 1 3983 ? 180.203 118.665 179.232 1.00 46.62  ? 3983 ILE A CB    1 
ATOM   19074 C CG1   . ILE A 1 3983 ? 180.850 117.782 178.164 1.00 46.62  ? 3983 ILE A CG1   1 
ATOM   19075 C CG2   . ILE A 1 3983 ? 179.983 120.067 178.696 1.00 46.62  ? 3983 ILE A CG2   1 
ATOM   19076 C CD1   . ILE A 1 3983 ? 180.071 117.712 176.872 1.00 46.62  ? 3983 ILE A CD1   1 
ATOM   19077 N N     . GLY A 1 3984 ? 179.546 118.643 182.385 1.00 47.10  ? 3984 GLY A N     1 
ATOM   19078 C CA    . GLY A 1 3984 ? 178.918 119.208 183.570 1.00 47.10  ? 3984 GLY A CA    1 
ATOM   19079 C C     . GLY A 1 3984 ? 179.927 119.564 184.644 1.00 47.10  ? 3984 GLY A C     1 
ATOM   19080 O O     . GLY A 1 3984 ? 179.801 120.592 185.318 1.00 47.10  ? 3984 GLY A O     1 
ATOM   19081 N N     . GLN A 1 3985 ? 180.945 118.718 184.816 1.00 47.76  ? 3985 GLN A N     1 
ATOM   19082 C CA    . GLN A 1 3985 ? 182.036 119.051 185.723 1.00 47.76  ? 3985 GLN A CA    1 
ATOM   19083 C C     . GLN A 1 3985 ? 182.737 120.325 185.277 1.00 47.76  ? 3985 GLN A C     1 
ATOM   19084 O O     . GLN A 1 3985 ? 183.094 121.168 186.107 1.00 47.76  ? 3985 GLN A O     1 
ATOM   19085 C CB    . GLN A 1 3985 ? 183.028 117.892 185.800 1.00 47.76  ? 3985 GLN A CB    1 
ATOM   19086 C CG    . GLN A 1 3985 ? 182.477 116.644 186.463 1.00 47.76  ? 3985 GLN A CG    1 
ATOM   19087 C CD    . GLN A 1 3985 ? 183.511 115.937 187.316 1.00 47.76  ? 3985 GLN A CD    1 
ATOM   19088 O OE1   . GLN A 1 3985 ? 184.015 116.494 188.291 1.00 47.76  ? 3985 GLN A OE1   1 
ATOM   19089 N NE2   . GLN A 1 3985 ? 183.833 114.702 186.951 1.00 47.76  ? 3985 GLN A NE2   1 
ATOM   19090 N N     . ALA A 1 3986 ? 182.941 120.482 183.968 1.00 40.04  ? 3986 ALA A N     1 
ATOM   19091 C CA    . ALA A 1 3986 ? 183.557 121.700 183.454 1.00 40.04  ? 3986 ALA A CA    1 
ATOM   19092 C C     . ALA A 1 3986 ? 182.697 122.920 183.752 1.00 40.04  ? 3986 ALA A C     1 
ATOM   19093 O O     . ALA A 1 3986 ? 183.217 123.972 184.134 1.00 40.04  ? 3986 ALA A O     1 
ATOM   19094 C CB    . ALA A 1 3986 ? 183.804 121.571 181.952 1.00 40.04  ? 3986 ALA A CB    1 
ATOM   19095 N N     . ILE A 1 3987 ? 181.378 122.798 183.589 1.00 38.87  ? 3987 ILE A N     1 
ATOM   19096 C CA    . ILE A 1 3987 ? 180.484 123.916 183.889 1.00 38.87  ? 3987 ILE A CA    1 
ATOM   19097 C C     . ILE A 1 3987 ? 180.565 124.292 185.363 1.00 38.87  ? 3987 ILE A C     1 
ATOM   19098 O O     . ILE A 1 3987 ? 180.646 125.477 185.716 1.00 38.87  ? 3987 ILE A O     1 
ATOM   19099 C CB    . ILE A 1 3987 ? 179.038 123.580 183.481 1.00 38.87  ? 3987 ILE A CB    1 
ATOM   19100 C CG1   . ILE A 1 3987 ? 178.956 123.272 181.989 1.00 38.87  ? 3987 ILE A CG1   1 
ATOM   19101 C CG2   . ILE A 1 3987 ? 178.110 124.729 183.828 1.00 38.87  ? 3987 ILE A CG2   1 
ATOM   19102 C CD1   . ILE A 1 3987 ? 179.373 124.429 181.126 1.00 38.87  ? 3987 ILE A CD1   1 
ATOM   19103 N N     . HIS A 1 3988 ? 180.535 123.295 186.247 1.00 44.06  ? 3988 HIS A N     1 
ATOM   19104 C CA    . HIS A 1 3988 ? 180.560 123.591 187.677 1.00 44.06  ? 3988 HIS A CA    1 
ATOM   19105 C C     . HIS A 1 3988 ? 181.898 124.193 188.097 1.00 44.06  ? 3988 HIS A C     1 
ATOM   19106 O O     . HIS A 1 3988 ? 181.938 125.143 188.891 1.00 44.06  ? 3988 HIS A O     1 
ATOM   19107 C CB    . HIS A 1 3988 ? 180.243 122.328 188.473 1.00 44.06  ? 3988 HIS A CB    1 
ATOM   19108 C CG    . HIS A 1 3988 ? 178.804 121.920 188.397 1.00 44.06  ? 3988 HIS A CG    1 
ATOM   19109 N ND1   . HIS A 1 3988 ? 178.088 121.502 189.498 1.00 44.06  ? 3988 HIS A ND1   1 
ATOM   19110 C CD2   . HIS A 1 3988 ? 177.945 121.877 187.352 1.00 44.06  ? 3988 HIS A CD2   1 
ATOM   19111 C CE1   . HIS A 1 3988 ? 176.852 121.213 189.132 1.00 44.06  ? 3988 HIS A CE1   1 
ATOM   19112 N NE2   . HIS A 1 3988 ? 176.739 121.433 187.835 1.00 44.06  ? 3988 HIS A NE2   1 
ATOM   19113 N N     . ARG A 1 3989 ? 183.004 123.667 187.565 1.00 37.72  ? 3989 ARG A N     1 
ATOM   19114 C CA    . ARG A 1 3989 ? 184.309 124.247 187.859 1.00 37.72  ? 3989 ARG A CA    1 
ATOM   19115 C C     . ARG A 1 3989 ? 184.432 125.655 187.293 1.00 37.72  ? 3989 ARG A C     1 
ATOM   19116 O O     . ARG A 1 3989 ? 185.079 126.510 187.904 1.00 37.72  ? 3989 ARG A O     1 
ATOM   19117 C CB    . ARG A 1 3989 ? 185.416 123.348 187.311 1.00 37.72  ? 3989 ARG A CB    1 
ATOM   19118 C CG    . ARG A 1 3989 ? 185.452 121.968 187.942 1.00 37.72  ? 3989 ARG A CG    1 
ATOM   19119 C CD    . ARG A 1 3989 ? 186.630 121.149 187.446 1.00 37.72  ? 3989 ARG A CD    1 
ATOM   19120 N NE    . ARG A 1 3989 ? 186.908 120.020 188.325 1.00 37.72  ? 3989 ARG A NE    1 
ATOM   19121 C CZ    . ARG A 1 3989 ? 187.711 119.011 188.018 1.00 37.72  ? 3989 ARG A CZ    1 
ATOM   19122 N NH1   . ARG A 1 3989 ? 188.341 118.958 186.856 1.00 37.72  ? 3989 ARG A NH1   1 
ATOM   19123 N NH2   . ARG A 1 3989 ? 187.886 118.030 188.899 1.00 37.72  ? 3989 ARG A NH2   1 
ATOM   19124 N N     . LEU A 1 3990 ? 183.821 125.915 186.135 1.00 33.39  ? 3990 LEU A N     1 
ATOM   19125 C CA    . LEU A 1 3990 ? 183.813 127.263 185.580 1.00 33.39  ? 3990 LEU A CA    1 
ATOM   19126 C C     . LEU A 1 3990 ? 183.041 128.221 186.474 1.00 33.39  ? 3990 LEU A C     1 
ATOM   19127 O O     . LEU A 1 3990 ? 183.459 129.367 186.674 1.00 33.39  ? 3990 LEU A O     1 
ATOM   19128 C CB    . LEU A 1 3990 ? 183.221 127.235 184.172 1.00 33.39  ? 3990 LEU A CB    1 
ATOM   19129 C CG    . LEU A 1 3990 ? 182.975 128.565 183.465 1.00 33.39  ? 3990 LEU A CG    1 
ATOM   19130 C CD1   . LEU A 1 3990 ? 184.285 129.158 182.985 1.00 33.39  ? 3990 LEU A CD1   1 
ATOM   19131 C CD2   . LEU A 1 3990 ? 182.021 128.362 182.302 1.00 33.39  ? 3990 LEU A CD2   1 
ATOM   19132 N N     . LEU A 1 3991 ? 181.910 127.771 187.021 1.00 35.39  ? 3991 LEU A N     1 
ATOM   19133 C CA    . LEU A 1 3991 ? 181.177 128.597 187.976 1.00 35.39  ? 3991 LEU A CA    1 
ATOM   19134 C C     . LEU A 1 3991 ? 182.019 128.881 189.215 1.00 35.39  ? 3991 LEU A C     1 
ATOM   19135 O O     . LEU A 1 3991 ? 182.046 130.014 189.714 1.00 35.39  ? 3991 LEU A O     1 
ATOM   19136 C CB    . LEU A 1 3991 ? 179.866 127.916 188.363 1.00 35.39  ? 3991 LEU A CB    1 
ATOM   19137 C CG    . LEU A 1 3991 ? 178.794 127.846 187.276 1.00 35.39  ? 3991 LEU A CG    1 
ATOM   19138 C CD1   . LEU A 1 3991 ? 177.442 127.523 187.882 1.00 35.39  ? 3991 LEU A CD1   1 
ATOM   19139 C CD2   . LEU A 1 3991 ? 178.737 129.152 186.509 1.00 35.39  ? 3991 LEU A CD2   1 
ATOM   19140 N N     . LEU A 1 3992 ? 182.719 127.863 189.721 1.00 36.62  ? 3992 LEU A N     1 
ATOM   19141 C CA    . LEU A 1 3992 ? 183.580 128.068 190.884 1.00 36.62  ? 3992 LEU A CA    1 
ATOM   19142 C C     . LEU A 1 3992 ? 184.699 129.057 190.579 1.00 36.62  ? 3992 LEU A C     1 
ATOM   19143 O O     . LEU A 1 3992 ? 185.034 129.904 191.415 1.00 36.62  ? 3992 LEU A O     1 
ATOM   19144 C CB    . LEU A 1 3992 ? 184.160 126.734 191.353 1.00 36.62  ? 3992 LEU A CB    1 
ATOM   19145 C CG    . LEU A 1 3992 ? 183.205 125.807 192.105 1.00 36.62  ? 3992 LEU A CG    1 
ATOM   19146 C CD1   . LEU A 1 3992 ? 183.931 124.558 192.573 1.00 36.62  ? 3992 LEU A CD1   1 
ATOM   19147 C CD2   . LEU A 1 3992 ? 182.574 126.534 193.279 1.00 36.62  ? 3992 LEU A CD2   1 
ATOM   19148 N N     . ILE A 1 3993 ? 185.293 128.961 189.387 1.00 31.56  ? 3993 ILE A N     1 
ATOM   19149 C CA    . ILE A 1 3993 ? 186.358 129.882 189.000 1.00 31.56  ? 3993 ILE A CA    1 
ATOM   19150 C C     . ILE A 1 3993 ? 185.812 131.297 188.849 1.00 31.56  ? 3993 ILE A C     1 
ATOM   19151 O O     . ILE A 1 3993 ? 186.491 132.278 189.174 1.00 31.56  ? 3993 ILE A O     1 
ATOM   19152 C CB    . ILE A 1 3993 ? 187.041 129.388 187.712 1.00 31.56  ? 3993 ILE A CB    1 
ATOM   19153 C CG1   . ILE A 1 3993 ? 187.871 128.138 187.999 1.00 31.56  ? 3993 ILE A CG1   1 
ATOM   19154 C CG2   . ILE A 1 3993 ? 187.923 130.469 187.116 1.00 31.56  ? 3993 ILE A CG2   1 
ATOM   19155 C CD1   . ILE A 1 3993 ? 188.971 128.358 189.006 1.00 31.56  ? 3993 ILE A CD1   1 
ATOM   19156 N N     . GLN A 1 3994 ? 184.581 131.429 188.353 1.00 33.93  ? 3994 GLN A N     1 
ATOM   19157 C CA    . GLN A 1 3994 ? 183.949 132.742 188.319 1.00 33.93  ? 3994 GLN A CA    1 
ATOM   19158 C C     . GLN A 1 3994 ? 183.738 133.287 189.724 1.00 33.93  ? 3994 GLN A C     1 
ATOM   19159 O O     . GLN A 1 3994 ? 183.851 134.498 189.945 1.00 33.93  ? 3994 GLN A O     1 
ATOM   19160 C CB    . GLN A 1 3994 ? 182.621 132.673 187.565 1.00 33.93  ? 3994 GLN A CB    1 
ATOM   19161 C CG    . GLN A 1 3994 ? 181.934 134.018 187.411 1.00 33.93  ? 3994 GLN A CG    1 
ATOM   19162 C CD    . GLN A 1 3994 ? 180.625 133.923 186.657 1.00 33.93  ? 3994 GLN A CD    1 
ATOM   19163 O OE1   . GLN A 1 3994 ? 179.705 133.222 187.074 1.00 33.93  ? 3994 GLN A OE1   1 
ATOM   19164 N NE2   . GLN A 1 3994 ? 180.534 134.635 185.541 1.00 33.93  ? 3994 GLN A NE2   1 
ATOM   19165 N N     . ALA A 1 3995 ? 183.437 132.412 190.686 1.00 34.53  ? 3995 ALA A N     1 
ATOM   19166 C CA    . ALA A 1 3995 ? 183.300 132.850 192.072 1.00 34.53  ? 3995 ALA A CA    1 
ATOM   19167 C C     . ALA A 1 3995 ? 184.663 133.097 192.714 1.00 34.53  ? 3995 ALA A C     1 
ATOM   19168 O O     . ALA A 1 3995 ? 184.955 134.208 193.169 1.00 34.53  ? 3995 ALA A O     1 
ATOM   19169 C CB    . ALA A 1 3995 ? 182.505 131.817 192.873 1.00 34.53  ? 3995 ALA A CB    1 
ATOM   19170 N N     . PHE A 1 3996 ? 185.510 132.072 192.756 1.00 37.52  ? 3996 PHE A N     1 
ATOM   19171 C CA    . PHE A 1 3996 ? 186.839 132.167 193.348 1.00 37.52  ? 3996 PHE A CA    1 
ATOM   19172 C C     . PHE A 1 3996 ? 187.873 132.410 192.259 1.00 37.52  ? 3996 PHE A C     1 
ATOM   19173 O O     . PHE A 1 3996 ? 187.966 131.631 191.305 1.00 37.52  ? 3996 PHE A O     1 
ATOM   19174 C CB    . PHE A 1 3996 ? 187.193 130.890 194.111 1.00 37.52  ? 3996 PHE A CB    1 
ATOM   19175 C CG    . PHE A 1 3996 ? 186.142 130.450 195.080 1.00 37.52  ? 3996 PHE A CG    1 
ATOM   19176 C CD1   . PHE A 1 3996 ? 185.789 131.252 196.147 1.00 37.52  ? 3996 PHE A CD1   1 
ATOM   19177 C CD2   . PHE A 1 3996 ? 185.511 129.228 194.928 1.00 37.52  ? 3996 PHE A CD2   1 
ATOM   19178 C CE1   . PHE A 1 3996 ? 184.825 130.847 197.041 1.00 37.52  ? 3996 PHE A CE1   1 
ATOM   19179 C CE2   . PHE A 1 3996 ? 184.544 128.817 195.822 1.00 37.52  ? 3996 PHE A CE2   1 
ATOM   19180 C CZ    . PHE A 1 3996 ? 184.200 129.628 196.879 1.00 37.52  ? 3996 PHE A CZ    1 
ATOM   19181 N N     . ARG A 1 3997 ? 188.664 133.473 192.418 1.00 28.22  ? 3997 ARG A N     1 
ATOM   19182 C CA    . ARG A 1 3997 ? 189.710 133.831 191.466 1.00 28.22  ? 3997 ARG A CA    1 
ATOM   19183 C C     . ARG A 1 3997 ? 189.123 134.052 190.077 1.00 28.22  ? 3997 ARG A C     1 
ATOM   19184 O O     . ARG A 1 3997 ? 189.342 133.234 189.175 1.00 28.22  ? 3997 ARG A O     1 
ATOM   19185 C CB    . ARG A 1 3997 ? 190.792 132.750 191.418 1.00 28.22  ? 3997 ARG A CB    1 
ATOM   19186 C CG    . ARG A 1 3997 ? 191.716 132.737 192.621 1.00 28.22  ? 3997 ARG A CG    1 
ATOM   19187 C CD    . ARG A 1 3997 ? 192.607 133.966 192.636 1.00 28.22  ? 3997 ARG A CD    1 
ATOM   19188 N NE    . ARG A 1 3997 ? 193.538 133.976 191.513 1.00 28.22  ? 3997 ARG A NE    1 
ATOM   19189 C CZ    . ARG A 1 3997 ? 194.627 133.225 191.435 1.00 28.22  ? 3997 ARG A CZ    1 
ATOM   19190 N NH1   . ARG A 1 3997 ? 194.968 132.398 192.409 1.00 28.22  ? 3997 ARG A NH1   1 
ATOM   19191 N NH2   . ARG A 1 3997 ? 195.396 133.309 190.354 1.00 28.22  ? 3997 ARG A NH2   1 
ATOM   19192 N N     . PRO A 1 3998 ? 188.372 135.135 189.863 1.00 26.64  ? 3998 PRO A N     1 
ATOM   19193 C CA    . PRO A 1 3998 ? 187.796 135.373 188.531 1.00 26.64  ? 3998 PRO A CA    1 
ATOM   19194 C C     . PRO A 1 3998 ? 188.827 135.717 187.473 1.00 26.64  ? 3998 PRO A C     1 
ATOM   19195 O O     . PRO A 1 3998 ? 188.481 135.756 186.286 1.00 26.64  ? 3998 PRO A O     1 
ATOM   19196 C CB    . PRO A 1 3998 ? 186.831 136.541 188.771 1.00 26.64  ? 3998 PRO A CB    1 
ATOM   19197 C CG    . PRO A 1 3998 ? 187.403 137.255 189.943 1.00 26.64  ? 3998 PRO A CG    1 
ATOM   19198 C CD    . PRO A 1 3998 ? 188.009 136.195 190.819 1.00 26.64  ? 3998 PRO A CD    1 
ATOM   19199 N N     . ASP A 1 3999 ? 190.077 135.983 187.858 1.00 24.55  ? 3999 ASP A N     1 
ATOM   19200 C CA    . ASP A 1 3999 ? 191.099 136.301 186.867 1.00 24.55  ? 3999 ASP A CA    1 
ATOM   19201 C C     . ASP A 1 3999 ? 191.401 135.111 185.967 1.00 24.55  ? 3999 ASP A C     1 
ATOM   19202 O O     . ASP A 1 3999 ? 191.740 135.292 184.793 1.00 24.55  ? 3999 ASP A O     1 
ATOM   19203 C CB    . ASP A 1 3999 ? 192.373 136.781 187.559 1.00 24.55  ? 3999 ASP A CB    1 
ATOM   19204 C CG    . ASP A 1 3999 ? 192.873 135.803 188.599 1.00 24.55  ? 3999 ASP A CG    1 
ATOM   19205 O OD1   . ASP A 1 3999 ? 192.183 135.619 189.623 1.00 24.55  ? 3999 ASP A OD1   1 
ATOM   19206 O OD2   . ASP A 1 3999 ? 193.957 135.220 188.396 1.00 24.55  ? 3999 ASP A OD2   1 
ATOM   19207 N N     . ARG A 1 4000 ? 191.284 133.894 186.491 1.00 26.97  ? 4000 ARG A N     1 
ATOM   19208 C CA    . ARG A 1 4000 ? 191.505 132.688 185.706 1.00 26.97  ? 4000 ARG A CA    1 
ATOM   19209 C C     . ARG A 1 4000 ? 190.270 132.258 184.927 1.00 26.97  ? 4000 ARG A C     1 
ATOM   19210 O O     . ARG A 1 4000 ? 190.202 131.104 184.487 1.00 26.97  ? 4000 ARG A O     1 
ATOM   19211 C CB    . ARG A 1 4000 ? 191.963 131.545 186.615 1.00 26.97  ? 4000 ARG A CB    1 
ATOM   19212 C CG    . ARG A 1 4000 ? 192.994 131.956 187.647 1.00 26.97  ? 4000 ARG A CG    1 
ATOM   19213 C CD    . ARG A 1 4000 ? 194.311 132.352 187.001 1.00 26.97  ? 4000 ARG A CD    1 
ATOM   19214 N NE    . ARG A 1 4000 ? 194.965 131.224 186.349 1.00 26.97  ? 4000 ARG A NE    1 
ATOM   19215 C CZ    . ARG A 1 4000 ? 195.430 131.244 185.108 1.00 26.97  ? 4000 ARG A CZ    1 
ATOM   19216 N NH1   . ARG A 1 4000 ? 195.329 132.322 184.349 1.00 26.97  ? 4000 ARG A NH1   1 
ATOM   19217 N NH2   . ARG A 1 4000 ? 196.013 130.155 184.616 1.00 26.97  ? 4000 ARG A NH2   1 
ATOM   19218 N N     . LEU A 1 4001 ? 189.294 133.152 184.754 1.00 26.90  ? 4001 LEU A N     1 
ATOM   19219 C CA    . LEU A 1 4001 ? 188.075 132.795 184.037 1.00 26.90  ? 4001 LEU A CA    1 
ATOM   19220 C C     . LEU A 1 4001 ? 188.367 132.483 182.575 1.00 26.90  ? 4001 LEU A C     1 
ATOM   19221 O O     . LEU A 1 4001 ? 187.773 131.571 181.996 1.00 26.90  ? 4001 LEU A O     1 
ATOM   19222 C CB    . LEU A 1 4001 ? 187.046 133.918 184.151 1.00 26.90  ? 4001 LEU A CB    1 
ATOM   19223 C CG    . LEU A 1 4001 ? 185.639 133.544 183.686 1.00 26.90  ? 4001 LEU A CG    1 
ATOM   19224 C CD1   . LEU A 1 4001 ? 185.060 132.469 184.587 1.00 26.90  ? 4001 LEU A CD1   1 
ATOM   19225 C CD2   . LEU A 1 4001 ? 184.741 134.766 183.658 1.00 26.90  ? 4001 LEU A CD2   1 
ATOM   19226 N N     . LEU A 1 4002 ? 189.275 133.242 181.958 1.00 25.18  ? 4002 LEU A N     1 
ATOM   19227 C CA    . LEU A 1 4002 ? 189.636 132.976 180.568 1.00 25.18  ? 4002 LEU A CA    1 
ATOM   19228 C C     . LEU A 1 4002 ? 190.289 131.606 180.422 1.00 25.18  ? 4002 LEU A C     1 
ATOM   19229 O O     . LEU A 1 4002 ? 189.987 130.855 179.488 1.00 25.18  ? 4002 LEU A O     1 
ATOM   19230 C CB    . LEU A 1 4002 ? 190.565 134.072 180.049 1.00 25.18  ? 4002 LEU A CB    1 
ATOM   19231 C CG    . LEU A 1 4002 ? 189.963 135.469 179.914 1.00 25.18  ? 4002 LEU A CG    1 
ATOM   19232 C CD1   . LEU A 1 4002 ? 191.014 136.440 179.413 1.00 25.18  ? 4002 LEU A CD1   1 
ATOM   19233 C CD2   . LEU A 1 4002 ? 188.763 135.447 178.986 1.00 25.18  ? 4002 LEU A CD2   1 
ATOM   19234 N N     . ALA A 1 4003 ? 191.192 131.264 181.342 1.00 27.07  ? 4003 ALA A N     1 
ATOM   19235 C CA    . ALA A 1 4003 ? 191.846 129.961 181.289 1.00 27.07  ? 4003 ALA A CA    1 
ATOM   19236 C C     . ALA A 1 4003 ? 190.844 128.835 181.511 1.00 27.07  ? 4003 ALA A C     1 
ATOM   19237 O O     . ALA A 1 4003 ? 190.897 127.795 180.841 1.00 27.07  ? 4003 ALA A O     1 
ATOM   19238 C CB    . ALA A 1 4003 ? 192.970 129.899 182.321 1.00 27.07  ? 4003 ALA A CB    1 
ATOM   19239 N N     . MET A 1 4004 ? 189.918 129.023 182.453 1.00 28.29  ? 4004 MET A N     1 
ATOM   19240 C CA    . MET A 1 4004 ? 188.908 127.997 182.682 1.00 28.29  ? 4004 MET A CA    1 
ATOM   19241 C C     . MET A 1 4004 ? 187.965 127.875 181.492 1.00 28.29  ? 4004 MET A C     1 
ATOM   19242 O O     . MET A 1 4004 ? 187.492 126.776 181.183 1.00 28.29  ? 4004 MET A O     1 
ATOM   19243 C CB    . MET A 1 4004 ? 188.125 128.295 183.958 1.00 28.29  ? 4004 MET A CB    1 
ATOM   19244 C CG    . MET A 1 4004 ? 187.183 127.176 184.354 1.00 28.29  ? 4004 MET A CG    1 
ATOM   19245 S SD    . MET A 1 4004 ? 187.898 125.555 184.020 1.00 28.29  ? 4004 MET A SD    1 
ATOM   19246 C CE    . MET A 1 4004 ? 186.443 124.519 184.089 1.00 28.29  ? 4004 MET A CE    1 
ATOM   19247 N N     . ALA A 1 4005 ? 187.685 128.984 180.807 1.00 23.35  ? 4005 ALA A N     1 
ATOM   19248 C CA    . ALA A 1 4005 ? 186.895 128.927 179.584 1.00 23.35  ? 4005 ALA A CA    1 
ATOM   19249 C C     . ALA A 1 4005 ? 187.637 128.165 178.494 1.00 23.35  ? 4005 ALA A C     1 
ATOM   19250 O O     . ALA A 1 4005 ? 187.035 127.409 177.727 1.00 23.35  ? 4005 ALA A O     1 
ATOM   19251 C CB    . ALA A 1 4005 ? 186.547 130.341 179.118 1.00 23.35  ? 4005 ALA A CB    1 
ATOM   19252 N N     . HIS A 1 4006 ? 188.954 128.361 178.410 1.00 22.92  ? 4006 HIS A N     1 
ATOM   19253 C CA    . HIS A 1 4006 ? 189.756 127.579 177.472 1.00 22.92  ? 4006 HIS A CA    1 
ATOM   19254 C C     . HIS A 1 4006 ? 189.668 126.092 177.792 1.00 22.92  ? 4006 HIS A C     1 
ATOM   19255 O O     . HIS A 1 4006 ? 189.528 125.257 176.891 1.00 22.92  ? 4006 HIS A O     1 
ATOM   19256 C CB    . HIS A 1 4006 ? 191.212 128.046 177.493 1.00 22.92  ? 4006 HIS A CB    1 
ATOM   19257 C CG    . HIS A 1 4006 ? 191.437 129.368 176.827 1.00 22.92  ? 4006 HIS A CG    1 
ATOM   19258 N ND1   . HIS A 1 4006 ? 191.015 129.634 175.543 1.00 22.92  ? 4006 HIS A ND1   1 
ATOM   19259 C CD2   . HIS A 1 4006 ? 192.055 130.492 177.260 1.00 22.92  ? 4006 HIS A CD2   1 
ATOM   19260 C CE1   . HIS A 1 4006 ? 191.355 130.869 175.217 1.00 22.92  ? 4006 HIS A CE1   1 
ATOM   19261 N NE2   . HIS A 1 4006 ? 191.987 131.411 176.242 1.00 22.92  ? 4006 HIS A NE2   1 
ATOM   19262 N N     . MET A 1 4007 ? 189.744 125.741 179.077 1.00 25.31  ? 4007 MET A N     1 
ATOM   19263 C CA    . MET A 1 4007 ? 189.631 124.334 179.456 1.00 25.31  ? 4007 MET A CA    1 
ATOM   19264 C C     . MET A 1 4007 ? 188.247 123.779 179.139 1.00 25.31  ? 4007 MET A C     1 
ATOM   19265 O O     . MET A 1 4007 ? 188.111 122.625 178.720 1.00 25.31  ? 4007 MET A O     1 
ATOM   19266 C CB    . MET A 1 4007 ? 189.954 124.137 180.936 1.00 25.31  ? 4007 MET A CB    1 
ATOM   19267 C CG    . MET A 1 4007 ? 191.393 124.409 181.304 1.00 25.31  ? 4007 MET A CG    1 
ATOM   19268 S SD    . MET A 1 4007 ? 191.641 124.219 183.073 1.00 25.31  ? 4007 MET A SD    1 
ATOM   19269 C CE    . MET A 1 4007 ? 191.480 122.444 183.242 1.00 25.31  ? 4007 MET A CE    1 
ATOM   19270 N N     . PHE A 1 4008 ? 187.201 124.577 179.359 1.00 22.28  ? 4008 PHE A N     1 
ATOM   19271 C CA    . PHE A 1 4008 ? 185.853 124.120 179.035 1.00 22.28  ? 4008 PHE A CA    1 
ATOM   19272 C C     . PHE A 1 4008 ? 185.689 123.909 177.536 1.00 22.28  ? 4008 PHE A C     1 
ATOM   19273 O O     . PHE A 1 4008 ? 185.057 122.938 177.103 1.00 22.28  ? 4008 PHE A O     1 
ATOM   19274 C CB    . PHE A 1 4008 ? 184.814 125.111 179.554 1.00 22.28  ? 4008 PHE A CB    1 
ATOM   19275 C CG    . PHE A 1 4008 ? 183.465 124.950 178.923 1.00 22.28  ? 4008 PHE A CG    1 
ATOM   19276 C CD1   . PHE A 1 4008 ? 182.712 123.813 179.149 1.00 22.28  ? 4008 PHE A CD1   1 
ATOM   19277 C CD2   . PHE A 1 4008 ? 182.947 125.935 178.105 1.00 22.28  ? 4008 PHE A CD2   1 
ATOM   19278 C CE1   . PHE A 1 4008 ? 181.472 123.659 178.564 1.00 22.28  ? 4008 PHE A CE1   1 
ATOM   19279 C CE2   . PHE A 1 4008 ? 181.705 125.791 177.522 1.00 22.28  ? 4008 PHE A CE2   1 
ATOM   19280 C CZ    . PHE A 1 4008 ? 180.966 124.652 177.753 1.00 22.28  ? 4008 PHE A CZ    1 
ATOM   19281 N N     . VAL A 1 4009 ? 186.246 124.812 176.728 1.00 19.80  ? 4009 VAL A N     1 
ATOM   19282 C CA    . VAL A 1 4009 ? 186.224 124.631 175.280 1.00 19.80  ? 4009 VAL A CA    1 
ATOM   19283 C C     . VAL A 1 4009 ? 186.970 123.361 174.897 1.00 19.80  ? 4009 VAL A C     1 
ATOM   19284 O O     . VAL A 1 4009 ? 186.532 122.606 174.022 1.00 19.80  ? 4009 VAL A O     1 
ATOM   19285 C CB    . VAL A 1 4009 ? 186.808 125.871 174.578 1.00 19.80  ? 4009 VAL A CB    1 
ATOM   19286 C CG1   . VAL A 1 4009 ? 187.092 125.575 173.117 1.00 19.80  ? 4009 VAL A CG1   1 
ATOM   19287 C CG2   . VAL A 1 4009 ? 185.854 127.043 174.706 1.00 19.80  ? 4009 VAL A CG2   1 
ATOM   19288 N N     . SER A 1 4010 ? 188.103 123.099 175.550 1.00 21.43  ? 4010 SER A N     1 
ATOM   19289 C CA    . SER A 1 4010 ? 188.843 121.870 175.291 1.00 21.43  ? 4010 SER A CA    1 
ATOM   19290 C C     . SER A 1 4010 ? 188.050 120.623 175.662 1.00 21.43  ? 4010 SER A C     1 
ATOM   19291 O O     . SER A 1 4010 ? 188.105 119.629 174.931 1.00 21.43  ? 4010 SER A O     1 
ATOM   19292 C CB    . SER A 1 4010 ? 190.168 121.885 176.050 1.00 21.43  ? 4010 SER A CB    1 
ATOM   19293 O OG    . SER A 1 4010 ? 189.954 121.795 177.447 1.00 21.43  ? 4010 SER A OG    1 
ATOM   19294 N N     . THR A 1 4011 ? 187.329 120.644 176.779 1.00 20.96  ? 4011 THR A N     1 
ATOM   19295 C CA    . THR A 1 4011 ? 186.547 119.491 177.208 1.00 20.96  ? 4011 THR A CA    1 
ATOM   19296 C C     . THR A 1 4011 ? 185.260 119.309 176.416 1.00 20.96  ? 4011 THR A C     1 
ATOM   19297 O O     . THR A 1 4011 ? 184.727 118.195 176.382 1.00 20.96  ? 4011 THR A O     1 
ATOM   19298 C CB    . THR A 1 4011 ? 186.202 119.597 178.697 1.00 20.96  ? 4011 THR A CB    1 
ATOM   19299 O OG1   . THR A 1 4011 ? 185.464 120.801 178.936 1.00 20.96  ? 4011 THR A OG1   1 
ATOM   19300 C CG2   . THR A 1 4011 ? 187.465 119.596 179.543 1.00 20.96  ? 4011 THR A CG2   1 
ATOM   19301 N N     . ASN A 1 4012 ? 184.748 120.362 175.786 1.00 21.02  ? 4012 ASN A N     1 
ATOM   19302 C CA    . ASN A 1 4012 ? 183.505 120.271 175.031 1.00 21.02  ? 4012 ASN A CA    1 
ATOM   19303 C C     . ASN A 1 4012 ? 183.737 120.044 173.546 1.00 21.02  ? 4012 ASN A C     1 
ATOM   19304 O O     . ASN A 1 4012 ? 183.221 119.070 172.986 1.00 21.02  ? 4012 ASN A O     1 
ATOM   19305 C CB    . ASN A 1 4012 ? 182.671 121.544 175.247 1.00 21.02  ? 4012 ASN A CB    1 
ATOM   19306 C CG    . ASN A 1 4012 ? 181.243 121.395 174.768 1.00 21.02  ? 4012 ASN A CG    1 
ATOM   19307 O OD1   . ASN A 1 4012 ? 180.856 120.351 174.244 1.00 21.02  ? 4012 ASN A OD1   1 
ATOM   19308 N ND2   . ASN A 1 4012 ? 180.447 122.439 174.955 1.00 21.02  ? 4012 ASN A ND2   1 
ATOM   19309 N N     . LEU A 1 4013 ? 184.497 120.915 172.889 1.00 20.42  ? 4013 LEU A N     1 
ATOM   19310 C CA    . LEU A 1 4013 ? 184.778 120.804 171.464 1.00 20.42  ? 4013 LEU A CA    1 
ATOM   19311 C C     . LEU A 1 4013 ? 186.036 120.003 171.163 1.00 20.42  ? 4013 LEU A C     1 
ATOM   19312 O O     . LEU A 1 4013 ? 186.386 119.846 169.989 1.00 20.42  ? 4013 LEU A O     1 
ATOM   19313 C CB    . LEU A 1 4013 ? 184.901 122.200 170.847 1.00 20.42  ? 4013 LEU A CB    1 
ATOM   19314 C CG    . LEU A 1 4013 ? 183.616 123.023 170.834 1.00 20.42  ? 4013 LEU A CG    1 
ATOM   19315 C CD1   . LEU A 1 4013 ? 183.811 124.315 170.074 1.00 20.42  ? 4013 LEU A CD1   1 
ATOM   19316 C CD2   . LEU A 1 4013 ? 182.511 122.210 170.205 1.00 20.42  ? 4013 LEU A CD2   1 
ATOM   19317 N N     . GLY A 1 4014 ? 186.718 119.499 172.178 1.00 21.30  ? 4014 GLY A N     1 
ATOM   19318 C CA    . GLY A 1 4014 ? 187.929 118.732 171.936 1.00 21.30  ? 4014 GLY A CA    1 
ATOM   19319 C C     . GLY A 1 4014 ? 189.186 119.552 172.145 1.00 21.30  ? 4014 GLY A C     1 
ATOM   19320 O O     . GLY A 1 4014 ? 189.228 120.760 171.912 1.00 21.30  ? 4014 GLY A O     1 
ATOM   19321 N N     . GLU A 1 4015 ? 190.233 118.872 172.602 1.00 28.14  ? 4015 GLU A N     1 
ATOM   19322 C CA    . GLU A 1 4015 ? 191.523 119.508 172.813 1.00 28.14  ? 4015 GLU A CA    1 
ATOM   19323 C C     . GLU A 1 4015 ? 192.098 119.990 171.484 1.00 28.14  ? 4015 GLU A C     1 
ATOM   19324 O O     . GLU A 1 4015 ? 191.805 119.446 170.416 1.00 28.14  ? 4015 GLU A O     1 
ATOM   19325 C CB    . GLU A 1 4015 ? 192.489 118.536 173.497 1.00 28.14  ? 4015 GLU A CB    1 
ATOM   19326 C CG    . GLU A 1 4015 ? 193.869 119.103 173.812 1.00 28.14  ? 4015 GLU A CG    1 
ATOM   19327 C CD    . GLU A 1 4015 ? 193.833 120.223 174.833 1.00 28.14  ? 4015 GLU A CD    1 
ATOM   19328 O OE1   . GLU A 1 4015 ? 192.890 120.257 175.650 1.00 28.14  ? 4015 GLU A OE1   1 
ATOM   19329 O OE2   . GLU A 1 4015 ? 194.749 121.072 174.817 1.00 28.14  ? 4015 GLU A OE2   1 
ATOM   19330 N N     . SER A 1 4016 ? 192.911 121.044 171.562 1.00 28.00  ? 4016 SER A N     1 
ATOM   19331 C CA    . SER A 1 4016 ? 193.568 121.658 170.410 1.00 28.00  ? 4016 SER A CA    1 
ATOM   19332 C C     . SER A 1 4016 ? 192.570 122.263 169.428 1.00 28.00  ? 4016 SER A C     1 
ATOM   19333 O O     . SER A 1 4016 ? 192.859 122.372 168.233 1.00 28.00  ? 4016 SER A O     1 
ATOM   19334 C CB    . SER A 1 4016 ? 194.484 120.663 169.684 1.00 28.00  ? 4016 SER A CB    1 
ATOM   19335 O OG    . SER A 1 4016 ? 193.731 119.683 168.992 1.00 28.00  ? 4016 SER A OG    1 
ATOM   19336 N N     . PHE A 1 4017 ? 191.387 122.646 169.914 1.00 22.33  ? 4017 PHE A N     1 
ATOM   19337 C CA    . PHE A 1 4017 ? 190.441 123.367 169.069 1.00 22.33  ? 4017 PHE A CA    1 
ATOM   19338 C C     . PHE A 1 4017 ? 190.992 124.732 168.678 1.00 22.33  ? 4017 PHE A C     1 
ATOM   19339 O O     . PHE A 1 4017 ? 190.846 125.164 167.529 1.00 22.33  ? 4017 PHE A O     1 
ATOM   19340 C CB    . PHE A 1 4017 ? 189.103 123.512 169.792 1.00 22.33  ? 4017 PHE A CB    1 
ATOM   19341 C CG    . PHE A 1 4017 ? 187.981 123.969 168.908 1.00 22.33  ? 4017 PHE A CG    1 
ATOM   19342 C CD1   . PHE A 1 4017 ? 187.413 123.105 167.990 1.00 22.33  ? 4017 PHE A CD1   1 
ATOM   19343 C CD2   . PHE A 1 4017 ? 187.489 125.259 168.998 1.00 22.33  ? 4017 PHE A CD2   1 
ATOM   19344 C CE1   . PHE A 1 4017 ? 186.380 123.518 167.178 1.00 22.33  ? 4017 PHE A CE1   1 
ATOM   19345 C CE2   . PHE A 1 4017 ? 186.456 125.678 168.187 1.00 22.33  ? 4017 PHE A CE2   1 
ATOM   19346 C CZ    . PHE A 1 4017 ? 185.901 124.806 167.276 1.00 22.33  ? 4017 PHE A CZ    1 
ATOM   19347 N N     . MET A 1 4018 ? 191.631 125.420 169.621 1.00 28.14  ? 4018 MET A N     1 
ATOM   19348 C CA    . MET A 1 4018 ? 192.260 126.711 169.385 1.00 28.14  ? 4018 MET A CA    1 
ATOM   19349 C C     . MET A 1 4018 ? 193.730 126.600 169.002 1.00 28.14  ? 4018 MET A C     1 
ATOM   19350 O O     . MET A 1 4018 ? 194.378 127.631 168.798 1.00 28.14  ? 4018 MET A O     1 
ATOM   19351 C CB    . MET A 1 4018 ? 192.130 127.590 170.631 1.00 28.14  ? 4018 MET A CB    1 
ATOM   19352 C CG    . MET A 1 4018 ? 190.797 127.474 171.346 1.00 28.14  ? 4018 MET A CG    1 
ATOM   19353 S SD    . MET A 1 4018 ? 190.423 128.960 172.294 1.00 28.14  ? 4018 MET A SD    1 
ATOM   19354 C CE    . MET A 1 4018 ? 189.610 129.967 171.062 1.00 28.14  ? 4018 MET A CE    1 
ATOM   19355 N N     . SER A 1 4019 ? 194.269 125.384 168.895 1.00 31.56  ? 4019 SER A N     1 
ATOM   19356 C CA    . SER A 1 4019 ? 195.693 125.232 168.612 1.00 31.56  ? 4019 SER A CA    1 
ATOM   19357 C C     . SER A 1 4019 ? 196.064 125.779 167.239 1.00 31.56  ? 4019 SER A C     1 
ATOM   19358 O O     . SER A 1 4019 ? 197.177 126.284 167.058 1.00 31.56  ? 4019 SER A O     1 
ATOM   19359 C CB    . SER A 1 4019 ? 196.097 123.763 168.720 1.00 31.56  ? 4019 SER A CB    1 
ATOM   19360 O OG    . SER A 1 4019 ? 195.615 123.022 167.614 1.00 31.56  ? 4019 SER A OG    1 
ATOM   19361 N N     . ILE A 1 4020 ? 195.160 125.685 166.262 1.00 32.39  ? 4020 ILE A N     1 
ATOM   19362 C CA    . ILE A 1 4020 ? 195.474 126.179 164.924 1.00 32.39  ? 4020 ILE A CA    1 
ATOM   19363 C C     . ILE A 1 4020 ? 195.661 127.690 164.932 1.00 32.39  ? 4020 ILE A C     1 
ATOM   19364 O O     . ILE A 1 4020 ? 196.503 128.223 164.198 1.00 32.39  ? 4020 ILE A O     1 
ATOM   19365 C CB    . ILE A 1 4020 ? 194.393 125.736 163.921 1.00 32.39  ? 4020 ILE A CB    1 
ATOM   19366 C CG1   . ILE A 1 4020 ? 194.698 124.324 163.415 1.00 32.39  ? 4020 ILE A CG1   1 
ATOM   19367 C CG2   . ILE A 1 4020 ? 194.286 126.713 162.759 1.00 32.39  ? 4020 ILE A CG2   1 
ATOM   19368 C CD1   . ILE A 1 4020 ? 193.543 123.653 162.715 1.00 32.39  ? 4020 ILE A CD1   1 
ATOM   19369 N N     . MET A 1 4021 ? 194.904 128.402 165.767 1.00 31.75  ? 4021 MET A N     1 
ATOM   19370 C CA    . MET A 1 4021 ? 195.044 129.852 165.843 1.00 31.75  ? 4021 MET A CA    1 
ATOM   19371 C C     . MET A 1 4021 ? 196.428 130.253 166.340 1.00 31.75  ? 4021 MET A C     1 
ATOM   19372 O O     . MET A 1 4021 ? 196.994 131.252 165.882 1.00 31.75  ? 4021 MET A O     1 
ATOM   19373 C CB    . MET A 1 4021 ? 193.958 130.421 166.755 1.00 31.75  ? 4021 MET A CB    1 
ATOM   19374 C CG    . MET A 1 4021 ? 192.613 130.629 166.070 1.00 31.75  ? 4021 MET A CG    1 
ATOM   19375 S SD    . MET A 1 4021 ? 192.723 130.914 164.294 1.00 31.75  ? 4021 MET A SD    1 
ATOM   19376 C CE    . MET A 1 4021 ? 193.385 132.579 164.278 1.00 31.75  ? 4021 MET A CE    1 
ATOM   19377 N N     . GLU A 1 4022 ? 196.992 129.482 167.274 1.00 38.76  ? 4022 GLU A N     1 
ATOM   19378 C CA    . GLU A 1 4022 ? 198.308 129.809 167.817 1.00 38.76  ? 4022 GLU A CA    1 
ATOM   19379 C C     . GLU A 1 4022 ? 199.406 129.648 166.773 1.00 38.76  ? 4022 GLU A C     1 
ATOM   19380 O O     . GLU A 1 4022 ? 200.432 130.335 166.841 1.00 38.76  ? 4022 GLU A O     1 
ATOM   19381 C CB    . GLU A 1 4022 ? 198.602 128.936 169.040 1.00 38.76  ? 4022 GLU A CB    1 
ATOM   19382 C CG    . GLU A 1 4022 ? 197.411 128.666 169.978 1.00 38.76  ? 4022 GLU A CG    1 
ATOM   19383 C CD    . GLU A 1 4022 ? 196.552 129.888 170.316 1.00 38.76  ? 4022 GLU A CD    1 
ATOM   19384 O OE1   . GLU A 1 4022 ? 197.015 131.041 170.186 1.00 38.76  ? 4022 GLU A OE1   1 
ATOM   19385 O OE2   . GLU A 1 4022 ? 195.379 129.684 170.695 1.00 38.76  ? 4022 GLU A OE2   1 
ATOM   19386 N N     . GLN A 1 4023 ? 199.219 128.741 165.819 1.00 40.43  ? 4023 GLN A N     1 
ATOM   19387 C CA    . GLN A 1 4023 ? 200.174 128.582 164.736 1.00 40.43  ? 4023 GLN A CA    1 
ATOM   19388 C C     . GLN A 1 4023 ? 200.147 129.810 163.827 1.00 40.43  ? 4023 GLN A C     1 
ATOM   19389 O O     . GLN A 1 4023 ? 199.133 130.507 163.744 1.00 40.43  ? 4023 GLN A O     1 
ATOM   19390 C CB    . GLN A 1 4023 ? 199.856 127.329 163.925 1.00 40.43  ? 4023 GLN A CB    1 
ATOM   19391 C CG    . GLN A 1 4023 ? 200.468 126.060 164.487 1.00 40.43  ? 4023 GLN A CG    1 
ATOM   19392 C CD    . GLN A 1 4023 ? 199.556 124.859 164.344 1.00 40.43  ? 4023 GLN A CD    1 
ATOM   19393 O OE1   . GLN A 1 4023 ? 198.447 124.964 163.821 1.00 40.43  ? 4023 GLN A OE1   1 
ATOM   19394 N NE2   . GLN A 1 4023 ? 200.022 123.707 164.810 1.00 40.43  ? 4023 GLN A NE2   1 
ATOM   19395 N N     . PRO A 1 4024 ? 201.254 130.103 163.144 1.00 43.15  ? 4024 PRO A N     1 
ATOM   19396 C CA    . PRO A 1 4024 ? 201.280 131.269 162.256 1.00 43.15  ? 4024 PRO A CA    1 
ATOM   19397 C C     . PRO A 1 4024 ? 200.287 131.123 161.113 1.00 43.15  ? 4024 PRO A C     1 
ATOM   19398 O O     . PRO A 1 4024 ? 199.995 130.023 160.638 1.00 43.15  ? 4024 PRO A O     1 
ATOM   19399 C CB    . PRO A 1 4024 ? 202.725 131.294 161.741 1.00 43.15  ? 4024 PRO A CB    1 
ATOM   19400 C CG    . PRO A 1 4024 ? 203.207 129.892 161.904 1.00 43.15  ? 4024 PRO A CG    1 
ATOM   19401 C CD    . PRO A 1 4024 ? 202.541 129.388 163.147 1.00 43.15  ? 4024 PRO A CD    1 
ATOM   19402 N N     . LEU A 1 4025 ? 199.760 132.264 160.675 1.00 38.57  ? 4025 LEU A N     1 
ATOM   19403 C CA    . LEU A 1 4025 ? 198.755 132.296 159.616 1.00 38.57  ? 4025 LEU A CA    1 
ATOM   19404 C C     . LEU A 1 4025 ? 199.421 131.928 158.298 1.00 38.57  ? 4025 LEU A C     1 
ATOM   19405 O O     . LEU A 1 4025 ? 200.107 132.746 157.680 1.00 38.57  ? 4025 LEU A O     1 
ATOM   19406 C CB    . LEU A 1 4025 ? 198.090 133.667 159.548 1.00 38.57  ? 4025 LEU A CB    1 
ATOM   19407 C CG    . LEU A 1 4025 ? 197.256 133.975 158.303 1.00 38.57  ? 4025 LEU A CG    1 
ATOM   19408 C CD1   . LEU A 1 4025 ? 196.078 133.032 158.192 1.00 38.57  ? 4025 LEU A CD1   1 
ATOM   19409 C CD2   . LEU A 1 4025 ? 196.776 135.413 158.335 1.00 38.57  ? 4025 LEU A CD2   1 
ATOM   19410 N N     . ASP A 1 4026 ? 199.234 130.678 157.873 1.00 44.46  ? 4026 ASP A N     1 
ATOM   19411 C CA    . ASP A 1 4026 ? 199.712 130.213 156.572 1.00 44.46  ? 4026 ASP A CA    1 
ATOM   19412 C C     . ASP A 1 4026 ? 198.633 130.499 155.527 1.00 44.46  ? 4026 ASP A C     1 
ATOM   19413 O O     . ASP A 1 4026 ? 197.901 129.620 155.068 1.00 44.46  ? 4026 ASP A O     1 
ATOM   19414 C CB    . ASP A 1 4026 ? 200.069 128.734 156.629 1.00 44.46  ? 4026 ASP A CB    1 
ATOM   19415 C CG    . ASP A 1 4026 ? 200.581 128.206 155.303 1.00 44.46  ? 4026 ASP A CG    1 
ATOM   19416 O OD1   . ASP A 1 4026 ? 201.596 128.734 154.802 1.00 44.46  ? 4026 ASP A OD1   1 
ATOM   19417 O OD2   . ASP A 1 4026 ? 199.968 127.262 154.761 1.00 44.46  ? 4026 ASP A OD2   1 
ATOM   19418 N N     . LEU A 1 4027 ? 198.541 131.775 155.154 1.00 43.40  ? 4027 LEU A N     1 
ATOM   19419 C CA    . LEU A 1 4027 ? 197.497 132.214 154.237 1.00 43.40  ? 4027 LEU A CA    1 
ATOM   19420 C C     . LEU A 1 4027 ? 197.833 131.945 152.777 1.00 43.40  ? 4027 LEU A C     1 
ATOM   19421 O O     . LEU A 1 4027 ? 197.086 132.394 151.903 1.00 43.40  ? 4027 LEU A O     1 
ATOM   19422 C CB    . LEU A 1 4027 ? 197.200 133.703 154.439 1.00 43.40  ? 4027 LEU A CB    1 
ATOM   19423 C CG    . LEU A 1 4027 ? 198.201 134.757 153.962 1.00 43.40  ? 4027 LEU A CG    1 
ATOM   19424 C CD1   . LEU A 1 4027 ? 197.537 136.122 153.922 1.00 43.40  ? 4027 LEU A CD1   1 
ATOM   19425 C CD2   . LEU A 1 4027 ? 199.436 134.802 154.849 1.00 43.40  ? 4027 LEU A CD2   1 
ATOM   19426 N N     . THR A 1 4028 ? 198.927 131.238 152.487 1.00 45.83  ? 4028 THR A N     1 
ATOM   19427 C CA    . THR A 1 4028 ? 199.183 130.808 151.116 1.00 45.83  ? 4028 THR A CA    1 
ATOM   19428 C C     . THR A 1 4028 ? 198.096 129.852 150.641 1.00 45.83  ? 4028 THR A C     1 
ATOM   19429 O O     . THR A 1 4028 ? 197.617 129.945 149.505 1.00 45.83  ? 4028 THR A O     1 
ATOM   19430 C CB    . THR A 1 4028 ? 200.558 130.149 151.019 1.00 45.83  ? 4028 THR A CB    1 
ATOM   19431 O OG1   . THR A 1 4028 ? 200.531 128.887 151.698 1.00 45.83  ? 4028 THR A OG1   1 
ATOM   19432 C CG2   . THR A 1 4028 ? 201.607 131.033 151.662 1.00 45.83  ? 4028 THR A CG2   1 
ATOM   19433 N N     . HIS A 1 4029 ? 197.693 128.922 151.508 1.00 44.85  ? 4029 HIS A N     1 
ATOM   19434 C CA    . HIS A 1 4029 ? 196.585 128.032 151.184 1.00 44.85  ? 4029 HIS A CA    1 
ATOM   19435 C C     . HIS A 1 4029 ? 195.283 128.809 151.036 1.00 44.85  ? 4029 HIS A C     1 
ATOM   19436 O O     . HIS A 1 4029 ? 194.430 128.454 150.216 1.00 44.85  ? 4029 HIS A O     1 
ATOM   19437 C CB    . HIS A 1 4029 ? 196.456 126.957 152.263 1.00 44.85  ? 4029 HIS A CB    1 
ATOM   19438 C CG    . HIS A 1 4029 ? 195.440 125.903 151.955 1.00 44.85  ? 4029 HIS A CG    1 
ATOM   19439 N ND1   . HIS A 1 4029 ? 195.658 124.907 151.027 1.00 44.85  ? 4029 HIS A ND1   1 
ATOM   19440 C CD2   . HIS A 1 4029 ? 194.203 125.681 152.459 1.00 44.85  ? 4029 HIS A CD2   1 
ATOM   19441 C CE1   . HIS A 1 4029 ? 194.599 124.121 150.970 1.00 44.85  ? 4029 HIS A CE1   1 
ATOM   19442 N NE2   . HIS A 1 4029 ? 193.701 124.569 151.829 1.00 44.85  ? 4029 HIS A NE2   1 
ATOM   19443 N N     . ILE A 1 4030 ? 195.116 129.873 151.824 1.00 40.13  ? 4030 ILE A N     1 
ATOM   19444 C CA    . ILE A 1 4030 ? 193.883 130.653 151.780 1.00 40.13  ? 4030 ILE A CA    1 
ATOM   19445 C C     . ILE A 1 4030 ? 193.812 131.494 150.510 1.00 40.13  ? 4030 ILE A C     1 
ATOM   19446 O O     . ILE A 1 4030 ? 192.723 131.766 149.993 1.00 40.13  ? 4030 ILE A O     1 
ATOM   19447 C CB    . ILE A 1 4030 ? 193.757 131.519 153.044 1.00 40.13  ? 4030 ILE A CB    1 
ATOM   19448 C CG1   . ILE A 1 4030 ? 194.101 130.695 154.284 1.00 40.13  ? 4030 ILE A CG1   1 
ATOM   19449 C CG2   . ILE A 1 4030 ? 192.354 132.081 153.157 1.00 40.13  ? 4030 ILE A CG2   1 
ATOM   19450 C CD1   . ILE A 1 4030 ? 193.957 131.454 155.581 1.00 40.13  ? 4030 ILE A CD1   1 
ATOM   19451 N N     . VAL A 1 4031 ? 194.958 131.949 150.001 1.00 42.47  ? 4031 VAL A N     1 
ATOM   19452 C CA    . VAL A 1 4031 ? 194.922 132.715 148.759 1.00 42.47  ? 4031 VAL A CA    1 
ATOM   19453 C C     . VAL A 1 4031 ? 194.902 131.784 147.554 1.00 42.47  ? 4031 VAL A C     1 
ATOM   19454 O O     . VAL A 1 4031 ? 194.422 132.162 146.478 1.00 42.47  ? 4031 VAL A O     1 
ATOM   19455 C CB    . VAL A 1 4031 ? 196.095 133.711 148.688 1.00 42.47  ? 4031 VAL A CB    1 
ATOM   19456 C CG1   . VAL A 1 4031 ? 196.005 134.714 149.827 1.00 42.47  ? 4031 VAL A CG1   1 
ATOM   19457 C CG2   . VAL A 1 4031 ? 197.426 132.984 148.709 1.00 42.47  ? 4031 VAL A CG2   1 
ATOM   19458 N N     . GLY A 1 4032 ? 195.414 130.564 147.702 1.00 45.73  ? 4032 GLY A N     1 
ATOM   19459 C CA    . GLY A 1 4032 ? 195.312 129.581 146.641 1.00 45.73  ? 4032 GLY A CA    1 
ATOM   19460 C C     . GLY A 1 4032 ? 193.896 129.073 146.472 1.00 45.73  ? 4032 GLY A C     1 
ATOM   19461 O O     . GLY A 1 4032 ? 193.253 129.326 145.449 1.00 45.73  ? 4032 GLY A O     1 
ATOM   19462 N N     . THR A 1 4033 ? 193.400 128.354 147.474 1.00 42.98  ? 4033 THR A N     1 
ATOM   19463 C CA    . THR A 1 4033 ? 192.021 127.899 147.497 1.00 42.98  ? 4033 THR A CA    1 
ATOM   19464 C C     . THR A 1 4033 ? 191.274 128.587 148.637 1.00 42.98  ? 4033 THR A C     1 
ATOM   19465 O O     . THR A 1 4033 ? 191.847 129.355 149.410 1.00 42.98  ? 4033 THR A O     1 
ATOM   19466 C CB    . THR A 1 4033 ? 191.957 126.380 147.635 1.00 42.98  ? 4033 THR A CB    1 
ATOM   19467 O OG1   . THR A 1 4033 ? 190.600 125.943 147.489 1.00 42.98  ? 4033 THR A OG1   1 
ATOM   19468 C CG2   . THR A 1 4033 ? 192.475 125.952 148.994 1.00 42.98  ? 4033 THR A CG2   1 
ATOM   19469 N N     . GLU A 1 4034 ? 189.975 128.309 148.741 1.00 41.56  ? 4034 GLU A N     1 
ATOM   19470 C CA    . GLU A 1 4034 ? 189.049 128.867 149.726 1.00 41.56  ? 4034 GLU A CA    1 
ATOM   19471 C C     . GLU A 1 4034 ? 188.764 130.346 149.500 1.00 41.56  ? 4034 GLU A C     1 
ATOM   19472 O O     . GLU A 1 4034 ? 187.935 130.915 150.220 1.00 41.56  ? 4034 GLU A O     1 
ATOM   19473 C CB    . GLU A 1 4034 ? 189.532 128.679 151.173 1.00 41.56  ? 4034 GLU A CB    1 
ATOM   19474 C CG    . GLU A 1 4034 ? 189.977 127.267 151.513 1.00 41.56  ? 4034 GLU A CG    1 
ATOM   19475 C CD    . GLU A 1 4034 ? 190.539 127.158 152.916 1.00 41.56  ? 4034 GLU A CD    1 
ATOM   19476 O OE1   . GLU A 1 4034 ? 190.419 128.136 153.683 1.00 41.56  ? 4034 GLU A OE1   1 
ATOM   19477 O OE2   . GLU A 1 4034 ? 191.101 126.094 153.252 1.00 41.56  ? 4034 GLU A OE2   1 
ATOM   19478 N N     . VAL A 1 4035 ? 189.414 130.990 148.532 1.00 39.97  ? 4035 VAL A N     1 
ATOM   19479 C CA    . VAL A 1 4035 ? 189.133 132.379 148.188 1.00 39.97  ? 4035 VAL A CA    1 
ATOM   19480 C C     . VAL A 1 4035 ? 188.962 132.460 146.679 1.00 39.97  ? 4035 VAL A C     1 
ATOM   19481 O O     . VAL A 1 4035 ? 189.888 132.133 145.928 1.00 39.97  ? 4035 VAL A O     1 
ATOM   19482 C CB    . VAL A 1 4035 ? 190.241 133.338 148.658 1.00 39.97  ? 4035 VAL A CB    1 
ATOM   19483 C CG1   . VAL A 1 4035 ? 190.195 134.636 147.867 1.00 39.97  ? 4035 VAL A CG1   1 
ATOM   19484 C CG2   . VAL A 1 4035 ? 190.098 133.620 150.141 1.00 39.97  ? 4035 VAL A CG2   1 
ATOM   19485 N N     . LYS A 1 4036 ? 187.786 132.879 146.236 1.00 43.22  ? 4036 LYS A N     1 
ATOM   19486 C CA    . LYS A 1 4036 ? 187.546 133.062 144.817 1.00 43.22  ? 4036 LYS A CA    1 
ATOM   19487 C C     . LYS A 1 4036 ? 188.189 134.362 144.337 1.00 43.22  ? 4036 LYS A C     1 
ATOM   19488 O O     . LYS A 1 4036 ? 188.344 135.308 145.114 1.00 43.22  ? 4036 LYS A O     1 
ATOM   19489 C CB    . LYS A 1 4036 ? 186.049 133.085 144.530 1.00 43.22  ? 4036 LYS A CB    1 
ATOM   19490 C CG    . LYS A 1 4036 ? 185.265 132.014 145.270 1.00 43.22  ? 4036 LYS A CG    1 
ATOM   19491 C CD    . LYS A 1 4036 ? 185.084 130.773 144.412 1.00 43.22  ? 4036 LYS A CD    1 
ATOM   19492 C CE    . LYS A 1 4036 ? 184.621 129.589 145.244 1.00 43.22  ? 4036 LYS A CE    1 
ATOM   19493 N NZ    . LYS A 1 4036 ? 185.767 128.791 145.761 1.00 43.22  ? 4036 LYS A NZ    1 
ATOM   19494 N N     . PRO A 1 4037 ? 188.579 134.429 143.061 1.00 46.25  ? 4037 PRO A N     1 
ATOM   19495 C CA    . PRO A 1 4037 ? 189.158 135.680 142.545 1.00 46.25  ? 4037 PRO A CA    1 
ATOM   19496 C C     . PRO A 1 4037 ? 188.219 136.865 142.656 1.00 46.25  ? 4037 PRO A C     1 
ATOM   19497 O O     . PRO A 1 4037 ? 188.682 138.008 142.753 1.00 46.25  ? 4037 PRO A O     1 
ATOM   19498 C CB    . PRO A 1 4037 ? 189.474 135.344 141.079 1.00 46.25  ? 4037 PRO A CB    1 
ATOM   19499 C CG    . PRO A 1 4037 ? 188.660 134.132 140.766 1.00 46.25  ? 4037 PRO A CG    1 
ATOM   19500 C CD    . PRO A 1 4037 ? 188.548 133.368 142.042 1.00 46.25  ? 4037 PRO A CD    1 
ATOM   19501 N N     . ASN A 1 4038 ? 186.907 136.626 142.642 1.00 49.48  ? 4038 ASN A N     1 
ATOM   19502 C CA    . ASN A 1 4038 ? 185.942 137.705 142.802 1.00 49.48  ? 4038 ASN A CA    1 
ATOM   19503 C C     . ASN A 1 4038 ? 186.011 138.351 144.180 1.00 49.48  ? 4038 ASN A C     1 
ATOM   19504 O O     . ASN A 1 4038 ? 185.776 139.558 144.296 1.00 49.48  ? 4038 ASN A O     1 
ATOM   19505 C CB    . ASN A 1 4038 ? 184.530 137.177 142.543 1.00 49.48  ? 4038 ASN A CB    1 
ATOM   19506 C CG    . ASN A 1 4038 ? 183.518 138.286 142.368 1.00 49.48  ? 4038 ASN A CG    1 
ATOM   19507 O OD1   . ASN A 1 4038 ? 183.879 139.449 142.209 1.00 49.48  ? 4038 ASN A OD1   1 
ATOM   19508 N ND2   . ASN A 1 4038 ? 182.239 137.930 142.397 1.00 49.48  ? 4038 ASN A ND2   1 
ATOM   19509 N N     . THR A 1 4039 ? 186.332 137.584 145.220 1.00 39.66  ? 4039 THR A N     1 
ATOM   19510 C CA    . THR A 1 4039 ? 186.340 138.104 146.581 1.00 39.66  ? 4039 THR A CA    1 
ATOM   19511 C C     . THR A 1 4039 ? 187.702 138.704 146.900 1.00 39.66  ? 4039 THR A C     1 
ATOM   19512 O O     . THR A 1 4039 ? 188.713 137.996 146.811 1.00 39.66  ? 4039 THR A O     1 
ATOM   19513 C CB    . THR A 1 4039 ? 186.019 137.005 147.580 1.00 39.66  ? 4039 THR A CB    1 
ATOM   19514 O OG1   . THR A 1 4039 ? 187.051 136.011 147.546 1.00 39.66  ? 4039 THR A OG1   1 
ATOM   19515 C CG2   . THR A 1 4039 ? 184.689 136.353 147.244 1.00 39.66  ? 4039 THR A CG2   1 
ATOM   19516 N N     . PRO A 1 4040 ? 187.780 139.980 147.265 1.00 33.14  ? 4040 PRO A N     1 
ATOM   19517 C CA    . PRO A 1 4040 ? 189.061 140.555 147.680 1.00 33.14  ? 4040 PRO A CA    1 
ATOM   19518 C C     . PRO A 1 4040 ? 189.505 140.014 149.031 1.00 33.14  ? 4040 PRO A C     1 
ATOM   19519 O O     . PRO A 1 4040 ? 188.700 139.594 149.863 1.00 33.14  ? 4040 PRO A O     1 
ATOM   19520 C CB    . PRO A 1 4040 ? 188.766 142.056 147.759 1.00 33.14  ? 4040 PRO A CB    1 
ATOM   19521 C CG    . PRO A 1 4040 ? 187.311 142.131 148.053 1.00 33.14  ? 4040 PRO A CG    1 
ATOM   19522 C CD    . PRO A 1 4040 ? 186.673 140.945 147.378 1.00 33.14  ? 4040 PRO A CD    1 
ATOM   19523 N N     . VAL A 1 4041 ? 190.817 140.035 149.237 1.00 30.57  ? 4041 VAL A N     1 
ATOM   19524 C CA    . VAL A 1 4041 ? 191.431 139.587 150.481 1.00 30.57  ? 4041 VAL A CA    1 
ATOM   19525 C C     . VAL A 1 4041 ? 191.750 140.829 151.301 1.00 30.57  ? 4041 VAL A C     1 
ATOM   19526 O O     . VAL A 1 4041 ? 192.656 141.597 150.956 1.00 30.57  ? 4041 VAL A O     1 
ATOM   19527 C CB    . VAL A 1 4041 ? 192.688 138.746 150.230 1.00 30.57  ? 4041 VAL A CB    1 
ATOM   19528 C CG1   . VAL A 1 4041 ? 193.316 138.331 151.549 1.00 30.57  ? 4041 VAL A CG1   1 
ATOM   19529 C CG2   . VAL A 1 4041 ? 192.347 137.527 149.392 1.00 30.57  ? 4041 VAL A CG2   1 
ATOM   19530 N N     . LEU A 1 4042 ? 191.013 141.025 152.388 1.00 29.38  ? 4042 LEU A N     1 
ATOM   19531 C CA    . LEU A 1 4042 ? 191.159 142.212 153.219 1.00 29.38  ? 4042 LEU A CA    1 
ATOM   19532 C C     . LEU A 1 4042 ? 192.108 141.916 154.372 1.00 29.38  ? 4042 LEU A C     1 
ATOM   19533 O O     . LEU A 1 4042 ? 191.895 140.966 155.131 1.00 29.38  ? 4042 LEU A O     1 
ATOM   19534 C CB    . LEU A 1 4042 ? 189.800 142.668 153.752 1.00 29.38  ? 4042 LEU A CB    1 
ATOM   19535 C CG    . LEU A 1 4042 ? 188.872 143.417 152.791 1.00 29.38  ? 4042 LEU A CG    1 
ATOM   19536 C CD1   . LEU A 1 4042 ? 188.253 142.486 151.762 1.00 29.38  ? 4042 LEU A CD1   1 
ATOM   19537 C CD2   . LEU A 1 4042 ? 187.787 144.139 153.565 1.00 29.38  ? 4042 LEU A CD2   1 
ATOM   19538 N N     . MET A 1 4043 ? 193.152 142.731 154.500 1.00 28.77  ? 4043 MET A N     1 
ATOM   19539 C CA    . MET A 1 4043 ? 194.174 142.561 155.530 1.00 28.77  ? 4043 MET A CA    1 
ATOM   19540 C C     . MET A 1 4043 ? 194.071 143.745 156.486 1.00 28.77  ? 4043 MET A C     1 
ATOM   19541 O O     . MET A 1 4043 ? 194.770 144.748 156.326 1.00 28.77  ? 4043 MET A O     1 
ATOM   19542 C CB    . MET A 1 4043 ? 195.562 142.461 154.906 1.00 28.77  ? 4043 MET A CB    1 
ATOM   19543 C CG    . MET A 1 4043 ? 195.718 141.318 153.918 1.00 28.77  ? 4043 MET A CG    1 
ATOM   19544 S SD    . MET A 1 4043 ? 196.399 139.823 154.654 1.00 28.77  ? 4043 MET A SD    1 
ATOM   19545 C CE    . MET A 1 4043 ? 198.147 140.202 154.619 1.00 28.77  ? 4043 MET A CE    1 
ATOM   19546 N N     . CYS A 1 4044 ? 193.200 143.625 157.483 1.00 25.49  ? 4044 CYS A N     1 
ATOM   19547 C CA    . CYS A 1 4044 ? 192.992 144.685 158.459 1.00 25.49  ? 4044 CYS A CA    1 
ATOM   19548 C C     . CYS A 1 4044 ? 194.004 144.553 159.589 1.00 25.49  ? 4044 CYS A C     1 
ATOM   19549 O O     . CYS A 1 4044 ? 194.194 143.463 160.136 1.00 25.49  ? 4044 CYS A O     1 
ATOM   19550 C CB    . CYS A 1 4044 ? 191.568 144.635 159.011 1.00 25.49  ? 4044 CYS A CB    1 
ATOM   19551 S SG    . CYS A 1 4044 ? 190.286 144.597 157.742 1.00 25.49  ? 4044 CYS A SG    1 
ATOM   19552 N N     . SER A 1 4045 ? 194.650 145.663 159.933 1.00 32.46  ? 4045 SER A N     1 
ATOM   19553 C CA    . SER A 1 4045 ? 195.675 145.684 160.965 1.00 32.46  ? 4045 SER A CA    1 
ATOM   19554 C C     . SER A 1 4045 ? 195.286 146.648 162.076 1.00 32.46  ? 4045 SER A C     1 
ATOM   19555 O O     . SER A 1 4045 ? 194.663 147.685 161.833 1.00 32.46  ? 4045 SER A O     1 
ATOM   19556 C CB    . SER A 1 4045 ? 197.035 146.088 160.389 1.00 32.46  ? 4045 SER A CB    1 
ATOM   19557 O OG    . SER A 1 4045 ? 197.483 145.145 159.434 1.00 32.46  ? 4045 SER A OG    1 
ATOM   19558 N N     . VAL A 1 4046 ? 195.665 146.290 163.300 1.00 35.68  ? 4046 VAL A N     1 
ATOM   19559 C CA    . VAL A 1 4046 ? 195.457 147.187 164.441 1.00 35.68  ? 4046 VAL A CA    1 
ATOM   19560 C C     . VAL A 1 4046 ? 196.265 148.458 164.221 1.00 35.68  ? 4046 VAL A C     1 
ATOM   19561 O O     . VAL A 1 4046 ? 197.401 148.383 163.710 1.00 35.68  ? 4046 VAL A O     1 
ATOM   19562 C CB    . VAL A 1 4046 ? 195.861 146.488 165.750 1.00 35.68  ? 4046 VAL A CB    1 
ATOM   19563 C CG1   . VAL A 1 4046 ? 195.988 147.479 166.895 1.00 35.68  ? 4046 VAL A CG1   1 
ATOM   19564 C CG2   . VAL A 1 4046 ? 194.853 145.413 166.093 1.00 35.68  ? 4046 VAL A CG2   1 
ATOM   19565 N N     . PRO A 1 4047 ? 195.729 149.651 164.542 1.00 38.01  ? 4047 PRO A N     1 
ATOM   19566 C CA    . PRO A 1 4047 ? 196.497 150.891 164.353 1.00 38.01  ? 4047 PRO A CA    1 
ATOM   19567 C C     . PRO A 1 4047 ? 197.908 150.835 164.918 1.00 38.01  ? 4047 PRO A C     1 
ATOM   19568 O O     . PRO A 1 4047 ? 198.105 150.629 166.119 1.00 38.01  ? 4047 PRO A O     1 
ATOM   19569 C CB    . PRO A 1 4047 ? 195.644 151.937 165.079 1.00 38.01  ? 4047 PRO A CB    1 
ATOM   19570 C CG    . PRO A 1 4047 ? 194.255 151.422 164.950 1.00 38.01  ? 4047 PRO A CG    1 
ATOM   19571 C CD    . PRO A 1 4047 ? 194.350 149.919 164.987 1.00 38.01  ? 4047 PRO A CD    1 
ATOM   19572 N N     . GLY A 1 4048 ? 198.896 151.018 164.046 1.00 37.29  ? 4048 GLY A N     1 
ATOM   19573 C CA    . GLY A 1 4048 ? 200.289 150.900 164.414 1.00 37.29  ? 4048 GLY A CA    1 
ATOM   19574 C C     . GLY A 1 4048 ? 200.995 149.664 163.896 1.00 37.29  ? 4048 GLY A C     1 
ATOM   19575 O O     . GLY A 1 4048 ? 202.139 149.417 164.294 1.00 37.29  ? 4048 GLY A O     1 
ATOM   19576 N N     . TYR A 1 4049 ? 200.357 148.881 163.029 1.00 36.24  ? 4049 TYR A N     1 
ATOM   19577 C CA    . TYR A 1 4049 ? 200.933 147.650 162.512 1.00 36.24  ? 4049 TYR A CA    1 
ATOM   19578 C C     . TYR A 1 4049 ? 200.783 147.608 160.998 1.00 36.24  ? 4049 TYR A C     1 
ATOM   19579 O O     . TYR A 1 4049 ? 199.871 148.216 160.431 1.00 36.24  ? 4049 TYR A O     1 
ATOM   19580 C CB    . TYR A 1 4049 ? 200.267 146.417 163.137 1.00 36.24  ? 4049 TYR A CB    1 
ATOM   19581 C CG    . TYR A 1 4049 ? 201.113 145.165 163.095 1.00 36.24  ? 4049 TYR A CG    1 
ATOM   19582 C CD1   . TYR A 1 4049 ? 202.200 145.009 163.943 1.00 36.24  ? 4049 TYR A CD1   1 
ATOM   19583 C CD2   . TYR A 1 4049 ? 200.822 144.137 162.210 1.00 36.24  ? 4049 TYR A CD2   1 
ATOM   19584 C CE1   . TYR A 1 4049 ? 202.975 143.866 163.908 1.00 36.24  ? 4049 TYR A CE1   1 
ATOM   19585 C CE2   . TYR A 1 4049 ? 201.590 142.991 162.168 1.00 36.24  ? 4049 TYR A CE2   1 
ATOM   19586 C CZ    . TYR A 1 4049 ? 202.665 142.860 163.019 1.00 36.24  ? 4049 TYR A CZ    1 
ATOM   19587 O OH    . TYR A 1 4049 ? 203.433 141.720 162.981 1.00 36.24  ? 4049 TYR A OH    1 
ATOM   19588 N N     . ASP A 1 4050 ? 201.690 146.882 160.348 1.00 43.54  ? 4050 ASP A N     1 
ATOM   19589 C CA    . ASP A 1 4050 ? 201.699 146.741 158.898 1.00 43.54  ? 4050 ASP A CA    1 
ATOM   19590 C C     . ASP A 1 4050 ? 201.473 145.282 158.530 1.00 43.54  ? 4050 ASP A C     1 
ATOM   19591 O O     . ASP A 1 4050 ? 202.028 144.382 159.169 1.00 43.54  ? 4050 ASP A O     1 
ATOM   19592 C CB    . ASP A 1 4050 ? 203.015 147.250 158.301 1.00 43.54  ? 4050 ASP A CB    1 
ATOM   19593 C CG    . ASP A 1 4050 ? 204.196 146.360 158.639 1.00 43.54  ? 4050 ASP A CG    1 
ATOM   19594 O OD1   . ASP A 1 4050 ? 204.853 146.608 159.672 1.00 43.54  ? 4050 ASP A OD1   1 
ATOM   19595 O OD2   . ASP A 1 4050 ? 204.471 145.416 157.869 1.00 43.54  ? 4050 ASP A OD2   1 
ATOM   19596 N N     . ALA A 1 4051 ? 200.649 145.052 157.509 1.00 45.11  ? 4051 ALA A N     1 
ATOM   19597 C CA    . ALA A 1 4051 ? 200.342 143.709 157.041 1.00 45.11  ? 4051 ALA A CA    1 
ATOM   19598 C C     . ALA A 1 4051 ? 200.902 143.417 155.658 1.00 45.11  ? 4051 ALA A C     1 
ATOM   19599 O O     . ALA A 1 4051 ? 200.789 142.281 155.187 1.00 45.11  ? 4051 ALA A O     1 
ATOM   19600 C CB    . ALA A 1 4051 ? 198.827 143.483 157.037 1.00 45.11  ? 4051 ALA A CB    1 
ATOM   19601 N N     . SER A 1 4052 ? 201.501 144.408 154.994 1.00 51.29  ? 4052 SER A N     1 
ATOM   19602 C CA    . SER A 1 4052 ? 202.029 144.200 153.652 1.00 51.29  ? 4052 SER A CA    1 
ATOM   19603 C C     . SER A 1 4052 ? 203.186 143.210 153.625 1.00 51.29  ? 4052 SER A C     1 
ATOM   19604 O O     . SER A 1 4052 ? 203.453 142.617 152.574 1.00 51.29  ? 4052 SER A O     1 
ATOM   19605 C CB    . SER A 1 4052 ? 202.474 145.535 153.054 1.00 51.29  ? 4052 SER A CB    1 
ATOM   19606 O OG    . SER A 1 4052 ? 201.380 146.426 152.927 1.00 51.29  ? 4052 SER A OG    1 
ATOM   19607 N N     . GLY A 1 4053 ? 203.874 143.018 154.752 1.00 59.20  ? 4053 GLY A N     1 
ATOM   19608 C CA    . GLY A 1 4053 ? 205.019 142.124 154.762 1.00 59.20  ? 4053 GLY A CA    1 
ATOM   19609 C C     . GLY A 1 4053 ? 204.652 140.685 154.456 1.00 59.20  ? 4053 GLY A C     1 
ATOM   19610 O O     . GLY A 1 4053 ? 205.316 140.025 153.653 1.00 59.20  ? 4053 GLY A O     1 
ATOM   19611 N N     . HIS A 1 4054 ? 203.588 140.180 155.086 1.00 56.12  ? 4054 HIS A N     1 
ATOM   19612 C CA    . HIS A 1 4054 ? 203.200 138.786 154.890 1.00 56.12  ? 4054 HIS A CA    1 
ATOM   19613 C C     . HIS A 1 4054 ? 202.806 138.523 153.442 1.00 56.12  ? 4054 HIS A C     1 
ATOM   19614 O O     . HIS A 1 4054 ? 203.228 137.529 152.838 1.00 56.12  ? 4054 HIS A O     1 
ATOM   19615 C CB    . HIS A 1 4054 ? 202.050 138.428 155.832 1.00 56.12  ? 4054 HIS A CB    1 
ATOM   19616 C CG    . HIS A 1 4054 ? 202.316 138.757 157.268 1.00 56.12  ? 4054 HIS A CG    1 
ATOM   19617 N ND1   . HIS A 1 4054 ? 202.169 140.028 157.780 1.00 56.12  ? 4054 HIS A ND1   1 
ATOM   19618 C CD2   . HIS A 1 4054 ? 202.716 137.979 158.302 1.00 56.12  ? 4054 HIS A CD2   1 
ATOM   19619 C CE1   . HIS A 1 4054 ? 202.468 140.020 159.067 1.00 56.12  ? 4054 HIS A CE1   1 
ATOM   19620 N NE2   . HIS A 1 4054 ? 202.804 138.789 159.409 1.00 56.12  ? 4054 HIS A NE2   1 
ATOM   19621 N N     . VAL A 1 4055 ? 201.998 139.413 152.865 1.00 59.85  ? 4055 VAL A N     1 
ATOM   19622 C CA    . VAL A 1 4055 ? 201.533 139.214 151.498 1.00 59.85  ? 4055 VAL A CA    1 
ATOM   19623 C C     . VAL A 1 4055 ? 202.676 139.390 150.500 1.00 59.85  ? 4055 VAL A C     1 
ATOM   19624 O O     . VAL A 1 4055 ? 202.777 138.644 149.517 1.00 59.85  ? 4055 VAL A O     1 
ATOM   19625 C CB    . VAL A 1 4055 ? 200.337 140.139 151.203 1.00 59.85  ? 4055 VAL A CB    1 
ATOM   19626 C CG1   . VAL A 1 4055 ? 200.745 141.587 151.262 1.00 59.85  ? 4055 VAL A CG1   1 
ATOM   19627 C CG2   . VAL A 1 4055 ? 199.749 139.816 149.842 1.00 59.85  ? 4055 VAL A CG2   1 
ATOM   19628 N N     . GLU A 1 4056 ? 203.570 140.352 150.743 1.00 64.92  ? 4056 GLU A N     1 
ATOM   19629 C CA    . GLU A 1 4056 ? 204.732 140.494 149.873 1.00 64.92  ? 4056 GLU A CA    1 
ATOM   19630 C C     . GLU A 1 4056 ? 205.619 139.257 149.938 1.00 64.92  ? 4056 GLU A C     1 
ATOM   19631 O O     . GLU A 1 4056 ? 206.133 138.800 148.910 1.00 64.92  ? 4056 GLU A O     1 
ATOM   19632 C CB    . GLU A 1 4056 ? 205.520 141.749 150.244 1.00 64.92  ? 4056 GLU A CB    1 
ATOM   19633 C CG    . GLU A 1 4056 ? 205.063 142.998 149.509 1.00 64.92  ? 4056 GLU A CG    1 
ATOM   19634 C CD    . GLU A 1 4056 ? 205.213 144.251 150.344 1.00 64.92  ? 4056 GLU A CD    1 
ATOM   19635 O OE1   . GLU A 1 4056 ? 205.970 144.219 151.337 1.00 64.92  ? 4056 GLU A OE1   1 
ATOM   19636 O OE2   . GLU A 1 4056 ? 204.574 145.269 150.007 1.00 64.92  ? 4056 GLU A OE2   1 
ATOM   19637 N N     . ASP A 1 4057 ? 205.797 138.689 151.133 1.00 67.46  ? 4057 ASP A N     1 
ATOM   19638 C CA    . ASP A 1 4057 ? 206.615 137.488 151.266 1.00 67.46  ? 4057 ASP A CA    1 
ATOM   19639 C C     . ASP A 1 4057 ? 205.979 136.296 150.561 1.00 67.46  ? 4057 ASP A C     1 
ATOM   19640 O O     . ASP A 1 4057 ? 206.677 135.518 149.897 1.00 67.46  ? 4057 ASP A O     1 
ATOM   19641 C CB    . ASP A 1 4057 ? 206.849 137.175 152.743 1.00 67.46  ? 4057 ASP A CB    1 
ATOM   19642 C CG    . ASP A 1 4057 ? 207.952 136.158 152.953 1.00 67.46  ? 4057 ASP A CG    1 
ATOM   19643 O OD1   . ASP A 1 4057 ? 209.089 136.409 152.501 1.00 67.46  ? 4057 ASP A OD1   1 
ATOM   19644 O OD2   . ASP A 1 4057 ? 207.682 135.107 153.571 1.00 67.46  ? 4057 ASP A OD2   1 
ATOM   19645 N N     . LEU A 1 4058 ? 204.660 136.125 150.696 1.00 65.73  ? 4058 LEU A N     1 
ATOM   19646 C CA    . LEU A 1 4058 ? 204.020 134.997 150.026 1.00 65.73  ? 4058 LEU A CA    1 
ATOM   19647 C C     . LEU A 1 4058 ? 204.067 135.168 148.514 1.00 65.73  ? 4058 LEU A C     1 
ATOM   19648 O O     . LEU A 1 4058 ? 204.173 134.181 147.777 1.00 65.73  ? 4058 LEU A O     1 
ATOM   19649 C CB    . LEU A 1 4058 ? 202.581 134.809 150.513 1.00 65.73  ? 4058 LEU A CB    1 
ATOM   19650 C CG    . LEU A 1 4058 ? 201.505 135.882 150.332 1.00 65.73  ? 4058 LEU A CG    1 
ATOM   19651 C CD1   . LEU A 1 4058 ? 200.863 135.830 148.953 1.00 65.73  ? 4058 LEU A CD1   1 
ATOM   19652 C CD2   . LEU A 1 4058 ? 200.449 135.744 151.405 1.00 65.73  ? 4058 LEU A CD2   1 
ATOM   19653 N N     . ALA A 1 4059 ? 203.987 136.410 148.031 1.00 66.59  ? 4059 ALA A N     1 
ATOM   19654 C CA    . ALA A 1 4059 ? 204.199 136.651 146.608 1.00 66.59  ? 4059 ALA A CA    1 
ATOM   19655 C C     . ALA A 1 4059 ? 205.619 136.289 146.197 1.00 66.59  ? 4059 ALA A C     1 
ATOM   19656 O O     . ALA A 1 4059 ? 205.838 135.717 145.123 1.00 66.59  ? 4059 ALA A O     1 
ATOM   19657 C CB    . ALA A 1 4059 ? 203.906 138.109 146.271 1.00 66.59  ? 4059 ALA A CB    1 
ATOM   19658 N N     . ALA A 1 4060 ? 206.598 136.629 147.039 1.00 68.62  ? 4060 ALA A N     1 
ATOM   19659 C CA    . ALA A 1 4060 ? 207.988 136.312 146.728 1.00 68.62  ? 4060 ALA A CA    1 
ATOM   19660 C C     . ALA A 1 4060 ? 208.206 134.808 146.628 1.00 68.62  ? 4060 ALA A C     1 
ATOM   19661 O O     . ALA A 1 4060 ? 208.901 134.334 145.721 1.00 68.62  ? 4060 ALA A O     1 
ATOM   19662 C CB    . ALA A 1 4060 ? 208.912 136.919 147.784 1.00 68.62  ? 4060 ALA A CB    1 
ATOM   19663 N N     . GLU A 1 4061 ? 207.624 134.038 147.550 1.00 71.29  ? 4061 GLU A N     1 
ATOM   19664 C CA    . GLU A 1 4061 ? 207.807 132.590 147.501 1.00 71.29  ? 4061 GLU A CA    1 
ATOM   19665 C C     . GLU A 1 4061 ? 206.952 131.956 146.408 1.00 71.29  ? 4061 GLU A C     1 
ATOM   19666 O O     . GLU A 1 4061 ? 207.337 130.934 145.829 1.00 71.29  ? 4061 GLU A O     1 
ATOM   19667 C CB    . GLU A 1 4061 ? 207.504 131.966 148.864 1.00 71.29  ? 4061 GLU A CB    1 
ATOM   19668 C CG    . GLU A 1 4061 ? 206.063 132.081 149.314 1.00 71.29  ? 4061 GLU A CG    1 
ATOM   19669 C CD    . GLU A 1 4061 ? 205.845 131.500 150.694 1.00 71.29  ? 4061 GLU A CD    1 
ATOM   19670 O OE1   . GLU A 1 4061 ? 206.827 131.026 151.303 1.00 71.29  ? 4061 GLU A OE1   1 
ATOM   19671 O OE2   . GLU A 1 4061 ? 204.693 131.520 151.172 1.00 71.29  ? 4061 GLU A OE2   1 
ATOM   19672 N N     . GLN A 1 4062 ? 205.792 132.541 146.112 1.00 70.90  ? 4062 GLN A N     1 
ATOM   19673 C CA    . GLN A 1 4062 ? 204.930 132.062 145.040 1.00 70.90  ? 4062 GLN A CA    1 
ATOM   19674 C C     . GLN A 1 4062 ? 205.231 132.725 143.702 1.00 70.90  ? 4062 GLN A C     1 
ATOM   19675 O O     . GLN A 1 4062 ? 204.387 132.669 142.803 1.00 70.90  ? 4062 GLN A O     1 
ATOM   19676 C CB    . GLN A 1 4062 ? 203.457 132.279 145.401 1.00 70.90  ? 4062 GLN A CB    1 
ATOM   19677 C CG    . GLN A 1 4062 ? 202.925 131.436 146.562 1.00 70.90  ? 4062 GLN A CG    1 
ATOM   19678 C CD    . GLN A 1 4062 ? 203.151 129.941 146.391 1.00 70.90  ? 4062 GLN A CD    1 
ATOM   19679 O OE1   . GLN A 1 4062 ? 204.279 129.452 146.460 1.00 70.90  ? 4062 GLN A OE1   1 
ATOM   19680 N NE2   . GLN A 1 4062 ? 202.068 129.207 146.163 1.00 70.90  ? 4062 GLN A NE2   1 
ATOM   19681 N N     . ASN A 1 4063 ? 206.387 133.390 143.589 1.00 73.82  ? 4063 ASN A N     1 
ATOM   19682 C CA    . ASN A 1 4063 ? 206.903 134.012 142.358 1.00 73.82  ? 4063 ASN A CA    1 
ATOM   19683 C C     . ASN A 1 4063 ? 205.798 134.606 141.482 1.00 73.82  ? 4063 ASN A C     1 
ATOM   19684 O O     . ASN A 1 4063 ? 205.766 134.419 140.264 1.00 73.82  ? 4063 ASN A O     1 
ATOM   19685 C CB    . ASN A 1 4063 ? 207.802 133.040 141.571 1.00 73.82  ? 4063 ASN A CB    1 
ATOM   19686 C CG    . ASN A 1 4063 ? 207.071 131.812 141.029 1.00 73.82  ? 4063 ASN A CG    1 
ATOM   19687 O OD1   . ASN A 1 4063 ? 205.850 131.776 140.915 1.00 73.82  ? 4063 ASN A OD1   1 
ATOM   19688 N ND2   . ASN A 1 4063 ? 207.845 130.787 140.692 1.00 73.82  ? 4063 ASN A ND2   1 
ATOM   19689 N N     . THR A 1 4064 ? 204.896 135.353 142.112 1.00 67.79  ? 4064 THR A N     1 
ATOM   19690 C CA    . THR A 1 4064 ? 203.863 136.105 141.416 1.00 67.79  ? 4064 THR A CA    1 
ATOM   19691 C C     . THR A 1 4064 ? 203.961 137.561 141.843 1.00 67.79  ? 4064 THR A C     1 
ATOM   19692 O O     . THR A 1 4064 ? 203.865 137.867 143.036 1.00 67.79  ? 4064 THR A O     1 
ATOM   19693 C CB    . THR A 1 4064 ? 202.467 135.552 141.719 1.00 67.79  ? 4064 THR A CB    1 
ATOM   19694 O OG1   . THR A 1 4064 ? 202.420 134.160 141.382 1.00 67.79  ? 4064 THR A OG1   1 
ATOM   19695 C CG2   . THR A 1 4064 ? 201.414 136.296 140.913 1.00 67.79  ? 4064 THR A CG2   1 
ATOM   19696 N N     . GLN A 1 4065 ? 204.151 138.451 140.875 1.00 63.03  ? 4065 GLN A N     1 
ATOM   19697 C CA    . GLN A 1 4065 ? 204.385 139.850 141.198 1.00 63.03  ? 4065 GLN A CA    1 
ATOM   19698 C C     . GLN A 1 4065 ? 203.086 140.529 141.615 1.00 63.03  ? 4065 GLN A C     1 
ATOM   19699 O O     . GLN A 1 4065 ? 201.991 140.136 141.205 1.00 63.03  ? 4065 GLN A O     1 
ATOM   19700 C CB    . GLN A 1 4065 ? 205.044 140.566 140.008 1.00 63.03  ? 4065 GLN A CB    1 
ATOM   19701 C CG    . GLN A 1 4065 ? 204.239 140.687 138.697 1.00 63.03  ? 4065 GLN A CG    1 
ATOM   19702 C CD    . GLN A 1 4065 ? 203.033 141.617 138.760 1.00 63.03  ? 4065 GLN A CD    1 
ATOM   19703 O OE1   . GLN A 1 4065 ? 202.949 142.497 139.618 1.00 63.03  ? 4065 GLN A OE1   1 
ATOM   19704 N NE2   . GLN A 1 4065 ? 202.100 141.431 137.838 1.00 63.03  ? 4065 GLN A NE2   1 
ATOM   19705 N N     . ILE A 1 4066 ? 203.219 141.558 142.448 1.00 56.35  ? 4066 ILE A N     1 
ATOM   19706 C CA    . ILE A 1 4066 ? 202.089 142.355 142.904 1.00 56.35  ? 4066 ILE A CA    1 
ATOM   19707 C C     . ILE A 1 4066 ? 202.343 143.810 142.544 1.00 56.35  ? 4066 ILE A C     1 
ATOM   19708 O O     . ILE A 1 4066 ? 203.443 144.328 142.772 1.00 56.35  ? 4066 ILE A O     1 
ATOM   19709 C CB    . ILE A 1 4066 ? 201.848 142.218 144.419 1.00 56.35  ? 4066 ILE A CB    1 
ATOM   19710 C CG1   . ILE A 1 4066 ? 201.485 140.786 144.798 1.00 56.35  ? 4066 ILE A CG1   1 
ATOM   19711 C CG2   . ILE A 1 4066 ? 200.735 143.123 144.850 1.00 56.35  ? 4066 ILE A CG2   1 
ATOM   19712 C CD1   . ILE A 1 4066 ? 201.491 140.562 146.294 1.00 56.35  ? 4066 ILE A CD1   1 
ATOM   19713 N N     . THR A 1 4067 ? 201.329 144.468 141.982 1.00 52.97  ? 4067 THR A N     1 
ATOM   19714 C CA    . THR A 1 4067 ? 201.389 145.901 141.702 1.00 52.97  ? 4067 THR A CA    1 
ATOM   19715 C C     . THR A 1 4067 ? 200.953 146.653 142.957 1.00 52.97  ? 4067 THR A C     1 
ATOM   19716 O O     . THR A 1 4067 ? 199.817 147.113 143.089 1.00 52.97  ? 4067 THR A O     1 
ATOM   19717 C CB    . THR A 1 4067 ? 200.519 146.251 140.501 1.00 52.97  ? 4067 THR A CB    1 
ATOM   19718 O OG1   . THR A 1 4067 ? 200.776 145.325 139.438 1.00 52.97  ? 4067 THR A OG1   1 
ATOM   19719 C CG2   . THR A 1 4067 ? 200.817 147.663 140.018 1.00 52.97  ? 4067 THR A CG2   1 
ATOM   19720 N N     . SER A 1 4068 ? 201.885 146.770 143.902 1.00 47.52  ? 4068 SER A N     1 
ATOM   19721 C CA    . SER A 1 4068 ? 201.597 147.448 145.159 1.00 47.52  ? 4068 SER A CA    1 
ATOM   19722 C C     . SER A 1 4068 ? 201.401 148.940 144.921 1.00 47.52  ? 4068 SER A C     1 
ATOM   19723 O O     . SER A 1 4068 ? 202.219 149.586 144.260 1.00 47.52  ? 4068 SER A O     1 
ATOM   19724 C CB    . SER A 1 4068 ? 202.726 147.213 146.160 1.00 47.52  ? 4068 SER A CB    1 
ATOM   19725 O OG    . SER A 1 4068 ? 203.928 147.823 145.727 1.00 47.52  ? 4068 SER A OG    1 
ATOM   19726 N N     . ILE A 1 4069 ? 200.313 149.487 145.461 1.00 49.09  ? 4069 ILE A N     1 
ATOM   19727 C CA    . ILE A 1 4069 ? 199.923 150.870 145.209 1.00 49.09  ? 4069 ILE A CA    1 
ATOM   19728 C C     . ILE A 1 4069 ? 199.446 151.500 146.510 1.00 49.09  ? 4069 ILE A C     1 
ATOM   19729 O O     . ILE A 1 4069 ? 198.659 150.896 147.246 1.00 49.09  ? 4069 ILE A O     1 
ATOM   19730 C CB    . ILE A 1 4069 ? 198.821 150.959 144.136 1.00 49.09  ? 4069 ILE A CB    1 
ATOM   19731 C CG1   . ILE A 1 4069 ? 199.339 150.427 142.802 1.00 49.09  ? 4069 ILE A CG1   1 
ATOM   19732 C CG2   . ILE A 1 4069 ? 198.331 152.389 143.982 1.00 49.09  ? 4069 ILE A CG2   1 
ATOM   19733 C CD1   . ILE A 1 4069 ? 198.260 150.166 141.806 1.00 49.09  ? 4069 ILE A CD1   1 
ATOM   19734 N N     . ALA A 1 4070 ? 199.918 152.712 146.790 1.00 47.19  ? 4070 ALA A N     1 
ATOM   19735 C CA    . ALA A 1 4070 ? 199.415 153.483 147.917 1.00 47.19  ? 4070 ALA A CA    1 
ATOM   19736 C C     . ALA A 1 4070 ? 198.220 154.315 147.471 1.00 47.19  ? 4070 ALA A C     1 
ATOM   19737 O O     . ALA A 1 4070 ? 198.238 154.915 146.392 1.00 47.19  ? 4070 ALA A O     1 
ATOM   19738 C CB    . ALA A 1 4070 ? 200.511 154.383 148.485 1.00 47.19  ? 4070 ALA A CB    1 
ATOM   19739 N N     . ILE A 1 4071 ? 197.179 154.351 148.303 1.00 47.17  ? 4071 ILE A N     1 
ATOM   19740 C CA    . ILE A 1 4071 ? 195.926 155.009 147.952 1.00 47.17  ? 4071 ILE A CA    1 
ATOM   19741 C C     . ILE A 1 4071 ? 195.828 156.405 148.567 1.00 47.17  ? 4071 ILE A C     1 
ATOM   19742 O O     . ILE A 1 4071 ? 194.750 157.008 148.569 1.00 47.17  ? 4071 ILE A O     1 
ATOM   19743 C CB    . ILE A 1 4071 ? 194.727 154.133 148.353 1.00 47.17  ? 4071 ILE A CB    1 
ATOM   19744 C CG1   . ILE A 1 4071 ? 195.027 152.665 148.053 1.00 47.17  ? 4071 ILE A CG1   1 
ATOM   19745 C CG2   . ILE A 1 4071 ? 193.484 154.504 147.562 1.00 47.17  ? 4071 ILE A CG2   1 
ATOM   19746 C CD1   . ILE A 1 4071 ? 195.288 152.380 146.586 1.00 47.17  ? 4071 ILE A CD1   1 
ATOM   19747 N N     . GLY A 1 4072 ? 196.935 156.937 149.086 1.00 53.91  ? 4072 GLY A N     1 
ATOM   19748 C CA    . GLY A 1 4072 ? 196.897 158.264 149.678 1.00 53.91  ? 4072 GLY A CA    1 
ATOM   19749 C C     . GLY A 1 4072 ? 196.628 159.362 148.665 1.00 53.91  ? 4072 GLY A C     1 
ATOM   19750 O O     . GLY A 1 4072 ? 195.842 160.277 148.923 1.00 53.91  ? 4072 GLY A O     1 
ATOM   19751 N N     . SER A 1 4073 ? 197.271 159.286 147.502 1.00 69.18  ? 4073 SER A N     1 
ATOM   19752 C CA    . SER A 1 4073 ? 197.150 160.331 146.498 1.00 69.18  ? 4073 SER A CA    1 
ATOM   19753 C C     . SER A 1 4073 ? 195.919 160.111 145.621 1.00 69.18  ? 4073 SER A C     1 
ATOM   19754 O O     . SER A 1 4073 ? 195.367 159.011 145.537 1.00 69.18  ? 4073 SER A O     1 
ATOM   19755 C CB    . SER A 1 4073 ? 198.406 160.388 145.629 1.00 69.18  ? 4073 SER A CB    1 
ATOM   19756 O OG    . SER A 1 4073 ? 198.276 161.362 144.609 1.00 69.18  ? 4073 SER A OG    1 
ATOM   19757 N N     . ALA A 1 4074 ? 195.492 161.191 144.960 1.00 74.69  ? 4074 ALA A N     1 
ATOM   19758 C CA    . ALA A 1 4074 ? 194.350 161.102 144.055 1.00 74.69  ? 4074 ALA A CA    1 
ATOM   19759 C C     . ALA A 1 4074 ? 194.709 160.346 142.782 1.00 74.69  ? 4074 ALA A C     1 
ATOM   19760 O O     . ALA A 1 4074 ? 193.886 159.594 142.247 1.00 74.69  ? 4074 ALA A O     1 
ATOM   19761 C CB    . ALA A 1 4074 ? 193.832 162.500 143.723 1.00 74.69  ? 4074 ALA A CB    1 
ATOM   19762 N N     . GLU A 1 4075 ? 195.931 160.539 142.277 1.00 77.36  ? 4075 GLU A N     1 
ATOM   19763 C CA    . GLU A 1 4075 ? 196.396 159.774 141.125 1.00 77.36  ? 4075 GLU A CA    1 
ATOM   19764 C C     . GLU A 1 4075 ? 196.477 158.285 141.436 1.00 77.36  ? 4075 GLU A C     1 
ATOM   19765 O O     . GLU A 1 4075 ? 196.388 157.458 140.517 1.00 77.36  ? 4075 GLU A O     1 
ATOM   19766 C CB    . GLU A 1 4075 ? 197.757 160.312 140.669 1.00 77.36  ? 4075 GLU A CB    1 
ATOM   19767 C CG    . GLU A 1 4075 ? 198.459 159.493 139.596 1.00 77.36  ? 4075 GLU A CG    1 
ATOM   19768 C CD    . GLU A 1 4075 ? 199.427 158.479 140.173 1.00 77.36  ? 4075 GLU A CD    1 
ATOM   19769 O OE1   . GLU A 1 4075 ? 199.883 158.676 141.319 1.00 77.36  ? 4075 GLU A OE1   1 
ATOM   19770 O OE2   . GLU A 1 4075 ? 199.729 157.485 139.481 1.00 77.36  ? 4075 GLU A OE2   1 
ATOM   19771 N N     . GLY A 1 4076 ? 196.634 157.932 142.715 1.00 70.73  ? 4076 GLY A N     1 
ATOM   19772 C CA    . GLY A 1 4076 ? 196.622 156.534 143.101 1.00 70.73  ? 4076 GLY A CA    1 
ATOM   19773 C C     . GLY A 1 4076 ? 195.326 155.834 142.750 1.00 70.73  ? 4076 GLY A C     1 
ATOM   19774 O O     . GLY A 1 4076 ? 195.321 154.631 142.494 1.00 70.73  ? 4076 GLY A O     1 
ATOM   19775 N N     . PHE A 1 4077 ? 194.216 156.575 142.716 1.00 64.63  ? 4077 PHE A N     1 
ATOM   19776 C CA    . PHE A 1 4077 ? 192.942 155.985 142.315 1.00 64.63  ? 4077 PHE A CA    1 
ATOM   19777 C C     . PHE A 1 4077 ? 193.016 155.448 140.890 1.00 64.63  ? 4077 PHE A C     1 
ATOM   19778 O O     . PHE A 1 4077 ? 192.698 154.280 140.631 1.00 64.63  ? 4077 PHE A O     1 
ATOM   19779 C CB    . PHE A 1 4077 ? 191.821 157.022 142.431 1.00 64.63  ? 4077 PHE A CB    1 
ATOM   19780 C CG    . PHE A 1 4077 ? 191.481 157.417 143.846 1.00 64.63  ? 4077 PHE A CG    1 
ATOM   19781 C CD1   . PHE A 1 4077 ? 190.394 158.238 144.097 1.00 64.63  ? 4077 PHE A CD1   1 
ATOM   19782 C CD2   . PHE A 1 4077 ? 192.229 156.966 144.921 1.00 64.63  ? 4077 PHE A CD2   1 
ATOM   19783 C CE1   . PHE A 1 4077 ? 190.066 158.609 145.387 1.00 64.63  ? 4077 PHE A CE1   1 
ATOM   19784 C CE2   . PHE A 1 4077 ? 191.906 157.335 146.213 1.00 64.63  ? 4077 PHE A CE2   1 
ATOM   19785 C CZ    . PHE A 1 4077 ? 190.823 158.156 146.446 1.00 64.63  ? 4077 PHE A CZ    1 
ATOM   19786 N N     . ASN A 1 4078 ? 193.452 156.292 139.951 1.00 69.93  ? 4078 ASN A N     1 
ATOM   19787 C CA    . ASN A 1 4078 ? 193.560 155.868 138.559 1.00 69.93  ? 4078 ASN A CA    1 
ATOM   19788 C C     . ASN A 1 4078 ? 194.642 154.811 138.387 1.00 69.93  ? 4078 ASN A C     1 
ATOM   19789 O O     . ASN A 1 4078 ? 194.488 153.881 137.584 1.00 69.93  ? 4078 ASN A O     1 
ATOM   19790 C CB    . ASN A 1 4078 ? 193.836 157.075 137.665 1.00 69.93  ? 4078 ASN A CB    1 
ATOM   19791 C CG    . ASN A 1 4078 ? 192.808 158.175 137.840 1.00 69.93  ? 4078 ASN A CG    1 
ATOM   19792 O OD1   . ASN A 1 4078 ? 191.672 158.057 137.381 1.00 69.93  ? 4078 ASN A OD1   1 
ATOM   19793 N ND2   . ASN A 1 4078 ? 193.202 159.252 138.510 1.00 69.93  ? 4078 ASN A ND2   1 
ATOM   19794 N N     . GLN A 1 4079 ? 195.748 154.940 139.126 1.00 68.88  ? 4079 GLN A N     1 
ATOM   19795 C CA    . GLN A 1 4079 ? 196.799 153.930 139.046 1.00 68.88  ? 4079 GLN A CA    1 
ATOM   19796 C C     . GLN A 1 4079 ? 196.280 152.566 139.487 1.00 68.88  ? 4079 GLN A C     1 
ATOM   19797 O O     . GLN A 1 4079 ? 196.541 151.552 138.830 1.00 68.88  ? 4079 GLN A O     1 
ATOM   19798 C CB    . GLN A 1 4079 ? 198.000 154.351 139.892 1.00 68.88  ? 4079 GLN A CB    1 
ATOM   19799 C CG    . GLN A 1 4079 ? 199.015 153.243 140.117 1.00 68.88  ? 4079 GLN A CG    1 
ATOM   19800 C CD    . GLN A 1 4079 ? 200.439 153.755 140.200 1.00 68.88  ? 4079 GLN A CD    1 
ATOM   19801 O OE1   . GLN A 1 4079 ? 200.673 154.956 140.331 1.00 68.88  ? 4079 GLN A OE1   1 
ATOM   19802 N NE2   . GLN A 1 4079 ? 201.400 152.843 140.123 1.00 68.88  ? 4079 GLN A NE2   1 
ATOM   19803 N N     . ALA A 1 4080 ? 195.518 152.528 140.583 1.00 66.61  ? 4080 ALA A N     1 
ATOM   19804 C CA    . ALA A 1 4080 ? 194.946 151.274 141.058 1.00 66.61  ? 4080 ALA A CA    1 
ATOM   19805 C C     . ALA A 1 4080 ? 193.914 150.729 140.081 1.00 66.61  ? 4080 ALA A C     1 
ATOM   19806 O O     . ALA A 1 4080 ? 193.837 149.514 139.873 1.00 66.61  ? 4080 ALA A O     1 
ATOM   19807 C CB    . ALA A 1 4080 ? 194.325 151.471 142.440 1.00 66.61  ? 4080 ALA A CB    1 
ATOM   19808 N N     . ASP A 1 4081 ? 193.103 151.605 139.485 1.00 66.66  ? 4081 ASP A N     1 
ATOM   19809 C CA    . ASP A 1 4081 ? 192.126 151.144 138.502 1.00 66.66  ? 4081 ASP A CA    1 
ATOM   19810 C C     . ASP A 1 4081 ? 192.819 150.483 137.315 1.00 66.66  ? 4081 ASP A C     1 
ATOM   19811 O O     . ASP A 1 4081 ? 192.444 149.380 136.890 1.00 66.66  ? 4081 ASP A O     1 
ATOM   19812 C CB    . ASP A 1 4081 ? 191.258 152.314 138.040 1.00 66.66  ? 4081 ASP A CB    1 
ATOM   19813 C CG    . ASP A 1 4081 ? 190.055 152.537 138.934 1.00 66.66  ? 4081 ASP A CG    1 
ATOM   19814 O OD1   . ASP A 1 4081 ? 189.954 153.626 139.537 1.00 66.66  ? 4081 ASP A OD1   1 
ATOM   19815 O OD2   . ASP A 1 4081 ? 189.209 151.624 139.033 1.00 66.66  ? 4081 ASP A OD2   1 
ATOM   19816 N N     . LYS A 1 4082 ? 193.853 151.137 136.781 1.00 65.38  ? 4082 LYS A N     1 
ATOM   19817 C CA    . LYS A 1 4082 ? 194.595 150.556 135.667 1.00 65.38  ? 4082 LYS A CA    1 
ATOM   19818 C C     . LYS A 1 4082 ? 195.258 149.247 136.073 1.00 65.38  ? 4082 LYS A C     1 
ATOM   19819 O O     . LYS A 1 4082 ? 195.252 148.274 135.307 1.00 65.38  ? 4082 LYS A O     1 
ATOM   19820 C CB    . LYS A 1 4082 ? 195.638 151.549 135.155 1.00 65.38  ? 4082 LYS A CB    1 
ATOM   19821 C CG    . LYS A 1 4082 ? 195.908 151.451 133.662 1.00 65.38  ? 4082 LYS A CG    1 
ATOM   19822 C CD    . LYS A 1 4082 ? 196.908 152.502 133.209 1.00 65.38  ? 4082 LYS A CD    1 
ATOM   19823 C CE    . LYS A 1 4082 ? 196.231 153.836 132.942 1.00 65.38  ? 4082 LYS A CE    1 
ATOM   19824 N NZ    . LYS A 1 4082 ? 197.197 154.969 133.001 1.00 65.38  ? 4082 LYS A NZ    1 
ATOM   19825 N N     . ALA A 1 4083 ? 195.830 149.203 137.279 1.00 62.74  ? 4083 ALA A N     1 
ATOM   19826 C CA    . ALA A 1 4083 ? 196.513 147.997 137.729 1.00 62.74  ? 4083 ALA A CA    1 
ATOM   19827 C C     . ALA A 1 4083 ? 195.548 146.830 137.871 1.00 62.74  ? 4083 ALA A C     1 
ATOM   19828 O O     . ALA A 1 4083 ? 195.862 145.711 137.458 1.00 62.74  ? 4083 ALA A O     1 
ATOM   19829 C CB    . ALA A 1 4083 ? 197.228 148.259 139.052 1.00 62.74  ? 4083 ALA A CB    1 
ATOM   19830 N N     . ILE A 1 4084 ? 194.367 147.064 138.450 1.00 61.42  ? 4084 ILE A N     1 
ATOM   19831 C CA    . ILE A 1 4084 ? 193.423 145.966 138.626 1.00 61.42  ? 4084 ILE A CA    1 
ATOM   19832 C C     . ILE A 1 4084 ? 192.882 145.509 137.279 1.00 61.42  ? 4084 ILE A C     1 
ATOM   19833 O O     . ILE A 1 4084 ? 192.722 144.305 137.042 1.00 61.42  ? 4084 ILE A O     1 
ATOM   19834 C CB    . ILE A 1 4084 ? 192.292 146.344 139.604 1.00 61.42  ? 4084 ILE A CB    1 
ATOM   19835 C CG1   . ILE A 1 4084 ? 191.413 147.466 139.051 1.00 61.42  ? 4084 ILE A CG1   1 
ATOM   19836 C CG2   . ILE A 1 4084 ? 192.861 146.710 140.966 1.00 61.42  ? 4084 ILE A CG2   1 
ATOM   19837 C CD1   . ILE A 1 4084 ? 190.136 147.679 139.830 1.00 61.42  ? 4084 ILE A CD1   1 
ATOM   19838 N N     . ASN A 1 4085 ? 192.620 146.448 136.363 1.00 61.99  ? 4085 ASN A N     1 
ATOM   19839 C CA    . ASN A 1 4085 ? 192.175 146.054 135.030 1.00 61.99  ? 4085 ASN A CA    1 
ATOM   19840 C C     . ASN A 1 4085 ? 193.215 145.169 134.351 1.00 61.99  ? 4085 ASN A C     1 
ATOM   19841 O O     . ASN A 1 4085 ? 192.901 144.069 133.878 1.00 61.99  ? 4085 ASN A O     1 
ATOM   19842 C CB    . ASN A 1 4085 ? 191.887 147.295 134.185 1.00 61.99  ? 4085 ASN A CB    1 
ATOM   19843 C CG    . ASN A 1 4085 ? 190.708 148.096 134.705 1.00 61.99  ? 4085 ASN A CG    1 
ATOM   19844 O OD1   . ASN A 1 4085 ? 189.716 147.536 135.171 1.00 61.99  ? 4085 ASN A OD1   1 
ATOM   19845 N ND2   . ASN A 1 4085 ? 190.815 149.418 134.630 1.00 61.99  ? 4085 ASN A ND2   1 
ATOM   19846 N N     . THR A 1 4086 ? 194.472 145.621 134.329 1.00 63.90  ? 4086 THR A N     1 
ATOM   19847 C CA    . THR A 1 4086 ? 195.525 144.856 133.670 1.00 63.90  ? 4086 THR A CA    1 
ATOM   19848 C C     . THR A 1 4086 ? 195.754 143.512 134.350 1.00 63.90  ? 4086 THR A C     1 
ATOM   19849 O O     . THR A 1 4086 ? 195.937 142.498 133.667 1.00 63.90  ? 4086 THR A O     1 
ATOM   19850 C CB    . THR A 1 4086 ? 196.821 145.669 133.643 1.00 63.90  ? 4086 THR A CB    1 
ATOM   19851 O OG1   . THR A 1 4086 ? 196.630 146.848 132.851 1.00 63.90  ? 4086 THR A OG1   1 
ATOM   19852 C CG2   . THR A 1 4086 ? 197.965 144.853 133.054 1.00 63.90  ? 4086 THR A CG2   1 
ATOM   19853 N N     . ALA A 1 4087 ? 195.727 143.480 135.684 1.00 63.52  ? 4087 ALA A N     1 
ATOM   19854 C CA    . ALA A 1 4087 ? 196.023 142.252 136.408 1.00 63.52  ? 4087 ALA A CA    1 
ATOM   19855 C C     . ALA A 1 4087 ? 194.894 141.240 136.293 1.00 63.52  ? 4087 ALA A C     1 
ATOM   19856 O O     . ALA A 1 4087 ? 195.145 140.032 136.360 1.00 63.52  ? 4087 ALA A O     1 
ATOM   19857 C CB    . ALA A 1 4087 ? 196.311 142.569 137.875 1.00 63.52  ? 4087 ALA A CB    1 
ATOM   19858 N N     . VAL A 1 4088 ? 193.651 141.698 136.126 1.00 66.07  ? 4088 VAL A N     1 
ATOM   19859 C CA    . VAL A 1 4088 ? 192.571 140.742 135.916 1.00 66.07  ? 4088 VAL A CA    1 
ATOM   19860 C C     . VAL A 1 4088 ? 192.475 140.301 134.460 1.00 66.07  ? 4088 VAL A C     1 
ATOM   19861 O O     . VAL A 1 4088 ? 192.013 139.185 134.193 1.00 66.07  ? 4088 VAL A O     1 
ATOM   19862 C CB    . VAL A 1 4088 ? 191.221 141.296 136.402 1.00 66.07  ? 4088 VAL A CB    1 
ATOM   19863 C CG1   . VAL A 1 4088 ? 190.660 142.350 135.442 1.00 66.07  ? 4088 VAL A CG1   1 
ATOM   19864 C CG2   . VAL A 1 4088 ? 190.247 140.150 136.604 1.00 66.07  ? 4088 VAL A CG2   1 
ATOM   19865 N N     . LYS A 1 4089 ? 192.909 141.128 133.506 1.00 66.17  ? 4089 LYS A N     1 
ATOM   19866 C CA    . LYS A 1 4089 ? 193.008 140.649 132.129 1.00 66.17  ? 4089 LYS A CA    1 
ATOM   19867 C C     . LYS A 1 4089 ? 194.120 139.614 131.988 1.00 66.17  ? 4089 LYS A C     1 
ATOM   19868 O O     . LYS A 1 4089 ? 193.926 138.554 131.383 1.00 66.17  ? 4089 LYS A O     1 
ATOM   19869 C CB    . LYS A 1 4089 ? 193.241 141.816 131.166 1.00 66.17  ? 4089 LYS A CB    1 
ATOM   19870 C CG    . LYS A 1 4089 ? 192.148 142.868 131.159 1.00 66.17  ? 4089 LYS A CG    1 
ATOM   19871 C CD    . LYS A 1 4089 ? 190.842 142.304 130.634 1.00 66.17  ? 4089 LYS A CD    1 
ATOM   19872 C CE    . LYS A 1 4089 ? 189.797 143.395 130.475 1.00 66.17  ? 4089 LYS A CE    1 
ATOM   19873 N NZ    . LYS A 1 4089 ? 189.344 143.940 131.784 1.00 66.17  ? 4089 LYS A NZ    1 
ATOM   19874 N N     . SER A 1 4090 ? 195.301 139.915 132.531 1.00 68.73  ? 4090 SER A N     1 
ATOM   19875 C CA    . SER A 1 4090 ? 196.429 138.997 132.410 1.00 68.73  ? 4090 SER A CA    1 
ATOM   19876 C C     . SER A 1 4090 ? 196.330 137.850 133.408 1.00 68.73  ? 4090 SER A C     1 
ATOM   19877 O O     . SER A 1 4090 ? 196.551 136.688 133.049 1.00 68.73  ? 4090 SER A O     1 
ATOM   19878 C CB    . SER A 1 4090 ? 197.740 139.760 132.592 1.00 68.73  ? 4090 SER A CB    1 
ATOM   19879 O OG    . SER A 1 4090 ? 197.789 140.380 133.864 1.00 68.73  ? 4090 SER A OG    1 
ATOM   19880 N N     . GLY A 1 4091 ? 196.000 138.153 134.662 1.00 66.73  ? 4091 GLY A N     1 
ATOM   19881 C CA    . GLY A 1 4091 ? 195.911 137.127 135.683 1.00 66.73  ? 4091 GLY A CA    1 
ATOM   19882 C C     . GLY A 1 4091 ? 196.934 137.280 136.789 1.00 66.73  ? 4091 GLY A C     1 
ATOM   19883 O O     . GLY A 1 4091 ? 197.363 136.288 137.385 1.00 66.73  ? 4091 GLY A O     1 
ATOM   19884 N N     . ARG A 1 4092 ? 197.336 138.515 137.071 1.00 65.54  ? 4092 ARG A N     1 
ATOM   19885 C CA    . ARG A 1 4092 ? 198.330 138.804 138.089 1.00 65.54  ? 4092 ARG A CA    1 
ATOM   19886 C C     . ARG A 1 4092 ? 197.644 139.270 139.373 1.00 65.54  ? 4092 ARG A C     1 
ATOM   19887 O O     . ARG A 1 4092 ? 196.417 139.226 139.502 1.00 65.54  ? 4092 ARG A O     1 
ATOM   19888 C CB    . ARG A 1 4092 ? 199.328 139.838 137.567 1.00 65.54  ? 4092 ARG A CB    1 
ATOM   19889 C CG    . ARG A 1 4092 ? 199.783 139.606 136.132 1.00 65.54  ? 4092 ARG A CG    1 
ATOM   19890 C CD    . ARG A 1 4092 ? 201.078 138.805 136.053 1.00 65.54  ? 4092 ARG A CD    1 
ATOM   19891 N NE    . ARG A 1 4092 ? 200.999 137.535 136.766 1.00 65.54  ? 4092 ARG A NE    1 
ATOM   19892 C CZ    . ARG A 1 4092 ? 200.351 136.465 136.324 1.00 65.54  ? 4092 ARG A CZ    1 
ATOM   19893 N NH1   . ARG A 1 4092 ? 199.721 136.468 135.161 1.00 65.54  ? 4092 ARG A NH1   1 
ATOM   19894 N NH2   . ARG A 1 4092 ? 200.337 135.362 137.069 1.00 65.54  ? 4092 ARG A NH2   1 
ATOM   19895 N N     . TRP A 1 4093 ? 198.442 139.720 140.338 1.00 55.68  ? 4093 TRP A N     1 
ATOM   19896 C CA    . TRP A 1 4093 ? 197.947 140.153 141.637 1.00 55.68  ? 4093 TRP A CA    1 
ATOM   19897 C C     . TRP A 1 4093 ? 198.135 141.657 141.780 1.00 55.68  ? 4093 TRP A C     1 
ATOM   19898 O O     . TRP A 1 4093 ? 199.054 142.235 141.191 1.00 55.68  ? 4093 TRP A O     1 
ATOM   19899 C CB    . TRP A 1 4093 ? 198.674 139.433 142.774 1.00 55.68  ? 4093 TRP A CB    1 
ATOM   19900 C CG    . TRP A 1 4093 ? 198.246 138.012 142.951 1.00 55.68  ? 4093 TRP A CG    1 
ATOM   19901 C CD1   . TRP A 1 4093 ? 197.247 137.370 142.284 1.00 55.68  ? 4093 TRP A CD1   1 
ATOM   19902 C CD2   . TRP A 1 4093 ? 198.804 137.055 143.859 1.00 55.68  ? 4093 TRP A CD2   1 
ATOM   19903 N NE1   . TRP A 1 4093 ? 197.150 136.069 142.715 1.00 55.68  ? 4093 TRP A NE1   1 
ATOM   19904 C CE2   . TRP A 1 4093 ? 198.094 135.851 143.684 1.00 55.68  ? 4093 TRP A CE2   1 
ATOM   19905 C CE3   . TRP A 1 4093 ? 199.834 137.098 144.801 1.00 55.68  ? 4093 TRP A CE3   1 
ATOM   19906 C CZ2   . TRP A 1 4093 ? 198.381 134.702 144.415 1.00 55.68  ? 4093 TRP A CZ2   1 
ATOM   19907 C CZ3   . TRP A 1 4093 ? 200.118 135.957 145.525 1.00 55.68  ? 4093 TRP A CZ3   1 
ATOM   19908 C CH2   . TRP A 1 4093 ? 199.394 134.775 145.329 1.00 55.68  ? 4093 TRP A CH2   1 
ATOM   19909 N N     . VAL A 1 4094 ? 197.264 142.286 142.566 1.00 50.08  ? 4094 VAL A N     1 
ATOM   19910 C CA    . VAL A 1 4094 ? 197.297 143.726 142.789 1.00 50.08  ? 4094 VAL A CA    1 
ATOM   19911 C C     . VAL A 1 4094 ? 197.166 143.983 144.285 1.00 50.08  ? 4094 VAL A C     1 
ATOM   19912 O O     . VAL A 1 4094 ? 196.489 143.229 144.992 1.00 50.08  ? 4094 VAL A O     1 
ATOM   19913 C CB    . VAL A 1 4094 ? 196.182 144.448 142.006 1.00 50.08  ? 4094 VAL A CB    1 
ATOM   19914 C CG1   . VAL A 1 4094 ? 194.817 143.924 142.415 1.00 50.08  ? 4094 VAL A CG1   1 
ATOM   19915 C CG2   . VAL A 1 4094 ? 196.272 145.957 142.188 1.00 50.08  ? 4094 VAL A CG2   1 
ATOM   19916 N N     . MET A 1 4095 ? 197.821 145.037 144.765 1.00 48.45  ? 4095 MET A N     1 
ATOM   19917 C CA    . MET A 1 4095 ? 197.786 145.430 146.167 1.00 48.45  ? 4095 MET A CA    1 
ATOM   19918 C C     . MET A 1 4095 ? 197.222 146.837 146.265 1.00 48.45  ? 4095 MET A C     1 
ATOM   19919 O O     . MET A 1 4095 ? 197.438 147.659 145.369 1.00 48.45  ? 4095 MET A O     1 
ATOM   19920 C CB    . MET A 1 4095 ? 199.185 145.409 146.782 1.00 48.45  ? 4095 MET A CB    1 
ATOM   19921 C CG    . MET A 1 4095 ? 199.251 145.678 148.270 1.00 48.45  ? 4095 MET A CG    1 
ATOM   19922 S SD    . MET A 1 4095 ? 200.963 145.617 148.824 1.00 48.45  ? 4095 MET A SD    1 
ATOM   19923 C CE    . MET A 1 4095 ? 201.284 143.866 148.705 1.00 48.45  ? 4095 MET A CE    1 
ATOM   19924 N N     . LEU A 1 4096 ? 196.508 147.115 147.349 1.00 40.15  ? 4096 LEU A N     1 
ATOM   19925 C CA    . LEU A 1 4096 ? 196.040 148.460 147.657 1.00 40.15  ? 4096 LEU A CA    1 
ATOM   19926 C C     . LEU A 1 4096 ? 196.286 148.702 149.139 1.00 40.15  ? 4096 LEU A C     1 
ATOM   19927 O O     . LEU A 1 4096 ? 195.610 148.113 149.990 1.00 40.15  ? 4096 LEU A O     1 
ATOM   19928 C CB    . LEU A 1 4096 ? 194.568 148.630 147.294 1.00 40.15  ? 4096 LEU A CB    1 
ATOM   19929 C CG    . LEU A 1 4096 ? 194.246 148.709 145.800 1.00 40.15  ? 4096 LEU A CG    1 
ATOM   19930 C CD1   . LEU A 1 4096 ? 194.019 147.329 145.201 1.00 40.15  ? 4096 LEU A CD1   1 
ATOM   19931 C CD2   . LEU A 1 4096 ? 193.042 149.594 145.576 1.00 40.15  ? 4096 LEU A CD2   1 
ATOM   19932 N N     . LYS A 1 4097 ? 197.252 149.561 149.446 1.00 40.45  ? 4097 LYS A N     1 
ATOM   19933 C CA    . LYS A 1 4097 ? 197.688 149.793 150.814 1.00 40.45  ? 4097 LYS A CA    1 
ATOM   19934 C C     . LYS A 1 4097 ? 197.001 151.023 151.388 1.00 40.45  ? 4097 LYS A C     1 
ATOM   19935 O O     . LYS A 1 4097 ? 196.852 152.039 150.703 1.00 40.45  ? 4097 LYS A O     1 
ATOM   19936 C CB    . LYS A 1 4097 ? 199.206 149.966 150.875 1.00 40.45  ? 4097 LYS A CB    1 
ATOM   19937 C CG    . LYS A 1 4097 ? 199.981 148.758 150.385 1.00 40.45  ? 4097 LYS A CG    1 
ATOM   19938 C CD    . LYS A 1 4097 ? 201.469 148.916 150.639 1.00 40.45  ? 4097 LYS A CD    1 
ATOM   19939 C CE    . LYS A 1 4097 ? 202.055 150.033 149.793 1.00 40.45  ? 4097 LYS A CE    1 
ATOM   19940 N NZ    . LYS A 1 4097 ? 201.989 149.724 148.338 1.00 40.45  ? 4097 LYS A NZ    1 
ATOM   19941 N N     . ASN A 1 4098 ? 196.586 150.920 152.651 1.00 38.39  ? 4098 ASN A N     1 
ATOM   19942 C CA    . ASN A 1 4098 ? 195.944 152.014 153.377 1.00 38.39  ? 4098 ASN A CA    1 
ATOM   19943 C C     . ASN A 1 4098 ? 194.688 152.495 152.646 1.00 38.39  ? 4098 ASN A C     1 
ATOM   19944 O O     . ASN A 1 4098 ? 194.540 153.670 152.306 1.00 38.39  ? 4098 ASN A O     1 
ATOM   19945 C CB    . ASN A 1 4098 ? 196.928 153.167 153.606 1.00 38.39  ? 4098 ASN A CB    1 
ATOM   19946 C CG    . ASN A 1 4098 ? 198.022 152.810 154.590 1.00 38.39  ? 4098 ASN A CG    1 
ATOM   19947 O OD1   . ASN A 1 4098 ? 197.769 152.180 155.616 1.00 38.39  ? 4098 ASN A OD1   1 
ATOM   19948 N ND2   . ASN A 1 4098 ? 199.250 153.209 154.279 1.00 38.39  ? 4098 ASN A ND2   1 
ATOM   19949 N N     . VAL A 1 4099 ? 193.774 151.550 152.407 1.00 37.18  ? 4099 VAL A N     1 
ATOM   19950 C CA    . VAL A 1 4099 ? 192.524 151.877 151.725 1.00 37.18  ? 4099 VAL A CA    1 
ATOM   19951 C C     . VAL A 1 4099 ? 191.467 152.430 152.663 1.00 37.18  ? 4099 VAL A C     1 
ATOM   19952 O O     . VAL A 1 4099 ? 190.391 152.828 152.199 1.00 37.18  ? 4099 VAL A O     1 
ATOM   19953 C CB    . VAL A 1 4099 ? 191.946 150.651 150.995 1.00 37.18  ? 4099 VAL A CB    1 
ATOM   19954 C CG1   . VAL A 1 4099 ? 193.011 150.005 150.142 1.00 37.18  ? 4099 VAL A CG1   1 
ATOM   19955 C CG2   . VAL A 1 4099 ? 191.381 149.658 151.988 1.00 37.18  ? 4099 VAL A CG2   1 
ATOM   19956 N N     . HIS A 1 4100 ? 191.737 152.469 153.968 1.00 39.00  ? 4100 HIS A N     1 
ATOM   19957 C CA    . HIS A 1 4100 ? 190.798 153.068 154.908 1.00 39.00  ? 4100 HIS A CA    1 
ATOM   19958 C C     . HIS A 1 4100 ? 190.692 154.577 154.743 1.00 39.00  ? 4100 HIS A C     1 
ATOM   19959 O O     . HIS A 1 4100 ? 189.786 155.184 155.325 1.00 39.00  ? 4100 HIS A O     1 
ATOM   19960 C CB    . HIS A 1 4100 ? 191.203 152.731 156.344 1.00 39.00  ? 4100 HIS A CB    1 
ATOM   19961 C CG    . HIS A 1 4100 ? 192.596 153.150 156.695 1.00 39.00  ? 4100 HIS A CG    1 
ATOM   19962 N ND1   . HIS A 1 4100 ? 193.713 152.504 156.211 1.00 39.00  ? 4100 HIS A ND1   1 
ATOM   19963 C CD2   . HIS A 1 4100 ? 193.054 154.150 157.485 1.00 39.00  ? 4100 HIS A CD2   1 
ATOM   19964 C CE1   . HIS A 1 4100 ? 194.798 153.088 156.687 1.00 39.00  ? 4100 HIS A CE1   1 
ATOM   19965 N NE2   . HIS A 1 4100 ? 194.426 154.089 157.463 1.00 39.00  ? 4100 HIS A NE2   1 
ATOM   19966 N N     . LEU A 1 4101 ? 191.589 155.192 153.972 1.00 40.37  ? 4101 LEU A N     1 
ATOM   19967 C CA    . LEU A 1 4101 ? 191.566 156.630 153.749 1.00 40.37  ? 4101 LEU A CA    1 
ATOM   19968 C C     . LEU A 1 4101 ? 190.580 157.051 152.668 1.00 40.37  ? 4101 LEU A C     1 
ATOM   19969 O O     . LEU A 1 4101 ? 190.312 158.249 152.532 1.00 40.37  ? 4101 LEU A O     1 
ATOM   19970 C CB    . LEU A 1 4101 ? 192.968 157.119 153.376 1.00 40.37  ? 4101 LEU A CB    1 
ATOM   19971 C CG    . LEU A 1 4101 ? 194.054 156.910 154.432 1.00 40.37  ? 4101 LEU A CG    1 
ATOM   19972 C CD1   . LEU A 1 4101 ? 195.417 157.310 153.891 1.00 40.37  ? 4101 LEU A CD1   1 
ATOM   19973 C CD2   . LEU A 1 4101 ? 193.727 157.687 155.691 1.00 40.37  ? 4101 LEU A CD2   1 
ATOM   19974 N N     . ALA A 1 4102 ? 190.036 156.107 151.900 1.00 46.78  ? 4102 ALA A N     1 
ATOM   19975 C CA    . ALA A 1 4102 ? 189.115 156.401 150.802 1.00 46.78  ? 4102 ALA A CA    1 
ATOM   19976 C C     . ALA A 1 4102 ? 187.884 155.516 150.935 1.00 46.78  ? 4102 ALA A C     1 
ATOM   19977 O O     . ALA A 1 4102 ? 187.750 154.506 150.230 1.00 46.78  ? 4102 ALA A O     1 
ATOM   19978 C CB    . ALA A 1 4102 ? 189.795 156.202 149.447 1.00 46.78  ? 4102 ALA A CB    1 
ATOM   19979 N N     . PRO A 1 4103 ? 186.959 155.863 151.835 1.00 50.99  ? 4103 PRO A N     1 
ATOM   19980 C CA    . PRO A 1 4103 ? 185.758 155.036 152.022 1.00 50.99  ? 4103 PRO A CA    1 
ATOM   19981 C C     . PRO A 1 4103 ? 184.857 155.009 150.797 1.00 50.99  ? 4103 PRO A C     1 
ATOM   19982 O O     . PRO A 1 4103 ? 184.397 153.941 150.376 1.00 50.99  ? 4103 PRO A O     1 
ATOM   19983 C CB    . PRO A 1 4103 ? 185.054 155.700 153.215 1.00 50.99  ? 4103 PRO A CB    1 
ATOM   19984 C CG    . PRO A 1 4103 ? 186.103 156.552 153.868 1.00 50.99  ? 4103 PRO A CG    1 
ATOM   19985 C CD    . PRO A 1 4103 ? 186.992 157.006 152.760 1.00 50.99  ? 4103 PRO A CD    1 
ATOM   19986 N N     . GLY A 1 4104 ? 184.590 156.183 150.222 1.00 49.35  ? 4104 GLY A N     1 
ATOM   19987 C CA    . GLY A 1 4104 ? 183.758 156.236 149.032 1.00 49.35  ? 4104 GLY A CA    1 
ATOM   19988 C C     . GLY A 1 4104 ? 184.373 155.493 147.863 1.00 49.35  ? 4104 GLY A C     1 
ATOM   19989 O O     . GLY A 1 4104 ? 183.684 154.761 147.145 1.00 49.35  ? 4104 GLY A O     1 
ATOM   19990 N N     . TRP A 1 4105 ? 185.680 155.666 147.658 1.00 51.09  ? 4105 TRP A N     1 
ATOM   19991 C CA    . TRP A 1 4105 ? 186.354 154.909 146.613 1.00 51.09  ? 4105 TRP A CA    1 
ATOM   19992 C C     . TRP A 1 4105 ? 186.339 153.419 146.917 1.00 51.09  ? 4105 TRP A C     1 
ATOM   19993 O O     . TRP A 1 4105 ? 186.289 152.602 145.995 1.00 51.09  ? 4105 TRP A O     1 
ATOM   19994 C CB    . TRP A 1 4105 ? 187.786 155.411 146.431 1.00 51.09  ? 4105 TRP A CB    1 
ATOM   19995 C CG    . TRP A 1 4105 ? 188.448 154.865 145.205 1.00 51.09  ? 4105 TRP A CG    1 
ATOM   19996 C CD1   . TRP A 1 4105 ? 188.549 155.479 143.993 1.00 51.09  ? 4105 TRP A CD1   1 
ATOM   19997 C CD2   . TRP A 1 4105 ? 189.114 153.605 145.073 1.00 51.09  ? 4105 TRP A CD2   1 
ATOM   19998 N NE1   . TRP A 1 4105 ? 189.227 154.677 143.110 1.00 51.09  ? 4105 TRP A NE1   1 
ATOM   19999 C CE2   . TRP A 1 4105 ? 189.586 153.520 143.749 1.00 51.09  ? 4105 TRP A CE2   1 
ATOM   20000 C CE3   . TRP A 1 4105 ? 189.356 152.539 145.943 1.00 51.09  ? 4105 TRP A CE3   1 
ATOM   20001 C CZ2   . TRP A 1 4105 ? 190.283 152.414 143.275 1.00 51.09  ? 4105 TRP A CZ2   1 
ATOM   20002 C CZ3   . TRP A 1 4105 ? 190.045 151.443 145.470 1.00 51.09  ? 4105 TRP A CZ3   1 
ATOM   20003 C CH2   . TRP A 1 4105 ? 190.501 151.388 144.148 1.00 51.09  ? 4105 TRP A CH2   1 
ATOM   20004 N N     . LEU A 1 4106 ? 186.371 153.045 148.199 1.00 47.09  ? 4106 LEU A N     1 
ATOM   20005 C CA    . LEU A 1 4106 ? 186.221 151.638 148.557 1.00 47.09  ? 4106 LEU A CA    1 
ATOM   20006 C C     . LEU A 1 4106 ? 184.853 151.108 148.148 1.00 47.09  ? 4106 LEU A C     1 
ATOM   20007 O O     . LEU A 1 4106 ? 184.739 149.983 147.646 1.00 47.09  ? 4106 LEU A O     1 
ATOM   20008 C CB    . LEU A 1 4106 ? 186.439 151.447 150.057 1.00 47.09  ? 4106 LEU A CB    1 
ATOM   20009 C CG    . LEU A 1 4106 ? 187.877 151.204 150.512 1.00 47.09  ? 4106 LEU A CG    1 
ATOM   20010 C CD1   . LEU A 1 4106 ? 187.896 150.745 151.959 1.00 47.09  ? 4106 LEU A CD1   1 
ATOM   20011 C CD2   . LEU A 1 4106 ? 188.551 150.184 149.612 1.00 47.09  ? 4106 LEU A CD2   1 
ATOM   20012 N N     . MET A 1 4107 ? 183.799 151.899 148.362 1.00 52.36  ? 4107 MET A N     1 
ATOM   20013 C CA    . MET A 1 4107 ? 182.467 151.465 147.953 1.00 52.36  ? 4107 MET A CA    1 
ATOM   20014 C C     . MET A 1 4107 ? 182.382 151.336 146.435 1.00 52.36  ? 4107 MET A C     1 
ATOM   20015 O O     . MET A 1 4107 ? 181.778 150.389 145.913 1.00 52.36  ? 4107 MET A O     1 
ATOM   20016 C CB    . MET A 1 4107 ? 181.413 152.444 148.471 1.00 52.36  ? 4107 MET A CB    1 
ATOM   20017 C CG    . MET A 1 4107 ? 180.592 151.918 149.644 1.00 52.36  ? 4107 MET A CG    1 
ATOM   20018 S SD    . MET A 1 4107 ? 179.778 150.328 149.391 1.00 52.36  ? 4107 MET A SD    1 
ATOM   20019 C CE    . MET A 1 4107 ? 178.886 150.617 147.870 1.00 52.36  ? 4107 MET A CE    1 
ATOM   20020 N N     . GLN A 1 4108 ? 182.991 152.280 145.712 1.00 55.78  ? 4108 GLN A N     1 
ATOM   20021 C CA    . GLN A 1 4108 ? 183.035 152.180 144.254 1.00 55.78  ? 4108 GLN A CA    1 
ATOM   20022 C C     . GLN A 1 4108 ? 183.791 150.933 143.809 1.00 55.78  ? 4108 GLN A C     1 
ATOM   20023 O O     . GLN A 1 4108 ? 183.383 150.257 142.857 1.00 55.78  ? 4108 GLN A O     1 
ATOM   20024 C CB    . GLN A 1 4108 ? 183.676 153.431 143.649 1.00 55.78  ? 4108 GLN A CB    1 
ATOM   20025 C CG    . GLN A 1 4108 ? 183.095 154.759 144.119 1.00 55.78  ? 4108 GLN A CG    1 
ATOM   20026 C CD    . GLN A 1 4108 ? 181.577 154.799 144.104 1.00 55.78  ? 4108 GLN A CD    1 
ATOM   20027 O OE1   . GLN A 1 4108 ? 180.933 154.198 143.244 1.00 55.78  ? 4108 GLN A OE1   1 
ATOM   20028 N NE2   . GLN A 1 4108 ? 180.998 155.510 145.064 1.00 55.78  ? 4108 GLN A NE2   1 
ATOM   20029 N N     . LEU A 1 4109 ? 184.902 150.621 144.478 1.00 53.31  ? 4109 LEU A N     1 
ATOM   20030 C CA    . LEU A 1 4109 ? 185.662 149.421 144.148 1.00 53.31  ? 4109 LEU A CA    1 
ATOM   20031 C C     . LEU A 1 4109 ? 184.833 148.170 144.399 1.00 53.31  ? 4109 LEU A C     1 
ATOM   20032 O O     . LEU A 1 4109 ? 184.872 147.218 143.611 1.00 53.31  ? 4109 LEU A O     1 
ATOM   20033 C CB    . LEU A 1 4109 ? 186.953 149.381 144.965 1.00 53.31  ? 4109 LEU A CB    1 
ATOM   20034 C CG    . LEU A 1 4109 ? 187.729 148.062 144.989 1.00 53.31  ? 4109 LEU A CG    1 
ATOM   20035 C CD1   . LEU A 1 4109 ? 188.110 147.647 143.577 1.00 53.31  ? 4109 LEU A CD1   1 
ATOM   20036 C CD2   . LEU A 1 4109 ? 188.957 148.152 145.879 1.00 53.31  ? 4109 LEU A CD2   1 
ATOM   20037 N N     . GLU A 1 4110 ? 184.080 148.152 145.501 1.00 53.64  ? 4110 GLU A N     1 
ATOM   20038 C CA    . GLU A 1 4110 ? 183.215 147.015 145.790 1.00 53.64  ? 4110 GLU A CA    1 
ATOM   20039 C C     . GLU A 1 4110 ? 182.151 146.854 144.713 1.00 53.64  ? 4110 GLU A C     1 
ATOM   20040 O O     . GLU A 1 4110 ? 181.841 145.730 144.298 1.00 53.64  ? 4110 GLU A O     1 
ATOM   20041 C CB    . GLU A 1 4110 ? 182.575 147.177 147.171 1.00 53.64  ? 4110 GLU A CB    1 
ATOM   20042 C CG    . GLU A 1 4110 ? 181.867 145.931 147.698 1.00 53.64  ? 4110 GLU A CG    1 
ATOM   20043 C CD    . GLU A 1 4110 ? 180.422 145.817 147.243 1.00 53.64  ? 4110 GLU A CD    1 
ATOM   20044 O OE1   . GLU A 1 4110 ? 179.918 146.755 146.591 1.00 53.64  ? 4110 GLU A OE1   1 
ATOM   20045 O OE2   . GLU A 1 4110 ? 179.788 144.783 147.539 1.00 53.64  ? 4110 GLU A OE2   1 
ATOM   20046 N N     . LYS A 1 4111 ? 181.572 147.966 144.253 1.00 59.65  ? 4111 LYS A N     1 
ATOM   20047 C CA    . LYS A 1 4111 ? 180.612 147.887 143.155 1.00 59.65  ? 4111 LYS A CA    1 
ATOM   20048 C C     . LYS A 1 4111 ? 181.266 147.347 141.888 1.00 59.65  ? 4111 LYS A C     1 
ATOM   20049 O O     . LYS A 1 4111 ? 180.688 146.505 141.191 1.00 59.65  ? 4111 LYS A O     1 
ATOM   20050 C CB    . LYS A 1 4111 ? 179.992 149.257 142.880 1.00 59.65  ? 4111 LYS A CB    1 
ATOM   20051 C CG    . LYS A 1 4111 ? 178.945 149.698 143.884 1.00 59.65  ? 4111 LYS A CG    1 
ATOM   20052 C CD    . LYS A 1 4111 ? 178.528 151.139 143.624 1.00 59.65  ? 4111 LYS A CD    1 
ATOM   20053 C CE    . LYS A 1 4111 ? 179.047 152.079 144.695 1.00 59.65  ? 4111 LYS A CE    1 
ATOM   20054 N NZ    . LYS A 1 4111 ? 178.109 153.208 144.943 1.00 59.65  ? 4111 LYS A NZ    1 
ATOM   20055 N N     . LYS A 1 4112 ? 182.473 147.824 141.574 1.00 59.18  ? 4112 LYS A N     1 
ATOM   20056 C CA    . LYS A 1 4112 ? 183.133 147.422 140.335 1.00 59.18  ? 4112 LYS A CA    1 
ATOM   20057 C C     . LYS A 1 4112 ? 183.514 145.946 140.351 1.00 59.18  ? 4112 LYS A C     1 
ATOM   20058 O O     . LYS A 1 4112 ? 183.369 145.254 139.337 1.00 59.18  ? 4112 LYS A O     1 
ATOM   20059 C CB    . LYS A 1 4112 ? 184.364 148.294 140.088 1.00 59.18  ? 4112 LYS A CB    1 
ATOM   20060 C CG    . LYS A 1 4112 ? 184.035 149.738 139.738 1.00 59.18  ? 4112 LYS A CG    1 
ATOM   20061 C CD    . LYS A 1 4112 ? 185.271 150.498 139.281 1.00 59.18  ? 4112 LYS A CD    1 
ATOM   20062 C CE    . LYS A 1 4112 ? 186.214 150.779 140.439 1.00 59.18  ? 4112 LYS A CE    1 
ATOM   20063 N NZ    . LYS A 1 4112 ? 185.641 151.768 141.392 1.00 59.18  ? 4112 LYS A NZ    1 
ATOM   20064 N N     . LEU A 1 4113 ? 184.005 145.446 141.487 1.00 64.04  ? 4113 LEU A N     1 
ATOM   20065 C CA    . LEU A 1 4113 ? 184.421 144.049 141.563 1.00 64.04  ? 4113 LEU A CA    1 
ATOM   20066 C C     . LEU A 1 4113 ? 183.254 143.079 141.454 1.00 64.04  ? 4113 LEU A C     1 
ATOM   20067 O O     . LEU A 1 4113 ? 183.474 141.905 141.142 1.00 64.04  ? 4113 LEU A O     1 
ATOM   20068 C CB    . LEU A 1 4113 ? 185.178 143.782 142.864 1.00 64.04  ? 4113 LEU A CB    1 
ATOM   20069 C CG    . LEU A 1 4113 ? 186.526 144.476 143.043 1.00 64.04  ? 4113 LEU A CG    1 
ATOM   20070 C CD1   . LEU A 1 4113 ? 187.073 144.217 144.436 1.00 64.04  ? 4113 LEU A CD1   1 
ATOM   20071 C CD2   . LEU A 1 4113 ? 187.509 144.012 141.981 1.00 64.04  ? 4113 LEU A CD2   1 
ATOM   20072 N N     . HIS A 1 4114 ? 182.024 143.538 141.697 1.00 71.40  ? 4114 HIS A N     1 
ATOM   20073 C CA    . HIS A 1 4114 ? 180.879 142.634 141.699 1.00 71.40  ? 4114 HIS A CA    1 
ATOM   20074 C C     . HIS A 1 4114 ? 180.657 141.996 140.332 1.00 71.40  ? 4114 HIS A C     1 
ATOM   20075 O O     . HIS A 1 4114 ? 180.061 140.917 140.250 1.00 71.40  ? 4114 HIS A O     1 
ATOM   20076 C CB    . HIS A 1 4114 ? 179.629 143.394 142.151 1.00 71.40  ? 4114 HIS A CB    1 
ATOM   20077 C CG    . HIS A 1 4114 ? 178.424 142.529 142.354 1.00 71.40  ? 4114 HIS A CG    1 
ATOM   20078 N ND1   . HIS A 1 4114 ? 178.500 141.154 142.410 1.00 71.40  ? 4114 HIS A ND1   1 
ATOM   20079 C CD2   . HIS A 1 4114 ? 177.110 142.836 142.467 1.00 71.40  ? 4114 HIS A CD2   1 
ATOM   20080 C CE1   . HIS A 1 4114 ? 177.289 140.653 142.579 1.00 71.40  ? 4114 HIS A CE1   1 
ATOM   20081 N NE2   . HIS A 1 4114 ? 176.427 141.653 142.617 1.00 71.40  ? 4114 HIS A NE2   1 
ATOM   20082 N N     . SER A 1 4115 ? 181.143 142.622 139.263 1.00 74.20  ? 4115 SER A N     1 
ATOM   20083 C CA    . SER A 1 4115 ? 181.037 142.037 137.935 1.00 74.20  ? 4115 SER A CA    1 
ATOM   20084 C C     . SER A 1 4115 ? 181.926 140.802 137.822 1.00 74.20  ? 4115 SER A C     1 
ATOM   20085 O O     . SER A 1 4115 ? 182.858 140.598 138.606 1.00 74.20  ? 4115 SER A O     1 
ATOM   20086 C CB    . SER A 1 4115 ? 181.426 143.059 136.867 1.00 74.20  ? 4115 SER A CB    1 
ATOM   20087 O OG    . SER A 1 4115 ? 182.828 143.264 136.848 1.00 74.20  ? 4115 SER A OG    1 
ATOM   20088 N N     . LEU A 1 4116 ? 181.627 139.970 136.826 1.00 81.76  ? 4116 LEU A N     1 
ATOM   20089 C CA    . LEU A 1 4116 ? 182.394 138.748 136.618 1.00 81.76  ? 4116 LEU A CA    1 
ATOM   20090 C C     . LEU A 1 4116 ? 183.839 139.084 136.272 1.00 81.76  ? 4116 LEU A C     1 
ATOM   20091 O O     . LEU A 1 4116 ? 184.104 139.939 135.422 1.00 81.76  ? 4116 LEU A O     1 
ATOM   20092 C CB    . LEU A 1 4116 ? 181.765 137.905 135.510 1.00 81.76  ? 4116 LEU A CB    1 
ATOM   20093 C CG    . LEU A 1 4116 ? 182.591 136.703 135.044 1.00 81.76  ? 4116 LEU A CG    1 
ATOM   20094 C CD1   . LEU A 1 4116 ? 182.611 135.610 136.104 1.00 81.76  ? 4116 LEU A CD1   1 
ATOM   20095 C CD2   . LEU A 1 4116 ? 182.064 136.164 133.720 1.00 81.76  ? 4116 LEU A CD2   1 
ATOM   20096 N N     . GLN A 1 4117 ? 184.775 138.410 136.941 1.00 81.67  ? 4117 GLN A N     1 
ATOM   20097 C CA    . GLN A 1 4117 ? 186.189 138.675 136.748 1.00 81.67  ? 4117 GLN A CA    1 
ATOM   20098 C C     . GLN A 1 4117 ? 186.784 137.557 135.909 1.00 81.67  ? 4117 GLN A C     1 
ATOM   20099 O O     . GLN A 1 4117 ? 186.855 136.414 136.388 1.00 81.67  ? 4117 GLN A O     1 
ATOM   20100 C CB    . GLN A 1 4117 ? 186.897 138.770 138.092 1.00 81.67  ? 4117 GLN A CB    1 
ATOM   20101 C CG    . GLN A 1 4117 ? 186.400 139.928 138.955 1.00 81.67  ? 4117 GLN A CG    1 
ATOM   20102 C CD    . GLN A 1 4117 ? 186.707 141.298 138.377 1.00 81.67  ? 4117 GLN A CD    1 
ATOM   20103 O OE1   . GLN A 1 4117 ? 187.775 141.523 137.812 1.00 81.67  ? 4117 GLN A OE1   1 
ATOM   20104 N NE2   . GLN A 1 4117 ? 185.762 142.220 138.513 1.00 81.67  ? 4117 GLN A NE2   1 
ATOM   20105 N N     . PRO A 1 4118 ? 187.228 137.828 134.679 1.00 84.22  ? 4118 PRO A N     1 
ATOM   20106 C CA    . PRO A 1 4118 ? 187.507 136.729 133.735 1.00 84.22  ? 4118 PRO A CA    1 
ATOM   20107 C C     . PRO A 1 4118 ? 188.569 135.745 134.200 1.00 84.22  ? 4118 PRO A C     1 
ATOM   20108 O O     . PRO A 1 4118 ? 188.470 134.554 133.878 1.00 84.22  ? 4118 PRO A O     1 
ATOM   20109 C CB    . PRO A 1 4118 ? 187.946 137.464 132.460 1.00 84.22  ? 4118 PRO A CB    1 
ATOM   20110 C CG    . PRO A 1 4118 ? 188.327 138.839 132.902 1.00 84.22  ? 4118 PRO A CG    1 
ATOM   20111 C CD    . PRO A 1 4118 ? 187.470 139.153 134.084 1.00 84.22  ? 4118 PRO A CD    1 
ATOM   20112 N N     . HIS A 1 4119 ? 189.576 136.190 134.942 1.00 70.36  ? 4119 HIS A N     1 
ATOM   20113 C CA    . HIS A 1 4119 ? 190.696 135.333 135.301 1.00 70.36  ? 4119 HIS A CA    1 
ATOM   20114 C C     . HIS A 1 4119 ? 190.522 134.758 136.700 1.00 70.36  ? 4119 HIS A C     1 
ATOM   20115 O O     . HIS A 1 4119 ? 189.930 135.383 137.583 1.00 70.36  ? 4119 HIS A O     1 
ATOM   20116 C CB    . HIS A 1 4119 ? 192.018 136.096 135.213 1.00 70.36  ? 4119 HIS A CB    1 
ATOM   20117 C CG    . HIS A 1 4119 ? 193.157 135.267 134.709 1.00 70.36  ? 4119 HIS A CG    1 
ATOM   20118 N ND1   . HIS A 1 4119 ? 193.649 134.181 135.401 1.00 70.36  ? 4119 HIS A ND1   1 
ATOM   20119 C CD2   . HIS A 1 4119 ? 193.890 135.353 133.575 1.00 70.36  ? 4119 HIS A CD2   1 
ATOM   20120 C CE1   . HIS A 1 4119 ? 194.643 133.641 134.719 1.00 70.36  ? 4119 HIS A CE1   1 
ATOM   20121 N NE2   . HIS A 1 4119 ? 194.810 134.334 133.607 1.00 70.36  ? 4119 HIS A NE2   1 
ATOM   20122 N N     . ALA A 1 4120 ? 191.048 133.546 136.889 1.00 62.95  ? 4120 ALA A N     1 
ATOM   20123 C CA    . ALA A 1 4120 ? 190.951 132.836 138.155 1.00 62.95  ? 4120 ALA A CA    1 
ATOM   20124 C C     . ALA A 1 4120 ? 192.214 132.929 138.999 1.00 62.95  ? 4120 ALA A C     1 
ATOM   20125 O O     . ALA A 1 4120 ? 192.160 132.632 140.197 1.00 62.95  ? 4120 ALA A O     1 
ATOM   20126 C CB    . ALA A 1 4120 ? 190.615 131.360 137.911 1.00 62.95  ? 4120 ALA A CB    1 
ATOM   20127 N N     . CYS A 1 4121 ? 193.341 133.329 138.416 1.00 58.23  ? 4121 CYS A N     1 
ATOM   20128 C CA    . CYS A 1 4121 ? 194.572 133.530 139.167 1.00 58.23  ? 4121 CYS A CA    1 
ATOM   20129 C C     . CYS A 1 4121 ? 194.681 134.935 139.741 1.00 58.23  ? 4121 CYS A C     1 
ATOM   20130 O O     . CYS A 1 4121 ? 195.693 135.258 140.371 1.00 58.23  ? 4121 CYS A O     1 
ATOM   20131 C CB    . CYS A 1 4121 ? 195.787 133.235 138.282 1.00 58.23  ? 4121 CYS A CB    1 
ATOM   20132 S SG    . CYS A 1 4121 ? 195.715 131.646 137.424 1.00 58.23  ? 4121 CYS A SG    1 
ATOM   20133 N N     . PHE A 1 4122 ? 193.667 135.769 139.536 1.00 54.96  ? 4122 PHE A N     1 
ATOM   20134 C CA    . PHE A 1 4122 ? 193.658 137.123 140.066 1.00 54.96  ? 4122 PHE A CA    1 
ATOM   20135 C C     . PHE A 1 4122 ? 193.305 137.122 141.546 1.00 54.96  ? 4122 PHE A C     1 
ATOM   20136 O O     . PHE A 1 4122 ? 192.349 136.469 141.973 1.00 54.96  ? 4122 PHE A O     1 
ATOM   20137 C CB    . PHE A 1 4122 ? 192.655 137.980 139.296 1.00 54.96  ? 4122 PHE A CB    1 
ATOM   20138 C CG    . PHE A 1 4122 ? 192.557 139.393 139.789 1.00 54.96  ? 4122 PHE A CG    1 
ATOM   20139 C CD1   . PHE A 1 4122 ? 193.547 140.313 139.501 1.00 54.96  ? 4122 PHE A CD1   1 
ATOM   20140 C CD2   . PHE A 1 4122 ? 191.468 139.801 140.537 1.00 54.96  ? 4122 PHE A CD2   1 
ATOM   20141 C CE1   . PHE A 1 4122 ? 193.454 141.613 139.953 1.00 54.96  ? 4122 PHE A CE1   1 
ATOM   20142 C CE2   . PHE A 1 4122 ? 191.371 141.098 140.992 1.00 54.96  ? 4122 PHE A CE2   1 
ATOM   20143 C CZ    . PHE A 1 4122 ? 192.364 142.006 140.699 1.00 54.96  ? 4122 PHE A CZ    1 
ATOM   20144 N N     . ARG A 1 4123 ? 194.089 137.855 142.331 1.00 49.04  ? 4123 ARG A N     1 
ATOM   20145 C CA    . ARG A 1 4123 ? 193.799 138.065 143.741 1.00 49.04  ? 4123 ARG A CA    1 
ATOM   20146 C C     . ARG A 1 4123 ? 194.016 139.534 144.064 1.00 49.04  ? 4123 ARG A C     1 
ATOM   20147 O O     . ARG A 1 4123 ? 195.038 140.114 143.686 1.00 49.04  ? 4123 ARG A O     1 
ATOM   20148 C CB    . ARG A 1 4123 ? 194.681 137.193 144.640 1.00 49.04  ? 4123 ARG A CB    1 
ATOM   20149 C CG    . ARG A 1 4123 ? 194.430 135.701 144.504 1.00 49.04  ? 4123 ARG A CG    1 
ATOM   20150 C CD    . ARG A 1 4123 ? 193.041 135.318 144.978 1.00 49.04  ? 4123 ARG A CD    1 
ATOM   20151 N NE    . ARG A 1 4123 ? 192.870 133.871 145.024 1.00 49.04  ? 4123 ARG A NE    1 
ATOM   20152 C CZ    . ARG A 1 4123 ? 192.686 133.102 143.959 1.00 49.04  ? 4123 ARG A CZ    1 
ATOM   20153 N NH1   . ARG A 1 4123 ? 192.628 133.611 142.740 1.00 49.04  ? 4123 ARG A NH1   1 
ATOM   20154 N NH2   . ARG A 1 4123 ? 192.554 131.789 144.122 1.00 49.04  ? 4123 ARG A NH2   1 
ATOM   20155 N N     . LEU A 1 4124 ? 193.057 140.130 144.763 1.00 40.54  ? 4124 LEU A N     1 
ATOM   20156 C CA    . LEU A 1 4124 ? 193.108 141.539 145.122 1.00 40.54  ? 4124 LEU A CA    1 
ATOM   20157 C C     . LEU A 1 4124 ? 193.237 141.662 146.632 1.00 40.54  ? 4124 LEU A C     1 
ATOM   20158 O O     . LEU A 1 4124 ? 192.390 141.157 147.375 1.00 40.54  ? 4124 LEU A O     1 
ATOM   20159 C CB    . LEU A 1 4124 ? 191.860 142.271 144.621 1.00 40.54  ? 4124 LEU A CB    1 
ATOM   20160 C CG    . LEU A 1 4124 ? 191.847 143.799 144.681 1.00 40.54  ? 4124 LEU A CG    1 
ATOM   20161 C CD1   . LEU A 1 4124 ? 191.145 144.364 143.461 1.00 40.54  ? 4124 LEU A CD1   1 
ATOM   20162 C CD2   . LEU A 1 4124 ? 191.161 144.278 145.939 1.00 40.54  ? 4124 LEU A CD2   1 
ATOM   20163 N N     . PHE A 1 4125 ? 194.295 142.331 147.080 1.00 35.91  ? 4125 PHE A N     1 
ATOM   20164 C CA    . PHE A 1 4125 ? 194.578 142.502 148.496 1.00 35.91  ? 4125 PHE A CA    1 
ATOM   20165 C C     . PHE A 1 4125 ? 194.343 143.951 148.893 1.00 35.91  ? 4125 PHE A C     1 
ATOM   20166 O O     . PHE A 1 4125 ? 194.809 144.873 148.217 1.00 35.91  ? 4125 PHE A O     1 
ATOM   20167 C CB    . PHE A 1 4125 ? 196.017 142.101 148.830 1.00 35.91  ? 4125 PHE A CB    1 
ATOM   20168 C CG    . PHE A 1 4125 ? 196.336 140.668 148.521 1.00 35.91  ? 4125 PHE A CG    1 
ATOM   20169 C CD1   . PHE A 1 4125 ? 196.740 140.293 147.252 1.00 35.91  ? 4125 PHE A CD1   1 
ATOM   20170 C CD2   . PHE A 1 4125 ? 196.231 139.695 149.498 1.00 35.91  ? 4125 PHE A CD2   1 
ATOM   20171 C CE1   . PHE A 1 4125 ? 197.036 138.977 146.964 1.00 35.91  ? 4125 PHE A CE1   1 
ATOM   20172 C CE2   . PHE A 1 4125 ? 196.525 138.376 149.216 1.00 35.91  ? 4125 PHE A CE2   1 
ATOM   20173 C CZ    . PHE A 1 4125 ? 196.928 138.017 147.948 1.00 35.91  ? 4125 PHE A CZ    1 
ATOM   20174 N N     . LEU A 1 4126 ? 193.620 144.145 149.991 1.00 32.85  ? 4126 LEU A N     1 
ATOM   20175 C CA    . LEU A 1 4126 ? 193.313 145.472 150.519 1.00 32.85  ? 4126 LEU A CA    1 
ATOM   20176 C C     . LEU A 1 4126 ? 193.915 145.576 151.916 1.00 32.85  ? 4126 LEU A C     1 
ATOM   20177 O O     . LEU A 1 4126 ? 193.260 145.258 152.910 1.00 32.85  ? 4126 LEU A O     1 
ATOM   20178 C CB    . LEU A 1 4126 ? 191.810 145.718 150.546 1.00 32.85  ? 4126 LEU A CB    1 
ATOM   20179 C CG    . LEU A 1 4126 ? 191.104 145.752 149.193 1.00 32.85  ? 4126 LEU A CG    1 
ATOM   20180 C CD1   . LEU A 1 4126 ? 189.605 145.572 149.366 1.00 32.85  ? 4126 LEU A CD1   1 
ATOM   20181 C CD2   . LEU A 1 4126 ? 191.412 147.048 148.467 1.00 32.85  ? 4126 LEU A CD2   1 
ATOM   20182 N N     . THR A 1 4127 ? 195.164 146.024 151.991 1.00 33.81  ? 4127 THR A N     1 
ATOM   20183 C CA    . THR A 1 4127 ? 195.811 146.277 153.269 1.00 33.81  ? 4127 THR A CA    1 
ATOM   20184 C C     . THR A 1 4127 ? 195.291 147.593 153.829 1.00 33.81  ? 4127 THR A C     1 
ATOM   20185 O O     . THR A 1 4127 ? 195.355 148.627 153.157 1.00 33.81  ? 4127 THR A O     1 
ATOM   20186 C CB    . THR A 1 4127 ? 197.330 146.330 153.113 1.00 33.81  ? 4127 THR A CB    1 
ATOM   20187 O OG1   . THR A 1 4127 ? 197.803 145.085 152.585 1.00 33.81  ? 4127 THR A OG1   1 
ATOM   20188 C CG2   . THR A 1 4127 ? 197.993 146.592 154.456 1.00 33.81  ? 4127 THR A CG2   1 
ATOM   20189 N N     . MET A 1 4128 ? 194.775 147.556 155.054 1.00 34.88  ? 4128 MET A N     1 
ATOM   20190 C CA    . MET A 1 4128 ? 194.161 148.737 155.644 1.00 34.88  ? 4128 MET A CA    1 
ATOM   20191 C C     . MET A 1 4128 ? 194.235 148.641 157.161 1.00 34.88  ? 4128 MET A C     1 
ATOM   20192 O O     . MET A 1 4128 ? 194.656 147.628 157.725 1.00 34.88  ? 4128 MET A O     1 
ATOM   20193 C CB    . MET A 1 4128 ? 192.713 148.903 155.182 1.00 34.88  ? 4128 MET A CB    1 
ATOM   20194 C CG    . MET A 1 4128 ? 191.716 148.046 155.937 1.00 34.88  ? 4128 MET A CG    1 
ATOM   20195 S SD    . MET A 1 4128 ? 190.134 147.948 155.084 1.00 34.88  ? 4128 MET A SD    1 
ATOM   20196 C CE    . MET A 1 4128 ? 190.422 146.556 154.000 1.00 34.88  ? 4128 MET A CE    1 
ATOM   20197 N N     . GLU A 1 4129 ? 193.811 149.716 157.813 1.00 38.71  ? 4129 GLU A N     1 
ATOM   20198 C CA    . GLU A 1 4129 ? 193.774 149.825 159.261 1.00 38.71  ? 4129 GLU A CA    1 
ATOM   20199 C C     . GLU A 1 4129 ? 192.349 149.576 159.741 1.00 38.71  ? 4129 GLU A C     1 
ATOM   20200 O O     . GLU A 1 4129 ? 191.382 149.848 159.027 1.00 38.71  ? 4129 GLU A O     1 
ATOM   20201 C CB    . GLU A 1 4129 ? 194.246 151.215 159.692 1.00 38.71  ? 4129 GLU A CB    1 
ATOM   20202 C CG    . GLU A 1 4129 ? 194.747 151.332 161.116 1.00 38.71  ? 4129 GLU A CG    1 
ATOM   20203 C CD    . GLU A 1 4129 ? 195.505 152.629 161.341 1.00 38.71  ? 4129 GLU A CD    1 
ATOM   20204 O OE1   . GLU A 1 4129 ? 194.901 153.705 161.151 1.00 38.71  ? 4129 GLU A OE1   1 
ATOM   20205 O OE2   . GLU A 1 4129 ? 196.706 152.578 161.676 1.00 38.71  ? 4129 GLU A OE2   1 
ATOM   20206 N N     . ILE A 1 4130 ? 192.221 149.056 160.960 1.00 35.80  ? 4130 ILE A N     1 
ATOM   20207 C CA    . ILE A 1 4130 ? 190.898 148.764 161.500 1.00 35.80  ? 4130 ILE A CA    1 
ATOM   20208 C C     . ILE A 1 4130 ? 190.217 150.071 161.881 1.00 35.80  ? 4130 ILE A C     1 
ATOM   20209 O O     . ILE A 1 4130 ? 190.463 150.622 162.959 1.00 35.80  ? 4130 ILE A O     1 
ATOM   20210 C CB    . ILE A 1 4130 ? 190.971 147.809 162.705 1.00 35.80  ? 4130 ILE A CB    1 
ATOM   20211 C CG1   . ILE A 1 4130 ? 191.736 146.539 162.337 1.00 35.80  ? 4130 ILE A CG1   1 
ATOM   20212 C CG2   . ILE A 1 4130 ? 189.576 147.470 163.200 1.00 35.80  ? 4130 ILE A CG2   1 
ATOM   20213 C CD1   . ILE A 1 4130 ? 191.795 145.524 163.454 1.00 35.80  ? 4130 ILE A CD1   1 
ATOM   20214 N N     . ASN A 1 4131 ? 189.359 150.570 160.998 1.00 37.15  ? 4131 ASN A N     1 
ATOM   20215 C CA    . ASN A 1 4131 ? 188.620 151.802 161.214 1.00 37.15  ? 4131 ASN A CA    1 
ATOM   20216 C C     . ASN A 1 4131 ? 187.157 151.590 160.860 1.00 37.15  ? 4131 ASN A C     1 
ATOM   20217 O O     . ASN A 1 4131 ? 186.841 150.814 159.953 1.00 37.15  ? 4131 ASN A O     1 
ATOM   20218 C CB    . ASN A 1 4131 ? 189.192 152.947 160.365 1.00 37.15  ? 4131 ASN A CB    1 
ATOM   20219 C CG    . ASN A 1 4131 ? 190.170 153.813 161.135 1.00 37.15  ? 4131 ASN A CG    1 
ATOM   20220 O OD1   . ASN A 1 4131 ? 190.577 153.474 162.246 1.00 37.15  ? 4131 ASN A OD1   1 
ATOM   20221 N ND2   . ASN A 1 4131 ? 190.557 154.936 160.543 1.00 37.15  ? 4131 ASN A ND2   1 
ATOM   20222 N N     . PRO A 1 4132 ? 186.240 152.268 161.557 1.00 36.68  ? 4132 PRO A N     1 
ATOM   20223 C CA    . PRO A 1 4132 ? 184.814 152.127 161.224 1.00 36.68  ? 4132 PRO A CA    1 
ATOM   20224 C C     . PRO A 1 4132 ? 184.427 152.765 159.901 1.00 36.68  ? 4132 PRO A C     1 
ATOM   20225 O O     . PRO A 1 4132 ? 183.309 152.527 159.427 1.00 36.68  ? 4132 PRO A O     1 
ATOM   20226 C CB    . PRO A 1 4132 ? 184.110 152.816 162.399 1.00 36.68  ? 4132 PRO A CB    1 
ATOM   20227 C CG    . PRO A 1 4132 ? 185.111 153.789 162.914 1.00 36.68  ? 4132 PRO A CG    1 
ATOM   20228 C CD    . PRO A 1 4132 ? 186.455 153.149 162.716 1.00 36.68  ? 4132 PRO A CD    1 
ATOM   20229 N N     . LYS A 1 4133 ? 185.308 153.558 159.292 1.00 41.83  ? 4133 LYS A N     1 
ATOM   20230 C CA    . LYS A 1 4133 ? 184.992 154.235 158.042 1.00 41.83  ? 4133 LYS A CA    1 
ATOM   20231 C C     . LYS A 1 4133 ? 184.887 153.289 156.853 1.00 41.83  ? 4133 LYS A C     1 
ATOM   20232 O O     . LYS A 1 4133 ? 184.360 153.692 155.811 1.00 41.83  ? 4133 LYS A O     1 
ATOM   20233 C CB    . LYS A 1 4133 ? 186.045 155.306 157.745 1.00 41.83  ? 4133 LYS A CB    1 
ATOM   20234 C CG    . LYS A 1 4133 ? 186.225 156.327 158.856 1.00 41.83  ? 4133 LYS A CG    1 
ATOM   20235 C CD    . LYS A 1 4133 ? 184.921 157.042 159.168 1.00 41.83  ? 4133 LYS A CD    1 
ATOM   20236 C CE    . LYS A 1 4133 ? 184.766 157.276 160.661 1.00 41.83  ? 4133 LYS A CE    1 
ATOM   20237 N NZ    . LYS A 1 4133 ? 185.837 158.160 161.197 1.00 41.83  ? 4133 LYS A NZ    1 
ATOM   20238 N N     . VAL A 1 4134 ? 185.373 152.057 156.975 1.00 37.02  ? 4134 VAL A N     1 
ATOM   20239 C CA    . VAL A 1 4134 ? 185.341 151.101 155.870 1.00 37.02  ? 4134 VAL A CA    1 
ATOM   20240 C C     . VAL A 1 4134 ? 183.895 150.723 155.572 1.00 37.02  ? 4134 VAL A C     1 
ATOM   20241 O O     . VAL A 1 4134 ? 183.078 150.613 156.498 1.00 37.02  ? 4134 VAL A O     1 
ATOM   20242 C CB    . VAL A 1 4134 ? 186.193 149.860 156.178 1.00 37.02  ? 4134 VAL A CB    1 
ATOM   20243 C CG1   . VAL A 1 4134 ? 187.650 150.253 156.351 1.00 37.02  ? 4134 VAL A CG1   1 
ATOM   20244 C CG2   . VAL A 1 4134 ? 185.682 149.151 157.421 1.00 37.02  ? 4134 VAL A CG2   1 
ATOM   20245 N N     . PRO A 1 4135 ? 183.528 150.539 154.306 1.00 37.86  ? 4135 PRO A N     1 
ATOM   20246 C CA    . PRO A 1 4135 ? 182.149 150.159 153.987 1.00 37.86  ? 4135 PRO A CA    1 
ATOM   20247 C C     . PRO A 1 4135 ? 181.817 148.764 154.489 1.00 37.86  ? 4135 PRO A C     1 
ATOM   20248 O O     . PRO A 1 4135 ? 182.667 147.871 154.536 1.00 37.86  ? 4135 PRO A O     1 
ATOM   20249 C CB    . PRO A 1 4135 ? 182.106 150.220 152.454 1.00 37.86  ? 4135 PRO A CB    1 
ATOM   20250 C CG    . PRO A 1 4135 ? 183.312 151.016 152.055 1.00 37.86  ? 4135 PRO A CG    1 
ATOM   20251 C CD    . PRO A 1 4135 ? 184.342 150.742 153.098 1.00 37.86  ? 4135 PRO A CD    1 
ATOM   20252 N N     . VAL A 1 4136 ? 180.551 148.585 154.869 1.00 33.61  ? 4136 VAL A N     1 
ATOM   20253 C CA    . VAL A 1 4136 ? 180.090 147.283 155.338 1.00 33.61  ? 4136 VAL A CA    1 
ATOM   20254 C C     . VAL A 1 4136 ? 180.049 146.281 154.191 1.00 33.61  ? 4136 VAL A C     1 
ATOM   20255 O O     . VAL A 1 4136 ? 180.362 145.098 154.371 1.00 33.61  ? 4136 VAL A O     1 
ATOM   20256 C CB    . VAL A 1 4136 ? 178.718 147.420 156.021 1.00 33.61  ? 4136 VAL A CB    1 
ATOM   20257 C CG1   . VAL A 1 4136 ? 178.310 146.107 156.664 1.00 33.61  ? 4136 VAL A CG1   1 
ATOM   20258 C CG2   . VAL A 1 4136 ? 178.751 148.535 157.052 1.00 33.61  ? 4136 VAL A CG2   1 
ATOM   20259 N N     . ASN A 1 4137 ? 179.654 146.734 152.998 1.00 35.58  ? 4137 ASN A N     1 
ATOM   20260 C CA    . ASN A 1 4137 ? 179.529 145.826 151.862 1.00 35.58  ? 4137 ASN A CA    1 
ATOM   20261 C C     . ASN A 1 4137 ? 180.874 145.221 151.480 1.00 35.58  ? 4137 ASN A C     1 
ATOM   20262 O O     . ASN A 1 4137 ? 180.958 144.030 151.159 1.00 35.58  ? 4137 ASN A O     1 
ATOM   20263 C CB    . ASN A 1 4137 ? 178.913 146.559 150.671 1.00 35.58  ? 4137 ASN A CB    1 
ATOM   20264 C CG    . ASN A 1 4137 ? 177.542 147.121 150.981 1.00 35.58  ? 4137 ASN A CG    1 
ATOM   20265 O OD1   . ASN A 1 4137 ? 176.742 146.491 151.672 1.00 35.58  ? 4137 ASN A OD1   1 
ATOM   20266 N ND2   . ASN A 1 4137 ? 177.262 148.314 150.470 1.00 35.58  ? 4137 ASN A ND2   1 
ATOM   20267 N N     . LEU A 1 4138 ? 181.937 146.028 151.500 1.00 33.95  ? 4138 LEU A N     1 
ATOM   20268 C CA    . LEU A 1 4138 ? 183.262 145.501 151.193 1.00 33.95  ? 4138 LEU A CA    1 
ATOM   20269 C C     . LEU A 1 4138 ? 183.689 144.460 152.218 1.00 33.95  ? 4138 LEU A C     1 
ATOM   20270 O O     . LEU A 1 4138 ? 184.278 143.432 151.863 1.00 33.95  ? 4138 LEU A O     1 
ATOM   20271 C CB    . LEU A 1 4138 ? 184.281 146.637 151.127 1.00 33.95  ? 4138 LEU A CB    1 
ATOM   20272 C CG    . LEU A 1 4138 ? 185.719 146.200 150.847 1.00 33.95  ? 4138 LEU A CG    1 
ATOM   20273 C CD1   . LEU A 1 4138 ? 185.863 145.729 149.411 1.00 33.95  ? 4138 LEU A CD1   1 
ATOM   20274 C CD2   . LEU A 1 4138 ? 186.691 147.327 151.143 1.00 33.95  ? 4138 LEU A CD2   1 
ATOM   20275 N N     . LEU A 1 4139 ? 183.401 144.709 153.498 1.00 29.38  ? 4139 LEU A N     1 
ATOM   20276 C CA    . LEU A 1 4139 ? 183.726 143.732 154.532 1.00 29.38  ? 4139 LEU A CA    1 
ATOM   20277 C C     . LEU A 1 4139 ? 182.961 142.433 154.320 1.00 29.38  ? 4139 LEU A C     1 
ATOM   20278 O O     . LEU A 1 4139 ? 183.522 141.342 154.467 1.00 29.38  ? 4139 LEU A O     1 
ATOM   20279 C CB    . LEU A 1 4139 ? 183.422 144.311 155.912 1.00 29.38  ? 4139 LEU A CB    1 
ATOM   20280 C CG    . LEU A 1 4139 ? 184.396 145.368 156.429 1.00 29.38  ? 4139 LEU A CG    1 
ATOM   20281 C CD1   . LEU A 1 4139 ? 183.953 145.885 157.786 1.00 29.38  ? 4139 LEU A CD1   1 
ATOM   20282 C CD2   . LEU A 1 4139 ? 185.796 144.799 156.500 1.00 29.38  ? 4139 LEU A CD2   1 
ATOM   20283 N N     . ARG A 1 4140 ? 181.676 142.531 153.974 1.00 28.49  ? 4140 ARG A N     1 
ATOM   20284 C CA    . ARG A 1 4140 ? 180.880 141.329 153.751 1.00 28.49  ? 4140 ARG A CA    1 
ATOM   20285 C C     . ARG A 1 4140 ? 181.341 140.564 152.519 1.00 28.49  ? 4140 ARG A C     1 
ATOM   20286 O O     . ARG A 1 4140 ? 181.275 139.330 152.497 1.00 28.49  ? 4140 ARG A O     1 
ATOM   20287 C CB    . ARG A 1 4140 ? 179.401 141.693 153.619 1.00 28.49  ? 4140 ARG A CB    1 
ATOM   20288 C CG    . ARG A 1 4140 ? 178.782 142.249 154.885 1.00 28.49  ? 4140 ARG A CG    1 
ATOM   20289 C CD    . ARG A 1 4140 ? 177.305 142.541 154.692 1.00 28.49  ? 4140 ARG A CD    1 
ATOM   20290 N NE    . ARG A 1 4140 ? 176.598 141.404 154.117 1.00 28.49  ? 4140 ARG A NE    1 
ATOM   20291 C CZ    . ARG A 1 4140 ? 175.736 140.646 154.780 1.00 28.49  ? 4140 ARG A CZ    1 
ATOM   20292 N NH1   . ARG A 1 4140 ? 175.449 140.875 156.051 1.00 28.49  ? 4140 ARG A NH1   1 
ATOM   20293 N NH2   . ARG A 1 4140 ? 175.148 139.631 154.153 1.00 28.49  ? 4140 ARG A NH2   1 
ATOM   20294 N N     . ALA A 1 4141 ? 181.809 141.268 151.491 1.00 30.50  ? 4141 ALA A N     1 
ATOM   20295 C CA    . ALA A 1 4141 ? 182.146 140.637 150.222 1.00 30.50  ? 4141 ALA A CA    1 
ATOM   20296 C C     . ALA A 1 4141 ? 183.560 140.072 150.178 1.00 30.50  ? 4141 ALA A C     1 
ATOM   20297 O O     . ALA A 1 4141 ? 183.918 139.437 149.180 1.00 30.50  ? 4141 ALA A O     1 
ATOM   20298 C CB    . ALA A 1 4141 ? 181.960 141.635 149.077 1.00 30.50  ? 4141 ALA A CB    1 
ATOM   20299 N N     . GLY A 1 4142 ? 184.370 140.276 151.217 1.00 28.74  ? 4142 GLY A N     1 
ATOM   20300 C CA    . GLY A 1 4142 ? 185.748 139.833 151.202 1.00 28.74  ? 4142 GLY A CA    1 
ATOM   20301 C C     . GLY A 1 4142 ? 186.095 139.035 152.443 1.00 28.74  ? 4142 GLY A C     1 
ATOM   20302 O O     . GLY A 1 4142 ? 185.318 138.962 153.397 1.00 28.74  ? 4142 GLY A O     1 
ATOM   20303 N N     . ARG A 1 4143 ? 187.281 138.434 152.409 1.00 28.93  ? 4143 ARG A N     1 
ATOM   20304 C CA    . ARG A 1 4143 ? 187.813 137.670 153.530 1.00 28.93  ? 4143 ARG A CA    1 
ATOM   20305 C C     . ARG A 1 4143 ? 188.651 138.597 154.400 1.00 28.93  ? 4143 ARG A C     1 
ATOM   20306 O O     . ARG A 1 4143 ? 189.679 139.114 153.950 1.00 28.93  ? 4143 ARG A O     1 
ATOM   20307 C CB    . ARG A 1 4143 ? 188.652 136.489 153.040 1.00 28.93  ? 4143 ARG A CB    1 
ATOM   20308 C CG    . ARG A 1 4143 ? 187.837 135.308 152.544 1.00 28.93  ? 4143 ARG A CG    1 
ATOM   20309 C CD    . ARG A 1 4143 ? 187.362 134.438 153.695 1.00 28.93  ? 4143 ARG A CD    1 
ATOM   20310 N NE    . ARG A 1 4143 ? 188.218 133.275 153.899 1.00 28.93  ? 4143 ARG A NE    1 
ATOM   20311 C CZ    . ARG A 1 4143 ? 188.919 133.045 155.001 1.00 28.93  ? 4143 ARG A CZ    1 
ATOM   20312 N NH1   . ARG A 1 4143 ? 188.900 133.887 156.021 1.00 28.93  ? 4143 ARG A NH1   1 
ATOM   20313 N NH2   . ARG A 1 4143 ? 189.655 131.941 155.083 1.00 28.93  ? 4143 ARG A NH2   1 
ATOM   20314 N N     . ILE A 1 4144 ? 188.217 138.801 155.634 1.00 25.15  ? 4144 ILE A N     1 
ATOM   20315 C CA    . ILE A 1 4144 ? 188.901 139.690 156.564 1.00 25.15  ? 4144 ILE A CA    1 
ATOM   20316 C C     . ILE A 1 4144 ? 190.027 138.923 157.239 1.00 25.15  ? 4144 ILE A C     1 
ATOM   20317 O O     . ILE A 1 4144 ? 189.859 137.764 157.634 1.00 25.15  ? 4144 ILE A O     1 
ATOM   20318 C CB    . ILE A 1 4144 ? 187.920 140.265 157.602 1.00 25.15  ? 4144 ILE A CB    1 
ATOM   20319 C CG1   . ILE A 1 4144 ? 186.768 141.001 156.915 1.00 25.15  ? 4144 ILE A CG1   1 
ATOM   20320 C CG2   . ILE A 1 4144 ? 188.639 141.202 158.555 1.00 25.15  ? 4144 ILE A CG2   1 
ATOM   20321 C CD1   . ILE A 1 4144 ? 185.509 140.173 156.771 1.00 25.15  ? 4144 ILE A CD1   1 
ATOM   20322 N N     . PHE A 1 4145 ? 191.186 139.566 157.360 1.00 25.99  ? 4145 PHE A N     1 
ATOM   20323 C CA    . PHE A 1 4145 ? 192.327 139.016 158.085 1.00 25.99  ? 4145 PHE A CA    1 
ATOM   20324 C C     . PHE A 1 4145 ? 192.798 140.064 159.081 1.00 25.99  ? 4145 PHE A C     1 
ATOM   20325 O O     . PHE A 1 4145 ? 193.208 141.159 158.685 1.00 25.99  ? 4145 PHE A O     1 
ATOM   20326 C CB    . PHE A 1 4145 ? 193.454 138.620 157.134 1.00 25.99  ? 4145 PHE A CB    1 
ATOM   20327 C CG    . PHE A 1 4145 ? 193.216 137.323 156.425 1.00 25.99  ? 4145 PHE A CG    1 
ATOM   20328 C CD1   . PHE A 1 4145 ? 193.472 136.120 157.056 1.00 25.99  ? 4145 PHE A CD1   1 
ATOM   20329 C CD2   . PHE A 1 4145 ? 192.735 137.306 155.130 1.00 25.99  ? 4145 PHE A CD2   1 
ATOM   20330 C CE1   . PHE A 1 4145 ? 193.255 134.925 156.409 1.00 25.99  ? 4145 PHE A CE1   1 
ATOM   20331 C CE2   . PHE A 1 4145 ? 192.516 136.113 154.477 1.00 25.99  ? 4145 PHE A CE2   1 
ATOM   20332 C CZ    . PHE A 1 4145 ? 192.776 134.921 155.118 1.00 25.99  ? 4145 PHE A CZ    1 
ATOM   20333 N N     . VAL A 1 4146 ? 192.742 139.732 160.364 1.00 25.36  ? 4146 VAL A N     1 
ATOM   20334 C CA    . VAL A 1 4146 ? 193.102 140.666 161.423 1.00 25.36  ? 4146 VAL A CA    1 
ATOM   20335 C C     . VAL A 1 4146 ? 194.520 140.369 161.883 1.00 25.36  ? 4146 VAL A C     1 
ATOM   20336 O O     . VAL A 1 4146 ? 194.841 139.232 162.248 1.00 25.36  ? 4146 VAL A O     1 
ATOM   20337 C CB    . VAL A 1 4146 ? 192.112 140.575 162.594 1.00 25.36  ? 4146 VAL A CB    1 
ATOM   20338 C CG1   . VAL A 1 4146 ? 192.666 141.292 163.809 1.00 25.36  ? 4146 VAL A CG1   1 
ATOM   20339 C CG2   . VAL A 1 4146 ? 190.773 141.158 162.192 1.00 25.36  ? 4146 VAL A CG2   1 
ATOM   20340 N N     . PHE A 1 4147 ? 195.370 141.392 161.867 1.00 30.07  ? 4147 PHE A N     1 
ATOM   20341 C CA    . PHE A 1 4147 ? 196.760 141.275 162.282 1.00 30.07  ? 4147 PHE A CA    1 
ATOM   20342 C C     . PHE A 1 4147 ? 197.000 142.164 163.491 1.00 30.07  ? 4147 PHE A C     1 
ATOM   20343 O O     . PHE A 1 4147 ? 196.625 143.341 163.485 1.00 30.07  ? 4147 PHE A O     1 
ATOM   20344 C CB    . PHE A 1 4147 ? 197.707 141.659 161.144 1.00 30.07  ? 4147 PHE A CB    1 
ATOM   20345 C CG    . PHE A 1 4147 ? 197.815 140.617 160.072 1.00 30.07  ? 4147 PHE A CG    1 
ATOM   20346 C CD1   . PHE A 1 4147 ? 196.910 140.584 159.030 1.00 30.07  ? 4147 PHE A CD1   1 
ATOM   20347 C CD2   . PHE A 1 4147 ? 198.825 139.673 160.106 1.00 30.07  ? 4147 PHE A CD2   1 
ATOM   20348 C CE1   . PHE A 1 4147 ? 197.006 139.627 158.045 1.00 30.07  ? 4147 PHE A CE1   1 
ATOM   20349 C CE2   . PHE A 1 4147 ? 198.927 138.715 159.122 1.00 30.07  ? 4147 PHE A CE2   1 
ATOM   20350 C CZ    . PHE A 1 4147 ? 198.017 138.692 158.089 1.00 30.07  ? 4147 PHE A CZ    1 
ATOM   20351 N N     . GLU A 1 4148 ? 197.624 141.602 164.520 1.00 30.20  ? 4148 GLU A N     1 
ATOM   20352 C CA    . GLU A 1 4148 ? 197.942 142.334 165.733 1.00 30.20  ? 4148 GLU A CA    1 
ATOM   20353 C C     . GLU A 1 4148 ? 199.427 142.216 166.033 1.00 30.20  ? 4148 GLU A C     1 
ATOM   20354 O O     . GLU A 1 4148 ? 200.051 141.200 165.714 1.00 30.20  ? 4148 GLU A O     1 
ATOM   20355 C CB    . GLU A 1 4148 ? 197.150 141.804 166.936 1.00 30.20  ? 4148 GLU A CB    1 
ATOM   20356 C CG    . GLU A 1 4148 ? 195.657 142.039 166.872 1.00 30.20  ? 4148 GLU A CG    1 
ATOM   20357 C CD    . GLU A 1 4148 ? 194.961 141.614 168.147 1.00 30.20  ? 4148 GLU A CD    1 
ATOM   20358 O OE1   . GLU A 1 4148 ? 195.630 141.021 169.019 1.00 30.20  ? 4148 GLU A OE1   1 
ATOM   20359 O OE2   . GLU A 1 4148 ? 193.750 141.877 168.284 1.00 30.20  ? 4148 GLU A OE2   1 
ATOM   20360 N N     . PRO A 1 4149 ? 200.016 143.236 166.645 1.00 26.12  ? 4149 PRO A N     1 
ATOM   20361 C CA    . PRO A 1 4149 ? 201.395 143.118 167.109 1.00 26.12  ? 4149 PRO A CA    1 
ATOM   20362 C C     . PRO A 1 4149 ? 201.477 142.169 168.289 1.00 26.12  ? 4149 PRO A C     1 
ATOM   20363 O O     . PRO A 1 4149 ? 200.693 142.287 169.243 1.00 26.12  ? 4149 PRO A O     1 
ATOM   20364 C CB    . PRO A 1 4149 ? 201.755 144.554 167.517 1.00 26.12  ? 4149 PRO A CB    1 
ATOM   20365 C CG    . PRO A 1 4149 ? 200.446 145.192 167.831 1.00 26.12  ? 4149 PRO A CG    1 
ATOM   20366 C CD    . PRO A 1 4149 ? 199.464 144.582 166.878 1.00 26.12  ? 4149 PRO A CD    1 
ATOM   20367 N N     . PRO A 1 4150 ? 202.389 141.202 168.253 1.00 22.09  ? 4150 PRO A N     1 
ATOM   20368 C CA    . PRO A 1 4150 ? 202.525 140.266 169.371 1.00 22.09  ? 4150 PRO A CA    1 
ATOM   20369 C C     . PRO A 1 4150 ? 202.870 140.999 170.653 1.00 22.09  ? 4150 PRO A C     1 
ATOM   20370 O O     . PRO A 1 4150 ? 203.741 141.881 170.660 1.00 22.09  ? 4150 PRO A O     1 
ATOM   20371 C CB    . PRO A 1 4150 ? 203.671 139.345 168.927 1.00 22.09  ? 4150 PRO A CB    1 
ATOM   20372 C CG    . PRO A 1 4150 ? 203.716 139.477 167.441 1.00 22.09  ? 4150 PRO A CG    1 
ATOM   20373 C CD    . PRO A 1 4150 ? 203.306 140.886 167.146 1.00 22.09  ? 4150 PRO A CD    1 
ATOM   20374 N N     . PRO A 1 4151 ? 202.208 140.667 171.756 1.00 18.42  ? 4151 PRO A N     1 
ATOM   20375 C CA    . PRO A 1 4151 ? 202.507 141.331 173.027 1.00 18.42  ? 4151 PRO A CA    1 
ATOM   20376 C C     . PRO A 1 4151 ? 203.868 140.918 173.564 1.00 18.42  ? 4151 PRO A C     1 
ATOM   20377 O O     . PRO A 1 4151 ? 204.394 139.846 173.259 1.00 18.42  ? 4151 PRO A O     1 
ATOM   20378 C CB    . PRO A 1 4151 ? 201.378 140.863 173.956 1.00 18.42  ? 4151 PRO A CB    1 
ATOM   20379 C CG    . PRO A 1 4151 ? 200.358 140.210 173.056 1.00 18.42  ? 4151 PRO A CG    1 
ATOM   20380 C CD    . PRO A 1 4151 ? 201.118 139.690 171.887 1.00 18.42  ? 4151 PRO A CD    1 
ATOM   20381 N N     . GLY A 1 4152 ? 204.437 141.797 174.381 1.00 15.32  ? 4152 GLY A N     1 
ATOM   20382 C CA    . GLY A 1 4152 ? 205.729 141.538 174.981 1.00 15.32  ? 4152 GLY A CA    1 
ATOM   20383 C C     . GLY A 1 4152 ? 206.709 142.667 174.757 1.00 15.32  ? 4152 GLY A C     1 
ATOM   20384 O O     . GLY A 1 4152 ? 206.655 143.349 173.730 1.00 15.32  ? 4152 GLY A O     1 
ATOM   20385 N N     . VAL A 1 4153 ? 207.604 142.884 175.721 1.00 15.03  ? 4153 VAL A N     1 
ATOM   20386 C CA    . VAL A 1 4153 ? 208.653 143.882 175.544 1.00 15.03  ? 4153 VAL A CA    1 
ATOM   20387 C C     . VAL A 1 4153 ? 209.663 143.408 174.509 1.00 15.03  ? 4153 VAL A C     1 
ATOM   20388 O O     . VAL A 1 4153 ? 210.143 144.192 173.682 1.00 15.03  ? 4153 VAL A O     1 
ATOM   20389 C CB    . VAL A 1 4153 ? 209.322 144.196 176.895 1.00 15.03  ? 4153 VAL A CB    1 
ATOM   20390 C CG1   . VAL A 1 4153 ? 210.672 144.859 176.690 1.00 15.03  ? 4153 VAL A CG1   1 
ATOM   20391 C CG2   . VAL A 1 4153 ? 208.421 145.077 177.736 1.00 15.03  ? 4153 VAL A CG2   1 
ATOM   20392 N N     . LYS A 1 4154 ? 209.994 142.115 174.533 1.00 14.66  ? 4154 LYS A N     1 
ATOM   20393 C CA    . LYS A 1 4154 ? 210.965 141.569 173.592 1.00 14.66  ? 4154 LYS A CA    1 
ATOM   20394 C C     . LYS A 1 4154 ? 210.493 141.717 172.151 1.00 14.66  ? 4154 LYS A C     1 
ATOM   20395 O O     . LYS A 1 4154 ? 211.261 142.144 171.280 1.00 14.66  ? 4154 LYS A O     1 
ATOM   20396 C CB    . LYS A 1 4154 ? 211.230 140.101 173.926 1.00 14.66  ? 4154 LYS A CB    1 
ATOM   20397 C CG    . LYS A 1 4154 ? 211.905 139.300 172.830 1.00 14.66  ? 4154 LYS A CG    1 
ATOM   20398 C CD    . LYS A 1 4154 ? 212.270 137.914 173.338 1.00 14.66  ? 4154 LYS A CD    1 
ATOM   20399 C CE    . LYS A 1 4154 ? 212.285 136.893 172.216 1.00 14.66  ? 4154 LYS A CE    1 
ATOM   20400 N NZ    . LYS A 1 4154 ? 213.304 137.215 171.184 1.00 14.66  ? 4154 LYS A NZ    1 
ATOM   20401 N N     . ALA A 1 4155 ? 209.232 141.375 171.880 1.00 14.58  ? 4155 ALA A N     1 
ATOM   20402 C CA    . ALA A 1 4155 ? 208.711 141.494 170.522 1.00 14.58  ? 4155 ALA A CA    1 
ATOM   20403 C C     . ALA A 1 4155 ? 208.667 142.949 170.073 1.00 14.58  ? 4155 ALA A C     1 
ATOM   20404 O O     . ALA A 1 4155 ? 209.007 143.264 168.926 1.00 14.58  ? 4155 ALA A O     1 
ATOM   20405 C CB    . ALA A 1 4155 ? 207.323 140.863 170.436 1.00 14.58  ? 4155 ALA A CB    1 
ATOM   20406 N N     . ASN A 1 4156 ? 208.251 143.849 170.966 1.00 17.18  ? 4156 ASN A N     1 
ATOM   20407 C CA    . ASN A 1 4156 ? 208.200 145.266 170.624 1.00 17.18  ? 4156 ASN A CA    1 
ATOM   20408 C C     . ASN A 1 4156 ? 209.587 145.806 170.306 1.00 17.18  ? 4156 ASN A C     1 
ATOM   20409 O O     . ASN A 1 4156 ? 209.766 146.554 169.337 1.00 17.18  ? 4156 ASN A O     1 
ATOM   20410 C CB    . ASN A 1 4156 ? 207.566 146.054 171.769 1.00 17.18  ? 4156 ASN A CB    1 
ATOM   20411 C CG    . ASN A 1 4156 ? 206.997 147.381 171.319 1.00 17.18  ? 4156 ASN A CG    1 
ATOM   20412 O OD1   . ASN A 1 4156 ? 207.441 147.958 170.328 1.00 17.18  ? 4156 ASN A OD1   1 
ATOM   20413 N ND2   . ASN A 1 4156 ? 206.006 147.875 172.050 1.00 17.18  ? 4156 ASN A ND2   1 
ATOM   20414 N N     . MET A 1 4157 ? 210.587 145.432 171.107 1.00 16.81  ? 4157 MET A N     1 
ATOM   20415 C CA    . MET A 1 4157 ? 211.934 145.928 170.865 1.00 16.81  ? 4157 MET A CA    1 
ATOM   20416 C C     . MET A 1 4157 ? 212.528 145.324 169.601 1.00 16.81  ? 4157 MET A C     1 
ATOM   20417 O O     . MET A 1 4157 ? 213.262 146.005 168.878 1.00 16.81  ? 4157 MET A O     1 
ATOM   20418 C CB    . MET A 1 4157 ? 212.824 145.644 172.073 1.00 16.81  ? 4157 MET A CB    1 
ATOM   20419 C CG    . MET A 1 4157 ? 212.432 146.463 173.287 1.00 16.81  ? 4157 MET A CG    1 
ATOM   20420 S SD    . MET A 1 4157 ? 213.625 146.493 174.630 1.00 16.81  ? 4157 MET A SD    1 
ATOM   20421 C CE    . MET A 1 4157 ? 215.152 146.521 173.712 1.00 16.81  ? 4157 MET A CE    1 
ATOM   20422 N N     . LEU A 1 4158 ? 212.214 144.058 169.310 1.00 16.15  ? 4158 LEU A N     1 
ATOM   20423 C CA    . LEU A 1 4158 ? 212.652 143.463 168.052 1.00 16.15  ? 4158 LEU A CA    1 
ATOM   20424 C C     . LEU A 1 4158 ? 212.037 144.185 166.861 1.00 16.15  ? 4158 LEU A C     1 
ATOM   20425 O O     . LEU A 1 4158 ? 212.720 144.450 165.866 1.00 16.15  ? 4158 LEU A O     1 
ATOM   20426 C CB    . LEU A 1 4158 ? 212.299 141.978 168.020 1.00 16.15  ? 4158 LEU A CB    1 
ATOM   20427 C CG    . LEU A 1 4158 ? 213.264 141.040 168.744 1.00 16.15  ? 4158 LEU A CG    1 
ATOM   20428 C CD1   . LEU A 1 4158 ? 212.619 139.686 168.976 1.00 16.15  ? 4158 LEU A CD1   1 
ATOM   20429 C CD2   . LEU A 1 4158 ? 214.555 140.895 167.960 1.00 16.15  ? 4158 LEU A CD2   1 
ATOM   20430 N N     . ARG A 1 4159 ? 210.745 144.513 166.945 1.00 18.18  ? 4159 ARG A N     1 
ATOM   20431 C CA    . ARG A 1 4159 ? 210.103 145.263 165.870 1.00 18.18  ? 4159 ARG A CA    1 
ATOM   20432 C C     . ARG A 1 4159 ? 210.742 146.634 165.700 1.00 18.18  ? 4159 ARG A C     1 
ATOM   20433 O O     . ARG A 1 4159 ? 210.994 147.076 164.572 1.00 18.18  ? 4159 ARG A O     1 
ATOM   20434 C CB    . ARG A 1 4159 ? 208.609 145.410 166.148 1.00 18.18  ? 4159 ARG A CB    1 
ATOM   20435 C CG    . ARG A 1 4159 ? 207.785 144.179 165.836 1.00 18.18  ? 4159 ARG A CG    1 
ATOM   20436 C CD    . ARG A 1 4159 ? 206.310 144.465 166.030 1.00 18.18  ? 4159 ARG A CD    1 
ATOM   20437 N NE    . ARG A 1 4159 ? 205.857 144.078 167.360 1.00 18.18  ? 4159 ARG A NE    1 
ATOM   20438 C CZ    . ARG A 1 4159 ? 205.168 144.865 168.174 1.00 18.18  ? 4159 ARG A CZ    1 
ATOM   20439 N NH1   . ARG A 1 4159 ? 204.831 146.095 167.823 1.00 18.18  ? 4159 ARG A NH1   1 
ATOM   20440 N NH2   . ARG A 1 4159 ? 204.809 144.407 169.370 1.00 18.18  ? 4159 ARG A NH2   1 
ATOM   20441 N N     . THR A 1 4160 ? 211.013 147.321 166.812 1.00 17.67  ? 4160 THR A N     1 
ATOM   20442 C CA    . THR A 1 4160 ? 211.629 148.641 166.738 1.00 17.67  ? 4160 THR A CA    1 
ATOM   20443 C C     . THR A 1 4160 ? 213.017 148.569 166.115 1.00 17.67  ? 4160 THR A C     1 
ATOM   20444 O O     . THR A 1 4160 ? 213.373 149.400 165.272 1.00 17.67  ? 4160 THR A O     1 
ATOM   20445 C CB    . THR A 1 4160 ? 211.698 149.265 168.131 1.00 17.67  ? 4160 THR A CB    1 
ATOM   20446 O OG1   . THR A 1 4160 ? 210.375 149.581 168.580 1.00 17.67  ? 4160 THR A OG1   1 
ATOM   20447 C CG2   . THR A 1 4160 ? 212.536 150.531 168.110 1.00 17.67  ? 4160 THR A CG2   1 
ATOM   20448 N N     . PHE A 1 4161 ? 213.814 147.574 166.511 1.00 17.87  ? 4161 PHE A N     1 
ATOM   20449 C CA    . PHE A 1 4161 ? 215.160 147.443 165.966 1.00 17.87  ? 4161 PHE A CA    1 
ATOM   20450 C C     . PHE A 1 4161 ? 215.138 147.051 164.496 1.00 17.87  ? 4161 PHE A C     1 
ATOM   20451 O O     . PHE A 1 4161 ? 215.997 147.495 163.726 1.00 17.87  ? 4161 PHE A O     1 
ATOM   20452 C CB    . PHE A 1 4161 ? 215.957 146.425 166.779 1.00 17.87  ? 4161 PHE A CB    1 
ATOM   20453 C CG    . PHE A 1 4161 ? 216.714 147.029 167.924 1.00 17.87  ? 4161 PHE A CG    1 
ATOM   20454 C CD1   . PHE A 1 4161 ? 217.744 147.924 167.694 1.00 17.87  ? 4161 PHE A CD1   1 
ATOM   20455 C CD2   . PHE A 1 4161 ? 216.392 146.709 169.229 1.00 17.87  ? 4161 PHE A CD2   1 
ATOM   20456 C CE1   . PHE A 1 4161 ? 218.440 148.483 168.744 1.00 17.87  ? 4161 PHE A CE1   1 
ATOM   20457 C CE2   . PHE A 1 4161 ? 217.084 147.264 170.283 1.00 17.87  ? 4161 PHE A CE2   1 
ATOM   20458 C CZ    . PHE A 1 4161 ? 218.110 148.153 170.040 1.00 17.87  ? 4161 PHE A CZ    1 
ATOM   20459 N N     . SER A 1 4162 ? 214.176 146.220 164.088 1.00 15.51  ? 4162 SER A N     1 
ATOM   20460 C CA    . SER A 1 4162 ? 214.067 145.858 162.679 1.00 15.51  ? 4162 SER A CA    1 
ATOM   20461 C C     . SER A 1 4162 ? 213.625 147.047 161.836 1.00 15.51  ? 4162 SER A C     1 
ATOM   20462 O O     . SER A 1 4162 ? 214.080 147.210 160.698 1.00 15.51  ? 4162 SER A O     1 
ATOM   20463 C CB    . SER A 1 4162 ? 213.098 144.689 162.513 1.00 15.51  ? 4162 SER A CB    1 
ATOM   20464 O OG    . SER A 1 4162 ? 212.694 144.552 161.162 1.00 15.51  ? 4162 SER A OG    1 
ATOM   20465 N N     . SER A 1 4163 ? 212.732 147.883 162.372 1.00 16.61  ? 4163 SER A N     1 
ATOM   20466 C CA    . SER A 1 4163 ? 212.251 149.035 161.616 1.00 16.61  ? 4163 SER A CA    1 
ATOM   20467 C C     . SER A 1 4163 ? 213.372 150.028 161.335 1.00 16.61  ? 4163 SER A C     1 
ATOM   20468 O O     . SER A 1 4163 ? 213.478 150.551 160.220 1.00 16.61  ? 4163 SER A O     1 
ATOM   20469 C CB    . SER A 1 4163 ? 211.111 149.717 162.370 1.00 16.61  ? 4163 SER A CB    1 
ATOM   20470 O OG    . SER A 1 4163 ? 210.670 150.874 161.684 1.00 16.61  ? 4163 SER A OG    1 
ATOM   20471 N N     . ILE A 1 4164 ? 214.211 150.301 162.325 1.00 20.69  ? 4164 ILE A N     1 
ATOM   20472 C CA    . ILE A 1 4164 ? 215.294 151.275 162.146 1.00 20.69  ? 4164 ILE A CA    1 
ATOM   20473 C C     . ILE A 1 4164 ? 216.373 150.670 161.255 1.00 20.69  ? 4164 ILE A C     1 
ATOM   20474 O O     . ILE A 1 4164 ? 216.839 149.549 161.527 1.00 20.69  ? 4164 ILE A O     1 
ATOM   20475 C CB    . ILE A 1 4164 ? 215.869 151.688 163.500 1.00 20.69  ? 4164 ILE A CB    1 
ATOM   20476 C CG1   . ILE A 1 4164 ? 214.774 152.286 164.385 1.00 20.69  ? 4164 ILE A CG1   1 
ATOM   20477 C CG2   . ILE A 1 4164 ? 216.995 152.687 163.313 1.00 20.69  ? 4164 ILE A CG2   1 
ATOM   20478 C CD1   . ILE A 1 4164 ? 215.181 152.443 165.831 1.00 20.69  ? 4164 ILE A CD1   1 
ATOM   20479 N N     . PRO A 1 4165 ? 216.793 151.351 160.191 1.00 22.29  ? 4165 PRO A N     1 
ATOM   20480 C CA    . PRO A 1 4165 ? 217.863 150.811 159.346 1.00 22.29  ? 4165 PRO A CA    1 
ATOM   20481 C C     . PRO A 1 4165 ? 219.167 150.678 160.116 1.00 22.29  ? 4165 PRO A C     1 
ATOM   20482 O O     . PRO A 1 4165 ? 219.446 151.435 161.048 1.00 22.29  ? 4165 PRO A O     1 
ATOM   20483 C CB    . PRO A 1 4165 ? 217.982 151.841 158.216 1.00 22.29  ? 4165 PRO A CB    1 
ATOM   20484 C CG    . PRO A 1 4165 ? 216.686 152.586 158.233 1.00 22.29  ? 4165 PRO A CG    1 
ATOM   20485 C CD    . PRO A 1 4165 ? 216.257 152.616 159.664 1.00 22.29  ? 4165 PRO A CD    1 
ATOM   20486 N N     . VAL A 1 4166 ? 219.970 149.692 159.712 1.00 22.51  ? 4166 VAL A N     1 
ATOM   20487 C CA    . VAL A 1 4166 ? 221.231 149.422 160.395 1.00 22.51  ? 4166 VAL A CA    1 
ATOM   20488 C C     . VAL A 1 4166 ? 222.194 150.593 160.245 1.00 22.51  ? 4166 VAL A C     1 
ATOM   20489 O O     . VAL A 1 4166 ? 223.005 150.858 161.141 1.00 22.51  ? 4166 VAL A O     1 
ATOM   20490 C CB    . VAL A 1 4166 ? 221.842 148.111 159.867 1.00 22.51  ? 4166 VAL A CB    1 
ATOM   20491 C CG1   . VAL A 1 4166 ? 223.172 147.819 160.547 1.00 22.51  ? 4166 VAL A CG1   1 
ATOM   20492 C CG2   . VAL A 1 4166 ? 220.872 146.958 160.067 1.00 22.51  ? 4166 VAL A CG2   1 
ATOM   20493 N N     . SER A 1 4167 ? 222.122 151.315 159.124 1.00 23.20  ? 4167 SER A N     1 
ATOM   20494 C CA    . SER A 1 4167 ? 223.058 152.408 158.879 1.00 23.20  ? 4167 SER A CA    1 
ATOM   20495 C C     . SER A 1 4167 ? 222.911 153.509 159.923 1.00 23.20  ? 4167 SER A C     1 
ATOM   20496 O O     . SER A 1 4167 ? 223.907 154.078 160.383 1.00 23.20  ? 4167 SER A O     1 
ATOM   20497 C CB    . SER A 1 4167 ? 222.852 152.969 157.472 1.00 23.20  ? 4167 SER A CB    1 
ATOM   20498 O OG    . SER A 1 4167 ? 221.560 153.532 157.332 1.00 23.20  ? 4167 SER A OG    1 
ATOM   20499 N N     . ARG A 1 4168 ? 221.672 153.828 160.305 1.00 21.76  ? 4168 ARG A N     1 
ATOM   20500 C CA    . ARG A 1 4168 ? 221.444 154.888 161.283 1.00 21.76  ? 4168 ARG A CA    1 
ATOM   20501 C C     . ARG A 1 4168 ? 222.064 154.541 162.631 1.00 21.76  ? 4168 ARG A C     1 
ATOM   20502 O O     . ARG A 1 4168 ? 222.729 155.373 163.258 1.00 21.76  ? 4168 ARG A O     1 
ATOM   20503 C CB    . ARG A 1 4168 ? 219.945 155.149 161.436 1.00 21.76  ? 4168 ARG A CB    1 
ATOM   20504 C CG    . ARG A 1 4168 ? 219.296 155.822 160.244 1.00 21.76  ? 4168 ARG A CG    1 
ATOM   20505 C CD    . ARG A 1 4168 ? 217.814 156.035 160.495 1.00 21.76  ? 4168 ARG A CD    1 
ATOM   20506 N NE    . ARG A 1 4168 ? 217.573 156.661 161.790 1.00 21.76  ? 4168 ARG A NE    1 
ATOM   20507 C CZ    . ARG A 1 4168 ? 216.923 157.803 161.963 1.00 21.76  ? 4168 ARG A CZ    1 
ATOM   20508 N NH1   . ARG A 1 4168 ? 216.420 158.473 160.940 1.00 21.76  ? 4168 ARG A NH1   1 
ATOM   20509 N NH2   . ARG A 1 4168 ? 216.775 158.285 163.193 1.00 21.76  ? 4168 ARG A NH2   1 
ATOM   20510 N N     . ILE A 1 4169 ? 221.851 153.309 163.097 1.00 22.71  ? 4169 ILE A N     1 
ATOM   20511 C CA    . ILE A 1 4169 ? 222.365 152.916 164.406 1.00 22.71  ? 4169 ILE A CA    1 
ATOM   20512 C C     . ILE A 1 4169 ? 223.883 152.795 164.372 1.00 22.71  ? 4169 ILE A C     1 
ATOM   20513 O O     . ILE A 1 4169 ? 224.577 153.253 165.288 1.00 22.71  ? 4169 ILE A O     1 
ATOM   20514 C CB    . ILE A 1 4169 ? 221.700 151.608 164.869 1.00 22.71  ? 4169 ILE A CB    1 
ATOM   20515 C CG1   . ILE A 1 4169 ? 220.182 151.770 164.900 1.00 22.71  ? 4169 ILE A CG1   1 
ATOM   20516 C CG2   . ILE A 1 4169 ? 222.211 151.213 166.240 1.00 22.71  ? 4169 ILE A CG2   1 
ATOM   20517 C CD1   . ILE A 1 4169 ? 219.453 150.571 165.459 1.00 22.71  ? 4169 ILE A CD1   1 
ATOM   20518 N N     . CYS A 1 4170 ? 224.424 152.177 163.321 1.00 26.18  ? 4170 CYS A N     1 
ATOM   20519 C CA    . CYS A 1 4170 ? 225.869 151.995 163.187 1.00 26.18  ? 4170 CYS A CA    1 
ATOM   20520 C C     . CYS A 1 4170 ? 226.435 153.165 162.387 1.00 26.18  ? 4170 CYS A C     1 
ATOM   20521 O O     . CYS A 1 4170 ? 226.753 153.063 161.201 1.00 26.18  ? 4170 CYS A O     1 
ATOM   20522 C CB    . CYS A 1 4170 ? 226.183 150.655 162.533 1.00 26.18  ? 4170 CYS A CB    1 
ATOM   20523 S SG    . CYS A 1 4170 ? 225.433 149.230 163.352 1.00 26.18  ? 4170 CYS A SG    1 
ATOM   20524 N N     . LYS A 1 4171 ? 226.564 154.300 163.068 1.00 24.58  ? 4171 LYS A N     1 
ATOM   20525 C CA    . LYS A 1 4171 ? 227.052 155.536 162.472 1.00 24.58  ? 4171 LYS A CA    1 
ATOM   20526 C C     . LYS A 1 4171 ? 227.415 156.483 163.604 1.00 24.58  ? 4171 LYS A C     1 
ATOM   20527 O O     . LYS A 1 4171 ? 226.904 156.344 164.720 1.00 24.58  ? 4171 LYS A O     1 
ATOM   20528 C CB    . LYS A 1 4171 ? 225.995 156.162 161.549 1.00 24.58  ? 4171 LYS A CB    1 
ATOM   20529 C CG    . LYS A 1 4171 ? 226.330 157.541 160.999 1.00 24.58  ? 4171 LYS A CG    1 
ATOM   20530 C CD    . LYS A 1 4171 ? 225.094 158.245 160.466 1.00 24.58  ? 4171 LYS A CD    1 
ATOM   20531 C CE    . LYS A 1 4171 ? 224.316 157.356 159.510 1.00 24.58  ? 4171 LYS A CE    1 
ATOM   20532 N NZ    . LYS A 1 4171 ? 223.076 158.019 159.021 1.00 24.58  ? 4171 LYS A NZ    1 
ATOM   20533 N N     . SER A 1 4172 ? 228.326 157.424 163.317 1.00 27.70  ? 4172 SER A N     1 
ATOM   20534 C CA    . SER A 1 4172 ? 228.655 158.499 164.247 1.00 27.70  ? 4172 SER A CA    1 
ATOM   20535 C C     . SER A 1 4172 ? 229.317 157.896 165.487 1.00 27.70  ? 4172 SER A C     1 
ATOM   20536 O O     . SER A 1 4172 ? 229.757 156.741 165.426 1.00 27.70  ? 4172 SER A O     1 
ATOM   20537 C CB    . SER A 1 4172 ? 227.383 159.292 164.567 1.00 27.70  ? 4172 SER A CB    1 
ATOM   20538 O OG    . SER A 1 4172 ? 226.880 159.938 163.410 1.00 27.70  ? 4172 SER A OG    1 
ATOM   20539 N N     . PRO A 1 4173 ? 229.460 158.635 166.620 1.00 31.68  ? 4173 PRO A N     1 
ATOM   20540 C CA    . PRO A 1 4173 ? 229.928 157.985 167.852 1.00 31.68  ? 4173 PRO A CA    1 
ATOM   20541 C C     . PRO A 1 4173 ? 229.234 156.671 168.172 1.00 31.68  ? 4173 PRO A C     1 
ATOM   20542 O O     . PRO A 1 4173 ? 228.037 156.506 167.918 1.00 31.68  ? 4173 PRO A O     1 
ATOM   20543 C CB    . PRO A 1 4173 ? 229.634 159.043 168.917 1.00 31.68  ? 4173 PRO A CB    1 
ATOM   20544 C CG    . PRO A 1 4173 ? 229.932 160.301 168.217 1.00 31.68  ? 4173 PRO A CG    1 
ATOM   20545 C CD    . PRO A 1 4173 ? 229.534 160.104 166.766 1.00 31.68  ? 4173 PRO A CD    1 
ATOM   20546 N N     . ASN A 1 4174 ? 229.994 155.725 168.730 1.00 32.67  ? 4174 ASN A N     1 
ATOM   20547 C CA    . ASN A 1 4174 ? 229.450 154.412 169.055 1.00 32.67  ? 4174 ASN A CA    1 
ATOM   20548 C C     . ASN A 1 4174 ? 228.386 154.480 170.139 1.00 32.67  ? 4174 ASN A C     1 
ATOM   20549 O O     . ASN A 1 4174 ? 227.644 153.509 170.326 1.00 32.67  ? 4174 ASN A O     1 
ATOM   20550 C CB    . ASN A 1 4174 ? 230.577 153.474 169.488 1.00 32.67  ? 4174 ASN A CB    1 
ATOM   20551 C CG    . ASN A 1 4174 ? 231.820 153.627 168.636 1.00 32.67  ? 4174 ASN A CG    1 
ATOM   20552 O OD1   . ASN A 1 4174 ? 231.783 153.429 167.422 1.00 32.67  ? 4174 ASN A OD1   1 
ATOM   20553 N ND2   . ASN A 1 4174 ? 232.932 153.981 169.271 1.00 32.67  ? 4174 ASN A ND2   1 
ATOM   20554 N N     . GLU A 1 4175 ? 228.296 155.600 170.859 1.00 27.38  ? 4175 GLU A N     1 
ATOM   20555 C CA    . GLU A 1 4175 ? 227.249 155.772 171.857 1.00 27.38  ? 4175 GLU A CA    1 
ATOM   20556 C C     . GLU A 1 4175 ? 225.867 155.863 171.225 1.00 27.38  ? 4175 GLU A C     1 
ATOM   20557 O O     . GLU A 1 4175 ? 224.861 155.755 171.937 1.00 27.38  ? 4175 GLU A O     1 
ATOM   20558 C CB    . GLU A 1 4175 ? 227.531 157.021 172.694 1.00 27.38  ? 4175 GLU A CB    1 
ATOM   20559 C CG    . GLU A 1 4175 ? 228.768 156.921 173.581 1.00 27.38  ? 4175 GLU A CG    1 
ATOM   20560 C CD    . GLU A 1 4175 ? 230.071 157.043 172.816 1.00 27.38  ? 4175 GLU A CD    1 
ATOM   20561 O OE1   . GLU A 1 4175 ? 230.031 157.344 171.606 1.00 27.38  ? 4175 GLU A OE1   1 
ATOM   20562 O OE2   . GLU A 1 4175 ? 231.138 156.826 173.427 1.00 27.38  ? 4175 GLU A OE2   1 
ATOM   20563 N N     . ARG A 1 4176 ? 225.799 156.059 169.906 1.00 19.81  ? 4176 ARG A N     1 
ATOM   20564 C CA    . ARG A 1 4176 ? 224.513 156.120 169.223 1.00 19.81  ? 4176 ARG A CA    1 
ATOM   20565 C C     . ARG A 1 4176 ? 223.760 154.803 169.339 1.00 19.81  ? 4176 ARG A C     1 
ATOM   20566 O O     . ARG A 1 4176 ? 222.535 154.792 169.490 1.00 19.81  ? 4176 ARG A O     1 
ATOM   20567 C CB    . ARG A 1 4176 ? 224.719 156.488 167.755 1.00 19.81  ? 4176 ARG A CB    1 
ATOM   20568 C CG    . ARG A 1 4176 ? 223.434 156.701 166.979 1.00 19.81  ? 4176 ARG A CG    1 
ATOM   20569 C CD    . ARG A 1 4176 ? 223.723 157.356 165.646 1.00 19.81  ? 4176 ARG A CD    1 
ATOM   20570 N NE    . ARG A 1 4176 ? 224.392 158.637 165.823 1.00 19.81  ? 4176 ARG A NE    1 
ATOM   20571 C CZ    . ARG A 1 4176 ? 224.041 159.756 165.207 1.00 19.81  ? 4176 ARG A CZ    1 
ATOM   20572 N NH1   . ARG A 1 4176 ? 223.055 159.780 164.327 1.00 19.81  ? 4176 ARG A NH1   1 
ATOM   20573 N NH2   . ARG A 1 4176 ? 224.699 160.879 165.478 1.00 19.81  ? 4176 ARG A NH2   1 
ATOM   20574 N N     . ALA A 1 4177 ? 224.476 153.680 169.263 1.00 18.14  ? 4177 ALA A N     1 
ATOM   20575 C CA    . ALA A 1 4177 ? 223.824 152.380 169.387 1.00 18.14  ? 4177 ALA A CA    1 
ATOM   20576 C C     . ALA A 1 4177 ? 223.180 152.218 170.758 1.00 18.14  ? 4177 ALA A C     1 
ATOM   20577 O O     . ALA A 1 4177 ? 222.038 151.757 170.871 1.00 18.14  ? 4177 ALA A O     1 
ATOM   20578 C CB    . ALA A 1 4177 ? 224.832 151.262 169.127 1.00 18.14  ? 4177 ALA A CB    1 
ATOM   20579 N N     . ARG A 1 4178 ? 223.896 152.604 171.815 1.00 19.15  ? 4178 ARG A N     1 
ATOM   20580 C CA    . ARG A 1 4178 ? 223.343 152.486 173.161 1.00 19.15  ? 4178 ARG A CA    1 
ATOM   20581 C C     . ARG A 1 4178 ? 222.180 153.450 173.359 1.00 19.15  ? 4178 ARG A C     1 
ATOM   20582 O O     . ARG A 1 4178 ? 221.189 153.118 174.019 1.00 19.15  ? 4178 ARG A O     1 
ATOM   20583 C CB    . ARG A 1 4178 ? 224.435 152.729 174.202 1.00 19.15  ? 4178 ARG A CB    1 
ATOM   20584 C CG    . ARG A 1 4178 ? 223.923 152.778 175.629 1.00 19.15  ? 4178 ARG A CG    1 
ATOM   20585 C CD    . ARG A 1 4178 ? 225.000 152.356 176.612 1.00 19.15  ? 4178 ARG A CD    1 
ATOM   20586 N NE    . ARG A 1 4178 ? 224.977 150.924 176.877 1.00 19.15  ? 4178 ARG A NE    1 
ATOM   20587 C CZ    . ARG A 1 4178 ? 226.046 150.205 177.187 1.00 19.15  ? 4178 ARG A CZ    1 
ATOM   20588 N NH1   . ARG A 1 4178 ? 227.246 150.753 177.275 1.00 19.15  ? 4178 ARG A NH1   1 
ATOM   20589 N NH2   . ARG A 1 4178 ? 225.908 148.902 177.414 1.00 19.15  ? 4178 ARG A NH2   1 
ATOM   20590 N N     . LEU A 1 4179 ? 222.282 154.654 172.789 1.00 16.01  ? 4179 LEU A N     1 
ATOM   20591 C CA    . LEU A 1 4179 ? 221.177 155.605 172.872 1.00 16.01  ? 4179 LEU A CA    1 
ATOM   20592 C C     . LEU A 1 4179 ? 219.934 155.060 172.179 1.00 16.01  ? 4179 LEU A C     1 
ATOM   20593 O O     . LEU A 1 4179 ? 218.815 155.185 172.688 1.00 16.01  ? 4179 LEU A O     1 
ATOM   20594 C CB    . LEU A 1 4179 ? 221.589 156.944 172.261 1.00 16.01  ? 4179 LEU A CB    1 
ATOM   20595 C CG    . LEU A 1 4179 ? 222.310 157.914 173.195 1.00 16.01  ? 4179 LEU A CG    1 
ATOM   20596 C CD1   . LEU A 1 4179 ? 222.440 159.281 172.549 1.00 16.01  ? 4179 LEU A CD1   1 
ATOM   20597 C CD2   . LEU A 1 4179 ? 221.575 158.015 174.516 1.00 16.01  ? 4179 LEU A CD2   1 
ATOM   20598 N N     . TYR A 1 4180 ? 220.117 154.444 171.011 1.00 15.34  ? 4180 TYR A N     1 
ATOM   20599 C CA    . TYR A 1 4180 ? 218.990 153.868 170.289 1.00 15.34  ? 4180 TYR A CA    1 
ATOM   20600 C C     . TYR A 1 4180 ? 218.400 152.686 171.046 1.00 15.34  ? 4180 TYR A C     1 
ATOM   20601 O O     . TYR A 1 4180 ? 217.183 152.482 171.046 1.00 15.34  ? 4180 TYR A O     1 
ATOM   20602 C CB    . TYR A 1 4180 ? 219.426 153.453 168.886 1.00 15.34  ? 4180 TYR A CB    1 
ATOM   20603 C CG    . TYR A 1 4180 ? 219.179 154.515 167.844 1.00 15.34  ? 4180 TYR A CG    1 
ATOM   20604 C CD1   . TYR A 1 4180 ? 220.057 155.576 167.684 1.00 15.34  ? 4180 TYR A CD1   1 
ATOM   20605 C CD2   . TYR A 1 4180 ? 218.067 154.458 167.020 1.00 15.34  ? 4180 TYR A CD2   1 
ATOM   20606 C CE1   . TYR A 1 4180 ? 219.835 156.548 166.734 1.00 15.34  ? 4180 TYR A CE1   1 
ATOM   20607 C CE2   . TYR A 1 4180 ? 217.837 155.425 166.067 1.00 15.34  ? 4180 TYR A CE2   1 
ATOM   20608 C CZ    . TYR A 1 4180 ? 218.723 156.467 165.929 1.00 15.34  ? 4180 TYR A CZ    1 
ATOM   20609 O OH    . TYR A 1 4180 ? 218.492 157.432 164.977 1.00 15.34  ? 4180 TYR A OH    1 
ATOM   20610 N N     . PHE A 1 4181 ? 219.251 151.889 171.695 1.00 14.11  ? 4181 PHE A N     1 
ATOM   20611 C CA    . PHE A 1 4181 ? 218.748 150.798 172.523 1.00 14.11  ? 4181 PHE A CA    1 
ATOM   20612 C C     . PHE A 1 4181 ? 217.914 151.330 173.680 1.00 14.11  ? 4181 PHE A C     1 
ATOM   20613 O O     . PHE A 1 4181 ? 216.852 150.785 174.002 1.00 14.11  ? 4181 PHE A O     1 
ATOM   20614 C CB    . PHE A 1 4181 ? 219.907 149.951 173.047 1.00 14.11  ? 4181 PHE A CB    1 
ATOM   20615 C CG    . PHE A 1 4181 ? 219.501 148.968 174.105 1.00 14.11  ? 4181 PHE A CG    1 
ATOM   20616 C CD1   . PHE A 1 4181 ? 218.862 147.790 173.766 1.00 14.11  ? 4181 PHE A CD1   1 
ATOM   20617 C CD2   . PHE A 1 4181 ? 219.754 149.225 175.441 1.00 14.11  ? 4181 PHE A CD2   1 
ATOM   20618 C CE1   . PHE A 1 4181 ? 218.487 146.886 174.739 1.00 14.11  ? 4181 PHE A CE1   1 
ATOM   20619 C CE2   . PHE A 1 4181 ? 219.379 148.325 176.417 1.00 14.11  ? 4181 PHE A CE2   1 
ATOM   20620 C CZ    . PHE A 1 4181 ? 218.745 147.155 176.065 1.00 14.11  ? 4181 PHE A CZ    1 
ATOM   20621 N N     . LEU A 1 4182 ? 218.390 152.396 174.327 1.00 13.02  ? 4182 LEU A N     1 
ATOM   20622 C CA    . LEU A 1 4182 ? 217.637 153.005 175.418 1.00 13.02  ? 4182 LEU A CA    1 
ATOM   20623 C C     . LEU A 1 4182 ? 216.297 153.532 174.923 1.00 13.02  ? 4182 LEU A C     1 
ATOM   20624 O O     . LEU A 1 4182 ? 215.265 153.367 175.582 1.00 13.02  ? 4182 LEU A O     1 
ATOM   20625 C CB    . LEU A 1 4182 ? 218.453 154.130 176.051 1.00 13.02  ? 4182 LEU A CB    1 
ATOM   20626 C CG    . LEU A 1 4182 ? 219.440 153.727 177.143 1.00 13.02  ? 4182 LEU A CG    1 
ATOM   20627 C CD1   . LEU A 1 4182 ? 220.242 154.933 177.588 1.00 13.02  ? 4182 LEU A CD1   1 
ATOM   20628 C CD2   . LEU A 1 4182 ? 218.709 153.103 178.314 1.00 13.02  ? 4182 LEU A CD2   1 
ATOM   20629 N N     . LEU A 1 4183 ? 216.301 154.175 173.754 1.00 17.47  ? 4183 LEU A N     1 
ATOM   20630 C CA    . LEU A 1 4183 ? 215.066 154.693 173.177 1.00 17.47  ? 4183 LEU A CA    1 
ATOM   20631 C C     . LEU A 1 4183 ? 214.090 153.565 172.860 1.00 17.47  ? 4183 LEU A C     1 
ATOM   20632 O O     . LEU A 1 4183 ? 212.886 153.677 173.116 1.00 17.47  ? 4183 LEU A O     1 
ATOM   20633 C CB    . LEU A 1 4183 ? 215.389 155.503 171.922 1.00 17.47  ? 4183 LEU A CB    1 
ATOM   20634 C CG    . LEU A 1 4183 ? 214.226 156.089 171.125 1.00 17.47  ? 4183 LEU A CG    1 
ATOM   20635 C CD1   . LEU A 1 4183 ? 213.203 156.721 172.045 1.00 17.47  ? 4183 LEU A CD1   1 
ATOM   20636 C CD2   . LEU A 1 4183 ? 214.749 157.103 170.127 1.00 17.47  ? 4183 LEU A CD2   1 
ATOM   20637 N N     . ALA A 1 4184 ? 214.597 152.468 172.295 1.00 18.90  ? 4184 ALA A N     1 
ATOM   20638 C CA    . ALA A 1 4184 ? 213.746 151.326 171.980 1.00 18.90  ? 4184 ALA A CA    1 
ATOM   20639 C C     . ALA A 1 4184 ? 213.153 150.721 173.244 1.00 18.90  ? 4184 ALA A C     1 
ATOM   20640 O O     . ALA A 1 4184 ? 211.968 150.370 173.283 1.00 18.90  ? 4184 ALA A O     1 
ATOM   20641 C CB    . ALA A 1 4184 ? 214.543 150.278 171.203 1.00 18.90  ? 4184 ALA A CB    1 
ATOM   20642 N N     . TRP A 1 4185 ? 213.967 150.595 174.295 1.00 19.31  ? 4185 TRP A N     1 
ATOM   20643 C CA    . TRP A 1 4185 ? 213.468 150.060 175.557 1.00 19.31  ? 4185 TRP A CA    1 
ATOM   20644 C C     . TRP A 1 4185 ? 212.399 150.967 176.153 1.00 19.31  ? 4185 TRP A C     1 
ATOM   20645 O O     . TRP A 1 4185 ? 211.375 150.492 176.655 1.00 19.31  ? 4185 TRP A O     1 
ATOM   20646 C CB    . TRP A 1 4185 ? 214.623 149.868 176.541 1.00 19.31  ? 4185 TRP A CB    1 
ATOM   20647 C CG    . TRP A 1 4185 ? 214.172 149.565 177.937 1.00 19.31  ? 4185 TRP A CG    1 
ATOM   20648 C CD1   . TRP A 1 4185 ? 213.936 150.463 178.935 1.00 19.31  ? 4185 TRP A CD1   1 
ATOM   20649 C CD2   . TRP A 1 4185 ? 213.899 148.272 178.490 1.00 19.31  ? 4185 TRP A CD2   1 
ATOM   20650 N NE1   . TRP A 1 4185 ? 213.534 149.811 180.074 1.00 19.31  ? 4185 TRP A NE1   1 
ATOM   20651 C CE2   . TRP A 1 4185 ? 213.503 148.465 179.826 1.00 19.31  ? 4185 TRP A CE2   1 
ATOM   20652 C CE3   . TRP A 1 4185 ? 213.952 146.971 177.985 1.00 19.31  ? 4185 TRP A CE3   1 
ATOM   20653 C CZ2   . TRP A 1 4185 ? 213.162 147.406 180.662 1.00 19.31  ? 4185 TRP A CZ2   1 
ATOM   20654 C CZ3   . TRP A 1 4185 ? 213.613 145.922 178.816 1.00 19.31  ? 4185 TRP A CZ3   1 
ATOM   20655 C CH2   . TRP A 1 4185 ? 213.223 146.145 180.139 1.00 19.31  ? 4185 TRP A CH2   1 
ATOM   20656 N N     . PHE A 1 4186 ? 212.623 152.281 176.107 1.00 18.37  ? 4186 PHE A N     1 
ATOM   20657 C CA    . PHE A 1 4186 ? 211.641 153.224 176.633 1.00 18.37  ? 4186 PHE A CA    1 
ATOM   20658 C C     . PHE A 1 4186 ? 210.330 153.139 175.862 1.00 18.37  ? 4186 PHE A C     1 
ATOM   20659 O O     . PHE A 1 4186 ? 209.242 153.131 176.454 1.00 18.37  ? 4186 PHE A O     1 
ATOM   20660 C CB    . PHE A 1 4186 ? 212.205 154.643 176.581 1.00 18.37  ? 4186 PHE A CB    1 
ATOM   20661 C CG    . PHE A 1 4186 ? 211.205 155.704 176.925 1.00 18.37  ? 4186 PHE A CG    1 
ATOM   20662 C CD1   . PHE A 1 4186 ? 210.740 155.843 178.219 1.00 18.37  ? 4186 PHE A CD1   1 
ATOM   20663 C CD2   . PHE A 1 4186 ? 210.731 156.565 175.953 1.00 18.37  ? 4186 PHE A CD2   1 
ATOM   20664 C CE1   . PHE A 1 4186 ? 209.821 156.820 178.537 1.00 18.37  ? 4186 PHE A CE1   1 
ATOM   20665 C CE2   . PHE A 1 4186 ? 209.812 157.543 176.265 1.00 18.37  ? 4186 PHE A CE2   1 
ATOM   20666 C CZ    . PHE A 1 4186 ? 209.356 157.671 177.558 1.00 18.37  ? 4186 PHE A CZ    1 
ATOM   20667 N N     . HIS A 1 4187 ? 210.419 153.076 174.532 1.00 19.47  ? 4187 HIS A N     1 
ATOM   20668 C CA    . HIS A 1 4187 ? 209.222 152.953 173.710 1.00 19.47  ? 4187 HIS A CA    1 
ATOM   20669 C C     . HIS A 1 4187 ? 208.476 151.664 174.022 1.00 19.47  ? 4187 HIS A C     1 
ATOM   20670 O O     . HIS A 1 4187 ? 207.246 151.657 174.142 1.00 19.47  ? 4187 HIS A O     1 
ATOM   20671 C CB    . HIS A 1 4187 ? 209.596 153.013 172.230 1.00 19.47  ? 4187 HIS A CB    1 
ATOM   20672 C CG    . HIS A 1 4187 ? 208.422 153.167 171.317 1.00 19.47  ? 4187 HIS A CG    1 
ATOM   20673 N ND1   . HIS A 1 4187 ? 207.514 154.196 171.439 1.00 19.47  ? 4187 HIS A ND1   1 
ATOM   20674 C CD2   . HIS A 1 4187 ? 208.006 152.422 170.266 1.00 19.47  ? 4187 HIS A CD2   1 
ATOM   20675 C CE1   . HIS A 1 4187 ? 206.589 154.078 170.503 1.00 19.47  ? 4187 HIS A CE1   1 
ATOM   20676 N NE2   . HIS A 1 4187 ? 206.865 153.010 169.778 1.00 19.47  ? 4187 HIS A NE2   1 
ATOM   20677 N N     . ALA A 1 4188 ? 209.211 150.561 174.172 1.00 24.62  ? 4188 ALA A N     1 
ATOM   20678 C CA    . ALA A 1 4188 ? 208.579 149.287 174.492 1.00 24.62  ? 4188 ALA A CA    1 
ATOM   20679 C C     . ALA A 1 4188 ? 207.886 149.341 175.845 1.00 24.62  ? 4188 ALA A C     1 
ATOM   20680 O O     . ALA A 1 4188 ? 206.772 148.833 176.004 1.00 24.62  ? 4188 ALA A O     1 
ATOM   20681 C CB    . ALA A 1 4188 ? 209.616 148.167 174.467 1.00 24.62  ? 4188 ALA A CB    1 
ATOM   20682 N N     . ILE A 1 4189 ? 208.533 149.958 176.835 1.00 34.96  ? 4189 ILE A N     1 
ATOM   20683 C CA    . ILE A 1 4189 ? 207.947 150.036 178.171 1.00 34.96  ? 4189 ILE A CA    1 
ATOM   20684 C C     . ILE A 1 4189 ? 206.661 150.853 178.140 1.00 34.96  ? 4189 ILE A C     1 
ATOM   20685 O O     . ILE A 1 4189 ? 205.622 150.429 178.660 1.00 34.96  ? 4189 ILE A O     1 
ATOM   20686 C CB    . ILE A 1 4189 ? 208.957 150.620 179.173 1.00 34.96  ? 4189 ILE A CB    1 
ATOM   20687 C CG1   . ILE A 1 4189 ? 210.099 149.633 179.413 1.00 34.96  ? 4189 ILE A CG1   1 
ATOM   20688 C CG2   . ILE A 1 4189 ? 208.270 150.967 180.478 1.00 34.96  ? 4189 ILE A CG2   1 
ATOM   20689 C CD1   . ILE A 1 4189 ? 209.649 148.316 179.990 1.00 34.96  ? 4189 ILE A CD1   1 
ATOM   20690 N N     . ILE A 1 4190 ? 206.706 152.034 177.518 1.00 28.76  ? 4190 ILE A N     1 
ATOM   20691 C CA    . ILE A 1 4190 ? 205.522 152.886 177.507 1.00 28.76  ? 4190 ILE A CA    1 
ATOM   20692 C C     . ILE A 1 4190 ? 204.433 152.372 176.580 1.00 28.76  ? 4190 ILE A C     1 
ATOM   20693 O O     . ILE A 1 4190 ? 203.276 152.779 176.724 1.00 28.76  ? 4190 ILE A O     1 
ATOM   20694 C CB    . ILE A 1 4190 ? 205.864 154.337 177.122 1.00 28.76  ? 4190 ILE A CB    1 
ATOM   20695 C CG1   . ILE A 1 4190 ? 206.435 154.397 175.712 1.00 28.76  ? 4190 ILE A CG1   1 
ATOM   20696 C CG2   . ILE A 1 4190 ? 206.837 154.936 178.118 1.00 28.76  ? 4190 ILE A CG2   1 
ATOM   20697 C CD1   . ILE A 1 4190 ? 206.571 155.793 175.195 1.00 28.76  ? 4190 ILE A CD1   1 
ATOM   20698 N N     . GLN A 1 4191 ? 204.761 151.492 175.635 1.00 20.67  ? 4191 GLN A N     1 
ATOM   20699 C CA    . GLN A 1 4191 ? 203.730 150.884 174.804 1.00 20.67  ? 4191 GLN A CA    1 
ATOM   20700 C C     . GLN A 1 4191 ? 203.108 149.664 175.470 1.00 20.67  ? 4191 GLN A C     1 
ATOM   20701 O O     . GLN A 1 4191 ? 201.913 149.406 175.295 1.00 20.67  ? 4191 GLN A O     1 
ATOM   20702 C CB    . GLN A 1 4191 ? 204.308 150.498 173.441 1.00 20.67  ? 4191 GLN A CB    1 
ATOM   20703 C CG    . GLN A 1 4191 ? 204.193 151.582 172.386 1.00 20.67  ? 4191 GLN A CG    1 
ATOM   20704 C CD    . GLN A 1 4191 ? 204.072 151.018 170.985 1.00 20.67  ? 4191 GLN A CD    1 
ATOM   20705 O OE1   . GLN A 1 4191 ? 204.905 150.226 170.550 1.00 20.67  ? 4191 GLN A OE1   1 
ATOM   20706 N NE2   . GLN A 1 4191 ? 203.028 151.423 170.272 1.00 20.67  ? 4191 GLN A NE2   1 
ATOM   20707 N N     . GLU A 1 4192 ? 203.901 148.902 176.226 1.00 19.32  ? 4192 GLU A N     1 
ATOM   20708 C CA    . GLU A 1 4192 ? 203.357 147.761 176.948 1.00 19.32  ? 4192 GLU A CA    1 
ATOM   20709 C C     . GLU A 1 4192 ? 202.569 148.196 178.174 1.00 19.32  ? 4192 GLU A C     1 
ATOM   20710 O O     . GLU A 1 4192 ? 201.657 147.481 178.603 1.00 19.32  ? 4192 GLU A O     1 
ATOM   20711 C CB    . GLU A 1 4192 ? 204.481 146.803 177.341 1.00 19.32  ? 4192 GLU A CB    1 
ATOM   20712 C CG    . GLU A 1 4192 ? 204.697 145.663 176.351 1.00 19.32  ? 4192 GLU A CG    1 
ATOM   20713 C CD    . GLU A 1 4192 ? 203.555 144.659 176.323 1.00 19.32  ? 4192 GLU A CD    1 
ATOM   20714 O OE1   . GLU A 1 4192 ? 202.579 144.826 177.082 1.00 19.32  ? 4192 GLU A OE1   1 
ATOM   20715 O OE2   . GLU A 1 4192 ? 203.627 143.703 175.525 1.00 19.32  ? 4192 GLU A OE2   1 
ATOM   20716 N N     . ARG A 1 4193 ? 202.899 149.351 178.755 1.00 12.95  ? 4193 ARG A N     1 
ATOM   20717 C CA    . ARG A 1 4193 ? 202.091 149.849 179.860 1.00 12.95  ? 4193 ARG A CA    1 
ATOM   20718 C C     . ARG A 1 4193 ? 200.708 150.296 179.410 1.00 12.95  ? 4193 ARG A C     1 
ATOM   20719 O O     . ARG A 1 4193 ? 199.833 150.488 180.259 1.00 12.95  ? 4193 ARG A O     1 
ATOM   20720 C CB    . ARG A 1 4193 ? 202.798 151.005 180.566 1.00 12.95  ? 4193 ARG A CB    1 
ATOM   20721 C CG    . ARG A 1 4193 ? 203.980 150.575 181.411 1.00 12.95  ? 4193 ARG A CG    1 
ATOM   20722 C CD    . ARG A 1 4193 ? 204.589 151.741 182.163 1.00 12.95  ? 4193 ARG A CD    1 
ATOM   20723 N NE    . ARG A 1 4193 ? 203.633 152.338 183.086 1.00 12.95  ? 4193 ARG A NE    1 
ATOM   20724 C CZ    . ARG A 1 4193 ? 203.747 152.296 184.406 1.00 12.95  ? 4193 ARG A CZ    1 
ATOM   20725 N NH1   . ARG A 1 4193 ? 204.776 151.707 184.991 1.00 12.95  ? 4193 ARG A NH1   1 
ATOM   20726 N NH2   . ARG A 1 4193 ? 202.804 152.855 185.157 1.00 12.95  ? 4193 ARG A NH2   1 
ATOM   20727 N N     . LEU A 1 4194 ? 200.495 150.466 178.104 1.00 15.47  ? 4194 LEU A N     1 
ATOM   20728 C CA    . LEU A 1 4194 ? 199.196 150.906 177.608 1.00 15.47  ? 4194 LEU A CA    1 
ATOM   20729 C C     . LEU A 1 4194 ? 198.133 149.827 177.760 1.00 15.47  ? 4194 LEU A C     1 
ATOM   20730 O O     . LEU A 1 4194 ? 196.959 150.150 177.973 1.00 15.47  ? 4194 LEU A O     1 
ATOM   20731 C CB    . LEU A 1 4194 ? 199.312 151.326 176.145 1.00 15.47  ? 4194 LEU A CB    1 
ATOM   20732 C CG    . LEU A 1 4194 ? 199.784 152.755 175.885 1.00 15.47  ? 4194 LEU A CG    1 
ATOM   20733 C CD1   . LEU A 1 4194 ? 199.975 152.984 174.399 1.00 15.47  ? 4194 LEU A CD1   1 
ATOM   20734 C CD2   . LEU A 1 4194 ? 198.796 153.750 176.458 1.00 15.47  ? 4194 LEU A CD2   1 
ATOM   20735 N N     . ARG A 1 4195 ? 198.515 148.551 177.652 1.00 16.95  ? 4195 ARG A N     1 
ATOM   20736 C CA    . ARG A 1 4195 ? 197.535 147.473 177.751 1.00 16.95  ? 4195 ARG A CA    1 
ATOM   20737 C C     . ARG A 1 4195 ? 196.824 147.496 179.097 1.00 16.95  ? 4195 ARG A C     1 
ATOM   20738 O O     . ARG A 1 4195 ? 195.674 147.058 179.209 1.00 16.95  ? 4195 ARG A O     1 
ATOM   20739 C CB    . ARG A 1 4195 ? 198.210 146.119 177.530 1.00 16.95  ? 4195 ARG A CB    1 
ATOM   20740 C CG    . ARG A 1 4195 ? 198.935 145.989 176.204 1.00 16.95  ? 4195 ARG A CG    1 
ATOM   20741 C CD    . ARG A 1 4195 ? 199.390 144.560 175.968 1.00 16.95  ? 4195 ARG A CD    1 
ATOM   20742 N NE    . ARG A 1 4195 ? 200.376 144.126 176.949 1.00 16.95  ? 4195 ARG A NE    1 
ATOM   20743 C CZ    . ARG A 1 4195 ? 200.195 143.126 177.801 1.00 16.95  ? 4195 ARG A CZ    1 
ATOM   20744 N NH1   . ARG A 1 4195 ? 199.070 142.430 177.820 1.00 16.95  ? 4195 ARG A NH1   1 
ATOM   20745 N NH2   . ARG A 1 4195 ? 201.167 142.816 178.654 1.00 16.95  ? 4195 ARG A NH2   1 
ATOM   20746 N N     . TYR A 1 4196 ? 197.495 148.003 180.128 1.00 11.19  ? 4196 TYR A N     1 
ATOM   20747 C CA    . TYR A 1 4196 ? 196.890 148.175 181.448 1.00 11.19  ? 4196 TYR A CA    1 
ATOM   20748 C C     . TYR A 1 4196 ? 196.394 149.617 181.563 1.00 11.19  ? 4196 TYR A C     1 
ATOM   20749 O O     . TYR A 1 4196 ? 196.964 150.461 182.255 1.00 11.19  ? 4196 TYR A O     1 
ATOM   20750 C CB    . TYR A 1 4196 ? 197.893 147.822 182.539 1.00 11.19  ? 4196 TYR A CB    1 
ATOM   20751 C CG    . TYR A 1 4196 ? 198.663 146.544 182.274 1.00 11.19  ? 4196 TYR A CG    1 
ATOM   20752 C CD1   . TYR A 1 4196 ? 198.294 145.349 182.871 1.00 11.19  ? 4196 TYR A CD1   1 
ATOM   20753 C CD2   . TYR A 1 4196 ? 199.773 146.539 181.438 1.00 11.19  ? 4196 TYR A CD2   1 
ATOM   20754 C CE1   . TYR A 1 4196 ? 198.997 144.184 182.630 1.00 11.19  ? 4196 TYR A CE1   1 
ATOM   20755 C CE2   . TYR A 1 4196 ? 200.479 145.381 181.193 1.00 11.19  ? 4196 TYR A CE2   1 
ATOM   20756 C CZ    . TYR A 1 4196 ? 200.088 144.207 181.791 1.00 11.19  ? 4196 TYR A CZ    1 
ATOM   20757 O OH    . TYR A 1 4196 ? 200.793 143.053 181.548 1.00 11.19  ? 4196 TYR A OH    1 
ATOM   20758 N N     . ALA A 1 4197 ? 195.303 149.884 180.845 1.00 11.48  ? 4197 ALA A N     1 
ATOM   20759 C CA    . ALA A 1 4197 ? 194.878 151.264 180.609 1.00 11.48  ? 4197 ALA A CA    1 
ATOM   20760 C C     . ALA A 1 4197 ? 194.561 152.037 181.883 1.00 11.48  ? 4197 ALA A C     1 
ATOM   20761 O O     . ALA A 1 4197 ? 195.082 153.155 182.039 1.00 11.48  ? 4197 ALA A O     1 
ATOM   20762 C CB    . ALA A 1 4197 ? 193.689 151.275 179.642 1.00 11.48  ? 4197 ALA A CB    1 
ATOM   20763 N N     . PRO A 1 4198 ? 193.734 151.540 182.820 1.00 10.59  ? 4198 PRO A N     1 
ATOM   20764 C CA    . PRO A 1 4198 ? 193.448 152.345 184.015 1.00 10.59  ? 4198 PRO A CA    1 
ATOM   20765 C C     . PRO A 1 4198 ? 194.663 152.479 184.915 1.00 10.59  ? 4198 PRO A C     1 
ATOM   20766 O O     . PRO A 1 4198 ? 194.985 153.576 185.382 1.00 10.59  ? 4198 PRO A O     1 
ATOM   20767 C CB    . PRO A 1 4198 ? 192.316 151.571 184.707 1.00 10.59  ? 4198 PRO A CB    1 
ATOM   20768 C CG    . PRO A 1 4198 ? 191.805 150.612 183.681 1.00 10.59  ? 4198 PRO A CG    1 
ATOM   20769 C CD    . PRO A 1 4198 ? 192.990 150.269 182.849 1.00 10.59  ? 4198 PRO A CD    1 
ATOM   20770 N N     . LEU A 1 4199 ? 195.349 151.367 185.155 1.00 11.00  ? 4199 LEU A N     1 
ATOM   20771 C CA    . LEU A 1 4199 ? 196.510 151.325 186.040 1.00 11.00  ? 4199 LEU A CA    1 
ATOM   20772 C C     . LEU A 1 4199 ? 197.768 151.278 185.181 1.00 11.00  ? 4199 LEU A C     1 
ATOM   20773 O O     . LEU A 1 4199 ? 198.192 150.209 184.739 1.00 11.00  ? 4199 LEU A O     1 
ATOM   20774 C CB    . LEU A 1 4199 ? 196.430 150.123 186.974 1.00 11.00  ? 4199 LEU A CB    1 
ATOM   20775 C CG    . LEU A 1 4199 ? 197.591 149.940 187.949 1.00 11.00  ? 4199 LEU A CG    1 
ATOM   20776 C CD1   . LEU A 1 4199 ? 197.632 151.079 188.946 1.00 11.00  ? 4199 LEU A CD1   1 
ATOM   20777 C CD2   . LEU A 1 4199 ? 197.479 148.606 188.663 1.00 11.00  ? 4199 LEU A CD2   1 
ATOM   20778 N N     . GLY A 1 4200 ? 198.373 152.440 184.958 1.00 10.59  ? 4200 GLY A N     1 
ATOM   20779 C CA    . GLY A 1 4200 ? 199.611 152.503 184.210 1.00 10.59  ? 4200 GLY A CA    1 
ATOM   20780 C C     . GLY A 1 4200 ? 199.699 153.661 183.240 1.00 10.59  ? 4200 GLY A C     1 
ATOM   20781 O O     . GLY A 1 4200 ? 200.774 154.242 183.069 1.00 10.59  ? 4200 GLY A O     1 
ATOM   20782 N N     . TRP A 1 4201 ? 198.587 154.013 182.594 1.00 12.41  ? 4201 TRP A N     1 
ATOM   20783 C CA    . TRP A 1 4201 ? 198.585 155.180 181.723 1.00 12.41  ? 4201 TRP A CA    1 
ATOM   20784 C C     . TRP A 1 4201 ? 197.306 156.004 181.817 1.00 12.41  ? 4201 TRP A C     1 
ATOM   20785 O O     . TRP A 1 4201 ? 197.125 156.919 181.003 1.00 12.41  ? 4201 TRP A O     1 
ATOM   20786 C CB    . TRP A 1 4201 ? 198.823 154.775 180.265 1.00 12.41  ? 4201 TRP A CB    1 
ATOM   20787 C CG    . TRP A 1 4201 ? 200.269 154.779 179.872 1.00 12.41  ? 4201 TRP A CG    1 
ATOM   20788 C CD1   . TRP A 1 4201 ? 200.956 153.762 179.281 1.00 12.41  ? 4201 TRP A CD1   1 
ATOM   20789 C CD2   . TRP A 1 4201 ? 201.210 155.847 180.048 1.00 12.41  ? 4201 TRP A CD2   1 
ATOM   20790 N NE1   . TRP A 1 4201 ? 202.261 154.129 179.073 1.00 12.41  ? 4201 TRP A NE1   1 
ATOM   20791 C CE2   . TRP A 1 4201 ? 202.443 155.404 179.536 1.00 12.41  ? 4201 TRP A CE2   1 
ATOM   20792 C CE3   . TRP A 1 4201 ? 201.129 157.135 180.585 1.00 12.41  ? 4201 TRP A CE3   1 
ATOM   20793 C CZ2   . TRP A 1 4201 ? 203.583 156.200 179.547 1.00 12.41  ? 4201 TRP A CZ2   1 
ATOM   20794 C CZ3   . TRP A 1 4201 ? 202.261 157.921 180.595 1.00 12.41  ? 4201 TRP A CZ3   1 
ATOM   20795 C CH2   . TRP A 1 4201 ? 203.472 157.453 180.079 1.00 12.41  ? 4201 TRP A CH2   1 
ATOM   20796 N N     . SER A 1 4202 ? 196.409 155.697 182.755 1.00 11.92  ? 4202 SER A N     1 
ATOM   20797 C CA    . SER A 1 4202 ? 195.165 156.441 182.938 1.00 11.92  ? 4202 SER A CA    1 
ATOM   20798 C C     . SER A 1 4202 ? 194.286 156.369 181.694 1.00 11.92  ? 4202 SER A C     1 
ATOM   20799 O O     . SER A 1 4202 ? 193.190 155.802 181.736 1.00 11.92  ? 4202 SER A O     1 
ATOM   20800 C CB    . SER A 1 4202 ? 195.453 157.898 183.308 1.00 11.92  ? 4202 SER A CB    1 
ATOM   20801 O OG    . SER A 1 4202 ? 194.280 158.685 183.222 1.00 11.92  ? 4202 SER A OG    1 
ATOM   20802 N N     . LYS A 1 4203 ? 194.751 156.940 180.588 1.00 11.82  ? 4203 LYS A N     1 
ATOM   20803 C CA    . LYS A 1 4203 ? 194.044 156.897 179.318 1.00 11.82  ? 4203 LYS A CA    1 
ATOM   20804 C C     . LYS A 1 4203 ? 194.821 156.058 178.312 1.00 11.82  ? 4203 LYS A C     1 
ATOM   20805 O O     . LYS A 1 4203 ? 195.921 155.571 178.584 1.00 11.82  ? 4203 LYS A O     1 
ATOM   20806 C CB    . LYS A 1 4203 ? 193.815 158.310 178.771 1.00 11.82  ? 4203 LYS A CB    1 
ATOM   20807 C CG    . LYS A 1 4203 ? 193.422 159.324 179.825 1.00 11.82  ? 4203 LYS A CG    1 
ATOM   20808 C CD    . LYS A 1 4203 ? 193.312 160.718 179.235 1.00 11.82  ? 4203 LYS A CD    1 
ATOM   20809 C CE    . LYS A 1 4203 ? 192.999 161.744 180.312 1.00 11.82  ? 4203 LYS A CE    1 
ATOM   20810 N NZ    . LYS A 1 4203 ? 191.747 161.420 181.050 1.00 11.82  ? 4203 LYS A NZ    1 
ATOM   20811 N N     . LYS A 1 4204 ? 194.228 155.896 177.133 1.00 14.68  ? 4204 LYS A N     1 
ATOM   20812 C CA    . LYS A 1 4204 ? 194.818 155.117 176.046 1.00 14.68  ? 4204 LYS A CA    1 
ATOM   20813 C C     . LYS A 1 4204 ? 195.464 156.085 175.061 1.00 14.68  ? 4204 LYS A C     1 
ATOM   20814 O O     . LYS A 1 4204 ? 194.863 156.474 174.059 1.00 14.68  ? 4204 LYS A O     1 
ATOM   20815 C CB    . LYS A 1 4204 ? 193.762 154.252 175.368 1.00 14.68  ? 4204 LYS A CB    1 
ATOM   20816 C CG    . LYS A 1 4204 ? 193.550 152.891 176.005 1.00 14.68  ? 4204 LYS A CG    1 
ATOM   20817 C CD    . LYS A 1 4204 ? 194.484 151.856 175.403 1.00 14.68  ? 4204 LYS A CD    1 
ATOM   20818 C CE    . LYS A 1 4204 ? 194.404 150.539 176.152 1.00 14.68  ? 4204 LYS A CE    1 
ATOM   20819 N NZ    . LYS A 1 4204 ? 193.004 150.050 176.272 1.00 14.68  ? 4204 LYS A NZ    1 
ATOM   20820 N N     . TYR A 1 4205 ? 196.702 156.476 175.348 1.00 14.13  ? 4205 TYR A N     1 
ATOM   20821 C CA    . TYR A 1 4205 ? 197.428 157.344 174.435 1.00 14.13  ? 4205 TYR A CA    1 
ATOM   20822 C C     . TYR A 1 4205 ? 197.881 156.559 173.208 1.00 14.13  ? 4205 TYR A C     1 
ATOM   20823 O O     . TYR A 1 4205 ? 197.916 155.325 173.203 1.00 14.13  ? 4205 TYR A O     1 
ATOM   20824 C CB    . TYR A 1 4205 ? 198.632 157.975 175.133 1.00 14.13  ? 4205 TYR A CB    1 
ATOM   20825 C CG    . TYR A 1 4205 ? 198.277 158.743 176.383 1.00 14.13  ? 4205 TYR A CG    1 
ATOM   20826 C CD1   . TYR A 1 4205 ? 197.439 159.847 176.328 1.00 14.13  ? 4205 TYR A CD1   1 
ATOM   20827 C CD2   . TYR A 1 4205 ? 198.782 158.367 177.617 1.00 14.13  ? 4205 TYR A CD2   1 
ATOM   20828 C CE1   . TYR A 1 4205 ? 197.113 160.551 177.467 1.00 14.13  ? 4205 TYR A CE1   1 
ATOM   20829 C CE2   . TYR A 1 4205 ? 198.462 159.065 178.761 1.00 14.13  ? 4205 TYR A CE2   1 
ATOM   20830 C CZ    . TYR A 1 4205 ? 197.627 160.156 178.681 1.00 14.13  ? 4205 TYR A CZ    1 
ATOM   20831 O OH    . TYR A 1 4205 ? 197.306 160.853 179.821 1.00 14.13  ? 4205 TYR A OH    1 
ATOM   20832 N N     . GLU A 1 4206 ? 198.228 157.293 172.151 1.00 16.85  ? 4206 GLU A N     1 
ATOM   20833 C CA    . GLU A 1 4206 ? 198.627 156.646 170.906 1.00 16.85  ? 4206 GLU A CA    1 
ATOM   20834 C C     . GLU A 1 4206 ? 200.012 156.023 171.031 1.00 16.85  ? 4206 GLU A C     1 
ATOM   20835 O O     . GLU A 1 4206 ? 200.163 154.798 170.960 1.00 16.85  ? 4206 GLU A O     1 
ATOM   20836 C CB    . GLU A 1 4206 ? 198.587 157.653 169.757 1.00 16.85  ? 4206 GLU A CB    1 
ATOM   20837 C CG    . GLU A 1 4206 ? 197.396 158.597 169.799 1.00 16.85  ? 4206 GLU A CG    1 
ATOM   20838 C CD    . GLU A 1 4206 ? 196.092 157.912 169.441 1.00 16.85  ? 4206 GLU A CD    1 
ATOM   20839 O OE1   . GLU A 1 4206 ? 196.136 156.813 168.852 1.00 16.85  ? 4206 GLU A OE1   1 
ATOM   20840 O OE2   . GLU A 1 4206 ? 195.021 158.476 169.749 1.00 16.85  ? 4206 GLU A OE2   1 
ATOM   20841 N N     . PHE A 1 4207 ? 201.034 156.855 171.242 1.00 13.38  ? 4207 PHE A N     1 
ATOM   20842 C CA    . PHE A 1 4207 ? 202.417 156.395 171.392 1.00 13.38  ? 4207 PHE A CA    1 
ATOM   20843 C C     . PHE A 1 4207 ? 202.820 155.466 170.249 1.00 13.38  ? 4207 PHE A C     1 
ATOM   20844 O O     . PHE A 1 4207 ? 203.357 154.378 170.462 1.00 13.38  ? 4207 PHE A O     1 
ATOM   20845 C CB    . PHE A 1 4207 ? 202.620 155.717 172.748 1.00 13.38  ? 4207 PHE A CB    1 
ATOM   20846 C CG    . PHE A 1 4207 ? 202.555 156.663 173.911 1.00 13.38  ? 4207 PHE A CG    1 
ATOM   20847 C CD1   . PHE A 1 4207 ? 202.761 158.019 173.730 1.00 13.38  ? 4207 PHE A CD1   1 
ATOM   20848 C CD2   . PHE A 1 4207 ? 202.279 156.200 175.184 1.00 13.38  ? 4207 PHE A CD2   1 
ATOM   20849 C CE1   . PHE A 1 4207 ? 202.698 158.892 174.796 1.00 13.38  ? 4207 PHE A CE1   1 
ATOM   20850 C CE2   . PHE A 1 4207 ? 202.215 157.069 176.253 1.00 13.38  ? 4207 PHE A CE2   1 
ATOM   20851 C CZ    . PHE A 1 4207 ? 202.425 158.416 176.058 1.00 13.38  ? 4207 PHE A CZ    1 
ATOM   20852 N N     . GLY A 1 4208 ? 202.555 155.902 169.023 1.00 17.33  ? 4208 GLY A N     1 
ATOM   20853 C CA    . GLY A 1 4208 ? 202.764 155.077 167.852 1.00 17.33  ? 4208 GLY A CA    1 
ATOM   20854 C C     . GLY A 1 4208 ? 204.159 155.198 167.275 1.00 17.33  ? 4208 GLY A C     1 
ATOM   20855 O O     . GLY A 1 4208 ? 205.108 155.628 167.934 1.00 17.33  ? 4208 GLY A O     1 
ATOM   20856 N N     . GLU A 1 4209 ? 204.275 154.796 166.007 1.00 23.64  ? 4209 GLU A N     1 
ATOM   20857 C CA    . GLU A 1 4209 ? 205.565 154.821 165.326 1.00 23.64  ? 4209 GLU A CA    1 
ATOM   20858 C C     . GLU A 1 4209 ? 206.040 156.245 165.064 1.00 23.64  ? 4209 GLU A C     1 
ATOM   20859 O O     . GLU A 1 4209 ? 207.250 156.492 165.005 1.00 23.64  ? 4209 GLU A O     1 
ATOM   20860 C CB    . GLU A 1 4209 ? 205.470 154.035 164.017 1.00 23.64  ? 4209 GLU A CB    1 
ATOM   20861 C CG    . GLU A 1 4209 ? 206.703 154.109 163.131 1.00 23.64  ? 4209 GLU A CG    1 
ATOM   20862 C CD    . GLU A 1 4209 ? 206.418 153.689 161.703 1.00 23.64  ? 4209 GLU A CD    1 
ATOM   20863 O OE1   . GLU A 1 4209 ? 207.202 154.062 160.805 1.00 23.64  ? 4209 GLU A OE1   1 
ATOM   20864 O OE2   . GLU A 1 4209 ? 205.410 152.987 161.479 1.00 23.64  ? 4209 GLU A OE2   1 
ATOM   20865 N N     . SER A 1 4210 ? 205.110 157.190 164.905 1.00 22.95  ? 4210 SER A N     1 
ATOM   20866 C CA    . SER A 1 4210 ? 205.494 158.573 164.641 1.00 22.95  ? 4210 SER A CA    1 
ATOM   20867 C C     . SER A 1 4210 ? 206.312 159.150 165.788 1.00 22.95  ? 4210 SER A C     1 
ATOM   20868 O O     . SER A 1 4210 ? 207.316 159.838 165.562 1.00 22.95  ? 4210 SER A O     1 
ATOM   20869 C CB    . SER A 1 4210 ? 204.249 159.423 164.395 1.00 22.95  ? 4210 SER A CB    1 
ATOM   20870 O OG    . SER A 1 4210 ? 204.552 160.804 164.483 1.00 22.95  ? 4210 SER A OG    1 
ATOM   20871 N N     . ASP A 1 4211 ? 205.897 158.883 167.027 1.00 18.08  ? 4211 ASP A N     1 
ATOM   20872 C CA    . ASP A 1 4211 ? 206.643 159.376 168.179 1.00 18.08  ? 4211 ASP A CA    1 
ATOM   20873 C C     . ASP A 1 4211 ? 208.031 158.752 168.244 1.00 18.08  ? 4211 ASP A C     1 
ATOM   20874 O O     . ASP A 1 4211 ? 209.009 159.430 168.579 1.00 18.08  ? 4211 ASP A O     1 
ATOM   20875 C CB    . ASP A 1 4211 ? 205.865 159.099 169.461 1.00 18.08  ? 4211 ASP A CB    1 
ATOM   20876 C CG    . ASP A 1 4211 ? 204.486 159.717 169.449 1.00 18.08  ? 4211 ASP A CG    1 
ATOM   20877 O OD1   . ASP A 1 4211 ? 204.142 160.384 168.452 1.00 18.08  ? 4211 ASP A OD1   1 
ATOM   20878 O OD2   . ASP A 1 4211 ? 203.742 159.537 170.435 1.00 18.08  ? 4211 ASP A OD2   1 
ATOM   20879 N N     . LEU A 1 4212 ? 208.137 157.459 167.931 1.00 18.10  ? 4212 LEU A N     1 
ATOM   20880 C CA    . LEU A 1 4212 ? 209.444 156.809 167.919 1.00 18.10  ? 4212 LEU A CA    1 
ATOM   20881 C C     . LEU A 1 4212 ? 210.355 157.418 166.861 1.00 18.10  ? 4212 LEU A C     1 
ATOM   20882 O O     . LEU A 1 4212 ? 211.541 157.654 167.116 1.00 18.10  ? 4212 LEU A O     1 
ATOM   20883 C CB    . LEU A 1 4212 ? 209.283 155.309 167.687 1.00 18.10  ? 4212 LEU A CB    1 
ATOM   20884 C CG    . LEU A 1 4212 ? 210.571 154.546 167.375 1.00 18.10  ? 4212 LEU A CG    1 
ATOM   20885 C CD1   . LEU A 1 4212 ? 211.479 154.509 168.590 1.00 18.10  ? 4212 LEU A CD1   1 
ATOM   20886 C CD2   . LEU A 1 4212 ? 210.253 153.142 166.894 1.00 18.10  ? 4212 LEU A CD2   1 
ATOM   20887 N N     . ARG A 1 4213 ? 209.820 157.676 165.665 1.00 20.47  ? 4213 ARG A N     1 
ATOM   20888 C CA    . ARG A 1 4213 ? 210.628 158.293 164.618 1.00 20.47  ? 4213 ARG A CA    1 
ATOM   20889 C C     . ARG A 1 4213 ? 211.063 159.698 165.014 1.00 20.47  ? 4213 ARG A C     1 
ATOM   20890 O O     . ARG A 1 4213 ? 212.206 160.096 164.760 1.00 20.47  ? 4213 ARG A O     1 
ATOM   20891 C CB    . ARG A 1 4213 ? 209.857 158.320 163.299 1.00 20.47  ? 4213 ARG A CB    1 
ATOM   20892 C CG    . ARG A 1 4213 ? 209.602 156.947 162.704 1.00 20.47  ? 4213 ARG A CG    1 
ATOM   20893 C CD    . ARG A 1 4213 ? 208.841 157.046 161.392 1.00 20.47  ? 4213 ARG A CD    1 
ATOM   20894 N NE    . ARG A 1 4213 ? 207.485 157.548 161.581 1.00 20.47  ? 4213 ARG A NE    1 
ATOM   20895 C CZ    . ARG A 1 4213 ? 206.658 157.858 160.592 1.00 20.47  ? 4213 ARG A CZ    1 
ATOM   20896 N NH1   . ARG A 1 4213 ? 207.014 157.725 159.325 1.00 20.47  ? 4213 ARG A NH1   1 
ATOM   20897 N NH2   . ARG A 1 4213 ? 205.442 158.312 160.882 1.00 20.47  ? 4213 ARG A NH2   1 
ATOM   20898 N N     . SER A 1 4214 ? 210.165 160.466 165.635 1.00 15.28  ? 4214 SER A N     1 
ATOM   20899 C CA    . SER A 1 4214 ? 210.527 161.807 166.082 1.00 15.28  ? 4214 SER A CA    1 
ATOM   20900 C C     . SER A 1 4214 ? 211.610 161.760 167.153 1.00 15.28  ? 4214 SER A C     1 
ATOM   20901 O O     . SER A 1 4214 ? 212.544 162.571 167.139 1.00 15.28  ? 4214 SER A O     1 
ATOM   20902 C CB    . SER A 1 4214 ? 209.291 162.539 166.599 1.00 15.28  ? 4214 SER A CB    1 
ATOM   20903 O OG    . SER A 1 4214 ? 208.306 162.645 165.587 1.00 15.28  ? 4214 SER A OG    1 
ATOM   20904 N N     . ALA A 1 4215 ? 211.502 160.818 168.091 1.00 13.98  ? 4215 ALA A N     1 
ATOM   20905 C CA    . ALA A 1 4215 ? 212.527 160.679 169.120 1.00 13.98  ? 4215 ALA A CA    1 
ATOM   20906 C C     . ALA A 1 4215 ? 213.862 160.272 168.514 1.00 13.98  ? 4215 ALA A C     1 
ATOM   20907 O O     . ALA A 1 4215 ? 214.918 160.760 168.934 1.00 13.98  ? 4215 ALA A O     1 
ATOM   20908 C CB    . ALA A 1 4215 ? 212.080 159.668 170.174 1.00 13.98  ? 4215 ALA A CB    1 
ATOM   20909 N N     . CYS A 1 4216 ? 213.837 159.372 167.529 1.00 15.59  ? 4216 CYS A N     1 
ATOM   20910 C CA    . CYS A 1 4216 ? 215.070 158.985 166.852 1.00 15.59  ? 4216 CYS A CA    1 
ATOM   20911 C C     . CYS A 1 4216 ? 215.697 160.172 166.135 1.00 15.59  ? 4216 CYS A C     1 
ATOM   20912 O O     . CYS A 1 4216 ? 216.920 160.353 166.172 1.00 15.59  ? 4216 CYS A O     1 
ATOM   20913 C CB    . CYS A 1 4216 ? 214.794 157.849 165.868 1.00 15.59  ? 4216 CYS A CB    1 
ATOM   20914 S SG    . CYS A 1 4216 ? 214.467 156.249 166.640 1.00 15.59  ? 4216 CYS A SG    1 
ATOM   20915 N N     . ASP A 1 4217 ? 214.876 160.993 165.475 1.00 14.64  ? 4217 ASP A N     1 
ATOM   20916 C CA    . ASP A 1 4217 ? 215.397 162.182 164.808 1.00 14.64  ? 4217 ASP A CA    1 
ATOM   20917 C C     . ASP A 1 4217 ? 216.005 163.155 165.809 1.00 14.64  ? 4217 ASP A C     1 
ATOM   20918 O O     . ASP A 1 4217 ? 217.061 163.745 165.551 1.00 14.64  ? 4217 ASP A O     1 
ATOM   20919 C CB    . ASP A 1 4217 ? 214.290 162.866 164.007 1.00 14.64  ? 4217 ASP A CB    1 
ATOM   20920 C CG    . ASP A 1 4217 ? 213.858 162.058 162.803 1.00 14.64  ? 4217 ASP A CG    1 
ATOM   20921 O OD1   . ASP A 1 4217 ? 214.423 160.966 162.585 1.00 14.64  ? 4217 ASP A OD1   1 
ATOM   20922 O OD2   . ASP A 1 4217 ? 212.955 162.516 162.073 1.00 14.64  ? 4217 ASP A OD2   1 
ATOM   20923 N N     . THR A 1 4218 ? 215.345 163.344 166.954 1.00 11.70  ? 4218 THR A N     1 
ATOM   20924 C CA    . THR A 1 4218 ? 215.885 164.227 167.982 1.00 11.70  ? 4218 THR A CA    1 
ATOM   20925 C C     . THR A 1 4218 ? 217.221 163.713 168.502 1.00 11.70  ? 4218 THR A C     1 
ATOM   20926 O O     . THR A 1 4218 ? 218.176 164.486 168.658 1.00 11.70  ? 4218 THR A O     1 
ATOM   20927 C CB    . THR A 1 4218 ? 214.881 164.372 169.127 1.00 11.70  ? 4218 THR A CB    1 
ATOM   20928 O OG1   . THR A 1 4218 ? 213.816 165.241 168.722 1.00 11.70  ? 4218 THR A OG1   1 
ATOM   20929 C CG2   . THR A 1 4218 ? 215.550 164.942 170.365 1.00 11.70  ? 4218 THR A CG2   1 
ATOM   20930 N N     . VAL A 1 4219 ? 217.310 162.407 168.762 1.00 15.00  ? 4219 VAL A N     1 
ATOM   20931 C CA    . VAL A 1 4219 ? 218.561 161.822 169.237 1.00 15.00  ? 4219 VAL A CA    1 
ATOM   20932 C C     . VAL A 1 4219 ? 219.659 162.015 168.200 1.00 15.00  ? 4219 VAL A C     1 
ATOM   20933 O O     . VAL A 1 4219 ? 220.784 162.408 168.528 1.00 15.00  ? 4219 VAL A O     1 
ATOM   20934 C CB    . VAL A 1 4219 ? 218.364 160.334 169.578 1.00 15.00  ? 4219 VAL A CB    1 
ATOM   20935 C CG1   . VAL A 1 4219 ? 219.706 159.632 169.687 1.00 15.00  ? 4219 VAL A CG1   1 
ATOM   20936 C CG2   . VAL A 1 4219 ? 217.577 160.187 170.868 1.00 15.00  ? 4219 VAL A CG2   1 
ATOM   20937 N N     . ASP A 1 4220 ? 219.342 161.756 166.930 1.00 16.75  ? 4220 ASP A N     1 
ATOM   20938 C CA    . ASP A 1 4220 ? 220.326 161.919 165.866 1.00 16.75  ? 4220 ASP A CA    1 
ATOM   20939 C C     . ASP A 1 4220 ? 220.829 163.355 165.800 1.00 16.75  ? 4220 ASP A C     1 
ATOM   20940 O O     . ASP A 1 4220 ? 222.041 163.601 165.788 1.00 16.75  ? 4220 ASP A O     1 
ATOM   20941 C CB    . ASP A 1 4220 ? 219.715 161.509 164.526 1.00 16.75  ? 4220 ASP A CB    1 
ATOM   20942 C CG    . ASP A 1 4220 ? 219.834 160.024 164.261 1.00 16.75  ? 4220 ASP A CG    1 
ATOM   20943 O OD1   . ASP A 1 4220 ? 220.871 159.433 164.623 1.00 16.75  ? 4220 ASP A OD1   1 
ATOM   20944 O OD2   . ASP A 1 4220 ? 218.887 159.446 163.688 1.00 16.75  ? 4220 ASP A OD2   1 
ATOM   20945 N N     . THR A 1 4221 ? 219.905 164.320 165.766 1.00 15.65  ? 4221 THR A N     1 
ATOM   20946 C CA    . THR A 1 4221 ? 220.297 165.718 165.623 1.00 15.65  ? 4221 THR A CA    1 
ATOM   20947 C C     . THR A 1 4221 ? 221.120 166.191 166.813 1.00 15.65  ? 4221 THR A C     1 
ATOM   20948 O O     . THR A 1 4221 ? 222.145 166.859 166.640 1.00 15.65  ? 4221 THR A O     1 
ATOM   20949 C CB    . THR A 1 4221 ? 219.061 166.600 165.450 1.00 15.65  ? 4221 THR A CB    1 
ATOM   20950 O OG1   . THR A 1 4221 ? 218.106 166.290 166.471 1.00 15.65  ? 4221 THR A OG1   1 
ATOM   20951 C CG2   . THR A 1 4221 ? 218.430 166.372 164.088 1.00 15.65  ? 4221 THR A CG2   1 
ATOM   20952 N N     . TRP A 1 4222 ? 220.702 165.841 168.032 1.00 12.66  ? 4222 TRP A N     1 
ATOM   20953 C CA    . TRP A 1 4222 ? 221.420 166.333 169.201 1.00 12.66  ? 4222 TRP A CA    1 
ATOM   20954 C C     . TRP A 1 4222 ? 222.765 165.641 169.379 1.00 12.66  ? 4222 TRP A C     1 
ATOM   20955 O O     . TRP A 1 4222 ? 223.725 166.273 169.835 1.00 12.66  ? 4222 TRP A O     1 
ATOM   20956 C CB    . TRP A 1 4222 ? 220.557 166.181 170.450 1.00 12.66  ? 4222 TRP A CB    1 
ATOM   20957 C CG    . TRP A 1 4222 ? 219.551 167.274 170.562 1.00 12.66  ? 4222 TRP A CG    1 
ATOM   20958 C CD1   . TRP A 1 4222 ? 218.235 167.216 170.221 1.00 12.66  ? 4222 TRP A CD1   1 
ATOM   20959 C CD2   . TRP A 1 4222 ? 219.789 168.608 171.022 1.00 12.66  ? 4222 TRP A CD2   1 
ATOM   20960 N NE1   . TRP A 1 4222 ? 217.633 168.427 170.451 1.00 12.66  ? 4222 TRP A NE1   1 
ATOM   20961 C CE2   . TRP A 1 4222 ? 218.567 169.300 170.943 1.00 12.66  ? 4222 TRP A CE2   1 
ATOM   20962 C CE3   . TRP A 1 4222 ? 220.916 169.282 171.498 1.00 12.66  ? 4222 TRP A CE3   1 
ATOM   20963 C CZ2   . TRP A 1 4222 ? 218.439 170.631 171.324 1.00 12.66  ? 4222 TRP A CZ2   1 
ATOM   20964 C CZ3   . TRP A 1 4222 ? 220.787 170.604 171.875 1.00 12.66  ? 4222 TRP A CZ3   1 
ATOM   20965 C CH2   . TRP A 1 4222 ? 219.558 171.265 171.787 1.00 12.66  ? 4222 TRP A CH2   1 
ATOM   20966 N N     . LEU A 1 4223 ? 222.869 164.361 169.016 1.00 18.59  ? 4223 LEU A N     1 
ATOM   20967 C CA    . LEU A 1 4223 ? 224.158 163.689 169.101 1.00 18.59  ? 4223 LEU A CA    1 
ATOM   20968 C C     . LEU A 1 4223 ? 225.114 164.206 168.034 1.00 18.59  ? 4223 LEU A C     1 
ATOM   20969 O O     . LEU A 1 4223 ? 226.322 164.305 168.273 1.00 18.59  ? 4223 LEU A O     1 
ATOM   20970 C CB    . LEU A 1 4223 ? 223.969 162.179 168.983 1.00 18.59  ? 4223 LEU A CB    1 
ATOM   20971 C CG    . LEU A 1 4223 ? 225.187 161.322 169.320 1.00 18.59  ? 4223 LEU A CG    1 
ATOM   20972 C CD1   . LEU A 1 4223 ? 225.613 161.565 170.754 1.00 18.59  ? 4223 LEU A CD1   1 
ATOM   20973 C CD2   . LEU A 1 4223 ? 224.872 159.858 169.102 1.00 18.59  ? 4223 LEU A CD2   1 
ATOM   20974 N N     . ASP A 1 4224 ? 224.596 164.543 166.849 1.00 22.25  ? 4224 ASP A N     1 
ATOM   20975 C CA    . ASP A 1 4224 ? 225.437 165.183 165.842 1.00 22.25  ? 4224 ASP A CA    1 
ATOM   20976 C C     . ASP A 1 4224 ? 225.894 166.561 166.302 1.00 22.25  ? 4224 ASP A C     1 
ATOM   20977 O O     . ASP A 1 4224 ? 227.049 166.944 166.084 1.00 22.25  ? 4224 ASP A O     1 
ATOM   20978 C CB    . ASP A 1 4224 ? 224.687 165.283 164.515 1.00 22.25  ? 4224 ASP A CB    1 
ATOM   20979 C CG    . ASP A 1 4224 ? 224.441 163.930 163.881 1.00 22.25  ? 4224 ASP A CG    1 
ATOM   20980 O OD1   . ASP A 1 4224 ? 223.924 163.886 162.745 1.00 22.25  ? 4224 ASP A OD1   1 
ATOM   20981 O OD2   . ASP A 1 4224 ? 224.771 162.910 164.518 1.00 22.25  ? 4224 ASP A OD2   1 
ATOM   20982 N N     . ASP A 1 4225 ? 224.998 167.323 166.932 1.00 21.97  ? 4225 ASP A N     1 
ATOM   20983 C CA    . ASP A 1 4225 ? 225.354 168.661 167.392 1.00 21.97  ? 4225 ASP A CA    1 
ATOM   20984 C C     . ASP A 1 4225 ? 226.419 168.601 168.481 1.00 21.97  ? 4225 ASP A C     1 
ATOM   20985 O O     . ASP A 1 4225 ? 227.422 169.322 168.423 1.00 21.97  ? 4225 ASP A O     1 
ATOM   20986 C CB    . ASP A 1 4225 ? 224.102 169.385 167.893 1.00 21.97  ? 4225 ASP A CB    1 
ATOM   20987 C CG    . ASP A 1 4225 ? 224.368 170.831 168.273 1.00 21.97  ? 4225 ASP A CG    1 
ATOM   20988 O OD1   . ASP A 1 4225 ? 225.477 171.337 167.999 1.00 21.97  ? 4225 ASP A OD1   1 
ATOM   20989 O OD2   . ASP A 1 4225 ? 223.455 171.466 168.843 1.00 21.97  ? 4225 ASP A OD2   1 
ATOM   20990 N N     . THR A 1 4226 ? 226.226 167.736 169.479 1.00 23.10  ? 4226 THR A N     1 
ATOM   20991 C CA    . THR A 1 4226 ? 227.190 167.651 170.571 1.00 23.10  ? 4226 THR A CA    1 
ATOM   20992 C C     . THR A 1 4226 ? 228.483 166.984 170.120 1.00 23.10  ? 4226 THR A C     1 
ATOM   20993 O O     . THR A 1 4226 ? 229.574 167.382 170.545 1.00 23.10  ? 4226 THR A O     1 
ATOM   20994 C CB    . THR A 1 4226 ? 226.579 166.903 171.754 1.00 23.10  ? 4226 THR A CB    1 
ATOM   20995 O OG1   . THR A 1 4226 ? 225.343 167.527 172.120 1.00 23.10  ? 4226 THR A OG1   1 
ATOM   20996 C CG2   . THR A 1 4226 ? 227.521 166.937 172.946 1.00 23.10  ? 4226 THR A CG2   1 
ATOM   20997 N N     . ALA A 1 4227 ? 228.388 165.978 169.257 1.00 26.91  ? 4227 ALA A N     1 
ATOM   20998 C CA    . ALA A 1 4227 ? 229.550 165.236 168.773 1.00 26.91  ? 4227 ALA A CA    1 
ATOM   20999 C C     . ALA A 1 4227 ? 229.793 165.616 167.315 1.00 26.91  ? 4227 ALA A C     1 
ATOM   21000 O O     . ALA A 1 4227 ? 229.169 165.072 166.403 1.00 26.91  ? 4227 ALA A O     1 
ATOM   21001 C CB    . ALA A 1 4227 ? 229.344 163.737 168.928 1.00 26.91  ? 4227 ALA A CB    1 
ATOM   21002 N N     . LYS A 1 4228 ? 230.708 166.564 167.105 1.00 34.74  ? 4228 LYS A N     1 
ATOM   21003 C CA    . LYS A 1 4228 ? 231.058 166.972 165.749 1.00 34.74  ? 4228 LYS A CA    1 
ATOM   21004 C C     . LYS A 1 4228 ? 231.788 165.860 165.005 1.00 34.74  ? 4228 LYS A C     1 
ATOM   21005 O O     . LYS A 1 4228 ? 231.539 165.633 163.815 1.00 34.74  ? 4228 LYS A O     1 
ATOM   21006 C CB    . LYS A 1 4228 ? 231.906 168.242 165.788 1.00 34.74  ? 4228 LYS A CB    1 
ATOM   21007 C CG    . LYS A 1 4228 ? 231.579 169.166 166.950 1.00 34.74  ? 4228 LYS A CG    1 
ATOM   21008 C CD    . LYS A 1 4228 ? 230.235 169.847 166.751 1.00 34.74  ? 4228 LYS A CD    1 
ATOM   21009 C CE    . LYS A 1 4228 ? 230.253 170.748 165.527 1.00 34.74  ? 4228 LYS A CE    1 
ATOM   21010 N NZ    . LYS A 1 4228 ? 228.882 171.089 165.057 1.00 34.74  ? 4228 LYS A NZ    1 
ATOM   21011 N N     . GLY A 1 4229 ? 232.696 165.160 165.687 1.00 42.49  ? 4229 GLY A N     1 
ATOM   21012 C CA    . GLY A 1 4229 ? 233.477 164.125 165.048 1.00 42.49  ? 4229 GLY A CA    1 
ATOM   21013 C C     . GLY A 1 4229 ? 232.948 162.726 165.302 1.00 42.49  ? 4229 GLY A C     1 
ATOM   21014 O O     . GLY A 1 4229 ? 232.074 162.506 166.137 1.00 42.49  ? 4229 GLY A O     1 
ATOM   21015 N N     . ARG A 1 4230 ? 233.504 161.769 164.557 1.00 49.06  ? 4230 ARG A N     1 
ATOM   21016 C CA    . ARG A 1 4230 ? 233.104 160.372 164.674 1.00 49.06  ? 4230 ARG A CA    1 
ATOM   21017 C C     . ARG A 1 4230 ? 233.638 159.707 165.935 1.00 49.06  ? 4230 ARG A C     1 
ATOM   21018 O O     . ARG A 1 4230 ? 233.143 158.637 166.306 1.00 49.06  ? 4230 ARG A O     1 
ATOM   21019 C CB    . ARG A 1 4230 ? 233.572 159.599 163.438 1.00 49.06  ? 4230 ARG A CB    1 
ATOM   21020 C CG    . ARG A 1 4230 ? 232.902 158.248 163.244 1.00 49.06  ? 4230 ARG A CG    1 
ATOM   21021 C CD    . ARG A 1 4230 ? 233.924 157.166 162.929 1.00 49.06  ? 4230 ARG A CD    1 
ATOM   21022 N NE    . ARG A 1 4230 ? 235.012 157.129 163.899 1.00 49.06  ? 4230 ARG A NE    1 
ATOM   21023 C CZ    . ARG A 1 4230 ? 234.941 156.543 165.087 1.00 49.06  ? 4230 ARG A CZ    1 
ATOM   21024 N NH1   . ARG A 1 4230 ? 233.844 155.924 165.489 1.00 49.06  ? 4230 ARG A NH1   1 
ATOM   21025 N NH2   . ARG A 1 4230 ? 236.000 156.577 165.891 1.00 49.06  ? 4230 ARG A NH2   1 
ATOM   21026 N N     . GLN A 1 4231 ? 234.616 160.312 166.604 1.00 46.06  ? 4231 GLN A N     1 
ATOM   21027 C CA    . GLN A 1 4231 ? 235.211 159.691 167.778 1.00 46.06  ? 4231 GLN A CA    1 
ATOM   21028 C C     . GLN A 1 4231 ? 234.170 159.523 168.877 1.00 46.06  ? 4231 GLN A C     1 
ATOM   21029 O O     . GLN A 1 4231 ? 233.211 160.292 168.981 1.00 46.06  ? 4231 GLN A O     1 
ATOM   21030 C CB    . GLN A 1 4231 ? 236.383 160.530 168.291 1.00 46.06  ? 4231 GLN A CB    1 
ATOM   21031 C CG    . GLN A 1 4231 ? 235.969 161.831 168.959 1.00 46.06  ? 4231 GLN A CG    1 
ATOM   21032 C CD    . GLN A 1 4231 ? 235.804 162.964 167.969 1.00 46.06  ? 4231 GLN A CD    1 
ATOM   21033 O OE1   . GLN A 1 4231 ? 235.791 162.745 166.759 1.00 46.06  ? 4231 GLN A OE1   1 
ATOM   21034 N NE2   . GLN A 1 4231 ? 235.670 164.182 168.479 1.00 46.06  ? 4231 GLN A NE2   1 
ATOM   21035 N N     . ASN A 1 4232 ? 234.357 158.489 169.692 1.00 40.86  ? 4232 ASN A N     1 
ATOM   21036 C CA    . ASN A 1 4232 ? 233.459 158.250 170.814 1.00 40.86  ? 4232 ASN A CA    1 
ATOM   21037 C C     . ASN A 1 4232 ? 233.498 159.422 171.791 1.00 40.86  ? 4232 ASN A C     1 
ATOM   21038 O O     . ASN A 1 4232 ? 234.551 160.030 172.010 1.00 40.86  ? 4232 ASN A O     1 
ATOM   21039 C CB    . ASN A 1 4232 ? 233.798 156.923 171.498 1.00 40.86  ? 4232 ASN A CB    1 
ATOM   21040 C CG    . ASN A 1 4232 ? 235.194 156.890 172.120 1.00 40.86  ? 4232 ASN A CG    1 
ATOM   21041 O OD1   . ASN A 1 4232 ? 235.912 157.886 172.166 1.00 40.86  ? 4232 ASN A OD1   1 
ATOM   21042 N ND2   . ASN A 1 4232 ? 235.573 155.720 172.617 1.00 40.86  ? 4232 ASN A ND2   1 
ATOM   21043 N N     . ILE A 1 4233 ? 232.340 159.786 172.320 1.00 28.91  ? 4233 ILE A N     1 
ATOM   21044 C CA    . ILE A 1 4233 ? 232.251 160.891 173.265 1.00 28.91  ? 4233 ILE A CA    1 
ATOM   21045 C C     . ILE A 1 4233 ? 231.944 160.356 174.655 1.00 28.91  ? 4233 ILE A C     1 
ATOM   21046 O O     . ILE A 1 4233 ? 231.360 159.277 174.812 1.00 28.91  ? 4233 ILE A O     1 
ATOM   21047 C CB    . ILE A 1 4233 ? 231.206 161.915 172.791 1.00 28.91  ? 4233 ILE A CB    1 
ATOM   21048 C CG1   . ILE A 1 4233 ? 229.786 161.391 173.013 1.00 28.91  ? 4233 ILE A CG1   1 
ATOM   21049 C CG2   . ILE A 1 4233 ? 231.446 162.254 171.338 1.00 28.91  ? 4233 ILE A CG2   1 
ATOM   21050 C CD1   . ILE A 1 4233 ? 228.721 162.460 172.925 1.00 28.91  ? 4233 ILE A CD1   1 
ATOM   21051 N N     . SER A 1 4234 ? 232.359 161.105 175.669 1.00 24.17  ? 4234 SER A N     1 
ATOM   21052 C CA    . SER A 1 4234 ? 232.188 160.658 177.041 1.00 24.17  ? 4234 SER A CA    1 
ATOM   21053 C C     . SER A 1 4234 ? 230.702 160.547 177.369 1.00 24.17  ? 4234 SER A C     1 
ATOM   21054 O O     . SER A 1 4234 ? 229.906 161.386 176.932 1.00 24.17  ? 4234 SER A O     1 
ATOM   21055 C CB    . SER A 1 4234 ? 232.874 161.625 178.006 1.00 24.17  ? 4234 SER A CB    1 
ATOM   21056 O OG    . SER A 1 4234 ? 232.848 161.133 179.335 1.00 24.17  ? 4234 SER A OG    1 
ATOM   21057 N N     . PRO A 1 4235 ? 230.292 159.523 178.120 1.00 20.39  ? 4235 PRO A N     1 
ATOM   21058 C CA    . PRO A 1 4235 ? 228.865 159.384 178.454 1.00 20.39  ? 4235 PRO A CA    1 
ATOM   21059 C C     . PRO A 1 4235 ? 228.296 160.579 179.194 1.00 20.39  ? 4235 PRO A C     1 
ATOM   21060 O O     . PRO A 1 4235 ? 227.101 160.867 179.057 1.00 20.39  ? 4235 PRO A O     1 
ATOM   21061 C CB    . PRO A 1 4235 ? 228.834 158.116 179.318 1.00 20.39  ? 4235 PRO A CB    1 
ATOM   21062 C CG    . PRO A 1 4235 ? 230.058 157.362 178.927 1.00 20.39  ? 4235 PRO A CG    1 
ATOM   21063 C CD    . PRO A 1 4235 ? 231.093 158.398 178.625 1.00 20.39  ? 4235 PRO A CD    1 
ATOM   21064 N N     . ASP A 1 4236 ? 229.110 161.282 179.981 1.00 20.43  ? 4236 ASP A N     1 
ATOM   21065 C CA    . ASP A 1 4236 ? 228.657 162.489 180.658 1.00 20.43  ? 4236 ASP A CA    1 
ATOM   21066 C C     . ASP A 1 4236 ? 228.544 163.685 179.722 1.00 20.43  ? 4236 ASP A C     1 
ATOM   21067 O O     . ASP A 1 4236 ? 227.964 164.703 180.114 1.00 20.43  ? 4236 ASP A O     1 
ATOM   21068 C CB    . ASP A 1 4236 ? 229.599 162.826 181.817 1.00 20.43  ? 4236 ASP A CB    1 
ATOM   21069 C CG    . ASP A 1 4236 ? 231.025 163.062 181.359 1.00 20.43  ? 4236 ASP A CG    1 
ATOM   21070 O OD1   . ASP A 1 4236 ? 231.342 164.204 180.965 1.00 20.43  ? 4236 ASP A OD1   1 
ATOM   21071 O OD2   . ASP A 1 4236 ? 231.828 162.107 181.390 1.00 20.43  ? 4236 ASP A OD2   1 
ATOM   21072 N N     . LYS A 1 4237 ? 229.078 163.590 178.505 1.00 20.43  ? 4237 LYS A N     1 
ATOM   21073 C CA    . LYS A 1 4237 ? 228.951 164.650 177.515 1.00 20.43  ? 4237 LYS A CA    1 
ATOM   21074 C C     . LYS A 1 4237 ? 227.715 164.502 176.640 1.00 20.43  ? 4237 LYS A C     1 
ATOM   21075 O O     . LYS A 1 4237 ? 227.467 165.369 175.796 1.00 20.43  ? 4237 LYS A O     1 
ATOM   21076 C CB    . LYS A 1 4237 ? 230.199 164.705 176.629 1.00 20.43  ? 4237 LYS A CB    1 
ATOM   21077 C CG    . LYS A 1 4237 ? 231.447 165.171 177.358 1.00 20.43  ? 4237 LYS A CG    1 
ATOM   21078 C CD    . LYS A 1 4237 ? 231.217 166.523 178.014 1.00 20.43  ? 4237 LYS A CD    1 
ATOM   21079 C CE    . LYS A 1 4237 ? 232.497 167.066 178.620 1.00 20.43  ? 4237 LYS A CE    1 
ATOM   21080 N NZ    . LYS A 1 4237 ? 233.060 166.113 179.614 1.00 20.43  ? 4237 LYS A NZ    1 
ATOM   21081 N N     . ILE A 1 4238 ? 226.947 163.433 176.811 1.00 15.78  ? 4238 ILE A N     1 
ATOM   21082 C CA    . ILE A 1 4238 ? 225.692 163.281 176.065 1.00 15.78  ? 4238 ILE A CA    1 
ATOM   21083 C C     . ILE A 1 4238 ? 224.720 164.372 176.498 1.00 15.78  ? 4238 ILE A C     1 
ATOM   21084 O O     . ILE A 1 4238 ? 224.593 164.636 177.708 1.00 15.78  ? 4238 ILE A O     1 
ATOM   21085 C CB    . ILE A 1 4238 ? 225.097 161.891 176.303 1.00 15.78  ? 4238 ILE A CB    1 
ATOM   21086 C CG1   . ILE A 1 4238 ? 226.113 160.797 175.973 1.00 15.78  ? 4238 ILE A CG1   1 
ATOM   21087 C CG2   . ILE A 1 4238 ? 223.830 161.703 175.488 1.00 15.78  ? 4238 ILE A CG2   1 
ATOM   21088 C CD1   . ILE A 1 4238 ? 226.187 160.455 174.507 1.00 15.78  ? 4238 ILE A CD1   1 
ATOM   21089 N N     . PRO A 1 4239 ? 224.019 165.026 175.573 1.00 15.56  ? 4239 PRO A N     1 
ATOM   21090 C CA    . PRO A 1 4239 ? 223.003 166.005 175.979 1.00 15.56  ? 4239 PRO A CA    1 
ATOM   21091 C C     . PRO A 1 4239 ? 221.801 165.335 176.623 1.00 15.56  ? 4239 PRO A C     1 
ATOM   21092 O O     . PRO A 1 4239 ? 220.720 165.278 176.028 1.00 15.56  ? 4239 PRO A O     1 
ATOM   21093 C CB    . PRO A 1 4239 ? 222.628 166.688 174.659 1.00 15.56  ? 4239 PRO A CB    1 
ATOM   21094 C CG    . PRO A 1 4239 ? 222.961 165.681 173.612 1.00 15.56  ? 4239 PRO A CG    1 
ATOM   21095 C CD    . PRO A 1 4239 ? 224.178 164.966 174.111 1.00 15.56  ? 4239 PRO A CD    1 
ATOM   21096 N N     . TRP A 1 4240 ? 221.984 164.820 177.841 1.00 13.57  ? 4240 TRP A N     1 
ATOM   21097 C CA    . TRP A 1 4240 ? 220.899 164.119 178.519 1.00 13.57  ? 4240 TRP A CA    1 
ATOM   21098 C C     . TRP A 1 4240 ? 219.729 165.049 178.804 1.00 13.57  ? 4240 TRP A C     1 
ATOM   21099 O O     . TRP A 1 4240 ? 218.566 164.660 178.651 1.00 13.57  ? 4240 TRP A O     1 
ATOM   21100 C CB    . TRP A 1 4240 ? 221.407 163.491 179.815 1.00 13.57  ? 4240 TRP A CB    1 
ATOM   21101 C CG    . TRP A 1 4240 ? 222.415 162.410 179.608 1.00 13.57  ? 4240 TRP A CG    1 
ATOM   21102 C CD1   . TRP A 1 4240 ? 223.726 162.432 179.979 1.00 13.57  ? 4240 TRP A CD1   1 
ATOM   21103 C CD2   . TRP A 1 4240 ? 222.198 161.143 178.978 1.00 13.57  ? 4240 TRP A CD2   1 
ATOM   21104 N NE1   . TRP A 1 4240 ? 224.339 161.256 179.623 1.00 13.57  ? 4240 TRP A NE1   1 
ATOM   21105 C CE2   . TRP A 1 4240 ? 223.421 160.448 179.006 1.00 13.57  ? 4240 TRP A CE2   1 
ATOM   21106 C CE3   . TRP A 1 4240 ? 221.086 160.528 178.395 1.00 13.57  ? 4240 TRP A CE3   1 
ATOM   21107 C CZ2   . TRP A 1 4240 ? 223.566 159.172 178.473 1.00 13.57  ? 4240 TRP A CZ2   1 
ATOM   21108 C CZ3   . TRP A 1 4240 ? 221.232 159.261 177.867 1.00 13.57  ? 4240 TRP A CZ3   1 
ATOM   21109 C CH2   . TRP A 1 4240 ? 222.462 158.597 177.909 1.00 13.57  ? 4240 TRP A CH2   1 
ATOM   21110 N N     . SER A 1 4241 ? 220.018 166.282 179.227 1.00 11.23  ? 4241 SER A N     1 
ATOM   21111 C CA    . SER A 1 4241 ? 218.949 167.229 179.525 1.00 11.23  ? 4241 SER A CA    1 
ATOM   21112 C C     . SER A 1 4241 ? 218.124 167.537 178.284 1.00 11.23  ? 4241 SER A C     1 
ATOM   21113 O O     . SER A 1 4241 ? 216.891 167.595 178.349 1.00 11.23  ? 4241 SER A O     1 
ATOM   21114 C CB    . SER A 1 4241 ? 219.536 168.512 180.111 1.00 11.23  ? 4241 SER A CB    1 
ATOM   21115 O OG    . SER A 1 4241 ? 220.304 168.238 181.268 1.00 11.23  ? 4241 SER A OG    1 
ATOM   21116 N N     . ALA A 1 4242 ? 218.789 167.733 177.143 1.00 9.97   ? 4242 ALA A N     1 
ATOM   21117 C CA    . ALA A 1 4242 ? 218.075 168.028 175.905 1.00 9.97   ? 4242 ALA A CA    1 
ATOM   21118 C C     . ALA A 1 4242 ? 217.149 166.884 175.518 1.00 9.97   ? 4242 ALA A C     1 
ATOM   21119 O O     . ALA A 1 4242 ? 215.973 167.100 175.200 1.00 9.97   ? 4242 ALA A O     1 
ATOM   21120 C CB    . ALA A 1 4242 ? 219.072 168.312 174.784 1.00 9.97   ? 4242 ALA A CB    1 
ATOM   21121 N N     . LEU A 1 4243 ? 217.665 165.653 175.542 1.00 9.16   ? 4243 LEU A N     1 
ATOM   21122 C CA    . LEU A 1 4243 ? 216.850 164.500 175.177 1.00 9.16   ? 4243 LEU A CA    1 
ATOM   21123 C C     . LEU A 1 4243 ? 215.677 164.334 176.134 1.00 9.16   ? 4243 LEU A C     1 
ATOM   21124 O O     . LEU A 1 4243 ? 214.541 164.113 175.705 1.00 9.16   ? 4243 LEU A O     1 
ATOM   21125 C CB    . LEU A 1 4243 ? 217.707 163.235 175.151 1.00 9.16   ? 4243 LEU A CB    1 
ATOM   21126 C CG    . LEU A 1 4243 ? 218.897 163.222 174.192 1.00 9.16   ? 4243 LEU A CG    1 
ATOM   21127 C CD1   . LEU A 1 4243 ? 219.555 161.856 174.178 1.00 9.16   ? 4243 LEU A CD1   1 
ATOM   21128 C CD2   . LEU A 1 4243 ? 218.456 163.616 172.796 1.00 9.16   ? 4243 LEU A CD2   1 
ATOM   21129 N N     . LYS A 1 4244 ? 215.932 164.452 177.438 1.00 9.39   ? 4244 LYS A N     1 
ATOM   21130 C CA    . LYS A 1 4244 ? 214.863 164.278 178.415 1.00 9.39   ? 4244 LYS A CA    1 
ATOM   21131 C C     . LYS A 1 4244 ? 213.779 165.334 178.240 1.00 9.39   ? 4244 LYS A C     1 
ATOM   21132 O O     . LYS A 1 4244 ? 212.585 165.018 178.238 1.00 9.39   ? 4244 LYS A O     1 
ATOM   21133 C CB    . LYS A 1 4244 ? 215.436 164.318 179.831 1.00 9.39   ? 4244 LYS A CB    1 
ATOM   21134 C CG    . LYS A 1 4244 ? 216.232 163.084 180.208 1.00 9.39   ? 4244 LYS A CG    1 
ATOM   21135 C CD    . LYS A 1 4244 ? 216.277 162.897 181.713 1.00 9.39   ? 4244 LYS A CD    1 
ATOM   21136 C CE    . LYS A 1 4244 ? 216.992 164.049 182.393 1.00 9.39   ? 4244 LYS A CE    1 
ATOM   21137 N NZ    . LYS A 1 4244 ? 218.453 164.023 182.119 1.00 9.39   ? 4244 LYS A NZ    1 
ATOM   21138 N N     . THR A 1 4245 ? 214.175 166.597 178.069 1.00 8.81   ? 4245 THR A N     1 
ATOM   21139 C CA    . THR A 1 4245 ? 213.186 167.658 177.923 1.00 8.81   ? 4245 THR A CA    1 
ATOM   21140 C C     . THR A 1 4245 ? 212.391 167.507 176.632 1.00 8.81   ? 4245 THR A C     1 
ATOM   21141 O O     . THR A 1 4245 ? 211.165 167.674 176.631 1.00 8.81   ? 4245 THR A O     1 
ATOM   21142 C CB    . THR A 1 4245 ? 213.867 169.022 177.980 1.00 8.81   ? 4245 THR A CB    1 
ATOM   21143 O OG1   . THR A 1 4245 ? 214.584 169.148 179.214 1.00 8.81   ? 4245 THR A OG1   1 
ATOM   21144 C CG2   . THR A 1 4245 ? 212.838 170.135 177.886 1.00 8.81   ? 4245 THR A CG2   1 
ATOM   21145 N N     . LEU A 1 4246 ? 213.060 167.182 175.524 1.00 9.17   ? 4246 LEU A N     1 
ATOM   21146 C CA    . LEU A 1 4246 ? 212.359 167.067 174.252 1.00 9.17   ? 4246 LEU A CA    1 
ATOM   21147 C C     . LEU A 1 4246 ? 211.504 165.811 174.156 1.00 9.17   ? 4246 LEU A C     1 
ATOM   21148 O O     . LEU A 1 4246 ? 210.548 165.792 173.375 1.00 9.17   ? 4246 LEU A O     1 
ATOM   21149 C CB    . LEU A 1 4246 ? 213.355 167.104 173.093 1.00 9.17   ? 4246 LEU A CB    1 
ATOM   21150 C CG    . LEU A 1 4246 ? 213.956 168.476 172.787 1.00 9.17   ? 4246 LEU A CG    1 
ATOM   21151 C CD1   . LEU A 1 4246 ? 214.511 168.505 171.380 1.00 9.17   ? 4246 LEU A CD1   1 
ATOM   21152 C CD2   . LEU A 1 4246 ? 212.922 169.570 172.973 1.00 9.17   ? 4246 LEU A CD2   1 
ATOM   21153 N N     . MET A 1 4247 ? 211.819 164.768 174.922 1.00 10.23  ? 4247 MET A N     1 
ATOM   21154 C CA    . MET A 1 4247 ? 210.994 163.571 174.977 1.00 10.23  ? 4247 MET A CA    1 
ATOM   21155 C C     . MET A 1 4247 ? 210.000 163.600 176.128 1.00 10.23  ? 4247 MET A C     1 
ATOM   21156 O O     . MET A 1 4247 ? 209.234 162.647 176.296 1.00 10.23  ? 4247 MET A O     1 
ATOM   21157 C CB    . MET A 1 4247 ? 211.880 162.330 175.076 1.00 10.23  ? 4247 MET A CB    1 
ATOM   21158 C CG    . MET A 1 4247 ? 212.898 162.207 173.958 1.00 10.23  ? 4247 MET A CG    1 
ATOM   21159 S SD    . MET A 1 4247 ? 213.663 160.582 173.926 1.00 10.23  ? 4247 MET A SD    1 
ATOM   21160 C CE    . MET A 1 4247 ? 212.208 159.549 173.991 1.00 10.23  ? 4247 MET A CE    1 
ATOM   21161 N N     . ALA A 1 4248 ? 210.014 164.654 176.942 1.00 11.27  ? 4248 ALA A N     1 
ATOM   21162 C CA    . ALA A 1 4248 ? 208.996 164.842 177.962 1.00 11.27  ? 4248 ALA A CA    1 
ATOM   21163 C C     . ALA A 1 4248 ? 208.017 165.964 177.661 1.00 11.27  ? 4248 ALA A C     1 
ATOM   21164 O O     . ALA A 1 4248 ? 206.935 165.983 178.257 1.00 11.27  ? 4248 ALA A O     1 
ATOM   21165 C CB    . ALA A 1 4248 ? 209.644 165.117 179.327 1.00 11.27  ? 4248 ALA A CB    1 
ATOM   21166 N N     . GLN A 1 4249 ? 208.356 166.896 176.767 1.00 12.29  ? 4249 GLN A N     1 
ATOM   21167 C CA    . GLN A 1 4249 ? 207.484 168.028 176.489 1.00 12.29  ? 4249 GLN A CA    1 
ATOM   21168 C C     . GLN A 1 4249 ? 207.009 168.114 175.046 1.00 12.29  ? 4249 GLN A C     1 
ATOM   21169 O O     . GLN A 1 4249 ? 205.953 168.704 174.802 1.00 12.29  ? 4249 GLN A O     1 
ATOM   21170 C CB    . GLN A 1 4249 ? 208.187 169.341 176.860 1.00 12.29  ? 4249 GLN A CB    1 
ATOM   21171 C CG    . GLN A 1 4249 ? 208.429 169.499 178.350 1.00 12.29  ? 4249 GLN A CG    1 
ATOM   21172 C CD    . GLN A 1 4249 ? 209.136 170.793 178.693 1.00 12.29  ? 4249 GLN A CD    1 
ATOM   21173 O OE1   . GLN A 1 4249 ? 209.511 171.563 177.810 1.00 12.29  ? 4249 GLN A OE1   1 
ATOM   21174 N NE2   . GLN A 1 4249 ? 209.324 171.038 179.984 1.00 12.29  ? 4249 GLN A NE2   1 
ATOM   21175 N N     . SER A 1 4250 ? 207.747 167.552 174.091 1.00 12.37  ? 4250 SER A N     1 
ATOM   21176 C CA    . SER A 1 4250 ? 207.328 167.609 172.696 1.00 12.37  ? 4250 SER A CA    1 
ATOM   21177 C C     . SER A 1 4250 ? 206.992 166.220 172.168 1.00 12.37  ? 4250 SER A C     1 
ATOM   21178 O O     . SER A 1 4250 ? 205.887 165.989 171.669 1.00 12.37  ? 4250 SER A O     1 
ATOM   21179 C CB    . SER A 1 4250 ? 208.417 168.251 171.836 1.00 12.37  ? 4250 SER A CB    1 
ATOM   21180 O OG    . SER A 1 4250 ? 209.575 167.438 171.800 1.00 12.37  ? 4250 SER A OG    1 
ATOM   21181 N N     . ILE A 1 4251 ? 207.942 165.291 172.276 1.00 10.99  ? 4251 ILE A N     1 
ATOM   21182 C CA    . ILE A 1 4251 ? 207.708 163.919 171.848 1.00 10.99  ? 4251 ILE A CA    1 
ATOM   21183 C C     . ILE A 1 4251 ? 207.257 163.094 173.043 1.00 10.99  ? 4251 ILE A C     1 
ATOM   21184 O O     . ILE A 1 4251 ? 207.793 163.235 174.149 1.00 10.99  ? 4251 ILE A O     1 
ATOM   21185 C CB    . ILE A 1 4251 ? 208.981 163.333 171.218 1.00 10.99  ? 4251 ILE A CB    1 
ATOM   21186 C CG1   . ILE A 1 4251 ? 209.571 164.312 170.207 1.00 10.99  ? 4251 ILE A CG1   1 
ATOM   21187 C CG2   . ILE A 1 4251 ? 208.676 162.012 170.546 1.00 10.99  ? 4251 ILE A CG2   1 
ATOM   21188 C CD1   . ILE A 1 4251 ? 210.995 163.997 169.825 1.00 10.99  ? 4251 ILE A CD1   1 
ATOM   21189 N N     . TYR A 1 4252 ? 206.227 162.269 172.841 1.00 12.81  ? 4252 TYR A N     1 
ATOM   21190 C CA    . TYR A 1 4252 ? 205.668 161.410 173.883 1.00 12.81  ? 4252 TYR A CA    1 
ATOM   21191 C C     . TYR A 1 4252 ? 204.992 162.222 174.982 1.00 12.81  ? 4252 TYR A C     1 
ATOM   21192 O O     . TYR A 1 4252 ? 204.390 161.652 175.897 1.00 12.81  ? 4252 TYR A O     1 
ATOM   21193 C CB    . TYR A 1 4252 ? 206.741 160.509 174.507 1.00 12.81  ? 4252 TYR A CB    1 
ATOM   21194 C CG    . TYR A 1 4252 ? 207.312 159.454 173.591 1.00 12.81  ? 4252 TYR A CG    1 
ATOM   21195 C CD1   . TYR A 1 4252 ? 206.500 158.482 173.030 1.00 12.81  ? 4252 TYR A CD1   1 
ATOM   21196 C CD2   . TYR A 1 4252 ? 208.667 159.421 173.303 1.00 12.81  ? 4252 TYR A CD2   1 
ATOM   21197 C CE1   . TYR A 1 4252 ? 207.021 157.509 172.204 1.00 12.81  ? 4252 TYR A CE1   1 
ATOM   21198 C CE2   . TYR A 1 4252 ? 209.196 158.455 172.473 1.00 12.81  ? 4252 TYR A CE2   1 
ATOM   21199 C CZ    . TYR A 1 4252 ? 208.368 157.502 171.926 1.00 12.81  ? 4252 TYR A CZ    1 
ATOM   21200 O OH    . TYR A 1 4252 ? 208.890 156.536 171.100 1.00 12.81  ? 4252 TYR A OH    1 
ATOM   21201 N N     . GLY A 1 4253 ? 205.078 163.550 174.902 1.00 12.75  ? 4253 GLY A N     1 
ATOM   21202 C CA    . GLY A 1 4253 ? 204.513 164.393 175.938 1.00 12.75  ? 4253 GLY A CA    1 
ATOM   21203 C C     . GLY A 1 4253 ? 203.440 165.334 175.444 1.00 12.75  ? 4253 GLY A C     1 
ATOM   21204 O O     . GLY A 1 4253 ? 202.642 165.824 176.249 1.00 12.75  ? 4253 GLY A O     1 
ATOM   21205 N N     . GLY A 1 4254 ? 203.406 165.604 174.139 1.00 13.26  ? 4254 GLY A N     1 
ATOM   21206 C CA    . GLY A 1 4254 ? 202.373 166.471 173.603 1.00 13.26  ? 4254 GLY A CA    1 
ATOM   21207 C C     . GLY A 1 4254 ? 200.980 165.909 173.804 1.00 13.26  ? 4254 GLY A C     1 
ATOM   21208 O O     . GLY A 1 4254 ? 200.041 166.645 174.113 1.00 13.26  ? 4254 GLY A O     1 
ATOM   21209 N N     . ARG A 1 4255 ? 200.827 164.597 173.638 1.00 14.68  ? 4255 ARG A N     1 
ATOM   21210 C CA    . ARG A 1 4255 ? 199.526 163.961 173.790 1.00 14.68  ? 4255 ARG A CA    1 
ATOM   21211 C C     . ARG A 1 4255 ? 199.166 163.666 175.240 1.00 14.68  ? 4255 ARG A C     1 
ATOM   21212 O O     . ARG A 1 4255 ? 198.026 163.272 175.506 1.00 14.68  ? 4255 ARG A O     1 
ATOM   21213 C CB    . ARG A 1 4255 ? 199.481 162.673 172.967 1.00 14.68  ? 4255 ARG A CB    1 
ATOM   21214 C CG    . ARG A 1 4255 ? 200.687 161.777 173.151 1.00 14.68  ? 4255 ARG A CG    1 
ATOM   21215 C CD    . ARG A 1 4255 ? 200.501 160.464 172.415 1.00 14.68  ? 4255 ARG A CD    1 
ATOM   21216 N NE    . ARG A 1 4255 ? 200.028 160.657 171.048 1.00 14.68  ? 4255 ARG A NE    1 
ATOM   21217 C CZ    . ARG A 1 4255 ? 200.760 161.149 170.057 1.00 14.68  ? 4255 ARG A CZ    1 
ATOM   21218 N NH1   . ARG A 1 4255 ? 202.022 161.503 170.238 1.00 14.68  ? 4255 ARG A NH1   1 
ATOM   21219 N NH2   . ARG A 1 4255 ? 200.213 161.284 168.853 1.00 14.68  ? 4255 ARG A NH2   1 
ATOM   21220 N N     . VAL A 1 4256 ? 200.095 163.842 176.179 1.00 14.74  ? 4256 VAL A N     1 
ATOM   21221 C CA    . VAL A 1 4256 ? 199.777 163.660 177.589 1.00 14.74  ? 4256 VAL A CA    1 
ATOM   21222 C C     . VAL A 1 4256 ? 199.141 164.934 178.126 1.00 14.74  ? 4256 VAL A C     1 
ATOM   21223 O O     . VAL A 1 4256 ? 199.715 166.025 178.017 1.00 14.74  ? 4256 VAL A O     1 
ATOM   21224 C CB    . VAL A 1 4256 ? 201.036 163.288 178.383 1.00 14.74  ? 4256 VAL A CB    1 
ATOM   21225 C CG1   . VAL A 1 4256 ? 200.728 163.238 179.867 1.00 14.74  ? 4256 VAL A CG1   1 
ATOM   21226 C CG2   . VAL A 1 4256 ? 201.590 161.958 177.905 1.00 14.74  ? 4256 VAL A CG2   1 
ATOM   21227 N N     . ASP A 1 4257 ? 197.954 164.802 178.717 1.00 17.59  ? 4257 ASP A N     1 
ATOM   21228 C CA    . ASP A 1 4257 ? 197.183 165.955 179.165 1.00 17.59  ? 4257 ASP A CA    1 
ATOM   21229 C C     . ASP A 1 4257 ? 197.209 166.130 180.679 1.00 17.59  ? 4257 ASP A C     1 
ATOM   21230 O O     . ASP A 1 4257 ? 197.575 167.204 181.164 1.00 17.59  ? 4257 ASP A O     1 
ATOM   21231 C CB    . ASP A 1 4257 ? 195.738 165.848 178.655 1.00 17.59  ? 4257 ASP A CB    1 
ATOM   21232 C CG    . ASP A 1 4257 ? 195.083 164.536 179.023 1.00 17.59  ? 4257 ASP A CG    1 
ATOM   21233 O OD1   . ASP A 1 4257 ? 195.758 163.681 179.632 1.00 17.59  ? 4257 ASP A OD1   1 
ATOM   21234 O OD2   . ASP A 1 4257 ? 193.891 164.357 178.696 1.00 17.59  ? 4257 ASP A OD2   1 
ATOM   21235 N N     . ASN A 1 4258 ? 196.833 165.110 181.446 1.00 15.22  ? 4258 ASN A N     1 
ATOM   21236 C CA    . ASN A 1 4258 ? 196.815 165.256 182.895 1.00 15.22  ? 4258 ASN A CA    1 
ATOM   21237 C C     . ASN A 1 4258 ? 198.232 165.269 183.461 1.00 15.22  ? 4258 ASN A C     1 
ATOM   21238 O O     . ASN A 1 4258 ? 199.186 164.808 182.829 1.00 15.22  ? 4258 ASN A O     1 
ATOM   21239 C CB    . ASN A 1 4258 ? 195.967 164.156 183.544 1.00 15.22  ? 4258 ASN A CB    1 
ATOM   21240 C CG    . ASN A 1 4258 ? 196.519 162.762 183.320 1.00 15.22  ? 4258 ASN A CG    1 
ATOM   21241 O OD1   . ASN A 1 4258 ? 197.605 162.584 182.780 1.00 15.22  ? 4258 ASN A OD1   1 
ATOM   21242 N ND2   . ASN A 1 4258 ? 195.766 161.760 183.754 1.00 15.22  ? 4258 ASN A ND2   1 
ATOM   21243 N N     . GLU A 1 4259 ? 198.363 165.829 184.664 1.00 16.55  ? 4259 GLU A N     1 
ATOM   21244 C CA    . GLU A 1 4259 ? 199.687 166.072 185.227 1.00 16.55  ? 4259 GLU A CA    1 
ATOM   21245 C C     . GLU A 1 4259 ? 200.345 164.787 185.715 1.00 16.55  ? 4259 GLU A C     1 
ATOM   21246 O O     . GLU A 1 4259 ? 201.575 164.685 185.705 1.00 16.55  ? 4259 GLU A O     1 
ATOM   21247 C CB    . GLU A 1 4259 ? 199.583 167.096 186.361 1.00 16.55  ? 4259 GLU A CB    1 
ATOM   21248 C CG    . GLU A 1 4259 ? 200.915 167.624 186.887 1.00 16.55  ? 4259 GLU A CG    1 
ATOM   21249 C CD    . GLU A 1 4259 ? 201.555 166.720 187.924 1.00 16.55  ? 4259 GLU A CD    1 
ATOM   21250 O OE1   . GLU A 1 4259 ? 200.814 166.013 188.638 1.00 16.55  ? 4259 GLU A OE1   1 
ATOM   21251 O OE2   . GLU A 1 4259 ? 202.800 166.718 188.023 1.00 16.55  ? 4259 GLU A OE2   1 
ATOM   21252 N N     . PHE A 1 4260 ? 199.555 163.797 186.134 1.00 15.93  ? 4260 PHE A N     1 
ATOM   21253 C CA    . PHE A 1 4260 ? 200.135 162.608 186.753 1.00 15.93  ? 4260 PHE A CA    1 
ATOM   21254 C C     . PHE A 1 4260 ? 200.773 161.675 185.730 1.00 15.93  ? 4260 PHE A C     1 
ATOM   21255 O O     . PHE A 1 4260 ? 201.825 161.086 186.006 1.00 15.93  ? 4260 PHE A O     1 
ATOM   21256 C CB    . PHE A 1 4260 ? 199.070 161.891 187.575 1.00 15.93  ? 4260 PHE A CB    1 
ATOM   21257 C CG    . PHE A 1 4260 ? 198.524 162.730 188.689 1.00 15.93  ? 4260 PHE A CG    1 
ATOM   21258 C CD1   . PHE A 1 4260 ? 199.241 162.896 189.859 1.00 15.93  ? 4260 PHE A CD1   1 
ATOM   21259 C CD2   . PHE A 1 4260 ? 197.313 163.382 188.554 1.00 15.93  ? 4260 PHE A CD2   1 
ATOM   21260 C CE1   . PHE A 1 4260 ? 198.753 163.679 190.881 1.00 15.93  ? 4260 PHE A CE1   1 
ATOM   21261 C CE2   . PHE A 1 4260 ? 196.821 164.167 189.573 1.00 15.93  ? 4260 PHE A CE2   1 
ATOM   21262 C CZ    . PHE A 1 4260 ? 197.541 164.315 190.738 1.00 15.93  ? 4260 PHE A CZ    1 
ATOM   21263 N N     . ASP A 1 4261 ? 200.173 161.531 184.547 1.00 16.64  ? 4261 ASP A N     1 
ATOM   21264 C CA    . ASP A 1 4261 ? 200.849 160.792 183.486 1.00 16.64  ? 4261 ASP A CA    1 
ATOM   21265 C C     . ASP A 1 4261 ? 202.123 161.495 183.040 1.00 16.64  ? 4261 ASP A C     1 
ATOM   21266 O O     . ASP A 1 4261 ? 203.113 160.829 182.722 1.00 16.64  ? 4261 ASP A O     1 
ATOM   21267 C CB    . ASP A 1 4261 ? 199.919 160.588 182.293 1.00 16.64  ? 4261 ASP A CB    1 
ATOM   21268 C CG    . ASP A 1 4261 ? 198.766 159.663 182.609 1.00 16.64  ? 4261 ASP A CG    1 
ATOM   21269 O OD1   . ASP A 1 4261 ? 198.817 158.987 183.658 1.00 16.64  ? 4261 ASP A OD1   1 
ATOM   21270 O OD2   . ASP A 1 4261 ? 197.807 159.612 181.812 1.00 16.64  ? 4261 ASP A OD2   1 
ATOM   21271 N N     . GLN A 1 4262 ? 202.119 162.829 183.010 1.00 17.33  ? 4262 GLN A N     1 
ATOM   21272 C CA    . GLN A 1 4262 ? 203.343 163.562 182.707 1.00 17.33  ? 4262 GLN A CA    1 
ATOM   21273 C C     . GLN A 1 4262 ? 204.403 163.319 183.774 1.00 17.33  ? 4262 GLN A C     1 
ATOM   21274 O O     . GLN A 1 4262 ? 205.591 163.186 183.460 1.00 17.33  ? 4262 GLN A O     1 
ATOM   21275 C CB    . GLN A 1 4262 ? 203.042 165.053 182.575 1.00 17.33  ? 4262 GLN A CB    1 
ATOM   21276 C CG    . GLN A 1 4262 ? 204.237 165.892 182.167 1.00 17.33  ? 4262 GLN A CG    1 
ATOM   21277 C CD    . GLN A 1 4262 ? 204.629 165.678 180.721 1.00 17.33  ? 4262 GLN A CD    1 
ATOM   21278 O OE1   . GLN A 1 4262 ? 203.825 165.879 179.813 1.00 17.33  ? 4262 GLN A OE1   1 
ATOM   21279 N NE2   . GLN A 1 4262 ? 205.871 165.268 180.499 1.00 17.33  ? 4262 GLN A NE2   1 
ATOM   21280 N N     . ARG A 1 4263 ? 203.992 163.261 185.042 1.00 16.38  ? 4263 ARG A N     1 
ATOM   21281 C CA    . ARG A 1 4263 ? 204.927 162.951 186.119 1.00 16.38  ? 4263 ARG A CA    1 
ATOM   21282 C C     . ARG A 1 4263 ? 205.511 161.554 185.954 1.00 16.38  ? 4263 ARG A C     1 
ATOM   21283 O O     . ARG A 1 4263 ? 206.714 161.346 186.149 1.00 16.38  ? 4263 ARG A O     1 
ATOM   21284 C CB    . ARG A 1 4263 ? 204.222 163.085 187.468 1.00 16.38  ? 4263 ARG A CB    1 
ATOM   21285 C CG    . ARG A 1 4263 ? 205.094 162.794 188.672 1.00 16.38  ? 4263 ARG A CG    1 
ATOM   21286 C CD    . ARG A 1 4263 ? 204.296 162.911 189.962 1.00 16.38  ? 4263 ARG A CD    1 
ATOM   21287 N NE    . ARG A 1 4263 ? 203.278 161.874 190.075 1.00 16.38  ? 4263 ARG A NE    1 
ATOM   21288 C CZ    . ARG A 1 4263 ? 202.346 161.839 191.018 1.00 16.38  ? 4263 ARG A CZ    1 
ATOM   21289 N NH1   . ARG A 1 4263 ? 202.266 162.779 191.945 1.00 16.38  ? 4263 ARG A NH1   1 
ATOM   21290 N NH2   . ARG A 1 4263 ? 201.474 160.836 191.031 1.00 16.38  ? 4263 ARG A NH2   1 
ATOM   21291 N N     . LEU A 1 4264 ? 204.670 160.586 185.594 1.00 14.50  ? 4264 LEU A N     1 
ATOM   21292 C CA    . LEU A 1 4264 ? 205.147 159.225 185.362 1.00 14.50  ? 4264 LEU A CA    1 
ATOM   21293 C C     . LEU A 1 4264 ? 206.125 159.170 184.192 1.00 14.50  ? 4264 LEU A C     1 
ATOM   21294 O O     . LEU A 1 4264 ? 207.158 158.488 184.261 1.00 14.50  ? 4264 LEU A O     1 
ATOM   21295 C CB    . LEU A 1 4264 ? 203.948 158.308 185.125 1.00 14.50  ? 4264 LEU A CB    1 
ATOM   21296 C CG    . LEU A 1 4264 ? 204.125 156.814 184.886 1.00 14.50  ? 4264 LEU A CG    1 
ATOM   21297 C CD1   . LEU A 1 4264 ? 202.948 156.086 185.491 1.00 14.50  ? 4264 LEU A CD1   1 
ATOM   21298 C CD2   . LEU A 1 4264 ? 204.195 156.530 183.404 1.00 14.50  ? 4264 LEU A CD2   1 
ATOM   21299 N N     . LEU A 1 4265 ? 205.813 159.881 183.108 1.00 34.96  ? 4265 LEU A N     1 
ATOM   21300 C CA    . LEU A 1 4265 ? 206.705 159.921 181.954 1.00 34.96  ? 4265 LEU A CA    1 
ATOM   21301 C C     . LEU A 1 4265 ? 208.038 160.563 182.313 1.00 34.96  ? 4265 LEU A C     1 
ATOM   21302 O O     . LEU A 1 4265 ? 209.099 160.092 181.886 1.00 34.96  ? 4265 LEU A O     1 
ATOM   21303 C CB    . LEU A 1 4265 ? 206.035 160.675 180.809 1.00 34.96  ? 4265 LEU A CB    1 
ATOM   21304 C CG    . LEU A 1 4265 ? 206.704 160.616 179.439 1.00 34.96  ? 4265 LEU A CG    1 
ATOM   21305 C CD1   . LEU A 1 4265 ? 206.416 159.290 178.768 1.00 34.96  ? 4265 LEU A CD1   1 
ATOM   21306 C CD2   . LEU A 1 4265 ? 206.223 161.766 178.580 1.00 34.96  ? 4265 LEU A CD2   1 
ATOM   21307 N N     . ASN A 1 4266 ? 208.003 161.644 183.095 1.00 20.27  ? 4266 ASN A N     1 
ATOM   21308 C CA    . ASN A 1 4266 ? 209.236 162.273 183.552 1.00 20.27  ? 4266 ASN A CA    1 
ATOM   21309 C C     . ASN A 1 4266 ? 210.040 161.328 184.431 1.00 20.27  ? 4266 ASN A C     1 
ATOM   21310 O O     . ASN A 1 4266 ? 211.273 161.298 184.353 1.00 20.27  ? 4266 ASN A O     1 
ATOM   21311 C CB    . ASN A 1 4266 ? 208.918 163.564 184.303 1.00 20.27  ? 4266 ASN A CB    1 
ATOM   21312 C CG    . ASN A 1 4266 ? 208.707 164.739 183.375 1.00 20.27  ? 4266 ASN A CG    1 
ATOM   21313 O OD1   . ASN A 1 4266 ? 207.617 165.305 183.309 1.00 20.27  ? 4266 ASN A OD1   1 
ATOM   21314 N ND2   . ASN A 1 4266 ? 209.754 165.115 182.652 1.00 20.27  ? 4266 ASN A ND2   1 
ATOM   21315 N N     . THR A 1 4267 ? 209.361 160.554 185.280 1.00 16.53  ? 4267 THR A N     1 
ATOM   21316 C CA    . THR A 1 4267 ? 210.053 159.572 186.107 1.00 16.53  ? 4267 THR A CA    1 
ATOM   21317 C C     . THR A 1 4267 ? 210.778 158.547 185.243 1.00 16.53  ? 4267 THR A C     1 
ATOM   21318 O O     . THR A 1 4267 ? 211.962 158.261 185.458 1.00 16.53  ? 4267 THR A O     1 
ATOM   21319 C CB    . THR A 1 4267 ? 209.059 158.881 187.040 1.00 16.53  ? 4267 THR A CB    1 
ATOM   21320 O OG1   . THR A 1 4267 ? 208.635 159.800 188.054 1.00 16.53  ? 4267 THR A OG1   1 
ATOM   21321 C CG2   . THR A 1 4267 ? 209.697 157.669 187.696 1.00 16.53  ? 4267 THR A CG2   1 
ATOM   21322 N N     . PHE A 1 4268 ? 210.082 157.999 184.244 1.00 13.07  ? 4268 PHE A N     1 
ATOM   21323 C CA    . PHE A 1 4268 ? 210.719 157.027 183.357 1.00 13.07  ? 4268 PHE A CA    1 
ATOM   21324 C C     . PHE A 1 4268 ? 211.899 157.639 182.613 1.00 13.07  ? 4268 PHE A C     1 
ATOM   21325 O O     . PHE A 1 4268 ? 212.961 157.014 182.498 1.00 13.07  ? 4268 PHE A O     1 
ATOM   21326 C CB    . PHE A 1 4268 ? 209.707 156.463 182.362 1.00 13.07  ? 4268 PHE A CB    1 
ATOM   21327 C CG    . PHE A 1 4268 ? 208.929 155.297 182.887 1.00 13.07  ? 4268 PHE A CG    1 
ATOM   21328 C CD1   . PHE A 1 4268 ? 209.542 154.070 183.062 1.00 13.07  ? 4268 PHE A CD1   1 
ATOM   21329 C CD2   . PHE A 1 4268 ? 207.588 155.420 183.195 1.00 13.07  ? 4268 PHE A CD2   1 
ATOM   21330 C CE1   . PHE A 1 4268 ? 208.836 152.991 183.543 1.00 13.07  ? 4268 PHE A CE1   1 
ATOM   21331 C CE2   . PHE A 1 4268 ? 206.877 154.343 183.676 1.00 13.07  ? 4268 PHE A CE2   1 
ATOM   21332 C CZ    . PHE A 1 4268 ? 207.501 153.128 183.849 1.00 13.07  ? 4268 PHE A CZ    1 
ATOM   21333 N N     . LEU A 1 4269 ? 211.733 158.858 182.099 1.00 11.71  ? 4269 LEU A N     1 
ATOM   21334 C CA    . LEU A 1 4269 ? 212.803 159.484 181.331 1.00 11.71  ? 4269 LEU A CA    1 
ATOM   21335 C C     . LEU A 1 4269 ? 214.020 159.775 182.199 1.00 11.71  ? 4269 LEU A C     1 
ATOM   21336 O O     . LEU A 1 4269 ? 215.158 159.544 181.776 1.00 11.71  ? 4269 LEU A O     1 
ATOM   21337 C CB    . LEU A 1 4269 ? 212.294 160.761 180.672 1.00 11.71  ? 4269 LEU A CB    1 
ATOM   21338 C CG    . LEU A 1 4269 ? 211.465 160.526 179.414 1.00 11.71  ? 4269 LEU A CG    1 
ATOM   21339 C CD1   . LEU A 1 4269 ? 211.018 161.844 178.845 1.00 11.71  ? 4269 LEU A CD1   1 
ATOM   21340 C CD2   . LEU A 1 4269 ? 212.264 159.745 178.391 1.00 11.71  ? 4269 LEU A CD2   1 
ATOM   21341 N N     . GLU A 1 4270 ? 213.806 160.283 183.414 1.00 15.17  ? 4270 GLU A N     1 
ATOM   21342 C CA    . GLU A 1 4270 ? 214.934 160.579 184.288 1.00 15.17  ? 4270 GLU A CA    1 
ATOM   21343 C C     . GLU A 1 4270 ? 215.585 159.306 184.810 1.00 15.17  ? 4270 GLU A C     1 
ATOM   21344 O O     . GLU A 1 4270 ? 216.772 159.318 185.152 1.00 15.17  ? 4270 GLU A O     1 
ATOM   21345 C CB    . GLU A 1 4270 ? 214.485 161.473 185.445 1.00 15.17  ? 4270 GLU A CB    1 
ATOM   21346 C CG    . GLU A 1 4270 ? 214.041 160.727 186.692 1.00 15.17  ? 4270 GLU A CG    1 
ATOM   21347 C CD    . GLU A 1 4270 ? 213.480 161.652 187.754 1.00 15.17  ? 4270 GLU A CD    1 
ATOM   21348 O OE1   . GLU A 1 4270 ? 213.076 161.154 188.826 1.00 15.17  ? 4270 GLU A OE1   1 
ATOM   21349 O OE2   . GLU A 1 4270 ? 213.440 162.877 187.516 1.00 15.17  ? 4270 GLU A OE2   1 
ATOM   21350 N N     . ARG A 1 4271 ? 214.835 158.203 184.881 1.00 14.73  ? 4271 ARG A N     1 
ATOM   21351 C CA    . ARG A 1 4271 ? 215.443 156.940 185.286 1.00 14.73  ? 4271 ARG A CA    1 
ATOM   21352 C C     . ARG A 1 4271 ? 216.287 156.347 184.166 1.00 14.73  ? 4271 ARG A C     1 
ATOM   21353 O O     . ARG A 1 4271 ? 217.393 155.852 184.412 1.00 14.73  ? 4271 ARG A O     1 
ATOM   21354 C CB    . ARG A 1 4271 ? 214.362 155.953 185.720 1.00 14.73  ? 4271 ARG A CB    1 
ATOM   21355 C CG    . ARG A 1 4271 ? 214.901 154.735 186.445 1.00 14.73  ? 4271 ARG A CG    1 
ATOM   21356 C CD    . ARG A 1 4271 ? 213.786 153.772 186.808 1.00 14.73  ? 4271 ARG A CD    1 
ATOM   21357 N NE    . ARG A 1 4271 ? 213.441 152.897 185.695 1.00 14.73  ? 4271 ARG A NE    1 
ATOM   21358 C CZ    . ARG A 1 4271 ? 212.205 152.525 185.390 1.00 14.73  ? 4271 ARG A CZ    1 
ATOM   21359 N NH1   . ARG A 1 4271 ? 211.166 152.937 186.097 1.00 14.73  ? 4271 ARG A NH1   1 
ATOM   21360 N NH2   . ARG A 1 4271 ? 212.008 151.720 184.351 1.00 14.73  ? 4271 ARG A NH2   1 
ATOM   21361 N N     . LEU A 1 4272 ? 215.787 156.387 182.930 1.00 14.29  ? 4272 LEU A N     1 
ATOM   21362 C CA    . LEU A 1 4272 ? 216.497 155.752 181.823 1.00 14.29  ? 4272 LEU A CA    1 
ATOM   21363 C C     . LEU A 1 4272 ? 217.584 156.658 181.254 1.00 14.29  ? 4272 LEU A C     1 
ATOM   21364 O O     . LEU A 1 4272 ? 218.769 156.314 181.276 1.00 14.29  ? 4272 LEU A O     1 
ATOM   21365 C CB    . LEU A 1 4272 ? 215.507 155.347 180.728 1.00 14.29  ? 4272 LEU A CB    1 
ATOM   21366 C CG    . LEU A 1 4272 ? 214.676 154.096 181.008 1.00 14.29  ? 4272 LEU A CG    1 
ATOM   21367 C CD1   . LEU A 1 4272 ? 213.593 153.930 179.960 1.00 14.29  ? 4272 LEU A CD1   1 
ATOM   21368 C CD2   . LEU A 1 4272 ? 215.569 152.872 181.054 1.00 14.29  ? 4272 LEU A CD2   1 
ATOM   21369 N N     . PHE A 1 4273 ? 217.196 157.825 180.739 1.00 11.52  ? 4273 PHE A N     1 
ATOM   21370 C CA    . PHE A 1 4273 ? 218.125 158.710 180.037 1.00 11.52  ? 4273 PHE A CA    1 
ATOM   21371 C C     . PHE A 1 4273 ? 218.969 159.467 181.057 1.00 11.52  ? 4273 PHE A C     1 
ATOM   21372 O O     . PHE A 1 4273 ? 218.669 160.594 181.459 1.00 11.52  ? 4273 PHE A O     1 
ATOM   21373 C CB    . PHE A 1 4273 ? 217.369 159.658 179.116 1.00 11.52  ? 4273 PHE A CB    1 
ATOM   21374 C CG    . PHE A 1 4273 ? 216.812 158.993 177.894 1.00 11.52  ? 4273 PHE A CG    1 
ATOM   21375 C CD1   . PHE A 1 4273 ? 215.579 158.369 177.931 1.00 11.52  ? 4273 PHE A CD1   1 
ATOM   21376 C CD2   . PHE A 1 4273 ? 217.526 158.985 176.709 1.00 11.52  ? 4273 PHE A CD2   1 
ATOM   21377 C CE1   . PHE A 1 4273 ? 215.067 157.754 176.808 1.00 11.52  ? 4273 PHE A CE1   1 
ATOM   21378 C CE2   . PHE A 1 4273 ? 217.019 158.372 175.584 1.00 11.52  ? 4273 PHE A CE2   1 
ATOM   21379 C CZ    . PHE A 1 4273 ? 215.788 157.756 175.634 1.00 11.52  ? 4273 PHE A CZ    1 
ATOM   21380 N N     . THR A 1 4274 ? 220.055 158.825 181.477 1.00 16.96  ? 4274 THR A N     1 
ATOM   21381 C CA    . THR A 1 4274 ? 221.015 159.443 182.378 1.00 16.96  ? 4274 THR A CA    1 
ATOM   21382 C C     . THR A 1 4274 ? 222.389 158.854 182.100 1.00 16.96  ? 4274 THR A C     1 
ATOM   21383 O O     . THR A 1 4274 ? 222.518 157.796 181.480 1.00 16.96  ? 4274 THR A O     1 
ATOM   21384 C CB    . THR A 1 4274 ? 220.630 159.246 183.848 1.00 16.96  ? 4274 THR A CB    1 
ATOM   21385 O OG1   . THR A 1 4274 ? 221.481 160.047 184.677 1.00 16.96  ? 4274 THR A OG1   1 
ATOM   21386 C CG2   . THR A 1 4274 ? 220.778 157.788 184.246 1.00 16.96  ? 4274 THR A CG2   1 
ATOM   21387 N N     . THR A 1 4275 ? 223.422 159.559 182.566 1.00 20.13  ? 4275 THR A N     1 
ATOM   21388 C CA    . THR A 1 4275 ? 224.791 159.121 182.319 1.00 20.13  ? 4275 THR A CA    1 
ATOM   21389 C C     . THR A 1 4275 ? 225.107 157.793 182.993 1.00 20.13  ? 4275 THR A C     1 
ATOM   21390 O O     . THR A 1 4275 ? 226.082 157.135 182.612 1.00 20.13  ? 4275 THR A O     1 
ATOM   21391 C CB    . THR A 1 4275 ? 225.782 160.190 182.786 1.00 20.13  ? 4275 THR A CB    1 
ATOM   21392 O OG1   . THR A 1 4275 ? 227.110 159.811 182.405 1.00 20.13  ? 4275 THR A OG1   1 
ATOM   21393 C CG2   . THR A 1 4275 ? 225.719 160.354 184.297 1.00 20.13  ? 4275 THR A CG2   1 
ATOM   21394 N N     . ARG A 1 4276 ? 224.313 157.384 183.984 1.00 26.50  ? 4276 ARG A N     1 
ATOM   21395 C CA    . ARG A 1 4276 ? 224.524 156.092 184.624 1.00 26.50  ? 4276 ARG A CA    1 
ATOM   21396 C C     . ARG A 1 4276 ? 224.175 154.929 183.706 1.00 26.50  ? 4276 ARG A C     1 
ATOM   21397 O O     . ARG A 1 4276 ? 224.575 153.794 183.986 1.00 26.50  ? 4276 ARG A O     1 
ATOM   21398 C CB    . ARG A 1 4276 ? 223.701 155.999 185.910 1.00 26.50  ? 4276 ARG A CB    1 
ATOM   21399 C CG    . ARG A 1 4276 ? 224.138 156.964 186.997 1.00 26.50  ? 4276 ARG A CG    1 
ATOM   21400 C CD    . ARG A 1 4276 ? 225.370 156.455 187.724 1.00 26.50  ? 4276 ARG A CD    1 
ATOM   21401 N NE    . ARG A 1 4276 ? 226.549 157.261 187.429 1.00 26.50  ? 4276 ARG A NE    1 
ATOM   21402 C CZ    . ARG A 1 4276 ? 227.757 157.030 187.923 1.00 26.50  ? 4276 ARG A CZ    1 
ATOM   21403 N NH1   . ARG A 1 4276 ? 227.987 156.018 188.743 1.00 26.50  ? 4276 ARG A NH1   1 
ATOM   21404 N NH2   . ARG A 1 4276 ? 228.761 157.834 187.584 1.00 26.50  ? 4276 ARG A NH2   1 
ATOM   21405 N N     . SER A 1 4277 ? 223.439 155.183 182.622 1.00 25.05  ? 4277 SER A N     1 
ATOM   21406 C CA    . SER A 1 4277 ? 223.028 154.111 181.724 1.00 25.05  ? 4277 SER A CA    1 
ATOM   21407 C C     . SER A 1 4277 ? 224.200 153.488 180.979 1.00 25.05  ? 4277 SER A C     1 
ATOM   21408 O O     . SER A 1 4277 ? 224.081 152.355 180.502 1.00 25.05  ? 4277 SER A O     1 
ATOM   21409 C CB    . SER A 1 4277 ? 222.002 154.631 180.718 1.00 25.05  ? 4277 SER A CB    1 
ATOM   21410 O OG    . SER A 1 4277 ? 220.842 155.109 181.374 1.00 25.05  ? 4277 SER A OG    1 
ATOM   21411 N N     . PHE A 1 4278 ? 225.320 154.194 180.866 1.00 23.29  ? 4278 PHE A N     1 
ATOM   21412 C CA    . PHE A 1 4278 ? 226.475 153.692 180.136 1.00 23.29  ? 4278 PHE A CA    1 
ATOM   21413 C C     . PHE A 1 4278 ? 227.418 152.874 181.004 1.00 23.29  ? 4278 PHE A C     1 
ATOM   21414 O O     . PHE A 1 4278 ? 228.460 152.428 180.513 1.00 23.29  ? 4278 PHE A O     1 
ATOM   21415 C CB    . PHE A 1 4278 ? 227.235 154.854 179.495 1.00 23.29  ? 4278 PHE A CB    1 
ATOM   21416 C CG    . PHE A 1 4278 ? 226.658 155.296 178.185 1.00 23.29  ? 4278 PHE A CG    1 
ATOM   21417 C CD1   . PHE A 1 4278 ? 225.486 156.029 178.142 1.00 23.29  ? 4278 PHE A CD1   1 
ATOM   21418 C CD2   . PHE A 1 4278 ? 227.281 154.968 176.996 1.00 23.29  ? 4278 PHE A CD2   1 
ATOM   21419 C CE1   . PHE A 1 4278 ? 224.952 156.431 176.936 1.00 23.29  ? 4278 PHE A CE1   1 
ATOM   21420 C CE2   . PHE A 1 4278 ? 226.749 155.366 175.791 1.00 23.29  ? 4278 PHE A CE2   1 
ATOM   21421 C CZ    . PHE A 1 4278 ? 225.584 156.100 175.760 1.00 23.29  ? 4278 PHE A CZ    1 
ATOM   21422 N N     . ASP A 1 4279 ? 227.085 152.667 182.272 1.00 31.50  ? 4279 ASP A N     1 
ATOM   21423 C CA    . ASP A 1 4279 ? 227.867 151.823 183.159 1.00 31.50  ? 4279 ASP A CA    1 
ATOM   21424 C C     . ASP A 1 4279 ? 227.370 150.385 183.083 1.00 31.50  ? 4279 ASP A C     1 
ATOM   21425 O O     . ASP A 1 4279 ? 226.254 150.110 182.637 1.00 31.50  ? 4279 ASP A O     1 
ATOM   21426 C CB    . ASP A 1 4279 ? 227.794 152.335 184.600 1.00 31.50  ? 4279 ASP A CB    1 
ATOM   21427 C CG    . ASP A 1 4279 ? 228.470 153.680 184.774 1.00 31.50  ? 4279 ASP A CG    1 
ATOM   21428 O OD1   . ASP A 1 4279 ? 229.403 153.982 184.001 1.00 31.50  ? 4279 ASP A OD1   1 
ATOM   21429 O OD2   . ASP A 1 4279 ? 228.070 154.434 185.685 1.00 31.50  ? 4279 ASP A OD2   1 
ATOM   21430 N N     . SER A 1 4280 ? 228.223 149.460 183.523 1.00 34.28  ? 4280 SER A N     1 
ATOM   21431 C CA    . SER A 1 4280 ? 227.876 148.046 183.482 1.00 34.28  ? 4280 SER A CA    1 
ATOM   21432 C C     . SER A 1 4280 ? 226.919 147.637 184.593 1.00 34.28  ? 4280 SER A C     1 
ATOM   21433 O O     . SER A 1 4280 ? 226.342 146.547 184.519 1.00 34.28  ? 4280 SER A O     1 
ATOM   21434 C CB    . SER A 1 4280 ? 229.144 147.195 183.558 1.00 34.28  ? 4280 SER A CB    1 
ATOM   21435 O OG    . SER A 1 4280 ? 229.870 147.473 184.742 1.00 34.28  ? 4280 SER A OG    1 
ATOM   21436 N N     . GLU A 1 4281 ? 226.734 148.477 185.610 1.00 36.65  ? 4281 GLU A N     1 
ATOM   21437 C CA    . GLU A 1 4281 ? 225.881 148.160 186.747 1.00 36.65  ? 4281 GLU A CA    1 
ATOM   21438 C C     . GLU A 1 4281 ? 224.469 148.714 186.602 1.00 36.65  ? 4281 GLU A C     1 
ATOM   21439 O O     . GLU A 1 4281 ? 223.679 148.613 187.546 1.00 36.65  ? 4281 GLU A O     1 
ATOM   21440 C CB    . GLU A 1 4281 ? 226.500 148.678 188.052 1.00 36.65  ? 4281 GLU A CB    1 
ATOM   21441 C CG    . GLU A 1 4281 ? 227.781 147.975 188.535 1.00 36.65  ? 4281 GLU A CG    1 
ATOM   21442 C CD    . GLU A 1 4281 ? 228.996 148.165 187.633 1.00 36.65  ? 4281 GLU A CD    1 
ATOM   21443 O OE1   . GLU A 1 4281 ? 230.107 147.787 188.065 1.00 36.65  ? 4281 GLU A OE1   1 
ATOM   21444 O OE2   . GLU A 1 4281 ? 228.868 148.723 186.526 1.00 36.65  ? 4281 GLU A OE2   1 
ATOM   21445 N N     . PHE A 1 4282 ? 224.136 149.307 185.459 1.00 27.31  ? 4282 PHE A N     1 
ATOM   21446 C CA    . PHE A 1 4282 ? 222.814 149.893 185.287 1.00 27.31  ? 4282 PHE A CA    1 
ATOM   21447 C C     . PHE A 1 4282 ? 221.741 148.813 185.264 1.00 27.31  ? 4282 PHE A C     1 
ATOM   21448 O O     . PHE A 1 4282 ? 221.924 147.741 184.681 1.00 27.31  ? 4282 PHE A O     1 
ATOM   21449 C CB    . PHE A 1 4282 ? 222.753 150.712 184.001 1.00 27.31  ? 4282 PHE A CB    1 
ATOM   21450 C CG    . PHE A 1 4282 ? 221.542 151.591 183.905 1.00 27.31  ? 4282 PHE A CG    1 
ATOM   21451 C CD1   . PHE A 1 4282 ? 221.177 152.406 184.963 1.00 27.31  ? 4282 PHE A CD1   1 
ATOM   21452 C CD2   . PHE A 1 4282 ? 220.761 151.595 182.764 1.00 27.31  ? 4282 PHE A CD2   1 
ATOM   21453 C CE1   . PHE A 1 4282 ? 220.062 153.213 184.881 1.00 27.31  ? 4282 PHE A CE1   1 
ATOM   21454 C CE2   . PHE A 1 4282 ? 219.645 152.400 182.676 1.00 27.31  ? 4282 PHE A CE2   1 
ATOM   21455 C CZ    . PHE A 1 4282 ? 219.294 153.210 183.736 1.00 27.31  ? 4282 PHE A CZ    1 
ATOM   21456 N N     . LYS A 1 4283 ? 220.613 149.102 185.908 1.00 27.69  ? 4283 LYS A N     1 
ATOM   21457 C CA    . LYS A 1 4283 ? 219.483 148.183 185.989 1.00 27.69  ? 4283 LYS A CA    1 
ATOM   21458 C C     . LYS A 1 4283 ? 218.306 148.807 185.251 1.00 27.69  ? 4283 LYS A C     1 
ATOM   21459 O O     . LYS A 1 4283 ? 217.760 149.825 185.691 1.00 27.69  ? 4283 LYS A O     1 
ATOM   21460 C CB    . LYS A 1 4283 ? 219.123 147.889 187.444 1.00 27.69  ? 4283 LYS A CB    1 
ATOM   21461 C CG    . LYS A 1 4283 ? 220.313 147.877 188.386 1.00 27.69  ? 4283 LYS A CG    1 
ATOM   21462 C CD    . LYS A 1 4283 ? 221.218 146.687 188.129 1.00 27.69  ? 4283 LYS A CD    1 
ATOM   21463 C CE    . LYS A 1 4283 ? 220.582 145.399 188.608 1.00 27.69  ? 4283 LYS A CE    1 
ATOM   21464 N NZ    . LYS A 1 4283 ? 220.237 145.451 190.055 1.00 27.69  ? 4283 LYS A NZ    1 
ATOM   21465 N N     . LEU A 1 4284 ? 217.919 148.200 184.127 1.00 22.41  ? 4284 LEU A N     1 
ATOM   21466 C CA    . LEU A 1 4284 ? 216.778 148.707 183.372 1.00 22.41  ? 4284 LEU A CA    1 
ATOM   21467 C C     . LEU A 1 4284 ? 215.494 148.610 184.184 1.00 22.41  ? 4284 LEU A C     1 
ATOM   21468 O O     . LEU A 1 4284 ? 214.677 149.539 184.183 1.00 22.41  ? 4284 LEU A O     1 
ATOM   21469 C CB    . LEU A 1 4284 ? 216.640 147.945 182.055 1.00 22.41  ? 4284 LEU A CB    1 
ATOM   21470 C CG    . LEU A 1 4284 ? 217.758 148.169 181.038 1.00 22.41  ? 4284 LEU A CG    1 
ATOM   21471 C CD1   . LEU A 1 4284 ? 217.615 147.214 179.870 1.00 22.41  ? 4284 LEU A CD1   1 
ATOM   21472 C CD2   . LEU A 1 4284 ? 217.745 149.607 180.557 1.00 22.41  ? 4284 LEU A CD2   1 
ATOM   21473 N N     . ALA A 1 4285 ? 215.298 147.496 184.881 1.00 29.24  ? 4285 ALA A N     1 
ATOM   21474 C CA    . ALA A 1 4285 ? 214.137 147.307 185.736 1.00 29.24  ? 4285 ALA A CA    1 
ATOM   21475 C C     . ALA A 1 4285 ? 214.558 146.546 186.982 1.00 29.24  ? 4285 ALA A C     1 
ATOM   21476 O O     . ALA A 1 4285 ? 215.311 145.571 186.897 1.00 29.24  ? 4285 ALA A O     1 
ATOM   21477 C CB    . ALA A 1 4285 ? 213.019 146.557 185.007 1.00 29.24  ? 4285 ALA A CB    1 
ATOM   21478 N N     . CYS A 1 4286 ? 214.070 146.993 188.134 1.00 39.78  ? 4286 CYS A N     1 
ATOM   21479 C CA    . CYS A 1 4286 ? 214.409 146.398 189.416 1.00 39.78  ? 4286 CYS A CA    1 
ATOM   21480 C C     . CYS A 1 4286 ? 213.203 145.667 189.990 1.00 39.78  ? 4286 CYS A C     1 
ATOM   21481 O O     . CYS A 1 4286 ? 212.077 145.819 189.505 1.00 39.78  ? 4286 CYS A O     1 
ATOM   21482 C CB    . CYS A 1 4286 ? 214.889 147.463 190.407 1.00 39.78  ? 4286 CYS A CB    1 
ATOM   21483 S SG    . CYS A 1 4286 ? 216.442 148.263 189.951 1.00 39.78  ? 4286 CYS A SG    1 
ATOM   21484 N N     . LYS A 1 4287 ? 213.461 144.844 191.011 1.00 40.31  ? 4287 LYS A N     1 
ATOM   21485 C CA    . LYS A 1 4287 ? 212.416 144.149 191.770 1.00 40.31  ? 4287 LYS A CA    1 
ATOM   21486 C C     . LYS A 1 4287 ? 211.715 143.085 190.917 1.00 40.31  ? 4287 LYS A C     1 
ATOM   21487 O O     . LYS A 1 4287 ? 210.886 142.321 191.414 1.00 40.31  ? 4287 LYS A O     1 
ATOM   21488 C CB    . LYS A 1 4287 ? 211.441 145.178 192.382 1.00 40.31  ? 4287 LYS A CB    1 
ATOM   21489 C CG    . LYS A 1 4287 ? 210.182 144.707 193.142 1.00 40.31  ? 4287 LYS A CG    1 
ATOM   21490 C CD    . LYS A 1 4287 ? 209.004 144.345 192.241 1.00 40.31  ? 4287 LYS A CD    1 
ATOM   21491 C CE    . LYS A 1 4287 ? 207.899 143.659 193.025 1.00 40.31  ? 4287 LYS A CE    1 
ATOM   21492 N NZ    . LYS A 1 4287 ? 206.612 143.649 192.278 1.00 40.31  ? 4287 LYS A NZ    1 
ATOM   21493 N N     . VAL A 1 4288 ? 212.125 142.964 189.652 1.00 37.12  ? 4288 VAL A N     1 
ATOM   21494 C CA    . VAL A 1 4288 ? 211.470 142.067 188.704 1.00 37.12  ? 4288 VAL A CA    1 
ATOM   21495 C C     . VAL A 1 4288 ? 211.391 140.658 189.275 1.00 37.12  ? 4288 VAL A C     1 
ATOM   21496 O O     . VAL A 1 4288 ? 212.411 140.057 189.635 1.00 37.12  ? 4288 VAL A O     1 
ATOM   21497 C CB    . VAL A 1 4288 ? 212.218 142.071 187.364 1.00 37.12  ? 4288 VAL A CB    1 
ATOM   21498 C CG1   . VAL A 1 4288 ? 211.604 141.061 186.419 1.00 37.12  ? 4288 VAL A CG1   1 
ATOM   21499 C CG2   . VAL A 1 4288 ? 212.195 143.460 186.755 1.00 37.12  ? 4288 VAL A CG2   1 
ATOM   21500 N N     . ASP A 1 4289 ? 210.170 140.128 189.359 1.00 37.93  ? 4289 ASP A N     1 
ATOM   21501 C CA    . ASP A 1 4289 ? 209.916 138.797 189.913 1.00 37.93  ? 4289 ASP A CA    1 
ATOM   21502 C C     . ASP A 1 4289 ? 210.489 138.669 191.322 1.00 37.93  ? 4289 ASP A C     1 
ATOM   21503 O O     . ASP A 1 4289 ? 211.018 137.626 191.711 1.00 37.93  ? 4289 ASP A O     1 
ATOM   21504 C CB    . ASP A 1 4289 ? 210.465 137.702 188.997 1.00 37.93  ? 4289 ASP A CB    1 
ATOM   21505 N N     . GLY A 1 4290 ? 210.383 139.747 192.094 1.00 46.41  ? 4290 GLY A N     1 
ATOM   21506 C CA    . GLY A 1 4290 ? 210.835 139.737 193.471 1.00 46.41  ? 4290 GLY A CA    1 
ATOM   21507 C C     . GLY A 1 4290 ? 212.276 140.163 193.663 1.00 46.41  ? 4290 GLY A C     1 
ATOM   21508 O O     . GLY A 1 4290 ? 212.546 141.181 194.306 1.00 46.41  ? 4290 GLY A O     1 
ATOM   21509 N N     . HIS A 1 4291 ? 213.214 139.395 193.108 1.00 52.63  ? 4291 HIS A N     1 
ATOM   21510 C CA    . HIS A 1 4291 ? 214.629 139.643 193.353 1.00 52.63  ? 4291 HIS A CA    1 
ATOM   21511 C C     . HIS A 1 4291 ? 215.411 139.824 192.058 1.00 52.63  ? 4291 HIS A C     1 
ATOM   21512 O O     . HIS A 1 4291 ? 216.439 140.508 192.039 1.00 52.63  ? 4291 HIS A O     1 
ATOM   21513 C CB    . HIS A 1 4291 ? 215.227 138.499 194.174 1.00 52.63  ? 4291 HIS A CB    1 
ATOM   21514 C CG    . HIS A 1 4291 ? 214.671 138.397 195.560 1.00 52.63  ? 4291 HIS A CG    1 
ATOM   21515 N ND1   . HIS A 1 4291 ? 213.545 137.659 195.856 1.00 52.63  ? 4291 HIS A ND1   1 
ATOM   21516 C CD2   . HIS A 1 4291 ? 215.082 138.942 196.729 1.00 52.63  ? 4291 HIS A CD2   1 
ATOM   21517 C CE1   . HIS A 1 4291 ? 213.288 137.753 197.149 1.00 52.63  ? 4291 HIS A CE1   1 
ATOM   21518 N NE2   . HIS A 1 4291 ? 214.206 138.526 197.701 1.00 52.63  ? 4291 HIS A NE2   1 
ATOM   21519 N N     . LYS A 1 4292 ? 214.940 139.212 190.975 1.00 46.87  ? 4292 LYS A N     1 
ATOM   21520 C CA    . LYS A 1 4292 ? 215.634 139.305 189.700 1.00 46.87  ? 4292 LYS A CA    1 
ATOM   21521 C C     . LYS A 1 4292 ? 215.605 140.735 189.170 1.00 46.87  ? 4292 LYS A C     1 
ATOM   21522 O O     . LYS A 1 4292 ? 214.692 141.512 189.457 1.00 46.87  ? 4292 LYS A O     1 
ATOM   21523 C CB    . LYS A 1 4292 ? 215.004 138.355 188.681 1.00 46.87  ? 4292 LYS A CB    1 
ATOM   21524 C CG    . LYS A 1 4292 ? 215.074 136.891 189.078 1.00 46.87  ? 4292 LYS A CG    1 
ATOM   21525 C CD    . LYS A 1 4292 ? 216.512 136.414 189.182 1.00 46.87  ? 4292 LYS A CD    1 
ATOM   21526 C CE    . LYS A 1 4292 ? 217.186 136.398 187.821 1.00 46.87  ? 4292 LYS A CE    1 
ATOM   21527 N NZ    . LYS A 1 4292 ? 216.545 135.418 186.902 1.00 46.87  ? 4292 LYS A NZ    1 
ATOM   21528 N N     . ASP A 1 4293 ? 216.629 141.081 188.394 1.00 39.08  ? 4293 ASP A N     1 
ATOM   21529 C CA    . ASP A 1 4293 ? 216.755 142.413 187.822 1.00 39.08  ? 4293 ASP A CA    1 
ATOM   21530 C C     . ASP A 1 4293 ? 217.124 142.302 186.352 1.00 39.08  ? 4293 ASP A C     1 
ATOM   21531 O O     . ASP A 1 4293 ? 217.839 141.379 185.953 1.00 39.08  ? 4293 ASP A O     1 
ATOM   21532 C CB    . ASP A 1 4293 ? 217.813 143.240 188.559 1.00 39.08  ? 4293 ASP A CB    1 
ATOM   21533 C CG    . ASP A 1 4293 ? 217.395 143.602 189.969 1.00 39.08  ? 4293 ASP A CG    1 
ATOM   21534 O OD1   . ASP A 1 4293 ? 216.179 143.733 190.217 1.00 39.08  ? 4293 ASP A OD1   1 
ATOM   21535 O OD2   . ASP A 1 4293 ? 218.285 143.759 190.830 1.00 39.08  ? 4293 ASP A OD2   1 
ATOM   21536 N N     . ILE A 1 4294 ? 216.632 143.245 185.551 1.00 29.16  ? 4294 ILE A N     1 
ATOM   21537 C CA    . ILE A 1 4294 ? 216.970 143.301 184.133 1.00 29.16  ? 4294 ILE A CA    1 
ATOM   21538 C C     . ILE A 1 4294 ? 218.246 144.112 183.969 1.00 29.16  ? 4294 ILE A C     1 
ATOM   21539 O O     . ILE A 1 4294 ? 218.206 145.344 183.878 1.00 29.16  ? 4294 ILE A O     1 
ATOM   21540 C CB    . ILE A 1 4294 ? 215.821 143.899 183.303 1.00 29.16  ? 4294 ILE A CB    1 
ATOM   21541 C CG1   . ILE A 1 4294 ? 214.500 143.213 183.649 1.00 29.16  ? 4294 ILE A CG1   1 
ATOM   21542 C CG2   . ILE A 1 4294 ? 216.110 143.759 181.820 1.00 29.16  ? 4294 ILE A CG2   1 
ATOM   21543 C CD1   . ILE A 1 4294 ? 214.473 141.745 183.300 1.00 29.16  ? 4294 ILE A CD1   1 
ATOM   21544 N N     . GLN A 1 4295 ? 219.385 143.428 183.932 1.00 28.59  ? 4295 GLN A N     1 
ATOM   21545 C CA    . GLN A 1 4295 ? 220.669 144.111 183.866 1.00 28.59  ? 4295 GLN A CA    1 
ATOM   21546 C C     . GLN A 1 4295 ? 220.890 144.714 182.484 1.00 28.59  ? 4295 GLN A C     1 
ATOM   21547 O O     . GLN A 1 4295 ? 220.515 144.128 181.465 1.00 28.59  ? 4295 GLN A O     1 
ATOM   21548 C CB    . GLN A 1 4295 ? 221.799 143.141 184.205 1.00 28.59  ? 4295 GLN A CB    1 
ATOM   21549 C CG    . GLN A 1 4295 ? 223.149 143.804 184.412 1.00 28.59  ? 4295 GLN A CG    1 
ATOM   21550 C CD    . GLN A 1 4295 ? 223.394 144.172 185.861 1.00 28.59  ? 4295 GLN A CD    1 
ATOM   21551 O OE1   . GLN A 1 4295 ? 222.689 143.712 186.758 1.00 28.59  ? 4295 GLN A OE1   1 
ATOM   21552 N NE2   . GLN A 1 4295 ? 224.398 145.010 186.096 1.00 28.59  ? 4295 GLN A NE2   1 
ATOM   21553 N N     . MET A 1 4296 ? 221.497 145.892 182.456 1.00 26.86  ? 4296 MET A N     1 
ATOM   21554 C CA    . MET A 1 4296 ? 221.807 146.546 181.191 1.00 26.86  ? 4296 MET A CA    1 
ATOM   21555 C C     . MET A 1 4296 ? 222.877 145.755 180.446 1.00 26.86  ? 4296 MET A C     1 
ATOM   21556 O O     . MET A 1 4296 ? 223.882 145.363 181.051 1.00 26.86  ? 4296 MET A O     1 
ATOM   21557 C CB    . MET A 1 4296 ? 222.282 147.977 181.435 1.00 26.86  ? 4296 MET A CB    1 
ATOM   21558 C CG    . MET A 1 4296 ? 222.602 148.755 180.172 1.00 26.86  ? 4296 MET A CG    1 
ATOM   21559 S SD    . MET A 1 4296 ? 221.215 149.761 179.617 1.00 26.86  ? 4296 MET A SD    1 
ATOM   21560 C CE    . MET A 1 4296 ? 221.933 150.575 178.195 1.00 26.86  ? 4296 MET A CE    1 
ATOM   21561 N N     . PRO A 1 4297 ? 222.702 145.495 179.153 1.00 25.98  ? 4297 PRO A N     1 
ATOM   21562 C CA    . PRO A 1 4297 ? 223.729 144.764 178.406 1.00 25.98  ? 4297 PRO A CA    1 
ATOM   21563 C C     . PRO A 1 4297 ? 225.011 145.570 178.278 1.00 25.98  ? 4297 PRO A C     1 
ATOM   21564 O O     . PRO A 1 4297 ? 224.998 146.802 178.229 1.00 25.98  ? 4297 PRO A O     1 
ATOM   21565 C CB    . PRO A 1 4297 ? 223.078 144.538 177.037 1.00 25.98  ? 4297 PRO A CB    1 
ATOM   21566 C CG    . PRO A 1 4297 ? 222.086 145.637 176.913 1.00 25.98  ? 4297 PRO A CG    1 
ATOM   21567 C CD    . PRO A 1 4297 ? 221.566 145.880 178.300 1.00 25.98  ? 4297 PRO A CD    1 
ATOM   21568 N N     . ASP A 1 4298 ? 226.132 144.852 178.225 1.00 29.47  ? 4298 ASP A N     1 
ATOM   21569 C CA    . ASP A 1 4298 ? 227.448 145.466 178.063 1.00 29.47  ? 4298 ASP A CA    1 
ATOM   21570 C C     . ASP A 1 4298 ? 227.859 145.326 176.600 1.00 29.47  ? 4298 ASP A C     1 
ATOM   21571 O O     . ASP A 1 4298 ? 228.489 144.353 176.188 1.00 29.47  ? 4298 ASP A O     1 
ATOM   21572 C CB    . ASP A 1 4298 ? 228.463 144.828 179.005 1.00 29.47  ? 4298 ASP A CB    1 
ATOM   21573 C CG    . ASP A 1 4298 ? 228.194 145.156 180.457 1.00 29.47  ? 4298 ASP A CG    1 
ATOM   21574 O OD1   . ASP A 1 4298 ? 227.638 146.241 180.727 1.00 29.47  ? 4298 ASP A OD1   1 
ATOM   21575 O OD2   . ASP A 1 4298 ? 228.539 144.331 181.330 1.00 29.47  ? 4298 ASP A OD2   1 
ATOM   21576 N N     . GLY A 1 4299 ? 227.487 146.329 175.805 1.00 25.87  ? 4299 GLY A N     1 
ATOM   21577 C CA    . GLY A 1 4299 ? 227.774 146.316 174.391 1.00 25.87  ? 4299 GLY A CA    1 
ATOM   21578 C C     . GLY A 1 4299 ? 228.147 147.695 173.886 1.00 25.87  ? 4299 GLY A C     1 
ATOM   21579 O O     . GLY A 1 4299 ? 227.956 148.707 174.560 1.00 25.87  ? 4299 GLY A O     1 
ATOM   21580 N N     . ILE A 1 4300 ? 228.690 147.714 172.671 1.00 27.47  ? 4300 ILE A N     1 
ATOM   21581 C CA    . ILE A 1 4300 ? 229.122 148.954 172.038 1.00 27.47  ? 4300 ILE A CA    1 
ATOM   21582 C C     . ILE A 1 4300 ? 228.462 149.078 170.671 1.00 27.47  ? 4300 ILE A C     1 
ATOM   21583 O O     . ILE A 1 4300 ? 228.296 150.185 170.146 1.00 27.47  ? 4300 ILE A O     1 
ATOM   21584 C CB    . ILE A 1 4300 ? 230.658 149.009 171.932 1.00 27.47  ? 4300 ILE A CB    1 
ATOM   21585 C CG1   . ILE A 1 4300 ? 231.121 150.359 171.381 1.00 27.47  ? 4300 ILE A CG1   1 
ATOM   21586 C CG2   . ILE A 1 4300 ? 231.180 147.866 171.074 1.00 27.47  ? 4300 ILE A CG2   1 
ATOM   21587 C CD1   . ILE A 1 4300 ? 232.622 150.535 171.381 1.00 27.47  ? 4300 ILE A CD1   1 
ATOM   21588 N N     . ARG A 1 4301 ? 228.061 147.950 170.094 1.00 27.24  ? 4301 ARG A N     1 
ATOM   21589 C CA    . ARG A 1 4301 ? 227.504 147.914 168.751 1.00 27.24  ? 4301 ARG A CA    1 
ATOM   21590 C C     . ARG A 1 4301 ? 226.056 147.439 168.778 1.00 27.24  ? 4301 ARG A C     1 
ATOM   21591 O O     . ARG A 1 4301 ? 225.559 146.922 169.782 1.00 27.24  ? 4301 ARG A O     1 
ATOM   21592 C CB    . ARG A 1 4301 ? 228.341 147.009 167.839 1.00 27.24  ? 4301 ARG A CB    1 
ATOM   21593 C CG    . ARG A 1 4301 ? 229.727 147.549 167.528 1.00 27.24  ? 4301 ARG A CG    1 
ATOM   21594 C CD    . ARG A 1 4301 ? 230.508 146.595 166.637 1.00 27.24  ? 4301 ARG A CD    1 
ATOM   21595 N NE    . ARG A 1 4301 ? 230.179 145.200 166.901 1.00 27.24  ? 4301 ARG A NE    1 
ATOM   21596 C CZ    . ARG A 1 4301 ? 229.570 144.397 166.038 1.00 27.24  ? 4301 ARG A CZ    1 
ATOM   21597 N NH1   . ARG A 1 4301 ? 229.207 144.820 164.838 1.00 27.24  ? 4301 ARG A NH1   1 
ATOM   21598 N NH2   . ARG A 1 4301 ? 229.317 143.140 166.388 1.00 27.24  ? 4301 ARG A NH2   1 
ATOM   21599 N N     . ARG A 1 4302 ? 225.384 147.624 167.640 1.00 25.42  ? 4302 ARG A N     1 
ATOM   21600 C CA    . ARG A 1 4302 ? 223.983 147.236 167.516 1.00 25.42  ? 4302 ARG A CA    1 
ATOM   21601 C C     . ARG A 1 4302 ? 223.794 145.729 167.633 1.00 25.42  ? 4302 ARG A C     1 
ATOM   21602 O O     . ARG A 1 4302 ? 222.785 145.273 168.187 1.00 25.42  ? 4302 ARG A O     1 
ATOM   21603 C CB    . ARG A 1 4302 ? 223.425 147.740 166.184 1.00 25.42  ? 4302 ARG A CB    1 
ATOM   21604 C CG    . ARG A 1 4302 ? 222.086 147.144 165.789 1.00 25.42  ? 4302 ARG A CG    1 
ATOM   21605 C CD    . ARG A 1 4302 ? 221.957 147.047 164.280 1.00 25.42  ? 4302 ARG A CD    1 
ATOM   21606 N NE    . ARG A 1 4302 ? 220.970 146.054 163.878 1.00 25.42  ? 4302 ARG A NE    1 
ATOM   21607 C CZ    . ARG A 1 4302 ? 219.701 146.327 163.606 1.00 25.42  ? 4302 ARG A CZ    1 
ATOM   21608 N NH1   . ARG A 1 4302 ? 219.227 147.559 163.687 1.00 25.42  ? 4302 ARG A NH1   1 
ATOM   21609 N NH2   . ARG A 1 4302 ? 218.889 145.339 163.244 1.00 25.42  ? 4302 ARG A NH2   1 
ATOM   21610 N N     . GLU A 1 4303 ? 224.747 144.945 167.121 1.00 25.43  ? 4303 GLU A N     1 
ATOM   21611 C CA    . GLU A 1 4303 ? 224.590 143.494 167.105 1.00 25.43  ? 4303 GLU A CA    1 
ATOM   21612 C C     . GLU A 1 4303 ? 224.455 142.933 168.514 1.00 25.43  ? 4303 GLU A C     1 
ATOM   21613 O O     . GLU A 1 4303 ? 223.618 142.058 168.763 1.00 25.43  ? 4303 GLU A O     1 
ATOM   21614 C CB    . GLU A 1 4303 ? 225.773 142.846 166.386 1.00 25.43  ? 4303 GLU A CB    1 
ATOM   21615 C CG    . GLU A 1 4303 ? 225.622 142.773 164.877 1.00 25.43  ? 4303 GLU A CG    1 
ATOM   21616 C CD    . GLU A 1 4303 ? 225.920 144.095 164.198 1.00 25.43  ? 4303 GLU A CD    1 
ATOM   21617 O OE1   . GLU A 1 4303 ? 226.709 144.886 164.756 1.00 25.43  ? 4303 GLU A OE1   1 
ATOM   21618 O OE2   . GLU A 1 4303 ? 225.367 144.342 163.106 1.00 25.43  ? 4303 GLU A OE2   1 
ATOM   21619 N N     . GLU A 1 4304 ? 225.274 143.422 169.448 1.00 24.50  ? 4304 GLU A N     1 
ATOM   21620 C CA    . GLU A 1 4304 ? 225.210 142.925 170.819 1.00 24.50  ? 4304 GLU A CA    1 
ATOM   21621 C C     . GLU A 1 4304 ? 223.861 143.246 171.449 1.00 24.50  ? 4304 GLU A C     1 
ATOM   21622 O O     . GLU A 1 4304 ? 223.261 142.398 172.118 1.00 24.50  ? 4304 GLU A O     1 
ATOM   21623 C CB    . GLU A 1 4304 ? 226.356 143.525 171.635 1.00 24.50  ? 4304 GLU A CB    1 
ATOM   21624 C CG    . GLU A 1 4304 ? 226.246 143.433 173.157 1.00 24.50  ? 4304 GLU A CG    1 
ATOM   21625 C CD    . GLU A 1 4304 ? 225.871 142.051 173.664 1.00 24.50  ? 4304 GLU A CD    1 
ATOM   21626 O OE1   . GLU A 1 4304 ? 224.753 141.882 174.192 1.00 24.50  ? 4304 GLU A OE1   1 
ATOM   21627 O OE2   . GLU A 1 4304 ? 226.701 141.127 173.531 1.00 24.50  ? 4304 GLU A OE2   1 
ATOM   21628 N N     . PHE A 1 4305 ? 223.356 144.462 171.228 1.00 20.47  ? 4305 PHE A N     1 
ATOM   21629 C CA    . PHE A 1 4305 ? 222.060 144.835 171.786 1.00 20.47  ? 4305 PHE A CA    1 
ATOM   21630 C C     . PHE A 1 4305 ? 220.938 143.985 171.204 1.00 20.47  ? 4305 PHE A C     1 
ATOM   21631 O O     . PHE A 1 4305 ? 220.050 143.534 171.938 1.00 20.47  ? 4305 PHE A O     1 
ATOM   21632 C CB    . PHE A 1 4305 ? 221.794 146.319 171.544 1.00 20.47  ? 4305 PHE A CB    1 
ATOM   21633 C CG    . PHE A 1 4305 ? 222.696 147.227 172.326 1.00 20.47  ? 4305 PHE A CG    1 
ATOM   21634 C CD1   . PHE A 1 4305 ? 222.817 147.088 173.696 1.00 20.47  ? 4305 PHE A CD1   1 
ATOM   21635 C CD2   . PHE A 1 4305 ? 223.426 148.213 171.691 1.00 20.47  ? 4305 PHE A CD2   1 
ATOM   21636 C CE1   . PHE A 1 4305 ? 223.647 147.917 174.419 1.00 20.47  ? 4305 PHE A CE1   1 
ATOM   21637 C CE2   . PHE A 1 4305 ? 224.258 149.045 172.409 1.00 20.47  ? 4305 PHE A CE2   1 
ATOM   21638 C CZ    . PHE A 1 4305 ? 224.368 148.897 173.774 1.00 20.47  ? 4305 PHE A CZ    1 
ATOM   21639 N N     . VAL A 1 4306 ? 220.962 143.747 169.891 1.00 21.50  ? 4306 VAL A N     1 
ATOM   21640 C CA    . VAL A 1 4306 ? 219.929 142.912 169.285 1.00 21.50  ? 4306 VAL A CA    1 
ATOM   21641 C C     . VAL A 1 4306 ? 220.013 141.485 169.811 1.00 21.50  ? 4306 VAL A C     1 
ATOM   21642 O O     . VAL A 1 4306 ? 218.981 140.849 170.067 1.00 21.50  ? 4306 VAL A O     1 
ATOM   21643 C CB    . VAL A 1 4306 ? 220.032 142.960 167.750 1.00 21.50  ? 4306 VAL A CB    1 
ATOM   21644 C CG1   . VAL A 1 4306 ? 219.041 141.997 167.121 1.00 21.50  ? 4306 VAL A CG1   1 
ATOM   21645 C CG2   . VAL A 1 4306 ? 219.784 144.372 167.252 1.00 21.50  ? 4306 VAL A CG2   1 
ATOM   21646 N N     . GLN A 1 4307 ? 221.227 140.957 169.988 1.00 23.73  ? 4307 GLN A N     1 
ATOM   21647 C CA    . GLN A 1 4307 ? 221.376 139.619 170.552 1.00 23.73  ? 4307 GLN A CA    1 
ATOM   21648 C C     . GLN A 1 4307 ? 220.838 139.556 171.975 1.00 23.73  ? 4307 GLN A C     1 
ATOM   21649 O O     . GLN A 1 4307 ? 220.177 138.583 172.352 1.00 23.73  ? 4307 GLN A O     1 
ATOM   21650 C CB    . GLN A 1 4307 ? 222.842 139.192 170.517 1.00 23.73  ? 4307 GLN A CB    1 
ATOM   21651 C CG    . GLN A 1 4307 ? 223.368 138.886 169.127 1.00 23.73  ? 4307 GLN A CG    1 
ATOM   21652 C CD    . GLN A 1 4307 ? 224.882 138.884 169.068 1.00 23.73  ? 4307 GLN A CD    1 
ATOM   21653 O OE1   . GLN A 1 4307 ? 225.554 138.962 170.096 1.00 23.73  ? 4307 GLN A OE1   1 
ATOM   21654 N NE2   . GLN A 1 4307 ? 225.427 138.796 167.861 1.00 23.73  ? 4307 GLN A NE2   1 
ATOM   21655 N N     . TRP A 1 4308 ? 221.112 140.585 172.779 1.00 20.60  ? 4308 TRP A N     1 
ATOM   21656 C CA    . TRP A 1 4308 ? 220.585 140.620 174.139 1.00 20.60  ? 4308 TRP A CA    1 
ATOM   21657 C C     . TRP A 1 4308 ? 219.064 140.667 174.131 1.00 20.60  ? 4308 TRP A C     1 
ATOM   21658 O O     . TRP A 1 4308 ? 218.410 140.047 174.978 1.00 20.60  ? 4308 TRP A O     1 
ATOM   21659 C CB    . TRP A 1 4308 ? 221.156 141.818 174.897 1.00 20.60  ? 4308 TRP A CB    1 
ATOM   21660 C CG    . TRP A 1 4308 ? 220.667 141.923 176.308 1.00 20.60  ? 4308 TRP A CG    1 
ATOM   21661 C CD1   . TRP A 1 4308 ? 221.223 141.346 177.411 1.00 20.60  ? 4308 TRP A CD1   1 
ATOM   21662 C CD2   . TRP A 1 4308 ? 219.523 142.651 176.771 1.00 20.60  ? 4308 TRP A CD2   1 
ATOM   21663 N NE1   . TRP A 1 4308 ? 220.497 141.667 178.531 1.00 20.60  ? 4308 TRP A NE1   1 
ATOM   21664 C CE2   . TRP A 1 4308 ? 219.448 142.469 178.164 1.00 20.60  ? 4308 TRP A CE2   1 
ATOM   21665 C CE3   . TRP A 1 4308 ? 218.556 143.439 176.141 1.00 20.60  ? 4308 TRP A CE3   1 
ATOM   21666 C CZ2   . TRP A 1 4308 ? 218.446 143.045 178.939 1.00 20.60  ? 4308 TRP A CZ2   1 
ATOM   21667 C CZ3   . TRP A 1 4308 ? 217.562 144.010 176.913 1.00 20.60  ? 4308 TRP A CZ3   1 
ATOM   21668 C CH2   . TRP A 1 4308 ? 217.514 143.810 178.296 1.00 20.60  ? 4308 TRP A CH2   1 
ATOM   21669 N N     . VAL A 1 4309 ? 218.485 141.407 173.184 1.00 19.99  ? 4309 VAL A N     1 
ATOM   21670 C CA    . VAL A 1 4309 ? 217.031 141.434 173.043 1.00 19.99  ? 4309 VAL A CA    1 
ATOM   21671 C C     . VAL A 1 4309 ? 216.509 140.041 172.719 1.00 19.99  ? 4309 VAL A C     1 
ATOM   21672 O O     . VAL A 1 4309 ? 215.519 139.577 173.296 1.00 19.99  ? 4309 VAL A O     1 
ATOM   21673 C CB    . VAL A 1 4309 ? 216.617 142.450 171.966 1.00 19.99  ? 4309 VAL A CB    1 
ATOM   21674 C CG1   . VAL A 1 4309 ? 215.140 142.309 171.644 1.00 19.99  ? 4309 VAL A CG1   1 
ATOM   21675 C CG2   . VAL A 1 4309 ? 216.942 143.851 172.416 1.00 19.99  ? 4309 VAL A CG2   1 
ATOM   21676 N N     . GLU A 1 4310 ? 217.173 139.350 171.789 1.00 20.59  ? 4310 GLU A N     1 
ATOM   21677 C CA    . GLU A 1 4310 ? 216.738 138.016 171.395 1.00 20.59  ? 4310 GLU A CA    1 
ATOM   21678 C C     . GLU A 1 4310 ? 216.925 136.990 172.504 1.00 20.59  ? 4310 GLU A C     1 
ATOM   21679 O O     . GLU A 1 4310 ? 216.295 135.929 172.460 1.00 20.59  ? 4310 GLU A O     1 
ATOM   21680 C CB    . GLU A 1 4310 ? 217.488 137.570 170.141 1.00 20.59  ? 4310 GLU A CB    1 
ATOM   21681 C CG    . GLU A 1 4310 ? 216.918 138.133 168.852 1.00 20.59  ? 4310 GLU A CG    1 
ATOM   21682 C CD    . GLU A 1 4310 ? 217.934 138.166 167.729 1.00 20.59  ? 4310 GLU A CD    1 
ATOM   21683 O OE1   . GLU A 1 4310 ? 217.641 138.773 166.678 1.00 20.59  ? 4310 GLU A OE1   1 
ATOM   21684 O OE2   . GLU A 1 4310 ? 219.026 137.583 167.897 1.00 20.59  ? 4310 GLU A OE2   1 
ATOM   21685 N N     . LEU A 1 4311 ? 217.768 137.279 173.492 1.00 20.36  ? 4311 LEU A N     1 
ATOM   21686 C CA    . LEU A 1 4311 ? 217.992 136.382 174.617 1.00 20.36  ? 4311 LEU A CA    1 
ATOM   21687 C C     . LEU A 1 4311 ? 217.094 136.685 175.809 1.00 20.36  ? 4311 LEU A C     1 
ATOM   21688 O O     . LEU A 1 4311 ? 217.261 136.063 176.863 1.00 20.36  ? 4311 LEU A O     1 
ATOM   21689 C CB    . LEU A 1 4311 ? 219.460 136.439 175.055 1.00 20.36  ? 4311 LEU A CB    1 
ATOM   21690 C CG    . LEU A 1 4311 ? 220.387 135.349 174.514 1.00 20.36  ? 4311 LEU A CG    1 
ATOM   21691 C CD1   . LEU A 1 4311 ? 220.562 135.466 173.008 1.00 20.36  ? 4311 LEU A CD1   1 
ATOM   21692 C CD2   . LEU A 1 4311 ? 221.734 135.403 175.219 1.00 20.36  ? 4311 LEU A CD2   1 
ATOM   21693 N N     . LEU A 1 4312 ? 216.160 137.621 175.674 1.00 19.49  ? 4312 LEU A N     1 
ATOM   21694 C CA    . LEU A 1 4312 ? 215.274 137.949 176.779 1.00 19.49  ? 4312 LEU A CA    1 
ATOM   21695 C C     . LEU A 1 4312 ? 214.386 136.753 177.116 1.00 19.49  ? 4312 LEU A C     1 
ATOM   21696 O O     . LEU A 1 4312 ? 213.859 136.095 176.214 1.00 19.49  ? 4312 LEU A O     1 
ATOM   21697 C CB    . LEU A 1 4312 ? 214.407 139.158 176.431 1.00 19.49  ? 4312 LEU A CB    1 
ATOM   21698 C CG    . LEU A 1 4312 ? 214.936 140.532 176.840 1.00 19.49  ? 4312 LEU A CG    1 
ATOM   21699 C CD1   . LEU A 1 4312 ? 213.855 141.584 176.677 1.00 19.49  ? 4312 LEU A CD1   1 
ATOM   21700 C CD2   . LEU A 1 4312 ? 215.445 140.505 178.269 1.00 19.49  ? 4312 LEU A CD2   1 
ATOM   21701 N N     . PRO A 1 4313 ? 214.207 136.444 178.398 1.00 21.00  ? 4313 PRO A N     1 
ATOM   21702 C CA    . PRO A 1 4313 ? 213.338 135.324 178.770 1.00 21.00  ? 4313 PRO A CA    1 
ATOM   21703 C C     . PRO A 1 4313 ? 211.886 135.601 178.419 1.00 21.00  ? 4313 PRO A C     1 
ATOM   21704 O O     . PRO A 1 4313 ? 211.433 136.748 178.394 1.00 21.00  ? 4313 PRO A O     1 
ATOM   21705 C CB    . PRO A 1 4313 ? 213.532 135.210 180.286 1.00 21.00  ? 4313 PRO A CB    1 
ATOM   21706 C CG    . PRO A 1 4313 ? 213.988 136.564 180.710 1.00 21.00  ? 4313 PRO A CG    1 
ATOM   21707 C CD    . PRO A 1 4313 ? 214.809 137.093 179.574 1.00 21.00  ? 4313 PRO A CD    1 
ATOM   21708 N N     . ASP A 1 4314 ? 211.152 134.521 178.144 1.00 24.81  ? 4314 ASP A N     1 
ATOM   21709 C CA    . ASP A 1 4314 ? 209.743 134.649 177.792 1.00 24.81  ? 4314 ASP A CA    1 
ATOM   21710 C C     . ASP A 1 4314 ? 208.891 135.022 178.999 1.00 24.81  ? 4314 ASP A C     1 
ATOM   21711 O O     . ASP A 1 4314 ? 207.798 135.576 178.838 1.00 24.81  ? 4314 ASP A O     1 
ATOM   21712 C CB    . ASP A 1 4314 ? 209.245 133.345 177.167 1.00 24.81  ? 4314 ASP A CB    1 
ATOM   21713 C CG    . ASP A 1 4314 ? 207.895 133.495 176.494 1.00 24.81  ? 4314 ASP A CG    1 
ATOM   21714 O OD1   . ASP A 1 4314 ? 206.871 133.536 177.207 1.00 24.81  ? 4314 ASP A OD1   1 
ATOM   21715 O OD2   . ASP A 1 4314 ? 207.858 133.567 175.248 1.00 24.81  ? 4314 ASP A OD2   1 
ATOM   21716 N N     . THR A 1 4315 ? 209.374 134.738 180.209 1.00 24.61  ? 4315 THR A N     1 
ATOM   21717 C CA    . THR A 1 4315 ? 208.617 134.990 181.436 1.00 24.61  ? 4315 THR A CA    1 
ATOM   21718 C C     . THR A 1 4315 ? 208.657 136.481 181.778 1.00 24.61  ? 4315 THR A C     1 
ATOM   21719 O O     . THR A 1 4315 ? 209.354 136.945 182.684 1.00 24.61  ? 4315 THR A O     1 
ATOM   21720 C CB    . THR A 1 4315 ? 209.135 134.101 182.568 1.00 24.61  ? 4315 THR A CB    1 
ATOM   21721 O OG1   . THR A 1 4315 ? 208.296 134.235 183.724 1.00 24.61  ? 4315 THR A OG1   1 
ATOM   21722 C CG2   . THR A 1 4315 ? 210.616 134.358 182.907 1.00 24.61  ? 4315 THR A CG2   1 
ATOM   21723 N N     . GLN A 1 4316 ? 207.860 137.250 181.042 1.00 19.41  ? 4316 GLN A N     1 
ATOM   21724 C CA    . GLN A 1 4316 ? 207.761 138.689 181.262 1.00 19.41  ? 4316 GLN A CA    1 
ATOM   21725 C C     . GLN A 1 4316 ? 206.547 138.979 182.135 1.00 19.41  ? 4316 GLN A C     1 
ATOM   21726 O O     . GLN A 1 4316 ? 205.406 138.917 181.667 1.00 19.41  ? 4316 GLN A O     1 
ATOM   21727 C CB    . GLN A 1 4316 ? 207.664 139.444 179.941 1.00 19.41  ? 4316 GLN A CB    1 
ATOM   21728 C CG    . GLN A 1 4316 ? 207.497 140.940 180.135 1.00 19.41  ? 4316 GLN A CG    1 
ATOM   21729 C CD    . GLN A 1 4316 ? 206.614 141.575 179.087 1.00 19.41  ? 4316 GLN A CD    1 
ATOM   21730 O OE1   . GLN A 1 4316 ? 206.858 141.439 177.890 1.00 19.41  ? 4316 GLN A OE1   1 
ATOM   21731 N NE2   . GLN A 1 4316 ? 205.575 142.271 179.532 1.00 19.41  ? 4316 GLN A NE2   1 
ATOM   21732 N N     . THR A 1 4317 ? 206.793 139.294 183.391 1.00 19.20  ? 4317 THR A N     1 
ATOM   21733 C CA    . THR A 1 4317 ? 205.767 139.756 184.309 1.00 19.20  ? 4317 THR A CA    1 
ATOM   21734 C C     . THR A 1 4317 ? 205.564 141.256 184.155 1.00 19.20  ? 4317 THR A C     1 
ATOM   21735 O O     . THR A 1 4317 ? 206.422 141.955 183.607 1.00 19.20  ? 4317 THR A O     1 
ATOM   21736 C CB    . THR A 1 4317 ? 206.164 139.421 185.744 1.00 19.20  ? 4317 THR A CB    1 
ATOM   21737 O OG1   . THR A 1 4317 ? 207.397 140.076 186.065 1.00 19.20  ? 4317 THR A OG1   1 
ATOM   21738 C CG2   . THR A 1 4317 ? 206.339 137.921 185.905 1.00 19.20  ? 4317 THR A CG2   1 
ATOM   21739 N N     . PRO A 1 4318 ? 204.430 141.790 184.616 1.00 16.01  ? 4318 PRO A N     1 
ATOM   21740 C CA    . PRO A 1 4318 ? 204.241 143.249 184.568 1.00 16.01  ? 4318 PRO A CA    1 
ATOM   21741 C C     . PRO A 1 4318 ? 205.267 144.021 185.377 1.00 16.01  ? 4318 PRO A C     1 
ATOM   21742 O O     . PRO A 1 4318 ? 205.393 145.236 185.186 1.00 16.01  ? 4318 PRO A O     1 
ATOM   21743 C CB    . PRO A 1 4318 ? 202.826 143.439 185.127 1.00 16.01  ? 4318 PRO A CB    1 
ATOM   21744 C CG    . PRO A 1 4318 ? 202.147 142.148 184.864 1.00 16.01  ? 4318 PRO A CG    1 
ATOM   21745 C CD    . PRO A 1 4318 ? 203.199 141.095 185.029 1.00 16.01  ? 4318 PRO A CD    1 
ATOM   21746 N N     . SER A 1 4319 ? 206.001 143.361 186.277 1.00 21.07  ? 4319 SER A N     1 
ATOM   21747 C CA    . SER A 1 4319 ? 207.036 144.052 187.039 1.00 21.07  ? 4319 SER A CA    1 
ATOM   21748 C C     . SER A 1 4319 ? 208.164 144.547 186.141 1.00 21.07  ? 4319 SER A C     1 
ATOM   21749 O O     . SER A 1 4319 ? 208.957 145.398 186.558 1.00 21.07  ? 4319 SER A O     1 
ATOM   21750 C CB    . SER A 1 4319 ? 207.585 143.135 188.130 1.00 21.07  ? 4319 SER A CB    1 
ATOM   21751 O OG    . SER A 1 4319 ? 208.329 142.066 187.575 1.00 21.07  ? 4319 SER A OG    1 
ATOM   21752 N N     . TRP A 1 4320 ? 208.260 144.023 184.916 1.00 17.78  ? 4320 TRP A N     1 
ATOM   21753 C CA    . TRP A 1 4320 ? 209.205 144.573 183.949 1.00 17.78  ? 4320 TRP A CA    1 
ATOM   21754 C C     . TRP A 1 4320 ? 208.881 146.027 183.640 1.00 17.78  ? 4320 TRP A C     1 
ATOM   21755 O O     . TRP A 1 4320 ? 209.782 146.867 183.538 1.00 17.78  ? 4320 TRP A O     1 
ATOM   21756 C CB    . TRP A 1 4320 ? 209.189 143.752 182.660 1.00 17.78  ? 4320 TRP A CB    1 
ATOM   21757 C CG    . TRP A 1 4320 ? 209.711 142.356 182.785 1.00 17.78  ? 4320 TRP A CG    1 
ATOM   21758 C CD1   . TRP A 1 4320 ? 209.491 141.484 183.808 1.00 17.78  ? 4320 TRP A CD1   1 
ATOM   21759 C CD2   . TRP A 1 4320 ? 210.526 141.661 181.835 1.00 17.78  ? 4320 TRP A CD2   1 
ATOM   21760 N NE1   . TRP A 1 4320 ? 210.129 140.294 183.562 1.00 17.78  ? 4320 TRP A NE1   1 
ATOM   21761 C CE2   . TRP A 1 4320 ? 210.771 140.377 182.355 1.00 17.78  ? 4320 TRP A CE2   1 
ATOM   21762 C CE3   . TRP A 1 4320 ? 211.076 142.003 180.597 1.00 17.78  ? 4320 TRP A CE3   1 
ATOM   21763 C CZ2   . TRP A 1 4320 ? 211.542 139.434 181.681 1.00 17.78  ? 4320 TRP A CZ2   1 
ATOM   21764 C CZ3   . TRP A 1 4320 ? 211.840 141.067 179.930 1.00 17.78  ? 4320 TRP A CZ3   1 
ATOM   21765 C CH2   . TRP A 1 4320 ? 212.066 139.798 180.473 1.00 17.78  ? 4320 TRP A CH2   1 
ATOM   21766 N N     . LEU A 1 4321 ? 207.596 146.340 183.486 1.00 11.46  ? 4321 LEU A N     1 
ATOM   21767 C CA    . LEU A 1 4321 ? 207.150 147.685 183.154 1.00 11.46  ? 4321 LEU A CA    1 
ATOM   21768 C C     . LEU A 1 4321 ? 207.164 148.628 184.348 1.00 11.46  ? 4321 LEU A C     1 
ATOM   21769 O O     . LEU A 1 4321 ? 206.961 149.832 184.168 1.00 11.46  ? 4321 LEU A O     1 
ATOM   21770 C CB    . LEU A 1 4321 ? 205.736 147.631 182.572 1.00 11.46  ? 4321 LEU A CB    1 
ATOM   21771 C CG    . LEU A 1 4321 ? 205.429 146.508 181.582 1.00 11.46  ? 4321 LEU A CG    1 
ATOM   21772 C CD1   . LEU A 1 4321 ? 204.022 146.657 181.039 1.00 11.46  ? 4321 LEU A CD1   1 
ATOM   21773 C CD2   . LEU A 1 4321 ? 206.436 146.500 180.450 1.00 11.46  ? 4321 LEU A CD2   1 
ATOM   21774 N N     . GLY A 1 4322 ? 207.395 148.115 185.553 1.00 15.44  ? 4322 GLY A N     1 
ATOM   21775 C CA    . GLY A 1 4322 ? 207.265 148.881 186.767 1.00 15.44  ? 4322 GLY A CA    1 
ATOM   21776 C C     . GLY A 1 4322 ? 205.923 148.731 187.451 1.00 15.44  ? 4322 GLY A C     1 
ATOM   21777 O O     . GLY A 1 4322 ? 205.791 149.113 188.618 1.00 15.44  ? 4322 GLY A O     1 
ATOM   21778 N N     . LEU A 1 4323 ? 204.930 148.184 186.754 1.00 12.17  ? 4323 LEU A N     1 
ATOM   21779 C CA    . LEU A 1 4323 ? 203.623 147.955 187.338 1.00 12.17  ? 4323 LEU A CA    1 
ATOM   21780 C C     . LEU A 1 4323 ? 203.684 146.812 188.347 1.00 12.17  ? 4323 LEU A C     1 
ATOM   21781 O O     . LEU A 1 4323 ? 204.567 145.955 188.278 1.00 12.17  ? 4323 LEU A O     1 
ATOM   21782 C CB    . LEU A 1 4323 ? 202.608 147.631 186.247 1.00 12.17  ? 4323 LEU A CB    1 
ATOM   21783 C CG    . LEU A 1 4323 ? 202.185 148.768 185.320 1.00 12.17  ? 4323 LEU A CG    1 
ATOM   21784 C CD1   . LEU A 1 4323 ? 201.317 148.234 184.200 1.00 12.17  ? 4323 LEU A CD1   1 
ATOM   21785 C CD2   . LEU A 1 4323 ? 201.448 149.837 186.100 1.00 12.17  ? 4323 LEU A CD2   1 
ATOM   21786 N N     . PRO A 1 4324 ? 202.758 146.783 189.305 1.00 17.55  ? 4324 PRO A N     1 
ATOM   21787 C CA    . PRO A 1 4324 ? 202.674 145.627 190.203 1.00 17.55  ? 4324 PRO A CA    1 
ATOM   21788 C C     . PRO A 1 4324 ? 202.264 144.378 189.438 1.00 17.55  ? 4324 PRO A C     1 
ATOM   21789 O O     . PRO A 1 4324 ? 201.568 144.451 188.424 1.00 17.55  ? 4324 PRO A O     1 
ATOM   21790 C CB    . PRO A 1 4324 ? 201.608 146.044 191.221 1.00 17.55  ? 4324 PRO A CB    1 
ATOM   21791 C CG    . PRO A 1 4324 ? 200.797 147.074 190.512 1.00 17.55  ? 4324 PRO A CG    1 
ATOM   21792 C CD    . PRO A 1 4324 ? 201.765 147.815 189.643 1.00 17.55  ? 4324 PRO A CD    1 
ATOM   21793 N N     . ASN A 1 4325 ? 202.705 143.220 189.934 1.00 20.28  ? 4325 ASN A N     1 
ATOM   21794 C CA    . ASN A 1 4325 ? 202.419 141.968 189.240 1.00 20.28  ? 4325 ASN A CA    1 
ATOM   21795 C C     . ASN A 1 4325 ? 200.934 141.630 189.266 1.00 20.28  ? 4325 ASN A C     1 
ATOM   21796 O O     . ASN A 1 4325 ? 200.474 140.806 188.468 1.00 20.28  ? 4325 ASN A O     1 
ATOM   21797 C CB    . ASN A 1 4325 ? 203.236 140.831 189.850 1.00 20.28  ? 4325 ASN A CB    1 
ATOM   21798 C CG    . ASN A 1 4325 ? 204.728 141.055 189.722 1.00 20.28  ? 4325 ASN A CG    1 
ATOM   21799 O OD1   . ASN A 1 4325 ? 205.269 142.027 190.249 1.00 20.28  ? 4325 ASN A OD1   1 
ATOM   21800 N ND2   . ASN A 1 4325 ? 205.403 140.156 189.016 1.00 20.28  ? 4325 ASN A ND2   1 
ATOM   21801 N N     . ASN A 1 4326 ? 200.168 142.248 190.167 1.00 20.13  ? 4326 ASN A N     1 
ATOM   21802 C CA    . ASN A 1 4326 ? 198.730 142.012 190.202 1.00 20.13  ? 4326 ASN A CA    1 
ATOM   21803 C C     . ASN A 1 4326 ? 198.001 142.717 189.064 1.00 20.13  ? 4326 ASN A C     1 
ATOM   21804 O O     . ASN A 1 4326 ? 196.798 142.495 188.880 1.00 20.13  ? 4326 ASN A O     1 
ATOM   21805 C CB    . ASN A 1 4326 ? 198.159 142.452 191.550 1.00 20.13  ? 4326 ASN A CB    1 
ATOM   21806 C CG    . ASN A 1 4326 ? 198.400 143.920 191.835 1.00 20.13  ? 4326 ASN A CG    1 
ATOM   21807 O OD1   . ASN A 1 4326 ? 197.915 144.795 191.118 1.00 20.13  ? 4326 ASN A OD1   1 
ATOM   21808 N ND2   . ASN A 1 4326 ? 199.153 144.199 192.891 1.00 20.13  ? 4326 ASN A ND2   1 
ATOM   21809 N N     . ALA A 1 4327 ? 198.697 143.570 188.309 1.00 17.61  ? 4327 ALA A N     1 
ATOM   21810 C CA    . ALA A 1 4327 ? 198.071 144.234 187.171 1.00 17.61  ? 4327 ALA A CA    1 
ATOM   21811 C C     . ALA A 1 4327 ? 197.628 143.218 186.128 1.00 17.61  ? 4327 ALA A C     1 
ATOM   21812 O O     . ALA A 1 4327 ? 196.582 143.378 185.491 1.00 17.61  ? 4327 ALA A O     1 
ATOM   21813 C CB    . ALA A 1 4327 ? 199.033 145.253 186.561 1.00 17.61  ? 4327 ALA A CB    1 
ATOM   21814 N N     . GLU A 1 4328 ? 198.419 142.161 185.940 1.00 18.85  ? 4328 GLU A N     1 
ATOM   21815 C CA    . GLU A 1 4328 ? 198.043 141.099 185.014 1.00 18.85  ? 4328 GLU A CA    1 
ATOM   21816 C C     . GLU A 1 4328 ? 196.755 140.419 185.464 1.00 18.85  ? 4328 GLU A C     1 
ATOM   21817 O O     . GLU A 1 4328 ? 195.869 140.129 184.653 1.00 18.85  ? 4328 GLU A O     1 
ATOM   21818 C CB    . GLU A 1 4328 ? 199.181 140.083 184.899 1.00 18.85  ? 4328 GLU A CB    1 
ATOM   21819 C CG    . GLU A 1 4328 ? 198.869 138.882 184.022 1.00 18.85  ? 4328 GLU A CG    1 
ATOM   21820 C CD    . GLU A 1 4328 ? 198.870 139.213 182.541 1.00 18.85  ? 4328 GLU A CD    1 
ATOM   21821 O OE1   . GLU A 1 4328 ? 199.219 140.356 182.178 1.00 18.85  ? 4328 GLU A OE1   1 
ATOM   21822 O OE2   . GLU A 1 4328 ? 198.523 138.324 181.736 1.00 18.85  ? 4328 GLU A OE2   1 
ATOM   21823 N N     . ARG A 1 4329 ? 196.641 140.159 186.767 1.00 20.90  ? 4329 ARG A N     1 
ATOM   21824 C CA    . ARG A 1 4329 ? 195.433 139.546 187.309 1.00 20.90  ? 4329 ARG A CA    1 
ATOM   21825 C C     . ARG A 1 4329 ? 194.222 140.449 187.108 1.00 20.90  ? 4329 ARG A C     1 
ATOM   21826 O O     . ARG A 1 4329 ? 193.138 139.987 186.728 1.00 20.90  ? 4329 ARG A O     1 
ATOM   21827 C CB    . ARG A 1 4329 ? 195.644 139.232 188.791 1.00 20.90  ? 4329 ARG A CB    1 
ATOM   21828 C CG    . ARG A 1 4329 ? 194.375 139.037 189.594 1.00 20.90  ? 4329 ARG A CG    1 
ATOM   21829 C CD    . ARG A 1 4329 ? 194.685 138.902 191.079 1.00 20.90  ? 4329 ARG A CD    1 
ATOM   21830 N NE    . ARG A 1 4329 ? 195.153 137.565 191.425 1.00 20.90  ? 4329 ARG A NE    1 
ATOM   21831 C CZ    . ARG A 1 4329 ? 196.430 137.221 191.532 1.00 20.90  ? 4329 ARG A CZ    1 
ATOM   21832 N NH1   . ARG A 1 4329 ? 197.401 138.098 191.334 1.00 20.90  ? 4329 ARG A NH1   1 
ATOM   21833 N NH2   . ARG A 1 4329 ? 196.740 135.967 191.848 1.00 20.90  ? 4329 ARG A NH2   1 
ATOM   21834 N N     . VAL A 1 4330 ? 194.396 141.749 187.350 1.00 18.66  ? 4330 VAL A N     1 
ATOM   21835 C CA    . VAL A 1 4330 ? 193.297 142.697 187.158 1.00 18.66  ? 4330 VAL A CA    1 
ATOM   21836 C C     . VAL A 1 4330 ? 192.874 142.730 185.693 1.00 18.66  ? 4330 VAL A C     1 
ATOM   21837 O O     . VAL A 1 4330 ? 191.680 142.752 185.368 1.00 18.66  ? 4330 VAL A O     1 
ATOM   21838 C CB    . VAL A 1 4330 ? 193.699 144.095 187.659 1.00 18.66  ? 4330 VAL A CB    1 
ATOM   21839 C CG1   . VAL A 1 4330 ? 192.578 145.087 187.411 1.00 18.66  ? 4330 VAL A CG1   1 
ATOM   21840 C CG2   . VAL A 1 4330 ? 194.040 144.046 189.134 1.00 18.66  ? 4330 VAL A CG2   1 
ATOM   21841 N N     . LEU A 1 4331 ? 193.854 142.741 184.787 1.00 18.76  ? 4331 LEU A N     1 
ATOM   21842 C CA    . LEU A 1 4331 ? 193.553 142.766 183.360 1.00 18.76  ? 4331 LEU A CA    1 
ATOM   21843 C C     . LEU A 1 4331 ? 192.819 141.502 182.930 1.00 18.76  ? 4331 LEU A C     1 
ATOM   21844 O O     . LEU A 1 4331 ? 191.884 141.555 182.122 1.00 18.76  ? 4331 LEU A O     1 
ATOM   21845 C CB    . LEU A 1 4331 ? 194.844 142.941 182.560 1.00 18.76  ? 4331 LEU A CB    1 
ATOM   21846 C CG    . LEU A 1 4331 ? 194.679 143.053 181.045 1.00 18.76  ? 4331 LEU A CG    1 
ATOM   21847 C CD1   . LEU A 1 4331 ? 194.144 144.424 180.672 1.00 18.76  ? 4331 LEU A CD1   1 
ATOM   21848 C CD2   . LEU A 1 4331 ? 195.992 142.773 180.336 1.00 18.76  ? 4331 LEU A CD2   1 
ATOM   21849 N N     . LEU A 1 4332 ? 193.238 140.348 183.454 1.00 17.43  ? 4332 LEU A N     1 
ATOM   21850 C CA    . LEU A 1 4332 ? 192.560 139.097 183.130 1.00 17.43  ? 4332 LEU A CA    1 
ATOM   21851 C C     . LEU A 1 4332 ? 191.122 139.107 183.635 1.00 17.43  ? 4332 LEU A C     1 
ATOM   21852 O O     . LEU A 1 4332 ? 190.205 138.637 182.951 1.00 17.43  ? 4332 LEU A O     1 
ATOM   21853 C CB    . LEU A 1 4332 ? 193.333 137.915 183.715 1.00 17.43  ? 4332 LEU A CB    1 
ATOM   21854 C CG    . LEU A 1 4332 ? 194.667 137.584 183.043 1.00 17.43  ? 4332 LEU A CG    1 
ATOM   21855 C CD1   . LEU A 1 4332 ? 195.197 136.248 183.535 1.00 17.43  ? 4332 LEU A CD1   1 
ATOM   21856 C CD2   . LEU A 1 4332 ? 194.525 137.582 181.531 1.00 17.43  ? 4332 LEU A CD2   1 
ATOM   21857 N N     . THR A 1 4333 ? 190.908 139.642 184.840 1.00 20.27  ? 4333 THR A N     1 
ATOM   21858 C CA    . THR A 1 4333 ? 189.551 139.760 185.366 1.00 20.27  ? 4333 THR A CA    1 
ATOM   21859 C C     . THR A 1 4333 ? 188.695 140.648 184.470 1.00 20.27  ? 4333 THR A C     1 
ATOM   21860 O O     . THR A 1 4333 ? 187.539 140.323 184.165 1.00 20.27  ? 4333 THR A O     1 
ATOM   21861 C CB    . THR A 1 4333 ? 189.588 140.314 186.791 1.00 20.27  ? 4333 THR A CB    1 
ATOM   21862 O OG1   . THR A 1 4333 ? 190.370 139.449 187.623 1.00 20.27  ? 4333 THR A OG1   1 
ATOM   21863 C CG2   . THR A 1 4333 ? 188.184 140.420 187.358 1.00 20.27  ? 4333 THR A CG2   1 
ATOM   21864 N N     . THR A 1 4334 ? 189.256 141.777 184.033 1.00 20.32  ? 4334 THR A N     1 
ATOM   21865 C CA    . THR A 1 4334 ? 188.520 142.684 183.157 1.00 20.32  ? 4334 THR A CA    1 
ATOM   21866 C C     . THR A 1 4334 ? 188.185 142.015 181.829 1.00 20.32  ? 4334 THR A C     1 
ATOM   21867 O O     . THR A 1 4334 ? 187.082 142.181 181.295 1.00 20.32  ? 4334 THR A O     1 
ATOM   21868 C CB    . THR A 1 4334 ? 189.327 143.961 182.928 1.00 20.32  ? 4334 THR A CB    1 
ATOM   21869 O OG1   . THR A 1 4334 ? 189.632 144.567 184.190 1.00 20.32  ? 4334 THR A OG1   1 
ATOM   21870 C CG2   . THR A 1 4334 ? 188.536 144.944 182.081 1.00 20.32  ? 4334 THR A CG2   1 
ATOM   21871 N N     . GLN A 1 4335 ? 189.130 141.251 181.279 1.00 21.06  ? 4335 GLN A N     1 
ATOM   21872 C CA    . GLN A 1 4335 ? 188.888 140.566 180.013 1.00 21.06  ? 4335 GLN A CA    1 
ATOM   21873 C C     . GLN A 1 4335 ? 187.808 139.499 180.162 1.00 21.06  ? 4335 GLN A C     1 
ATOM   21874 O O     . GLN A 1 4335 ? 186.977 139.311 179.267 1.00 21.06  ? 4335 GLN A O     1 
ATOM   21875 C CB    . GLN A 1 4335 ? 190.188 139.957 179.491 1.00 21.06  ? 4335 GLN A CB    1 
ATOM   21876 C CG    . GLN A 1 4335 ? 191.124 140.966 178.853 1.00 21.06  ? 4335 GLN A CG    1 
ATOM   21877 C CD    . GLN A 1 4335 ? 192.448 140.357 178.448 1.00 21.06  ? 4335 GLN A CD    1 
ATOM   21878 O OE1   . GLN A 1 4335 ? 192.748 139.215 178.790 1.00 21.06  ? 4335 GLN A OE1   1 
ATOM   21879 N NE2   . GLN A 1 4335 ? 193.250 141.119 177.715 1.00 21.06  ? 4335 GLN A NE2   1 
ATOM   21880 N N     . GLY A 1 4336 ? 187.809 138.782 181.287 1.00 22.18  ? 4336 GLY A N     1 
ATOM   21881 C CA    . GLY A 1 4336 ? 186.744 137.820 181.533 1.00 22.18  ? 4336 GLY A CA    1 
ATOM   21882 C C     . GLY A 1 4336 ? 185.385 138.484 181.645 1.00 22.18  ? 4336 GLY A C     1 
ATOM   21883 O O     . GLY A 1 4336 ? 184.382 137.982 181.125 1.00 22.18  ? 4336 GLY A O     1 
ATOM   21884 N N     . VAL A 1 4337 ? 185.337 139.631 182.326 1.00 23.03  ? 4337 VAL A N     1 
ATOM   21885 C CA    . VAL A 1 4337 ? 184.089 140.386 182.422 1.00 23.03  ? 4337 VAL A CA    1 
ATOM   21886 C C     . VAL A 1 4337 ? 183.623 140.813 181.035 1.00 23.03  ? 4337 VAL A C     1 
ATOM   21887 O O     . VAL A 1 4337 ? 182.430 140.750 180.713 1.00 23.03  ? 4337 VAL A O     1 
ATOM   21888 C CB    . VAL A 1 4337 ? 184.265 141.594 183.360 1.00 23.03  ? 4337 VAL A CB    1 
ATOM   21889 C CG1   . VAL A 1 4337 ? 183.083 142.541 183.238 1.00 23.03  ? 4337 VAL A CG1   1 
ATOM   21890 C CG2   . VAL A 1 4337 ? 184.427 141.126 184.794 1.00 23.03  ? 4337 VAL A CG2   1 
ATOM   21891 N N     . ASP A 1 4338 ? 184.560 141.253 180.193 1.00 24.91  ? 4338 ASP A N     1 
ATOM   21892 C CA    . ASP A 1 4338 ? 184.210 141.650 178.831 1.00 24.91  ? 4338 ASP A CA    1 
ATOM   21893 C C     . ASP A 1 4338 ? 183.680 140.469 178.026 1.00 24.91  ? 4338 ASP A C     1 
ATOM   21894 O O     . ASP A 1 4338 ? 182.747 140.614 177.230 1.00 24.91  ? 4338 ASP A O     1 
ATOM   21895 C CB    . ASP A 1 4338 ? 185.419 142.276 178.136 1.00 24.91  ? 4338 ASP A CB    1 
ATOM   21896 C CG    . ASP A 1 4338 ? 185.768 143.640 178.693 1.00 24.91  ? 4338 ASP A CG    1 
ATOM   21897 O OD1   . ASP A 1 4338 ? 184.853 144.336 179.178 1.00 24.91  ? 4338 ASP A OD1   1 
ATOM   21898 O OD2   . ASP A 1 4338 ? 186.957 144.019 178.640 1.00 24.91  ? 4338 ASP A OD2   1 
ATOM   21899 N N     . MET A 1 4339 ? 184.278 139.290 178.208 1.00 25.80  ? 4339 MET A N     1 
ATOM   21900 C CA    . MET A 1 4339 ? 183.792 138.102 177.512 1.00 25.80  ? 4339 MET A CA    1 
ATOM   21901 C C     . MET A 1 4339 ? 182.367 137.768 177.936 1.00 25.80  ? 4339 MET A C     1 
ATOM   21902 O O     . MET A 1 4339 ? 181.513 137.442 177.102 1.00 25.80  ? 4339 MET A O     1 
ATOM   21903 C CB    . MET A 1 4339 ? 184.724 136.918 177.775 1.00 25.80  ? 4339 MET A CB    1 
ATOM   21904 C CG    . MET A 1 4339 ? 184.193 135.589 177.267 1.00 25.80  ? 4339 MET A CG    1 
ATOM   21905 S SD    . MET A 1 4339 ? 185.072 134.173 177.951 1.00 25.80  ? 4339 MET A SD    1 
ATOM   21906 C CE    . MET A 1 4339 ? 184.302 134.039 179.560 1.00 25.80  ? 4339 MET A CE    1 
ATOM   21907 N N     . ILE A 1 4340 ? 182.094 137.851 179.240 1.00 26.02  ? 4340 ILE A N     1 
ATOM   21908 C CA    . ILE A 1 4340 ? 180.739 137.605 179.734 1.00 26.02  ? 4340 ILE A CA    1 
ATOM   21909 C C     . ILE A 1 4340 ? 179.768 138.621 179.144 1.00 26.02  ? 4340 ILE A C     1 
ATOM   21910 O O     . ILE A 1 4340 ? 178.647 138.282 178.743 1.00 26.02  ? 4340 ILE A O     1 
ATOM   21911 C CB    . ILE A 1 4340 ? 180.715 137.629 181.272 1.00 26.02  ? 4340 ILE A CB    1 
ATOM   21912 C CG1   . ILE A 1 4340 ? 181.567 136.494 181.833 1.00 26.02  ? 4340 ILE A CG1   1 
ATOM   21913 C CG2   . ILE A 1 4340 ? 179.291 137.516 181.784 1.00 26.02  ? 4340 ILE A CG2   1 
ATOM   21914 C CD1   . ILE A 1 4340 ? 181.182 135.146 181.299 1.00 26.02  ? 4340 ILE A CD1   1 
ATOM   21915 N N     . SER A 1 4341 ? 180.187 139.887 179.088 1.00 25.99  ? 4341 SER A N     1 
ATOM   21916 C CA    . SER A 1 4341 ? 179.335 140.929 178.526 1.00 25.99  ? 4341 SER A CA    1 
ATOM   21917 C C     . SER A 1 4341 ? 179.042 140.670 177.054 1.00 25.99  ? 4341 SER A C     1 
ATOM   21918 O O     . SER A 1 4341 ? 177.919 140.889 176.591 1.00 25.99  ? 4341 SER A O     1 
ATOM   21919 C CB    . SER A 1 4341 ? 179.990 142.297 178.713 1.00 25.99  ? 4341 SER A CB    1 
ATOM   21920 O OG    . SER A 1 4341 ? 180.375 142.496 180.062 1.00 25.99  ? 4341 SER A OG    1 
ATOM   21921 N N     . LYS A 1 4342 ? 180.044 140.212 176.301 1.00 25.98  ? 4342 LYS A N     1 
ATOM   21922 C CA    . LYS A 1 4342 ? 179.831 139.893 174.891 1.00 25.98  ? 4342 LYS A CA    1 
ATOM   21923 C C     . LYS A 1 4342 ? 178.861 138.729 174.727 1.00 25.98  ? 4342 LYS A C     1 
ATOM   21924 O O     . LYS A 1 4342 ? 177.966 138.768 173.868 1.00 25.98  ? 4342 LYS A O     1 
ATOM   21925 C CB    . LYS A 1 4342 ? 181.168 139.572 174.226 1.00 25.98  ? 4342 LYS A CB    1 
ATOM   21926 C CG    . LYS A 1 4342 ? 182.084 140.769 174.064 1.00 25.98  ? 4342 LYS A CG    1 
ATOM   21927 C CD    . LYS A 1 4342 ? 183.453 140.342 173.566 1.00 25.98  ? 4342 LYS A CD    1 
ATOM   21928 C CE    . LYS A 1 4342 ? 184.540 141.256 174.099 1.00 25.98  ? 4342 LYS A CE    1 
ATOM   21929 N NZ    . LYS A 1 4342 ? 184.934 142.282 173.097 1.00 25.98  ? 4342 LYS A NZ    1 
ATOM   21930 N N     . MET A 1 4343 ? 179.020 137.684 175.544 1.00 27.66  ? 4343 MET A N     1 
ATOM   21931 C CA    . MET A 1 4343 ? 178.101 136.552 175.473 1.00 27.66  ? 4343 MET A CA    1 
ATOM   21932 C C     . MET A 1 4343 ? 176.676 136.984 175.796 1.00 27.66  ? 4343 MET A C     1 
ATOM   21933 O O     . MET A 1 4343 ? 175.720 136.517 175.165 1.00 27.66  ? 4343 MET A O     1 
ATOM   21934 C CB    . MET A 1 4343 ? 178.555 135.436 176.413 1.00 27.66  ? 4343 MET A CB    1 
ATOM   21935 C CG    . MET A 1 4343 ? 179.949 134.911 176.121 1.00 27.66  ? 4343 MET A CG    1 
ATOM   21936 S SD    . MET A 1 4343 ? 180.113 133.143 176.417 1.00 27.66  ? 4343 MET A SD    1 
ATOM   21937 C CE    . MET A 1 4343 ? 178.845 132.503 175.330 1.00 27.66  ? 4343 MET A CE    1 
ATOM   21938 N N     . LEU A 1 4344 ? 176.512 137.872 176.780 1.00 28.80  ? 4344 LEU A N     1 
ATOM   21939 C CA    . LEU A 1 4344 ? 175.192 138.436 177.045 1.00 28.80  ? 4344 LEU A CA    1 
ATOM   21940 C C     . LEU A 1 4344 ? 174.674 139.236 175.858 1.00 28.80  ? 4344 LEU A C     1 
ATOM   21941 O O     . LEU A 1 4344 ? 173.502 139.107 175.486 1.00 28.80  ? 4344 LEU A O     1 
ATOM   21942 C CB    . LEU A 1 4344 ? 175.231 139.318 178.292 1.00 28.80  ? 4344 LEU A CB    1 
ATOM   21943 C CG    . LEU A 1 4344 ? 175.327 138.588 179.629 1.00 28.80  ? 4344 LEU A CG    1 
ATOM   21944 C CD1   . LEU A 1 4344 ? 175.537 139.573 180.766 1.00 28.80  ? 4344 LEU A CD1   1 
ATOM   21945 C CD2   . LEU A 1 4344 ? 174.064 137.784 179.844 1.00 28.80  ? 4344 LEU A CD2   1 
ATOM   21946 N N     . LYS A 1 4345 ? 175.527 140.061 175.252 1.00 28.72  ? 4345 LYS A N     1 
ATOM   21947 C CA    . LYS A 1 4345 ? 175.141 140.887 174.118 1.00 28.72  ? 4345 LYS A CA    1 
ATOM   21948 C C     . LYS A 1 4345 ? 174.742 140.071 172.898 1.00 28.72  ? 4345 LYS A C     1 
ATOM   21949 O O     . LYS A 1 4345 ? 174.001 140.580 172.051 1.00 28.72  ? 4345 LYS A O     1 
ATOM   21950 C CB    . LYS A 1 4345 ? 176.287 141.836 173.751 1.00 28.72  ? 4345 LYS A CB    1 
ATOM   21951 C CG    . LYS A 1 4345 ? 175.843 143.114 173.058 1.00 28.72  ? 4345 LYS A CG    1 
ATOM   21952 C CD    . LYS A 1 4345 ? 177.010 144.067 172.834 1.00 28.72  ? 4345 LYS A CD    1 
ATOM   21953 C CE    . LYS A 1 4345 ? 177.884 144.189 174.073 1.00 28.72  ? 4345 LYS A CE    1 
ATOM   21954 N NZ    . LYS A 1 4345 ? 179.176 144.870 173.777 1.00 28.72  ? 4345 LYS A NZ    1 
ATOM   21955 N N     . MET A 1 4346 ? 175.200 138.825 172.792 1.00 27.94  ? 4346 MET A N     1 
ATOM   21956 C CA    . MET A 1 4346 ? 174.835 137.950 171.679 1.00 27.94  ? 4346 MET A CA    1 
ATOM   21957 C C     . MET A 1 4346 ? 173.903 136.840 172.146 1.00 27.94  ? 4346 MET A C     1 
ATOM   21958 O O     . MET A 1 4346 ? 174.075 135.667 171.809 1.00 27.94  ? 4346 MET A O     1 
ATOM   21959 C CB    . MET A 1 4346 ? 176.058 137.338 171.008 1.00 27.94  ? 4346 MET A CB    1 
ATOM   21960 C CG    . MET A 1 4346 ? 176.949 138.320 170.286 1.00 27.94  ? 4346 MET A CG    1 
ATOM   21961 S SD    . MET A 1 4346 ? 178.391 137.479 169.616 1.00 27.94  ? 4346 MET A SD    1 
ATOM   21962 C CE    . MET A 1 4346 ? 177.647 136.520 168.302 1.00 27.94  ? 4346 MET A CE    1 
ATOM   21963 N N     . GLN A 1 4347 ? 172.896 137.195 172.936 1.00 30.78  ? 4347 GLN A N     1 
ATOM   21964 C CA    . GLN A 1 4347 ? 171.874 136.226 173.311 1.00 30.78  ? 4347 GLN A CA    1 
ATOM   21965 C C     . GLN A 1 4347 ? 170.547 136.563 172.642 1.00 30.78  ? 4347 GLN A C     1 
ATOM   21966 O O     . GLN A 1 4347 ? 169.798 135.672 172.242 0.00 30.78  ? 4347 GLN A O     1 
ATOM   21967 C CB    . GLN A 1 4347 ? 171.704 136.165 174.830 1.00 30.78  ? 4347 GLN A CB    1 
ATOM   21968 C CG    . GLN A 1 4347 ? 170.874 134.979 175.300 1.00 30.78  ? 4347 GLN A CG    1 
ATOM   21969 C CD    . GLN A 1 4347 ? 171.721 133.760 175.607 1.00 30.78  ? 4347 GLN A CD    1 
ATOM   21970 O OE1   . GLN A 1 4347 ? 172.671 133.455 174.886 1.00 30.78  ? 4347 GLN A OE1   1 
ATOM   21971 N NE2   . GLN A 1 4347 ? 171.375 133.051 176.674 1.00 30.78  ? 4347 GLN A NE2   1 
ATOM   21972 N N     . ALA A 1 4375 ? 157.001 138.922 175.021 1.00 72.89  ? 4375 ALA A N     1 
ATOM   21973 C CA    . ALA A 1 4375 ? 157.604 137.957 175.933 1.00 72.89  ? 4375 ALA A CA    1 
ATOM   21974 C C     . ALA A 1 4375 ? 158.461 138.662 176.979 1.00 72.89  ? 4375 ALA A C     1 
ATOM   21975 O O     . ALA A 1 4375 ? 158.646 138.160 178.087 1.00 72.89  ? 4375 ALA A O     1 
ATOM   21976 C CB    . ALA A 1 4375 ? 158.433 136.944 175.160 1.00 72.89  ? 4375 ALA A CB    1 
ATOM   21977 N N     . TRP A 1 4376 ? 158.981 139.833 176.613 1.00 75.88  ? 4376 TRP A N     1 
ATOM   21978 C CA    . TRP A 1 4376 ? 159.784 140.634 177.529 1.00 75.88  ? 4376 TRP A CA    1 
ATOM   21979 C C     . TRP A 1 4376 ? 158.949 141.394 178.551 1.00 75.88  ? 4376 TRP A C     1 
ATOM   21980 O O     . TRP A 1 4376 ? 159.507 141.900 179.531 1.00 75.88  ? 4376 TRP A O     1 
ATOM   21981 C CB    . TRP A 1 4376 ? 160.645 141.622 176.739 1.00 75.88  ? 4376 TRP A CB    1 
ATOM   21982 C CG    . TRP A 1 4376 ? 159.839 142.595 175.926 1.00 75.88  ? 4376 TRP A CG    1 
ATOM   21983 C CD1   . TRP A 1 4376 ? 159.416 142.428 174.640 1.00 75.88  ? 4376 TRP A CD1   1 
ATOM   21984 C CD2   . TRP A 1 4376 ? 159.326 143.863 176.355 1.00 75.88  ? 4376 TRP A CD2   1 
ATOM   21985 N NE1   . TRP A 1 4376 ? 158.693 143.522 174.232 1.00 75.88  ? 4376 TRP A NE1   1 
ATOM   21986 C CE2   . TRP A 1 4376 ? 158.620 144.416 175.268 1.00 75.88  ? 4376 TRP A CE2   1 
ATOM   21987 C CE3   . TRP A 1 4376 ? 159.401 144.587 177.547 1.00 75.88  ? 4376 TRP A CE3   1 
ATOM   21988 C CZ2   . TRP A 1 4376 ? 157.994 145.658 175.338 1.00 75.88  ? 4376 TRP A CZ2   1 
ATOM   21989 C CZ3   . TRP A 1 4376 ? 158.779 145.820 177.615 1.00 75.88  ? 4376 TRP A CZ3   1 
ATOM   21990 C CH2   . TRP A 1 4376 ? 158.085 146.343 176.518 1.00 75.88  ? 4376 TRP A CH2   1 
ATOM   21991 N N     . MET A 1 4377 ? 157.633 141.483 178.351 1.00 75.14  ? 4377 MET A N     1 
ATOM   21992 C CA    . MET A 1 4377 ? 156.814 142.312 179.227 1.00 75.14  ? 4377 MET A CA    1 
ATOM   21993 C C     . MET A 1 4377 ? 156.843 141.809 180.667 1.00 75.14  ? 4377 MET A C     1 
ATOM   21994 O O     . MET A 1 4377 ? 156.956 142.609 181.601 1.00 75.14  ? 4377 MET A O     1 
ATOM   21995 C CB    . MET A 1 4377 ? 155.382 142.393 178.687 1.00 75.14  ? 4377 MET A CB    1 
ATOM   21996 C CG    . MET A 1 4377 ? 154.560 141.119 178.807 1.00 75.14  ? 4377 MET A CG    1 
ATOM   21997 S SD    . MET A 1 4377 ? 153.246 141.025 177.575 1.00 75.14  ? 4377 MET A SD    1 
ATOM   21998 C CE    . MET A 1 4377 ? 154.017 139.992 176.329 1.00 75.14  ? 4377 MET A CE    1 
ATOM   21999 N N     . ARG A 1 4378 ? 156.788 140.490 180.870 1.00 71.74  ? 4378 ARG A N     1 
ATOM   22000 C CA    . ARG A 1 4378 ? 156.746 139.950 182.227 1.00 71.74  ? 4378 ARG A CA    1 
ATOM   22001 C C     . ARG A 1 4378 ? 158.053 140.207 182.969 1.00 71.74  ? 4378 ARG A C     1 
ATOM   22002 O O     . ARG A 1 4378 ? 158.049 140.665 184.121 1.00 71.74  ? 4378 ARG A O     1 
ATOM   22003 C CB    . ARG A 1 4378 ? 156.439 138.453 182.185 1.00 71.74  ? 4378 ARG A CB    1 
ATOM   22004 C CG    . ARG A 1 4378 ? 155.453 138.041 181.102 1.00 71.74  ? 4378 ARG A CG    1 
ATOM   22005 C CD    . ARG A 1 4378 ? 154.015 138.282 181.534 1.00 71.74  ? 4378 ARG A CD    1 
ATOM   22006 N NE    . ARG A 1 4378 ? 153.074 138.060 180.443 1.00 71.74  ? 4378 ARG A NE    1 
ATOM   22007 C CZ    . ARG A 1 4378 ? 152.114 138.906 180.095 1.00 71.74  ? 4378 ARG A CZ    1 
ATOM   22008 N NH1   . ARG A 1 4378 ? 151.937 140.050 180.735 1.00 71.74  ? 4378 ARG A NH1   1 
ATOM   22009 N NH2   . ARG A 1 4378 ? 151.313 138.597 179.080 1.00 71.74  ? 4378 ARG A NH2   1 
ATOM   22010 N N     . THR A 1 4379 ? 159.187 139.913 182.327 1.00 68.85  ? 4379 THR A N     1 
ATOM   22011 C CA    . THR A 1 4379 ? 160.471 140.094 182.993 1.00 68.85  ? 4379 THR A CA    1 
ATOM   22012 C C     . THR A 1 4379 ? 160.774 141.571 183.223 1.00 68.85  ? 4379 THR A C     1 
ATOM   22013 O O     . THR A 1 4379 ? 161.317 141.940 184.271 1.00 68.85  ? 4379 THR A O     1 
ATOM   22014 C CB    . THR A 1 4379 ? 161.590 139.414 182.197 1.00 68.85  ? 4379 THR A CB    1 
ATOM   22015 O OG1   . THR A 1 4379 ? 162.840 139.582 182.879 1.00 68.85  ? 4379 THR A OG1   1 
ATOM   22016 C CG2   . THR A 1 4379 ? 161.697 139.971 180.785 1.00 68.85  ? 4379 THR A CG2   1 
ATOM   22017 N N     . LEU A 1 4380 ? 160.412 142.438 182.273 1.00 68.58  ? 4380 LEU A N     1 
ATOM   22018 C CA    . LEU A 1 4380 ? 160.592 143.868 182.503 1.00 68.58  ? 4380 LEU A CA    1 
ATOM   22019 C C     . LEU A 1 4380 ? 159.698 144.368 183.630 1.00 68.58  ? 4380 LEU A C     1 
ATOM   22020 O O     . LEU A 1 4380 ? 160.121 145.203 184.437 1.00 68.58  ? 4380 LEU A O     1 
ATOM   22021 C CB    . LEU A 1 4380 ? 160.348 144.659 181.218 1.00 68.58  ? 4380 LEU A CB    1 
ATOM   22022 C CG    . LEU A 1 4380 ? 161.558 144.817 180.291 1.00 68.58  ? 4380 LEU A CG    1 
ATOM   22023 C CD1   . LEU A 1 4380 ? 162.631 145.637 180.991 1.00 68.58  ? 4380 LEU A CD1   1 
ATOM   22024 C CD2   . LEU A 1 4380 ? 162.137 143.489 179.827 1.00 68.58  ? 4380 LEU A CD2   1 
ATOM   22025 N N     . HIS A 1 4381 ? 158.464 143.864 183.714 1.00 66.52  ? 4381 HIS A N     1 
ATOM   22026 C CA    . HIS A 1 4381 ? 157.582 144.266 184.803 1.00 66.52  ? 4381 HIS A CA    1 
ATOM   22027 C C     . HIS A 1 4381 ? 158.156 143.857 186.151 1.00 66.52  ? 4381 HIS A C     1 
ATOM   22028 O O     . HIS A 1 4381 ? 158.168 144.651 187.099 1.00 66.52  ? 4381 HIS A O     1 
ATOM   22029 C CB    . HIS A 1 4381 ? 156.194 143.659 184.612 1.00 66.52  ? 4381 HIS A CB    1 
ATOM   22030 C CG    . HIS A 1 4381 ? 155.302 143.814 185.804 1.00 66.52  ? 4381 HIS A CG    1 
ATOM   22031 N ND1   . HIS A 1 4381 ? 155.291 144.953 186.581 1.00 66.52  ? 4381 HIS A ND1   1 
ATOM   22032 C CD2   . HIS A 1 4381 ? 154.400 142.971 186.359 1.00 66.52  ? 4381 HIS A CD2   1 
ATOM   22033 C CE1   . HIS A 1 4381 ? 154.417 144.806 187.561 1.00 66.52  ? 4381 HIS A CE1   1 
ATOM   22034 N NE2   . HIS A 1 4381 ? 153.862 143.613 187.448 1.00 66.52  ? 4381 HIS A NE2   1 
ATOM   22035 N N     . THR A 1 4382 ? 158.638 142.616 186.260 1.00 60.93  ? 4382 THR A N     1 
ATOM   22036 C CA    . THR A 1 4382 ? 159.163 142.172 187.548 1.00 60.93  ? 4382 THR A CA    1 
ATOM   22037 C C     . THR A 1 4382 ? 160.454 142.908 187.900 1.00 60.93  ? 4382 THR A C     1 
ATOM   22038 O O     . THR A 1 4382 ? 160.673 143.257 189.067 1.00 60.93  ? 4382 THR A O     1 
ATOM   22039 C CB    . THR A 1 4382 ? 159.356 140.650 187.565 1.00 60.93  ? 4382 THR A CB    1 
ATOM   22040 O OG1   . THR A 1 4382 ? 159.594 140.216 188.910 1.00 60.93  ? 4382 THR A OG1   1 
ATOM   22041 C CG2   . THR A 1 4382 ? 160.515 140.209 186.690 1.00 60.93  ? 4382 THR A CG2   1 
ATOM   22042 N N     . THR A 1 4383 ? 161.299 143.197 186.903 1.00 56.46  ? 4383 THR A N     1 
ATOM   22043 C CA    . THR A 1 4383 ? 162.514 143.959 187.170 1.00 56.46  ? 4383 THR A CA    1 
ATOM   22044 C C     . THR A 1 4383 ? 162.189 145.374 187.630 1.00 56.46  ? 4383 THR A C     1 
ATOM   22045 O O     . THR A 1 4383 ? 162.798 145.882 188.578 1.00 56.46  ? 4383 THR A O     1 
ATOM   22046 C CB    . THR A 1 4383 ? 163.399 143.994 185.924 1.00 56.46  ? 4383 THR A CB    1 
ATOM   22047 O OG1   . THR A 1 4383 ? 163.501 142.677 185.371 1.00 56.46  ? 4383 THR A OG1   1 
ATOM   22048 C CG2   . THR A 1 4383 ? 164.789 144.497 186.275 1.00 56.46  ? 4383 THR A CG2   1 
ATOM   22049 N N     . ALA A 1 4384 ? 161.224 146.024 186.977 1.00 54.18  ? 4384 ALA A N     1 
ATOM   22050 C CA    . ALA A 1 4384 ? 160.861 147.384 187.357 1.00 54.18  ? 4384 ALA A CA    1 
ATOM   22051 C C     . ALA A 1 4384 ? 160.216 147.421 188.737 1.00 54.18  ? 4384 ALA A C     1 
ATOM   22052 O O     . ALA A 1 4384 ? 160.458 148.348 189.517 1.00 54.18  ? 4384 ALA A O     1 
ATOM   22053 C CB    . ALA A 1 4384 ? 159.934 147.991 186.307 1.00 54.18  ? 4384 ALA A CB    1 
ATOM   22054 N N     . SER A 1 4385 ? 159.386 146.424 189.057 1.00 54.20  ? 4385 SER A N     1 
ATOM   22055 C CA    . SER A 1 4385 ? 158.798 146.363 190.392 1.00 54.20  ? 4385 SER A CA    1 
ATOM   22056 C C     . SER A 1 4385 ? 159.868 146.150 191.456 1.00 54.20  ? 4385 SER A C     1 
ATOM   22057 O O     . SER A 1 4385 ? 159.827 146.774 192.525 1.00 54.20  ? 4385 SER A O     1 
ATOM   22058 C CB    . SER A 1 4385 ? 157.747 145.255 190.453 1.00 54.20  ? 4385 SER A CB    1 
ATOM   22059 O OG    . SER A 1 4385 ? 158.320 143.993 190.163 1.00 54.20  ? 4385 SER A OG    1 
ATOM   22060 N N     . ASN A 1 4386 ? 160.840 145.276 191.180 1.00 52.62  ? 4386 ASN A N     1 
ATOM   22061 C CA    . ASN A 1 4386 ? 161.935 145.077 192.122 1.00 52.62  ? 4386 ASN A CA    1 
ATOM   22062 C C     . ASN A 1 4386 ? 162.751 146.351 192.291 1.00 52.62  ? 4386 ASN A C     1 
ATOM   22063 O O     . ASN A 1 4386 ? 163.198 146.668 193.399 1.00 52.62  ? 4386 ASN A O     1 
ATOM   22064 C CB    . ASN A 1 4386 ? 162.822 143.923 191.658 1.00 52.62  ? 4386 ASN A CB    1 
ATOM   22065 C CG    . ASN A 1 4386 ? 162.124 142.581 191.751 1.00 52.62  ? 4386 ASN A CG    1 
ATOM   22066 O OD1   . ASN A 1 4386 ? 161.164 142.420 192.503 1.00 52.62  ? 4386 ASN A OD1   1 
ATOM   22067 N ND2   . ASN A 1 4386 ? 162.604 141.610 190.984 1.00 52.62  ? 4386 ASN A ND2   1 
ATOM   22068 N N     . TRP A 1 4387 ? 162.963 147.093 191.202 1.00 46.05  ? 4387 TRP A N     1 
ATOM   22069 C CA    . TRP A 1 4387 ? 163.679 148.361 191.299 1.00 46.05  ? 4387 TRP A CA    1 
ATOM   22070 C C     . TRP A 1 4387 ? 162.905 149.373 192.136 1.00 46.05  ? 4387 TRP A C     1 
ATOM   22071 O O     . TRP A 1 4387 ? 163.494 150.086 192.957 1.00 46.05  ? 4387 TRP A O     1 
ATOM   22072 C CB    . TRP A 1 4387 ? 163.953 148.917 189.903 1.00 46.05  ? 4387 TRP A CB    1 
ATOM   22073 C CG    . TRP A 1 4387 ? 165.051 148.203 189.190 1.00 46.05  ? 4387 TRP A CG    1 
ATOM   22074 C CD1   . TRP A 1 4387 ? 165.916 147.293 189.721 1.00 46.05  ? 4387 TRP A CD1   1 
ATOM   22075 C CD2   . TRP A 1 4387 ? 165.407 148.338 187.811 1.00 46.05  ? 4387 TRP A CD2   1 
ATOM   22076 N NE1   . TRP A 1 4387 ? 166.788 146.851 188.758 1.00 46.05  ? 4387 TRP A NE1   1 
ATOM   22077 C CE2   . TRP A 1 4387 ? 166.497 147.478 187.575 1.00 46.05  ? 4387 TRP A CE2   1 
ATOM   22078 C CE3   . TRP A 1 4387 ? 164.910 149.103 186.752 1.00 46.05  ? 4387 TRP A CE3   1 
ATOM   22079 C CZ2   . TRP A 1 4387 ? 167.098 147.362 186.326 1.00 46.05  ? 4387 TRP A CZ2   1 
ATOM   22080 C CZ3   . TRP A 1 4387 ? 165.508 148.985 185.513 1.00 46.05  ? 4387 TRP A CZ3   1 
ATOM   22081 C CH2   . TRP A 1 4387 ? 166.590 148.122 185.310 1.00 46.05  ? 4387 TRP A CH2   1 
ATOM   22082 N N     . LEU A 1 4388 ? 161.587 149.453 191.938 1.00 45.88  ? 4388 LEU A N     1 
ATOM   22083 C CA    . LEU A 1 4388 ? 160.770 150.360 192.739 1.00 45.88  ? 4388 LEU A CA    1 
ATOM   22084 C C     . LEU A 1 4388 ? 160.827 149.991 194.214 1.00 45.88  ? 4388 LEU A C     1 
ATOM   22085 O O     . LEU A 1 4388 ? 160.871 150.872 195.081 1.00 45.88  ? 4388 LEU A O     1 
ATOM   22086 C CB    . LEU A 1 4388 ? 159.326 150.353 192.238 1.00 45.88  ? 4388 LEU A CB    1 
ATOM   22087 C CG    . LEU A 1 4388 ? 159.061 151.049 190.904 1.00 45.88  ? 4388 LEU A CG    1 
ATOM   22088 C CD1   . LEU A 1 4388 ? 157.595 151.424 190.782 1.00 45.88  ? 4388 LEU A CD1   1 
ATOM   22089 C CD2   . LEU A 1 4388 ? 159.935 152.281 190.773 1.00 45.88  ? 4388 LEU A CD2   1 
ATOM   22090 N N     . HIS A 1 4389 ? 160.816 148.693 194.522 1.00 50.86  ? 4389 HIS A N     1 
ATOM   22091 C CA    . HIS A 1 4389 ? 161.004 148.272 195.906 1.00 50.86  ? 4389 HIS A CA    1 
ATOM   22092 C C     . HIS A 1 4389 ? 162.398 148.619 196.413 1.00 50.86  ? 4389 HIS A C     1 
ATOM   22093 O O     . HIS A 1 4389 ? 162.573 148.912 197.601 1.00 50.86  ? 4389 HIS A O     1 
ATOM   22094 C CB    . HIS A 1 4389 ? 160.745 146.772 196.044 1.00 50.86  ? 4389 HIS A CB    1 
ATOM   22095 C CG    . HIS A 1 4389 ? 159.326 146.379 195.782 1.00 50.86  ? 4389 HIS A CG    1 
ATOM   22096 N ND1   . HIS A 1 4389 ? 158.859 146.066 194.524 1.00 50.86  ? 4389 HIS A ND1   1 
ATOM   22097 C CD2   . HIS A 1 4389 ? 158.269 146.248 196.618 1.00 50.86  ? 4389 HIS A CD2   1 
ATOM   22098 C CE1   . HIS A 1 4389 ? 157.577 145.760 194.595 1.00 50.86  ? 4389 HIS A CE1   1 
ATOM   22099 N NE2   . HIS A 1 4389 ? 157.194 145.862 195.855 1.00 50.86  ? 4389 HIS A NE2   1 
ATOM   22100 N N     . LEU A 1 4390 ? 163.399 148.593 195.531 1.00 44.70  ? 4390 LEU A N     1 
ATOM   22101 C CA    . LEU A 1 4390 ? 164.772 148.877 195.933 1.00 44.70  ? 4390 LEU A CA    1 
ATOM   22102 C C     . LEU A 1 4390 ? 165.015 150.375 196.080 1.00 44.70  ? 4390 LEU A C     1 
ATOM   22103 O O     . LEU A 1 4390 ? 165.539 150.828 197.103 1.00 44.70  ? 4390 LEU A O     1 
ATOM   22104 C CB    . LEU A 1 4390 ? 165.745 148.278 194.916 1.00 44.70  ? 4390 LEU A CB    1 
ATOM   22105 C CG    . LEU A 1 4390 ? 167.185 148.051 195.381 1.00 44.70  ? 4390 LEU A CG    1 
ATOM   22106 C CD1   . LEU A 1 4390 ? 167.225 147.097 196.563 1.00 44.70  ? 4390 LEU A CD1   1 
ATOM   22107 C CD2   . LEU A 1 4390 ? 168.041 147.533 194.236 1.00 44.70  ? 4390 LEU A CD2   1 
ATOM   22108 N N     . ILE A 1 4391 ? 164.649 151.151 195.068 1.00 39.77  ? 4391 ILE A N     1 
ATOM   22109 C CA    . ILE A 1 4391 ? 164.882 152.599 195.100 1.00 39.77  ? 4391 ILE A CA    1 
ATOM   22110 C C     . ILE A 1 4391 ? 164.010 153.226 196.180 1.00 39.77  ? 4391 ILE A C     1 
ATOM   22111 O O     . ILE A 1 4391 ? 162.808 152.912 196.258 1.00 39.77  ? 4391 ILE A O     1 
ATOM   22112 C CB    . ILE A 1 4391 ? 164.591 153.212 193.729 1.00 39.77  ? 4391 ILE A CB    1 
ATOM   22113 C CG1   . ILE A 1 4391 ? 165.528 152.626 192.673 1.00 39.77  ? 4391 ILE A CG1   1 
ATOM   22114 C CG2   . ILE A 1 4391 ? 164.736 154.719 193.775 1.00 39.77  ? 4391 ILE A CG2   1 
ATOM   22115 C CD1   . ILE A 1 4391 ? 165.295 153.172 191.283 1.00 39.77  ? 4391 ILE A CD1   1 
ATOM   22116 N N     . PRO A 1 4392 ? 164.555 154.093 197.034 1.00 39.18  ? 4392 PRO A N     1 
ATOM   22117 C CA    . PRO A 1 4392 ? 163.727 154.743 198.056 1.00 39.18  ? 4392 PRO A CA    1 
ATOM   22118 C C     . PRO A 1 4392 ? 162.629 155.588 197.428 1.00 39.18  ? 4392 PRO A C     1 
ATOM   22119 O O     . PRO A 1 4392 ? 162.778 156.124 196.328 1.00 39.18  ? 4392 PRO A O     1 
ATOM   22120 C CB    . PRO A 1 4392 ? 164.730 155.607 198.827 1.00 39.18  ? 4392 PRO A CB    1 
ATOM   22121 C CG    . PRO A 1 4392 ? 166.047 154.948 198.595 1.00 39.18  ? 4392 PRO A CG    1 
ATOM   22122 C CD    . PRO A 1 4392 ? 165.983 154.410 197.197 1.00 39.18  ? 4392 PRO A CD    1 
ATOM   22123 N N     . GLN A 1 4393 ? 161.508 155.692 198.146 1.00 41.94  ? 4393 GLN A N     1 
ATOM   22124 C CA    . GLN A 1 4393 ? 160.307 156.294 197.576 1.00 41.94  ? 4393 GLN A CA    1 
ATOM   22125 C C     . GLN A 1 4393 ? 160.530 157.756 197.207 1.00 41.94  ? 4393 GLN A C     1 
ATOM   22126 O O     . GLN A 1 4393 ? 160.508 158.122 196.027 1.00 41.94  ? 4393 GLN A O     1 
ATOM   22127 C CB    . GLN A 1 4393 ? 159.139 156.153 198.553 1.00 41.94  ? 4393 GLN A CB    1 
ATOM   22128 C CG    . GLN A 1 4393 ? 158.939 154.741 199.074 1.00 41.94  ? 4393 GLN A CG    1 
ATOM   22129 C CD    . GLN A 1 4393 ? 157.560 154.529 199.665 1.00 41.94  ? 4393 GLN A CD    1 
ATOM   22130 O OE1   . GLN A 1 4393 ? 156.797 155.478 199.847 1.00 41.94  ? 4393 GLN A OE1   1 
ATOM   22131 N NE2   . GLN A 1 4393 ? 157.232 153.278 199.966 1.00 41.94  ? 4393 GLN A NE2   1 
ATOM   22132 N N     . THR A 1 4394 ? 160.757 158.611 198.202 1.00 41.36  ? 4394 THR A N     1 
ATOM   22133 C CA    . THR A 1 4394 ? 160.860 160.039 197.934 1.00 41.36  ? 4394 THR A CA    1 
ATOM   22134 C C     . THR A 1 4394 ? 161.531 160.735 199.109 1.00 41.36  ? 4394 THR A C     1 
ATOM   22135 O O     . THR A 1 4394 ? 161.198 160.474 200.267 1.00 41.36  ? 4394 THR A O     1 
ATOM   22136 C CB    . THR A 1 4394 ? 159.479 160.661 197.675 1.00 41.36  ? 4394 THR A CB    1 
ATOM   22137 O OG1   . THR A 1 4394 ? 158.902 160.089 196.493 1.00 41.36  ? 4394 THR A OG1   1 
ATOM   22138 C CG2   . THR A 1 4394 ? 159.588 162.168 197.494 1.00 41.36  ? 4394 THR A CG2   1 
ATOM   22139 N N     . LEU A 1 4395 ? 162.476 161.619 198.795 1.00 41.72  ? 4395 LEU A N     1 
ATOM   22140 C CA    . LEU A 1 4395 ? 163.073 162.527 199.763 1.00 41.72  ? 4395 LEU A CA    1 
ATOM   22141 C C     . LEU A 1 4395 ? 162.649 163.948 199.420 1.00 41.72  ? 4395 LEU A C     1 
ATOM   22142 O O     . LEU A 1 4395 ? 162.643 164.339 198.248 1.00 41.72  ? 4395 LEU A O     1 
ATOM   22143 C CB    . LEU A 1 4395 ? 164.606 162.399 199.783 1.00 41.72  ? 4395 LEU A CB    1 
ATOM   22144 C CG    . LEU A 1 4395 ? 165.443 162.807 198.565 1.00 41.72  ? 4395 LEU A CG    1 
ATOM   22145 C CD1   . LEU A 1 4395 ? 165.855 164.269 198.624 1.00 41.72  ? 4395 LEU A CD1   1 
ATOM   22146 C CD2   . LEU A 1 4395 ? 166.667 161.921 198.444 1.00 41.72  ? 4395 LEU A CD2   1 
ATOM   22147 N N     . SER A 1 4396 ? 162.281 164.714 200.440 1.00 48.84  ? 4396 SER A N     1 
ATOM   22148 C CA    . SER A 1 4396 ? 161.731 166.046 200.250 1.00 48.84  ? 4396 SER A CA    1 
ATOM   22149 C C     . SER A 1 4396 ? 162.787 167.111 200.512 1.00 48.84  ? 4396 SER A C     1 
ATOM   22150 O O     . SER A 1 4396 ? 163.723 166.910 201.290 1.00 48.84  ? 4396 SER A O     1 
ATOM   22151 C CB    . SER A 1 4396 ? 160.528 166.274 201.168 1.00 48.84  ? 4396 SER A CB    1 
ATOM   22152 O OG    . SER A 1 4396 ? 160.923 166.294 202.529 1.00 48.84  ? 4396 SER A OG    1 
ATOM   22153 N N     . HIS A 1 4397 ? 162.624 168.253 199.848 1.00 51.13  ? 4397 HIS A N     1 
ATOM   22154 C CA    . HIS A 1 4397 ? 163.513 169.390 200.059 1.00 51.13  ? 4397 HIS A CA    1 
ATOM   22155 C C     . HIS A 1 4397 ? 163.230 169.991 201.428 1.00 51.13  ? 4397 HIS A C     1 
ATOM   22156 O O     . HIS A 1 4397 ? 162.263 170.740 201.595 1.00 51.13  ? 4397 HIS A O     1 
ATOM   22157 C CB    . HIS A 1 4397 ? 163.320 170.442 198.970 1.00 51.13  ? 4397 HIS A CB    1 
ATOM   22158 C CG    . HIS A 1 4397 ? 163.337 169.899 197.576 1.00 51.13  ? 4397 HIS A CG    1 
ATOM   22159 N ND1   . HIS A 1 4397 ? 162.973 170.656 196.484 1.00 51.13  ? 4397 HIS A ND1   1 
ATOM   22160 C CD2   . HIS A 1 4397 ? 163.688 168.685 197.090 1.00 51.13  ? 4397 HIS A CD2   1 
ATOM   22161 C CE1   . HIS A 1 4397 ? 163.087 169.930 195.387 1.00 51.13  ? 4397 HIS A CE1   1 
ATOM   22162 N NE2   . HIS A 1 4397 ? 163.519 168.729 195.727 1.00 51.13  ? 4397 HIS A NE2   1 
ATOM   22163 N N     . LEU A 1 4398 ? 164.066 169.669 202.410 1.00 57.51  ? 4398 LEU A N     1 
ATOM   22164 C CA    . LEU A 1 4398 ? 163.992 170.283 203.731 1.00 57.51  ? 4398 LEU A CA    1 
ATOM   22165 C C     . LEU A 1 4398 ? 165.229 171.168 203.844 1.00 57.51  ? 4398 LEU A C     1 
ATOM   22166 O O     . LEU A 1 4398 ? 166.269 170.764 204.365 1.00 57.51  ? 4398 LEU A O     1 
ATOM   22167 C CB    . LEU A 1 4398 ? 163.915 169.212 204.844 1.00 57.51  ? 4398 LEU A CB    1 
ATOM   22168 C CG    . LEU A 1 4398 ? 163.613 169.645 206.283 1.00 57.51  ? 4398 LEU A CG    1 
ATOM   22169 C CD1   . LEU A 1 4398 ? 162.929 168.507 207.023 1.00 57.51  ? 4398 LEU A CD1   1 
ATOM   22170 C CD2   . LEU A 1 4398 ? 164.861 170.079 207.037 1.00 57.51  ? 4398 LEU A CD2   1 
ATOM   22171 N N     . LYS A 1 4399 ? 165.105 172.390 203.337 1.00 52.59  ? 4399 LYS A N     1 
ATOM   22172 C CA    . LYS A 1 4399 ? 166.244 173.272 203.116 1.00 52.59  ? 4399 LYS A CA    1 
ATOM   22173 C C     . LYS A 1 4399 ? 165.739 174.711 203.075 1.00 52.59  ? 4399 LYS A C     1 
ATOM   22174 O O     . LYS A 1 4399 ? 164.612 175.005 203.490 1.00 52.59  ? 4399 LYS A O     1 
ATOM   22175 C CB    . LYS A 1 4399 ? 166.975 172.899 201.820 1.00 52.59  ? 4399 LYS A CB    1 
ATOM   22176 C CG    . LYS A 1 4399 ? 167.932 171.717 201.917 1.00 52.59  ? 4399 LYS A CG    1 
ATOM   22177 C CD    . LYS A 1 4399 ? 168.917 171.879 203.061 1.00 52.59  ? 4399 LYS A CD    1 
ATOM   22178 C CE    . LYS A 1 4399 ? 169.735 170.615 203.258 1.00 52.59  ? 4399 LYS A CE    1 
ATOM   22179 N NZ    . LYS A 1 4399 ? 169.048 169.658 204.162 1.00 52.59  ? 4399 LYS A NZ    1 
ATOM   22180 N N     . ARG A 1 4400 ? 166.591 175.611 202.576 1.00 55.92  ? 4400 ARG A N     1 
ATOM   22181 C CA    . ARG A 1 4400 ? 166.237 177.012 202.333 1.00 55.92  ? 4400 ARG A CA    1 
ATOM   22182 C C     . ARG A 1 4400 ? 165.788 177.714 203.612 1.00 55.92  ? 4400 ARG A C     1 
ATOM   22183 O O     . ARG A 1 4400 ? 164.733 178.349 203.658 1.00 55.92  ? 4400 ARG A O     1 
ATOM   22184 C CB    . ARG A 1 4400 ? 165.170 177.134 201.243 1.00 55.92  ? 4400 ARG A CB    1 
ATOM   22185 C CG    . ARG A 1 4400 ? 165.220 178.447 200.476 1.00 55.92  ? 4400 ARG A CG    1 
ATOM   22186 C CD    . ARG A 1 4400 ? 164.517 178.336 199.132 1.00 55.92  ? 4400 ARG A CD    1 
ATOM   22187 N NE    . ARG A 1 4400 ? 165.143 177.348 198.260 1.00 55.92  ? 4400 ARG A NE    1 
ATOM   22188 C CZ    . ARG A 1 4400 ? 166.262 177.550 197.578 1.00 55.92  ? 4400 ARG A CZ    1 
ATOM   22189 N NH1   . ARG A 1 4400 ? 166.910 178.703 197.636 1.00 55.92  ? 4400 ARG A NH1   1 
ATOM   22190 N NH2   . ARG A 1 4400 ? 166.742 176.572 196.816 1.00 55.92  ? 4400 ARG A NH2   1 
ATOM   22191 N N     . THR A 1 4401 ? 166.594 177.597 204.662 1.00 62.70  ? 4401 THR A N     1 
ATOM   22192 C CA    . THR A 1 4401 ? 166.354 178.349 205.885 1.00 62.70  ? 4401 THR A CA    1 
ATOM   22193 C C     . THR A 1 4401 ? 167.048 179.702 205.795 1.00 62.70  ? 4401 THR A C     1 
ATOM   22194 O O     . THR A 1 4401 ? 168.231 179.779 205.451 1.00 62.70  ? 4401 THR A O     1 
ATOM   22195 C CB    . THR A 1 4401 ? 166.857 177.574 207.102 1.00 62.70  ? 4401 THR A CB    1 
ATOM   22196 O OG1   . THR A 1 4401 ? 166.391 176.221 207.035 1.00 62.70  ? 4401 THR A OG1   1 
ATOM   22197 C CG2   . THR A 1 4401 ? 166.354 178.218 208.386 1.00 62.70  ? 4401 THR A CG2   1 
ATOM   22198 N N     . VAL A 1 4402 ? 166.306 180.770 206.096 1.00 69.47  ? 4402 VAL A N     1 
ATOM   22199 C CA    . VAL A 1 4402 ? 166.879 182.112 206.034 1.00 69.47  ? 4402 VAL A CA    1 
ATOM   22200 C C     . VAL A 1 4402 ? 168.019 182.249 207.033 1.00 69.47  ? 4402 VAL A C     1 
ATOM   22201 O O     . VAL A 1 4402 ? 169.084 182.793 206.714 1.00 69.47  ? 4402 VAL A O     1 
ATOM   22202 C CB    . VAL A 1 4402 ? 165.788 183.173 206.269 1.00 69.47  ? 4402 VAL A CB    1 
ATOM   22203 C CG1   . VAL A 1 4402 ? 166.381 184.571 206.186 1.00 69.47  ? 4402 VAL A CG1   1 
ATOM   22204 C CG2   . VAL A 1 4402 ? 164.660 183.005 205.263 1.00 69.47  ? 4402 VAL A CG2   1 
ATOM   22205 N N     . GLU A 1 4403 ? 167.817 181.762 208.252 1.00 71.83  ? 4403 GLU A N     1 
ATOM   22206 C CA    . GLU A 1 4403 ? 168.879 181.750 209.244 1.00 71.83  ? 4403 GLU A CA    1 
ATOM   22207 C C     . GLU A 1 4403 ? 169.891 180.658 208.918 1.00 71.83  ? 4403 GLU A C     1 
ATOM   22208 O O     . GLU A 1 4403 ? 169.539 179.581 208.429 1.00 71.83  ? 4403 GLU A O     1 
ATOM   22209 C CB    . GLU A 1 4403 ? 168.302 181.537 210.644 1.00 71.83  ? 4403 GLU A CB    1 
ATOM   22210 C CG    . GLU A 1 4403 ? 169.282 181.797 211.780 1.00 71.83  ? 4403 GLU A CG    1 
ATOM   22211 C CD    . GLU A 1 4403 ? 170.110 180.577 212.134 1.00 71.83  ? 4403 GLU A CD    1 
ATOM   22212 O OE1   . GLU A 1 4403 ? 169.615 179.446 211.946 1.00 71.83  ? 4403 GLU A OE1   1 
ATOM   22213 O OE2   . GLU A 1 4403 ? 171.255 180.750 212.600 1.00 71.83  ? 4403 GLU A OE2   1 
ATOM   22214 N N     . ASN A 1 4404 ? 171.161 180.956 209.185 1.00 66.59  ? 4404 ASN A N     1 
ATOM   22215 C CA    . ASN A 1 4404 ? 172.292 180.055 208.983 1.00 66.59  ? 4404 ASN A CA    1 
ATOM   22216 C C     . ASN A 1 4404 ? 172.452 179.627 207.530 1.00 66.59  ? 4404 ASN A C     1 
ATOM   22217 O O     . ASN A 1 4404 ? 172.965 178.532 207.265 1.00 66.59  ? 4404 ASN A O     1 
ATOM   22218 C CB    . ASN A 1 4404 ? 172.194 178.814 209.879 1.00 66.59  ? 4404 ASN A CB    1 
ATOM   22219 C CG    . ASN A 1 4404 ? 173.555 178.277 210.281 1.00 66.59  ? 4404 ASN A CG    1 
ATOM   22220 O OD1   . ASN A 1 4404 ? 174.588 178.805 209.872 1.00 66.59  ? 4404 ASN A OD1   1 
ATOM   22221 N ND2   . ASN A 1 4404 ? 173.561 177.231 211.098 1.00 66.59  ? 4404 ASN A ND2   1 
ATOM   22222 N N     . ILE A 1 4405 ? 172.019 180.455 206.576 1.00 54.08  ? 4405 ILE A N     1 
ATOM   22223 C CA    . ILE A 1 4405 ? 172.303 180.198 205.170 1.00 54.08  ? 4405 ILE A CA    1 
ATOM   22224 C C     . ILE A 1 4405 ? 173.775 180.442 204.861 1.00 54.08  ? 4405 ILE A C     1 
ATOM   22225 O O     . ILE A 1 4405 ? 174.286 179.962 203.843 1.00 54.08  ? 4405 ILE A O     1 
ATOM   22226 C CB    . ILE A 1 4405 ? 171.385 181.070 204.288 1.00 54.08  ? 4405 ILE A CB    1 
ATOM   22227 C CG1   . ILE A 1 4405 ? 171.600 180.787 202.798 1.00 54.08  ? 4405 ILE A CG1   1 
ATOM   22228 C CG2   . ILE A 1 4405 ? 171.611 182.544 204.582 1.00 54.08  ? 4405 ILE A CG2   1 
ATOM   22229 C CD1   . ILE A 1 4405 ? 171.209 179.393 202.378 1.00 54.08  ? 4405 ILE A CD1   1 
ATOM   22230 N N     . LYS A 1 4406 ? 174.481 181.157 205.741 1.00 49.69  ? 4406 LYS A N     1 
ATOM   22231 C CA    . LYS A 1 4406 ? 175.875 181.503 205.495 1.00 49.69  ? 4406 LYS A CA    1 
ATOM   22232 C C     . LYS A 1 4406 ? 176.788 180.285 205.454 1.00 49.69  ? 4406 LYS A C     1 
ATOM   22233 O O     . LYS A 1 4406 ? 177.904 180.382 204.932 1.00 49.69  ? 4406 LYS A O     1 
ATOM   22234 C CB    . LYS A 1 4406 ? 176.369 182.480 206.565 1.00 49.69  ? 4406 LYS A CB    1 
ATOM   22235 C CG    . LYS A 1 4406 ? 175.629 183.809 206.591 1.00 49.69  ? 4406 LYS A CG    1 
ATOM   22236 C CD    . LYS A 1 4406 ? 174.515 183.806 207.626 1.00 49.69  ? 4406 LYS A CD    1 
ATOM   22237 C CE    . LYS A 1 4406 ? 173.782 185.138 207.652 1.00 49.69  ? 4406 LYS A CE    1 
ATOM   22238 N NZ    . LYS A 1 4406 ? 172.683 185.148 208.656 1.00 49.69  ? 4406 LYS A NZ    1 
ATOM   22239 N N     . ASP A 1 4407 ? 176.354 179.150 205.989 1.00 43.34  ? 4407 ASP A N     1 
ATOM   22240 C CA    . ASP A 1 4407 ? 177.190 177.956 205.955 1.00 43.34  ? 4407 ASP A CA    1 
ATOM   22241 C C     . ASP A 1 4407 ? 177.299 177.441 204.524 1.00 43.34  ? 4407 ASP A C     1 
ATOM   22242 O O     . ASP A 1 4407 ? 176.277 177.118 203.908 1.00 43.34  ? 4407 ASP A O     1 
ATOM   22243 C CB    . ASP A 1 4407 ? 176.623 176.869 206.863 1.00 43.34  ? 4407 ASP A CB    1 
ATOM   22244 C CG    . ASP A 1 4407 ? 176.975 177.083 208.321 1.00 43.34  ? 4407 ASP A CG    1 
ATOM   22245 O OD1   . ASP A 1 4407 ? 178.019 177.712 208.596 1.00 43.34  ? 4407 ASP A OD1   1 
ATOM   22246 O OD2   . ASP A 1 4407 ? 176.214 176.614 209.193 1.00 43.34  ? 4407 ASP A OD2   1 
ATOM   22247 N N     . PRO A 1 4408 ? 178.507 177.360 203.961 1.00 30.90  ? 4408 PRO A N     1 
ATOM   22248 C CA    . PRO A 1 4408 ? 178.637 176.815 202.600 1.00 30.90  ? 4408 PRO A CA    1 
ATOM   22249 C C     . PRO A 1 4408 ? 178.209 175.364 202.501 1.00 30.90  ? 4408 PRO A C     1 
ATOM   22250 O O     . PRO A 1 4408 ? 177.710 174.938 201.450 1.00 30.90  ? 4408 PRO A O     1 
ATOM   22251 C CB    . PRO A 1 4408 ? 180.130 176.997 202.291 1.00 30.90  ? 4408 PRO A CB    1 
ATOM   22252 C CG    . PRO A 1 4408 ? 180.633 177.966 203.325 1.00 30.90  ? 4408 PRO A CG    1 
ATOM   22253 C CD    . PRO A 1 4408 ? 179.806 177.733 204.535 1.00 30.90  ? 4408 PRO A CD    1 
ATOM   22254 N N     . LEU A 1 4409 ? 178.395 174.589 203.573 1.00 30.48  ? 4409 LEU A N     1 
ATOM   22255 C CA    . LEU A 1 4409 ? 177.923 173.210 203.577 1.00 30.48  ? 4409 LEU A CA    1 
ATOM   22256 C C     . LEU A 1 4409 ? 176.415 173.152 203.395 1.00 30.48  ? 4409 LEU A C     1 
ATOM   22257 O O     . LEU A 1 4409 ? 175.899 172.258 202.716 1.00 30.48  ? 4409 LEU A O     1 
ATOM   22258 C CB    . LEU A 1 4409 ? 178.329 172.514 204.874 1.00 30.48  ? 4409 LEU A CB    1 
ATOM   22259 C CG    . LEU A 1 4409 ? 179.822 172.439 205.185 1.00 30.48  ? 4409 LEU A CG    1 
ATOM   22260 C CD1   . LEU A 1 4409 ? 180.039 172.075 206.641 1.00 30.48  ? 4409 LEU A CD1   1 
ATOM   22261 C CD2   . LEU A 1 4409 ? 180.494 171.428 204.275 1.00 30.48  ? 4409 LEU A CD2   1 
ATOM   22262 N N     . PHE A 1 4410 ? 175.691 174.096 203.996 1.00 39.39  ? 4410 PHE A N     1 
ATOM   22263 C CA    . PHE A 1 4410 ? 174.239 174.110 203.871 1.00 39.39  ? 4410 PHE A CA    1 
ATOM   22264 C C     . PHE A 1 4410 ? 173.814 174.333 202.425 1.00 39.39  ? 4410 PHE A C     1 
ATOM   22265 O O     . PHE A 1 4410 ? 172.933 173.639 201.913 1.00 39.39  ? 4410 PHE A O     1 
ATOM   22266 C CB    . PHE A 1 4410 ? 173.645 175.179 204.788 1.00 39.39  ? 4410 PHE A CB    1 
ATOM   22267 C CG    . PHE A 1 4410 ? 172.147 175.237 204.755 1.00 39.39  ? 4410 PHE A CG    1 
ATOM   22268 C CD1   . PHE A 1 4410 ? 171.391 174.278 205.407 1.00 39.39  ? 4410 PHE A CD1   1 
ATOM   22269 C CD2   . PHE A 1 4410 ? 171.494 176.254 204.083 1.00 39.39  ? 4410 PHE A CD2   1 
ATOM   22270 C CE1   . PHE A 1 4410 ? 170.014 174.329 205.381 1.00 39.39  ? 4410 PHE A CE1   1 
ATOM   22271 C CE2   . PHE A 1 4410 ? 170.117 176.311 204.058 1.00 39.39  ? 4410 PHE A CE2   1 
ATOM   22272 C CZ    . PHE A 1 4410 ? 169.376 175.346 204.705 1.00 39.39  ? 4410 PHE A CZ    1 
ATOM   22273 N N     . ARG A 1 4411 ? 174.442 175.295 201.743 1.00 30.71  ? 4411 ARG A N     1 
ATOM   22274 C CA    . ARG A 1 4411 ? 174.107 175.542 200.342 1.00 30.71  ? 4411 ARG A CA    1 
ATOM   22275 C C     . ARG A 1 4411 ? 174.487 174.357 199.462 1.00 30.71  ? 4411 ARG A C     1 
ATOM   22276 O O     . ARG A 1 4411 ? 173.732 173.971 198.558 1.00 30.71  ? 4411 ARG A O     1 
ATOM   22277 C CB    . ARG A 1 4411 ? 174.799 176.811 199.849 1.00 30.71  ? 4411 ARG A CB    1 
ATOM   22278 C CG    . ARG A 1 4411 ? 174.297 178.092 200.489 1.00 30.71  ? 4411 ARG A CG    1 
ATOM   22279 C CD    . ARG A 1 4411 ? 175.068 179.291 199.969 1.00 30.71  ? 4411 ARG A CD    1 
ATOM   22280 N NE    . ARG A 1 4411 ? 176.452 179.280 200.423 1.00 30.71  ? 4411 ARG A NE    1 
ATOM   22281 C CZ    . ARG A 1 4411 ? 177.381 180.132 200.011 1.00 30.71  ? 4411 ARG A CZ    1 
ATOM   22282 N NH1   . ARG A 1 4411 ? 177.109 181.076 199.126 1.00 30.71  ? 4411 ARG A NH1   1 
ATOM   22283 N NH2   . ARG A 1 4411 ? 178.614 180.033 200.499 1.00 30.71  ? 4411 ARG A NH2   1 
ATOM   22284 N N     . PHE A 1 4412 ? 175.660 173.770 199.707 1.00 27.37  ? 4412 PHE A N     1 
ATOM   22285 C CA    . PHE A 1 4412 ? 176.087 172.624 198.912 1.00 27.37  ? 4412 PHE A CA    1 
ATOM   22286 C C     . PHE A 1 4412 ? 175.130 171.450 199.079 1.00 27.37  ? 4412 PHE A C     1 
ATOM   22287 O O     . PHE A 1 4412 ? 174.725 170.823 198.092 1.00 27.37  ? 4412 PHE A O     1 
ATOM   22288 C CB    . PHE A 1 4412 ? 177.506 172.221 199.306 1.00 27.37  ? 4412 PHE A CB    1 
ATOM   22289 C CG    . PHE A 1 4412 ? 177.868 170.827 198.908 1.00 27.37  ? 4412 PHE A CG    1 
ATOM   22290 C CD1   . PHE A 1 4412 ? 178.091 170.508 197.582 1.00 27.37  ? 4412 PHE A CD1   1 
ATOM   22291 C CD2   . PHE A 1 4412 ? 177.968 169.828 199.858 1.00 27.37  ? 4412 PHE A CD2   1 
ATOM   22292 C CE1   . PHE A 1 4412 ? 178.423 169.225 197.216 1.00 27.37  ? 4412 PHE A CE1   1 
ATOM   22293 C CE2   . PHE A 1 4412 ? 178.292 168.541 199.495 1.00 27.37  ? 4412 PHE A CE2   1 
ATOM   22294 C CZ    . PHE A 1 4412 ? 178.517 168.238 198.172 1.00 27.37  ? 4412 PHE A CZ    1 
ATOM   22295 N N     . PHE A 1 4413 ? 174.744 171.147 200.320 1.00 30.32  ? 4413 PHE A N     1 
ATOM   22296 C CA    . PHE A 1 4413 ? 173.814 170.051 200.549 1.00 30.32  ? 4413 PHE A CA    1 
ATOM   22297 C C     . PHE A 1 4413 ? 172.421 170.390 200.043 1.00 30.32  ? 4413 PHE A C     1 
ATOM   22298 O O     . PHE A 1 4413 ? 171.684 169.491 199.634 1.00 30.32  ? 4413 PHE A O     1 
ATOM   22299 C CB    . PHE A 1 4413 ? 173.780 169.688 202.032 1.00 30.32  ? 4413 PHE A CB    1 
ATOM   22300 C CG    . PHE A 1 4413 ? 174.932 168.830 202.465 1.00 30.32  ? 4413 PHE A CG    1 
ATOM   22301 C CD1   . PHE A 1 4413 ? 175.211 167.644 201.811 1.00 30.32  ? 4413 PHE A CD1   1 
ATOM   22302 C CD2   . PHE A 1 4413 ? 175.735 169.208 203.526 1.00 30.32  ? 4413 PHE A CD2   1 
ATOM   22303 C CE1   . PHE A 1 4413 ? 176.271 166.853 202.205 1.00 30.32  ? 4413 PHE A CE1   1 
ATOM   22304 C CE2   . PHE A 1 4413 ? 176.796 168.419 203.925 1.00 30.32  ? 4413 PHE A CE2   1 
ATOM   22305 C CZ    . PHE A 1 4413 ? 177.064 167.241 203.263 1.00 30.32  ? 4413 PHE A CZ    1 
ATOM   22306 N N     . GLU A 1 4414 ? 172.046 171.670 200.050 1.00 39.48  ? 4414 GLU A N     1 
ATOM   22307 C CA    . GLU A 1 4414 ? 170.806 172.087 199.406 1.00 39.48  ? 4414 GLU A CA    1 
ATOM   22308 C C     . GLU A 1 4414 ? 170.811 171.717 197.932 1.00 39.48  ? 4414 GLU A C     1 
ATOM   22309 O O     . GLU A 1 4414 ? 169.852 171.127 197.421 1.00 39.48  ? 4414 GLU A O     1 
ATOM   22310 C CB    . GLU A 1 4414 ? 170.618 173.594 199.575 1.00 39.48  ? 4414 GLU A CB    1 
ATOM   22311 C CG    . GLU A 1 4414 ? 169.196 174.074 199.391 1.00 39.48  ? 4414 GLU A CG    1 
ATOM   22312 C CD    . GLU A 1 4414 ? 168.932 175.374 200.116 1.00 39.48  ? 4414 GLU A CD    1 
ATOM   22313 O OE1   . GLU A 1 4414 ? 169.510 175.572 201.203 1.00 39.48  ? 4414 GLU A OE1   1 
ATOM   22314 O OE2   . GLU A 1 4414 ? 168.149 176.198 199.601 1.00 39.48  ? 4414 GLU A OE2   1 
ATOM   22315 N N     . ARG A 1 4415 ? 171.891 172.065 197.230 1.00 33.28  ? 4415 ARG A N     1 
ATOM   22316 C CA    . ARG A 1 4415 ? 171.975 171.742 195.809 1.00 33.28  ? 4415 ARG A CA    1 
ATOM   22317 C C     . ARG A 1 4415 ? 171.968 170.235 195.585 1.00 33.28  ? 4415 ARG A C     1 
ATOM   22318 O O     . ARG A 1 4415 ? 171.289 169.737 194.676 1.00 33.28  ? 4415 ARG A O     1 
ATOM   22319 C CB    . ARG A 1 4415 ? 173.222 172.378 195.197 1.00 33.28  ? 4415 ARG A CB    1 
ATOM   22320 C CG    . ARG A 1 4415 ? 173.150 172.543 193.687 1.00 33.28  ? 4415 ARG A CG    1 
ATOM   22321 C CD    . ARG A 1 4415 ? 174.350 173.305 193.152 1.00 33.28  ? 4415 ARG A CD    1 
ATOM   22322 N NE    . ARG A 1 4415 ? 174.659 174.472 193.970 1.00 33.28  ? 4415 ARG A NE    1 
ATOM   22323 C CZ    . ARG A 1 4415 ? 175.792 174.643 194.636 1.00 33.28  ? 4415 ARG A CZ    1 
ATOM   22324 N NH1   . ARG A 1 4415 ? 176.757 173.740 194.602 1.00 33.28  ? 4415 ARG A NH1   1 
ATOM   22325 N NH2   . ARG A 1 4415 ? 175.961 175.750 195.354 1.00 33.28  ? 4415 ARG A NH2   1 
ATOM   22326 N N     . GLU A 1 4416 ? 172.709 169.490 196.411 1.00 33.97  ? 4416 GLU A N     1 
ATOM   22327 C CA    . GLU A 1 4416 ? 172.723 168.035 196.273 1.00 33.97  ? 4416 GLU A CA    1 
ATOM   22328 C C     . GLU A 1 4416 ? 171.342 167.435 196.497 1.00 33.97  ? 4416 GLU A C     1 
ATOM   22329 O O     . GLU A 1 4416 ? 170.910 166.562 195.738 1.00 33.97  ? 4416 GLU A O     1 
ATOM   22330 C CB    . GLU A 1 4416 ? 173.733 167.415 197.236 1.00 33.97  ? 4416 GLU A CB    1 
ATOM   22331 C CG    . GLU A 1 4416 ? 175.147 167.901 197.033 1.00 33.97  ? 4416 GLU A CG    1 
ATOM   22332 C CD    . GLU A 1 4416 ? 175.783 167.299 195.800 1.00 33.97  ? 4416 GLU A CD    1 
ATOM   22333 O OE1   . GLU A 1 4416 ? 176.639 167.963 195.184 1.00 33.97  ? 4416 GLU A OE1   1 
ATOM   22334 O OE2   . GLU A 1 4416 ? 175.432 166.155 195.449 1.00 33.97  ? 4416 GLU A OE2   1 
ATOM   22335 N N     . VAL A 1 4417 ? 170.634 167.888 197.533 1.00 33.98  ? 4417 VAL A N     1 
ATOM   22336 C CA    . VAL A 1 4417 ? 169.314 167.344 197.832 1.00 33.98  ? 4417 VAL A CA    1 
ATOM   22337 C C     . VAL A 1 4417 ? 168.332 167.683 196.720 1.00 33.98  ? 4417 VAL A C     1 
ATOM   22338 O O     . VAL A 1 4417 ? 167.527 166.840 196.311 1.00 33.98  ? 4417 VAL A O     1 
ATOM   22339 C CB    . VAL A 1 4417 ? 168.825 167.847 199.202 1.00 33.98  ? 4417 VAL A CB    1 
ATOM   22340 C CG1   . VAL A 1 4417 ? 167.347 167.560 199.379 1.00 33.98  ? 4417 VAL A CG1   1 
ATOM   22341 C CG2   . VAL A 1 4417 ? 169.620 167.190 200.317 1.00 33.98  ? 4417 VAL A CG2   1 
ATOM   22342 N N     . LYS A 1 4418 ? 168.383 168.915 196.206 1.00 38.97  ? 4418 LYS A N     1 
ATOM   22343 C CA    . LYS A 1 4418 ? 167.493 169.286 195.110 1.00 38.97  ? 4418 LYS A CA    1 
ATOM   22344 C C     . LYS A 1 4418 ? 167.749 168.429 193.876 1.00 38.97  ? 4418 LYS A C     1 
ATOM   22345 O O     . LYS A 1 4418 ? 166.809 167.899 193.268 1.00 38.97  ? 4418 LYS A O     1 
ATOM   22346 C CB    . LYS A 1 4418 ? 167.650 170.770 194.776 1.00 38.97  ? 4418 LYS A CB    1 
ATOM   22347 C CG    . LYS A 1 4418 ? 167.074 171.711 195.819 1.00 38.97  ? 4418 LYS A CG    1 
ATOM   22348 C CD    . LYS A 1 4418 ? 167.831 173.026 195.848 1.00 38.97  ? 4418 LYS A CD    1 
ATOM   22349 C CE    . LYS A 1 4418 ? 167.434 173.917 194.685 1.00 38.97  ? 4418 LYS A CE    1 
ATOM   22350 N NZ    . LYS A 1 4418 ? 168.375 175.059 194.522 1.00 38.97  ? 4418 LYS A NZ    1 
ATOM   22351 N N     . MET A 1 4419 ? 169.021 168.273 193.493 1.00 38.44  ? 4419 MET A N     1 
ATOM   22352 C CA    . MET A 1 4419 ? 169.335 167.470 192.314 1.00 38.44  ? 4419 MET A CA    1 
ATOM   22353 C C     . MET A 1 4419 ? 168.929 166.016 192.512 1.00 38.44  ? 4419 MET A C     1 
ATOM   22354 O O     . MET A 1 4419 ? 168.343 165.396 191.614 1.00 38.44  ? 4419 MET A O     1 
ATOM   22355 C CB    . MET A 1 4419 ? 170.825 167.570 191.992 1.00 38.44  ? 4419 MET A CB    1 
ATOM   22356 C CG    . MET A 1 4419 ? 171.239 168.892 191.371 1.00 38.44  ? 4419 MET A CG    1 
ATOM   22357 S SD    . MET A 1 4419 ? 173.028 169.116 191.348 1.00 38.44  ? 4419 MET A SD    1 
ATOM   22358 C CE    . MET A 1 4419 ? 173.545 167.609 190.530 1.00 38.44  ? 4419 MET A CE    1 
ATOM   22359 N N     . GLY A 1 4420 ? 169.226 165.457 193.687 1.00 36.39  ? 4420 GLY A N     1 
ATOM   22360 C CA    . GLY A 1 4420 ? 168.872 164.076 193.951 1.00 36.39  ? 4420 GLY A CA    1 
ATOM   22361 C C     . GLY A 1 4420 ? 167.376 163.848 193.950 1.00 36.39  ? 4420 GLY A C     1 
ATOM   22362 O O     . GLY A 1 4420 ? 166.895 162.854 193.408 1.00 36.39  ? 4420 GLY A O     1 
ATOM   22363 N N     . ALA A 1 4421 ? 166.617 164.769 194.548 1.00 37.03  ? 4421 ALA A N     1 
ATOM   22364 C CA    . ALA A 1 4421 ? 165.166 164.632 194.565 1.00 37.03  ? 4421 ALA A CA    1 
ATOM   22365 C C     . ALA A 1 4421 ? 164.581 164.757 193.166 1.00 37.03  ? 4421 ALA A C     1 
ATOM   22366 O O     . ALA A 1 4421 ? 163.677 163.998 192.801 1.00 37.03  ? 4421 ALA A O     1 
ATOM   22367 C CB    . ALA A 1 4421 ? 164.551 165.670 195.500 1.00 37.03  ? 4421 ALA A CB    1 
ATOM   22368 N N     . LYS A 1 4422 ? 165.079 165.703 192.367 1.00 37.75  ? 4422 LYS A N     1 
ATOM   22369 C CA    . LYS A 1 4422 ? 164.594 165.834 190.996 1.00 37.75  ? 4422 LYS A CA    1 
ATOM   22370 C C     . LYS A 1 4422 ? 164.856 164.562 190.200 1.00 37.75  ? 4422 LYS A C     1 
ATOM   22371 O O     . LYS A 1 4422 ? 163.957 164.033 189.530 1.00 37.75  ? 4422 LYS A O     1 
ATOM   22372 C CB    . LYS A 1 4422 ? 165.252 167.038 190.322 1.00 37.75  ? 4422 LYS A CB    1 
ATOM   22373 C CG    . LYS A 1 4422 ? 164.808 167.271 188.888 1.00 37.75  ? 4422 LYS A CG    1 
ATOM   22374 C CD    . LYS A 1 4422 ? 163.364 167.732 188.815 1.00 37.75  ? 4422 LYS A CD    1 
ATOM   22375 C CE    . LYS A 1 4422 ? 162.966 168.059 187.385 1.00 37.75  ? 4422 LYS A CE    1 
ATOM   22376 N NZ    . LYS A 1 4422 ? 161.533 168.446 187.283 1.00 37.75  ? 4422 LYS A NZ    1 
ATOM   22377 N N     . LEU A 1 4423 ? 166.084 164.044 190.276 1.00 38.71  ? 4423 LEU A N     1 
ATOM   22378 C CA    . LEU A 1 4423 ? 166.413 162.836 189.528 1.00 38.71  ? 4423 LEU A CA    1 
ATOM   22379 C C     . LEU A 1 4423 ? 165.626 161.639 190.044 1.00 38.71  ? 4423 LEU A C     1 
ATOM   22380 O O     . LEU A 1 4423 ? 165.204 160.781 189.261 1.00 38.71  ? 4423 LEU A O     1 
ATOM   22381 C CB    . LEU A 1 4423 ? 167.918 162.575 189.590 1.00 38.71  ? 4423 LEU A CB    1 
ATOM   22382 C CG    . LEU A 1 4423 ? 168.436 161.393 188.774 1.00 38.71  ? 4423 LEU A CG    1 
ATOM   22383 C CD1   . LEU A 1 4423 ? 167.874 161.434 187.367 1.00 38.71  ? 4423 LEU A CD1   1 
ATOM   22384 C CD2   . LEU A 1 4423 ? 169.952 161.423 188.730 1.00 38.71  ? 4423 LEU A CD2   1 
ATOM   22385 N N     . LEU A 1 4424 ? 165.408 161.568 191.359 1.00 38.41  ? 4424 LEU A N     1 
ATOM   22386 C CA    . LEU A 1 4424 ? 164.646 160.467 191.936 1.00 38.41  ? 4424 LEU A CA    1 
ATOM   22387 C C     . LEU A 1 4424 ? 163.199 160.494 191.465 1.00 38.41  ? 4424 LEU A C     1 
ATOM   22388 O O     . LEU A 1 4424 ? 162.633 159.454 191.112 1.00 38.41  ? 4424 LEU A O     1 
ATOM   22389 C CB    . LEU A 1 4424 ? 164.721 160.533 193.461 1.00 38.41  ? 4424 LEU A CB    1 
ATOM   22390 C CG    . LEU A 1 4424 ? 163.708 159.702 194.244 1.00 38.41  ? 4424 LEU A CG    1 
ATOM   22391 C CD1   . LEU A 1 4424 ? 163.938 158.226 194.007 1.00 38.41  ? 4424 LEU A CD1   1 
ATOM   22392 C CD2   . LEU A 1 4424 ? 163.797 160.025 195.723 1.00 38.41  ? 4424 LEU A CD2   1 
ATOM   22393 N N     . GLN A 1 4425 ? 162.582 161.678 191.453 1.00 43.63  ? 4425 GLN A N     1 
ATOM   22394 C CA    . GLN A 1 4425 ? 161.217 161.784 190.949 1.00 43.63  ? 4425 GLN A CA    1 
ATOM   22395 C C     . GLN A 1 4425 ? 161.144 161.408 189.476 1.00 43.63  ? 4425 GLN A C     1 
ATOM   22396 O O     . GLN A 1 4425 ? 160.232 160.685 189.061 1.00 43.63  ? 4425 GLN A O     1 
ATOM   22397 C CB    . GLN A 1 4425 ? 160.668 163.195 191.167 1.00 43.63  ? 4425 GLN A CB    1 
ATOM   22398 C CG    . GLN A 1 4425 ? 160.607 163.633 192.620 1.00 43.63  ? 4425 GLN A CG    1 
ATOM   22399 C CD    . GLN A 1 4425 ? 160.156 162.523 193.547 1.00 43.63  ? 4425 GLN A CD    1 
ATOM   22400 O OE1   . GLN A 1 4425 ? 160.893 162.110 194.442 1.00 43.63  ? 4425 GLN A OE1   1 
ATOM   22401 N NE2   . GLN A 1 4425 ? 158.937 162.038 193.342 1.00 43.63  ? 4425 GLN A NE2   1 
ATOM   22402 N N     . ASP A 1 4426 ? 162.101 161.878 188.671 1.00 44.92  ? 4426 ASP A N     1 
ATOM   22403 C CA    . ASP A 1 4426 ? 162.091 161.535 187.251 1.00 44.92  ? 4426 ASP A CA    1 
ATOM   22404 C C     . ASP A 1 4426 ? 162.217 160.029 187.048 1.00 44.92  ? 4426 ASP A C     1 
ATOM   22405 O O     . ASP A 1 4426 ? 161.461 159.426 186.274 1.00 44.92  ? 4426 ASP A O     1 
ATOM   22406 C CB    . ASP A 1 4426 ? 163.216 162.274 186.526 1.00 44.92  ? 4426 ASP A CB    1 
ATOM   22407 C CG    . ASP A 1 4426 ? 162.843 163.698 186.173 1.00 44.92  ? 4426 ASP A CG    1 
ATOM   22408 O OD1   . ASP A 1 4426 ? 163.673 164.396 185.554 1.00 44.92  ? 4426 ASP A OD1   1 
ATOM   22409 O OD2   . ASP A 1 4426 ? 161.719 164.121 186.514 1.00 44.92  ? 4426 ASP A OD2   1 
ATOM   22410 N N     . VAL A 1 4427 ? 163.158 159.401 187.757 1.00 44.52  ? 4427 VAL A N     1 
ATOM   22411 C CA    . VAL A 1 4427 ? 163.376 157.967 187.613 1.00 44.52  ? 4427 VAL A CA    1 
ATOM   22412 C C     . VAL A 1 4427 ? 162.151 157.188 188.068 1.00 44.52  ? 4427 VAL A C     1 
ATOM   22413 O O     . VAL A 1 4427 ? 161.734 156.226 187.412 1.00 44.52  ? 4427 VAL A O     1 
ATOM   22414 C CB    . VAL A 1 4427 ? 164.638 157.541 188.385 1.00 44.52  ? 4427 VAL A CB    1 
ATOM   22415 C CG1   . VAL A 1 4427 ? 164.679 156.032 188.556 1.00 44.52  ? 4427 VAL A CG1   1 
ATOM   22416 C CG2   . VAL A 1 4427 ? 165.885 158.030 187.669 1.00 44.52  ? 4427 VAL A CG2   1 
ATOM   22417 N N     . ARG A 1 4428 ? 161.554 157.582 189.195 1.00 44.65  ? 4428 ARG A N     1 
ATOM   22418 C CA    . ARG A 1 4428 ? 160.402 156.852 189.712 1.00 44.65  ? 4428 ARG A CA    1 
ATOM   22419 C C     . ARG A 1 4428 ? 159.201 156.991 188.786 1.00 44.65  ? 4428 ARG A C     1 
ATOM   22420 O O     . ARG A 1 4428 ? 158.476 156.020 188.547 1.00 44.65  ? 4428 ARG A O     1 
ATOM   22421 C CB    . ARG A 1 4428 ? 160.062 157.335 191.120 1.00 44.65  ? 4428 ARG A CB    1 
ATOM   22422 C CG    . ARG A 1 4428 ? 159.475 156.249 192.000 1.00 44.65  ? 4428 ARG A CG    1 
ATOM   22423 C CD    . ARG A 1 4428 ? 159.482 156.654 193.460 1.00 44.65  ? 4428 ARG A CD    1 
ATOM   22424 N NE    . ARG A 1 4428 ? 159.206 155.528 194.346 1.00 44.65  ? 4428 ARG A NE    1 
ATOM   22425 C CZ    . ARG A 1 4428 ? 160.040 154.521 194.566 1.00 44.65  ? 4428 ARG A CZ    1 
ATOM   22426 N NH1   . ARG A 1 4428 ? 161.237 154.477 194.002 1.00 44.65  ? 4428 ARG A NH1   1 
ATOM   22427 N NH2   . ARG A 1 4428 ? 159.669 153.537 195.379 1.00 44.65  ? 4428 ARG A NH2   1 
ATOM   22428 N N     . GLN A 1 4429 ? 158.973 158.194 188.251 1.00 51.42  ? 4429 GLN A N     1 
ATOM   22429 C CA    . GLN A 1 4429 ? 157.875 158.378 187.307 1.00 51.42  ? 4429 GLN A CA    1 
ATOM   22430 C C     . GLN A 1 4429 ? 158.090 157.558 186.042 1.00 51.42  ? 4429 GLN A C     1 
ATOM   22431 O O     . GLN A 1 4429 ? 157.154 156.926 185.537 1.00 51.42  ? 4429 GLN A O     1 
ATOM   22432 C CB    . GLN A 1 4429 ? 157.715 159.859 186.966 1.00 51.42  ? 4429 GLN A CB    1 
ATOM   22433 C CG    . GLN A 1 4429 ? 157.231 160.716 188.123 1.00 51.42  ? 4429 GLN A CG    1 
ATOM   22434 C CD    . GLN A 1 4429 ? 156.534 161.980 187.660 1.00 51.42  ? 4429 GLN A CD    1 
ATOM   22435 O OE1   . GLN A 1 4429 ? 156.399 162.224 186.461 1.00 51.42  ? 4429 GLN A OE1   1 
ATOM   22436 N NE2   . GLN A 1 4429 ? 156.089 162.793 188.611 1.00 51.42  ? 4429 GLN A NE2   1 
ATOM   22437 N N     . ASP A 1 4430 ? 159.318 157.548 185.518 1.00 56.21  ? 4430 ASP A N     1 
ATOM   22438 C CA    . ASP A 1 4430 ? 159.590 156.772 184.313 1.00 56.21  ? 4430 ASP A CA    1 
ATOM   22439 C C     . ASP A 1 4430 ? 159.422 155.278 184.567 1.00 56.21  ? 4430 ASP A C     1 
ATOM   22440 O O     . ASP A 1 4430 ? 158.864 154.557 183.730 1.00 56.21  ? 4430 ASP A O     1 
ATOM   22441 C CB    . ASP A 1 4430 ? 160.994 157.088 183.802 1.00 56.21  ? 4430 ASP A CB    1 
ATOM   22442 C CG    . ASP A 1 4430 ? 161.072 158.445 183.125 1.00 56.21  ? 4430 ASP A CG    1 
ATOM   22443 O OD1   . ASP A 1 4430 ? 160.116 159.234 183.270 1.00 56.21  ? 4430 ASP A OD1   1 
ATOM   22444 O OD2   . ASP A 1 4430 ? 162.090 158.728 182.460 1.00 56.21  ? 4430 ASP A OD2   1 
ATOM   22445 N N     . LEU A 1 4431 ? 159.885 154.797 185.723 1.00 55.61  ? 4431 LEU A N     1 
ATOM   22446 C CA    . LEU A 1 4431 ? 159.730 153.384 186.053 1.00 55.61  ? 4431 LEU A CA    1 
ATOM   22447 C C     . LEU A 1 4431 ? 158.263 153.018 186.246 1.00 55.61  ? 4431 LEU A C     1 
ATOM   22448 O O     . LEU A 1 4431 ? 157.835 151.930 185.848 1.00 55.61  ? 4431 LEU A O     1 
ATOM   22449 C CB    . LEU A 1 4431 ? 160.543 153.045 187.301 1.00 55.61  ? 4431 LEU A CB    1 
ATOM   22450 C CG    . LEU A 1 4431 ? 162.020 152.719 187.066 1.00 55.61  ? 4431 LEU A CG    1 
ATOM   22451 C CD1   . LEU A 1 4431 ? 162.652 152.127 188.314 1.00 55.61  ? 4431 LEU A CD1   1 
ATOM   22452 C CD2   . LEU A 1 4431 ? 162.181 151.776 185.886 1.00 55.61  ? 4431 LEU A CD2   1 
ATOM   22453 N N     . ALA A 1 4432 ? 157.478 153.908 186.858 1.00 60.33  ? 4432 ALA A N     1 
ATOM   22454 C CA    . ALA A 1 4432 ? 156.047 153.656 186.997 1.00 60.33  ? 4432 ALA A CA    1 
ATOM   22455 C C     . ALA A 1 4432 ? 155.363 153.611 185.637 1.00 60.33  ? 4432 ALA A C     1 
ATOM   22456 O O     . ALA A 1 4432 ? 154.462 152.794 185.413 1.00 60.33  ? 4432 ALA A O     1 
ATOM   22457 C CB    . ALA A 1 4432 ? 155.409 154.721 187.887 1.00 60.33  ? 4432 ALA A CB    1 
ATOM   22458 N N     . ASP A 1 4433 ? 155.770 154.492 184.720 1.00 66.05  ? 4433 ASP A N     1 
ATOM   22459 C CA    . ASP A 1 4433 ? 155.236 154.449 183.361 1.00 66.05  ? 4433 ASP A CA    1 
ATOM   22460 C C     . ASP A 1 4433 ? 155.565 153.120 182.690 1.00 66.05  ? 4433 ASP A C     1 
ATOM   22461 O O     . ASP A 1 4433 ? 154.700 152.501 182.053 1.00 66.05  ? 4433 ASP A O     1 
ATOM   22462 C CB    . ASP A 1 4433 ? 155.798 155.620 182.553 1.00 66.05  ? 4433 ASP A CB    1 
ATOM   22463 C CG    . ASP A 1 4433 ? 155.137 155.776 181.195 1.00 66.05  ? 4433 ASP A CG    1 
ATOM   22464 O OD1   . ASP A 1 4433 ? 154.257 154.963 180.846 1.00 66.05  ? 4433 ASP A OD1   1 
ATOM   22465 O OD2   . ASP A 1 4433 ? 155.506 156.722 180.468 1.00 66.05  ? 4433 ASP A OD2   1 
ATOM   22466 N N     . VAL A 1 4434 ? 156.810 152.660 182.836 1.00 64.28  ? 4434 VAL A N     1 
ATOM   22467 C CA    . VAL A 1 4434 ? 157.199 151.370 182.272 1.00 64.28  ? 4434 VAL A CA    1 
ATOM   22468 C C     . VAL A 1 4434 ? 156.357 150.252 182.872 1.00 64.28  ? 4434 VAL A C     1 
ATOM   22469 O O     . VAL A 1 4434 ? 155.876 149.364 182.155 1.00 64.28  ? 4434 VAL A O     1 
ATOM   22470 C CB    . VAL A 1 4434 ? 158.704 151.122 182.484 1.00 64.28  ? 4434 VAL A CB    1 
ATOM   22471 C CG1   . VAL A 1 4434 ? 159.076 149.717 182.048 1.00 64.28  ? 4434 VAL A CG1   1 
ATOM   22472 C CG2   . VAL A 1 4434 ? 159.520 152.141 181.714 1.00 64.28  ? 4434 VAL A CG2   1 
ATOM   22473 N N     . VAL A 1 4435 ? 156.154 150.283 184.191 1.00 64.97  ? 4435 VAL A N     1 
ATOM   22474 C CA    . VAL A 1 4435 ? 155.342 149.262 184.849 1.00 64.97  ? 4435 VAL A CA    1 
ATOM   22475 C C     . VAL A 1 4435 ? 153.933 149.256 184.276 1.00 64.97  ? 4435 VAL A C     1 
ATOM   22476 O O     . VAL A 1 4435 ? 153.406 148.208 183.891 1.00 64.97  ? 4435 VAL A O     1 
ATOM   22477 C CB    . VAL A 1 4435 ? 155.320 149.484 186.372 1.00 64.97  ? 4435 VAL A CB    1 
ATOM   22478 C CG1   . VAL A 1 4435 ? 154.264 148.601 187.017 1.00 64.97  ? 4435 VAL A CG1   1 
ATOM   22479 C CG2   . VAL A 1 4435 ? 156.676 149.191 186.972 1.00 64.97  ? 4435 VAL A CG2   1 
ATOM   22480 N N     . GLN A 1 4436 ? 153.312 150.434 184.187 1.00 70.38  ? 4436 GLN A N     1 
ATOM   22481 C CA    . GLN A 1 4436 ? 151.939 150.511 183.699 1.00 70.38  ? 4436 GLN A CA    1 
ATOM   22482 C C     . GLN A 1 4436 ? 151.831 149.997 182.270 1.00 70.38  ? 4436 GLN A C     1 
ATOM   22483 O O     . GLN A 1 4436 ? 150.850 149.334 181.913 1.00 70.38  ? 4436 GLN A O     1 
ATOM   22484 C CB    . GLN A 1 4436 ? 151.424 151.948 183.796 1.00 70.38  ? 4436 GLN A CB    1 
ATOM   22485 C CG    . GLN A 1 4436 ? 151.232 152.477 185.219 1.00 70.38  ? 4436 GLN A CG    1 
ATOM   22486 C CD    . GLN A 1 4436 ? 150.718 151.431 186.197 1.00 70.38  ? 4436 GLN A CD    1 
ATOM   22487 O OE1   . GLN A 1 4436 ? 151.476 150.603 186.706 1.00 70.38  ? 4436 GLN A OE1   1 
ATOM   22488 N NE2   . GLN A 1 4436 ? 149.417 151.463 186.460 1.00 70.38  ? 4436 GLN A NE2   1 
ATOM   22489 N N     . VAL A 1 4437 ? 152.830 150.290 181.435 1.00 68.27  ? 4437 VAL A N     1 
ATOM   22490 C CA    . VAL A 1 4437 ? 152.804 149.790 180.066 1.00 68.27  ? 4437 VAL A CA    1 
ATOM   22491 C C     . VAL A 1 4437 ? 153.085 148.291 180.001 1.00 68.27  ? 4437 VAL A C     1 
ATOM   22492 O O     . VAL A 1 4437 ? 152.663 147.627 179.046 1.00 68.27  ? 4437 VAL A O     1 
ATOM   22493 C CB    . VAL A 1 4437 ? 153.782 150.616 179.211 1.00 68.27  ? 4437 VAL A CB    1 
ATOM   22494 C CG1   . VAL A 1 4437 ? 153.894 150.063 177.801 1.00 68.27  ? 4437 VAL A CG1   1 
ATOM   22495 C CG2   . VAL A 1 4437 ? 153.295 152.043 179.164 1.00 68.27  ? 4437 VAL A CG2   1 
ATOM   22496 N N     . CYS A 1 4438 ? 153.761 147.727 181.006 1.00 71.13  ? 4438 CYS A N     1 
ATOM   22497 C CA    . CYS A 1 4438 ? 154.010 146.286 181.003 1.00 71.13  ? 4438 CYS A CA    1 
ATOM   22498 C C     . CYS A 1 4438 ? 152.707 145.492 181.018 1.00 71.13  ? 4438 CYS A C     1 
ATOM   22499 O O     . CYS A 1 4438 ? 152.577 144.494 180.300 1.00 71.13  ? 4438 CYS A O     1 
ATOM   22500 C CB    . CYS A 1 4438 ? 154.891 145.894 182.188 1.00 71.13  ? 4438 CYS A CB    1 
ATOM   22501 S SG    . CYS A 1 4438 ? 156.623 146.388 182.036 1.00 71.13  ? 4438 CYS A SG    1 
ATOM   22502 N N     . GLU A 1 4439 ? 151.732 145.912 181.826 1.00 75.04  ? 4439 GLU A N     1 
ATOM   22503 C CA    . GLU A 1 4439 ? 150.410 145.300 181.761 1.00 75.04  ? 4439 GLU A CA    1 
ATOM   22504 C C     . GLU A 1 4439 ? 149.540 145.895 180.662 1.00 75.04  ? 4439 GLU A C     1 
ATOM   22505 O O     . GLU A 1 4439 ? 148.407 145.439 180.479 1.00 75.04  ? 4439 GLU A O     1 
ATOM   22506 C CB    . GLU A 1 4439 ? 149.668 145.419 183.099 1.00 75.04  ? 4439 GLU A CB    1 
ATOM   22507 C CG    . GLU A 1 4439 ? 150.238 144.588 184.239 1.00 75.04  ? 4439 GLU A CG    1 
ATOM   22508 C CD    . GLU A 1 4439 ? 151.371 145.278 184.959 1.00 75.04  ? 4439 GLU A CD    1 
ATOM   22509 O OE1   . GLU A 1 4439 ? 151.665 146.436 184.616 1.00 75.04  ? 4439 GLU A OE1   1 
ATOM   22510 O OE2   . GLU A 1 4439 ? 151.960 144.665 185.870 1.00 75.04  ? 4439 GLU A OE2   1 
ATOM   22511 N N     . GLY A 1 4440 ? 150.035 146.888 179.933 1.00 71.92  ? 4440 GLY A N     1 
ATOM   22512 C CA    . GLY A 1 4440 ? 149.237 147.531 178.905 1.00 71.92  ? 4440 GLY A CA    1 
ATOM   22513 C C     . GLY A 1 4440 ? 148.061 148.309 179.451 1.00 71.92  ? 4440 GLY A C     1 
ATOM   22514 O O     . GLY A 1 4440 ? 146.985 148.310 178.839 1.00 71.92  ? 4440 GLY A O     1 
ATOM   22515 N N     . LYS A 1 4441 ? 148.237 148.972 180.591 1.00 72.15  ? 4441 LYS A N     1 
ATOM   22516 C CA    . LYS A 1 4441 ? 147.189 149.780 181.196 1.00 72.15  ? 4441 LYS A CA    1 
ATOM   22517 C C     . LYS A 1 4441 ? 147.200 151.220 180.703 1.00 72.15  ? 4441 LYS A C     1 
ATOM   22518 O O     . LYS A 1 4441 ? 146.342 152.008 181.114 1.00 72.15  ? 4441 LYS A O     1 
ATOM   22519 C CB    . LYS A 1 4441 ? 147.320 149.756 182.723 1.00 72.15  ? 4441 LYS A CB    1 
ATOM   22520 C CG    . LYS A 1 4441 ? 146.722 148.525 183.384 1.00 72.15  ? 4441 LYS A CG    1 
ATOM   22521 C CD    . LYS A 1 4441 ? 147.265 148.342 184.793 1.00 72.15  ? 4441 LYS A CD    1 
ATOM   22522 C CE    . LYS A 1 4441 ? 146.206 147.787 185.732 1.00 72.15  ? 4441 LYS A CE    1 
ATOM   22523 N NZ    . LYS A 1 4441 ? 146.040 146.315 185.580 1.00 72.15  ? 4441 LYS A NZ    1 
ATOM   22524 N N     . LYS A 1 4442 ? 148.143 151.580 179.837 1.00 74.23  ? 4442 LYS A N     1 
ATOM   22525 C CA    . LYS A 1 4442 ? 148.247 152.943 179.336 1.00 74.23  ? 4442 LYS A CA    1 
ATOM   22526 C C     . LYS A 1 4442 ? 149.028 152.928 178.030 1.00 74.23  ? 4442 LYS A C     1 
ATOM   22527 O O     . LYS A 1 4442 ? 149.679 151.939 177.684 1.00 74.23  ? 4442 LYS A O     1 
ATOM   22528 C CB    . LYS A 1 4442 ? 148.909 153.870 180.360 1.00 74.23  ? 4442 LYS A CB    1 
ATOM   22529 C CG    . LYS A 1 4442 ? 150.405 153.662 180.511 1.00 74.23  ? 4442 LYS A CG    1 
ATOM   22530 C CD    . LYS A 1 4442 ? 151.059 154.825 181.239 1.00 74.23  ? 4442 LYS A CD    1 
ATOM   22531 C CE    . LYS A 1 4442 ? 150.700 156.154 180.596 1.00 74.23  ? 4442 LYS A CE    1 
ATOM   22532 N NZ    . LYS A 1 4442 ? 151.385 157.294 181.264 1.00 74.23  ? 4442 LYS A NZ    1 
ATOM   22533 N N     . LYS A 1 4443 ? 148.951 154.044 177.310 1.00 80.96  ? 4443 LYS A N     1 
ATOM   22534 C CA    . LYS A 1 4443 ? 149.562 154.150 175.995 1.00 80.96  ? 4443 LYS A CA    1 
ATOM   22535 C C     . LYS A 1 4443 ? 151.080 154.245 176.096 1.00 80.96  ? 4443 LYS A C     1 
ATOM   22536 O O     . LYS A 1 4443 ? 151.643 154.477 177.170 1.00 80.96  ? 4443 LYS A O     1 
ATOM   22537 C CB    . LYS A 1 4443 ? 149.014 155.365 175.247 1.00 80.96  ? 4443 LYS A CB    1 
ATOM   22538 C CG    . LYS A 1 4443 ? 147.509 155.333 175.040 1.00 80.96  ? 4443 LYS A CG    1 
ATOM   22539 C CD    . LYS A 1 4443 ? 147.100 154.175 174.144 1.00 80.96  ? 4443 LYS A CD    1 
ATOM   22540 C CE    . LYS A 1 4443 ? 145.612 154.212 173.838 1.00 80.96  ? 4443 LYS A CE    1 
ATOM   22541 N NZ    . LYS A 1 4443 ? 144.790 153.935 175.048 1.00 80.96  ? 4443 LYS A NZ    1 
ATOM   22542 N N     . GLN A 1 4444 ? 151.739 154.058 174.956 1.00 80.76  ? 4444 GLN A N     1 
ATOM   22543 C CA    . GLN A 1 4444 ? 153.193 154.062 174.857 1.00 80.76  ? 4444 GLN A CA    1 
ATOM   22544 C C     . GLN A 1 4444 ? 153.637 155.180 173.923 1.00 80.76  ? 4444 GLN A C     1 
ATOM   22545 O O     . GLN A 1 4444 ? 153.115 155.306 172.810 1.00 80.76  ? 4444 GLN A O     1 
ATOM   22546 C CB    . GLN A 1 4444 ? 153.696 152.707 174.355 1.00 80.76  ? 4444 GLN A CB    1 
ATOM   22547 C CG    . GLN A 1 4444 ? 155.083 152.731 173.755 1.00 80.76  ? 4444 GLN A CG    1 
ATOM   22548 C CD    . GLN A 1 4444 ? 155.380 151.489 172.937 1.00 80.76  ? 4444 GLN A CD    1 
ATOM   22549 O OE1   . GLN A 1 4444 ? 155.290 151.505 171.709 1.00 80.76  ? 4444 GLN A OE1   1 
ATOM   22550 N NE2   . GLN A 1 4444 ? 155.736 150.404 173.614 1.00 80.76  ? 4444 GLN A NE2   1 
ATOM   22551 N N     . THR A 1 4445 ? 154.598 155.984 174.372 1.00 81.44  ? 4445 THR A N     1 
ATOM   22552 C CA    . THR A 1 4445 ? 155.077 157.144 173.632 1.00 81.44  ? 4445 THR A CA    1 
ATOM   22553 C C     . THR A 1 4445 ? 156.530 156.942 173.203 1.00 81.44  ? 4445 THR A C     1 
ATOM   22554 O O     . THR A 1 4445 ? 157.176 155.950 173.548 1.00 81.44  ? 4445 THR A O     1 
ATOM   22555 C CB    . THR A 1 4445 ? 154.925 158.416 174.470 1.00 81.44  ? 4445 THR A CB    1 
ATOM   22556 O OG1   . THR A 1 4445 ? 155.495 159.526 173.765 1.00 81.44  ? 4445 THR A OG1   1 
ATOM   22557 C CG2   . THR A 1 4445 ? 155.625 158.258 175.811 1.00 81.44  ? 4445 THR A CG2   1 
ATOM   22558 N N     . ASN A 1 4446 ? 157.045 157.918 172.449 1.00 79.31  ? 4446 ASN A N     1 
ATOM   22559 C CA    . ASN A 1 4446 ? 158.375 157.796 171.854 1.00 79.31  ? 4446 ASN A CA    1 
ATOM   22560 C C     . ASN A 1 4446 ? 159.468 157.788 172.918 1.00 79.31  ? 4446 ASN A C     1 
ATOM   22561 O O     . ASN A 1 4446 ? 160.367 156.937 172.897 1.00 79.31  ? 4446 ASN A O     1 
ATOM   22562 C CB    . ASN A 1 4446 ? 158.602 158.936 170.861 1.00 79.31  ? 4446 ASN A CB    1 
ATOM   22563 C CG    . ASN A 1 4446 ? 158.268 160.295 171.447 1.00 79.31  ? 4446 ASN A CG    1 
ATOM   22564 O OD1   . ASN A 1 4446 ? 157.822 160.398 172.590 1.00 79.31  ? 4446 ASN A OD1   1 
ATOM   22565 N ND2   . ASN A 1 4446 ? 158.483 161.346 170.665 1.00 79.31  ? 4446 ASN A ND2   1 
ATOM   22566 N N     . TYR A 1 4447 ? 159.419 158.752 173.842 1.00 72.91  ? 4447 TYR A N     1 
ATOM   22567 C CA    . TYR A 1 4447 ? 160.349 158.770 174.966 1.00 72.91  ? 4447 TYR A CA    1 
ATOM   22568 C C     . TYR A 1 4447 ? 160.334 157.438 175.700 1.00 72.91  ? 4447 TYR A C     1 
ATOM   22569 O O     . TYR A 1 4447 ? 161.387 156.869 176.020 1.00 72.91  ? 4447 TYR A O     1 
ATOM   22570 C CB    . TYR A 1 4447 ? 159.978 159.913 175.911 1.00 72.91  ? 4447 TYR A CB    1 
ATOM   22571 C CG    . TYR A 1 4447 ? 160.881 160.073 177.110 1.00 72.91  ? 4447 TYR A CG    1 
ATOM   22572 C CD1   . TYR A 1 4447 ? 162.143 160.637 176.990 1.00 72.91  ? 4447 TYR A CD1   1 
ATOM   22573 C CD2   . TYR A 1 4447 ? 160.462 159.667 178.370 1.00 72.91  ? 4447 TYR A CD2   1 
ATOM   22574 C CE1   . TYR A 1 4447 ? 162.964 160.786 178.092 1.00 72.91  ? 4447 TYR A CE1   1 
ATOM   22575 C CE2   . TYR A 1 4447 ? 161.274 159.811 179.475 1.00 72.91  ? 4447 TYR A CE2   1 
ATOM   22576 C CZ    . TYR A 1 4447 ? 162.523 160.371 179.332 1.00 72.91  ? 4447 TYR A CZ    1 
ATOM   22577 O OH    . TYR A 1 4447 ? 163.331 160.514 180.435 1.00 72.91  ? 4447 TYR A OH    1 
ATOM   22578 N N     . LEU A 1 4448 ? 159.135 156.917 175.954 1.00 75.31  ? 4448 LEU A N     1 
ATOM   22579 C CA    . LEU A 1 4448 ? 159.010 155.637 176.633 1.00 75.31  ? 4448 LEU A CA    1 
ATOM   22580 C C     . LEU A 1 4448 ? 159.575 154.503 175.790 1.00 75.31  ? 4448 LEU A C     1 
ATOM   22581 O O     . LEU A 1 4448 ? 160.173 153.566 176.329 1.00 75.31  ? 4448 LEU A O     1 
ATOM   22582 C CB    . LEU A 1 4448 ? 157.549 155.379 176.977 1.00 75.31  ? 4448 LEU A CB    1 
ATOM   22583 C CG    . LEU A 1 4448 ? 157.272 154.101 177.752 1.00 75.31  ? 4448 LEU A CG    1 
ATOM   22584 C CD1   . LEU A 1 4448 ? 157.957 154.139 179.105 1.00 75.31  ? 4448 LEU A CD1   1 
ATOM   22585 C CD2   . LEU A 1 4448 ? 155.788 153.969 177.908 1.00 75.31  ? 4448 LEU A CD2   1 
ATOM   22586 N N     . ARG A 1 4449 ? 159.387 154.557 174.467 1.00 77.46  ? 4449 ARG A N     1 
ATOM   22587 C CA    . ARG A 1 4449 ? 159.944 153.512 173.610 1.00 77.46  ? 4449 ARG A CA    1 
ATOM   22588 C C     . ARG A 1 4449 ? 161.463 153.494 173.687 1.00 77.46  ? 4449 ARG A C     1 
ATOM   22589 O O     . ARG A 1 4449 ? 162.075 152.429 173.829 1.00 77.46  ? 4449 ARG A O     1 
ATOM   22590 C CB    . ARG A 1 4449 ? 159.485 153.692 172.161 1.00 77.46  ? 4449 ARG A CB    1 
ATOM   22591 C CG    . ARG A 1 4449 ? 158.007 153.442 171.942 1.00 77.46  ? 4449 ARG A CG    1 
ATOM   22592 C CD    . ARG A 1 4449 ? 157.614 153.554 170.477 1.00 77.46  ? 4449 ARG A CD    1 
ATOM   22593 N NE    . ARG A 1 4449 ? 157.696 154.917 169.966 1.00 77.46  ? 4449 ARG A NE    1 
ATOM   22594 C CZ    . ARG A 1 4449 ? 158.567 155.318 169.050 1.00 77.46  ? 4449 ARG A CZ    1 
ATOM   22595 N NH1   . ARG A 1 4449 ? 159.457 154.487 168.532 1.00 77.46  ? 4449 ARG A NH1   1 
ATOM   22596 N NH2   . ARG A 1 4449 ? 158.541 156.582 168.639 1.00 77.46  ? 4449 ARG A NH2   1 
ATOM   22597 N N     . THR A 1 4450 ? 162.092 154.668 173.607 1.00 72.48  ? 4450 THR A N     1 
ATOM   22598 C CA    . THR A 1 4450 ? 163.547 154.724 173.726 1.00 72.48  ? 4450 THR A CA    1 
ATOM   22599 C C     . THR A 1 4450 ? 164.000 154.208 175.086 1.00 72.48  ? 4450 THR A C     1 
ATOM   22600 O O     . THR A 1 4450 ? 164.951 153.419 175.184 1.00 72.48  ? 4450 THR A O     1 
ATOM   22601 C CB    . THR A 1 4450 ? 164.044 156.153 173.502 1.00 72.48  ? 4450 THR A CB    1 
ATOM   22602 O OG1   . THR A 1 4450 ? 163.662 156.975 174.613 1.00 72.48  ? 4450 THR A OG1   1 
ATOM   22603 C CG2   . THR A 1 4450 ? 163.466 156.730 172.219 1.00 72.48  ? 4450 THR A CG2   1 
ATOM   22604 N N     . LEU A 1 4451 ? 163.311 154.630 176.149 1.00 65.79  ? 4451 LEU A N     1 
ATOM   22605 C CA    . LEU A 1 4451 ? 163.701 154.222 177.494 1.00 65.79  ? 4451 LEU A CA    1 
ATOM   22606 C C     . LEU A 1 4451 ? 163.591 152.710 177.667 1.00 65.79  ? 4451 LEU A C     1 
ATOM   22607 O O     . LEU A 1 4451 ? 164.500 152.066 178.204 1.00 65.79  ? 4451 LEU A O     1 
ATOM   22608 C CB    . LEU A 1 4451 ? 162.843 154.961 178.521 1.00 65.79  ? 4451 LEU A CB    1 
ATOM   22609 C CG    . LEU A 1 4451 ? 163.306 154.979 179.976 1.00 65.79  ? 4451 LEU A CG    1 
ATOM   22610 C CD1   . LEU A 1 4451 ? 162.959 156.311 180.602 1.00 65.79  ? 4451 LEU A CD1   1 
ATOM   22611 C CD2   . LEU A 1 4451 ? 162.649 153.861 180.751 1.00 65.79  ? 4451 LEU A CD2   1 
ATOM   22612 N N     . ILE A 1 4452 ? 162.491 152.119 177.195 1.00 66.95  ? 4452 ILE A N     1 
ATOM   22613 C CA    . ILE A 1 4452 ? 162.293 150.684 177.379 1.00 66.95  ? 4452 ILE A CA    1 
ATOM   22614 C C     . ILE A 1 4452 ? 163.249 149.893 176.494 1.00 66.95  ? 4452 ILE A C     1 
ATOM   22615 O O     . ILE A 1 4452 ? 163.711 148.812 176.876 1.00 66.95  ? 4452 ILE A O     1 
ATOM   22616 C CB    . ILE A 1 4452 ? 160.821 150.296 177.134 1.00 66.95  ? 4452 ILE A CB    1 
ATOM   22617 C CG1   . ILE A 1 4452 ? 160.589 148.832 177.513 1.00 66.95  ? 4452 ILE A CG1   1 
ATOM   22618 C CG2   . ILE A 1 4452 ? 160.422 150.510 175.687 1.00 66.95  ? 4452 ILE A CG2   1 
ATOM   22619 C CD1   . ILE A 1 4452 ? 160.808 148.537 178.980 1.00 66.95  ? 4452 ILE A CD1   1 
ATOM   22620 N N     . ASN A 1 4453 ? 163.568 150.411 175.304 1.00 67.64  ? 4453 ASN A N     1 
ATOM   22621 C CA    . ASN A 1 4453 ? 164.546 149.737 174.456 1.00 67.64  ? 4453 ASN A CA    1 
ATOM   22622 C C     . ASN A 1 4453 ? 165.915 149.711 175.122 1.00 67.64  ? 4453 ASN A C     1 
ATOM   22623 O O     . ASN A 1 4453 ? 166.603 148.681 175.121 1.00 67.64  ? 4453 ASN A O     1 
ATOM   22624 C CB    . ASN A 1 4453 ? 164.622 150.417 173.090 1.00 67.64  ? 4453 ASN A CB    1 
ATOM   22625 C CG    . ASN A 1 4453 ? 163.355 150.236 172.278 1.00 67.64  ? 4453 ASN A CG    1 
ATOM   22626 O OD1   . ASN A 1 4453 ? 162.753 149.162 172.276 1.00 67.64  ? 4453 ASN A OD1   1 
ATOM   22627 N ND2   . ASN A 1 4453 ? 162.943 151.289 171.583 1.00 67.64  ? 4453 ASN A ND2   1 
ATOM   22628 N N     . GLU A 1 4454 ? 166.325 150.834 175.714 1.00 62.40  ? 4454 GLU A N     1 
ATOM   22629 C CA    . GLU A 1 4454 ? 167.618 150.849 176.389 1.00 62.40  ? 4454 GLU A CA    1 
ATOM   22630 C C     . GLU A 1 4454 ? 167.594 149.998 177.655 1.00 62.40  ? 4454 GLU A C     1 
ATOM   22631 O O     . GLU A 1 4454 ? 168.621 149.425 178.039 1.00 62.40  ? 4454 GLU A O     1 
ATOM   22632 C CB    . GLU A 1 4454 ? 168.047 152.284 176.688 1.00 62.40  ? 4454 GLU A CB    1 
ATOM   22633 C CG    . GLU A 1 4454 ? 168.043 153.174 175.455 1.00 62.40  ? 4454 GLU A CG    1 
ATOM   22634 C CD    . GLU A 1 4454 ? 168.515 154.582 175.740 1.00 62.40  ? 4454 GLU A CD    1 
ATOM   22635 O OE1   . GLU A 1 4454 ? 168.334 155.460 174.870 1.00 62.40  ? 4454 GLU A OE1   1 
ATOM   22636 O OE2   . GLU A 1 4454 ? 169.085 154.808 176.824 1.00 62.40  ? 4454 GLU A OE2   1 
ATOM   22637 N N     . LEU A 1 4455 ? 166.437 149.887 178.312 1.00 57.55  ? 4455 LEU A N     1 
ATOM   22638 C CA    . LEU A 1 4455 ? 166.346 149.009 179.477 1.00 57.55  ? 4455 LEU A CA    1 
ATOM   22639 C C     . LEU A 1 4455 ? 166.468 147.542 179.080 1.00 57.55  ? 4455 LEU A C     1 
ATOM   22640 O O     . LEU A 1 4455 ? 167.215 146.780 179.705 1.00 57.55  ? 4455 LEU A O     1 
ATOM   22641 C CB    . LEU A 1 4455 ? 165.040 149.247 180.235 1.00 57.55  ? 4455 LEU A CB    1 
ATOM   22642 C CG    . LEU A 1 4455 ? 164.898 150.542 181.032 1.00 57.55  ? 4455 LEU A CG    1 
ATOM   22643 C CD1   . LEU A 1 4455 ? 163.540 150.582 181.708 1.00 57.55  ? 4455 LEU A CD1   1 
ATOM   22644 C CD2   . LEU A 1 4455 ? 166.013 150.666 182.055 1.00 57.55  ? 4455 LEU A CD2   1 
ATOM   22645 N N     . VAL A 1 4456 ? 165.733 147.123 178.047 1.00 62.59  ? 4456 VAL A N     1 
ATOM   22646 C CA    . VAL A 1 4456 ? 165.763 145.718 177.640 1.00 62.59  ? 4456 VAL A CA    1 
ATOM   22647 C C     . VAL A 1 4456 ? 167.136 145.360 177.083 1.00 62.59  ? 4456 VAL A C     1 
ATOM   22648 O O     . VAL A 1 4456 ? 167.622 144.236 177.254 1.00 62.59  ? 4456 VAL A O     1 
ATOM   22649 C CB    . VAL A 1 4456 ? 164.638 145.408 176.633 1.00 62.59  ? 4456 VAL A CB    1 
ATOM   22650 C CG1   . VAL A 1 4456 ? 163.280 145.717 177.237 1.00 62.59  ? 4456 VAL A CG1   1 
ATOM   22651 C CG2   . VAL A 1 4456 ? 164.828 146.159 175.327 1.00 62.59  ? 4456 VAL A CG2   1 
ATOM   22652 N N     . LYS A 1 4457 ? 167.784 146.314 176.409 1.00 57.24  ? 4457 LYS A N     1 
ATOM   22653 C CA    . LYS A 1 4457 ? 169.126 146.055 175.903 1.00 57.24  ? 4457 LYS A CA    1 
ATOM   22654 C C     . LYS A 1 4457 ? 170.185 146.178 176.991 1.00 57.24  ? 4457 LYS A C     1 
ATOM   22655 O O     . LYS A 1 4457 ? 171.336 145.790 176.764 1.00 57.24  ? 4457 LYS A O     1 
ATOM   22656 C CB    . LYS A 1 4457 ? 169.442 146.996 174.741 1.00 57.24  ? 4457 LYS A CB    1 
ATOM   22657 C CG    . LYS A 1 4457 ? 168.863 146.534 173.415 1.00 57.24  ? 4457 LYS A CG    1 
ATOM   22658 C CD    . LYS A 1 4457 ? 169.489 145.218 172.979 1.00 57.24  ? 4457 LYS A CD    1 
ATOM   22659 C CE    . LYS A 1 4457 ? 168.731 144.595 171.819 1.00 57.24  ? 4457 LYS A CE    1 
ATOM   22660 N NZ    . LYS A 1 4457 ? 169.155 145.157 170.509 1.00 57.24  ? 4457 LYS A NZ    1 
ATOM   22661 N N     . GLY A 1 4458 ? 169.828 146.700 178.160 1.00 52.31  ? 4458 GLY A N     1 
ATOM   22662 C CA    . GLY A 1 4458 ? 170.745 146.786 179.275 1.00 52.31  ? 4458 GLY A CA    1 
ATOM   22663 C C     . GLY A 1 4458 ? 171.579 148.045 179.352 1.00 52.31  ? 4458 GLY A C     1 
ATOM   22664 O O     . GLY A 1 4458 ? 172.502 148.102 180.172 1.00 52.31  ? 4458 GLY A O     1 
ATOM   22665 N N     . ILE A 1 4459 ? 171.289 149.051 178.533 1.00 53.31  ? 4459 ILE A N     1 
ATOM   22666 C CA    . ILE A 1 4459 ? 172.032 150.305 178.523 1.00 53.31  ? 4459 ILE A CA    1 
ATOM   22667 C C     . ILE A 1 4459 ? 171.260 151.331 179.338 1.00 53.31  ? 4459 ILE A C     1 
ATOM   22668 O O     . ILE A 1 4459 ? 170.046 151.491 179.159 1.00 53.31  ? 4459 ILE A O     1 
ATOM   22669 C CB    . ILE A 1 4459 ? 172.270 150.805 177.087 1.00 53.31  ? 4459 ILE A CB    1 
ATOM   22670 C CG1   . ILE A 1 4459 ? 173.194 149.850 176.324 1.00 53.31  ? 4459 ILE A CG1   1 
ATOM   22671 C CG2   . ILE A 1 4459 ? 172.843 152.214 177.094 1.00 53.31  ? 4459 ILE A CG2   1 
ATOM   22672 C CD1   . ILE A 1 4459 ? 172.478 148.750 175.572 1.00 53.31  ? 4459 ILE A CD1   1 
ATOM   22673 N N     . LEU A 1 4460 ? 171.958 152.019 180.238 1.00 49.85  ? 4460 LEU A N     1 
ATOM   22674 C CA    . LEU A 1 4460 ? 171.316 153.019 181.074 1.00 49.85  ? 4460 LEU A CA    1 
ATOM   22675 C C     . LEU A 1 4460 ? 170.718 154.130 180.211 1.00 49.85  ? 4460 LEU A C     1 
ATOM   22676 O O     . LEU A 1 4460 ? 171.308 154.535 179.206 1.00 49.85  ? 4460 LEU A O     1 
ATOM   22677 C CB    . LEU A 1 4460 ? 172.310 153.614 182.070 1.00 49.85  ? 4460 LEU A CB    1 
ATOM   22678 C CG    . LEU A 1 4460 ? 173.385 154.583 181.564 1.00 49.85  ? 4460 LEU A CG    1 
ATOM   22679 C CD1   . LEU A 1 4460 ? 173.998 155.348 182.723 1.00 49.85  ? 4460 LEU A CD1   1 
ATOM   22680 C CD2   . LEU A 1 4460 ? 174.474 153.861 180.781 1.00 49.85  ? 4460 LEU A CD2   1 
ATOM   22681 N N     . PRO A 1 4461 ? 169.529 154.614 180.565 1.00 49.91  ? 4461 PRO A N     1 
ATOM   22682 C CA    . PRO A 1 4461 ? 168.924 155.705 179.794 1.00 49.91  ? 4461 PRO A CA    1 
ATOM   22683 C C     . PRO A 1 4461 ? 169.769 156.966 179.859 1.00 49.91  ? 4461 PRO A C     1 
ATOM   22684 O O     . PRO A 1 4461 ? 170.284 157.339 180.915 1.00 49.91  ? 4461 PRO A O     1 
ATOM   22685 C CB    . PRO A 1 4461 ? 167.561 155.906 180.467 1.00 49.91  ? 4461 PRO A CB    1 
ATOM   22686 C CG    . PRO A 1 4461 ? 167.301 154.625 181.196 1.00 49.91  ? 4461 PRO A CG    1 
ATOM   22687 C CD    . PRO A 1 4461 ? 168.643 154.140 181.639 1.00 49.91  ? 4461 PRO A CD    1 
ATOM   22688 N N     . ARG A 1 4462 ? 169.909 157.624 178.706 1.00 55.27  ? 4462 ARG A N     1 
ATOM   22689 C CA    . ARG A 1 4462 ? 170.656 158.876 178.662 1.00 55.27  ? 4462 ARG A CA    1 
ATOM   22690 C C     . ARG A 1 4462 ? 169.955 159.967 179.457 1.00 55.27  ? 4462 ARG A C     1 
ATOM   22691 O O     . ARG A 1 4462 ? 170.615 160.823 180.056 1.00 55.27  ? 4462 ARG A O     1 
ATOM   22692 C CB    . ARG A 1 4462 ? 170.861 159.321 177.215 1.00 55.27  ? 4462 ARG A CB    1 
ATOM   22693 C CG    . ARG A 1 4462 ? 172.174 160.043 176.974 1.00 55.27  ? 4462 ARG A CG    1 
ATOM   22694 C CD    . ARG A 1 4462 ? 172.042 161.076 175.861 1.00 55.27  ? 4462 ARG A CD    1 
ATOM   22695 N NE    . ARG A 1 4462 ? 171.229 162.227 176.244 1.00 55.27  ? 4462 ARG A NE    1 
ATOM   22696 C CZ    . ARG A 1 4462 ? 171.514 163.070 177.229 1.00 55.27  ? 4462 ARG A CZ    1 
ATOM   22697 N NH1   . ARG A 1 4462 ? 172.625 162.959 177.940 1.00 55.27  ? 4462 ARG A NH1   1 
ATOM   22698 N NH2   . ARG A 1 4462 ? 170.667 164.059 177.499 1.00 55.27  ? 4462 ARG A NH2   1 
ATOM   22699 N N     . SER A 1 4463 ? 168.621 159.953 179.477 1.00 52.21  ? 4463 SER A N     1 
ATOM   22700 C CA    . SER A 1 4463 ? 167.875 160.927 180.261 1.00 52.21  ? 4463 SER A CA    1 
ATOM   22701 C C     . SER A 1 4463 ? 167.964 160.655 181.755 1.00 52.21  ? 4463 SER A C     1 
ATOM   22702 O O     . SER A 1 4463 ? 167.516 161.487 182.550 1.00 52.21  ? 4463 SER A O     1 
ATOM   22703 C CB    . SER A 1 4463 ? 166.413 160.946 179.820 1.00 52.21  ? 4463 SER A CB    1 
ATOM   22704 O OG    . SER A 1 4463 ? 165.595 161.562 180.800 1.00 52.21  ? 4463 SER A OG    1 
ATOM   22705 N N     . TRP A 1 4464 ? 168.516 159.510 182.155 1.00 47.55  ? 4464 TRP A N     1 
ATOM   22706 C CA    . TRP A 1 4464 ? 168.702 159.206 183.567 1.00 47.55  ? 4464 TRP A CA    1 
ATOM   22707 C C     . TRP A 1 4464 ? 170.057 159.656 184.091 1.00 47.55  ? 4464 TRP A C     1 
ATOM   22708 O O     . TRP A 1 4464 ? 170.208 159.862 185.301 1.00 47.55  ? 4464 TRP A O     1 
ATOM   22709 C CB    . TRP A 1 4464 ? 168.545 157.704 183.814 1.00 47.55  ? 4464 TRP A CB    1 
ATOM   22710 C CG    . TRP A 1 4464 ? 167.126 157.244 183.876 1.00 47.55  ? 4464 TRP A CG    1 
ATOM   22711 C CD1   . TRP A 1 4464 ? 166.019 157.946 183.504 1.00 47.55  ? 4464 TRP A CD1   1 
ATOM   22712 C CD2   . TRP A 1 4464 ? 166.659 155.976 184.348 1.00 47.55  ? 4464 TRP A CD2   1 
ATOM   22713 N NE1   . TRP A 1 4464 ? 164.890 157.191 183.709 1.00 47.55  ? 4464 TRP A NE1   1 
ATOM   22714 C CE2   . TRP A 1 4464 ? 165.256 155.977 184.228 1.00 47.55  ? 4464 TRP A CE2   1 
ATOM   22715 C CE3   . TRP A 1 4464 ? 167.290 154.838 184.859 1.00 47.55  ? 4464 TRP A CE3   1 
ATOM   22716 C CZ2   . TRP A 1 4464 ? 164.475 154.887 184.600 1.00 47.55  ? 4464 TRP A CZ2   1 
ATOM   22717 C CZ3   . TRP A 1 4464 ? 166.514 153.758 185.227 1.00 47.55  ? 4464 TRP A CZ3   1 
ATOM   22718 C CH2   . TRP A 1 4464 ? 165.121 153.789 185.097 1.00 47.55  ? 4464 TRP A CH2   1 
ATOM   22719 N N     . SER A 1 4465 ? 171.045 159.812 183.213 1.00 47.49  ? 4465 SER A N     1 
ATOM   22720 C CA    . SER A 1 4465 ? 172.406 160.158 183.621 1.00 47.49  ? 4465 SER A CA    1 
ATOM   22721 C C     . SER A 1 4465 ? 172.516 161.672 183.746 1.00 47.49  ? 4465 SER A C     1 
ATOM   22722 O O     . SER A 1 4465 ? 172.807 162.381 182.782 1.00 47.49  ? 4465 SER A O     1 
ATOM   22723 C CB    . SER A 1 4465 ? 173.420 159.607 182.627 1.00 47.49  ? 4465 SER A CB    1 
ATOM   22724 O OG    . SER A 1 4465 ? 174.658 160.288 182.735 1.00 47.49  ? 4465 SER A OG    1 
ATOM   22725 N N     . HIS A 1 4466 ? 172.281 162.173 184.958 1.00 44.84  ? 4466 HIS A N     1 
ATOM   22726 C CA    . HIS A 1 4466 ? 172.462 163.585 185.264 1.00 44.84  ? 4466 HIS A CA    1 
ATOM   22727 C C     . HIS A 1 4466 ? 173.751 163.871 186.021 1.00 44.84  ? 4466 HIS A C     1 
ATOM   22728 O O     . HIS A 1 4466 ? 174.101 165.043 186.192 1.00 44.84  ? 4466 HIS A O     1 
ATOM   22729 C CB    . HIS A 1 4466 ? 171.273 164.113 186.074 1.00 44.84  ? 4466 HIS A CB    1 
ATOM   22730 C CG    . HIS A 1 4466 ? 170.036 164.332 185.260 1.00 44.84  ? 4466 HIS A CG    1 
ATOM   22731 N ND1   . HIS A 1 4466 ? 169.123 163.332 185.008 1.00 44.84  ? 4466 HIS A ND1   1 
ATOM   22732 C CD2   . HIS A 1 4466 ? 169.560 165.441 184.646 1.00 44.84  ? 4466 HIS A CD2   1 
ATOM   22733 C CE1   . HIS A 1 4466 ? 168.137 163.815 184.272 1.00 44.84  ? 4466 HIS A CE1   1 
ATOM   22734 N NE2   . HIS A 1 4466 ? 168.379 165.092 184.038 1.00 44.84  ? 4466 HIS A NE2   1 
ATOM   22735 N N     . TYR A 1 4467 ? 174.457 162.844 186.475 1.00 34.42  ? 4467 TYR A N     1 
ATOM   22736 C CA    . TYR A 1 4467 ? 175.721 162.993 187.179 1.00 34.42  ? 4467 TYR A CA    1 
ATOM   22737 C C     . TYR A 1 4467 ? 176.793 162.171 186.470 1.00 34.42  ? 4467 TYR A C     1 
ATOM   22738 O O     . TYR A 1 4467 ? 176.533 161.502 185.467 1.00 34.42  ? 4467 TYR A O     1 
ATOM   22739 C CB    . TYR A 1 4467 ? 175.581 162.579 188.647 1.00 34.42  ? 4467 TYR A CB    1 
ATOM   22740 C CG    . TYR A 1 4467 ? 175.032 161.186 188.854 1.00 34.42  ? 4467 TYR A CG    1 
ATOM   22741 C CD1   . TYR A 1 4467 ? 175.870 160.081 188.849 1.00 34.42  ? 4467 TYR A CD1   1 
ATOM   22742 C CD2   . TYR A 1 4467 ? 173.676 160.976 189.054 1.00 34.42  ? 4467 TYR A CD2   1 
ATOM   22743 C CE1   . TYR A 1 4467 ? 175.375 158.807 189.040 1.00 34.42  ? 4467 TYR A CE1   1 
ATOM   22744 C CE2   . TYR A 1 4467 ? 173.171 159.705 189.246 1.00 34.42  ? 4467 TYR A CE2   1 
ATOM   22745 C CZ    . TYR A 1 4467 ? 174.025 158.625 189.237 1.00 34.42  ? 4467 TYR A CZ    1 
ATOM   22746 O OH    . TYR A 1 4467 ? 173.530 157.356 189.426 1.00 34.42  ? 4467 TYR A OH    1 
ATOM   22747 N N     . THR A 1 4468 ? 178.011 162.229 187.000 1.00 31.64  ? 4468 THR A N     1 
ATOM   22748 C CA    . THR A 1 4468 ? 179.118 161.506 186.390 1.00 31.64  ? 4468 THR A CA    1 
ATOM   22749 C C     . THR A 1 4468 ? 178.968 160.008 186.623 1.00 31.64  ? 4468 THR A C     1 
ATOM   22750 O O     . THR A 1 4468 ? 178.798 159.555 187.759 1.00 31.64  ? 4468 THR A O     1 
ATOM   22751 C CB    . THR A 1 4468 ? 180.449 161.997 186.955 1.00 31.64  ? 4468 THR A CB    1 
ATOM   22752 O OG1   . THR A 1 4468 ? 180.645 163.370 186.594 1.00 31.64  ? 4468 THR A OG1   1 
ATOM   22753 C CG2   . THR A 1 4468 ? 181.589 161.168 186.401 1.00 31.64  ? 4468 THR A CG2   1 
ATOM   22754 N N     . VAL A 1 4469 ? 179.042 159.241 185.541 1.00 31.53  ? 4469 VAL A N     1 
ATOM   22755 C CA    . VAL A 1 4469 ? 178.849 157.794 185.586 1.00 31.53  ? 4469 VAL A CA    1 
ATOM   22756 C C     . VAL A 1 4469 ? 180.029 157.124 184.891 1.00 31.53  ? 4469 VAL A C     1 
ATOM   22757 O O     . VAL A 1 4469 ? 180.464 157.594 183.829 1.00 31.53  ? 4469 VAL A O     1 
ATOM   22758 C CB    . VAL A 1 4469 ? 177.517 157.394 184.930 1.00 31.53  ? 4469 VAL A CB    1 
ATOM   22759 C CG1   . VAL A 1 4469 ? 177.354 155.885 184.908 1.00 31.53  ? 4469 VAL A CG1   1 
ATOM   22760 C CG2   . VAL A 1 4469 ? 176.349 158.043 185.656 1.00 31.53  ? 4469 VAL A CG2   1 
ATOM   22761 N N     . PRO A 1 4470 ? 180.587 156.050 185.450 1.00 30.65  ? 4470 PRO A N     1 
ATOM   22762 C CA    . PRO A 1 4470 ? 181.637 155.315 184.735 1.00 30.65  ? 4470 PRO A CA    1 
ATOM   22763 C C     . PRO A 1 4470 ? 181.122 154.785 183.406 1.00 30.65  ? 4470 PRO A C     1 
ATOM   22764 O O     . PRO A 1 4470 ? 179.964 154.382 183.284 1.00 30.65  ? 4470 PRO A O     1 
ATOM   22765 C CB    . PRO A 1 4470 ? 181.996 154.177 185.697 1.00 30.65  ? 4470 PRO A CB    1 
ATOM   22766 C CG    . PRO A 1 4470 ? 181.551 154.650 187.035 1.00 30.65  ? 4470 PRO A CG    1 
ATOM   22767 C CD    . PRO A 1 4470 ? 180.349 155.509 186.798 1.00 30.65  ? 4470 PRO A CD    1 
ATOM   22768 N N     . ALA A 1 4471 ? 181.997 154.798 182.403 1.00 33.65  ? 4471 ALA A N     1 
ATOM   22769 C CA    . ALA A 1 4471 ? 181.606 154.385 181.063 1.00 33.65  ? 4471 ALA A CA    1 
ATOM   22770 C C     . ALA A 1 4471 ? 181.201 152.917 181.049 1.00 33.65  ? 4471 ALA A C     1 
ATOM   22771 O O     . ALA A 1 4471 ? 181.846 152.074 181.679 1.00 33.65  ? 4471 ALA A O     1 
ATOM   22772 C CB    . ALA A 1 4471 ? 182.751 154.628 180.081 1.00 33.65  ? 4471 ALA A CB    1 
ATOM   22773 N N     . GLY A 1 4472 ? 180.126 152.616 180.325 1.00 33.49  ? 4472 GLY A N     1 
ATOM   22774 C CA    . GLY A 1 4472 ? 179.634 151.257 180.223 1.00 33.49  ? 4472 GLY A CA    1 
ATOM   22775 C C     . GLY A 1 4472 ? 179.138 150.685 181.534 1.00 33.49  ? 4472 GLY A C     1 
ATOM   22776 O O     . GLY A 1 4472 ? 179.472 149.551 181.887 1.00 33.49  ? 4472 GLY A O     1 
ATOM   22777 N N     . MET A 1 4473 ? 178.342 151.459 182.268 1.00 37.21  ? 4473 MET A N     1 
ATOM   22778 C CA    . MET A 1 4473 ? 177.783 151.008 183.534 1.00 37.21  ? 4473 MET A CA    1 
ATOM   22779 C C     . MET A 1 4473 ? 176.401 150.409 183.304 1.00 37.21  ? 4473 MET A C     1 
ATOM   22780 O O     . MET A 1 4473 ? 175.535 151.043 182.693 1.00 37.21  ? 4473 MET A O     1 
ATOM   22781 C CB    . MET A 1 4473 ? 177.701 152.161 184.535 1.00 37.21  ? 4473 MET A CB    1 
ATOM   22782 C CG    . MET A 1 4473 ? 177.421 151.714 185.961 1.00 37.21  ? 4473 MET A CG    1 
ATOM   22783 S SD    . MET A 1 4473 ? 177.205 153.085 187.110 1.00 37.21  ? 4473 MET A SD    1 
ATOM   22784 C CE    . MET A 1 4473 ? 178.017 152.434 188.567 1.00 37.21  ? 4473 MET A CE    1 
ATOM   22785 N N     . THR A 1 4474 ? 176.203 149.190 183.795 1.00 38.82  ? 4474 THR A N     1 
ATOM   22786 C CA    . THR A 1 4474 ? 174.941 148.489 183.611 1.00 38.82  ? 4474 THR A CA    1 
ATOM   22787 C C     . THR A 1 4474 ? 173.834 149.170 184.412 1.00 38.82  ? 4474 THR A C     1 
ATOM   22788 O O     . THR A 1 4474 ? 174.085 149.831 185.423 1.00 38.82  ? 4474 THR A O     1 
ATOM   22789 C CB    . THR A 1 4474 ? 175.090 147.024 184.031 1.00 38.82  ? 4474 THR A CB    1 
ATOM   22790 O OG1   . THR A 1 4474 ? 176.244 146.466 183.392 1.00 38.82  ? 4474 THR A OG1   1 
ATOM   22791 C CG2   . THR A 1 4474 ? 173.874 146.206 183.619 1.00 38.82  ? 4474 THR A CG2   1 
ATOM   22792 N N     . VAL A 1 4475 ? 172.595 149.009 183.940 1.00 40.44  ? 4475 VAL A N     1 
ATOM   22793 C CA    . VAL A 1 4475 ? 171.458 149.673 184.573 1.00 40.44  ? 4475 VAL A CA    1 
ATOM   22794 C C     . VAL A 1 4475 ? 171.276 149.185 186.005 1.00 40.44  ? 4475 VAL A C     1 
ATOM   22795 O O     . VAL A 1 4475 ? 170.875 149.952 186.887 1.00 40.44  ? 4475 VAL A O     1 
ATOM   22796 C CB    . VAL A 1 4475 ? 170.182 149.462 183.740 1.00 40.44  ? 4475 VAL A CB    1 
ATOM   22797 C CG1   . VAL A 1 4475 ? 169.094 150.421 184.190 1.00 40.44  ? 4475 VAL A CG1   1 
ATOM   22798 C CG2   . VAL A 1 4475 ? 170.477 149.640 182.265 1.00 40.44  ? 4475 VAL A CG2   1 
ATOM   22799 N N     . ILE A 1 4476 ? 171.543 147.902 186.257 1.00 39.86  ? 4476 ILE A N     1 
ATOM   22800 C CA    . ILE A 1 4476 ? 171.418 147.375 187.615 1.00 39.86  ? 4476 ILE A CA    1 
ATOM   22801 C C     . ILE A 1 4476 ? 172.417 148.055 188.545 1.00 39.86  ? 4476 ILE A C     1 
ATOM   22802 O O     . ILE A 1 4476 ? 172.073 148.470 189.661 1.00 39.86  ? 4476 ILE A O     1 
ATOM   22803 C CB    . ILE A 1 4476 ? 171.592 145.844 187.618 1.00 39.86  ? 4476 ILE A CB    1 
ATOM   22804 C CG1   . ILE A 1 4476 ? 170.469 145.164 186.828 1.00 39.86  ? 4476 ILE A CG1   1 
ATOM   22805 C CG2   . ILE A 1 4476 ? 171.635 145.316 189.042 1.00 39.86  ? 4476 ILE A CG2   1 
ATOM   22806 C CD1   . ILE A 1 4476 ? 170.775 144.948 185.358 1.00 39.86  ? 4476 ILE A CD1   1 
ATOM   22807 N N     . GLN A 1 4477 ? 173.667 148.185 188.100 1.00 39.50  ? 4477 GLN A N     1 
ATOM   22808 C CA    . GLN A 1 4477 ? 174.663 148.888 188.900 1.00 39.50  ? 4477 GLN A CA    1 
ATOM   22809 C C     . GLN A 1 4477 ? 174.275 150.347 189.090 1.00 39.50  ? 4477 GLN A C     1 
ATOM   22810 O O     . GLN A 1 4477 ? 174.449 150.908 190.179 1.00 39.50  ? 4477 GLN A O     1 
ATOM   22811 C CB    . GLN A 1 4477 ? 176.037 148.774 188.242 1.00 39.50  ? 4477 GLN A CB    1 
ATOM   22812 C CG    . GLN A 1 4477 ? 176.289 147.431 187.578 1.00 39.50  ? 4477 GLN A CG    1 
ATOM   22813 C CD    . GLN A 1 4477 ? 177.529 147.432 186.708 1.00 39.50  ? 4477 GLN A CD    1 
ATOM   22814 O OE1   . GLN A 1 4477 ? 178.261 148.419 186.651 1.00 39.50  ? 4477 GLN A OE1   1 
ATOM   22815 N NE2   . GLN A 1 4477 ? 177.772 146.320 186.025 1.00 39.50  ? 4477 GLN A NE2   1 
ATOM   22816 N N     . TRP A 1 4478 ? 173.740 150.975 188.041 1.00 37.36  ? 4478 TRP A N     1 
ATOM   22817 C CA    . TRP A 1 4478 ? 173.324 152.369 188.141 1.00 37.36  ? 4478 TRP A CA    1 
ATOM   22818 C C     . TRP A 1 4478 ? 172.227 152.542 189.182 1.00 37.36  ? 4478 TRP A C     1 
ATOM   22819 O O     . TRP A 1 4478 ? 172.279 153.465 190.000 1.00 37.36  ? 4478 TRP A O     1 
ATOM   22820 C CB    . TRP A 1 4478 ? 172.870 152.876 186.770 1.00 37.36  ? 4478 TRP A CB    1 
ATOM   22821 C CG    . TRP A 1 4478 ? 172.648 154.363 186.694 1.00 37.36  ? 4478 TRP A CG    1 
ATOM   22822 C CD1   . TRP A 1 4478 ? 173.442 155.270 186.061 1.00 37.36  ? 4478 TRP A CD1   1 
ATOM   22823 C CD2   . TRP A 1 4478 ? 171.525 155.101 187.201 1.00 37.36  ? 4478 TRP A CD2   1 
ATOM   22824 N NE1   . TRP A 1 4478 ? 172.912 156.531 186.177 1.00 37.36  ? 4478 TRP A NE1   1 
ATOM   22825 C CE2   . TRP A 1 4478 ? 171.732 156.454 186.869 1.00 37.36  ? 4478 TRP A CE2   1 
ATOM   22826 C CE3   . TRP A 1 4478 ? 170.374 154.753 187.914 1.00 37.36  ? 4478 TRP A CE3   1 
ATOM   22827 C CZ2   . TRP A 1 4478 ? 170.835 157.456 187.227 1.00 37.36  ? 4478 TRP A CZ2   1 
ATOM   22828 C CZ3   . TRP A 1 4478 ? 169.487 155.750 188.271 1.00 37.36  ? 4478 TRP A CZ3   1 
ATOM   22829 C CH2   . TRP A 1 4478 ? 169.721 157.085 187.926 1.00 37.36  ? 4478 TRP A CH2   1 
ATOM   22830 N N     . VAL A 1 4479 ? 171.225 151.660 189.175 1.00 38.82  ? 4479 VAL A N     1 
ATOM   22831 C CA    . VAL A 1 4479 ? 170.124 151.823 190.119 1.00 38.82  ? 4479 VAL A CA    1 
ATOM   22832 C C     . VAL A 1 4479 ? 170.570 151.489 191.537 1.00 38.82  ? 4479 VAL A C     1 
ATOM   22833 O O     . VAL A 1 4479 ? 170.108 152.118 192.495 1.00 38.82  ? 4479 VAL A O     1 
ATOM   22834 C CB    . VAL A 1 4479 ? 168.891 151.001 189.696 1.00 38.82  ? 4479 VAL A CB    1 
ATOM   22835 C CG1   . VAL A 1 4479 ? 168.390 151.461 188.336 1.00 38.82  ? 4479 VAL A CG1   1 
ATOM   22836 C CG2   . VAL A 1 4479 ? 169.188 149.516 189.689 1.00 38.82  ? 4479 VAL A CG2   1 
ATOM   22837 N N     . SER A 1 4480 ? 171.474 150.520 191.709 1.00 38.67  ? 4480 SER A N     1 
ATOM   22838 C CA    . SER A 1 4480 ? 171.996 150.256 193.049 1.00 38.67  ? 4480 SER A CA    1 
ATOM   22839 C C     . SER A 1 4480 ? 172.778 151.453 193.582 1.00 38.67  ? 4480 SER A C     1 
ATOM   22840 O O     . SER A 1 4480 ? 172.600 151.863 194.740 1.00 38.67  ? 4480 SER A O     1 
ATOM   22841 C CB    . SER A 1 4480 ? 172.871 149.003 193.035 1.00 38.67  ? 4480 SER A CB    1 
ATOM   22842 O OG    . SER A 1 4480 ? 173.981 149.167 192.171 1.00 38.67  ? 4480 SER A OG    1 
ATOM   22843 N N     . ASP A 1 4481 ? 173.640 152.038 192.745 1.00 37.15  ? 4481 ASP A N     1 
ATOM   22844 C CA    . ASP A 1 4481 ? 174.402 153.208 193.164 1.00 37.15  ? 4481 ASP A CA    1 
ATOM   22845 C C     . ASP A 1 4481 ? 173.474 154.379 193.462 1.00 37.15  ? 4481 ASP A C     1 
ATOM   22846 O O     . ASP A 1 4481 ? 173.685 155.119 194.430 1.00 37.15  ? 4481 ASP A O     1 
ATOM   22847 C CB    . ASP A 1 4481 ? 175.422 153.576 192.085 1.00 37.15  ? 4481 ASP A CB    1 
ATOM   22848 C CG    . ASP A 1 4481 ? 176.258 154.788 192.452 1.00 37.15  ? 4481 ASP A CG    1 
ATOM   22849 O OD1   . ASP A 1 4481 ? 176.383 155.091 193.657 1.00 37.15  ? 4481 ASP A OD1   1 
ATOM   22850 O OD2   . ASP A 1 4481 ? 176.793 155.441 191.532 1.00 37.15  ? 4481 ASP A OD2   1 
ATOM   22851 N N     . PHE A 1 4482 ? 172.435 154.559 192.643 1.00 36.79  ? 4482 PHE A N     1 
ATOM   22852 C CA    . PHE A 1 4482 ? 171.472 155.627 192.884 1.00 36.79  ? 4482 PHE A CA    1 
ATOM   22853 C C     . PHE A 1 4482 ? 170.720 155.413 194.189 1.00 36.79  ? 4482 PHE A C     1 
ATOM   22854 O O     . PHE A 1 4482 ? 170.455 156.372 194.921 1.00 36.79  ? 4482 PHE A O     1 
ATOM   22855 C CB    . PHE A 1 4482 ? 170.492 155.728 191.718 1.00 36.79  ? 4482 PHE A CB    1 
ATOM   22856 C CG    . PHE A 1 4482 ? 169.678 156.985 191.727 1.00 36.79  ? 4482 PHE A CG    1 
ATOM   22857 C CD1   . PHE A 1 4482 ? 168.324 156.946 192.009 1.00 36.79  ? 4482 PHE A CD1   1 
ATOM   22858 C CD2   . PHE A 1 4482 ? 170.268 158.208 191.470 1.00 36.79  ? 4482 PHE A CD2   1 
ATOM   22859 C CE1   . PHE A 1 4482 ? 167.574 158.103 192.023 1.00 36.79  ? 4482 PHE A CE1   1 
ATOM   22860 C CE2   . PHE A 1 4482 ? 169.523 159.367 191.487 1.00 36.79  ? 4482 PHE A CE2   1 
ATOM   22861 C CZ    . PHE A 1 4482 ? 168.174 159.315 191.761 1.00 36.79  ? 4482 PHE A CZ    1 
ATOM   22862 N N     . SER A 1 4483 ? 170.352 154.168 194.492 1.00 36.33  ? 4483 SER A N     1 
ATOM   22863 C CA    . SER A 1 4483 ? 169.688 153.888 195.759 1.00 36.33  ? 4483 SER A CA    1 
ATOM   22864 C C     . SER A 1 4483 ? 170.595 154.224 196.933 1.00 36.33  ? 4483 SER A C     1 
ATOM   22865 O O     . SER A 1 4483 ? 170.146 154.806 197.929 1.00 36.33  ? 4483 SER A O     1 
ATOM   22866 C CB    . SER A 1 4483 ? 169.255 152.423 195.812 1.00 36.33  ? 4483 SER A CB    1 
ATOM   22867 O OG    . SER A 1 4483 ? 170.358 151.576 196.079 1.00 36.33  ? 4483 SER A OG    1 
ATOM   22868 N N     . GLU A 1 4484 ? 171.880 153.876 196.830 1.00 36.08  ? 4484 GLU A N     1 
ATOM   22869 C CA    . GLU A 1 4484 ? 172.815 154.229 197.896 1.00 36.08  ? 4484 GLU A CA    1 
ATOM   22870 C C     . GLU A 1 4484 ? 172.945 155.743 198.045 1.00 36.08  ? 4484 GLU A C     1 
ATOM   22871 O O     . GLU A 1 4484 ? 172.964 156.269 199.168 1.00 36.08  ? 4484 GLU A O     1 
ATOM   22872 C CB    . GLU A 1 4484 ? 174.179 153.594 197.631 1.00 36.08  ? 4484 GLU A CB    1 
ATOM   22873 C CG    . GLU A 1 4484 ? 175.191 153.787 198.754 1.00 36.08  ? 4484 GLU A CG    1 
ATOM   22874 C CD    . GLU A 1 4484 ? 174.852 153.014 200.020 1.00 36.08  ? 4484 GLU A CD    1 
ATOM   22875 O OE1   . GLU A 1 4484 ? 173.815 152.317 200.053 1.00 36.08  ? 4484 GLU A OE1   1 
ATOM   22876 O OE2   . GLU A 1 4484 ? 175.629 153.108 200.992 1.00 36.08  ? 4484 GLU A OE2   1 
ATOM   22877 N N     . ARG A 1 4485 ? 173.034 156.462 196.922 1.00 31.36  ? 4485 ARG A N     1 
ATOM   22878 C CA    . ARG A 1 4485 ? 173.136 157.918 196.980 1.00 31.36  ? 4485 ARG A CA    1 
ATOM   22879 C C     . ARG A 1 4485 ? 171.891 158.536 197.602 1.00 31.36  ? 4485 ARG A C     1 
ATOM   22880 O O     . ARG A 1 4485 ? 171.985 159.486 198.388 1.00 31.36  ? 4485 ARG A O     1 
ATOM   22881 C CB    . ARG A 1 4485 ? 173.368 158.491 195.581 1.00 31.36  ? 4485 ARG A CB    1 
ATOM   22882 C CG    . ARG A 1 4485 ? 174.659 158.045 194.920 1.00 31.36  ? 4485 ARG A CG    1 
ATOM   22883 C CD    . ARG A 1 4485 ? 174.754 158.575 193.499 1.00 31.36  ? 4485 ARG A CD    1 
ATOM   22884 N NE    . ARG A 1 4485 ? 175.893 158.018 192.780 1.00 31.36  ? 4485 ARG A NE    1 
ATOM   22885 C CZ    . ARG A 1 4485 ? 177.065 158.623 192.648 1.00 31.36  ? 4485 ARG A CZ    1 
ATOM   22886 N NH1   . ARG A 1 4485 ? 177.292 159.813 193.177 1.00 31.36  ? 4485 ARG A NH1   1 
ATOM   22887 N NH2   . ARG A 1 4485 ? 178.034 158.018 191.967 1.00 31.36  ? 4485 ARG A NH2   1 
ATOM   22888 N N     . ILE A 1 4486 ? 170.713 158.016 197.256 1.00 31.71  ? 4486 ILE A N     1 
ATOM   22889 C CA    . ILE A 1 4486 ? 169.472 158.546 197.808 1.00 31.71  ? 4486 ILE A CA    1 
ATOM   22890 C C     . ILE A 1 4486 ? 169.381 158.256 199.301 1.00 31.71  ? 4486 ILE A C     1 
ATOM   22891 O O     . ILE A 1 4486 ? 168.892 159.084 200.076 1.00 31.71  ? 4486 ILE A O     1 
ATOM   22892 C CB    . ILE A 1 4486 ? 168.263 157.986 197.037 1.00 31.71  ? 4486 ILE A CB    1 
ATOM   22893 C CG1   . ILE A 1 4486 ? 168.272 158.502 195.599 1.00 31.71  ? 4486 ILE A CG1   1 
ATOM   22894 C CG2   . ILE A 1 4486 ? 166.963 158.367 197.719 1.00 31.71  ? 4486 ILE A CG2   1 
ATOM   22895 C CD1   . ILE A 1 4486 ? 168.206 160.007 195.494 1.00 31.71  ? 4486 ILE A CD1   1 
ATOM   22896 N N     . LYS A 1 4487 ? 169.852 157.084 199.732 1.00 32.94  ? 4487 LYS A N     1 
ATOM   22897 C CA    . LYS A 1 4487 ? 169.892 156.801 201.165 1.00 32.94  ? 4487 LYS A CA    1 
ATOM   22898 C C     . LYS A 1 4487 ? 170.813 157.775 201.891 1.00 32.94  ? 4487 LYS A C     1 
ATOM   22899 O O     . LYS A 1 4487 ? 170.474 158.281 202.971 1.00 32.94  ? 4487 LYS A O     1 
ATOM   22900 C CB    . LYS A 1 4487 ? 170.338 155.360 201.407 1.00 32.94  ? 4487 LYS A CB    1 
ATOM   22901 C CG    . LYS A 1 4487 ? 169.327 154.315 200.969 1.00 32.94  ? 4487 LYS A CG    1 
ATOM   22902 C CD    . LYS A 1 4487 ? 169.694 152.938 201.492 1.00 32.94  ? 4487 LYS A CD    1 
ATOM   22903 C CE    . LYS A 1 4487 ? 169.486 151.875 200.427 1.00 32.94  ? 4487 LYS A CE    1 
ATOM   22904 N NZ    . LYS A 1 4487 ? 168.167 151.199 200.568 1.00 32.94  ? 4487 LYS A NZ    1 
ATOM   22905 N N     . GLN A 1 4488 ? 171.980 158.058 201.309 1.00 30.83  ? 4488 GLN A N     1 
ATOM   22906 C CA    . GLN A 1 4488 ? 172.885 159.022 201.928 1.00 30.83  ? 4488 GLN A CA    1 
ATOM   22907 C C     . GLN A 1 4488 ? 172.251 160.407 201.995 1.00 30.83  ? 4488 GLN A C     1 
ATOM   22908 O O     . GLN A 1 4488 ? 172.370 161.105 203.008 1.00 30.83  ? 4488 GLN A O     1 
ATOM   22909 C CB    . GLN A 1 4488 ? 174.207 159.078 201.167 1.00 30.83  ? 4488 GLN A CB    1 
ATOM   22910 C CG    . GLN A 1 4488 ? 175.137 160.171 201.659 1.00 30.83  ? 4488 GLN A CG    1 
ATOM   22911 C CD    . GLN A 1 4488 ? 176.431 160.231 200.884 1.00 30.83  ? 4488 GLN A CD    1 
ATOM   22912 O OE1   . GLN A 1 4488 ? 177.513 160.190 201.464 1.00 30.83  ? 4488 GLN A OE1   1 
ATOM   22913 N NE2   . GLN A 1 4488 ? 176.329 160.336 199.566 1.00 30.83  ? 4488 GLN A NE2   1 
ATOM   22914 N N     . LEU A 1 4489 ? 171.575 160.823 200.923 1.00 31.01  ? 4489 LEU A N     1 
ATOM   22915 C CA    . LEU A 1 4489 ? 170.926 162.131 200.916 1.00 31.01  ? 4489 LEU A CA    1 
ATOM   22916 C C     . LEU A 1 4489 ? 169.800 162.197 201.940 1.00 31.01  ? 4489 LEU A C     1 
ATOM   22917 O O     . LEU A 1 4489 ? 169.582 163.241 202.566 1.00 31.01  ? 4489 LEU A O     1 
ATOM   22918 C CB    . LEU A 1 4489 ? 170.406 162.452 199.517 1.00 31.01  ? 4489 LEU A CB    1 
ATOM   22919 C CG    . LEU A 1 4489 ? 171.472 162.743 198.460 1.00 31.01  ? 4489 LEU A CG    1 
ATOM   22920 C CD1   . LEU A 1 4489 ? 170.858 163.442 197.261 1.00 31.01  ? 4489 LEU A CD1   1 
ATOM   22921 C CD2   . LEU A 1 4489 ? 172.600 163.575 199.045 1.00 31.01  ? 4489 LEU A CD2   1 
ATOM   22922 N N     . GLN A 1 4490 ? 169.065 161.097 202.118 1.00 32.71  ? 4490 GLN A N     1 
ATOM   22923 C CA    . GLN A 1 4490 ? 168.046 161.052 203.160 1.00 32.71  ? 4490 GLN A CA    1 
ATOM   22924 C C     . GLN A 1 4490 ? 168.667 161.190 204.542 1.00 32.71  ? 4490 GLN A C     1 
ATOM   22925 O O     . GLN A 1 4490 ? 168.118 161.878 205.410 1.00 32.71  ? 4490 GLN A O     1 
ATOM   22926 C CB    . GLN A 1 4490 ? 167.246 159.754 203.060 1.00 32.71  ? 4490 GLN A CB    1 
ATOM   22927 C CG    . GLN A 1 4490 ? 166.102 159.810 202.069 1.00 32.71  ? 4490 GLN A CG    1 
ATOM   22928 C CD    . GLN A 1 4490 ? 165.595 158.436 201.692 1.00 32.71  ? 4490 GLN A CD    1 
ATOM   22929 O OE1   . GLN A 1 4490 ? 165.061 158.237 200.603 1.00 32.71  ? 4490 GLN A OE1   1 
ATOM   22930 N NE2   . GLN A 1 4490 ? 165.760 157.476 202.595 1.00 32.71  ? 4490 GLN A NE2   1 
ATOM   22931 N N     . ASN A 1 4491 ? 169.809 160.536 204.768 1.00 32.54  ? 4491 ASN A N     1 
ATOM   22932 C CA    . ASN A 1 4491 ? 170.509 160.711 206.038 1.00 32.54  ? 4491 ASN A CA    1 
ATOM   22933 C C     . ASN A 1 4491 ? 170.939 162.161 206.231 1.00 32.54  ? 4491 ASN A C     1 
ATOM   22934 O O     . ASN A 1 4491 ? 170.853 162.701 207.340 1.00 32.54  ? 4491 ASN A O     1 
ATOM   22935 C CB    . ASN A 1 4491 ? 171.715 159.777 206.109 1.00 32.54  ? 4491 ASN A CB    1 
ATOM   22936 C CG    . ASN A 1 4491 ? 171.317 158.326 206.281 1.00 32.54  ? 4491 ASN A CG    1 
ATOM   22937 O OD1   . ASN A 1 4491 ? 170.406 158.006 207.044 1.00 32.54  ? 4491 ASN A OD1   1 
ATOM   22938 N ND2   . ASN A 1 4491 ? 172.001 157.436 205.571 1.00 32.54  ? 4491 ASN A ND2   1 
ATOM   22939 N N     . ILE A 1 4492 ? 171.402 162.804 205.157 1.00 33.32  ? 4492 ILE A N     1 
ATOM   22940 C CA    . ILE A 1 4492 ? 171.790 164.213 205.231 1.00 33.32  ? 4492 ILE A CA    1 
ATOM   22941 C C     . ILE A 1 4492 ? 170.594 165.073 205.620 1.00 33.32  ? 4492 ILE A C     1 
ATOM   22942 O O     . ILE A 1 4492 ? 170.695 165.964 206.473 1.00 33.32  ? 4492 ILE A O     1 
ATOM   22943 C CB    . ILE A 1 4492 ? 172.396 164.677 203.894 1.00 33.32  ? 4492 ILE A CB    1 
ATOM   22944 C CG1   . ILE A 1 4492 ? 173.660 163.884 203.566 1.00 33.32  ? 4492 ILE A CG1   1 
ATOM   22945 C CG2   . ILE A 1 4492 ? 172.693 166.165 203.935 1.00 33.32  ? 4492 ILE A CG2   1 
ATOM   22946 C CD1   . ILE A 1 4492 ? 174.759 164.052 204.576 1.00 33.32  ? 4492 ILE A CD1   1 
ATOM   22947 N N     . SER A 1 4493 ? 169.445 164.824 204.989 1.00 35.49  ? 4493 SER A N     1 
ATOM   22948 C CA    . SER A 1 4493 ? 168.248 165.605 205.287 1.00 35.49  ? 4493 SER A CA    1 
ATOM   22949 C C     . SER A 1 4493 ? 167.791 165.392 206.724 1.00 35.49  ? 4493 SER A C     1 
ATOM   22950 O O     . SER A 1 4493 ? 167.391 166.346 207.402 1.00 35.49  ? 4493 SER A O     1 
ATOM   22951 C CB    . SER A 1 4493 ? 167.130 165.247 204.311 1.00 35.49  ? 4493 SER A CB    1 
ATOM   22952 O OG    . SER A 1 4493 ? 166.689 163.917 204.514 1.00 35.49  ? 4493 SER A OG    1 
ATOM   22953 N N     . LEU A 1 4494 ? 167.839 164.147 207.205 1.00 38.27  ? 4494 LEU A N     1 
ATOM   22954 C CA    . LEU A 1 4494 ? 167.470 163.875 208.591 1.00 38.27  ? 4494 LEU A CA    1 
ATOM   22955 C C     . LEU A 1 4494 ? 168.408 164.583 209.560 1.00 38.27  ? 4494 LEU A C     1 
ATOM   22956 O O     . LEU A 1 4494 ? 167.962 165.151 210.564 1.00 38.27  ? 4494 LEU A O     1 
ATOM   22957 C CB    . LEU A 1 4494 ? 167.468 162.369 208.851 1.00 38.27  ? 4494 LEU A CB    1 
ATOM   22958 C CG    . LEU A 1 4494 ? 166.122 161.648 208.767 1.00 38.27  ? 4494 LEU A CG    1 
ATOM   22959 C CD1   . LEU A 1 4494 ? 165.551 161.709 207.360 1.00 38.27  ? 4494 LEU A CD1   1 
ATOM   22960 C CD2   . LEU A 1 4494 ? 166.268 160.205 209.224 1.00 38.27  ? 4494 LEU A CD2   1 
ATOM   22961 N N     . ALA A 1 4495 ? 169.713 164.558 209.278 1.00 40.39  ? 4495 ALA A N     1 
ATOM   22962 C CA    . ALA A 1 4495 ? 170.667 165.246 210.141 1.00 40.39  ? 4495 ALA A CA    1 
ATOM   22963 C C     . ALA A 1 4495 ? 170.423 166.749 210.145 1.00 40.39  ? 4495 ALA A C     1 
ATOM   22964 O O     . ALA A 1 4495 ? 170.514 167.398 211.194 1.00 40.39  ? 4495 ALA A O     1 
ATOM   22965 C CB    . ALA A 1 4495 ? 172.095 164.934 209.699 1.00 40.39  ? 4495 ALA A CB    1 
ATOM   22966 N N     . ALA A 1 4496 ? 170.119 167.322 208.978 1.00 42.71  ? 4496 ALA A N     1 
ATOM   22967 C CA    . ALA A 1 4496 ? 169.835 168.752 208.907 1.00 42.71  ? 4496 ALA A CA    1 
ATOM   22968 C C     . ALA A 1 4496 ? 168.569 169.104 209.679 1.00 42.71  ? 4496 ALA A C     1 
ATOM   22969 O O     . ALA A 1 4496 ? 168.512 170.137 210.355 1.00 42.71  ? 4496 ALA A O     1 
ATOM   22970 C CB    . ALA A 1 4496 ? 169.713 169.192 207.449 1.00 42.71  ? 4496 ALA A CB    1 
ATOM   22971 N N     . ALA A 1 4497 ? 167.540 168.261 209.583 1.00 49.19  ? 4497 ALA A N     1 
ATOM   22972 C CA    . ALA A 1 4497 ? 166.292 168.537 210.287 1.00 49.19  ? 4497 ALA A CA    1 
ATOM   22973 C C     . ALA A 1 4497 ? 166.452 168.380 211.795 1.00 49.19  ? 4497 ALA A C     1 
ATOM   22974 O O     . ALA A 1 4497 ? 165.817 169.105 212.569 1.00 49.19  ? 4497 ALA A O     1 
ATOM   22975 C CB    . ALA A 1 4497 ? 165.185 167.620 209.771 1.00 49.19  ? 4497 ALA A CB    1 
ATOM   22976 N N     . SER A 1 4498 ? 167.289 167.435 212.230 1.00 50.75  ? 4498 SER A N     1 
ATOM   22977 C CA    . SER A 1 4498 ? 167.384 167.126 213.654 1.00 50.75  ? 4498 SER A CA    1 
ATOM   22978 C C     . SER A 1 4498 ? 167.968 168.291 214.446 1.00 50.75  ? 4498 SER A C     1 
ATOM   22979 O O     . SER A 1 4498 ? 167.397 168.714 215.457 1.00 50.75  ? 4498 SER A O     1 
ATOM   22980 C CB    . SER A 1 4498 ? 168.221 165.864 213.859 1.00 50.75  ? 4498 SER A CB    1 
ATOM   22981 O OG    . SER A 1 4498 ? 168.408 165.594 215.237 1.00 50.75  ? 4498 SER A OG    1 
ATOM   22982 N N     . GLY A 1 4499 ? 169.104 168.825 214.003 1.00 56.78  ? 4499 GLY A N     1 
ATOM   22983 C CA    . GLY A 1 4499 ? 169.779 169.857 214.765 1.00 56.78  ? 4499 GLY A CA    1 
ATOM   22984 C C     . GLY A 1 4499 ? 169.983 171.165 214.028 1.00 56.78  ? 4499 GLY A C     1 
ATOM   22985 O O     . GLY A 1 4499 ? 170.091 172.224 214.652 1.00 56.78  ? 4499 GLY A O     1 
ATOM   22986 N N     . GLY A 1 4500 ? 170.040 171.106 212.697 1.00 53.16  ? 4500 GLY A N     1 
ATOM   22987 C CA    . GLY A 1 4500 ? 170.293 172.275 211.883 1.00 53.16  ? 4500 GLY A CA    1 
ATOM   22988 C C     . GLY A 1 4500 ? 171.548 172.106 211.043 1.00 53.16  ? 4500 GLY A C     1 
ATOM   22989 O O     . GLY A 1 4500 ? 171.930 170.985 210.687 1.00 53.16  ? 4500 GLY A O     1 
ATOM   22990 N N     . ALA A 1 4501 ? 172.186 173.234 210.735 1.00 53.53  ? 4501 ALA A N     1 
ATOM   22991 C CA    . ALA A 1 4501 ? 173.404 173.214 209.937 1.00 53.53  ? 4501 ALA A CA    1 
ATOM   22992 C C     . ALA A 1 4501 ? 174.649 172.906 210.756 1.00 53.53  ? 4501 ALA A C     1 
ATOM   22993 O O     . ALA A 1 4501 ? 175.696 172.612 210.170 1.00 53.53  ? 4501 ALA A O     1 
ATOM   22994 C CB    . ALA A 1 4501 ? 173.583 174.549 209.213 1.00 53.53  ? 4501 ALA A CB    1 
ATOM   22995 N N     . LYS A 1 4502 ? 174.569 172.969 212.087 1.00 52.96  ? 4502 LYS A N     1 
ATOM   22996 C CA    . LYS A 1 4502 ? 175.714 172.587 212.907 1.00 52.96  ? 4502 LYS A CA    1 
ATOM   22997 C C     . LYS A 1 4502 ? 176.020 171.102 212.762 1.00 52.96  ? 4502 LYS A C     1 
ATOM   22998 O O     . LYS A 1 4502 ? 177.189 170.704 212.719 1.00 52.96  ? 4502 LYS A O     1 
ATOM   22999 C CB    . LYS A 1 4502 ? 175.458 172.940 214.372 1.00 52.96  ? 4502 LYS A CB    1 
ATOM   23000 C CG    . LYS A 1 4502 ? 174.845 174.314 214.589 1.00 52.96  ? 4502 LYS A CG    1 
ATOM   23001 C CD    . LYS A 1 4502 ? 174.699 174.631 216.071 1.00 52.96  ? 4502 LYS A CD    1 
ATOM   23002 C CE    . LYS A 1 4502 ? 174.152 173.447 216.862 1.00 52.96  ? 4502 LYS A CE    1 
ATOM   23003 N NZ    . LYS A 1 4502 ? 172.873 172.920 216.306 1.00 52.96  ? 4502 LYS A NZ    1 
ATOM   23004 N N     . GLU A 1 4503 ? 174.980 170.268 212.686 1.00 54.43  ? 4503 GLU A N     1 
ATOM   23005 C CA    . GLU A 1 4503 ? 175.185 168.834 212.534 1.00 54.43  ? 4503 GLU A CA    1 
ATOM   23006 C C     . GLU A 1 4503 ? 175.629 168.457 211.127 1.00 54.43  ? 4503 GLU A C     1 
ATOM   23007 O O     . GLU A 1 4503 ? 176.161 167.359 210.937 1.00 54.43  ? 4503 GLU A O     1 
ATOM   23008 C CB    . GLU A 1 4503 ? 173.907 168.078 212.899 1.00 54.43  ? 4503 GLU A CB    1 
ATOM   23009 C CG    . GLU A 1 4503 ? 173.230 168.585 214.161 1.00 54.43  ? 4503 GLU A CG    1 
ATOM   23010 C CD    . GLU A 1 4503 ? 174.173 168.633 215.347 1.00 54.43  ? 4503 GLU A CD    1 
ATOM   23011 O OE1   . GLU A 1 4503 ? 174.716 167.571 215.719 1.00 54.43  ? 4503 GLU A OE1   1 
ATOM   23012 O OE2   . GLU A 1 4503 ? 174.372 169.732 215.905 1.00 54.43  ? 4503 GLU A OE2   1 
ATOM   23013 N N     . LEU A 1 4504 ? 175.427 169.337 210.143 1.00 43.42  ? 4504 LEU A N     1 
ATOM   23014 C CA    . LEU A 1 4504 ? 175.917 169.062 208.795 1.00 43.42  ? 4504 LEU A CA    1 
ATOM   23015 C C     . LEU A 1 4504 ? 177.434 168.943 208.778 1.00 43.42  ? 4504 LEU A C     1 
ATOM   23016 O O     . LEU A 1 4504 ? 177.997 168.167 207.997 1.00 43.42  ? 4504 LEU A O     1 
ATOM   23017 C CB    . LEU A 1 4504 ? 175.461 170.157 207.831 1.00 43.42  ? 4504 LEU A CB    1 
ATOM   23018 C CG    . LEU A 1 4504 ? 173.980 170.213 207.463 1.00 43.42  ? 4504 LEU A CG    1 
ATOM   23019 C CD1   . LEU A 1 4504 ? 173.694 171.445 206.621 1.00 43.42  ? 4504 LEU A CD1   1 
ATOM   23020 C CD2   . LEU A 1 4504 ? 173.568 168.951 206.725 1.00 43.42  ? 4504 LEU A CD2   1 
ATOM   23021 N N     . LYS A 1 4505 ? 178.112 169.718 209.626 1.00 37.62  ? 4505 LYS A N     1 
ATOM   23022 C CA    . LYS A 1 4505 ? 179.568 169.664 209.684 1.00 37.62  ? 4505 LYS A CA    1 
ATOM   23023 C C     . LYS A 1 4505 ? 180.052 168.291 210.136 1.00 37.62  ? 4505 LYS A C     1 
ATOM   23024 O O     . LYS A 1 4505 ? 181.016 167.749 209.581 1.00 37.62  ? 4505 LYS A O     1 
ATOM   23025 C CB    . LYS A 1 4505 ? 180.080 170.757 210.623 1.00 37.62  ? 4505 LYS A CB    1 
ATOM   23026 C CG    . LYS A 1 4505 ? 181.582 170.784 210.799 1.00 37.62  ? 4505 LYS A CG    1 
ATOM   23027 C CD    . LYS A 1 4505 ? 182.049 170.083 212.060 1.00 37.62  ? 4505 LYS A CD    1 
ATOM   23028 C CE    . LYS A 1 4505 ? 183.563 169.966 212.071 1.00 37.62  ? 4505 LYS A CE    1 
ATOM   23029 N NZ    . LYS A 1 4505 ? 184.089 169.453 213.363 1.00 37.62  ? 4505 LYS A NZ    1 
ATOM   23030 N N     . ASN A 1 4506 ? 179.396 167.713 211.141 1.00 41.50  ? 4506 ASN A N     1 
ATOM   23031 C CA    . ASN A 1 4506 ? 179.825 166.446 211.735 1.00 41.50  ? 4506 ASN A CA    1 
ATOM   23032 C C     . ASN A 1 4506 ? 179.117 165.262 211.074 1.00 41.50  ? 4506 ASN A C     1 
ATOM   23033 O O     . ASN A 1 4506 ? 178.434 164.466 211.716 1.00 41.50  ? 4506 ASN A O     1 
ATOM   23034 C CB    . ASN A 1 4506 ? 179.576 166.465 213.239 1.00 41.50  ? 4506 ASN A CB    1 
ATOM   23035 C CG    . ASN A 1 4506 ? 180.357 167.552 213.943 1.00 41.50  ? 4506 ASN A CG    1 
ATOM   23036 O OD1   . ASN A 1 4506 ? 179.779 168.490 214.491 1.00 41.50  ? 4506 ASN A OD1   1 
ATOM   23037 N ND2   . ASN A 1 4506 ? 181.678 167.424 213.947 1.00 41.50  ? 4506 ASN A ND2   1 
ATOM   23038 N N     . ILE A 1 4507 ? 179.296 165.152 209.760 1.00 37.25  ? 4507 ILE A N     1 
ATOM   23039 C CA    . ILE A 1 4507 ? 178.744 164.050 208.982 1.00 37.25  ? 4507 ILE A CA    1 
ATOM   23040 C C     . ILE A 1 4507 ? 179.873 163.396 208.202 1.00 37.25  ? 4507 ILE A C     1 
ATOM   23041 O O     . ILE A 1 4507 ? 180.632 164.081 207.508 1.00 37.25  ? 4507 ILE A O     1 
ATOM   23042 C CB    . ILE A 1 4507 ? 177.630 164.516 208.026 1.00 37.25  ? 4507 ILE A CB    1 
ATOM   23043 C CG1   . ILE A 1 4507 ? 176.416 164.998 208.815 1.00 37.25  ? 4507 ILE A CG1   1 
ATOM   23044 C CG2   . ILE A 1 4507 ? 177.235 163.391 207.089 1.00 37.25  ? 4507 ILE A CG2   1 
ATOM   23045 C CD1   . ILE A 1 4507 ? 175.303 165.529 207.945 1.00 37.25  ? 4507 ILE A CD1   1 
ATOM   23046 N N     . HIS A 1 4508 ? 179.983 162.072 208.316 1.00 35.58  ? 4508 HIS A N     1 
ATOM   23047 C CA    . HIS A 1 4508 ? 180.997 161.308 207.593 1.00 35.58  ? 4508 HIS A CA    1 
ATOM   23048 C C     . HIS A 1 4508 ? 180.454 160.976 206.207 1.00 35.58  ? 4508 HIS A C     1 
ATOM   23049 O O     . HIS A 1 4508 ? 180.103 159.837 205.889 1.00 35.58  ? 4508 HIS A O     1 
ATOM   23050 C CB    . HIS A 1 4508 ? 181.377 160.054 208.367 1.00 35.58  ? 4508 HIS A CB    1 
ATOM   23051 C CG    . HIS A 1 4508 ? 181.941 160.332 209.725 1.00 35.58  ? 4508 HIS A CG    1 
ATOM   23052 N ND1   . HIS A 1 4508 ? 183.200 160.860 209.913 1.00 35.58  ? 4508 HIS A ND1   1 
ATOM   23053 C CD2   . HIS A 1 4508 ? 181.419 160.155 210.961 1.00 35.58  ? 4508 HIS A CD2   1 
ATOM   23054 C CE1   . HIS A 1 4508 ? 183.429 160.997 211.206 1.00 35.58  ? 4508 HIS A CE1   1 
ATOM   23055 N NE2   . HIS A 1 4508 ? 182.364 160.576 211.864 1.00 35.58  ? 4508 HIS A NE2   1 
ATOM   23056 N N     . VAL A 1 4509 ? 180.384 162.006 205.364 1.00 29.25  ? 4509 VAL A N     1 
ATOM   23057 C CA    . VAL A 1 4509 ? 179.901 161.829 204.002 1.00 29.25  ? 4509 VAL A CA    1 
ATOM   23058 C C     . VAL A 1 4509 ? 180.930 161.049 203.191 1.00 29.25  ? 4509 VAL A C     1 
ATOM   23059 O O     . VAL A 1 4509 ? 182.136 161.092 203.465 1.00 29.25  ? 4509 VAL A O     1 
ATOM   23060 C CB    . VAL A 1 4509 ? 179.598 163.197 203.363 1.00 29.25  ? 4509 VAL A CB    1 
ATOM   23061 C CG1   . VAL A 1 4509 ? 180.881 163.900 202.969 1.00 29.25  ? 4509 VAL A CG1   1 
ATOM   23062 C CG2   . VAL A 1 4509 ? 178.680 163.045 202.166 1.00 29.25  ? 4509 VAL A CG2   1 
ATOM   23063 N N     . CYS A 1 4510 ? 180.451 160.308 202.196 1.00 27.01  ? 4510 CYS A N     1 
ATOM   23064 C CA    . CYS A 1 4510 ? 181.320 159.578 201.282 1.00 27.01  ? 4510 CYS A CA    1 
ATOM   23065 C C     . CYS A 1 4510 ? 181.337 160.305 199.944 1.00 27.01  ? 4510 CYS A C     1 
ATOM   23066 O O     . CYS A 1 4510 ? 180.280 160.651 199.407 1.00 27.01  ? 4510 CYS A O     1 
ATOM   23067 C CB    . CYS A 1 4510 ? 180.863 158.128 201.114 1.00 27.01  ? 4510 CYS A CB    1 
ATOM   23068 S SG    . CYS A 1 4510 ? 179.251 157.893 200.335 1.00 27.01  ? 4510 CYS A SG    1 
ATOM   23069 N N     . LEU A 1 4511 ? 182.539 160.551 199.419 1.00 22.10  ? 4511 LEU A N     1 
ATOM   23070 C CA    . LEU A 1 4511 ? 182.663 161.323 198.188 1.00 22.10  ? 4511 LEU A CA    1 
ATOM   23071 C C     . LEU A 1 4511 ? 182.017 160.603 197.012 1.00 22.10  ? 4511 LEU A C     1 
ATOM   23072 O O     . LEU A 1 4511 ? 181.493 161.245 196.095 1.00 22.10  ? 4511 LEU A O     1 
ATOM   23073 C CB    . LEU A 1 4511 ? 184.134 161.615 197.898 1.00 22.10  ? 4511 LEU A CB    1 
ATOM   23074 C CG    . LEU A 1 4511 ? 184.819 162.619 198.825 1.00 22.10  ? 4511 LEU A CG    1 
ATOM   23075 C CD1   . LEU A 1 4511 ? 186.062 163.188 198.167 1.00 22.10  ? 4511 LEU A CD1   1 
ATOM   23076 C CD2   . LEU A 1 4511 ? 183.861 163.729 199.206 1.00 22.10  ? 4511 LEU A CD2   1 
ATOM   23077 N N     . GLY A 1 4512 ? 182.047 159.270 197.017 1.00 24.00  ? 4512 GLY A N     1 
ATOM   23078 C CA    . GLY A 1 4512 ? 181.444 158.525 195.925 1.00 24.00  ? 4512 GLY A CA    1 
ATOM   23079 C C     . GLY A 1 4512 ? 179.951 158.765 195.803 1.00 24.00  ? 4512 GLY A C     1 
ATOM   23080 O O     . GLY A 1 4512 ? 179.423 158.903 194.697 1.00 24.00  ? 4512 GLY A O     1 
ATOM   23081 N N     . GLY A 1 4513 ? 179.251 158.818 196.937 1.00 26.06  ? 4513 GLY A N     1 
ATOM   23082 C CA    . GLY A 1 4513 ? 177.817 159.048 196.898 1.00 26.06  ? 4513 GLY A CA    1 
ATOM   23083 C C     . GLY A 1 4513 ? 177.454 160.432 196.394 1.00 26.06  ? 4513 GLY A C     1 
ATOM   23084 O O     . GLY A 1 4513 ? 176.455 160.603 195.690 1.00 26.06  ? 4513 GLY A O     1 
ATOM   23085 N N     . LEU A 1 4514 ? 178.250 161.438 196.752 1.00 26.46  ? 4514 LEU A N     1 
ATOM   23086 C CA    . LEU A 1 4514 ? 178.000 162.808 196.323 1.00 26.46  ? 4514 LEU A CA    1 
ATOM   23087 C C     . LEU A 1 4514 ? 178.099 162.927 194.809 1.00 26.46  ? 4514 LEU A C     1 
ATOM   23088 O O     . LEU A 1 4514 ? 179.010 162.364 194.195 1.00 26.46  ? 4514 LEU A O     1 
ATOM   23089 C CB    . LEU A 1 4514 ? 178.984 163.761 197.000 1.00 26.46  ? 4514 LEU A CB    1 
ATOM   23090 C CG    . LEU A 1 4514 ? 178.840 163.856 198.517 1.00 26.46  ? 4514 LEU A CG    1 
ATOM   23091 C CD1   . LEU A 1 4514 ? 179.865 164.809 199.090 1.00 26.46  ? 4514 LEU A CD1   1 
ATOM   23092 C CD2   . LEU A 1 4514 ? 177.436 164.296 198.885 1.00 26.46  ? 4514 LEU A CD2   1 
ATOM   23093 N N     . PHE A 1 4515 ? 177.160 163.649 194.199 1.00 26.68  ? 4515 PHE A N     1 
ATOM   23094 C CA    . PHE A 1 4515 ? 177.134 163.798 192.749 1.00 26.68  ? 4515 PHE A CA    1 
ATOM   23095 C C     . PHE A 1 4515 ? 178.354 164.560 192.244 1.00 26.68  ? 4515 PHE A C     1 
ATOM   23096 O O     . PHE A 1 4515 ? 178.937 164.193 191.219 1.00 26.68  ? 4515 PHE A O     1 
ATOM   23097 C CB    . PHE A 1 4515 ? 175.841 164.490 192.313 1.00 26.68  ? 4515 PHE A CB    1 
ATOM   23098 C CG    . PHE A 1 4515 ? 174.595 163.751 192.717 1.00 26.68  ? 4515 PHE A CG    1 
ATOM   23099 C CD1   . PHE A 1 4515 ? 174.119 162.703 191.951 1.00 26.68  ? 4515 PHE A CD1   1 
ATOM   23100 C CD2   . PHE A 1 4515 ? 173.905 164.100 193.863 1.00 26.68  ? 4515 PHE A CD2   1 
ATOM   23101 C CE1   . PHE A 1 4515 ? 172.977 162.020 192.320 1.00 26.68  ? 4515 PHE A CE1   1 
ATOM   23102 C CE2   . PHE A 1 4515 ? 172.763 163.421 194.236 1.00 26.68  ? 4515 PHE A CE2   1 
ATOM   23103 C CZ    . PHE A 1 4515 ? 172.299 162.379 193.463 1.00 26.68  ? 4515 PHE A CZ    1 
ATOM   23104 N N     . VAL A 1 4516 ? 178.748 165.617 192.948 1.00 24.07  ? 4516 VAL A N     1 
ATOM   23105 C CA    . VAL A 1 4516 ? 179.948 166.376 192.600 1.00 24.07  ? 4516 VAL A CA    1 
ATOM   23106 C C     . VAL A 1 4516 ? 180.834 166.540 193.833 1.00 24.07  ? 4516 VAL A C     1 
ATOM   23107 O O     . VAL A 1 4516 ? 180.694 167.516 194.585 1.00 24.07  ? 4516 VAL A O     1 
ATOM   23108 C CB    . VAL A 1 4516 ? 179.585 167.720 191.945 1.00 24.07  ? 4516 VAL A CB    1 
ATOM   23109 C CG1   . VAL A 1 4516 ? 178.998 167.481 190.569 1.00 24.07  ? 4516 VAL A CG1   1 
ATOM   23110 C CG2   . VAL A 1 4516 ? 178.554 168.465 192.768 1.00 24.07  ? 4516 VAL A CG2   1 
ATOM   23111 N N     . PRO A 1 4517 ? 181.750 165.601 194.085 1.00 19.16  ? 4517 PRO A N     1 
ATOM   23112 C CA    . PRO A 1 4517 ? 182.607 165.707 195.279 1.00 19.16  ? 4517 PRO A CA    1 
ATOM   23113 C C     . PRO A 1 4517 ? 183.483 166.947 195.299 1.00 19.16  ? 4517 PRO A C     1 
ATOM   23114 O O     . PRO A 1 4517 ? 183.806 167.451 196.385 1.00 19.16  ? 4517 PRO A O     1 
ATOM   23115 C CB    . PRO A 1 4517 ? 183.451 164.425 195.218 1.00 19.16  ? 4517 PRO A CB    1 
ATOM   23116 C CG    . PRO A 1 4517 ? 182.735 163.521 194.265 1.00 19.16  ? 4517 PRO A CG    1 
ATOM   23117 C CD    . PRO A 1 4517 ? 182.056 164.408 193.283 1.00 19.16  ? 4517 PRO A CD    1 
ATOM   23118 N N     . GLU A 1 4518 ? 183.897 167.444 194.131 1.00 19.47  ? 4518 GLU A N     1 
ATOM   23119 C CA    . GLU A 1 4518 ? 184.710 168.654 194.090 1.00 19.47  ? 4518 GLU A CA    1 
ATOM   23120 C C     . GLU A 1 4518 ? 183.972 169.827 194.719 1.00 19.47  ? 4518 GLU A C     1 
ATOM   23121 O O     . GLU A 1 4518 ? 184.578 170.662 195.404 1.00 19.47  ? 4518 GLU A O     1 
ATOM   23122 C CB    . GLU A 1 4518 ? 185.102 168.969 192.648 1.00 19.47  ? 4518 GLU A CB    1 
ATOM   23123 C CG    . GLU A 1 4518 ? 186.028 170.161 192.499 1.00 19.47  ? 4518 GLU A CG    1 
ATOM   23124 C CD    . GLU A 1 4518 ? 186.423 170.406 191.057 1.00 19.47  ? 4518 GLU A CD    1 
ATOM   23125 O OE1   . GLU A 1 4518 ? 185.966 169.645 190.179 1.00 19.47  ? 4518 GLU A OE1   1 
ATOM   23126 O OE2   . GLU A 1 4518 ? 187.188 171.360 190.801 1.00 19.47  ? 4518 GLU A OE2   1 
ATOM   23127 N N     . ALA A 1 4519 ? 182.657 169.901 194.505 1.00 18.76  ? 4519 ALA A N     1 
ATOM   23128 C CA    . ALA A 1 4519 ? 181.861 170.923 195.172 1.00 18.76  ? 4519 ALA A CA    1 
ATOM   23129 C C     . ALA A 1 4519 ? 181.886 170.736 196.681 1.00 18.76  ? 4519 ALA A C     1 
ATOM   23130 O O     . ALA A 1 4519 ? 181.889 171.716 197.432 1.00 18.76  ? 4519 ALA A O     1 
ATOM   23131 C CB    . ALA A 1 4519 ? 180.426 170.902 194.649 1.00 18.76  ? 4519 ALA A CB    1 
ATOM   23132 N N     . TYR A 1 4520 ? 181.900 169.484 197.150 1.00 16.09  ? 4520 TYR A N     1 
ATOM   23133 C CA    . TYR A 1 4520 ? 182.003 169.253 198.587 1.00 16.09  ? 4520 TYR A CA    1 
ATOM   23134 C C     . TYR A 1 4520 ? 183.336 169.741 199.132 1.00 16.09  ? 4520 TYR A C     1 
ATOM   23135 O O     . TYR A 1 4520 ? 183.389 170.325 200.218 1.00 16.09  ? 4520 TYR A O     1 
ATOM   23136 C CB    . TYR A 1 4520 ? 181.823 167.776 198.919 1.00 16.09  ? 4520 TYR A CB    1 
ATOM   23137 C CG    . TYR A 1 4520 ? 181.997 167.496 200.393 1.00 16.09  ? 4520 TYR A CG    1 
ATOM   23138 C CD1   . TYR A 1 4520 ? 181.105 168.011 201.322 1.00 16.09  ? 4520 TYR A CD1   1 
ATOM   23139 C CD2   . TYR A 1 4520 ? 183.059 166.737 200.859 1.00 16.09  ? 4520 TYR A CD2   1 
ATOM   23140 C CE1   . TYR A 1 4520 ? 181.259 167.769 202.669 1.00 16.09  ? 4520 TYR A CE1   1 
ATOM   23141 C CE2   . TYR A 1 4520 ? 183.221 166.490 202.207 1.00 16.09  ? 4520 TYR A CE2   1 
ATOM   23142 C CZ    . TYR A 1 4520 ? 182.318 167.010 203.107 1.00 16.09  ? 4520 TYR A CZ    1 
ATOM   23143 O OH    . TYR A 1 4520 ? 182.471 166.767 204.451 1.00 16.09  ? 4520 TYR A OH    1 
ATOM   23144 N N     . ILE A 1 4521 ? 184.426 169.496 198.403 1.00 17.92  ? 4521 ILE A N     1 
ATOM   23145 C CA    . ILE A 1 4521 ? 185.731 169.975 198.852 1.00 17.92  ? 4521 ILE A CA    1 
ATOM   23146 C C     . ILE A 1 4521 ? 185.752 171.498 198.888 1.00 17.92  ? 4521 ILE A C     1 
ATOM   23147 O O     . ILE A 1 4521 ? 186.288 172.110 199.822 1.00 17.92  ? 4521 ILE A O     1 
ATOM   23148 C CB    . ILE A 1 4521 ? 186.849 169.417 197.955 1.00 17.92  ? 4521 ILE A CB    1 
ATOM   23149 C CG1   . ILE A 1 4521 ? 186.717 167.901 197.824 1.00 17.92  ? 4521 ILE A CG1   1 
ATOM   23150 C CG2   . ILE A 1 4521 ? 188.206 169.779 198.524 1.00 17.92  ? 4521 ILE A CG2   1 
ATOM   23151 C CD1   . ILE A 1 4521 ? 186.942 167.166 199.116 1.00 17.92  ? 4521 ILE A CD1   1 
ATOM   23152 N N     . THR A 1 4522 ? 185.172 172.132 197.868 1.00 17.63  ? 4522 THR A N     1 
ATOM   23153 C CA    . THR A 1 4522 ? 185.104 173.589 197.844 1.00 17.63  ? 4522 THR A CA    1 
ATOM   23154 C C     . THR A 1 4522 ? 184.273 174.127 199.005 1.00 17.63  ? 4522 THR A C     1 
ATOM   23155 O O     . THR A 1 4522 ? 184.641 175.128 199.630 1.00 17.63  ? 4522 THR A O     1 
ATOM   23156 C CB    . THR A 1 4522 ? 184.533 174.059 196.508 1.00 17.63  ? 4522 THR A CB    1 
ATOM   23157 O OG1   . THR A 1 4522 ? 185.476 173.785 195.463 1.00 17.63  ? 4522 THR A OG1   1 
ATOM   23158 C CG2   . THR A 1 4522 ? 184.250 175.545 196.545 1.00 17.63  ? 4522 THR A CG2   1 
ATOM   23159 N N     . ALA A 1 4523 ? 183.145 173.478 199.307 1.00 18.84  ? 4523 ALA A N     1 
ATOM   23160 C CA    . ALA A 1 4523 ? 182.322 173.900 200.437 1.00 18.84  ? 4523 ALA A CA    1 
ATOM   23161 C C     . ALA A 1 4523 ? 183.059 173.713 201.753 1.00 18.84  ? 4523 ALA A C     1 
ATOM   23162 O O     . ALA A 1 4523 ? 182.933 174.535 202.667 1.00 18.84  ? 4523 ALA A O     1 
ATOM   23163 C CB    . ALA A 1 4523 ? 181.006 173.127 200.448 1.00 18.84  ? 4523 ALA A CB    1 
ATOM   23164 N N     . THR A 1 4524 ? 183.822 172.629 201.870 1.00 18.30  ? 4524 THR A N     1 
ATOM   23165 C CA    . THR A 1 4524 ? 184.673 172.433 203.035 1.00 18.30  ? 4524 THR A CA    1 
ATOM   23166 C C     . THR A 1 4524 ? 185.655 173.581 203.196 1.00 18.30  ? 4524 THR A C     1 
ATOM   23167 O O     . THR A 1 4524 ? 185.814 174.131 204.295 1.00 18.30  ? 4524 THR A O     1 
ATOM   23168 C CB    . THR A 1 4524 ? 185.421 171.112 202.889 1.00 18.30  ? 4524 THR A CB    1 
ATOM   23169 O OG1   . THR A 1 4524 ? 184.481 170.037 202.767 1.00 18.30  ? 4524 THR A OG1   1 
ATOM   23170 C CG2   . THR A 1 4524 ? 186.352 170.881 204.049 1.00 18.30  ? 4524 THR A CG2   1 
ATOM   23171 N N     . ARG A 1 4525 ? 186.317 173.958 202.103 1.00 16.86  ? 4525 ARG A N     1 
ATOM   23172 C CA    . ARG A 1 4525 ? 187.283 175.048 202.153 1.00 16.86  ? 4525 ARG A CA    1 
ATOM   23173 C C     . ARG A 1 4525 ? 186.612 176.354 202.554 1.00 16.86  ? 4525 ARG A C     1 
ATOM   23174 O O     . ARG A 1 4525 ? 187.131 177.096 203.397 1.00 16.86  ? 4525 ARG A O     1 
ATOM   23175 C CB    . ARG A 1 4525 ? 187.972 175.182 200.796 1.00 16.86  ? 4525 ARG A CB    1 
ATOM   23176 C CG    . ARG A 1 4525 ? 189.300 175.910 200.835 1.00 16.86  ? 4525 ARG A CG    1 
ATOM   23177 C CD    . ARG A 1 4525 ? 189.917 175.964 199.449 1.00 16.86  ? 4525 ARG A CD    1 
ATOM   23178 N NE    . ARG A 1 4525 ? 191.325 176.342 199.462 1.00 16.86  ? 4525 ARG A NE    1 
ATOM   23179 C CZ    . ARG A 1 4525 ? 192.042 176.563 198.369 1.00 16.86  ? 4525 ARG A CZ    1 
ATOM   23180 N NH1   . ARG A 1 4525 ? 191.511 176.452 197.163 1.00 16.86  ? 4525 ARG A NH1   1 
ATOM   23181 N NH2   . ARG A 1 4525 ? 193.324 176.895 198.488 1.00 16.86  ? 4525 ARG A NH2   1 
ATOM   23182 N N     . GLN A 1 4526 ? 185.444 176.638 201.976 1.00 18.18  ? 4526 GLN A N     1 
ATOM   23183 C CA    . GLN A 1 4526 ? 184.736 177.873 202.295 1.00 18.18  ? 4526 GLN A CA    1 
ATOM   23184 C C     . GLN A 1 4526 ? 184.293 177.901 203.753 1.00 18.18  ? 4526 GLN A C     1 
ATOM   23185 O O     . GLN A 1 4526 ? 184.374 178.943 204.410 1.00 18.18  ? 4526 GLN A O     1 
ATOM   23186 C CB    . GLN A 1 4526 ? 183.534 178.046 201.370 1.00 18.18  ? 4526 GLN A CB    1 
ATOM   23187 C CG    . GLN A 1 4526 ? 183.874 178.228 199.905 1.00 18.18  ? 4526 GLN A CG    1 
ATOM   23188 C CD    . GLN A 1 4526 ? 182.636 178.374 199.047 1.00 18.18  ? 4526 GLN A CD    1 
ATOM   23189 O OE1   . GLN A 1 4526 ? 181.535 178.568 199.559 1.00 18.18  ? 4526 GLN A OE1   1 
ATOM   23190 N NE2   . GLN A 1 4526 ? 182.807 178.280 197.735 1.00 18.18  ? 4526 GLN A NE2   1 
ATOM   23191 N N     . TYR A 1 4527 ? 183.807 176.771 204.272 1.00 22.03  ? 4527 TYR A N     1 
ATOM   23192 C CA    . TYR A 1 4527 ? 183.391 176.719 205.671 1.00 22.03  ? 4527 TYR A CA    1 
ATOM   23193 C C     . TYR A 1 4527 ? 184.572 176.927 206.607 1.00 22.03  ? 4527 TYR A C     1 
ATOM   23194 O O     . TYR A 1 4527 ? 184.470 177.674 207.590 1.00 22.03  ? 4527 TYR A O     1 
ATOM   23195 C CB    . TYR A 1 4527 ? 182.700 175.387 205.964 1.00 22.03  ? 4527 TYR A CB    1 
ATOM   23196 C CG    . TYR A 1 4527 ? 182.263 175.210 207.404 1.00 22.03  ? 4527 TYR A CG    1 
ATOM   23197 C CD1   . TYR A 1 4527 ? 183.129 174.687 208.357 1.00 22.03  ? 4527 TYR A CD1   1 
ATOM   23198 C CD2   . TYR A 1 4527 ? 180.984 175.563 207.809 1.00 22.03  ? 4527 TYR A CD2   1 
ATOM   23199 C CE1   . TYR A 1 4527 ? 182.734 174.524 209.669 1.00 22.03  ? 4527 TYR A CE1   1 
ATOM   23200 C CE2   . TYR A 1 4527 ? 180.581 175.403 209.122 1.00 22.03  ? 4527 TYR A CE2   1 
ATOM   23201 C CZ    . TYR A 1 4527 ? 181.460 174.882 210.047 1.00 22.03  ? 4527 TYR A CZ    1 
ATOM   23202 O OH    . TYR A 1 4527 ? 181.066 174.719 211.354 1.00 22.03  ? 4527 TYR A OH    1 
ATOM   23203 N N     . VAL A 1 4528 ? 185.698 176.265 206.328 1.00 20.20  ? 4528 VAL A N     1 
ATOM   23204 C CA    . VAL A 1 4528 ? 186.863 176.412 207.193 1.00 20.20  ? 4528 VAL A CA    1 
ATOM   23205 C C     . VAL A 1 4528 ? 187.423 177.826 207.104 1.00 20.20  ? 4528 VAL A C     1 
ATOM   23206 O O     . VAL A 1 4528 ? 188.017 178.325 208.066 1.00 20.20  ? 4528 VAL A O     1 
ATOM   23207 C CB    . VAL A 1 4528 ? 187.922 175.348 206.850 1.00 20.20  ? 4528 VAL A CB    1 
ATOM   23208 C CG1   . VAL A 1 4528 ? 189.170 175.538 207.695 1.00 20.20  ? 4528 VAL A CG1   1 
ATOM   23209 C CG2   . VAL A 1 4528 ? 187.355 173.957 207.069 1.00 20.20  ? 4528 VAL A CG2   1 
ATOM   23210 N N     . ALA A 1 4529 ? 187.258 178.496 205.961 1.00 20.73  ? 4529 ALA A N     1 
ATOM   23211 C CA    . ALA A 1 4529 ? 187.663 179.896 205.872 1.00 20.73  ? 4529 ALA A CA    1 
ATOM   23212 C C     . ALA A 1 4529 ? 186.730 180.792 206.680 1.00 20.73  ? 4529 ALA A C     1 
ATOM   23213 O O     . ALA A 1 4529 ? 187.186 181.633 207.467 1.00 20.73  ? 4529 ALA A O     1 
ATOM   23214 C CB    . ALA A 1 4529 ? 187.703 180.339 204.411 1.00 20.73  ? 4529 ALA A CB    1 
ATOM   23215 N N     . GLN A 1 4530 ? 185.417 180.616 206.504 1.00 23.36  ? 4530 GLN A N     1 
ATOM   23216 C CA    . GLN A 1 4530 ? 184.447 181.473 207.177 1.00 23.36  ? 4530 GLN A CA    1 
ATOM   23217 C C     . GLN A 1 4530 ? 184.572 181.352 208.688 1.00 23.36  ? 4530 GLN A C     1 
ATOM   23218 O O     . GLN A 1 4530 ? 184.521 182.355 209.410 1.00 23.36  ? 4530 GLN A O     1 
ATOM   23219 C CB    . GLN A 1 4530 ? 183.031 181.127 206.719 1.00 23.36  ? 4530 GLN A CB    1 
ATOM   23220 C CG    . GLN A 1 4530 ? 181.955 181.988 207.353 1.00 23.36  ? 4530 GLN A CG    1 
ATOM   23221 C CD    . GLN A 1 4530 ? 180.563 181.612 206.894 1.00 23.36  ? 4530 GLN A CD    1 
ATOM   23222 O OE1   . GLN A 1 4530 ? 179.575 182.220 207.306 1.00 23.36  ? 4530 GLN A OE1   1 
ATOM   23223 N NE2   . GLN A 1 4530 ? 180.476 180.607 206.033 1.00 23.36  ? 4530 GLN A NE2   1 
ATOM   23224 N N     . ALA A 1 4531 ? 184.733 180.131 209.188 1.00 22.84  ? 4531 ALA A N     1 
ATOM   23225 C CA    . ALA A 1 4531 ? 185.181 179.968 210.561 1.00 22.84  ? 4531 ALA A CA    1 
ATOM   23226 C C     . ALA A 1 4531 ? 186.616 180.462 210.673 1.00 22.84  ? 4531 ALA A C     1 
ATOM   23227 O O     . ALA A 1 4531 ? 187.462 180.143 209.837 1.00 22.84  ? 4531 ALA A O     1 
ATOM   23228 C CB    . ALA A 1 4531 ? 185.080 178.506 210.993 1.00 22.84  ? 4531 ALA A CB    1 
ATOM   23229 N N     . ASN A 1 4532 ? 186.881 181.276 211.693 1.00 26.43  ? 4532 ASN A N     1 
ATOM   23230 C CA    . ASN A 1 4532 ? 188.161 181.934 211.940 1.00 26.43  ? 4532 ASN A CA    1 
ATOM   23231 C C     . ASN A 1 4532 ? 188.476 183.025 210.920 1.00 26.43  ? 4532 ASN A C     1 
ATOM   23232 O O     . ASN A 1 4532 ? 189.510 183.691 211.058 1.00 26.43  ? 4532 ASN A O     1 
ATOM   23233 C CB    . ASN A 1 4532 ? 189.337 180.945 211.983 1.00 26.43  ? 4532 ASN A CB    1 
ATOM   23234 C CG    . ASN A 1 4532 ? 189.274 180.018 213.179 1.00 26.43  ? 4532 ASN A CG    1 
ATOM   23235 O OD1   . ASN A 1 4532 ? 188.969 180.442 214.293 1.00 26.43  ? 4532 ASN A OD1   1 
ATOM   23236 N ND2   . ASN A 1 4532 ? 189.559 178.741 212.952 1.00 26.43  ? 4532 ASN A ND2   1 
ATOM   23237 N N     . SER A 1 4533 ? 187.631 183.232 209.905 1.00 26.13  ? 4533 SER A N     1 
ATOM   23238 C CA    . SER A 1 4533 ? 187.716 184.395 209.021 1.00 26.13  ? 4533 SER A CA    1 
ATOM   23239 C C     . SER A 1 4533 ? 189.059 184.448 208.289 1.00 26.13  ? 4533 SER A C     1 
ATOM   23240 O O     . SER A 1 4533 ? 189.838 185.393 208.421 1.00 26.13  ? 4533 SER A O     1 
ATOM   23241 C CB    . SER A 1 4533 ? 187.461 185.690 209.801 1.00 26.13  ? 4533 SER A CB    1 
ATOM   23242 O OG    . SER A 1 4533 ? 186.233 185.628 210.503 1.00 26.13  ? 4533 SER A OG    1 
ATOM   23243 N N     . TRP A 1 4534 ? 189.316 183.407 207.507 1.00 26.12  ? 4534 TRP A N     1 
ATOM   23244 C CA    . TRP A 1 4534 ? 190.487 183.334 206.648 1.00 26.12  ? 4534 TRP A CA    1 
ATOM   23245 C C     . TRP A 1 4534 ? 190.074 183.515 205.193 1.00 26.12  ? 4534 TRP A C     1 
ATOM   23246 O O     . TRP A 1 4534 ? 188.889 183.570 204.856 1.00 26.12  ? 4534 TRP A O     1 
ATOM   23247 C CB    . TRP A 1 4534 ? 191.219 181.999 206.826 1.00 26.12  ? 4534 TRP A CB    1 
ATOM   23248 C CG    . TRP A 1 4534 ? 192.001 181.894 208.094 1.00 26.12  ? 4534 TRP A CG    1 
ATOM   23249 C CD1   . TRP A 1 4534 ? 192.724 182.881 208.694 1.00 26.12  ? 4534 TRP A CD1   1 
ATOM   23250 C CD2   . TRP A 1 4534 ? 192.150 180.731 208.915 1.00 26.12  ? 4534 TRP A CD2   1 
ATOM   23251 N NE1   . TRP A 1 4534 ? 193.310 182.406 209.843 1.00 26.12  ? 4534 TRP A NE1   1 
ATOM   23252 C CE2   . TRP A 1 4534 ? 192.972 181.088 210.000 1.00 26.12  ? 4534 TRP A CE2   1 
ATOM   23253 C CE3   . TRP A 1 4534 ? 191.665 179.423 208.839 1.00 26.12  ? 4534 TRP A CE3   1 
ATOM   23254 C CZ2   . TRP A 1 4534 ? 193.320 180.186 211.000 1.00 26.12  ? 4534 TRP A CZ2   1 
ATOM   23255 C CZ3   . TRP A 1 4534 ? 192.011 178.529 209.832 1.00 26.12  ? 4534 TRP A CZ3   1 
ATOM   23256 C CH2   . TRP A 1 4534 ? 192.830 178.913 210.899 1.00 26.12  ? 4534 TRP A CH2   1 
ATOM   23257 N N     . SER A 1 4535 ? 191.075 183.609 204.327 1.00 21.14  ? 4535 SER A N     1 
ATOM   23258 C CA    . SER A 1 4535 ? 190.862 183.661 202.891 1.00 21.14  ? 4535 SER A CA    1 
ATOM   23259 C C     . SER A 1 4535 ? 191.133 182.292 202.283 1.00 21.14  ? 4535 SER A C     1 
ATOM   23260 O O     . SER A 1 4535 ? 191.984 181.539 202.762 1.00 21.14  ? 4535 SER A O     1 
ATOM   23261 C CB    . SER A 1 4535 ? 191.760 184.713 202.240 1.00 21.14  ? 4535 SER A CB    1 
ATOM   23262 O OG    . SER A 1 4535 ? 191.749 184.584 200.830 1.00 21.14  ? 4535 SER A OG    1 
ATOM   23263 N N     . LEU A 1 4536 ? 190.394 181.973 201.218 1.00 19.06  ? 4536 LEU A N     1 
ATOM   23264 C CA    . LEU A 1 4536 ? 190.507 180.649 200.613 1.00 19.06  ? 4536 LEU A CA    1 
ATOM   23265 C C     . LEU A 1 4536 ? 191.891 180.402 200.026 1.00 19.06  ? 4536 LEU A C     1 
ATOM   23266 O O     . LEU A 1 4536 ? 192.299 179.245 199.882 1.00 19.06  ? 4536 LEU A O     1 
ATOM   23267 C CB    . LEU A 1 4536 ? 189.440 180.465 199.536 1.00 19.06  ? 4536 LEU A CB    1 
ATOM   23268 C CG    . LEU A 1 4536 ? 188.099 179.896 199.999 1.00 19.06  ? 4536 LEU A CG    1 
ATOM   23269 C CD1   . LEU A 1 4536 ? 187.302 180.934 200.766 1.00 19.06  ? 4536 LEU A CD1   1 
ATOM   23270 C CD2   . LEU A 1 4536 ? 187.309 179.377 198.815 1.00 19.06  ? 4536 LEU A CD2   1 
ATOM   23271 N N     . GLU A 1 4537 ? 192.624 181.462 199.678 1.00 22.05  ? 4537 GLU A N     1 
ATOM   23272 C CA    . GLU A 1 4537 ? 193.965 181.271 199.138 1.00 22.05  ? 4537 GLU A CA    1 
ATOM   23273 C C     . GLU A 1 4537 ? 194.924 180.720 200.186 1.00 22.05  ? 4537 GLU A C     1 
ATOM   23274 O O     . GLU A 1 4537 ? 195.894 180.039 199.837 1.00 22.05  ? 4537 GLU A O     1 
ATOM   23275 C CB    . GLU A 1 4537 ? 194.509 182.586 198.583 1.00 22.05  ? 4537 GLU A CB    1 
ATOM   23276 C CG    . GLU A 1 4537 ? 194.732 183.655 199.638 1.00 22.05  ? 4537 GLU A CG    1 
ATOM   23277 C CD    . GLU A 1 4537 ? 195.213 184.965 199.052 1.00 22.05  ? 4537 GLU A CD    1 
ATOM   23278 O OE1   . GLU A 1 4537 ? 195.353 185.047 197.815 1.00 22.05  ? 4537 GLU A OE1   1 
ATOM   23279 O OE2   . GLU A 1 4537 ? 195.459 185.910 199.830 1.00 22.05  ? 4537 GLU A OE2   1 
ATOM   23280 N N     . GLU A 1 4538 ? 194.673 180.996 201.463 1.00 27.42  ? 4538 GLU A N     1 
ATOM   23281 C CA    . GLU A 1 4538 ? 195.599 180.647 202.531 1.00 27.42  ? 4538 GLU A CA    1 
ATOM   23282 C C     . GLU A 1 4538 ? 195.346 179.267 203.121 1.00 27.42  ? 4538 GLU A C     1 
ATOM   23283 O O     . GLU A 1 4538 ? 196.070 178.862 204.036 1.00 27.42  ? 4538 GLU A O     1 
ATOM   23284 C CB    . GLU A 1 4538 ? 195.530 181.693 203.649 1.00 27.42  ? 4538 GLU A CB    1 
ATOM   23285 C CG    . GLU A 1 4538 ? 195.667 183.127 203.170 1.00 27.42  ? 4538 GLU A CG    1 
ATOM   23286 C CD    . GLU A 1 4538 ? 195.092 184.124 204.155 1.00 27.42  ? 4538 GLU A CD    1 
ATOM   23287 O OE1   . GLU A 1 4538 ? 193.920 183.959 204.554 1.00 27.42  ? 4538 GLU A OE1   1 
ATOM   23288 O OE2   . GLU A 1 4538 ? 195.810 185.074 204.530 1.00 27.42  ? 4538 GLU A OE2   1 
ATOM   23289 N N     . LEU A 1 4539 ? 194.353 178.537 202.627 1.00 22.49  ? 4539 LEU A N     1 
ATOM   23290 C CA    . LEU A 1 4539 ? 194.003 177.232 203.170 1.00 22.49  ? 4539 LEU A CA    1 
ATOM   23291 C C     . LEU A 1 4539 ? 194.585 176.131 202.295 1.00 22.49  ? 4539 LEU A C     1 
ATOM   23292 O O     . LEU A 1 4539 ? 194.435 176.158 201.070 1.00 22.49  ? 4539 LEU A O     1 
ATOM   23293 C CB    . LEU A 1 4539 ? 192.486 177.073 203.276 1.00 22.49  ? 4539 LEU A CB    1 
ATOM   23294 C CG    . LEU A 1 4539 ? 191.754 178.100 204.138 1.00 22.49  ? 4539 LEU A CG    1 
ATOM   23295 C CD1   . LEU A 1 4539 ? 190.299 177.709 204.299 1.00 22.49  ? 4539 LEU A CD1   1 
ATOM   23296 C CD2   . LEU A 1 4539 ? 192.425 178.234 205.491 1.00 22.49  ? 4539 LEU A CD2   1 
ATOM   23297 N N     . CYS A 1 4540 ? 195.247 175.168 202.930 1.00 24.14  ? 4540 CYS A N     1 
ATOM   23298 C CA    . CYS A 1 4540 ? 195.776 173.995 202.253 1.00 24.14  ? 4540 CYS A CA    1 
ATOM   23299 C C     . CYS A 1 4540 ? 195.220 172.749 202.922 1.00 24.14  ? 4540 CYS A C     1 
ATOM   23300 O O     . CYS A 1 4540 ? 194.958 172.737 204.128 1.00 24.14  ? 4540 CYS A O     1 
ATOM   23301 C CB    . CYS A 1 4540 ? 197.309 173.968 202.277 1.00 24.14  ? 4540 CYS A CB    1 
ATOM   23302 S SG    . CYS A 1 4540 ? 198.029 173.657 203.904 1.00 24.14  ? 4540 CYS A SG    1 
ATOM   23303 N N     . LEU A 1 4541 ? 195.037 171.699 202.129 1.00 18.59  ? 4541 LEU A N     1 
ATOM   23304 C CA    . LEU A 1 4541 ? 194.393 170.483 202.601 1.00 18.59  ? 4541 LEU A CA    1 
ATOM   23305 C C     . LEU A 1 4541 ? 195.412 169.558 203.251 1.00 18.59  ? 4541 LEU A C     1 
ATOM   23306 O O     . LEU A 1 4541 ? 196.433 169.221 202.643 1.00 18.59  ? 4541 LEU A O     1 
ATOM   23307 C CB    . LEU A 1 4541 ? 193.692 169.764 201.450 1.00 18.59  ? 4541 LEU A CB    1 
ATOM   23308 C CG    . LEU A 1 4541 ? 192.929 168.500 201.841 1.00 18.59  ? 4541 LEU A CG    1 
ATOM   23309 C CD1   . LEU A 1 4541 ? 191.840 168.825 202.843 1.00 18.59  ? 4541 LEU A CD1   1 
ATOM   23310 C CD2   . LEU A 1 4541 ? 192.339 167.845 200.612 1.00 18.59  ? 4541 LEU A CD2   1 
ATOM   23311 N N     . GLU A 1 4542 ? 195.128 169.151 204.484 1.00 20.39  ? 4542 GLU A N     1 
ATOM   23312 C CA    . GLU A 1 4542 ? 195.926 168.169 205.204 1.00 20.39  ? 4542 GLU A CA    1 
ATOM   23313 C C     . GLU A 1 4542 ? 195.058 166.949 205.468 1.00 20.39  ? 4542 GLU A C     1 
ATOM   23314 O O     . GLU A 1 4542 ? 193.966 167.072 206.032 1.00 20.39  ? 4542 GLU A O     1 
ATOM   23315 C CB    . GLU A 1 4542 ? 196.459 168.744 206.517 1.00 20.39  ? 4542 GLU A CB    1 
ATOM   23316 C CG    . GLU A 1 4542 ? 197.406 167.819 207.257 1.00 20.39  ? 4542 GLU A CG    1 
ATOM   23317 C CD    . GLU A 1 4542 ? 197.762 168.335 208.636 1.00 20.39  ? 4542 GLU A CD    1 
ATOM   23318 O OE1   . GLU A 1 4542 ? 198.145 169.518 208.749 1.00 20.39  ? 4542 GLU A OE1   1 
ATOM   23319 O OE2   . GLU A 1 4542 ? 197.658 167.557 209.608 1.00 20.39  ? 4542 GLU A OE2   1 
ATOM   23320 N N     . VAL A 1 4543 ? 195.542 165.778 205.066 1.00 18.04  ? 4543 VAL A N     1 
ATOM   23321 C CA    . VAL A 1 4543 ? 194.768 164.544 205.107 1.00 18.04  ? 4543 VAL A CA    1 
ATOM   23322 C C     . VAL A 1 4543 ? 195.356 163.628 206.169 1.00 18.04  ? 4543 VAL A C     1 
ATOM   23323 O O     . VAL A 1 4543 ? 196.557 163.334 206.151 1.00 18.04  ? 4543 VAL A O     1 
ATOM   23324 C CB    . VAL A 1 4543 ? 194.745 163.852 203.735 1.00 18.04  ? 4543 VAL A CB    1 
ATOM   23325 C CG1   . VAL A 1 4543 ? 194.069 162.502 203.838 1.00 18.04  ? 4543 VAL A CG1   1 
ATOM   23326 C CG2   . VAL A 1 4543 ? 194.032 164.728 202.727 1.00 18.04  ? 4543 VAL A CG2   1 
ATOM   23327 N N     . ASN A 1 4544 ? 194.506 163.174 207.087 1.00 22.66  ? 4544 ASN A N     1 
ATOM   23328 C CA    . ASN A 1 4544 ? 194.897 162.252 208.145 1.00 22.66  ? 4544 ASN A CA    1 
ATOM   23329 C C     . ASN A 1 4544 ? 193.885 161.120 208.189 1.00 22.66  ? 4544 ASN A C     1 
ATOM   23330 O O     . ASN A 1 4544 ? 192.683 161.366 208.326 1.00 22.66  ? 4544 ASN A O     1 
ATOM   23331 C CB    . ASN A 1 4544 ? 194.975 162.967 209.497 1.00 22.66  ? 4544 ASN A CB    1 
ATOM   23332 C CG    . ASN A 1 4544 ? 195.115 162.006 210.657 1.00 22.66  ? 4544 ASN A CG    1 
ATOM   23333 O OD1   . ASN A 1 4544 ? 196.103 161.281 210.761 1.00 22.66  ? 4544 ASN A OD1   1 
ATOM   23334 N ND2   . ASN A 1 4544 ? 194.128 162.002 211.544 1.00 22.66  ? 4544 ASN A ND2   1 
ATOM   23335 N N     . VAL A 1 4545 ? 194.365 159.887 208.069 1.00 24.04  ? 4545 VAL A N     1 
ATOM   23336 C CA    . VAL A 1 4545 ? 193.500 158.713 208.032 1.00 24.04  ? 4545 VAL A CA    1 
ATOM   23337 C C     . VAL A 1 4545 ? 193.437 158.123 209.436 1.00 24.04  ? 4545 VAL A C     1 
ATOM   23338 O O     . VAL A 1 4545 ? 194.449 157.672 209.977 1.00 24.04  ? 4545 VAL A O     1 
ATOM   23339 C CB    . VAL A 1 4545 ? 193.998 157.680 207.017 1.00 24.04  ? 4545 VAL A CB    1 
ATOM   23340 C CG1   . VAL A 1 4545 ? 193.088 156.465 207.015 1.00 24.04  ? 4545 VAL A CG1   1 
ATOM   23341 C CG2   . VAL A 1 4545 ? 194.072 158.296 205.631 1.00 24.04  ? 4545 VAL A CG2   1 
ATOM   23342 N N     . THR A 1 4546 ? 192.245 158.119 210.024 1.00 35.04  ? 4546 THR A N     1 
ATOM   23343 C CA    . THR A 1 4546 ? 192.031 157.588 211.360 1.00 35.04  ? 4546 THR A CA    1 
ATOM   23344 C C     . THR A 1 4546 ? 191.447 156.183 211.286 1.00 35.04  ? 4546 THR A C     1 
ATOM   23345 O O     . THR A 1 4546 ? 190.732 155.835 210.343 1.00 35.04  ? 4546 THR A O     1 
ATOM   23346 C CB    . THR A 1 4546 ? 191.099 158.492 212.169 1.00 35.04  ? 4546 THR A CB    1 
ATOM   23347 O OG1   . THR A 1 4546 ? 189.775 158.424 211.627 1.00 35.04  ? 4546 THR A OG1   1 
ATOM   23348 C CG2   . THR A 1 4546 ? 191.586 159.930 212.130 1.00 35.04  ? 4546 THR A CG2   1 
ATOM   23349 N N     . THR A 1 4547 ? 191.762 155.375 212.301 1.00 48.78  ? 4547 THR A N     1 
ATOM   23350 C CA    . THR A 1 4547 ? 191.288 153.995 212.322 1.00 48.78  ? 4547 THR A CA    1 
ATOM   23351 C C     . THR A 1 4547 ? 189.792 153.924 212.606 1.00 48.78  ? 4547 THR A C     1 
ATOM   23352 O O     . THR A 1 4547 ? 189.065 153.175 211.944 1.00 48.78  ? 4547 THR A O     1 
ATOM   23353 C CB    . THR A 1 4547 ? 192.064 153.188 213.363 1.00 48.78  ? 4547 THR A CB    1 
ATOM   23354 O OG1   . THR A 1 4547 ? 193.471 153.363 213.155 1.00 48.78  ? 4547 THR A OG1   1 
ATOM   23355 C CG2   . THR A 1 4547 ? 191.722 151.710 213.253 1.00 48.78  ? 4547 THR A CG2   1 
ATOM   23356 N N     . SER A 1 4548 ? 189.316 154.692 213.583 1.00 58.45  ? 4548 SER A N     1 
ATOM   23357 C CA    . SER A 1 4548 ? 187.907 154.651 213.947 1.00 58.45  ? 4548 SER A CA    1 
ATOM   23358 C C     . SER A 1 4548 ? 187.056 155.266 212.844 1.00 58.45  ? 4548 SER A C     1 
ATOM   23359 O O     . SER A 1 4548 ? 187.368 156.344 212.330 1.00 58.45  ? 4548 SER A O     1 
ATOM   23360 C CB    . SER A 1 4548 ? 187.679 155.388 215.265 1.00 58.45  ? 4548 SER A CB    1 
ATOM   23361 O OG    . SER A 1 4548 ? 186.296 155.561 215.520 1.00 58.45  ? 4548 SER A OG    1 
ATOM   23362 N N     . GLN A 1 4549 ? 185.975 154.574 212.477 1.00 62.02  ? 4549 GLN A N     1 
ATOM   23363 C CA    . GLN A 1 4549 ? 185.063 155.097 211.468 1.00 62.02  ? 4549 GLN A CA    1 
ATOM   23364 C C     . GLN A 1 4549 ? 184.238 156.266 211.989 1.00 62.02  ? 4549 GLN A C     1 
ATOM   23365 O O     . GLN A 1 4549 ? 183.604 156.965 211.192 1.00 62.02  ? 4549 GLN A O     1 
ATOM   23366 C CB    . GLN A 1 4549 ? 184.135 153.990 210.965 1.00 62.02  ? 4549 GLN A CB    1 
ATOM   23367 C CG    . GLN A 1 4549 ? 184.787 153.023 209.988 1.00 62.02  ? 4549 GLN A CG    1 
ATOM   23368 C CD    . GLN A 1 4549 ? 185.689 152.016 210.677 1.00 62.02  ? 4549 GLN A CD    1 
ATOM   23369 O OE1   . GLN A 1 4549 ? 186.882 151.933 210.388 1.00 62.02  ? 4549 GLN A OE1   1 
ATOM   23370 N NE2   . GLN A 1 4549 ? 185.120 151.243 211.595 1.00 62.02  ? 4549 GLN A NE2   1 
ATOM   23371 N N     . GLY A 1 4550 ? 184.228 156.488 213.301 1.00 70.80  ? 4550 GLY A N     1 
ATOM   23372 C CA    . GLY A 1 4550 ? 183.498 157.596 213.883 1.00 70.80  ? 4550 GLY A CA    1 
ATOM   23373 C C     . GLY A 1 4550 ? 184.342 158.418 214.833 1.00 70.80  ? 4550 GLY A C     1 
ATOM   23374 O O     . GLY A 1 4550 ? 183.848 158.894 215.859 1.00 70.80  ? 4550 GLY A O     1 
ATOM   23375 N N     . ALA A 1 4551 ? 185.623 158.586 214.503 1.00 65.94  ? 4551 ALA A N     1 
ATOM   23376 C CA    . ALA A 1 4551 ? 186.527 159.348 215.353 1.00 65.94  ? 4551 ALA A CA    1 
ATOM   23377 C C     . ALA A 1 4551 ? 186.082 160.802 215.439 1.00 65.94  ? 4551 ALA A C     1 
ATOM   23378 O O     . ALA A 1 4551 ? 185.532 161.358 214.486 1.00 65.94  ? 4551 ALA A O     1 
ATOM   23379 C CB    . ALA A 1 4551 ? 187.957 159.262 214.818 1.00 65.94  ? 4551 ALA A CB    1 
ATOM   23380 N N     . THR A 1 4552 ? 186.320 161.412 216.598 1.00 62.06  ? 4552 THR A N     1 
ATOM   23381 C CA    . THR A 1 4552 ? 185.868 162.777 216.832 1.00 62.06  ? 4552 THR A CA    1 
ATOM   23382 C C     . THR A 1 4552 ? 186.583 163.755 215.907 1.00 62.06  ? 4552 THR A C     1 
ATOM   23383 O O     . THR A 1 4552 ? 187.783 163.626 215.645 1.00 62.06  ? 4552 THR A O     1 
ATOM   23384 C CB    . THR A 1 4552 ? 186.084 163.163 218.298 1.00 62.06  ? 4552 THR A CB    1 
ATOM   23385 O OG1   . THR A 1 4552 ? 185.629 164.506 218.514 1.00 62.06  ? 4552 THR A OG1   1 
ATOM   23386 C CG2   . THR A 1 4552 ? 187.553 163.046 218.690 1.00 62.06  ? 4552 THR A CG2   1 
ATOM   23387 N N     . LEU A 1 4553 ? 185.829 164.721 215.391 1.00 46.61  ? 4553 LEU A N     1 
ATOM   23388 C CA    . LEU A 1 4553 ? 186.371 165.729 214.498 1.00 46.61  ? 4553 LEU A CA    1 
ATOM   23389 C C     . LEU A 1 4553 ? 186.633 167.028 215.253 1.00 46.61  ? 4553 LEU A C     1 
ATOM   23390 O O     . LEU A 1 4553 ? 185.916 167.391 216.189 1.00 46.61  ? 4553 LEU A O     1 
ATOM   23391 C CB    . LEU A 1 4553 ? 185.409 165.990 213.338 1.00 46.61  ? 4553 LEU A CB    1 
ATOM   23392 C CG    . LEU A 1 4553 ? 185.117 164.833 212.383 1.00 46.61  ? 4553 LEU A CG    1 
ATOM   23393 C CD1   . LEU A 1 4553 ? 184.018 165.216 211.406 1.00 46.61  ? 4553 LEU A CD1   1 
ATOM   23394 C CD2   . LEU A 1 4553 ? 186.370 164.424 211.636 1.00 46.61  ? 4553 LEU A CD2   1 
ATOM   23395 N N     . ASP A 1 4554 ? 187.680 167.735 214.831 1.00 37.90  ? 4554 ASP A N     1 
ATOM   23396 C CA    . ASP A 1 4554 ? 187.954 169.058 215.377 1.00 37.90  ? 4554 ASP A CA    1 
ATOM   23397 C C     . ASP A 1 4554 ? 187.254 170.117 214.535 1.00 37.90  ? 4554 ASP A C     1 
ATOM   23398 O O     . ASP A 1 4554 ? 186.384 169.793 213.721 1.00 37.90  ? 4554 ASP A O     1 
ATOM   23399 C CB    . ASP A 1 4554 ? 189.462 169.322 215.467 1.00 37.90  ? 4554 ASP A CB    1 
ATOM   23400 C CG    . ASP A 1 4554 ? 190.149 169.329 214.112 1.00 37.90  ? 4554 ASP A CG    1 
ATOM   23401 O OD1   . ASP A 1 4554 ? 189.483 169.086 213.088 1.00 37.90  ? 4554 ASP A OD1   1 
ATOM   23402 O OD2   . ASP A 1 4554 ? 191.371 169.583 214.075 1.00 37.90  ? 4554 ASP A OD2   1 
ATOM   23403 N N     . ALA A 1 4555 ? 187.618 171.383 214.727 1.00 33.97  ? 4555 ALA A N     1 
ATOM   23404 C CA    . ALA A 1 4555 ? 186.970 172.489 214.038 1.00 33.97  ? 4555 ALA A CA    1 
ATOM   23405 C C     . ALA A 1 4555 ? 187.244 172.524 212.540 1.00 33.97  ? 4555 ALA A C     1 
ATOM   23406 O O     . ALA A 1 4555 ? 186.589 173.292 211.829 1.00 33.97  ? 4555 ALA A O     1 
ATOM   23407 C CB    . ALA A 1 4555 ? 187.401 173.823 214.659 1.00 33.97  ? 4555 ALA A CB    1 
ATOM   23408 N N     . CYS A 1 4556 ? 188.186 171.722 212.040 1.00 31.56  ? 4556 CYS A N     1 
ATOM   23409 C CA    . CYS A 1 4556 ? 188.572 171.780 210.639 1.00 31.56  ? 4556 CYS A CA    1 
ATOM   23410 C C     . CYS A 1 4556 ? 188.507 170.444 209.912 1.00 31.56  ? 4556 CYS A C     1 
ATOM   23411 O O     . CYS A 1 4556 ? 188.536 170.436 208.677 1.00 31.56  ? 4556 CYS A O     1 
ATOM   23412 C CB    . CYS A 1 4556 ? 189.993 172.348 210.502 1.00 31.56  ? 4556 CYS A CB    1 
ATOM   23413 S SG    . CYS A 1 4556 ? 190.273 173.877 211.427 1.00 31.56  ? 4556 CYS A SG    1 
ATOM   23414 N N     . SER A 1 4557 ? 188.411 169.325 210.624 1.00 28.72  ? 4557 SER A N     1 
ATOM   23415 C CA    . SER A 1 4557 ? 188.401 168.009 209.997 1.00 28.72  ? 4557 SER A CA    1 
ATOM   23416 C C     . SER A 1 4557 ? 186.973 167.628 209.632 1.00 28.72  ? 4557 SER A C     1 
ATOM   23417 O O     . SER A 1 4557 ? 186.075 167.691 210.479 1.00 28.72  ? 4557 SER A O     1 
ATOM   23418 C CB    . SER A 1 4557 ? 188.998 166.955 210.928 1.00 28.72  ? 4557 SER A CB    1 
ATOM   23419 O OG    . SER A 1 4557 ? 190.311 167.297 211.322 1.00 28.72  ? 4557 SER A OG    1 
ATOM   23420 N N     . PHE A 1 4558 ? 186.762 167.232 208.378 1.00 26.01  ? 4558 PHE A N     1 
ATOM   23421 C CA    . PHE A 1 4558 ? 185.491 166.660 207.947 1.00 26.01  ? 4558 PHE A CA    1 
ATOM   23422 C C     . PHE A 1 4558 ? 185.739 165.196 207.616 1.00 26.01  ? 4558 PHE A C     1 
ATOM   23423 O O     . PHE A 1 4558 ? 186.594 164.883 206.782 1.00 26.01  ? 4558 PHE A O     1 
ATOM   23424 C CB    . PHE A 1 4558 ? 184.906 167.382 206.737 1.00 26.01  ? 4558 PHE A CB    1 
ATOM   23425 C CG    . PHE A 1 4558 ? 184.469 168.781 207.021 1.00 26.01  ? 4558 PHE A CG    1 
ATOM   23426 C CD1   . PHE A 1 4558 ? 184.335 169.229 208.317 1.00 26.01  ? 4558 PHE A CD1   1 
ATOM   23427 C CD2   . PHE A 1 4558 ? 184.108 169.624 205.991 1.00 26.01  ? 4558 PHE A CD2   1 
ATOM   23428 C CE1   . PHE A 1 4558 ? 183.936 170.513 208.573 1.00 26.01  ? 4558 PHE A CE1   1 
ATOM   23429 C CE2   . PHE A 1 4558 ? 183.694 170.909 206.244 1.00 26.01  ? 4558 PHE A CE2   1 
ATOM   23430 C CZ    . PHE A 1 4558 ? 183.602 171.351 207.539 1.00 26.01  ? 4558 PHE A CZ    1 
ATOM   23431 N N     . GLY A 1 4559 ? 184.996 164.305 208.264 1.00 23.48  ? 4559 GLY A N     1 
ATOM   23432 C CA    . GLY A 1 4559 ? 185.161 162.889 207.987 1.00 23.48  ? 4559 GLY A CA    1 
ATOM   23433 C C     . GLY A 1 4559 ? 184.685 162.540 206.588 1.00 23.48  ? 4559 GLY A C     1 
ATOM   23434 O O     . GLY A 1 4559 ? 183.622 162.978 206.143 1.00 23.48  ? 4559 GLY A O     1 
ATOM   23435 N N     . VAL A 1 4560 ? 185.489 161.746 205.889 1.00 22.68  ? 4560 VAL A N     1 
ATOM   23436 C CA    . VAL A 1 4560 ? 185.155 161.254 204.558 1.00 22.68  ? 4560 VAL A CA    1 
ATOM   23437 C C     . VAL A 1 4560 ? 185.379 159.749 204.548 1.00 22.68  ? 4560 VAL A C     1 
ATOM   23438 O O     . VAL A 1 4560 ? 186.474 159.280 204.877 1.00 22.68  ? 4560 VAL A O     1 
ATOM   23439 C CB    . VAL A 1 4560 ? 185.989 161.936 203.461 1.00 22.68  ? 4560 VAL A CB    1 
ATOM   23440 C CG1   . VAL A 1 4560 ? 185.852 161.186 202.151 1.00 22.68  ? 4560 VAL A CG1   1 
ATOM   23441 C CG2   . VAL A 1 4560 ? 185.556 163.381 203.293 1.00 22.68  ? 4560 VAL A CG2   1 
ATOM   23442 N N     . THR A 1 4561 ? 184.349 158.998 204.175 1.00 23.36  ? 4561 THR A N     1 
ATOM   23443 C CA    . THR A 1 4561 ? 184.411 157.546 204.126 1.00 23.36  ? 4561 THR A CA    1 
ATOM   23444 C C     . THR A 1 4561 ? 184.382 157.058 202.683 1.00 23.36  ? 4561 THR A C     1 
ATOM   23445 O O     . THR A 1 4561 ? 184.094 157.810 201.750 1.00 23.36  ? 4561 THR A O     1 
ATOM   23446 C CB    . THR A 1 4561 ? 183.248 156.922 204.903 1.00 23.36  ? 4561 THR A CB    1 
ATOM   23447 O OG1   . THR A 1 4561 ? 182.008 157.278 204.281 1.00 23.36  ? 4561 THR A OG1   1 
ATOM   23448 C CG2   . THR A 1 4561 ? 183.242 157.413 206.339 1.00 23.36  ? 4561 THR A CG2   1 
ATOM   23449 N N     . GLY A 1 4562 ? 184.692 155.775 202.512 1.00 15.79  ? 4562 GLY A N     1 
ATOM   23450 C CA    . GLY A 1 4562 ? 184.617 155.137 201.217 1.00 15.79  ? 4562 GLY A CA    1 
ATOM   23451 C C     . GLY A 1 4562 ? 185.837 155.293 200.338 1.00 15.79  ? 4562 GLY A C     1 
ATOM   23452 O O     . GLY A 1 4562 ? 185.860 154.722 199.240 1.00 15.79  ? 4562 GLY A O     1 
ATOM   23453 N N     . LEU A 1 4563 ? 186.847 156.041 200.773 1.00 16.33  ? 4563 LEU A N     1 
ATOM   23454 C CA    . LEU A 1 4563 ? 188.058 156.189 199.979 1.00 16.33  ? 4563 LEU A CA    1 
ATOM   23455 C C     . LEU A 1 4563 ? 188.825 154.874 199.946 1.00 16.33  ? 4563 LEU A C     1 
ATOM   23456 O O     . LEU A 1 4563 ? 189.050 154.248 200.986 1.00 16.33  ? 4563 LEU A O     1 
ATOM   23457 C CB    . LEU A 1 4563 ? 188.935 157.303 200.548 1.00 16.33  ? 4563 LEU A CB    1 
ATOM   23458 C CG    . LEU A 1 4563 ? 188.452 158.738 200.333 1.00 16.33  ? 4563 LEU A CG    1 
ATOM   23459 C CD1   . LEU A 1 4563 ? 189.586 159.721 200.563 1.00 16.33  ? 4563 LEU A CD1   1 
ATOM   23460 C CD2   . LEU A 1 4563 ? 187.872 158.909 198.942 1.00 16.33  ? 4563 LEU A CD2   1 
ATOM   23461 N N     . LYS A 1 4564 ? 189.226 154.455 198.749 1.00 16.21  ? 4564 LYS A N     1 
ATOM   23462 C CA    . LYS A 1 4564 ? 189.956 153.208 198.555 1.00 16.21  ? 4564 LYS A CA    1 
ATOM   23463 C C     . LYS A 1 4564 ? 191.323 153.522 197.969 1.00 16.21  ? 4564 LYS A C     1 
ATOM   23464 O O     . LYS A 1 4564 ? 191.421 154.195 196.938 1.00 16.21  ? 4564 LYS A O     1 
ATOM   23465 C CB    . LYS A 1 4564 ? 189.184 152.254 197.643 1.00 16.21  ? 4564 LYS A CB    1 
ATOM   23466 C CG    . LYS A 1 4564 ? 187.761 151.988 198.097 1.00 16.21  ? 4564 LYS A CG    1 
ATOM   23467 C CD    . LYS A 1 4564 ? 187.329 150.574 197.751 1.00 16.21  ? 4564 LYS A CD    1 
ATOM   23468 C CE    . LYS A 1 4564 ? 186.139 150.143 198.592 1.00 16.21  ? 4564 LYS A CE    1 
ATOM   23469 N NZ    . LYS A 1 4564 ? 186.342 150.446 200.036 1.00 16.21  ? 4564 LYS A NZ    1 
ATOM   23470 N N     . LEU A 1 4565 ? 192.370 153.034 198.625 1.00 13.63  ? 4565 LEU A N     1 
ATOM   23471 C CA    . LEU A 1 4565 ? 193.740 153.250 198.187 1.00 13.63  ? 4565 LEU A CA    1 
ATOM   23472 C C     . LEU A 1 4565 ? 194.227 152.034 197.412 1.00 13.63  ? 4565 LEU A C     1 
ATOM   23473 O O     . LEU A 1 4565 ? 194.115 150.902 197.892 1.00 13.63  ? 4565 LEU A O     1 
ATOM   23474 C CB    . LEU A 1 4565 ? 194.646 153.509 199.390 1.00 13.63  ? 4565 LEU A CB    1 
ATOM   23475 C CG    . LEU A 1 4565 ? 196.100 153.874 199.114 1.00 13.63  ? 4565 LEU A CG    1 
ATOM   23476 C CD1   . LEU A 1 4565 ? 196.191 155.012 198.117 1.00 13.63  ? 4565 LEU A CD1   1 
ATOM   23477 C CD2   . LEU A 1 4565 ? 196.782 154.242 200.411 1.00 13.63  ? 4565 LEU A CD2   1 
ATOM   23478 N N     . GLN A 1 4566 ? 194.769 152.268 196.221 1.00 14.70  ? 4566 GLN A N     1 
ATOM   23479 C CA    . GLN A 1 4566 ? 195.244 151.200 195.353 1.00 14.70  ? 4566 GLN A CA    1 
ATOM   23480 C C     . GLN A 1 4566 ? 196.763 151.202 195.296 1.00 14.70  ? 4566 GLN A C     1 
ATOM   23481 O O     . GLN A 1 4566 ? 197.380 152.250 195.083 1.00 14.70  ? 4566 GLN A O     1 
ATOM   23482 C CB    . GLN A 1 4566 ? 194.673 151.336 193.943 1.00 14.70  ? 4566 GLN A CB    1 
ATOM   23483 C CG    . GLN A 1 4566 ? 193.217 151.727 193.897 1.00 14.70  ? 4566 GLN A CG    1 
ATOM   23484 C CD    . GLN A 1 4566 ? 192.537 151.216 192.650 1.00 14.70  ? 4566 GLN A CD    1 
ATOM   23485 O OE1   . GLN A 1 4566 ? 192.920 151.564 191.534 1.00 14.70  ? 4566 GLN A OE1   1 
ATOM   23486 N NE2   . GLN A 1 4566 ? 191.524 150.377 192.831 1.00 14.70  ? 4566 GLN A NE2   1 
ATOM   23487 N N     . GLY A 1 4567 ? 197.358 150.025 195.480 1.00 17.55  ? 4567 GLY A N     1 
ATOM   23488 C CA    . GLY A 1 4567 ? 198.785 149.852 195.353 1.00 17.55  ? 4567 GLY A CA    1 
ATOM   23489 C C     . GLY A 1 4567 ? 199.586 150.136 196.602 1.00 17.55  ? 4567 GLY A C     1 
ATOM   23490 O O     . GLY A 1 4567 ? 200.806 149.932 196.592 1.00 17.55  ? 4567 GLY A O     1 
ATOM   23491 N N     . ALA A 1 4568 ? 198.950 150.596 197.677 1.00 17.93  ? 4568 ALA A N     1 
ATOM   23492 C CA    . ALA A 1 4568 ? 199.674 150.911 198.897 1.00 17.93  ? 4568 ALA A CA    1 
ATOM   23493 C C     . ALA A 1 4568 ? 198.732 150.816 200.085 1.00 17.93  ? 4568 ALA A C     1 
ATOM   23494 O O     . ALA A 1 4568 ? 197.509 150.876 199.942 1.00 17.93  ? 4568 ALA A O     1 
ATOM   23495 C CB    . ALA A 1 4568 ? 200.309 152.304 198.831 1.00 17.93  ? 4568 ALA A CB    1 
ATOM   23496 N N     . THR A 1 4569 ? 199.324 150.665 201.266 1.00 20.78  ? 4569 THR A N     1 
ATOM   23497 C CA    . THR A 1 4569 ? 198.598 150.637 202.526 1.00 20.78  ? 4569 THR A CA    1 
ATOM   23498 C C     . THR A 1 4569 ? 199.121 151.746 203.424 1.00 20.78  ? 4569 THR A C     1 
ATOM   23499 O O     . THR A 1 4569 ? 200.330 151.989 203.483 1.00 20.78  ? 4569 THR A O     1 
ATOM   23500 C CB    . THR A 1 4569 ? 198.747 149.287 203.231 1.00 20.78  ? 4569 THR A CB    1 
ATOM   23501 O OG1   . THR A 1 4569 ? 200.128 149.055 203.532 1.00 20.78  ? 4569 THR A OG1   1 
ATOM   23502 C CG2   . THR A 1 4569 ? 198.232 148.165 202.349 1.00 20.78  ? 4569 THR A CG2   1 
ATOM   23503 N N     . CYS A 1 4570 ? 198.211 152.417 204.122 1.00 24.87  ? 4570 CYS A N     1 
ATOM   23504 C CA    . CYS A 1 4570 ? 198.559 153.521 205.009 1.00 24.87  ? 4570 CYS A CA    1 
ATOM   23505 C C     . CYS A 1 4570 ? 198.470 153.033 206.450 1.00 24.87  ? 4570 CYS A C     1 
ATOM   23506 O O     . CYS A 1 4570 ? 197.478 152.410 206.844 1.00 24.87  ? 4570 CYS A O     1 
ATOM   23507 C CB    . CYS A 1 4570 ? 197.655 154.729 204.763 1.00 24.87  ? 4570 CYS A CB    1 
ATOM   23508 S SG    . CYS A 1 4570 ? 196.000 154.642 205.483 1.00 24.87  ? 4570 CYS A SG    1 
ATOM   23509 N N     . ASN A 1 4571 ? 199.523 153.286 207.222 1.00 27.00  ? 4571 ASN A N     1 
ATOM   23510 C CA    . ASN A 1 4571 ? 199.573 152.953 208.639 1.00 27.00  ? 4571 ASN A CA    1 
ATOM   23511 C C     . ASN A 1 4571 ? 200.142 154.149 209.386 1.00 27.00  ? 4571 ASN A C     1 
ATOM   23512 O O     . ASN A 1 4571 ? 201.285 154.548 209.140 1.00 27.00  ? 4571 ASN A O     1 
ATOM   23513 C CB    . ASN A 1 4571 ? 200.423 151.706 208.885 1.00 27.00  ? 4571 ASN A CB    1 
ATOM   23514 C CG    . ASN A 1 4571 ? 199.736 150.435 208.430 1.00 27.00  ? 4571 ASN A CG    1 
ATOM   23515 O OD1   . ASN A 1 4571 ? 198.533 150.262 208.627 1.00 27.00  ? 4571 ASN A OD1   1 
ATOM   23516 N ND2   . ASN A 1 4571 ? 200.497 149.537 207.817 1.00 27.00  ? 4571 ASN A ND2   1 
ATOM   23517 N N     . ASN A 1 4572 ? 199.346 154.712 210.297 1.00 28.21  ? 4572 ASN A N     1 
ATOM   23518 C CA    . ASN A 1 4572 ? 199.725 155.918 211.032 1.00 28.21  ? 4572 ASN A CA    1 
ATOM   23519 C C     . ASN A 1 4572 ? 200.100 157.046 210.075 1.00 28.21  ? 4572 ASN A C     1 
ATOM   23520 O O     . ASN A 1 4572 ? 201.115 157.725 210.246 1.00 28.21  ? 4572 ASN A O     1 
ATOM   23521 C CB    . ASN A 1 4572 ? 200.863 155.632 212.013 1.00 28.21  ? 4572 ASN A CB    1 
ATOM   23522 C CG    . ASN A 1 4572 ? 200.378 154.990 213.295 1.00 28.21  ? 4572 ASN A CG    1 
ATOM   23523 O OD1   . ASN A 1 4572 ? 199.225 154.574 213.396 1.00 28.21  ? 4572 ASN A OD1   1 
ATOM   23524 N ND2   . ASN A 1 4572 ? 201.260 154.904 214.284 1.00 28.21  ? 4572 ASN A ND2   1 
ATOM   23525 N N     . ASN A 1 4573 ? 199.274 157.231 209.044 1.00 22.23  ? 4573 ASN A N     1 
ATOM   23526 C CA    . ASN A 1 4573 ? 199.420 158.236 207.994 1.00 22.23  ? 4573 ASN A CA    1 
ATOM   23527 C C     . ASN A 1 4573 ? 200.652 158.014 207.127 1.00 22.23  ? 4573 ASN A C     1 
ATOM   23528 O O     . ASN A 1 4573 ? 200.988 158.891 206.323 1.00 22.23  ? 4573 ASN A O     1 
ATOM   23529 C CB    . ASN A 1 4573 ? 199.463 159.665 208.552 1.00 22.23  ? 4573 ASN A CB    1 
ATOM   23530 C CG    . ASN A 1 4573 ? 198.100 160.319 208.583 1.00 22.23  ? 4573 ASN A CG    1 
ATOM   23531 O OD1   . ASN A 1 4573 ? 197.086 159.682 208.299 1.00 22.23  ? 4573 ASN A OD1   1 
ATOM   23532 N ND2   . ASN A 1 4573 ? 198.067 161.600 208.931 1.00 22.23  ? 4573 ASN A ND2   1 
ATOM   23533 N N     . LYS A 1 4574 ? 201.333 156.880 207.254 1.00 22.60  ? 4574 LYS A N     1 
ATOM   23534 C CA    . LYS A 1 4574 ? 202.522 156.582 206.469 1.00 22.60  ? 4574 LYS A CA    1 
ATOM   23535 C C     . LYS A 1 4574 ? 202.179 155.544 205.410 1.00 22.60  ? 4574 LYS A C     1 
ATOM   23536 O O     . LYS A 1 4574 ? 201.607 154.496 205.726 1.00 22.60  ? 4574 LYS A O     1 
ATOM   23537 C CB    . LYS A 1 4574 ? 203.650 156.067 207.363 1.00 22.60  ? 4574 LYS A CB    1 
ATOM   23538 C CG    . LYS A 1 4574 ? 204.111 157.051 208.422 1.00 22.60  ? 4574 LYS A CG    1 
ATOM   23539 C CD    . LYS A 1 4574 ? 205.226 157.942 207.909 1.00 22.60  ? 4574 LYS A CD    1 
ATOM   23540 C CE    . LYS A 1 4574 ? 205.894 158.686 209.051 1.00 22.60  ? 4574 LYS A CE    1 
ATOM   23541 N NZ    . LYS A 1 4574 ? 205.903 157.878 210.302 1.00 22.60  ? 4574 LYS A NZ    1 
ATOM   23542 N N     . LEU A 1 4575 ? 202.530 155.832 204.160 1.00 19.06  ? 4575 LEU A N     1 
ATOM   23543 C CA    . LEU A 1 4575 ? 202.280 154.903 203.069 1.00 19.06  ? 4575 LEU A CA    1 
ATOM   23544 C C     . LEU A 1 4575 ? 203.369 153.845 203.002 1.00 19.06  ? 4575 LEU A C     1 
ATOM   23545 O O     . LEU A 1 4575 ? 204.524 154.096 203.357 1.00 19.06  ? 4575 LEU A O     1 
ATOM   23546 C CB    . LEU A 1 4575 ? 202.203 155.627 201.725 1.00 19.06  ? 4575 LEU A CB    1 
ATOM   23547 C CG    . LEU A 1 4575 ? 201.045 156.585 201.475 1.00 19.06  ? 4575 LEU A CG    1 
ATOM   23548 C CD1   . LEU A 1 4575 ? 201.207 157.219 200.108 1.00 19.06  ? 4575 LEU A CD1   1 
ATOM   23549 C CD2   . LEU A 1 4575 ? 199.721 155.866 201.588 1.00 19.06  ? 4575 LEU A CD2   1 
ATOM   23550 N N     . SER A 1 4576 ? 202.989 152.658 202.542 1.00 20.39  ? 4576 SER A N     1 
ATOM   23551 C CA    . SER A 1 4576 ? 203.926 151.586 202.254 1.00 20.39  ? 4576 SER A CA    1 
ATOM   23552 C C     . SER A 1 4576 ? 203.377 150.774 201.093 1.00 20.39  ? 4576 SER A C     1 
ATOM   23553 O O     . SER A 1 4576 ? 202.176 150.495 201.038 1.00 20.39  ? 4576 SER A O     1 
ATOM   23554 C CB    . SER A 1 4576 ? 204.154 150.690 203.477 1.00 20.39  ? 4576 SER A CB    1 
ATOM   23555 O OG    . SER A 1 4576 ? 202.967 150.007 203.838 1.00 20.39  ? 4576 SER A OG    1 
ATOM   23556 N N     . LEU A 1 4577 ? 204.254 150.408 200.164 1.00 20.18  ? 4577 LEU A N     1 
ATOM   23557 C CA    . LEU A 1 4577 ? 203.826 149.670 198.985 1.00 20.18  ? 4577 LEU A CA    1 
ATOM   23558 C C     . LEU A 1 4577 ? 203.303 148.294 199.372 1.00 20.18  ? 4577 LEU A C     1 
ATOM   23559 O O     . LEU A 1 4577 ? 203.834 147.637 200.271 1.00 20.18  ? 4577 LEU A O     1 
ATOM   23560 C CB    . LEU A 1 4577 ? 204.981 149.532 197.997 1.00 20.18  ? 4577 LEU A CB    1 
ATOM   23561 C CG    . LEU A 1 4577 ? 205.419 150.813 197.295 1.00 20.18  ? 4577 LEU A CG    1 
ATOM   23562 C CD1   . LEU A 1 4577 ? 206.660 150.551 196.471 1.00 20.18  ? 4577 LEU A CD1   1 
ATOM   23563 C CD2   . LEU A 1 4577 ? 204.299 151.347 196.423 1.00 20.18  ? 4577 LEU A CD2   1 
ATOM   23564 N N     . SER A 1 4578 ? 202.251 147.858 198.684 1.00 21.53  ? 4578 SER A N     1 
ATOM   23565 C CA    . SER A 1 4578 ? 201.655 146.556 198.929 1.00 21.53  ? 4578 SER A CA    1 
ATOM   23566 C C     . SER A 1 4578 ? 201.263 145.925 197.603 1.00 21.53  ? 4578 SER A C     1 
ATOM   23567 O O     . SER A 1 4578 ? 200.932 146.614 196.635 1.00 21.53  ? 4578 SER A O     1 
ATOM   23568 C CB    . SER A 1 4578 ? 200.432 146.660 199.850 1.00 21.53  ? 4578 SER A CB    1 
ATOM   23569 O OG    . SER A 1 4578 ? 199.588 145.531 199.709 1.00 21.53  ? 4578 SER A OG    1 
ATOM   23570 N N     . ASN A 1 4579 ? 201.308 144.593 197.569 1.00 23.66  ? 4579 ASN A N     1 
ATOM   23571 C CA    . ASN A 1 4579 ? 200.874 143.867 196.382 1.00 23.66  ? 4579 ASN A CA    1 
ATOM   23572 C C     . ASN A 1 4579 ? 199.355 143.853 196.265 1.00 23.66  ? 4579 ASN A C     1 
ATOM   23573 O O     . ASN A 1 4579 ? 198.815 143.894 195.154 1.00 23.66  ? 4579 ASN A O     1 
ATOM   23574 C CB    . ASN A 1 4579 ? 201.423 142.441 196.408 1.00 23.66  ? 4579 ASN A CB    1 
ATOM   23575 C CG    . ASN A 1 4579 ? 202.924 142.393 196.211 1.00 23.66  ? 4579 ASN A CG    1 
ATOM   23576 O OD1   . ASN A 1 4579 ? 203.437 142.789 195.164 1.00 23.66  ? 4579 ASN A OD1   1 
ATOM   23577 N ND2   . ASN A 1 4579 ? 203.638 141.909 197.220 1.00 23.66  ? 4579 ASN A ND2   1 
ATOM   23578 N N     . ALA A 1 4580 ? 198.656 143.792 197.394 1.00 23.55  ? 4580 ALA A N     1 
ATOM   23579 C CA    . ALA A 1 4580 ? 197.202 143.817 197.380 1.00 23.55  ? 4580 ALA A CA    1 
ATOM   23580 C C     . ALA A 1 4580 ? 196.694 145.169 196.896 1.00 23.55  ? 4580 ALA A C     1 
ATOM   23581 O O     . ALA A 1 4580 ? 197.287 146.216 197.169 1.00 23.55  ? 4580 ALA A O     1 
ATOM   23582 C CB    . ALA A 1 4580 ? 196.647 143.516 198.771 1.00 23.55  ? 4580 ALA A CB    1 
ATOM   23583 N N     . ILE A 1 4581 ? 195.582 145.138 196.171 1.00 22.63  ? 4581 ILE A N     1 
ATOM   23584 C CA    . ILE A 1 4581 ? 194.990 146.338 195.601 1.00 22.63  ? 4581 ILE A CA    1 
ATOM   23585 C C     . ILE A 1 4581 ? 193.757 146.723 196.405 1.00 22.63  ? 4581 ILE A C     1 
ATOM   23586 O O     . ILE A 1 4581 ? 193.156 145.906 197.110 1.00 22.63  ? 4581 ILE A O     1 
ATOM   23587 C CB    . ILE A 1 4581 ? 194.630 146.149 194.115 1.00 22.63  ? 4581 ILE A CB    1 
ATOM   23588 C CG1   . ILE A 1 4581 ? 193.666 144.973 193.954 1.00 22.63  ? 4581 ILE A CG1   1 
ATOM   23589 C CG2   . ILE A 1 4581 ? 195.882 145.938 193.292 1.00 22.63  ? 4581 ILE A CG2   1 
ATOM   23590 C CD1   . ILE A 1 4581 ? 193.094 144.839 192.566 1.00 22.63  ? 4581 ILE A CD1   1 
ATOM   23591 N N     . SER A 1 4582 ? 193.383 147.997 196.290 1.00 16.37  ? 4582 SER A N     1 
ATOM   23592 C CA    . SER A 1 4582 ? 192.166 148.537 196.893 1.00 16.37  ? 4582 SER A CA    1 
ATOM   23593 C C     . SER A 1 4582 ? 192.149 148.311 198.407 1.00 16.37  ? 4582 SER A C     1 
ATOM   23594 O O     . SER A 1 4582 ? 191.276 147.636 198.955 1.00 16.37  ? 4582 SER A O     1 
ATOM   23595 C CB    . SER A 1 4582 ? 190.919 147.943 196.230 1.00 16.37  ? 4582 SER A CB    1 
ATOM   23596 O OG    . SER A 1 4582 ? 189.743 148.578 196.699 1.00 16.37  ? 4582 SER A OG    1 
ATOM   23597 N N     . THR A 1 4583 ? 193.139 148.892 199.077 1.00 16.81  ? 4583 THR A N     1 
ATOM   23598 C CA    . THR A 1 4583 ? 193.185 148.882 200.535 1.00 16.81  ? 4583 THR A CA    1 
ATOM   23599 C C     . THR A 1 4583 ? 192.270 149.985 201.049 1.00 16.81  ? 4583 THR A C     1 
ATOM   23600 O O     . THR A 1 4583 ? 192.603 151.171 200.956 1.00 16.81  ? 4583 THR A O     1 
ATOM   23601 C CB    . THR A 1 4583 ? 194.614 149.073 201.033 1.00 16.81  ? 4583 THR A CB    1 
ATOM   23602 O OG1   . THR A 1 4583 ? 195.423 147.973 200.600 1.00 16.81  ? 4583 THR A OG1   1 
ATOM   23603 C CG2   . THR A 1 4583 ? 194.642 149.148 202.552 1.00 16.81  ? 4583 THR A CG2   1 
ATOM   23604 N N     . ALA A 1 4584 ? 191.116 149.599 201.585 1.00 17.37  ? 4584 ALA A N     1 
ATOM   23605 C CA    . ALA A 1 4584 ? 190.111 150.574 201.981 1.00 17.37  ? 4584 ALA A CA    1 
ATOM   23606 C C     . ALA A 1 4584 ? 190.602 151.426 203.143 1.00 17.37  ? 4584 ALA A C     1 
ATOM   23607 O O     . ALA A 1 4584 ? 191.180 150.920 204.109 1.00 17.37  ? 4584 ALA A O     1 
ATOM   23608 C CB    . ALA A 1 4584 ? 188.811 149.868 202.364 1.00 17.37  ? 4584 ALA A CB    1 
ATOM   23609 N N     . LEU A 1 4585 ? 190.366 152.733 203.043 1.00 18.15  ? 4585 LEU A N     1 
ATOM   23610 C CA    . LEU A 1 4585 ? 190.705 153.675 204.100 1.00 18.15  ? 4585 LEU A CA    1 
ATOM   23611 C C     . LEU A 1 4585 ? 189.574 153.735 205.111 1.00 18.15  ? 4585 LEU A C     1 
ATOM   23612 O O     . LEU A 1 4585 ? 188.423 153.983 204.724 1.00 18.15  ? 4585 LEU A O     1 
ATOM   23613 C CB    . LEU A 1 4585 ? 190.960 155.063 203.522 1.00 18.15  ? 4585 LEU A CB    1 
ATOM   23614 C CG    . LEU A 1 4585 ? 192.094 155.165 202.501 1.00 18.15  ? 4585 LEU A CG    1 
ATOM   23615 C CD1   . LEU A 1 4585 ? 192.409 156.616 202.185 1.00 18.15  ? 4585 LEU A CD1   1 
ATOM   23616 C CD2   . LEU A 1 4585 ? 193.331 154.450 203.008 1.00 18.15  ? 4585 LEU A CD2   1 
ATOM   23617 N N     . PRO A 1 4586 ? 189.851 153.503 206.396 1.00 28.14  ? 4586 PRO A N     1 
ATOM   23618 C CA    . PRO A 1 4586 ? 188.774 153.476 207.396 1.00 28.14  ? 4586 PRO A CA    1 
ATOM   23619 C C     . PRO A 1 4586 ? 187.979 154.770 207.452 1.00 28.14  ? 4586 PRO A C     1 
ATOM   23620 O O     . PRO A 1 4586 ? 186.760 154.767 207.257 1.00 28.14  ? 4586 PRO A O     1 
ATOM   23621 C CB    . PRO A 1 4586 ? 189.525 153.227 208.711 1.00 28.14  ? 4586 PRO A CB    1 
ATOM   23622 C CG    . PRO A 1 4586 ? 190.811 152.592 208.304 1.00 28.14  ? 4586 PRO A CG    1 
ATOM   23623 C CD    . PRO A 1 4586 ? 191.166 153.204 206.986 1.00 28.14  ? 4586 PRO A CD    1 
ATOM   23624 N N     . LEU A 1 4587 ? 188.662 155.882 207.710 1.00 30.02  ? 4587 LEU A N     1 
ATOM   23625 C CA    . LEU A 1 4587 ? 188.014 157.188 207.769 1.00 30.02  ? 4587 LEU A CA    1 
ATOM   23626 C C     . LEU A 1 4587 ? 189.049 158.249 207.440 1.00 30.02  ? 4587 LEU A C     1 
ATOM   23627 O O     . LEU A 1 4587 ? 190.104 158.305 208.079 1.00 30.02  ? 4587 LEU A O     1 
ATOM   23628 C CB    . LEU A 1 4587 ? 187.400 157.445 209.145 1.00 30.02  ? 4587 LEU A CB    1 
ATOM   23629 C CG    . LEU A 1 4587 ? 186.872 158.864 209.355 1.00 30.02  ? 4587 LEU A CG    1 
ATOM   23630 C CD1   . LEU A 1 4587 ? 185.630 159.089 208.518 1.00 30.02  ? 4587 LEU A CD1   1 
ATOM   23631 C CD2   . LEU A 1 4587 ? 186.583 159.127 210.822 1.00 30.02  ? 4587 LEU A CD2   1 
ATOM   23632 N N     . THR A 1 4588 ? 188.747 159.084 206.453 1.00 23.48  ? 4588 THR A N     1 
ATOM   23633 C CA    . THR A 1 4588 ? 189.667 160.120 206.003 1.00 23.48  ? 4588 THR A CA    1 
ATOM   23634 C C     . THR A 1 4588 ? 189.241 161.459 206.594 1.00 23.48  ? 4588 THR A C     1 
ATOM   23635 O O     . THR A 1 4588 ? 188.092 161.881 206.425 1.00 23.48  ? 4588 THR A O     1 
ATOM   23636 C CB    . THR A 1 4588 ? 189.693 160.187 204.478 1.00 23.48  ? 4588 THR A CB    1 
ATOM   23637 O OG1   . THR A 1 4588 ? 190.046 158.904 203.950 1.00 23.48  ? 4588 THR A OG1   1 
ATOM   23638 C CG2   . THR A 1 4588 ? 190.705 161.210 204.010 1.00 23.48  ? 4588 THR A CG2   1 
ATOM   23639 N N     . GLN A 1 4589 ? 190.163 162.120 207.287 1.00 24.84  ? 4589 GLN A N     1 
ATOM   23640 C CA    . GLN A 1 4589 ? 189.909 163.416 207.904 1.00 24.84  ? 4589 GLN A CA    1 
ATOM   23641 C C     . GLN A 1 4589 ? 190.535 164.491 207.024 1.00 24.84  ? 4589 GLN A C     1 
ATOM   23642 O O     . GLN A 1 4589 ? 191.761 164.566 206.904 1.00 24.84  ? 4589 GLN A O     1 
ATOM   23643 C CB    . GLN A 1 4589 ? 190.486 163.464 209.316 1.00 24.84  ? 4589 GLN A CB    1 
ATOM   23644 C CG    . GLN A 1 4589 ? 189.791 162.555 210.309 1.00 24.84  ? 4589 GLN A CG    1 
ATOM   23645 C CD    . GLN A 1 4589 ? 189.784 163.124 211.711 1.00 24.84  ? 4589 GLN A CD    1 
ATOM   23646 O OE1   . GLN A 1 4589 ? 190.579 164.004 212.039 1.00 24.84  ? 4589 GLN A OE1   1 
ATOM   23647 N NE2   . GLN A 1 4589 ? 188.901 162.607 212.555 1.00 24.84  ? 4589 GLN A NE2   1 
ATOM   23648 N N     . LEU A 1 4590 ? 189.696 165.321 206.413 1.00 19.04  ? 4590 LEU A N     1 
ATOM   23649 C CA    . LEU A 1 4590 ? 190.162 166.404 205.558 1.00 19.04  ? 4590 LEU A CA    1 
ATOM   23650 C C     . LEU A 1 4590 ? 190.300 167.672 206.391 1.00 19.04  ? 4590 LEU A C     1 
ATOM   23651 O O     . LEU A 1 4590 ? 189.295 168.263 206.799 1.00 19.04  ? 4590 LEU A O     1 
ATOM   23652 C CB    . LEU A 1 4590 ? 189.196 166.626 204.397 1.00 19.04  ? 4590 LEU A CB    1 
ATOM   23653 C CG    . LEU A 1 4590 ? 188.943 165.414 203.503 1.00 19.04  ? 4590 LEU A CG    1 
ATOM   23654 C CD1   . LEU A 1 4590 ? 188.167 165.821 202.267 1.00 19.04  ? 4590 LEU A CD1   1 
ATOM   23655 C CD2   . LEU A 1 4590 ? 190.254 164.755 203.120 1.00 19.04  ? 4590 LEU A CD2   1 
ATOM   23656 N N     . ARG A 1 4591 ? 191.538 168.091 206.637 1.00 23.77  ? 4591 ARG A N     1 
ATOM   23657 C CA    . ARG A 1 4591 ? 191.823 169.245 207.479 1.00 23.77  ? 4591 ARG A CA    1 
ATOM   23658 C C     . ARG A 1 4591 ? 192.361 170.371 206.612 1.00 23.77  ? 4591 ARG A C     1 
ATOM   23659 O O     . ARG A 1 4591 ? 193.322 170.175 205.862 1.00 23.77  ? 4591 ARG A O     1 
ATOM   23660 C CB    . ARG A 1 4591 ? 192.831 168.895 208.574 1.00 23.77  ? 4591 ARG A CB    1 
ATOM   23661 C CG    . ARG A 1 4591 ? 192.575 167.565 209.254 1.00 23.77  ? 4591 ARG A CG    1 
ATOM   23662 C CD    . ARG A 1 4591 ? 193.456 167.360 210.481 1.00 23.77  ? 4591 ARG A CD    1 
ATOM   23663 N NE    . ARG A 1 4591 ? 193.362 168.464 211.430 1.00 23.77  ? 4591 ARG A NE    1 
ATOM   23664 C CZ    . ARG A 1 4591 ? 194.231 169.462 211.512 1.00 23.77  ? 4591 ARG A CZ    1 
ATOM   23665 N NH1   . ARG A 1 4591 ? 195.294 169.518 210.727 1.00 23.77  ? 4591 ARG A NH1   1 
ATOM   23666 N NH2   . ARG A 1 4591 ? 194.030 170.426 212.405 1.00 23.77  ? 4591 ARG A NH2   1 
ATOM   23667 N N     . TRP A 1 4592 ? 191.742 171.544 206.716 1.00 19.48  ? 4592 TRP A N     1 
ATOM   23668 C CA    . TRP A 1 4592 ? 192.215 172.745 206.031 1.00 19.48  ? 4592 TRP A CA    1 
ATOM   23669 C C     . TRP A 1 4592 ? 192.925 173.624 207.050 1.00 19.48  ? 4592 TRP A C     1 
ATOM   23670 O O     . TRP A 1 4592 ? 192.289 174.263 207.890 1.00 19.48  ? 4592 TRP A O     1 
ATOM   23671 C CB    . TRP A 1 4592 ? 191.057 173.478 205.367 1.00 19.48  ? 4592 TRP A CB    1 
ATOM   23672 C CG    . TRP A 1 4592 ? 190.509 172.761 204.188 1.00 19.48  ? 4592 TRP A CG    1 
ATOM   23673 C CD1   . TRP A 1 4592 ? 189.437 171.934 204.170 1.00 19.48  ? 4592 TRP A CD1   1 
ATOM   23674 C CD2   . TRP A 1 4592 ? 190.984 172.834 202.839 1.00 19.48  ? 4592 TRP A CD2   1 
ATOM   23675 N NE1   . TRP A 1 4592 ? 189.222 171.462 202.900 1.00 19.48  ? 4592 TRP A NE1   1 
ATOM   23676 C CE2   . TRP A 1 4592 ? 190.157 172.005 202.061 1.00 19.48  ? 4592 TRP A CE2   1 
ATOM   23677 C CE3   . TRP A 1 4592 ? 192.033 173.513 202.215 1.00 19.48  ? 4592 TRP A CE3   1 
ATOM   23678 C CZ2   . TRP A 1 4592 ? 190.343 171.835 200.694 1.00 19.48  ? 4592 TRP A CZ2   1 
ATOM   23679 C CZ3   . TRP A 1 4592 ? 192.217 173.343 200.857 1.00 19.48  ? 4592 TRP A CZ3   1 
ATOM   23680 C CH2   . TRP A 1 4592 ? 191.376 172.511 200.111 1.00 19.48  ? 4592 TRP A CH2   1 
ATOM   23681 N N     . VAL A 1 4593 ? 194.250 173.653 206.977 1.00 23.47  ? 4593 VAL A N     1 
ATOM   23682 C CA    . VAL A 1 4593 ? 195.064 174.470 207.864 1.00 23.47  ? 4593 VAL A CA    1 
ATOM   23683 C C     . VAL A 1 4593 ? 195.619 175.641 207.070 1.00 23.47  ? 4593 VAL A C     1 
ATOM   23684 O O     . VAL A 1 4593 ? 195.768 175.574 205.844 1.00 23.47  ? 4593 VAL A O     1 
ATOM   23685 C CB    . VAL A 1 4593 ? 196.203 173.654 208.510 1.00 23.47  ? 4593 VAL A CB    1 
ATOM   23686 C CG1   . VAL A 1 4593 ? 195.646 172.411 209.175 1.00 23.47  ? 4593 VAL A CG1   1 
ATOM   23687 C CG2   . VAL A 1 4593 ? 197.244 173.281 207.471 1.00 23.47  ? 4593 VAL A CG2   1 
ATOM   23688 N N     . LYS A 1 4594 ? 195.908 176.731 207.777 1.00 30.96  ? 4594 LYS A N     1 
ATOM   23689 C CA    . LYS A 1 4594 ? 196.506 177.893 207.137 1.00 30.96  ? 4594 LYS A CA    1 
ATOM   23690 C C     . LYS A 1 4594 ? 197.875 177.530 206.579 1.00 30.96  ? 4594 LYS A C     1 
ATOM   23691 O O     . LYS A 1 4594 ? 198.691 176.903 207.260 1.00 30.96  ? 4594 LYS A O     1 
ATOM   23692 C CB    . LYS A 1 4594 ? 196.622 179.044 208.135 1.00 30.96  ? 4594 LYS A CB    1 
ATOM   23693 C CG    . LYS A 1 4594 ? 197.600 180.130 207.724 1.00 30.96  ? 4594 LYS A CG    1 
ATOM   23694 C CD    . LYS A 1 4594 ? 197.235 181.468 208.343 1.00 30.96  ? 4594 LYS A CD    1 
ATOM   23695 C CE    . LYS A 1 4594 ? 196.139 182.163 207.552 1.00 30.96  ? 4594 LYS A CE    1 
ATOM   23696 N NZ    . LYS A 1 4594 ? 195.832 183.513 208.100 1.00 30.96  ? 4594 LYS A NZ    1 
ATOM   23697 N N     . GLN A 1 4595 ? 198.123 177.922 205.332 1.00 43.43  ? 4595 GLN A N     1 
ATOM   23698 C CA    . GLN A 1 4595 ? 199.378 177.578 204.681 1.00 43.43  ? 4595 GLN A CA    1 
ATOM   23699 C C     . GLN A 1 4595 ? 200.538 178.286 205.367 1.00 43.43  ? 4595 GLN A C     1 
ATOM   23700 O O     . GLN A 1 4595 ? 200.506 179.504 205.570 1.00 43.43  ? 4595 GLN A O     1 
ATOM   23701 C CB    . GLN A 1 4595 ? 199.329 177.953 203.202 1.00 43.43  ? 4595 GLN A CB    1 
ATOM   23702 C CG    . GLN A 1 4595 ? 200.124 177.023 202.306 1.00 43.43  ? 4595 GLN A CG    1 
ATOM   23703 C CD    . GLN A 1 4595 ? 199.830 177.240 200.836 1.00 43.43  ? 4595 GLN A CD    1 
ATOM   23704 O OE1   . GLN A 1 4595 ? 198.673 177.258 200.419 1.00 43.43  ? 4595 GLN A OE1   1 
ATOM   23705 N NE2   . GLN A 1 4595 ? 200.880 177.404 200.042 1.00 43.43  ? 4595 GLN A NE2   1 
ATOM   23706 N N     . THR A 1 4596 ? 201.564 177.520 205.725 1.00 66.10  ? 4596 THR A N     1 
ATOM   23707 C CA    . THR A 1 4596 ? 202.746 178.061 206.380 1.00 66.10  ? 4596 THR A CA    1 
ATOM   23708 C C     . THR A 1 4596 ? 203.853 178.420 205.398 1.00 66.10  ? 4596 THR A C     1 
ATOM   23709 O O     . THR A 1 4596 ? 204.918 178.872 205.831 1.00 66.10  ? 4596 THR A O     1 
ATOM   23710 C CB    . THR A 1 4596 ? 203.278 177.066 207.416 1.00 66.10  ? 4596 THR A CB    1 
ATOM   23711 O OG1   . THR A 1 4596 ? 204.364 177.659 208.138 1.00 66.10  ? 4596 THR A OG1   1 
ATOM   23712 C CG2   . THR A 1 4596 ? 203.757 175.796 206.737 1.00 66.10  ? 4596 THR A CG2   1 
ATOM   23713 N N     . ASN A 1 4597 ? 203.625 178.228 204.097 1.00 75.91  ? 4597 ASN A N     1 
ATOM   23714 C CA    . ASN A 1 4597 ? 204.583 178.584 203.050 1.00 75.91  ? 4597 ASN A CA    1 
ATOM   23715 C C     . ASN A 1 4597 ? 205.928 177.889 203.272 1.00 75.91  ? 4597 ASN A C     1 
ATOM   23716 O O     . ASN A 1 4597 ? 206.965 178.523 203.477 1.00 75.91  ? 4597 ASN A O     1 
ATOM   23717 C CB    . ASN A 1 4597 ? 204.753 180.105 202.958 1.00 75.91  ? 4597 ASN A CB    1 
ATOM   23718 C CG    . ASN A 1 4597 ? 203.431 180.831 202.818 1.00 75.91  ? 4597 ASN A CG    1 
ATOM   23719 O OD1   . ASN A 1 4597 ? 202.685 180.979 203.786 1.00 75.91  ? 4597 ASN A OD1   1 
ATOM   23720 N ND2   . ASN A 1 4597 ? 203.132 181.288 201.607 1.00 75.91  ? 4597 ASN A ND2   1 
ATOM   23721 N N     . THR A 1 4598 ? 205.890 176.560 203.227 1.00 81.18  ? 4598 THR A N     1 
ATOM   23722 C CA    . THR A 1 4598 ? 207.082 175.743 203.386 1.00 81.18  ? 4598 THR A CA    1 
ATOM   23723 C C     . THR A 1 4598 ? 207.193 174.776 202.215 1.00 81.18  ? 4598 THR A C     1 
ATOM   23724 O O     . THR A 1 4598 ? 206.201 174.430 201.568 1.00 81.18  ? 4598 THR A O     1 
ATOM   23725 C CB    . THR A 1 4598 ? 207.070 174.961 204.709 1.00 81.18  ? 4598 THR A CB    1 
ATOM   23726 O OG1   . THR A 1 4598 ? 208.354 174.363 204.924 1.00 81.18  ? 4598 THR A OG1   1 
ATOM   23727 C CG2   . THR A 1 4598 ? 206.013 173.868 204.677 1.00 81.18  ? 4598 THR A CG2   1 
ATOM   23728 N N     . GLU A 1 4599 ? 208.424 174.355 201.941 1.00 74.81  ? 4599 GLU A N     1 
ATOM   23729 C CA    . GLU A 1 4599 ? 208.673 173.371 200.898 1.00 74.81  ? 4599 GLU A CA    1 
ATOM   23730 C C     . GLU A 1 4599 ? 208.430 171.973 201.448 1.00 74.81  ? 4599 GLU A C     1 
ATOM   23731 O O     . GLU A 1 4599 ? 208.957 171.613 202.506 1.00 74.81  ? 4599 GLU A O     1 
ATOM   23732 C CB    . GLU A 1 4599 ? 210.102 173.499 200.373 1.00 74.81  ? 4599 GLU A CB    1 
ATOM   23733 C CG    . GLU A 1 4599 ? 210.543 172.354 199.473 1.00 74.81  ? 4599 GLU A CG    1 
ATOM   23734 C CD    . GLU A 1 4599 ? 209.617 172.148 198.291 1.00 74.81  ? 4599 GLU A CD    1 
ATOM   23735 O OE1   . GLU A 1 4599 ? 209.221 173.152 197.660 1.00 74.81  ? 4599 GLU A OE1   1 
ATOM   23736 O OE2   . GLU A 1 4599 ? 209.285 170.982 197.990 1.00 74.81  ? 4599 GLU A OE2   1 
ATOM   23737 N N     . LYS A 1 4600 ? 207.626 171.189 200.735 1.00 59.42  ? 4600 LYS A N     1 
ATOM   23738 C CA    . LYS A 1 4600 ? 207.328 169.834 201.174 1.00 59.42  ? 4600 LYS A CA    1 
ATOM   23739 C C     . LYS A 1 4600 ? 208.591 168.982 201.157 1.00 59.42  ? 4600 LYS A C     1 
ATOM   23740 O O     . LYS A 1 4600 ? 209.427 169.094 200.256 1.00 59.42  ? 4600 LYS A O     1 
ATOM   23741 C CB    . LYS A 1 4600 ? 206.248 169.208 200.290 1.00 59.42  ? 4600 LYS A CB    1 
ATOM   23742 C CG    . LYS A 1 4600 ? 206.642 169.031 198.832 1.00 59.42  ? 4600 LYS A CG    1 
ATOM   23743 C CD    . LYS A 1 4600 ? 205.506 168.422 198.026 1.00 59.42  ? 4600 LYS A CD    1 
ATOM   23744 C CE    . LYS A 1 4600 ? 205.904 168.220 196.573 1.00 59.42  ? 4600 LYS A CE    1 
ATOM   23745 N NZ    . LYS A 1 4600 ? 204.798 167.629 195.770 1.00 59.42  ? 4600 LYS A NZ    1 
ATOM   23746 N N     . LYS A 1 4601 ? 208.734 168.138 202.173 1.00 44.86  ? 4601 LYS A N     1 
ATOM   23747 C CA    . LYS A 1 4601 ? 209.909 167.290 202.274 1.00 44.86  ? 4601 LYS A CA    1 
ATOM   23748 C C     . LYS A 1 4601 ? 209.901 166.235 201.173 1.00 44.86  ? 4601 LYS A C     1 
ATOM   23749 O O     . LYS A 1 4601 ? 208.870 165.935 200.566 1.00 44.86  ? 4601 LYS A O     1 
ATOM   23750 C CB    . LYS A 1 4601 ? 209.972 166.625 203.649 1.00 44.86  ? 4601 LYS A CB    1 
ATOM   23751 C CG    . LYS A 1 4601 ? 208.626 166.158 204.173 1.00 44.86  ? 4601 LYS A CG    1 
ATOM   23752 C CD    . LYS A 1 4601 ? 208.735 165.667 205.606 1.00 44.86  ? 4601 LYS A CD    1 
ATOM   23753 C CE    . LYS A 1 4601 ? 209.687 164.489 205.714 1.00 44.86  ? 4601 LYS A CE    1 
ATOM   23754 N NZ    . LYS A 1 4601 ? 209.626 163.849 207.057 1.00 44.86  ? 4601 LYS A NZ    1 
ATOM   23755 N N     . ALA A 1 4602 ? 211.080 165.670 200.913 1.00 38.47  ? 4602 ALA A N     1 
ATOM   23756 C CA    . ALA A 1 4602 ? 211.223 164.655 199.876 1.00 38.47  ? 4602 ALA A CA    1 
ATOM   23757 C C     . ALA A 1 4602 ? 210.596 163.320 200.256 1.00 38.47  ? 4602 ALA A C     1 
ATOM   23758 O O     . ALA A 1 4602 ? 210.709 162.365 199.481 1.00 38.47  ? 4602 ALA A O     1 
ATOM   23759 C CB    . ALA A 1 4602 ? 212.701 164.454 199.541 1.00 38.47  ? 4602 ALA A CB    1 
ATOM   23760 N N     . SER A 1 4603 ? 209.945 163.227 201.416 1.00 30.48  ? 4603 SER A N     1 
ATOM   23761 C CA    . SER A 1 4603 ? 209.331 161.991 201.877 1.00 30.48  ? 4603 SER A CA    1 
ATOM   23762 C C     . SER A 1 4603 ? 207.809 162.025 201.787 1.00 30.48  ? 4603 SER A C     1 
ATOM   23763 O O     . SER A 1 4603 ? 207.136 161.293 202.520 1.00 30.48  ? 4603 SER A O     1 
ATOM   23764 C CB    . SER A 1 4603 ? 209.769 161.689 203.310 1.00 30.48  ? 4603 SER A CB    1 
ATOM   23765 O OG    . SER A 1 4603 ? 209.345 160.399 203.711 1.00 30.48  ? 4603 SER A OG    1 
ATOM   23766 N N     . VAL A 1 4604 ? 207.252 162.859 200.908 1.00 25.81  ? 4604 VAL A N     1 
ATOM   23767 C CA    . VAL A 1 4604 ? 205.813 162.923 200.696 1.00 25.81  ? 4604 VAL A CA    1 
ATOM   23768 C C     . VAL A 1 4604 ? 205.532 162.752 199.210 1.00 25.81  ? 4604 VAL A C     1 
ATOM   23769 O O     . VAL A 1 4604 ? 206.378 163.022 198.355 1.00 25.81  ? 4604 VAL A O     1 
ATOM   23770 C CB    . VAL A 1 4604 ? 205.193 164.241 201.210 1.00 25.81  ? 4604 VAL A CB    1 
ATOM   23771 C CG1   . VAL A 1 4604 ? 205.504 164.440 202.684 1.00 25.81  ? 4604 VAL A CG1   1 
ATOM   23772 C CG2   . VAL A 1 4604 ? 205.680 165.420 200.388 1.00 25.81  ? 4604 VAL A CG2   1 
ATOM   23773 N N     . VAL A 1 4605 ? 204.321 162.289 198.912 1.00 17.94  ? 4605 VAL A N     1 
ATOM   23774 C CA    . VAL A 1 4605 ? 203.880 162.053 197.544 1.00 17.94  ? 4605 VAL A CA    1 
ATOM   23775 C C     . VAL A 1 4605 ? 202.536 162.736 197.338 1.00 17.94  ? 4605 VAL A C     1 
ATOM   23776 O O     . VAL A 1 4605 ? 201.703 162.777 198.250 1.00 17.94  ? 4605 VAL A O     1 
ATOM   23777 C CB    . VAL A 1 4605 ? 203.776 160.548 197.226 1.00 17.94  ? 4605 VAL A CB    1 
ATOM   23778 C CG1   . VAL A 1 4605 ? 205.155 159.941 197.094 1.00 17.94  ? 4605 VAL A CG1   1 
ATOM   23779 C CG2   . VAL A 1 4605 ? 202.985 159.837 198.304 1.00 17.94  ? 4605 VAL A CG2   1 
ATOM   23780 N N     . THR A 1 4606 ? 202.332 163.280 196.142 1.00 15.85  ? 4606 THR A N     1 
ATOM   23781 C CA    . THR A 1 4606 ? 201.072 163.920 195.772 1.00 15.85  ? 4606 THR A CA    1 
ATOM   23782 C C     . THR A 1 4606 ? 200.245 162.887 195.015 1.00 15.85  ? 4606 THR A C     1 
ATOM   23783 O O     . THR A 1 4606 ? 200.384 162.716 193.804 1.00 15.85  ? 4606 THR A O     1 
ATOM   23784 C CB    . THR A 1 4606 ? 201.319 165.172 194.940 1.00 15.85  ? 4606 THR A CB    1 
ATOM   23785 O OG1   . THR A 1 4606 ? 202.167 166.069 195.668 1.00 15.85  ? 4606 THR A OG1   1 
ATOM   23786 C CG2   . THR A 1 4606 ? 200.008 165.871 194.632 1.00 15.85  ? 4606 THR A CG2   1 
ATOM   23787 N N     . LEU A 1 4607 ? 199.381 162.189 195.745 1.00 11.59  ? 4607 LEU A N     1 
ATOM   23788 C CA    . LEU A 1 4607 ? 198.557 161.121 195.188 1.00 11.59  ? 4607 LEU A CA    1 
ATOM   23789 C C     . LEU A 1 4607 ? 197.261 161.692 194.628 1.00 11.59  ? 4607 LEU A C     1 
ATOM   23790 O O     . LEU A 1 4607 ? 196.589 162.468 195.314 1.00 11.59  ? 4607 LEU A O     1 
ATOM   23791 C CB    . LEU A 1 4607 ? 198.236 160.079 196.249 1.00 11.59  ? 4607 LEU A CB    1 
ATOM   23792 C CG    . LEU A 1 4607 ? 199.384 159.178 196.699 1.00 11.59  ? 4607 LEU A CG    1 
ATOM   23793 C CD1   . LEU A 1 4607 ? 198.838 157.939 197.379 1.00 11.59  ? 4607 LEU A CD1   1 
ATOM   23794 C CD2   . LEU A 1 4607 ? 200.263 158.801 195.521 1.00 11.59  ? 4607 LEU A CD2   1 
ATOM   23795 N N     . PRO A 1 4608 ? 196.888 161.349 193.400 1.00 11.52  ? 4608 PRO A N     1 
ATOM   23796 C CA    . PRO A 1 4608 ? 195.589 161.779 192.879 1.00 11.52  ? 4608 PRO A CA    1 
ATOM   23797 C C     . PRO A 1 4608 ? 194.451 161.052 193.574 1.00 11.52  ? 4608 PRO A C     1 
ATOM   23798 O O     . PRO A 1 4608 ? 194.611 159.958 194.118 1.00 11.52  ? 4608 PRO A O     1 
ATOM   23799 C CB    . PRO A 1 4608 ? 195.661 161.404 191.398 1.00 11.52  ? 4608 PRO A CB    1 
ATOM   23800 C CG    . PRO A 1 4608 ? 196.607 160.261 191.359 1.00 11.52  ? 4608 PRO A CG    1 
ATOM   23801 C CD    . PRO A 1 4608 ? 197.629 160.529 192.429 1.00 11.52  ? 4608 PRO A CD    1 
ATOM   23802 N N     . VAL A 1 4609 ? 193.284 161.681 193.551 1.00 12.05  ? 4609 VAL A N     1 
ATOM   23803 C CA    . VAL A 1 4609 ? 192.060 161.092 194.089 1.00 12.05  ? 4609 VAL A CA    1 
ATOM   23804 C C     . VAL A 1 4609 ? 191.037 161.112 192.960 1.00 12.05  ? 4609 VAL A C     1 
ATOM   23805 O O     . VAL A 1 4609 ? 190.329 162.101 192.751 1.00 12.05  ? 4609 VAL A O     1 
ATOM   23806 C CB    . VAL A 1 4609 ? 191.547 161.828 195.328 1.00 12.05  ? 4609 VAL A CB    1 
ATOM   23807 C CG1   . VAL A 1 4609 ? 190.283 161.165 195.847 1.00 12.05  ? 4609 VAL A CG1   1 
ATOM   23808 C CG2   . VAL A 1 4609 ? 192.612 161.847 196.405 1.00 12.05  ? 4609 VAL A CG2   1 
ATOM   23809 N N     . TYR A 1 4610 ? 190.958 160.014 192.217 1.00 13.02  ? 4610 TYR A N     1 
ATOM   23810 C CA    . TYR A 1 4610 ? 190.001 159.902 191.131 1.00 13.02  ? 4610 TYR A CA    1 
ATOM   23811 C C     . TYR A 1 4610 ? 188.619 159.548 191.674 1.00 13.02  ? 4610 TYR A C     1 
ATOM   23812 O O     . TYR A 1 4610 ? 188.455 159.151 192.830 1.00 13.02  ? 4610 TYR A O     1 
ATOM   23813 C CB    . TYR A 1 4610 ? 190.463 158.859 190.117 1.00 13.02  ? 4610 TYR A CB    1 
ATOM   23814 C CG    . TYR A 1 4610 ? 191.741 159.227 189.400 1.00 13.02  ? 4610 TYR A CG    1 
ATOM   23815 C CD1   . TYR A 1 4610 ? 191.729 160.107 188.328 1.00 13.02  ? 4610 TYR A CD1   1 
ATOM   23816 C CD2   . TYR A 1 4610 ? 192.958 158.693 189.793 1.00 13.02  ? 4610 TYR A CD2   1 
ATOM   23817 C CE1   . TYR A 1 4610 ? 192.892 160.445 187.670 1.00 13.02  ? 4610 TYR A CE1   1 
ATOM   23818 C CE2   . TYR A 1 4610 ? 194.126 159.026 189.140 1.00 13.02  ? 4610 TYR A CE2   1 
ATOM   23819 C CZ    . TYR A 1 4610 ? 194.088 159.902 188.080 1.00 13.02  ? 4610 TYR A CZ    1 
ATOM   23820 O OH    . TYR A 1 4610 ? 195.250 160.236 187.425 1.00 13.02  ? 4610 TYR A OH    1 
ATOM   23821 N N     . LEU A 1 4611 ? 187.611 159.696 190.817 1.00 15.56  ? 4611 LEU A N     1 
ATOM   23822 C CA    . LEU A 1 4611 ? 186.232 159.457 191.223 1.00 15.56  ? 4611 LEU A CA    1 
ATOM   23823 C C     . LEU A 1 4611 ? 185.891 157.971 191.267 1.00 15.56  ? 4611 LEU A C     1 
ATOM   23824 O O     . LEU A 1 4611 ? 185.382 157.480 192.278 1.00 15.56  ? 4611 LEU A O     1 
ATOM   23825 C CB    . LEU A 1 4611 ? 185.273 160.191 190.282 1.00 15.56  ? 4611 LEU A CB    1 
ATOM   23826 C CG    . LEU A 1 4611 ? 183.801 160.180 190.694 1.00 15.56  ? 4611 LEU A CG    1 
ATOM   23827 C CD1   . LEU A 1 4611 ? 183.652 160.584 192.149 1.00 15.56  ? 4611 LEU A CD1   1 
ATOM   23828 C CD2   . LEU A 1 4611 ? 182.990 161.098 189.799 1.00 15.56  ? 4611 LEU A CD2   1 
ATOM   23829 N N     . ASN A 1 4612 ? 186.164 157.244 190.187 1.00 16.86  ? 4612 ASN A N     1 
ATOM   23830 C CA    . ASN A 1 4612 ? 185.844 155.827 190.094 1.00 16.86  ? 4612 ASN A CA    1 
ATOM   23831 C C     . ASN A 1 4612 ? 187.067 155.068 189.592 1.00 16.86  ? 4612 ASN A C     1 
ATOM   23832 O O     . ASN A 1 4612 ? 188.131 155.647 189.358 1.00 16.86  ? 4612 ASN A O     1 
ATOM   23833 C CB    . ASN A 1 4612 ? 184.630 155.597 189.186 1.00 16.86  ? 4612 ASN A CB    1 
ATOM   23834 C CG    . ASN A 1 4612 ? 184.713 156.380 187.894 1.00 16.86  ? 4612 ASN A CG    1 
ATOM   23835 O OD1   . ASN A 1 4612 ? 185.669 156.247 187.135 1.00 16.86  ? 4612 ASN A OD1   1 
ATOM   23836 N ND2   . ASN A 1 4612 ? 183.708 157.209 187.639 1.00 16.86  ? 4612 ASN A ND2   1 
ATOM   23837 N N     . PHE A 1 4613 ? 186.908 153.752 189.426 1.00 16.94  ? 4613 PHE A N     1 
ATOM   23838 C CA    . PHE A 1 4613 ? 188.032 152.909 189.035 1.00 16.94  ? 4613 PHE A CA    1 
ATOM   23839 C C     . PHE A 1 4613 ? 188.576 153.269 187.659 1.00 16.94  ? 4613 PHE A C     1 
ATOM   23840 O O     . PHE A 1 4613 ? 189.752 153.007 187.385 1.00 16.94  ? 4613 PHE A O     1 
ATOM   23841 C CB    . PHE A 1 4613 ? 187.629 151.432 189.071 1.00 16.94  ? 4613 PHE A CB    1 
ATOM   23842 C CG    . PHE A 1 4613 ? 186.644 151.041 188.006 1.00 16.94  ? 4613 PHE A CG    1 
ATOM   23843 C CD1   . PHE A 1 4613 ? 185.298 151.333 188.145 1.00 16.94  ? 4613 PHE A CD1   1 
ATOM   23844 C CD2   . PHE A 1 4613 ? 187.063 150.365 186.873 1.00 16.94  ? 4613 PHE A CD2   1 
ATOM   23845 C CE1   . PHE A 1 4613 ? 184.392 150.970 187.168 1.00 16.94  ? 4613 PHE A CE1   1 
ATOM   23846 C CE2   . PHE A 1 4613 ? 186.161 149.997 185.895 1.00 16.94  ? 4613 PHE A CE2   1 
ATOM   23847 C CZ    . PHE A 1 4613 ? 184.824 150.301 186.042 1.00 16.94  ? 4613 PHE A CZ    1 
ATOM   23848 N N     . THR A 1 4614 ? 187.756 153.855 186.791 1.00 16.48  ? 4614 THR A N     1 
ATOM   23849 C CA    . THR A 1 4614 ? 188.239 154.389 185.523 1.00 16.48  ? 4614 THR A CA    1 
ATOM   23850 C C     . THR A 1 4614 ? 188.853 155.755 185.792 1.00 16.48  ? 4614 THR A C     1 
ATOM   23851 O O     . THR A 1 4614 ? 188.134 156.731 186.027 1.00 16.48  ? 4614 THR A O     1 
ATOM   23852 C CB    . THR A 1 4614 ? 187.108 154.491 184.505 1.00 16.48  ? 4614 THR A CB    1 
ATOM   23853 O OG1   . THR A 1 4614 ? 186.173 155.490 184.928 1.00 16.48  ? 4614 THR A OG1   1 
ATOM   23854 C CG2   . THR A 1 4614 ? 186.391 153.161 184.372 1.00 16.48  ? 4614 THR A CG2   1 
ATOM   23855 N N     . ARG A 1 4615 ? 190.179 155.834 185.749 1.00 13.55  ? 4615 ARG A N     1 
ATOM   23856 C CA    . ARG A 1 4615 ? 190.865 157.056 186.142 1.00 13.55  ? 4615 ARG A CA    1 
ATOM   23857 C C     . ARG A 1 4615 ? 190.691 158.132 185.079 1.00 13.55  ? 4615 ARG A C     1 
ATOM   23858 O O     . ARG A 1 4615 ? 191.643 158.485 184.378 1.00 13.55  ? 4615 ARG A O     1 
ATOM   23859 C CB    . ARG A 1 4615 ? 192.345 156.770 186.389 1.00 13.55  ? 4615 ARG A CB    1 
ATOM   23860 C CG    . ARG A 1 4615 ? 192.584 155.796 187.528 1.00 13.55  ? 4615 ARG A CG    1 
ATOM   23861 C CD    . ARG A 1 4615 ? 194.061 155.601 187.798 1.00 13.55  ? 4615 ARG A CD    1 
ATOM   23862 N NE    . ARG A 1 4615 ? 194.286 154.672 188.897 1.00 13.55  ? 4615 ARG A NE    1 
ATOM   23863 C CZ    . ARG A 1 4615 ? 195.480 154.362 189.381 1.00 13.55  ? 4615 ARG A CZ    1 
ATOM   23864 N NH1   . ARG A 1 4615 ? 196.583 154.904 188.894 1.00 13.55  ? 4615 ARG A NH1   1 
ATOM   23865 N NH2   . ARG A 1 4615 ? 195.568 153.489 190.379 1.00 13.55  ? 4615 ARG A NH2   1 
ATOM   23866 N N     . ALA A 1 4616 ? 189.472 158.656 184.956 1.00 16.17  ? 4616 ALA A N     1 
ATOM   23867 C CA    . ALA A 1 4616 ? 189.149 159.664 183.956 1.00 16.17  ? 4616 ALA A CA    1 
ATOM   23868 C C     . ALA A 1 4616 ? 188.789 161.017 184.544 1.00 16.17  ? 4616 ALA A C     1 
ATOM   23869 O O     . ALA A 1 4616 ? 188.858 162.020 183.832 1.00 16.17  ? 4616 ALA A O     1 
ATOM   23870 C CB    . ALA A 1 4616 ? 187.989 159.185 183.074 1.00 16.17  ? 4616 ALA A CB    1 
ATOM   23871 N N     . ASP A 1 4617 ? 188.406 161.072 185.816 1.00 18.33  ? 4617 ASP A N     1 
ATOM   23872 C CA    . ASP A 1 4617 ? 188.019 162.314 186.471 1.00 18.33  ? 4617 ASP A CA    1 
ATOM   23873 C C     . ASP A 1 4617 ? 188.834 162.492 187.741 1.00 18.33  ? 4617 ASP A C     1 
ATOM   23874 O O     . ASP A 1 4617 ? 188.869 161.598 188.592 1.00 18.33  ? 4617 ASP A O     1 
ATOM   23875 C CB    . ASP A 1 4617 ? 186.525 162.319 186.794 1.00 18.33  ? 4617 ASP A CB    1 
ATOM   23876 C CG    . ASP A 1 4617 ? 185.665 162.395 185.551 1.00 18.33  ? 4617 ASP A CG    1 
ATOM   23877 O OD1   . ASP A 1 4617 ? 186.122 162.977 184.545 1.00 18.33  ? 4617 ASP A OD1   1 
ATOM   23878 O OD2   . ASP A 1 4617 ? 184.536 161.867 185.576 1.00 18.33  ? 4617 ASP A OD2   1 
ATOM   23879 N N     . LEU A 1 4618 ? 189.477 163.648 187.870 1.00 15.75  ? 4618 LEU A N     1 
ATOM   23880 C CA    . LEU A 1 4618 ? 190.303 163.964 189.026 1.00 15.75  ? 4618 LEU A CA    1 
ATOM   23881 C C     . LEU A 1 4618 ? 189.543 164.906 189.948 1.00 15.75  ? 4618 LEU A C     1 
ATOM   23882 O O     . LEU A 1 4618 ? 189.099 165.976 189.521 1.00 15.75  ? 4618 LEU A O     1 
ATOM   23883 C CB    . LEU A 1 4618 ? 191.623 164.600 188.590 1.00 15.75  ? 4618 LEU A CB    1 
ATOM   23884 C CG    . LEU A 1 4618 ? 192.529 165.125 189.702 1.00 15.75  ? 4618 LEU A CG    1 
ATOM   23885 C CD1   . LEU A 1 4618 ? 192.935 164.002 190.637 1.00 15.75  ? 4618 LEU A CD1   1 
ATOM   23886 C CD2   . LEU A 1 4618 ? 193.750 165.807 189.113 1.00 15.75  ? 4618 LEU A CD2   1 
ATOM   23887 N N     . ILE A 1 4619 ? 189.399 164.508 191.210 1.00 15.69  ? 4619 ILE A N     1 
ATOM   23888 C CA    . ILE A 1 4619 ? 188.661 165.307 192.181 1.00 15.69  ? 4619 ILE A CA    1 
ATOM   23889 C C     . ILE A 1 4619 ? 189.619 166.277 192.856 1.00 15.69  ? 4619 ILE A C     1 
ATOM   23890 O O     . ILE A 1 4619 ? 189.439 167.498 192.781 1.00 15.69  ? 4619 ILE A O     1 
ATOM   23891 C CB    . ILE A 1 4619 ? 187.950 164.417 193.216 1.00 15.69  ? 4619 ILE A CB    1 
ATOM   23892 C CG1   . ILE A 1 4619 ? 187.065 163.386 192.518 1.00 15.69  ? 4619 ILE A CG1   1 
ATOM   23893 C CG2   . ILE A 1 4619 ? 187.100 165.262 194.140 1.00 15.69  ? 4619 ILE A CG2   1 
ATOM   23894 C CD1   . ILE A 1 4619 ? 186.158 163.971 191.461 1.00 15.69  ? 4619 ILE A CD1   1 
ATOM   23895 N N     . PHE A 1 4620 ? 190.642 165.744 193.513 1.00 13.80  ? 4620 PHE A N     1 
ATOM   23896 C CA    . PHE A 1 4620 ? 191.647 166.555 194.189 1.00 13.80  ? 4620 PHE A CA    1 
ATOM   23897 C C     . PHE A 1 4620 ? 192.880 165.688 194.418 1.00 13.80  ? 4620 PHE A C     1 
ATOM   23898 O O     . PHE A 1 4620 ? 192.902 164.506 194.059 1.00 13.80  ? 4620 PHE A O     1 
ATOM   23899 C CB    . PHE A 1 4620 ? 191.100 167.146 195.495 1.00 13.80  ? 4620 PHE A CB    1 
ATOM   23900 C CG    . PHE A 1 4620 ? 190.765 166.120 196.544 1.00 13.80  ? 4620 PHE A CG    1 
ATOM   23901 C CD1   . PHE A 1 4620 ? 189.730 165.222 196.360 1.00 13.80  ? 4620 PHE A CD1   1 
ATOM   23902 C CD2   . PHE A 1 4620 ? 191.483 166.064 197.724 1.00 13.80  ? 4620 PHE A CD2   1 
ATOM   23903 C CE1   . PHE A 1 4620 ? 189.423 164.286 197.326 1.00 13.80  ? 4620 PHE A CE1   1 
ATOM   23904 C CE2   . PHE A 1 4620 ? 191.178 165.131 198.694 1.00 13.80  ? 4620 PHE A CE2   1 
ATOM   23905 C CZ    . PHE A 1 4620 ? 190.148 164.241 198.494 1.00 13.80  ? 4620 PHE A CZ    1 
ATOM   23906 N N     . THR A 1 4621 ? 193.914 166.278 195.011 1.00 12.72  ? 4621 THR A N     1 
ATOM   23907 C CA    . THR A 1 4621 ? 195.156 165.577 195.296 1.00 12.72  ? 4621 THR A CA    1 
ATOM   23908 C C     . THR A 1 4621 ? 195.417 165.592 196.794 1.00 12.72  ? 4621 THR A C     1 
ATOM   23909 O O     . THR A 1 4621 ? 195.050 166.538 197.496 1.00 12.72  ? 4621 THR A O     1 
ATOM   23910 C CB    . THR A 1 4621 ? 196.345 166.206 194.557 1.00 12.72  ? 4621 THR A CB    1 
ATOM   23911 O OG1   . THR A 1 4621 ? 196.778 167.379 195.256 1.00 12.72  ? 4621 THR A OG1   1 
ATOM   23912 C CG2   . THR A 1 4621 ? 195.954 166.583 193.139 1.00 12.72  ? 4621 THR A CG2   1 
ATOM   23913 N N     . VAL A 1 4622 ? 196.059 164.532 197.277 1.00 13.59  ? 4622 VAL A N     1 
ATOM   23914 C CA    . VAL A 1 4622 ? 196.326 164.341 198.697 1.00 13.59  ? 4622 VAL A CA    1 
ATOM   23915 C C     . VAL A 1 4622 ? 197.826 164.185 198.890 1.00 13.59  ? 4622 VAL A C     1 
ATOM   23916 O O     . VAL A 1 4622 ? 198.502 163.563 198.063 1.00 13.59  ? 4622 VAL A O     1 
ATOM   23917 C CB    . VAL A 1 4622 ? 195.575 163.119 199.256 1.00 13.59  ? 4622 VAL A CB    1 
ATOM   23918 C CG1   . VAL A 1 4622 ? 194.102 163.425 199.387 1.00 13.59  ? 4622 VAL A CG1   1 
ATOM   23919 C CG2   . VAL A 1 4622 ? 195.783 161.919 198.357 1.00 13.59  ? 4622 VAL A CG2   1 
ATOM   23920 N N     . ASP A 1 4623 ? 198.344 164.757 199.973 1.00 17.90  ? 4623 ASP A N     1 
ATOM   23921 C CA    . ASP A 1 4623 ? 199.760 164.654 200.307 1.00 17.90  ? 4623 ASP A CA    1 
ATOM   23922 C C     . ASP A 1 4623 ? 199.919 163.669 201.459 1.00 17.90  ? 4623 ASP A C     1 
ATOM   23923 O O     . ASP A 1 4623 ? 199.551 163.971 202.599 1.00 17.90  ? 4623 ASP A O     1 
ATOM   23924 C CB    . ASP A 1 4623 ? 200.330 166.022 200.670 1.00 17.90  ? 4623 ASP A CB    1 
ATOM   23925 C CG    . ASP A 1 4623 ? 200.836 166.781 199.461 1.00 17.90  ? 4623 ASP A CG    1 
ATOM   23926 O OD1   . ASP A 1 4623 ? 200.406 166.461 198.334 1.00 17.90  ? 4623 ASP A OD1   1 
ATOM   23927 O OD2   . ASP A 1 4623 ? 201.664 167.699 199.638 1.00 17.90  ? 4623 ASP A OD2   1 
ATOM   23928 N N     . PHE A 1 4624 ? 200.468 162.495 201.162 1.00 17.32  ? 4624 PHE A N     1 
ATOM   23929 C CA    . PHE A 1 4624 ? 200.731 161.466 202.159 1.00 17.32  ? 4624 PHE A CA    1 
ATOM   23930 C C     . PHE A 1 4624 ? 202.232 161.314 202.342 1.00 17.32  ? 4624 PHE A C     1 
ATOM   23931 O O     . PHE A 1 4624 ? 202.989 161.384 201.369 1.00 17.32  ? 4624 PHE A O     1 
ATOM   23932 C CB    . PHE A 1 4624 ? 200.132 160.119 201.751 1.00 17.32  ? 4624 PHE A CB    1 
ATOM   23933 C CG    . PHE A 1 4624 ? 198.648 160.023 201.930 1.00 17.32  ? 4624 PHE A CG    1 
ATOM   23934 C CD1   . PHE A 1 4624 ? 198.091 160.014 203.196 1.00 17.32  ? 4624 PHE A CD1   1 
ATOM   23935 C CD2   . PHE A 1 4624 ? 197.811 159.903 200.836 1.00 17.32  ? 4624 PHE A CD2   1 
ATOM   23936 C CE1   . PHE A 1 4624 ? 196.726 159.911 203.365 1.00 17.32  ? 4624 PHE A CE1   1 
ATOM   23937 C CE2   . PHE A 1 4624 ? 196.446 159.798 201.001 1.00 17.32  ? 4624 PHE A CE2   1 
ATOM   23938 C CZ    . PHE A 1 4624 ? 195.903 159.803 202.266 1.00 17.32  ? 4624 PHE A CZ    1 
ATOM   23939 N N     . GLU A 1 4625 ? 202.655 161.108 203.584 1.00 24.00  ? 4625 GLU A N     1 
ATOM   23940 C CA    . GLU A 1 4625 ? 204.044 160.777 203.863 1.00 24.00  ? 4625 GLU A CA    1 
ATOM   23941 C C     . GLU A 1 4625 ? 204.263 159.282 203.680 1.00 24.00  ? 4625 GLU A C     1 
ATOM   23942 O O     . GLU A 1 4625 ? 203.410 158.468 204.042 1.00 24.00  ? 4625 GLU A O     1 
ATOM   23943 C CB    . GLU A 1 4625 ? 204.418 161.200 205.282 1.00 24.00  ? 4625 GLU A CB    1 
ATOM   23944 C CG    . GLU A 1 4625 ? 205.880 160.996 205.629 1.00 24.00  ? 4625 GLU A CG    1 
ATOM   23945 C CD    . GLU A 1 4625 ? 206.218 161.483 207.022 1.00 24.00  ? 4625 GLU A CD    1 
ATOM   23946 O OE1   . GLU A 1 4625 ? 205.301 161.957 207.725 1.00 24.00  ? 4625 GLU A OE1   1 
ATOM   23947 O OE2   . GLU A 1 4625 ? 207.400 161.391 207.415 1.00 24.00  ? 4625 GLU A OE2   1 
ATOM   23948 N N     . ILE A 1 4626 ? 205.407 158.922 203.109 1.00 23.80  ? 4626 ILE A N     1 
ATOM   23949 C CA    . ILE A 1 4626 ? 205.719 157.535 202.802 1.00 23.80  ? 4626 ILE A CA    1 
ATOM   23950 C C     . ILE A 1 4626 ? 206.682 156.993 203.853 1.00 23.80  ? 4626 ILE A C     1 
ATOM   23951 O O     . ILE A 1 4626 ? 207.318 157.740 204.596 1.00 23.80  ? 4626 ILE A O     1 
ATOM   23952 C CB    . ILE A 1 4626 ? 206.303 157.374 201.386 1.00 23.80  ? 4626 ILE A CB    1 
ATOM   23953 C CG1   . ILE A 1 4626 ? 207.615 158.147 201.264 1.00 23.80  ? 4626 ILE A CG1   1 
ATOM   23954 C CG2   . ILE A 1 4626 ? 205.312 157.849 200.344 1.00 23.80  ? 4626 ILE A CG2   1 
ATOM   23955 C CD1   . ILE A 1 4626 ? 208.370 157.860 199.993 1.00 23.80  ? 4626 ILE A CD1   1 
ATOM   23956 N N     . ALA A 1 4627 ? 206.779 155.668 203.912 1.00 32.10  ? 4627 ALA A N     1 
ATOM   23957 C CA    . ALA A 1 4627 ? 207.765 155.029 204.768 1.00 32.10  ? 4627 ALA A CA    1 
ATOM   23958 C C     . ALA A 1 4627 ? 209.169 155.283 204.230 1.00 32.10  ? 4627 ALA A C     1 
ATOM   23959 O O     . ALA A 1 4627 ? 209.373 155.476 203.029 1.00 32.10  ? 4627 ALA A O     1 
ATOM   23960 C CB    . ALA A 1 4627 ? 207.501 153.528 204.868 1.00 32.10  ? 4627 ALA A CB    1 
ATOM   23961 N N     . THR A 1 4628 ? 210.145 155.282 205.139 1.00 41.21  ? 4628 THR A N     1 
ATOM   23962 C CA    . THR A 1 4628 ? 211.506 155.657 204.772 1.00 41.21  ? 4628 THR A CA    1 
ATOM   23963 C C     . THR A 1 4628 ? 212.157 154.666 203.814 1.00 41.21  ? 4628 THR A C     1 
ATOM   23964 O O     . THR A 1 4628 ? 213.138 155.022 203.152 1.00 41.21  ? 4628 THR A O     1 
ATOM   23965 C CB    . THR A 1 4628 ? 212.368 155.807 206.027 1.00 41.21  ? 4628 THR A CB    1 
ATOM   23966 O OG1   . THR A 1 4628 ? 213.648 156.343 205.670 1.00 41.21  ? 4628 THR A OG1   1 
ATOM   23967 C CG2   . THR A 1 4628 ? 212.557 154.463 206.714 1.00 41.21  ? 4628 THR A CG2   1 
ATOM   23968 N N     . LYS A 1 4629 ? 211.644 153.437 203.721 1.00 37.89  ? 4629 LYS A N     1 
ATOM   23969 C CA    . LYS A 1 4629 ? 212.273 152.449 202.850 1.00 37.89  ? 4629 LYS A CA    1 
ATOM   23970 C C     . LYS A 1 4629 ? 211.991 152.733 201.378 1.00 37.89  ? 4629 LYS A C     1 
ATOM   23971 O O     . LYS A 1 4629 ? 212.893 152.624 200.539 1.00 37.89  ? 4629 LYS A O     1 
ATOM   23972 C CB    . LYS A 1 4629 ? 211.811 151.041 203.230 1.00 37.89  ? 4629 LYS A CB    1 
ATOM   23973 C CG    . LYS A 1 4629 ? 210.322 150.915 203.495 1.00 37.89  ? 4629 LYS A CG    1 
ATOM   23974 C CD    . LYS A 1 4629 ? 210.037 149.859 204.550 1.00 37.89  ? 4629 LYS A CD    1 
ATOM   23975 C CE    . LYS A 1 4629 ? 210.341 148.464 204.026 1.00 37.89  ? 4629 LYS A CE    1 
ATOM   23976 N NZ    . LYS A 1 4629 ? 209.789 147.400 204.910 1.00 37.89  ? 4629 LYS A NZ    1 
ATOM   23977 N N     . GLU A 1 4630 ? 210.756 153.097 201.043 1.00 31.45  ? 4630 GLU A N     1 
ATOM   23978 C CA    . GLU A 1 4630 ? 210.396 153.316 199.650 1.00 31.45  ? 4630 GLU A CA    1 
ATOM   23979 C C     . GLU A 1 4630 ? 210.814 154.712 199.191 1.00 31.45  ? 4630 GLU A C     1 
ATOM   23980 O O     . GLU A 1 4630 ? 211.298 155.539 199.968 1.00 31.45  ? 4630 GLU A O     1 
ATOM   23981 C CB    . GLU A 1 4630 ? 208.895 153.125 199.439 1.00 31.45  ? 4630 GLU A CB    1 
ATOM   23982 C CG    . GLU A 1 4630 ? 208.415 151.696 199.608 1.00 31.45  ? 4630 GLU A CG    1 
ATOM   23983 C CD    . GLU A 1 4630 ? 207.979 151.397 201.024 1.00 31.45  ? 4630 GLU A CD    1 
ATOM   23984 O OE1   . GLU A 1 4630 ? 207.973 152.333 201.850 1.00 31.45  ? 4630 GLU A OE1   1 
ATOM   23985 O OE2   . GLU A 1 4630 ? 207.646 150.229 201.314 1.00 31.45  ? 4630 GLU A OE2   1 
ATOM   23986 N N     . ASP A 1 4631 ? 210.618 154.963 197.901 1.00 21.99  ? 4631 ASP A N     1 
ATOM   23987 C CA    . ASP A 1 4631 ? 210.898 156.245 197.278 1.00 21.99  ? 4631 ASP A CA    1 
ATOM   23988 C C     . ASP A 1 4631 ? 209.704 156.691 196.447 1.00 21.99  ? 4631 ASP A C     1 
ATOM   23989 O O     . ASP A 1 4631 ? 208.938 155.857 195.956 1.00 21.99  ? 4631 ASP A O     1 
ATOM   23990 C CB    . ASP A 1 4631 ? 212.155 156.170 196.397 1.00 21.99  ? 4631 ASP A CB    1 
ATOM   23991 C CG    . ASP A 1 4631 ? 212.093 155.051 195.377 1.00 21.99  ? 4631 ASP A CG    1 
ATOM   23992 O OD1   . ASP A 1 4631 ? 211.145 154.241 195.433 1.00 21.99  ? 4631 ASP A OD1   1 
ATOM   23993 O OD2   . ASP A 1 4631 ? 212.996 154.981 194.518 1.00 21.99  ? 4631 ASP A OD2   1 
ATOM   23994 N N     . PRO A 1 4632 ? 209.512 158.004 196.289 1.00 18.28  ? 4632 PRO A N     1 
ATOM   23995 C CA    . PRO A 1 4632 ? 208.326 158.488 195.562 1.00 18.28  ? 4632 PRO A CA    1 
ATOM   23996 C C     . PRO A 1 4632 ? 208.250 158.025 194.118 1.00 18.28  ? 4632 PRO A C     1 
ATOM   23997 O O     . PRO A 1 4632 ? 207.143 157.919 193.573 1.00 18.28  ? 4632 PRO A O     1 
ATOM   23998 C CB    . PRO A 1 4632 ? 208.457 160.015 195.657 1.00 18.28  ? 4632 PRO A CB    1 
ATOM   23999 C CG    . PRO A 1 4632 ? 209.884 160.269 196.009 1.00 18.28  ? 4632 PRO A CG    1 
ATOM   24000 C CD    . PRO A 1 4632 ? 210.307 159.110 196.844 1.00 18.28  ? 4632 PRO A CD    1 
ATOM   24001 N N     . ARG A 1 4633 ? 209.388 157.754 193.474 1.00 19.25  ? 4633 ARG A N     1 
ATOM   24002 C CA    . ARG A 1 4633 ? 209.355 157.324 192.079 1.00 19.25  ? 4633 ARG A CA    1 
ATOM   24003 C C     . ARG A 1 4633 ? 208.632 155.993 191.927 1.00 19.25  ? 4633 ARG A C     1 
ATOM   24004 O O     . ARG A 1 4633 ? 207.892 155.786 190.957 1.00 19.25  ? 4633 ARG A O     1 
ATOM   24005 C CB    . ARG A 1 4633 ? 210.774 157.227 191.522 1.00 19.25  ? 4633 ARG A CB    1 
ATOM   24006 C CG    . ARG A 1 4633 ? 211.424 158.568 191.245 1.00 19.25  ? 4633 ARG A CG    1 
ATOM   24007 C CD    . ARG A 1 4633 ? 212.932 158.427 191.151 1.00 19.25  ? 4633 ARG A CD    1 
ATOM   24008 N NE    . ARG A 1 4633 ? 213.442 157.445 192.100 1.00 19.25  ? 4633 ARG A NE    1 
ATOM   24009 C CZ    . ARG A 1 4633 ? 214.515 156.693 191.895 1.00 19.25  ? 4633 ARG A CZ    1 
ATOM   24010 N NH1   . ARG A 1 4633 ? 215.217 156.782 190.778 1.00 19.25  ? 4633 ARG A NH1   1 
ATOM   24011 N NH2   . ARG A 1 4633 ? 214.890 155.830 192.834 1.00 19.25  ? 4633 ARG A NH2   1 
ATOM   24012 N N     . SER A 1 4634 ? 208.841 155.073 192.871 1.00 17.14  ? 4634 SER A N     1 
ATOM   24013 C CA    . SER A 1 4634 ? 208.147 153.792 192.810 1.00 17.14  ? 4634 SER A CA    1 
ATOM   24014 C C     . SER A 1 4634 ? 206.644 153.976 192.969 1.00 17.14  ? 4634 SER A C     1 
ATOM   24015 O O     . SER A 1 4634 ? 205.855 153.276 192.325 1.00 17.14  ? 4634 SER A O     1 
ATOM   24016 C CB    . SER A 1 4634 ? 208.692 152.846 193.878 1.00 17.14  ? 4634 SER A CB    1 
ATOM   24017 O OG    . SER A 1 4634 ? 208.027 151.599 193.828 1.00 17.14  ? 4634 SER A OG    1 
ATOM   24018 N N     . PHE A 1 4635 ? 206.228 154.910 193.825 1.00 15.82  ? 4635 PHE A N     1 
ATOM   24019 C CA    . PHE A 1 4635 ? 204.809 155.237 193.920 1.00 15.82  ? 4635 PHE A CA    1 
ATOM   24020 C C     . PHE A 1 4635 ? 204.290 155.802 192.605 1.00 15.82  ? 4635 PHE A C     1 
ATOM   24021 O O     . PHE A 1 4635 ? 203.170 155.490 192.185 1.00 15.82  ? 4635 PHE A O     1 
ATOM   24022 C CB    . PHE A 1 4635 ? 204.568 156.232 195.053 1.00 15.82  ? 4635 PHE A CB    1 
ATOM   24023 C CG    . PHE A 1 4635 ? 204.512 155.605 196.412 1.00 15.82  ? 4635 PHE A CG    1 
ATOM   24024 C CD1   . PHE A 1 4635 ? 205.673 155.298 197.095 1.00 15.82  ? 4635 PHE A CD1   1 
ATOM   24025 C CD2   . PHE A 1 4635 ? 203.297 155.329 197.009 1.00 15.82  ? 4635 PHE A CD2   1 
ATOM   24026 C CE1   . PHE A 1 4635 ? 205.624 154.724 198.346 1.00 15.82  ? 4635 PHE A CE1   1 
ATOM   24027 C CE2   . PHE A 1 4635 ? 203.241 154.755 198.259 1.00 15.82  ? 4635 PHE A CE2   1 
ATOM   24028 C CZ    . PHE A 1 4635 ? 204.406 154.452 198.929 1.00 15.82  ? 4635 PHE A CZ    1 
ATOM   24029 N N     . TYR A 1 4636 ? 205.088 156.645 191.948 1.00 16.11  ? 4636 TYR A N     1 
ATOM   24030 C CA    . TYR A 1 4636 ? 204.647 157.268 190.704 1.00 16.11  ? 4636 TYR A CA    1 
ATOM   24031 C C     . TYR A 1 4636 ? 204.474 156.236 189.596 1.00 16.11  ? 4636 TYR A C     1 
ATOM   24032 O O     . TYR A 1 4636 ? 203.477 156.257 188.866 1.00 16.11  ? 4636 TYR A O     1 
ATOM   24033 C CB    . TYR A 1 4636 ? 205.639 158.349 190.276 1.00 16.11  ? 4636 TYR A CB    1 
ATOM   24034 C CG    . TYR A 1 4636 ? 205.763 159.501 191.246 1.00 16.11  ? 4636 TYR A CG    1 
ATOM   24035 C CD1   . TYR A 1 4636 ? 204.754 159.784 192.155 1.00 16.11  ? 4636 TYR A CD1   1 
ATOM   24036 C CD2   . TYR A 1 4636 ? 206.892 160.307 191.251 1.00 16.11  ? 4636 TYR A CD2   1 
ATOM   24037 C CE1   . TYR A 1 4636 ? 204.866 160.836 193.041 1.00 16.11  ? 4636 TYR A CE1   1 
ATOM   24038 C CE2   . TYR A 1 4636 ? 207.013 161.361 192.133 1.00 16.11  ? 4636 TYR A CE2   1 
ATOM   24039 C CZ    . TYR A 1 4636 ? 205.997 161.621 193.025 1.00 16.11  ? 4636 TYR A CZ    1 
ATOM   24040 O OH    . TYR A 1 4636 ? 206.115 162.671 193.906 1.00 16.11  ? 4636 TYR A OH    1 
ATOM   24041 N N     . GLU A 1 4637 ? 205.435 155.324 189.453 1.00 17.04  ? 4637 GLU A N     1 
ATOM   24042 C CA    . GLU A 1 4637 ? 205.425 154.405 188.321 1.00 17.04  ? 4637 GLU A CA    1 
ATOM   24043 C C     . GLU A 1 4637 ? 204.542 153.182 188.535 1.00 17.04  ? 4637 GLU A C     1 
ATOM   24044 O O     . GLU A 1 4637 ? 204.270 152.464 187.566 1.00 17.04  ? 4637 GLU A O     1 
ATOM   24045 C CB    . GLU A 1 4637 ? 206.852 153.959 187.991 1.00 17.04  ? 4637 GLU A CB    1 
ATOM   24046 C CG    . GLU A 1 4637 ? 207.386 152.850 188.872 1.00 17.04  ? 4637 GLU A CG    1 
ATOM   24047 C CD    . GLU A 1 4637 ? 208.889 152.692 188.751 1.00 17.04  ? 4637 GLU A CD    1 
ATOM   24048 O OE1   . GLU A 1 4637 ? 209.504 153.446 187.968 1.00 17.04  ? 4637 GLU A OE1   1 
ATOM   24049 O OE2   . GLU A 1 4637 ? 209.454 151.814 189.436 1.00 17.04  ? 4637 GLU A OE2   1 
ATOM   24050 N N     . ARG A 1 4638 ? 204.088 152.923 189.758 1.00 13.45  ? 4638 ARG A N     1 
ATOM   24051 C CA    . ARG A 1 4638 ? 203.176 151.817 190.023 1.00 13.45  ? 4638 ARG A CA    1 
ATOM   24052 C C     . ARG A 1 4638 ? 201.713 152.232 189.972 1.00 13.45  ? 4638 ARG A C     1 
ATOM   24053 O O     . ARG A 1 4638 ? 200.839 151.398 190.226 1.00 13.45  ? 4638 ARG A O     1 
ATOM   24054 C CB    . ARG A 1 4638 ? 203.482 151.188 191.385 1.00 13.45  ? 4638 ARG A CB    1 
ATOM   24055 C CG    . ARG A 1 4638 ? 204.803 150.446 191.443 1.00 13.45  ? 4638 ARG A CG    1 
ATOM   24056 C CD    . ARG A 1 4638 ? 205.145 150.049 192.867 1.00 13.45  ? 4638 ARG A CD    1 
ATOM   24057 N NE    . ARG A 1 4638 ? 204.273 148.997 193.375 1.00 13.45  ? 4638 ARG A NE    1 
ATOM   24058 C CZ    . ARG A 1 4638 ? 204.541 147.702 193.295 1.00 13.45  ? 4638 ARG A CZ    1 
ATOM   24059 N NH1   . ARG A 1 4638 ? 205.651 147.260 192.726 1.00 13.45  ? 4638 ARG A NH1   1 
ATOM   24060 N NH2   . ARG A 1 4638 ? 203.676 146.828 193.800 1.00 13.45  ? 4638 ARG A NH2   1 
ATOM   24061 N N     . GLY A 1 4639 ? 201.428 153.490 189.652 1.00 11.68  ? 4639 GLY A N     1 
ATOM   24062 C CA    . GLY A 1 4639 ? 200.057 153.958 189.560 1.00 11.68  ? 4639 GLY A CA    1 
ATOM   24063 C C     . GLY A 1 4639 ? 199.293 153.945 190.865 1.00 11.68  ? 4639 GLY A C     1 
ATOM   24064 O O     . GLY A 1 4639 ? 198.107 153.592 190.879 1.00 11.68  ? 4639 GLY A O     1 
ATOM   24065 N N     . VAL A 1 4640 ? 199.935 154.328 191.963 1.00 11.59  ? 4640 VAL A N     1 
ATOM   24066 C CA    . VAL A 1 4640 ? 199.263 154.383 193.255 1.00 11.59  ? 4640 VAL A CA    1 
ATOM   24067 C C     . VAL A 1 4640 ? 198.366 155.611 193.289 1.00 11.59  ? 4640 VAL A C     1 
ATOM   24068 O O     . VAL A 1 4640 ? 198.823 156.736 193.056 1.00 11.59  ? 4640 VAL A O     1 
ATOM   24069 C CB    . VAL A 1 4640 ? 200.285 154.407 194.401 1.00 11.59  ? 4640 VAL A CB    1 
ATOM   24070 C CG1   . VAL A 1 4640 ? 199.600 154.745 195.711 1.00 11.59  ? 4640 VAL A CG1   1 
ATOM   24071 C CG2   . VAL A 1 4640 ? 200.995 153.071 194.501 1.00 11.59  ? 4640 VAL A CG2   1 
ATOM   24072 N N     . ALA A 1 4641 ? 197.084 155.400 193.577 1.00 11.75  ? 4641 ALA A N     1 
ATOM   24073 C CA    . ALA A 1 4641 ? 196.119 156.490 193.582 1.00 11.75  ? 4641 ALA A CA    1 
ATOM   24074 C C     . ALA A 1 4641 ? 194.970 156.132 194.510 1.00 11.75  ? 4641 ALA A C     1 
ATOM   24075 O O     . ALA A 1 4641 ? 194.757 154.965 194.844 1.00 11.75  ? 4641 ALA A O     1 
ATOM   24076 C CB    . ALA A 1 4641 ? 195.598 156.786 192.173 1.00 11.75  ? 4641 ALA A CB    1 
ATOM   24077 N N     . VAL A 1 4642 ? 194.233 157.159 194.920 1.00 11.50  ? 4642 VAL A N     1 
ATOM   24078 C CA    . VAL A 1 4642 ? 193.070 157.011 195.786 1.00 11.50  ? 4642 VAL A CA    1 
ATOM   24079 C C     . VAL A 1 4642 ? 191.817 157.108 194.931 1.00 11.50  ? 4642 VAL A C     1 
ATOM   24080 O O     . VAL A 1 4642 ? 191.769 157.883 193.968 1.00 11.50  ? 4642 VAL A O     1 
ATOM   24081 C CB    . VAL A 1 4642 ? 193.067 158.078 196.897 1.00 11.50  ? 4642 VAL A CB    1 
ATOM   24082 C CG1   . VAL A 1 4642 ? 192.018 157.756 197.944 1.00 11.50  ? 4642 VAL A CG1   1 
ATOM   24083 C CG2   . VAL A 1 4642 ? 194.441 158.184 197.531 1.00 11.50  ? 4642 VAL A CG2   1 
ATOM   24084 N N     . LEU A 1 4643 ? 190.802 156.318 195.270 1.00 13.72  ? 4643 LEU A N     1 
ATOM   24085 C CA    . LEU A 1 4643 ? 189.543 156.323 194.542 1.00 13.72  ? 4643 LEU A CA    1 
ATOM   24086 C C     . LEU A 1 4643 ? 188.395 156.603 195.497 1.00 13.72  ? 4643 LEU A C     1 
ATOM   24087 O O     . LEU A 1 4643 ? 188.405 156.150 196.645 1.00 13.72  ? 4643 LEU A O     1 
ATOM   24088 C CB    . LEU A 1 4643 ? 189.294 154.996 193.825 1.00 13.72  ? 4643 LEU A CB    1 
ATOM   24089 C CG    . LEU A 1 4643 ? 190.313 154.564 192.774 1.00 13.72  ? 4643 LEU A CG    1 
ATOM   24090 C CD1   . LEU A 1 4643 ? 189.914 153.219 192.210 1.00 13.72  ? 4643 LEU A CD1   1 
ATOM   24091 C CD2   . LEU A 1 4643 ? 190.431 155.597 191.674 1.00 13.72  ? 4643 LEU A CD2   1 
ATOM   24092 N N     . CYS A 1 4644 ? 187.406 157.356 195.014 1.00 14.18  ? 4644 CYS A N     1 
ATOM   24093 C CA    . CYS A 1 4644 ? 186.231 157.638 195.830 1.00 14.18  ? 4644 CYS A CA    1 
ATOM   24094 C C     . CYS A 1 4644 ? 185.318 156.421 195.920 1.00 14.18  ? 4644 CYS A C     1 
ATOM   24095 O O     . CYS A 1 4644 ? 184.685 156.188 196.956 1.00 14.18  ? 4644 CYS A O     1 
ATOM   24096 C CB    . CYS A 1 4644 ? 185.477 158.838 195.262 1.00 14.18  ? 4644 CYS A CB    1 
ATOM   24097 S SG    . CYS A 1 4644 ? 186.385 160.396 195.364 1.00 14.18  ? 4644 CYS A SG    1 
ATOM   24098 N N     . THR A 1 4645 ? 185.237 155.636 194.850 1.00 12.58  ? 4645 THR A N     1 
ATOM   24099 C CA    . THR A 1 4645 ? 184.406 154.437 194.839 1.00 12.58  ? 4645 THR A CA    1 
ATOM   24100 C C     . THR A 1 4645 ? 185.247 153.183 194.631 1.00 12.58  ? 4645 THR A C     1 
ATOM   24101 O O     . THR A 1 4645 ? 186.178 153.171 193.827 0.00 12.58  ? 4645 THR A O     1 
ATOM   24102 C CB    . THR A 1 4645 ? 183.333 154.500 193.739 1.00 12.58  ? 4645 THR A CB    1 
ATOM   24103 O OG1   . THR A 1 4645 ? 183.958 154.395 192.455 1.00 12.58  ? 4645 THR A OG1   1 
ATOM   24104 C CG2   . THR A 1 4645 ? 182.566 155.807 193.815 1.00 12.58  ? 4645 THR A CG2   1 
HETATM 24105 P PB    . ADP B 2 .    ? 190.874 178.619 172.071 1.00 34.96  ? 4701 ADP A PB    1 
HETATM 24106 O O1B   . ADP B 2 .    ? 192.271 178.248 171.643 1.00 34.96  ? 4701 ADP A O1B   1 
HETATM 24107 O O2B   . ADP B 2 .    ? 190.129 177.537 172.812 1.00 34.96  ? 4701 ADP A O2B   1 
HETATM 24108 O O3B   . ADP B 2 .    ? 190.066 179.312 171.003 1.00 34.96  ? 4701 ADP A O3B   1 
HETATM 24109 P PA    . ADP B 2 .    ? 191.441 181.265 172.756 1.00 34.96  ? 4701 ADP A PA    1 
HETATM 24110 O O1A   . ADP B 2 .    ? 192.722 181.261 171.963 1.00 34.96  ? 4701 ADP A O1A   1 
HETATM 24111 O O2A   . ADP B 2 .    ? 190.182 181.854 172.170 1.00 34.96  ? 4701 ADP A O2A   1 
HETATM 24112 O O3A   . ADP B 2 .    ? 191.111 179.752 173.186 1.00 34.96  ? 4701 ADP A O3A   1 
HETATM 24113 O "O5'" . ADP B 2 .    ? 191.711 181.963 174.180 1.00 34.96  ? 4701 ADP A "O5'" 1 
HETATM 24114 C "C5'" . ADP B 2 .    ? 190.710 182.797 174.755 1.00 34.96  ? 4701 ADP A "C5'" 1 
HETATM 24115 C "C4'" . ADP B 2 .    ? 191.353 183.898 175.585 1.00 34.96  ? 4701 ADP A "C4'" 1 
HETATM 24116 O "O4'" . ADP B 2 .    ? 192.325 183.369 176.488 1.00 34.96  ? 4701 ADP A "O4'" 1 
HETATM 24117 C "C3'" . ADP B 2 .    ? 192.075 184.893 174.695 1.00 34.96  ? 4701 ADP A "C3'" 1 
HETATM 24118 O "O3'" . ADP B 2 .    ? 191.375 186.138 174.690 1.00 34.96  ? 4701 ADP A "O3'" 1 
HETATM 24119 C "C2'" . ADP B 2 .    ? 193.440 185.081 175.318 1.00 34.96  ? 4701 ADP A "C2'" 1 
HETATM 24120 O "O2'" . ADP B 2 .    ? 193.666 186.469 175.565 1.00 34.96  ? 4701 ADP A "O2'" 1 
HETATM 24121 C "C1'" . ADP B 2 .    ? 193.393 184.306 176.622 1.00 34.96  ? 4701 ADP A "C1'" 1 
HETATM 24122 N N9    . ADP B 2 .    ? 194.683 183.614 176.850 1.00 34.96  ? 4701 ADP A N9    1 
HETATM 24123 C C8    . ADP B 2 .    ? 194.923 182.306 176.662 1.00 34.96  ? 4701 ADP A C8    1 
HETATM 24124 N N7    . ADP B 2 .    ? 196.208 181.996 176.968 1.00 34.96  ? 4701 ADP A N7    1 
HETATM 24125 C C5    . ADP B 2 .    ? 196.811 183.129 177.365 1.00 34.96  ? 4701 ADP A C5    1 
HETATM 24126 C C6    . ADP B 2 .    ? 198.163 183.512 177.827 1.00 34.96  ? 4701 ADP A C6    1 
HETATM 24127 N N6    . ADP B 2 .    ? 199.152 182.593 177.928 1.00 34.96  ? 4701 ADP A N6    1 
HETATM 24128 N N1    . ADP B 2 .    ? 198.375 184.806 178.145 1.00 34.96  ? 4701 ADP A N1    1 
HETATM 24129 C C2    . ADP B 2 .    ? 197.400 185.727 178.049 1.00 34.96  ? 4701 ADP A C2    1 
HETATM 24130 N N3    . ADP B 2 .    ? 196.152 185.450 177.637 1.00 34.96  ? 4701 ADP A N3    1 
HETATM 24131 C C4    . ADP B 2 .    ? 195.801 184.192 177.288 1.00 34.96  ? 4701 ADP A C4    1 
HETATM 24132 P PG    . ATP C 3 .    ? 157.239 191.544 178.014 1.00 16.07  ? 4702 ATP A PG    1 
HETATM 24133 O O1G   . ATP C 3 .    ? 156.548 191.716 176.706 1.00 16.07  ? 4702 ATP A O1G   1 
HETATM 24134 O O2G   . ATP C 3 .    ? 156.490 190.641 178.995 1.00 16.07  ? 4702 ATP A O2G   1 
HETATM 24135 O O3G   . ATP C 3 .    ? 158.683 191.054 177.883 1.00 16.07  ? 4702 ATP A O3G   1 
HETATM 24136 P PB    . ATP C 3 .    ? 158.468 193.927 179.302 1.00 16.07  ? 4702 ATP A PB    1 
HETATM 24137 O O1B   . ATP C 3 .    ? 158.915 194.859 178.249 1.00 16.07  ? 4702 ATP A O1B   1 
HETATM 24138 O O2B   . ATP C 3 .    ? 159.550 193.074 179.956 1.00 16.07  ? 4702 ATP A O2B   1 
HETATM 24139 O O3B   . ATP C 3 .    ? 157.360 192.939 178.768 1.00 16.07  ? 4702 ATP A O3B   1 
HETATM 24140 P PA    . ATP C 3 .    ? 157.384 196.191 180.849 1.00 16.07  ? 4702 ATP A PA    1 
HETATM 24141 O O1A   . ATP C 3 .    ? 158.548 196.838 181.486 1.00 16.07  ? 4702 ATP A O1A   1 
HETATM 24142 O O2A   . ATP C 3 .    ? 156.860 196.877 179.590 1.00 16.07  ? 4702 ATP A O2A   1 
HETATM 24143 O O3A   . ATP C 3 .    ? 157.699 194.688 180.468 1.00 16.07  ? 4702 ATP A O3A   1 
HETATM 24144 O "O5'" . ATP C 3 .    ? 156.200 196.068 181.885 1.00 16.07  ? 4702 ATP A "O5'" 1 
HETATM 24145 C "C5'" . ATP C 3 .    ? 156.255 196.741 183.159 1.00 16.07  ? 4702 ATP A "C5'" 1 
HETATM 24146 C "C4'" . ATP C 3 .    ? 154.889 196.724 183.792 1.00 16.07  ? 4702 ATP A "C4'" 1 
HETATM 24147 O "O4'" . ATP C 3 .    ? 155.004 197.095 185.184 1.00 16.07  ? 4702 ATP A "O4'" 1 
HETATM 24148 C "C3'" . ATP C 3 .    ? 153.883 197.697 183.185 1.00 16.07  ? 4702 ATP A "C3'" 1 
HETATM 24149 O "O3'" . ATP C 3 .    ? 152.562 197.176 183.264 1.00 16.07  ? 4702 ATP A "O3'" 1 
HETATM 24150 C "C2'" . ATP C 3 .    ? 154.050 198.936 184.064 1.00 16.07  ? 4702 ATP A "C2'" 1 
HETATM 24151 O "O2'" . ATP C 3 .    ? 152.870 199.729 184.087 1.00 16.07  ? 4702 ATP A "O2'" 1 
HETATM 24152 C "C1'" . ATP C 3 .    ? 154.293 198.293 185.429 1.00 16.07  ? 4702 ATP A "C1'" 1 
HETATM 24153 N N9    . ATP C 3 .    ? 155.072 199.116 186.350 1.00 16.07  ? 4702 ATP A N9    1 
HETATM 24154 C C8    . ATP C 3 .    ? 154.638 199.670 187.525 1.00 16.07  ? 4702 ATP A C8    1 
HETATM 24155 N N7    . ATP C 3 .    ? 155.547 200.373 188.155 1.00 16.07  ? 4702 ATP A N7    1 
HETATM 24156 C C5    . ATP C 3 .    ? 156.662 200.270 187.338 1.00 16.07  ? 4702 ATP A C5    1 
HETATM 24157 C C6    . ATP C 3 .    ? 157.966 200.790 187.442 1.00 16.07  ? 4702 ATP A C6    1 
HETATM 24158 N N6    . ATP C 3 .    ? 158.384 201.553 188.457 1.00 16.07  ? 4702 ATP A N6    1 
HETATM 24159 N N1    . ATP C 3 .    ? 158.838 200.499 186.454 1.00 16.07  ? 4702 ATP A N1    1 
HETATM 24160 C C2    . ATP C 3 .    ? 158.426 199.738 185.437 1.00 16.07  ? 4702 ATP A C2    1 
HETATM 24161 N N3    . ATP C 3 .    ? 157.226 199.195 185.230 1.00 16.07  ? 4702 ATP A N3    1 
HETATM 24162 C C4    . ATP C 3 .    ? 156.384 199.498 186.222 1.00 16.07  ? 4702 ATP A C4    1 
HETATM 24163 P PG    . ATP D 3 .    ? 135.704 174.960 167.907 1.00 35.36  ? 4703 ATP A PG    1 
HETATM 24164 O O1G   . ATP D 3 .    ? 136.758 175.006 168.960 1.00 35.36  ? 4703 ATP A O1G   1 
HETATM 24165 O O2G   . ATP D 3 .    ? 135.692 176.189 166.994 1.00 35.36  ? 4703 ATP A O2G   1 
HETATM 24166 O O3G   . ATP D 3 .    ? 135.750 173.694 167.046 1.00 35.36  ? 4703 ATP A O3G   1 
HETATM 24167 P PB    . ATP D 3 .    ? 133.480 175.552 169.814 1.00 35.36  ? 4703 ATP A PB    1 
HETATM 24168 O O1B   . ATP D 3 .    ? 133.834 174.875 171.076 1.00 35.36  ? 4703 ATP A O1B   1 
HETATM 24169 O O2B   . ATP D 3 .    ? 133.714 177.060 169.789 1.00 35.36  ? 4703 ATP A O2B   1 
HETATM 24170 O O3B   . ATP D 3 .    ? 134.252 174.941 168.570 1.00 35.36  ? 4703 ATP A O3B   1 
HETATM 24171 P PA    . ATP D 3 .    ? 130.850 176.085 168.581 1.00 35.36  ? 4703 ATP A PA    1 
HETATM 24172 O O1A   . ATP D 3 .    ? 130.462 177.337 169.261 1.00 35.36  ? 4703 ATP A O1A   1 
HETATM 24173 O O2A   . ATP D 3 .    ? 131.381 176.255 167.159 1.00 35.36  ? 4703 ATP A O2A   1 
HETATM 24174 O O3A   . ATP D 3 .    ? 131.961 175.311 169.407 1.00 35.36  ? 4703 ATP A O3A   1 
HETATM 24175 O "O5'" . ATP D 3 .    ? 129.648 175.063 168.550 1.00 35.36  ? 4703 ATP A "O5'" 1 
HETATM 24176 C "C5'" . ATP D 3 .    ? 129.049 174.573 169.769 1.00 35.36  ? 4703 ATP A "C5'" 1 
HETATM 24177 C "C4'" . ATP D 3 .    ? 127.795 173.813 169.418 1.00 35.36  ? 4703 ATP A "C4'" 1 
HETATM 24178 O "O4'" . ATP D 3 .    ? 126.991 173.632 170.604 1.00 35.36  ? 4703 ATP A "O4'" 1 
HETATM 24179 C "C3'" . ATP D 3 .    ? 126.877 174.511 168.424 1.00 35.36  ? 4703 ATP A "C3'" 1 
HETATM 24180 O "O3'" . ATP D 3 .    ? 126.082 173.569 167.713 1.00 35.36  ? 4703 ATP A "O3'" 1 
HETATM 24181 C "C2'" . ATP D 3 .    ? 126.029 175.395 169.339 1.00 35.36  ? 4703 ATP A "C2'" 1 
HETATM 24182 O "O2'" . ATP D 3 .    ? 124.756 175.678 168.770 1.00 35.36  ? 4703 ATP A "O2'" 1 
HETATM 24183 C "C1'" . ATP D 3 .    ? 125.877 174.509 170.580 1.00 35.36  ? 4703 ATP A "C1'" 1 
HETATM 24184 N N9    . ATP D 3 .    ? 125.847 175.237 171.846 1.00 35.36  ? 4703 ATP A N9    1 
HETATM 24185 C C8    . ATP D 3 .    ? 126.518 174.896 172.992 1.00 35.36  ? 4703 ATP A C8    1 
HETATM 24186 N N7    . ATP D 3 .    ? 126.322 175.716 173.994 1.00 35.36  ? 4703 ATP A N7    1 
HETATM 24187 C C5    . ATP D 3 .    ? 125.457 176.667 173.474 1.00 35.36  ? 4703 ATP A C5    1 
HETATM 24188 C C6    . ATP D 3 .    ? 124.864 177.816 174.031 1.00 35.36  ? 4703 ATP A C6    1 
HETATM 24189 N N6    . ATP D 3 .    ? 125.059 178.217 175.291 1.00 35.36  ? 4703 ATP A N6    1 
HETATM 24190 N N1    . ATP D 3 .    ? 124.049 178.550 173.241 1.00 35.36  ? 4703 ATP A N1    1 
HETATM 24191 C C2    . ATP D 3 .    ? 123.853 178.158 171.980 1.00 35.36  ? 4703 ATP A C2    1 
HETATM 24192 N N3    . ATP D 3 .    ? 124.349 177.090 171.350 1.00 35.36  ? 4703 ATP A N3    1 
HETATM 24193 C C4    . ATP D 3 .    ? 125.155 176.385 172.151 1.00 35.36  ? 4703 ATP A C4    1 
HETATM 24194 P PB    . ADP E 2 .    ? 138.589 150.786 151.280 1.00 36.77  ? 4704 ADP A PB    1 
HETATM 24195 O O1B   . ADP E 2 .    ? 137.423 151.738 151.185 1.00 36.77  ? 4704 ADP A O1B   1 
HETATM 24196 O O2B   . ADP E 2 .    ? 138.923 150.342 152.682 1.00 36.77  ? 4704 ADP A O2B   1 
HETATM 24197 O O3B   . ADP E 2 .    ? 139.788 151.188 150.457 1.00 36.77  ? 4704 ADP A O3B   1 
HETATM 24198 P PA    . ADP E 2 .    ? 137.626 149.441 149.020 1.00 36.77  ? 4704 ADP A PA    1 
HETATM 24199 O O1A   . ADP E 2 .    ? 136.300 150.146 148.874 1.00 36.77  ? 4704 ADP A O1A   1 
HETATM 24200 O O2A   . ADP E 2 .    ? 138.824 149.888 148.221 1.00 36.77  ? 4704 ADP A O2A   1 
HETATM 24201 O O3A   . ADP E 2 .    ? 138.045 149.446 150.573 1.00 36.77  ? 4704 ADP A O3A   1 
HETATM 24202 O "O5'" . ADP E 2 .    ? 137.407 147.874 148.732 1.00 36.77  ? 4704 ADP A "O5'" 1 
HETATM 24203 C "C5'" . ADP E 2 .    ? 138.200 147.245 147.730 1.00 36.77  ? 4704 ADP A "C5'" 1 
HETATM 24204 C "C4'" . ADP E 2 .    ? 137.586 145.928 147.282 1.00 36.77  ? 4704 ADP A "C4'" 1 
HETATM 24205 O "O4'" . ADP E 2 .    ? 136.822 145.322 148.326 1.00 36.77  ? 4704 ADP A "O4'" 1 
HETATM 24206 C "C3'" . ADP E 2 .    ? 136.636 146.137 146.116 1.00 36.77  ? 4704 ADP A "C3'" 1 
HETATM 24207 O "O3'" . ADP E 2 .    ? 137.260 145.727 144.898 1.00 36.77  ? 4704 ADP A "O3'" 1 
HETATM 24208 C "C2'" . ADP E 2 .    ? 135.439 145.258 146.410 1.00 36.77  ? 4704 ADP A "C2'" 1 
HETATM 24209 O "O2'" . ADP E 2 .    ? 135.299 144.264 145.392 1.00 36.77  ? 4704 ADP A "O2'" 1 
HETATM 24210 C "C1'" . ADP E 2 .    ? 135.739 144.596 147.743 1.00 36.77  ? 4704 ADP A "C1'" 1 
HETATM 24211 N N9    . ADP E 2 .    ? 134.529 144.647 148.596 1.00 36.77  ? 4704 ADP A N9    1 
HETATM 24212 C C8    . ADP E 2 .    ? 134.234 145.589 149.509 1.00 36.77  ? 4704 ADP A C8    1 
HETATM 24213 N N7    . ADP E 2 .    ? 133.045 145.330 150.111 1.00 36.77  ? 4704 ADP A N7    1 
HETATM 24214 C C5    . ADP E 2 .    ? 132.562 144.196 149.574 1.00 36.77  ? 4704 ADP A C5    1 
HETATM 24215 C C6    . ADP E 2 .    ? 131.355 143.359 149.751 1.00 36.77  ? 4704 ADP A C6    1 
HETATM 24216 N N6    . ADP E 2 .    ? 130.397 143.691 150.647 1.00 36.77  ? 4704 ADP A N6    1 
HETATM 24217 N N1    . ADP E 2 .    ? 131.241 142.253 148.986 1.00 36.77  ? 4704 ADP A N1    1 
HETATM 24218 C C2    . ADP E 2 .    ? 132.183 141.906 148.091 1.00 36.77  ? 4704 ADP A C2    1 
HETATM 24219 N N3    . ADP E 2 .    ? 133.302 142.619 147.879 1.00 36.77  ? 4704 ADP A N3    1 
HETATM 24220 C C4    . ADP E 2 .    ? 133.546 143.750 148.579 1.00 36.77  ? 4704 ADP A C4    1 
# 
